CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 240818122313878422

Job options:

ID        	=	 240818122313878422
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 -1
CUTOFF    	=	 10
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   SER A  96      11.806 -18.600  32.489  1.00 73.09           N  
ANISOU    1  N   SER A  96     8907   8233  10630   -669    480  -2453       N  
ATOM      2  CA  SER A  96      12.255 -17.300  32.999  1.00 71.26           C  
ANISOU    2  CA  SER A  96     8545   8095  10437   -573    433  -2462       C  
ATOM      3  C   SER A  96      11.258 -16.174  32.687  1.00 67.80           C  
ANISOU    3  C   SER A  96     8160   7839   9762   -774    572  -2139       C  
ATOM      4  O   SER A  96      11.537 -15.289  31.875  1.00 69.54           O  
ANISOU    4  O   SER A  96     8285   8165   9971   -933    807  -2187       O  
ATOM      5  CB  SER A  96      13.629 -16.953  32.405  1.00 67.80           C  
ANISOU    5  CB  SER A  96     7817   7675  10269   -618    555  -2909       C  
ATOM      6  OG  SER A  96      13.978 -15.605  32.675  1.00 64.86           O  
ANISOU    6  OG  SER A  96     7282   7364   9997   -638    660  -2981       O  
ATOM      7  N   VAL A  97      10.092 -16.217  33.323  1.00 58.94           N  
ANISOU    7  N   VAL A  97     7220   6727   8448   -740    472  -1810       N  
ATOM      8  CA  VAL A  97       9.072 -15.197  33.108  1.00 49.22           C  
ANISOU    8  CA  VAL A  97     6035   5686   6980   -863    558  -1514       C  
ATOM      9  C   VAL A  97       8.607 -14.514  34.402  1.00 48.05           C  
ANISOU    9  C   VAL A  97     5960   5496   6802   -701    417  -1286       C  
ATOM     10  O   VAL A  97       8.346 -15.190  35.400  1.00 50.46           O  
ANISOU   10  O   VAL A  97     6403   5656   7114   -535    261  -1212       O  
ATOM     11  CB  VAL A  97       7.869 -15.789  32.349  1.00 43.54           C  
ANISOU   11  CB  VAL A  97     5384   5133   6026  -1041    607  -1414       C  
ATOM     12  CG1 VAL A  97       6.865 -14.707  32.009  1.00 40.03           C  
ANISOU   12  CG1 VAL A  97     4964   4955   5291  -1077    660  -1156       C  
ATOM     13  CG2 VAL A  97       8.354 -16.459  31.066  1.00 44.54           C  
ANISOU   13  CG2 VAL A  97     5417   5347   6160  -1182    736  -1690       C  
ATOM     14  N   PRO A  98       8.553 -13.168  34.408  1.00 43.47           N  
ANISOU   14  N   PRO A  98     5317   5007   6194   -724    522  -1176       N  
ATOM     15  CA  PRO A  98       8.110 -12.448  35.610  1.00 40.30           C  
ANISOU   15  CA  PRO A  98     4950   4585   5776   -588    400   -997       C  
ATOM     16  C   PRO A  98       6.629 -12.698  35.909  1.00 42.44           C  
ANISOU   16  C   PRO A  98     5395   4925   5803   -630    328   -677       C  
ATOM     17  O   PRO A  98       5.829 -12.822  34.990  1.00 42.93           O  
ANISOU   17  O   PRO A  98     5479   5149   5683   -785    417   -589       O  
ATOM     18  CB  PRO A  98       8.338 -10.972  35.250  1.00 37.62           C  
ANISOU   18  CB  PRO A  98     4507   4288   5498   -664    648   -973       C  
ATOM     19  CG  PRO A  98       9.304 -10.991  34.091  1.00 39.28           C  
ANISOU   19  CG  PRO A  98     4622   4465   5836   -788    911  -1223       C  
ATOM     20  CD  PRO A  98       8.993 -12.248  33.343  1.00 41.53           C  
ANISOU   20  CD  PRO A  98     4995   4831   5955   -855    824  -1227       C  
ATOM     21  N   SER A  99       6.281 -12.793  37.187  1.00 47.25           N  
ANISOU   21  N   SER A  99     6110   5439   6404   -468    175   -560       N  
ATOM     22  CA  SER A  99       4.905 -13.036  37.618  1.00 47.78           C  
ANISOU   22  CA  SER A  99     6330   5518   6305   -529    167   -312       C  
ATOM     23  C   SER A  99       3.931 -11.954  37.182  1.00 44.59           C  
ANISOU   23  C   SER A  99     5857   5340   5745   -655    237   -123       C  
ATOM     24  O   SER A  99       4.302 -10.791  37.069  1.00 45.15           O  
ANISOU   24  O   SER A  99     5840   5471   5843   -618    298    -84       O  
ATOM     25  CB  SER A  99       4.848 -13.167  39.138  1.00 52.73           C  
ANISOU   25  CB  SER A  99     7126   5986   6925   -282     43   -206       C  
ATOM     26  OG  SER A  99       3.535 -13.473  39.573  1.00 54.41           O  
ANISOU   26  OG  SER A  99     7502   6151   7022   -377    120      2       O  
ATOM     27  N   GLN A 100       2.674 -12.337  36.981  1.00 45.70           N  
ANISOU   27  N   GLN A 100     6027   5588   5748   -783    260    -46       N  
ATOM     28  CA  GLN A 100       1.639 -11.381  36.600  1.00 48.96           C  
ANISOU   28  CA  GLN A 100     6365   6266   5970   -817    275    104       C  
ATOM     29  C   GLN A 100       0.444 -11.471  37.556  1.00 45.38           C  
ANISOU   29  C   GLN A 100     5958   5788   5496   -854    243    208       C  
ATOM     30  O   GLN A 100      -0.592 -10.828  37.342  1.00 44.00           O  
ANISOU   30  O   GLN A 100     5693   5851   5175   -870    227    282       O  
ATOM     31  CB  GLN A 100       1.137 -11.658  35.200  1.00 54.34           C  
ANISOU   31  CB  GLN A 100     6938   7249   6458   -899    314    -28       C  
ATOM     32  CG  GLN A 100       1.103 -13.121  34.880  1.00 58.98           C  
ANISOU   32  CG  GLN A 100     7490   7772   7146  -1058    342   -305       C  
ATOM     33  CD  GLN A 100       0.445 -13.364  33.558  1.00 62.31           C  
ANISOU   33  CD  GLN A 100     7734   8589   7351  -1119    341   -529       C  
ATOM     34  NE2 GLN A 100      -0.114 -14.556  33.377  1.00 65.76           N  
ANISOU   34  NE2 GLN A 100     8053   9031   7901  -1313    395   -850       N  
ATOM     35  OE1 GLN A 100       0.400 -12.473  32.718  1.00 61.42           O  
ANISOU   35  OE1 GLN A 100     7597   8778   6959   -963    323   -435       O  
ATOM     36  N   LYS A 101       0.599 -12.283  38.597  1.00 38.95           N  
ANISOU   36  N   LYS A 101     5308   4682   4811   -829    259    207       N  
ATOM     37  CA  LYS A 101      -0.461 -12.504  39.544  1.00 36.35           C  
ANISOU   37  CA  LYS A 101     5083   4248   4482   -880    329    296       C  
ATOM     38  C   LYS A 101      -0.759 -11.211  40.266  1.00 33.66           C  
ANISOU   38  C   LYS A 101     4717   4004   4070   -770    239    499       C  
ATOM     39  O   LYS A 101       0.139 -10.544  40.757  1.00 32.58           O  
ANISOU   39  O   LYS A 101     4600   3818   3963   -590    147    563       O  
ATOM     40  CB  LYS A 101      -0.091 -13.610  40.541  1.00 41.10           C  
ANISOU   40  CB  LYS A 101     5985   4454   5176   -775    440    323       C  
ATOM     41  CG  LYS A 101      -1.270 -14.131  41.324  1.00 47.84           C  
ANISOU   41  CG  LYS A 101     7002   5112   6061   -893    677    377       C  
ATOM     42  CD  LYS A 101      -0.924 -15.365  42.132  1.00 56.95           C  
ANISOU   42  CD  LYS A 101     8560   5803   7277   -747    912    441       C  
ATOM     43  CE  LYS A 101      -2.092 -15.747  43.061  1.00 61.49           C  
ANISOU   43  CE  LYS A 101     9372   6105   7887   -855   1265    535       C  
ATOM     44  NZ  LYS A 101      -1.853 -16.989  43.861  1.00 65.68           N1+
ANISOU   44  NZ  LYS A 101    10417   6091   8448   -667   1632    662       N1+
ATOM     45  N   THR A 102      -2.031 -10.846  40.282  1.00 36.41           N  
ANISOU   45  N   THR A 102     4968   4513   4353   -883    275    527       N  
ATOM     46  CA  THR A 102      -2.508  -9.666  40.983  1.00 40.15           C  
ANISOU   46  CA  THR A 102     5411   5067   4776   -799    219    708       C  
ATOM     47  C   THR A 102      -2.237  -9.833  42.489  1.00 37.13           C  
ANISOU   47  C   THR A 102     5258   4410   4438   -676    237    822       C  
ATOM     48  O   THR A 102      -2.354 -10.935  43.017  1.00 29.05           O  
ANISOU   48  O   THR A 102     4453   3142   3443   -694    372    801       O  
ATOM     49  CB  THR A 102      -4.011  -9.463  40.719  1.00 45.73           C  
ANISOU   49  CB  THR A 102     5947   6011   5419   -932    250    641       C  
ATOM     50  CG2 THR A 102      -4.515  -8.187  41.346  1.00 47.79           C  
ANISOU   50  CG2 THR A 102     6162   6361   5635   -830    194    826       C  
ATOM     51  OG1 THR A 102      -4.242  -9.433  39.305  1.00 46.47           O  
ANISOU   51  OG1 THR A 102     5842   6432   5383   -939    191    487       O  
ATOM     52  N   TYR A 103      -1.819  -8.757  43.154  1.00 35.25           N  
ANISOU   52  N   TYR A 103     4994   4205   4196   -513    136    924       N  
ATOM     53  CA  TYR A 103      -1.490  -8.801  44.581  1.00 37.61           C  
ANISOU   53  CA  TYR A 103     5484   4345   4461   -304     96    985       C  
ATOM     54  C   TYR A 103      -1.675  -7.431  45.214  1.00 35.34           C  
ANISOU   54  C   TYR A 103     5060   4182   4186   -236     31   1044       C  
ATOM     55  O   TYR A 103      -0.797  -6.581  45.135  1.00 36.64           O  
ANISOU   55  O   TYR A 103     5059   4411   4450   -138    -43    946       O  
ATOM     56  CB  TYR A 103      -0.045  -9.288  44.783  1.00 37.60           C  
ANISOU   56  CB  TYR A 103     5566   4246   4475    -50    -22    858       C  
ATOM     57  CG  TYR A 103       0.456  -9.215  46.215  1.00 38.00           C  
ANISOU   57  CG  TYR A 103     5778   4250   4408    309   -144    854       C  
ATOM     58  CD1 TYR A 103      -0.057 -10.054  47.203  1.00 40.72           C  
ANISOU   58  CD1 TYR A 103     6507   4401   4564    473    -33   1019       C  
ATOM     59  CD2 TYR A 103       1.456  -8.312  46.577  1.00 40.58           C  
ANISOU   59  CD2 TYR A 103     5877   4734   4809    514   -331    637       C  
ATOM     60  CE1 TYR A 103       0.415  -9.990  48.525  1.00 44.07           C  
ANISOU   60  CE1 TYR A 103     7131   4840   4772    917   -164   1024       C  
ATOM     61  CE2 TYR A 103       1.934  -8.240  47.892  1.00 42.04           C  
ANISOU   61  CE2 TYR A 103     6155   4981   4836    917   -502    538       C  
ATOM     62  CZ  TYR A 103       1.408  -9.081  48.855  1.00 43.53           C  
ANISOU   62  CZ  TYR A 103     6774   5028   4737   1156   -447    760       C  
ATOM     63  OH  TYR A 103       1.880  -9.012  50.141  1.00 46.30           O  
ANISOU   63  OH  TYR A 103     7264   5494   4834   1654   -632    673       O  
ATOM     64  N   GLN A 104      -2.774  -7.255  45.930  1.00 37.69           N  
ANISOU   64  N   GLN A 104     5422   4476   4424   -298    106   1156       N  
ATOM     65  CA  GLN A 104      -3.103  -5.953  46.493  1.00 38.77           C  
ANISOU   65  CA  GLN A 104     5413   4727   4593   -262     69   1204       C  
ATOM     66  C   GLN A 104      -2.207  -5.599  47.679  1.00 38.79           C  
ANISOU   66  C   GLN A 104     5459   4709   4569     12    -50   1117       C  
ATOM     67  O   GLN A 104      -1.900  -4.424  47.905  1.00 36.43           O  
ANISOU   67  O   GLN A 104     4942   4506   4393     56    -90   1025       O  
ATOM     68  CB  GLN A 104      -4.581  -5.937  46.876  1.00 42.76           C  
ANISOU   68  CB  GLN A 104     5942   5250   5055   -420    191   1296       C  
ATOM     69  CG  GLN A 104      -5.482  -5.945  45.634  1.00 45.03           C  
ANISOU   69  CG  GLN A 104     6036   5704   5370   -623    234   1254       C  
ATOM     70  CD  GLN A 104      -6.944  -5.658  45.922  1.00 46.88           C  
ANISOU   70  CD  GLN A 104     6159   6039   5613   -759    318   1235       C  
ATOM     71  NE2 GLN A 104      -7.796  -5.885  44.923  1.00 46.64           N  
ANISOU   71  NE2 GLN A 104     5926   6214   5579   -884    324   1085       N  
ATOM     72  OE1 GLN A 104      -7.307  -5.242  47.024  1.00 48.93           O  
ANISOU   72  OE1 GLN A 104     6483   6230   5877   -734    367   1301       O  
ATOM     73  N   GLY A 105      -1.774  -6.620  48.416  1.00 38.24           N  
ANISOU   73  N   GLY A 105     5672   4522   4337    238    -89   1110       N  
ATOM     74  CA  GLY A 105      -0.813  -6.427  49.484  1.00 37.36           C  
ANISOU   74  CA  GLY A 105     5592   4484   4118    623   -275    950       C  
ATOM     75  C   GLY A 105      -1.342  -5.638  50.667  1.00 39.73           C  
ANISOU   75  C   GLY A 105     5890   4885   4319    730   -292    968       C  
ATOM     76  O   GLY A 105      -2.535  -5.335  50.744  1.00 41.59           O  
ANISOU   76  O   GLY A 105     6147   5082   4571    492   -129   1146       O  
ATOM     77  N   SER A 106      -0.443  -5.278  51.579  1.00 37.32           N  
ANISOU   77  N   SER A 106     5509   4752   3921   1103   -504    715       N  
ATOM     78  CA  SER A 106      -0.827  -4.601  52.804  1.00 37.27           C  
ANISOU   78  CA  SER A 106     5503   4885   3771   1274   -547    672       C  
ATOM     79  C   SER A 106      -1.424  -3.229  52.570  1.00 37.69           C  
ANISOU   79  C   SER A 106     5193   5000   4126    936   -445    627       C  
ATOM     80  O   SER A 106      -2.114  -2.694  53.432  1.00 42.74           O  
ANISOU   80  O   SER A 106     5851   5704   4684    953   -404    669       O  
ATOM     81  CB  SER A 106       0.387  -4.435  53.717  1.00 37.36           C  
ANISOU   81  CB  SER A 106     5395   5169   3630   1791   -851    267       C  
ATOM     82  OG  SER A 106       0.822  -5.684  54.215  1.00 44.82           O  
ANISOU   82  OG  SER A 106     6778   6077   4174   2267   -954    361       O  
ATOM     83  N   TYR A 107      -1.179  -2.653  51.404  1.00 33.96           N  
ANISOU   83  N   TYR A 107     4432   4486   3984    659   -365    564       N  
ATOM     84  CA  TYR A 107      -1.602  -1.280  51.191  1.00 32.58           C  
ANISOU   84  CA  TYR A 107     3959   4328   4093    435   -221    527       C  
ATOM     85  C   TYR A 107      -2.839  -1.154  50.314  1.00 28.42           C  
ANISOU   85  C   TYR A 107     3494   3701   3603    140    -38    872       C  
ATOM     86  O   TYR A 107      -3.300  -0.043  50.049  1.00 25.88           O  
ANISOU   86  O   TYR A 107     2986   3371   3476     13    100    909       O  
ATOM     87  CB  TYR A 107      -0.442  -0.474  50.613  1.00 35.42           C  
ANISOU   87  CB  TYR A 107     3961   4685   4810    400   -160    177       C  
ATOM     88  CG  TYR A 107       0.728  -0.527  51.553  1.00 38.14           C  
ANISOU   88  CG  TYR A 107     4128   5222   5143    722   -383   -314       C  
ATOM     89  CD1 TYR A 107       0.705   0.163  52.754  1.00 37.40           C  
ANISOU   89  CD1 TYR A 107     3862   5315   5033    890   -471   -587       C  
ATOM     90  CD2 TYR A 107       1.848  -1.290  51.247  1.00 39.78           C  
ANISOU   90  CD2 TYR A 107     4311   5473   5332    901   -533   -556       C  
ATOM     91  CE1 TYR A 107       1.761   0.097  53.628  1.00 40.89           C  
ANISOU   91  CE1 TYR A 107     4096   6034   5407   1268   -734  -1125       C  
ATOM     92  CE2 TYR A 107       2.909  -1.354  52.106  1.00 45.41           C  
ANISOU   92  CE2 TYR A 107     4815   6440   6000   1280   -794  -1082       C  
ATOM     93  CZ  TYR A 107       2.860  -0.660  53.296  1.00 46.55           C  
ANISOU   93  CZ  TYR A 107     4773   6820   6093   1483   -909  -1382       C  
ATOM     94  OH  TYR A 107       3.921  -0.730  54.158  1.00 53.65           O  
ANISOU   94  OH  TYR A 107     5416   8071   6898   1941  -1224  -1996       O  
ATOM     95  N   GLY A 108      -3.398  -2.290  49.913  1.00 28.31           N  
ANISOU   95  N   GLY A 108     3729   3622   3404     68    -27   1077       N  
ATOM     96  CA  GLY A 108      -4.582  -2.282  49.087  1.00 26.35           C  
ANISOU   96  CA  GLY A 108     3471   3372   3171   -164     94   1274       C  
ATOM     97  C   GLY A 108      -4.258  -1.584  47.791  1.00 25.08           C  
ANISOU   97  C   GLY A 108     3125   3235   3168   -225    155   1287       C  
ATOM     98  O   GLY A 108      -4.843  -0.546  47.489  1.00 28.13           O  
ANISOU   98  O   GLY A 108     3380   3660   3647   -256    254   1374       O  
ATOM     99  N   PHE A 109      -3.299  -2.139  47.049  1.00 35.80           N  
ANISOU   99  N   PHE A 109     4483   6524   2595   -250    355    119       N  
ATOM    100  CA  PHE A 109      -2.833  -1.555  45.787  1.00 33.94           C  
ANISOU  100  CA  PHE A 109     4132   6107   2658   -398    262     57       C  
ATOM    101  C   PHE A 109      -3.748  -1.920  44.611  1.00 33.55           C  
ANISOU  101  C   PHE A 109     3907   6123   2718   -600    403    256       C  
ATOM    102  O   PHE A 109      -4.000  -3.099  44.355  1.00 34.02           O  
ANISOU  102  O   PHE A 109     3942   6236   2747   -751    468    423       O  
ATOM    103  CB  PHE A 109      -1.395  -1.999  45.497  1.00 34.21           C  
ANISOU  103  CB  PHE A 109     4227   5944   2827   -503     87    -32       C  
ATOM    104  CG  PHE A 109      -0.864  -1.527  44.173  1.00 35.90           C  
ANISOU  104  CG  PHE A 109     4309   6006   3326   -658     25    -50       C  
ATOM    105  CD1 PHE A 109      -0.898  -0.185  43.829  1.00 35.89           C  
ANISOU  105  CD1 PHE A 109     4231   5918   3488   -593    -26   -140       C  
ATOM    106  CD2 PHE A 109      -0.288  -2.427  43.284  1.00 35.92           C  
ANISOU  106  CD2 PHE A 109     4266   5953   3429   -853      6     26       C  
ATOM    107  CE1 PHE A 109      -0.409   0.242  42.605  1.00 33.94           C  
ANISOU  107  CE1 PHE A 109     3856   5547   3492   -735    -65   -111       C  
ATOM    108  CE2 PHE A 109       0.223  -2.000  42.065  1.00 32.20           C  
ANISOU  108  CE2 PHE A 109     3671   5380   3182   -969    -29     28       C  
ATOM    109  CZ  PHE A 109       0.157  -0.664  41.727  1.00 30.23           C  
ANISOU  109  CZ  PHE A 109     3340   5058   3087   -916    -52    -22       C  
ATOM    110  N   ARG A 110      -4.272  -0.906  43.924  1.00 34.09           N  
ANISOU  110  N   ARG A 110     3856   6175   2920   -590    425    233       N  
ATOM    111  CA  ARG A 110      -5.159  -1.123  42.772  1.00 36.97           C  
ANISOU  111  CA  ARG A 110     4060   6592   3394   -754    531    397       C  
ATOM    112  C   ARG A 110      -4.857  -0.132  41.642  1.00 36.13           C  
ANISOU  112  C   ARG A 110     3865   6348   3516   -807    453    339       C  
ATOM    113  O   ARG A 110      -4.379   0.974  41.897  1.00 37.69           O  
ANISOU  113  O   ARG A 110     4089   6437   3793   -688    349    190       O  
ATOM    114  CB  ARG A 110      -6.629  -0.993  43.185  1.00 42.49           C  
ANISOU  114  CB  ARG A 110     4678   7492   3975   -667    703    503       C  
ATOM    115  CG  ARG A 110      -7.177  -2.143  44.012  1.00 54.14           C  
ANISOU  115  CG  ARG A 110     6178   9133   5259   -673    832    667       C  
ATOM    116  CD  ARG A 110      -8.520  -1.765  44.601  1.00 63.17           C  
ANISOU  116  CD  ARG A 110     7231  10494   6278   -532   1013    749       C  
ATOM    117  NE  ARG A 110      -8.365  -0.636  45.507  1.00 72.44           N  
ANISOU  117  NE  ARG A 110     8497  11707   7322   -256    977    547       N  
ATOM    118  CZ  ARG A 110      -9.166   0.425  45.528  1.00 79.38           C  
ANISOU  118  CZ  ARG A 110     9290  12663   8208   -104   1025    473       C  
ATOM    119  NH1 ARG A 110     -10.202   0.507  44.696  1.00 75.97           N1+
ANISOU  119  NH1 ARG A 110     8674  12284   7906   -209   1125    597       N1+
ATOM    120  NH2 ARG A 110      -8.930   1.407  46.391  1.00 85.90           N  
ANISOU  120  NH2 ARG A 110    10217  13503   8918    171    948    256       N  
ATOM    121  N   LEU A 111      -5.151  -0.510  40.402  1.00 34.99           N  
ANISOU  121  N   LEU A 111     3612   6201   3480   -975    488    462       N  
ATOM    122  CA  LEU A 111      -4.947   0.405  39.272  1.00 35.91           C  
ANISOU  122  CA  LEU A 111     3642   6216   3788  -1020    436    451       C  
ATOM    123  C   LEU A 111      -6.241   1.078  38.810  1.00 38.15           C  
ANISOU  123  C   LEU A 111     3812   6576   4107   -989    516    517       C  
ATOM    124  O   LEU A 111      -7.310   0.458  38.805  1.00 32.74           O  
ANISOU  124  O   LEU A 111     3067   6025   3346  -1019    623    625       O  
ATOM    125  CB  LEU A 111      -4.326  -0.331  38.084  1.00 31.77           C  
ANISOU  125  CB  LEU A 111     3079   5647   3343  -1186    406    526       C  
ATOM    126  CG  LEU A 111      -2.910  -0.890  38.227  1.00 33.57           C  
ANISOU  126  CG  LEU A 111     3386   5781   3589  -1228    310    454       C  
ATOM    127  CD1 LEU A 111      -2.467  -1.484  36.890  1.00 25.80           C  
ANISOU  127  CD1 LEU A 111     2338   4792   2672  -1356    298    527       C  
ATOM    128  CD2 LEU A 111      -1.897   0.148  38.769  1.00 29.35           C  
ANISOU  128  CD2 LEU A 111     2892   5097   3163  -1135    201    313       C  
ATOM    129  N   GLY A 112      -6.128   2.347  38.417  1.00 41.42           N  
ANISOU  129  N   GLY A 112     4186   6888   4664   -933    450    460       N  
ATOM    130  CA  GLY A 112      -7.250   3.091  37.861  1.00 38.82           C  
ANISOU  130  CA  GLY A 112     3751   6600   4398   -902    494    511       C  
ATOM    131  C   GLY A 112      -6.915   3.779  36.542  1.00 33.96           C  
ANISOU  131  C   GLY A 112     3067   5868   3967   -984    430    572       C  
ATOM    132  O   GLY A 112      -5.741   3.975  36.211  1.00 29.03           O  
ANISOU  132  O   GLY A 112     2467   5119   3446  -1036    349    560       O  
ATOM    133  N   PHE A 113      -7.959   4.148  35.798  1.00 31.99           N  
ANISOU  133  N   PHE A 113     2726   5669   3761   -990    469    651       N  
ATOM    134  CA  PHE A 113      -7.832   4.799  34.488  1.00 32.47           C  
ANISOU  134  CA  PHE A 113     2725   5647   3966  -1052    422    743       C  
ATOM    135  C   PHE A 113      -8.880   5.885  34.188  1.00 30.43           C  
ANISOU  135  C   PHE A 113     2391   5373   3798   -969    402    752       C  
ATOM    136  O   PHE A 113     -10.003   5.871  34.699  1.00 36.87           O  
ANISOU  136  O   PHE A 113     3168   6293   4549   -888    458    716       O  
ATOM    137  CB  PHE A 113      -7.921   3.755  33.383  1.00 28.44           C  
ANISOU  137  CB  PHE A 113     2187   5220   3399  -1177    468    866       C  
ATOM    138  CG  PHE A 113      -6.950   2.635  33.531  1.00 27.55           C  
ANISOU  138  CG  PHE A 113     2172   5086   3212  -1224    456    834       C  
ATOM    139  CD1 PHE A 113      -5.665   2.757  33.031  1.00 27.20           C  
ANISOU  139  CD1 PHE A 113     2156   4946   3231  -1258    408    841       C  
ATOM    140  CD2 PHE A 113      -7.320   1.457  34.175  1.00 31.65           C  
ANISOU  140  CD2 PHE A 113     2754   5657   3616  -1216    484    801       C  
ATOM    141  CE1 PHE A 113      -4.759   1.726  33.157  1.00 39.46           C  
ANISOU  141  CE1 PHE A 113     3793   6478   4723  -1279    385    794       C  
ATOM    142  CE2 PHE A 113      -6.418   0.407  34.319  1.00 32.39           C  
ANISOU  142  CE2 PHE A 113     2938   5714   3657  -1250    447    767       C  
ATOM    143  CZ  PHE A 113      -5.136   0.541  33.808  1.00 37.95           C  
ANISOU  143  CZ  PHE A 113     3665   6343   4412  -1279    396    751       C  
ATOM    144  N   LEU A 114      -8.523   6.801  33.303  1.00 31.01           N  
ANISOU  144  N   LEU A 114     2431   5322   4028   -992    325    820       N  
ATOM    145  CA  LEU A 114      -9.490   7.770  32.833  1.00 35.96           C  
ANISOU  145  CA  LEU A 114     2990   5921   4751   -928    286    848       C  
ATOM    146  C   LEU A 114     -10.586   7.043  32.038  1.00 37.60           C  
ANISOU  146  C   LEU A 114     3142   6276   4868   -974    365    940       C  
ATOM    147  O   LEU A 114     -10.295   6.146  31.233  1.00 35.90           O  
ANISOU  147  O   LEU A 114     2937   6121   4584  -1076    399   1034       O  
ATOM    148  CB  LEU A 114      -8.823   8.854  31.971  1.00 32.25           C  
ANISOU  148  CB  LEU A 114     2497   5277   4479   -960    183    947       C  
ATOM    149  CG  LEU A 114      -7.798   9.736  32.667  1.00 33.10           C  
ANISOU  149  CG  LEU A 114     2628   5187   4761   -918     58    865       C  
ATOM    150  CD1 LEU A 114      -7.181  10.697  31.677  1.00 33.94           C  
ANISOU  150  CD1 LEU A 114     2678   5125   5092   -983    -28   1030       C  
ATOM    151  CD2 LEU A 114      -8.397  10.494  33.833  1.00 34.34           C  
ANISOU  151  CD2 LEU A 114     2799   5293   4954   -742    -31    667       C  
ATOM    152  N   HIS A 115     -11.838   7.415  32.310  1.00 32.11           N  
ANISOU  152  N   HIS A 115     2382   5637   4180   -881    378    896       N  
ATOM    153  CA  HIS A 115     -13.005   6.909  31.589  1.00 36.12           C  
ANISOU  153  CA  HIS A 115     2811   6255   4659   -908    419    970       C  
ATOM    154  C   HIS A 115     -13.252   7.796  30.350  1.00 34.70           C  
ANISOU  154  C   HIS A 115     2603   5988   4594   -903    327   1059       C  
ATOM    155  O   HIS A 115     -14.118   8.668  30.380  1.00 33.71           O  
ANISOU  155  O   HIS A 115     2419   5832   4557   -808    279   1023       O  
ATOM    156  CB  HIS A 115     -14.236   6.903  32.503  1.00 40.12           C  
ANISOU  156  CB  HIS A 115     3234   6875   5135   -804    487    890       C  
ATOM    157  CG  HIS A 115     -13.952   6.443  33.901  1.00 40.74           C  
ANISOU  157  CG  HIS A 115     3354   7031   5096   -753    571    802       C  
ATOM    158  CD2 HIS A 115     -14.049   7.086  35.088  1.00 40.97           C  
ANISOU  158  CD2 HIS A 115     3398   7080   5089   -592    581    667       C  
ATOM    159  ND1 HIS A 115     -13.504   5.171  34.193  1.00 42.25           N  
ANISOU  159  ND1 HIS A 115     3586   7293   5174   -853    643    848       N  
ATOM    160  CE1 HIS A 115     -13.342   5.054  35.498  1.00 41.46           C  
ANISOU  160  CE1 HIS A 115     3528   7257   4967   -765    705    766       C  
ATOM    161  NE2 HIS A 115     -13.667   6.202  36.066  1.00 40.06           N  
ANISOU  161  NE2 HIS A 115     3339   7061   4820   -594    672    648       N  
ATOM    162  N   SER A 116     -12.482   7.562  29.284  1.00 32.02           N  
ANISOU  162  N   SER A 116     2306   5620   4240   -989    304   1179       N  
ATOM    163  CA  SER A 116     -12.338   8.486  28.155  1.00 37.64           C  
ANISOU  163  CA  SER A 116     3016   6240   5044   -983    225   1303       C  
ATOM    164  C   SER A 116     -13.263   8.270  26.951  1.00 38.70           C  
ANISOU  164  C   SER A 116     3120   6446   5137   -972    195   1390       C  
ATOM    165  O   SER A 116     -13.326   9.125  26.063  1.00 41.68           O  
ANISOU  165  O   SER A 116     3500   6755   5582   -943    125   1499       O  
ATOM    166  CB  SER A 116     -10.895   8.430  27.644  1.00 37.79           C  
ANISOU  166  CB  SER A 116     3088   6213   5057  -1061    236   1412       C  
ATOM    167  OG  SER A 116      -9.993   8.911  28.624  1.00 45.53           O  
ANISOU  167  OG  SER A 116     4087   7075   6136  -1063    216   1340       O  
ATOM    168  N   GLY A 117     -13.948   7.132  26.904  1.00 35.94           N  
ANISOU  168  N   GLY A 117     2743   6220   4692   -992    229   1351       N  
ATOM    169  CA  GLY A 117     -14.858   6.829  25.811  1.00 35.76           C  
ANISOU  169  CA  GLY A 117     2689   6253   4645   -967    165   1402       C  
ATOM    170  C   GLY A 117     -14.132   6.446  24.530  1.00 38.29           C  
ANISOU  170  C   GLY A 117     3086   6613   4850   -983    135   1515       C  
ATOM    171  O   GLY A 117     -12.893   6.357  24.506  1.00 37.77           O  
ANISOU  171  O   GLY A 117     3079   6543   4728  -1028    185   1565       O  
ATOM    172  N   THR A 118     -14.891   6.271  23.448  1.00 37.99           N  
ANISOU  172  N   THR A 118     3043   6620   4773   -927     47   1554       N  
ATOM    173  CA  THR A 118     -14.311   5.817  22.188  1.00 34.98           C  
ANISOU  173  CA  THR A 118     2741   6316   4235   -896     12   1644       C  
ATOM    174  C   THR A 118     -14.584   6.753  21.017  1.00 41.61           C  
ANISOU  174  C   THR A 118     3614   7141   5057   -803    -63   1777       C  
ATOM    175  O   THR A 118     -14.737   6.307  19.884  1.00 46.98           O  
ANISOU  175  O   THR A 118     4345   7910   5596   -722   -136   1816       O  
ATOM    176  CB  THR A 118     -14.813   4.419  21.809  1.00 34.23           C  
ANISOU  176  CB  THR A 118     2640   6310   4054   -885    -62   1556       C  
ATOM    177  CG2 THR A 118     -14.310   3.393  22.798  1.00 32.48           C  
ANISOU  177  CG2 THR A 118     2407   6106   3826   -981      6   1467       C  
ATOM    178  OG1 THR A 118     -16.247   4.409  21.789  1.00 35.49           O  
ANISOU  178  OG1 THR A 118     2713   6445   4328   -849   -158   1494       O  
ATOM    179  N   ALA A 119     -14.648   8.049  21.288  1.00 41.59           N  
ANISOU  179  N   ALA A 119     3587   7021   5194   -799    -63   1842       N  
ATOM    180  CA  ALA A 119     -14.761   9.015  20.212  1.00 42.35           C  
ANISOU  180  CA  ALA A 119     3722   7084   5286   -722   -132   2008       C  
ATOM    181  C   ALA A 119     -13.463   8.982  19.392  1.00 48.26           C  
ANISOU  181  C   ALA A 119     4542   7910   5885   -725    -54   2195       C  
ATOM    182  O   ALA A 119     -12.377   8.772  19.938  1.00 49.61           O  
ANISOU  182  O   ALA A 119     4707   8081   6061   -807     50   2207       O  
ATOM    183  CB  ALA A 119     -15.033  10.408  20.765  1.00 40.72           C  
ANISOU  183  CB  ALA A 119     3468   6704   5298   -723   -172   2034       C  
ATOM    184  N   LYS A 120     -13.588   9.250  18.095  1.00 48.95           N  
ANISOU  184  N   LYS A 120     4689   8066   5842   -622   -104   2350       N  
ATOM    185  CA  LYS A 120     -12.505   9.090  17.127  1.00 49.87           C  
ANISOU  185  CA  LYS A 120     4868   8321   5758   -580    -18   2543       C  
ATOM    186  C   LYS A 120     -11.211   9.839  17.499  1.00 51.08           C  
ANISOU  186  C   LYS A 120     4978   8399   6030   -685    110   2723       C  
ATOM    187  O   LYS A 120     -10.111   9.414  17.142  1.00 40.87           O  
ANISOU  187  O   LYS A 120     3694   7230   4604   -690    226   2826       O  
ATOM    188  CB  LYS A 120     -13.013   9.560  15.764  1.00 51.69           C  
ANISOU  188  CB  LYS A 120     5170   8621   5850   -432   -101   2706       C  
ATOM    189  CG  LYS A 120     -12.105   9.347  14.584  1.00 54.86           C  
ANISOU  189  CG  LYS A 120     5643   9224   5978   -329    -13   2913       C  
ATOM    190  CD  LYS A 120     -12.014   7.876  14.226  1.00 59.75           C  
ANISOU  190  CD  LYS A 120     6319  10037   6348   -235    -31   2734       C  
ATOM    191  CE  LYS A 120     -11.049   7.657  13.060  1.00 68.72           C  
ANISOU  191  CE  LYS A 120     7523  11412   7174    -94     72   2927       C  
ATOM    192  NZ  LYS A 120      -9.609   7.771  13.493  1.00 71.53           N1+
ANISOU  192  NZ  LYS A 120     7807  11797   7574   -211    277   3065       N1+
ATOM    193  N   SER A 121     -11.342  10.941  18.229  1.00 50.91           N  
ANISOU  193  N   SER A 121     4897   8168   6278   -758     71   2750       N  
ATOM    194  CA  SER A 121     -10.194  11.804  18.523  1.00 54.08           C  
ANISOU  194  CA  SER A 121     5242   8447   6859   -854    139   2935       C  
ATOM    195  C   SER A 121      -9.397  11.475  19.804  1.00 52.24           C  
ANISOU  195  C   SER A 121     4957   8137   6754   -966    197   2783       C  
ATOM    196  O   SER A 121      -8.341  12.065  20.039  1.00 55.41           O  
ANISOU  196  O   SER A 121     5301   8436   7318  -1046    241   2923       O  
ATOM    197  CB  SER A 121     -10.662  13.260  18.585  1.00 58.14           C  
ANISOU  197  CB  SER A 121     5721   8738   7630   -858     20   3050       C  
ATOM    198  OG  SER A 121     -11.522  13.464  19.693  1.00 61.42           O  
ANISOU  198  OG  SER A 121     6108   9015   8214   -862    -84   2792       O  
ATOM    199  N   VAL A 122      -9.882  10.550  20.627  1.00 47.42           N  
ANISOU  199  N   VAL A 122     4362   7569   6087   -971    189   2514       N  
ATOM    200  CA  VAL A 122      -9.216  10.265  21.897  1.00 47.80           C  
ANISOU  200  CA  VAL A 122     4379   7542   6240  -1057    227   2363       C  
ATOM    201  C   VAL A 122      -7.839   9.629  21.664  1.00 48.61           C  
ANISOU  201  C   VAL A 122     4506   7722   6243  -1083    329   2409       C  
ATOM    202  O   VAL A 122      -7.661   8.792  20.779  1.00 50.39           O  
ANISOU  202  O   VAL A 122     4788   8117   6243  -1016    373   2423       O  
ATOM    203  CB  VAL A 122     -10.079   9.351  22.819  1.00 41.11           C  
ANISOU  203  CB  VAL A 122     3545   6741   5333  -1047    208   2091       C  
ATOM    204  CG1 VAL A 122     -11.467   9.959  23.012  1.00 44.32           C  
ANISOU  204  CG1 VAL A 122     3928   7078   5835   -982    108   2012       C  
ATOM    205  CG2 VAL A 122     -10.200   7.943  22.256  1.00 41.46           C  
ANISOU  205  CG2 VAL A 122     3635   6980   5139  -1023    244   2035       C  
ATOM    206  N   THR A 123      -6.859  10.051  22.456  1.00 44.93           N  
ANISOU  206  N   THR A 123     4024   7094   5953  -1133    328   2367       N  
ATOM    207  CA  THR A 123      -5.500   9.562  22.300  1.00 43.11           C  
ANISOU  207  CA  THR A 123     3835   6876   5668  -1118    392   2345       C  
ATOM    208  C   THR A 123      -5.252   8.313  23.125  1.00 37.45           C  
ANISOU  208  C   THR A 123     3184   6203   4843  -1122    409   2092       C  
ATOM    209  O   THR A 123      -4.280   7.584  22.896  1.00 35.99           O  
ANISOU  209  O   THR A 123     3036   6074   4563  -1098    459   2050       O  
ATOM    210  CB  THR A 123      -4.466  10.613  22.722  1.00 42.60           C  
ANISOU  210  CB  THR A 123     3704   6607   5875  -1177    368   2441       C  
ATOM    211  CG2 THR A 123      -4.671  11.912  21.963  1.00 42.83           C  
ANISOU  211  CG2 THR A 123     3661   6550   6062  -1184    328   2715       C  
ATOM    212  OG1 THR A 123      -4.595  10.844  24.127  1.00 42.03           O  
ANISOU  212  OG1 THR A 123     3602   6387   5982  -1239    296   2282       O  
ATOM    213  N   CYS A 124      -6.116   8.083  24.101  1.00 31.12           N  
ANISOU  213  N   CYS A 124     4281   3963   3579   -119   -658   1201       N  
ATOM    214  CA  CYS A 124      -5.869   7.044  25.085  1.00 35.97           C  
ANISOU  214  CA  CYS A 124     4842   4668   4156   -198   -641   1030       C  
ATOM    215  C   CYS A 124      -7.173   6.627  25.745  1.00 35.66           C  
ANISOU  215  C   CYS A 124     4898   4674   3976    -95   -660    677       C  
ATOM    216  O   CYS A 124      -7.892   7.478  26.259  1.00 39.51           O  
ANISOU  216  O   CYS A 124     5501   5020   4490    -69   -804    515       O  
ATOM    217  CB  CYS A 124      -4.861   7.575  26.127  1.00 39.51           C  
ANISOU  217  CB  CYS A 124     5260   4943   4810   -409   -790   1090       C  
ATOM    218  SG  CYS A 124      -4.495   6.517  27.484  1.00 49.91           S  
ANISOU  218  SG  CYS A 124     6520   6376   6067   -478   -802    922       S  
ATOM    219  N   THR A 125      -7.484   5.337  25.750  1.00 30.39           N  
ANISOU  219  N   THR A 125     4170   4194   3182    -37   -517    553       N  
ATOM    220  CA  THR A 125      -8.726   4.905  26.373  1.00 32.08           C  
ANISOU  220  CA  THR A 125     4445   4459   3284     35   -509    242       C  
ATOM    221  C   THR A 125      -8.673   3.472  26.873  1.00 33.19           C  
ANISOU  221  C   THR A 125     4508   4716   3388      5   -372    170       C  
ATOM    222  O   THR A 125      -8.037   2.609  26.270  1.00 34.11           O  
ANISOU  222  O   THR A 125     4520   4918   3524     12   -245    289       O  
ATOM    223  CB  THR A 125      -9.932   5.034  25.426  1.00 32.35           C  
ANISOU  223  CB  THR A 125     4511   4587   3195    223   -461     81       C  
ATOM    224  CG2 THR A 125      -9.805   4.082  24.193  1.00 23.20           C  
ANISOU  224  CG2 THR A 125     3223   3629   1963    329   -282    127       C  
ATOM    225  OG1 THR A 125     -11.137   4.768  26.161  1.00 24.42           O  
ANISOU  225  OG1 THR A 125     3551   3627   2103    266   -471   -232       O  
ATOM    226  N   TYR A 126      -9.351   3.232  27.992  1.00 32.24           N  
ANISOU  226  N   TYR A 126     4433   4600   3219    -18   -396    -17       N  
ATOM    227  CA  TYR A 126      -9.275   1.952  28.680  1.00 27.65           C  
ANISOU  227  CA  TYR A 126     3790   4087   2628    -61   -269    -29       C  
ATOM    228  C   TYR A 126     -10.588   1.174  28.622  1.00 29.74           C  
ANISOU  228  C   TYR A 126     4037   4432   2831      5   -135   -266       C  
ATOM    229  O   TYR A 126     -11.671   1.749  28.677  1.00 32.17           O  
ANISOU  229  O   TYR A 126     4397   4770   3057     66   -188   -476       O  
ATOM    230  CB  TYR A 126      -8.857   2.164  30.128  1.00 27.98           C  
ANISOU  230  CB  TYR A 126     3862   4115   2656   -144   -376      3       C  
ATOM    231  CG  TYR A 126      -8.941   0.923  30.979  1.00 30.47           C  
ANISOU  231  CG  TYR A 126     4132   4511   2935   -162   -241     21       C  
ATOM    232  CD1 TYR A 126      -7.974  -0.083  30.890  1.00 28.41           C  
ANISOU  232  CD1 TYR A 126     3794   4251   2750   -186   -134    222       C  
ATOM    233  CD2 TYR A 126      -9.990   0.751  31.874  1.00 31.40           C  
ANISOU  233  CD2 TYR A 126     4278   4708   2944   -142   -212   -143       C  
ATOM    234  CE1 TYR A 126      -8.051  -1.220  31.691  1.00 30.77           C  
ANISOU  234  CE1 TYR A 126     4063   4588   3039   -188     -5    282       C  
ATOM    235  CE2 TYR A 126     -10.073  -0.380  32.683  1.00 32.63           C  
ANISOU  235  CE2 TYR A 126     4390   4931   3077   -160    -66    -65       C  
ATOM    236  CZ  TYR A 126      -9.109  -1.357  32.588  1.00 32.20           C  
ANISOU  236  CZ  TYR A 126     4279   4836   3121   -182     37    158       C  
ATOM    237  OH  TYR A 126      -9.211  -2.467  33.385  1.00 32.58           O  
ANISOU  237  OH  TYR A 126     4294   4915   3167   -185    188    272       O  
ATOM    238  N   SER A 127     -10.475  -0.135  28.440  1.00 30.77           N  
ANISOU  238  N   SER A 127     4078   4588   3026     -4     38   -243       N  
ATOM    239  CA  SER A 127     -11.632  -1.010  28.432  1.00 29.72           C  
ANISOU  239  CA  SER A 127     3893   4498   2902     19    183   -462       C  
ATOM    240  C   SER A 127     -11.736  -1.856  29.716  1.00 27.09           C  
ANISOU  240  C   SER A 127     3550   4145   2596    -70    279   -402       C  
ATOM    241  O   SER A 127     -10.953  -2.791  29.920  1.00 23.35           O  
ANISOU  241  O   SER A 127     3033   3612   2229   -107    371   -221       O  
ATOM    242  CB  SER A 127     -11.576  -1.917  27.205  1.00 26.83           C  
ANISOU  242  CB  SER A 127     3410   4151   2633     86    315   -525       C  
ATOM    243  OG  SER A 127     -12.552  -2.936  27.274  1.00 26.73           O  
ANISOU  243  OG  SER A 127     3315   4135   2704     72    466   -736       O  
ATOM    244  N   PRO A 128     -12.704  -1.528  30.586  1.00 25.80           N  
ANISOU  244  N   PRO A 128     3423   4052   2327    -84    260   -539       N  
ATOM    245  CA  PRO A 128     -12.952  -2.388  31.753  1.00 26.44           C  
ANISOU  245  CA  PRO A 128     3475   4160   2410   -152    388   -458       C  
ATOM    246  C   PRO A 128     -13.252  -3.828  31.362  1.00 28.87           C  
ANISOU  246  C   PRO A 128     3679   4376   2915   -194    618   -463       C  
ATOM    247  O   PRO A 128     -12.734  -4.748  31.995  1.00 30.93           O  
ANISOU  247  O   PRO A 128     3919   4567   3267   -242    731   -241       O  
ATOM    248  CB  PRO A 128     -14.163  -1.736  32.429  1.00 22.80           C  
ANISOU  248  CB  PRO A 128     3035   3843   1786   -133    343   -672       C  
ATOM    249  CG  PRO A 128     -14.025  -0.293  32.100  1.00 22.24           C  
ANISOU  249  CG  PRO A 128     3053   3781   1615    -58    109   -773       C  
ATOM    250  CD  PRO A 128     -13.438  -0.252  30.676  1.00 25.13           C  
ANISOU  250  CD  PRO A 128     3411   4037   2099    -24     99   -728       C  
ATOM    251  N   ALA A 129     -14.081  -4.023  30.342  1.00 32.96           N  
ANISOU  251  N   ALA A 129     4123   4890   3511   -165    679   -722       N  
ATOM    252  CA  ALA A 129     -14.491  -5.369  29.940  1.00 31.88           C  
ANISOU  252  CA  ALA A 129     3858   4644   3610   -212    884   -807       C  
ATOM    253  C   ALA A 129     -13.318  -6.229  29.478  1.00 34.29           C  
ANISOU  253  C   ALA A 129     4132   4799   4099   -199    935   -622       C  
ATOM    254  O   ALA A 129     -13.301  -7.437  29.702  1.00 34.15           O  
ANISOU  254  O   ALA A 129     4045   4626   4305   -258   1099   -554       O  
ATOM    255  CB  ALA A 129     -15.534  -5.288  28.837  1.00 27.29           C  
ANISOU  255  CB  ALA A 129     3179   4134   3056   -152    897  -1179       C  
ATOM    256  N   LEU A 130     -12.325  -5.598  28.858  1.00 37.26           N  
ANISOU  256  N   LEU A 130     4550   5215   4392   -120    796   -530       N  
ATOM    257  CA  LEU A 130     -11.185  -6.322  28.285  1.00 40.59           C  
ANISOU  257  CA  LEU A 130     4918   5549   4954    -77    828   -389       C  
ATOM    258  C   LEU A 130     -10.019  -6.296  29.263  1.00 39.45           C  
ANISOU  258  C   LEU A 130     4848   5389   4752    -98    757    -50       C  
ATOM    259  O   LEU A 130      -9.113  -7.126  29.142  1.00 41.18           O  
ANISOU  259  O   LEU A 130     5020   5568   5058    -50    762     83       O  
ATOM    260  CB  LEU A 130     -10.902  -5.851  26.851  1.00 39.87           C  
ANISOU  260  CB  LEU A 130     4771   5569   4810     44    749   -521       C  
ATOM    261  CG  LEU A 130     -12.009  -5.973  25.791  1.00 39.89           C  
ANISOU  261  CG  LEU A 130     4668   5656   4832    126    791   -889       C  
ATOM    262  CD1 LEU A 130     -11.572  -5.322  24.480  1.00 36.27           C  
ANISOU  262  CD1 LEU A 130     4168   5375   4238    282    698   -931       C  
ATOM    263  CD2 LEU A 130     -12.403  -7.421  25.565  1.00 40.90           C  
ANISOU  263  CD2 LEU A 130     4655   5649   5238    106    954  -1075       C  
ATOM    264  N   ASN A 131     -10.015  -5.293  30.152  1.00 34.82           N  
ANISOU  264  N   ASN A 131     4356   4873   4001   -147    672     50       N  
ATOM    265  CA  ASN A 131      -8.876  -4.966  31.031  1.00 34.22           C  
ANISOU  265  CA  ASN A 131     4336   4844   3823   -153    553    308       C  
ATOM    266  C   ASN A 131      -7.704  -4.523  30.167  1.00 31.80           C  
ANISOU  266  C   ASN A 131     3994   4551   3536   -112    457    393       C  
ATOM    267  O   ASN A 131      -6.535  -4.875  30.422  1.00 26.38           O  
ANISOU  267  O   ASN A 131     3270   3851   2903    -93    459    596       O  
ATOM    268  CB  ASN A 131      -8.447  -6.013  32.068  1.00 32.20           C  
ANISOU  268  CB  ASN A 131     4072   4535   3626   -161    663    546       C  
ATOM    269  CG  ASN A 131      -7.316  -5.495  32.991  1.00 29.63           C  
ANISOU  269  CG  ASN A 131     3782   4322   3155   -141    518    771       C  
ATOM    270  ND2 ASN A 131      -6.442  -6.396  33.437  1.00 28.89           N  
ANISOU  270  ND2 ASN A 131     3658   4192   3125    -93    581   1012       N  
ATOM    271  OD1 ASN A 131      -7.234  -4.298  33.275  1.00 25.84           O  
ANISOU  271  OD1 ASN A 131     3344   3952   2523   -157    343    707       O  
ATOM    272  N   LYS A 132      -8.039  -3.739  29.147  1.00 30.19           N  
ANISOU  272  N   LYS A 132     3795   4396   3278    -87    378    251       N  
ATOM    273  CA  LYS A 132      -7.091  -3.433  28.095  1.00 28.66           C  
ANISOU  273  CA  LYS A 132     3539   4247   3104    -39    334    329       C  
ATOM    274  C   LYS A 132      -6.998  -1.964  27.738  1.00 28.15           C  
ANISOU  274  C   LYS A 132     3528   4230   2938    -51    178    344       C  
ATOM    275  O   LYS A 132      -7.989  -1.312  27.441  1.00 31.80           O  
ANISOU  275  O   LYS A 132     4043   4706   3333    -20    143    173       O  
ATOM    276  CB  LYS A 132      -7.503  -4.241  26.865  1.00 29.04           C  
ANISOU  276  CB  LYS A 132     3485   4313   3237     58    459    156       C  
ATOM    277  CG  LYS A 132      -6.602  -4.051  25.669  1.00 23.59           C  
ANISOU  277  CG  LYS A 132     2700   3736   2528    143    436    234       C  
ATOM    278  CD  LYS A 132      -6.885  -5.107  24.615  1.00 22.45           C  
ANISOU  278  CD  LYS A 132     2421   3637   2474    268    558     32       C  
ATOM    279  CE  LYS A 132      -5.997  -4.936  23.380  1.00 22.99           C  
ANISOU  279  CE  LYS A 132     2366   3895   2473    389    545    104       C  
ATOM    280  NZ  LYS A 132      -6.113  -6.154  22.564  1.00 30.76           N1+
ANISOU  280  NZ  LYS A 132     3199   4921   3568    526    650   -120       N1+
ATOM    281  N   MET A 133      -5.768  -1.476  27.726  1.00 30.02           N  
ANISOU  281  N   MET A 133     3735   4484   3187    -93     90    555       N  
ATOM    282  CA  MET A 133      -5.473  -0.110  27.360  1.00 32.77           C  
ANISOU  282  CA  MET A 133     4114   4828   3509   -130    -47    627       C  
ATOM    283  C   MET A 133      -5.185   0.025  25.870  1.00 32.89           C  
ANISOU  283  C   MET A 133     4045   4935   3518    -49     10    696       C  
ATOM    284  O   MET A 133      -4.395  -0.739  25.295  1.00 31.87           O  
ANISOU  284  O   MET A 133     3792   4899   3418     -4     98    793       O  
ATOM    285  CB  MET A 133      -4.279   0.402  28.173  1.00 36.21           C  
ANISOU  285  CB  MET A 133     4530   5239   3991   -241   -175    812       C  
ATOM    286  CG  MET A 133      -3.806   1.764  27.710  1.00 41.19           C  
ANISOU  286  CG  MET A 133     5161   5817   4673   -311   -302    919       C  
ATOM    287  SD  MET A 133      -5.049   3.051  27.961  1.00 80.80           S  
ANISOU  287  SD  MET A 133    10336  10702   9663   -305   -440    728       S  
ATOM    288  CE  MET A 133      -5.013   3.220  29.752  1.00 28.45           C  
ANISOU  288  CE  MET A 133     3751   4044   3014   -379   -589    607       C  
ATOM    289  N   PHE A 134      -5.862   0.982  25.248  1.00 30.15           N  
ANISOU  289  N   PHE A 134     3757   4585   3114     -1    -41    641       N  
ATOM    290  CA  PHE A 134      -5.599   1.331  23.868  1.00 32.74           C  
ANISOU  290  CA  PHE A 134     4009   5037   3394     96      3    756       C  
ATOM    291  C   PHE A 134      -5.042   2.747  23.848  1.00 34.97           C  
ANISOU  291  C   PHE A 134     4337   5217   3732      1   -122    983       C  
ATOM    292  O   PHE A 134      -5.712   3.688  24.287  1.00 32.90           O  
ANISOU  292  O   PHE A 134     4206   4809   3487    -24   -240    905       O  
ATOM    293  CB  PHE A 134      -6.867   1.262  23.005  1.00 33.88           C  
ANISOU  293  CB  PHE A 134     4168   5286   3421    270     59    530       C  
ATOM    294  CG  PHE A 134      -7.545  -0.084  22.983  1.00 31.00           C  
ANISOU  294  CG  PHE A 134     3737   4986   3057    344    178    258       C  
ATOM    295  CD1 PHE A 134      -8.315  -0.506  24.049  1.00 32.32           C  
ANISOU  295  CD1 PHE A 134     3977   5033   3271    271    181     76       C  
ATOM    296  CD2 PHE A 134      -7.462  -0.896  21.857  1.00 22.83           C  
ANISOU  296  CD2 PHE A 134     2550   4140   1982    496    289    173       C  
ATOM    297  CE1 PHE A 134      -8.963  -1.726  24.010  1.00 35.59           C  
ANISOU  297  CE1 PHE A 134     4317   5465   3741    312    304   -155       C  
ATOM    298  CE2 PHE A 134      -8.107  -2.114  21.810  1.00 22.61           C  
ANISOU  298  CE2 PHE A 134     2447   4127   2017    553    388   -112       C  
ATOM    299  CZ  PHE A 134      -8.855  -2.532  22.885  1.00 37.50           C  
ANISOU  299  CZ  PHE A 134     4409   5842   3996    445    402   -262       C  
ATOM    300  N   CYS A 135      -3.837   2.912  23.313  1.00 37.70           N  
ANISOU  300  N   CYS A 135     4564   5633   4128    -49    -95   1255       N  
ATOM    301  CA  CYS A 135      -3.225   4.234  23.250  1.00 39.31           C  
ANISOU  301  CA  CYS A 135     4783   5708   4447   -172   -196   1500       C  
ATOM    302  C   CYS A 135      -2.385   4.404  21.998  1.00 41.18           C  
ANISOU  302  C   CYS A 135     4868   6122   4657   -133    -90   1802       C  
ATOM    303  O   CYS A 135      -2.006   3.434  21.344  1.00 41.40           O  
ANISOU  303  O   CYS A 135     4754   6396   4579    -25     40   1812       O  
ATOM    304  CB  CYS A 135      -2.376   4.505  24.489  1.00 40.28           C  
ANISOU  304  CB  CYS A 135     4896   5676   4731   -376   -324   1540       C  
ATOM    305  SG  CYS A 135      -1.065   3.315  24.697  1.00 45.01           S  
ANISOU  305  SG  CYS A 135     5310   6455   5336   -415   -240   1641       S  
ATOM    306  N   GLN A 136      -2.114   5.662  21.685  1.00 41.86           N  
ANISOU  306  N   GLN A 136     4977   6078   4852   -216   -147   2047       N  
ATOM    307  CA  GLN A 136      -1.350   6.058  20.521  1.00 42.89           C  
ANISOU  307  CA  GLN A 136     4964   6368   4966   -197    -39   2405       C  
ATOM    308  C   GLN A 136       0.143   6.116  20.783  1.00 46.42           C  
ANISOU  308  C   GLN A 136     5238   6823   5577   -407    -36   2644       C  
ATOM    309  O   GLN A 136       0.574   6.464  21.881  1.00 47.09           O  
ANISOU  309  O   GLN A 136     5348   6682   5862   -609   -173   2590       O  
ATOM    310  CB  GLN A 136      -1.846   7.422  20.059  1.00 45.67           C  
ANISOU  310  CB  GLN A 136     5430   6535   5387   -184    -90   2593       C  
ATOM    311  CG  GLN A 136      -3.176   7.369  19.338  1.00 44.98           C  
ANISOU  311  CG  GLN A 136     5448   6572   5071     93    -51   2438       C  
ATOM    312  CD  GLN A 136      -3.638   8.732  18.907  1.00 49.17           C  
ANISOU  312  CD  GLN A 136     6102   6907   5674    134   -108   2652       C  
ATOM    313  NE2 GLN A 136      -4.581   8.775  17.973  1.00 52.98           N  
ANISOU  313  NE2 GLN A 136     6626   7583   5919    415    -47   2622       N  
ATOM    314  OE1 GLN A 136      -3.146   9.746  19.403  1.00 51.28           O  
ANISOU  314  OE1 GLN A 136     6417   6845   6223    -74   -212   2836       O  
ATOM    315  N   LEU A 137       0.914   5.808  19.740  1.00 49.10           N  
ANISOU  315  N   LEU A 137     5380   7442   5832   -332    110   2828       N  
ATOM    316  CA  LEU A 137       2.374   5.856  19.755  1.00 44.61           C  
ANISOU  316  CA  LEU A 137     4603   6938   5407   -487    129   2998       C  
ATOM    317  C   LEU A 137       2.907   7.172  20.319  1.00 44.94           C  
ANISOU  317  C   LEU A 137     4662   6661   5753   -757     10   3179       C  
ATOM    318  O   LEU A 137       2.544   8.252  19.851  1.00 46.18           O  
ANISOU  318  O   LEU A 137     4899   6645   6004   -769      3   3323       O  
ATOM    319  CB  LEU A 137       2.919   5.649  18.335  1.00 43.21           C  
ANISOU  319  CB  LEU A 137     4229   7093   5097   -322    284   3139       C  
ATOM    320  CG  LEU A 137       4.421   5.842  18.073  1.00 43.25           C  
ANISOU  320  CG  LEU A 137     3996   7218   5220   -448    315   3361       C  
ATOM    321  CD1 LEU A 137       5.228   4.714  18.654  1.00 41.01           C  
ANISOU  321  CD1 LEU A 137     3580   7094   4907   -463    303   3244       C  
ATOM    322  CD2 LEU A 137       4.700   5.975  16.589  1.00 48.12           C  
ANISOU  322  CD2 LEU A 137     4453   8131   5697   -272    452   3544       C  
ATOM    323  N   ALA A 138       3.732   7.059  21.356  1.00 43.01           N  
ANISOU  323  N   ALA A 138     4339   6332   5672   -964    -91   3155       N  
ATOM    324  CA  ALA A 138       4.442   8.188  21.960  1.00 46.80           C  
ANISOU  324  CA  ALA A 138     4769   6530   6481  -1243   -219   3278       C  
ATOM    325  C   ALA A 138       3.539   9.254  22.600  1.00 49.42           C  
ANISOU  325  C   ALA A 138     5317   6449   7010  -1351   -387   3219       C  
ATOM    326  O   ALA A 138       3.986  10.375  22.877  1.00 45.33           O  
ANISOU  326  O   ALA A 138     4769   5643   6810  -1556   -492   3305       O  
ATOM    327  CB  ALA A 138       5.336   8.834  20.929  1.00 45.81           C  
ANISOU  327  CB  ALA A 138     4472   6486   6448  -1277   -112   3545       C  
ATOM    328  N   LYS A 139       2.284   8.901  22.862  1.00 45.36           N  
ANISOU  328  N   LYS A 139     5017   5901   6316  -1172   -427   2965       N  
ATOM    329  CA  LYS A 139       1.388   9.810  23.554  1.00 44.17           C  
ANISOU  329  CA  LYS A 139     5074   5397   6311  -1200   -611   2766       C  
ATOM    330  C   LYS A 139       1.243   9.421  25.019  1.00 42.60           C  
ANISOU  330  C   LYS A 139     4930   5142   6115  -1238   -781   2381       C  
ATOM    331  O   LYS A 139       1.311   8.239  25.369  1.00 36.23           O  
ANISOU  331  O   LYS A 139     4086   4578   5103  -1147   -723   2238       O  
ATOM    332  CB  LYS A 139       0.024   9.823  22.870  1.00 44.98           C  
ANISOU  332  CB  LYS A 139     5364   5525   6201   -948   -551   2703       C  
ATOM    333  CG  LYS A 139       0.045  10.355  21.454  1.00 47.96           C  
ANISOU  333  CG  LYS A 139     5705   5971   6547   -864   -400   3092       C  
ATOM    334  CD  LYS A 139       0.442  11.820  21.423  1.00 55.43           C  
ANISOU  334  CD  LYS A 139     6660   6546   7854  -1050   -483   3324       C  
ATOM    335  CE  LYS A 139      -0.600  12.706  22.096  1.00 59.68           C  
ANISOU  335  CE  LYS A 139     7436   6693   8547  -1033   -691   3118       C  
ATOM    336  NZ  LYS A 139      -0.171  14.143  22.140  1.00 66.81           N1+
ANISOU  336  NZ  LYS A 139     8342   7165   9876  -1230   -792   3323       N1+
ATOM    337  N   THR A 140       1.013  10.421  25.860  1.00 34.72           N  
ANISOU  337  N   THR A 140     5147   4620   3426   -837  -1232    430       N  
ATOM    338  CA  THR A 140       0.768  10.195  27.280  1.00 45.36           C  
ANISOU  338  CA  THR A 140     6349   5789   5096   -613  -1132    280       C  
ATOM    339  C   THR A 140      -0.357   9.205  27.525  1.00 46.25           C  
ANISOU  339  C   THR A 140     6475   5708   5391   -440  -1168    145       C  
ATOM    340  O   THR A 140      -1.451   9.349  26.994  1.00 48.49           O  
ANISOU  340  O   THR A 140     6807   5821   5797   -514  -1409    240       O  
ATOM    341  CB  THR A 140       0.402  11.488  28.008  1.00 45.02           C  
ANISOU  341  CB  THR A 140     6271   5475   5360   -657  -1296    388       C  
ATOM    342  CG2 THR A 140       0.300  11.235  29.503  1.00 44.98           C  
ANISOU  342  CG2 THR A 140     6136   5366   5589   -416  -1145    213       C  
ATOM    343  OG1 THR A 140       1.404  12.475  27.765  1.00 49.49           O  
ANISOU  343  OG1 THR A 140     6874   6164   5767   -916  -1340    558       O  
ATOM    344  N   CYS A 141      -0.084   8.203  28.345  1.00 46.27           N  
ANISOU  344  N   CYS A 141     6420   5750   5412   -237   -955    -35       N  
ATOM    345  CA  CYS A 141      -1.120   7.278  28.757  1.00 46.88           C  
ANISOU  345  CA  CYS A 141     6497   5637   5680   -136   -999   -116       C  
ATOM    346  C   CYS A 141      -1.141   7.245  30.283  1.00 46.09           C  
ANISOU  346  C   CYS A 141     6208   5485   5820     45   -842   -179       C  
ATOM    347  O   CYS A 141      -0.285   6.621  30.913  1.00 48.06           O  
ANISOU  347  O   CYS A 141     6442   5850   5966    183   -632   -291       O  
ATOM    348  CB  CYS A 141      -0.867   5.893  28.164  1.00 49.41           C  
ANISOU  348  CB  CYS A 141     7045   5994   5734    -87   -936   -265       C  
ATOM    349  SG  CYS A 141      -1.960   4.602  28.777  1.00 95.76           S  
ANISOU  349  SG  CYS A 141    12968  11607  11812    -51  -1013   -332       S  
ATOM    350  N   PRO A 142      -2.114   7.938  30.884  1.00 39.64           N  
ANISOU  350  N   PRO A 142     5245   4518   5300     79   -940    -99       N  
ATOM    351  CA  PRO A 142      -2.214   8.066  32.340  1.00 36.82           C  
ANISOU  351  CA  PRO A 142     4732   4135   5124    262   -785   -161       C  
ATOM    352  C   PRO A 142      -2.608   6.766  33.010  1.00 35.21           C  
ANISOU  352  C   PRO A 142     4469   3941   4968    346   -669   -216       C  
ATOM    353  O   PRO A 142      -3.597   6.172  32.593  1.00 35.72           O  
ANISOU  353  O   PRO A 142     4514   3938   5121    257   -801   -137       O  
ATOM    354  CB  PRO A 142      -3.325   9.109  32.529  1.00 34.20           C  
ANISOU  354  CB  PRO A 142     4284   3655   5057    331   -927    -57       C  
ATOM    355  CG  PRO A 142      -3.456   9.777  31.230  1.00 31.18           C  
ANISOU  355  CG  PRO A 142     4015   3208   4624    161  -1170     79       C  
ATOM    356  CD  PRO A 142      -3.136   8.737  30.204  1.00 33.88           C  
ANISOU  356  CD  PRO A 142     4489   3661   4721    -13  -1199     64       C  
ATOM    357  N   VAL A 143      -1.831   6.314  33.990  1.00 31.50           N  
ANISOU  357  N   VAL A 143     3986   3557   4427    472   -465   -314       N  
ATOM    358  CA  VAL A 143      -2.256   5.196  34.817  1.00 28.29           C  
ANISOU  358  CA  VAL A 143     3533   3131   4085    543   -370   -319       C  
ATOM    359  C   VAL A 143      -2.379   5.625  36.273  1.00 31.05           C  
ANISOU  359  C   VAL A 143     3717   3546   4536    692   -215   -332       C  
ATOM    360  O   VAL A 143      -1.459   6.239  36.839  1.00 23.02           O  
ANISOU  360  O   VAL A 143     2717   2607   3423    765   -127   -412       O  
ATOM    361  CB  VAL A 143      -1.288   4.026  34.730  1.00 25.92           C  
ANISOU  361  CB  VAL A 143     3414   2857   3578    605   -277   -409       C  
ATOM    362  CG1 VAL A 143      -1.679   2.957  35.742  1.00 25.18           C  
ANISOU  362  CG1 VAL A 143     3309   2699   3560    661   -203   -375       C  
ATOM    363  CG2 VAL A 143      -1.267   3.461  33.326  1.00 27.10           C  
ANISOU  363  CG2 VAL A 143     3801   2924   3572    504   -411   -441       C  
ATOM    364  N   GLN A 144      -3.486   5.250  36.906  1.00 32.74           N  
ANISOU  364  N   GLN A 144     3771   3763   4907    713   -185   -239       N  
ATOM    365  CA  GLN A 144      -3.731   5.689  38.281  1.00 32.78           C  
ANISOU  365  CA  GLN A 144     3624   3873   4958    886     -9   -256       C  
ATOM    366  C   GLN A 144      -3.425   4.641  39.327  1.00 24.75           C  
ANISOU  366  C   GLN A 144     2613   2944   3847    916    146   -240       C  
ATOM    367  O   GLN A 144      -3.852   3.482  39.229  1.00 25.51           O  
ANISOU  367  O   GLN A 144     2720   3002   3971    794    109   -122       O  
ATOM    368  CB  GLN A 144      -5.168   6.126  38.461  1.00 36.51           C  
ANISOU  368  CB  GLN A 144     3839   4398   5633    954    -16   -132       C  
ATOM    369  CG  GLN A 144      -5.548   7.360  37.724  1.00 36.22           C  
ANISOU  369  CG  GLN A 144     3787   4264   5710   1021   -161   -133       C  
ATOM    370  CD  GLN A 144      -7.019   7.578  37.845  1.00 35.86           C  
ANISOU  370  CD  GLN A 144     3417   4333   5875   1135   -168     34       C  
ATOM    371  NE2 GLN A 144      -7.527   8.633  37.227  1.00 31.88           N  
ANISOU  371  NE2 GLN A 144     2870   3738   5505   1255   -315     73       N  
ATOM    372  OE1 GLN A 144      -7.707   6.756  38.438  1.00 31.58           O  
ANISOU  372  OE1 GLN A 144     2645   3979   5375   1099    -60    168       O  
ATOM    373  N   LEU A 145      -2.678   5.076  40.337  1.00 31.20           N  
ANISOU  373  N   LEU A 145     3460   3856   4539   1051    281   -343       N  
ATOM    374  CA  LEU A 145      -2.353   4.230  41.478  1.00 29.86           C  
ANISOU  374  CA  LEU A 145     3295   3796   4253   1101    420   -308       C  
ATOM    375  C   LEU A 145      -3.285   4.543  42.656  1.00 30.20           C  
ANISOU  375  C   LEU A 145     3163   3998   4313   1211    588   -259       C  
ATOM    376  O   LEU A 145      -3.307   5.670  43.159  1.00 32.82           O  
ANISOU  376  O   LEU A 145     3497   4371   4601   1366    653   -391       O  
ATOM    377  CB  LEU A 145      -0.895   4.430  41.885  1.00 23.58           C  
ANISOU  377  CB  LEU A 145     2623   3073   3263   1161    441   -420       C  
ATOM    378  CG  LEU A 145       0.228   4.433  40.835  1.00 22.62           C  
ANISOU  378  CG  LEU A 145     2601   2928   3065   1113    337   -472       C  
ATOM    379  CD1 LEU A 145       1.585   4.673  41.519  1.00 22.62           C  
ANISOU  379  CD1 LEU A 145     2606   3113   2875   1159    365   -517       C  
ATOM    380  CD2 LEU A 145       0.259   3.144  39.991  1.00 22.78           C  
ANISOU  380  CD2 LEU A 145     2725   2842   3090   1099    290   -416       C  
ATOM    381  N   TRP A 146      -4.029   3.530  43.100  1.00 32.04           N  
ANISOU  381  N   TRP A 146     3277   4318   4581   1128    654    -66       N  
ATOM    382  CA  TRP A 146      -4.959   3.634  44.231  1.00 34.10           C  
ANISOU  382  CA  TRP A 146     3314   4831   4812   1220    860     40       C  
ATOM    383  C   TRP A 146      -4.482   2.786  45.408  1.00 35.96           C  
ANISOU  383  C   TRP A 146     3626   5192   4843   1198    980    125       C  
ATOM    384  O   TRP A 146      -4.049   1.642  45.205  1.00 32.02           O  
ANISOU  384  O   TRP A 146     3269   4559   4337   1041    871    244       O  
ATOM    385  CB  TRP A 146      -6.369   3.197  43.813  1.00 35.99           C  
ANISOU  385  CB  TRP A 146     3261   5164   5249   1071    830    293       C  
ATOM    386  CG  TRP A 146      -6.978   4.111  42.793  1.00 41.07           C  
ANISOU  386  CG  TRP A 146     3778   5741   6085   1132    709    251       C  
ATOM    387  CD1 TRP A 146      -6.648   4.203  41.460  1.00 39.64           C  
ANISOU  387  CD1 TRP A 146     3757   5308   5999   1005    462    192       C  
ATOM    388  CD2 TRP A 146      -8.018   5.061  43.011  1.00 41.68           C  
ANISOU  388  CD2 TRP A 146     3554   6021   6264   1370    827    281       C  
ATOM    389  CE2 TRP A 146      -8.274   5.704  41.780  1.00 39.47           C  
ANISOU  389  CE2 TRP A 146     3266   5565   6165   1364    605    260       C  
ATOM    390  CE3 TRP A 146      -8.764   5.445  44.131  1.00 46.49           C  
ANISOU  390  CE3 TRP A 146     3897   6964   6801   1634   1113    325       C  
ATOM    391  NE1 TRP A 146      -7.420   5.159  40.849  1.00 37.13           N  
ANISOU  391  NE1 TRP A 146     3261   5004   5843   1109    387    208       N  
ATOM    392  CZ2 TRP A 146      -9.234   6.699  41.632  1.00 45.26           C  
ANISOU  392  CZ2 TRP A 146     3739   6409   7049   1629    630    296       C  
ATOM    393  CZ3 TRP A 146      -9.725   6.434  43.984  1.00 50.20           C  
ANISOU  393  CZ3 TRP A 146     4146   7540   7390   1892   1148    310       C  
ATOM    394  CH2 TRP A 146      -9.949   7.051  42.745  1.00 49.69           C  
ANISOU  394  CH2 TRP A 146     4054   7276   7549   1924    911    313       C  
ATOM    395  N   VAL A 147      -4.521   3.352  46.621  1.00 37.79           N  
ANISOU  395  N   VAL A 147     3819   5655   4883   1379   1186     55       N  
ATOM    396  CA  VAL A 147      -4.146   2.588  47.820  1.00 39.44           C  
ANISOU  396  CA  VAL A 147     4096   6031   4858   1348   1296    173       C  
ATOM    397  C   VAL A 147      -5.108   2.794  48.995  1.00 40.72           C  
ANISOU  397  C   VAL A 147     4048   6564   4858   1459   1578    272       C  
ATOM    398  O   VAL A 147      -5.600   3.904  49.215  1.00 38.17           O  
ANISOU  398  O   VAL A 147     3643   6363   4497   1709   1724     97       O  
ATOM    399  CB  VAL A 147      -2.700   2.947  48.286  1.00 31.91           C  
ANISOU  399  CB  VAL A 147     3404   5033   3688   1439   1233    -29       C  
ATOM    400  CG1 VAL A 147      -1.664   2.405  47.317  1.00 29.50           C  
ANISOU  400  CG1 VAL A 147     3242   4487   3479   1350   1012    -41       C  
ATOM    401  CG2 VAL A 147      -2.549   4.451  48.469  1.00 32.10           C  
ANISOU  401  CG2 VAL A 147     3508   5067   3623   1622   1268   -321       C  
ATOM    402  N   ASP A 148      -5.351   1.737  49.770  1.00 42.89           N  
ANISOU  402  N   ASP A 148     4266   7021   5010   1297   1661    558       N  
ATOM    403  CA  ASP A 148      -6.165   1.863  50.980  1.00 49.74           C  
ANISOU  403  CA  ASP A 148     4927   8331   5642   1393   1970    684       C  
ATOM    404  C   ASP A 148      -5.361   2.547  52.074  1.00 50.10           C  
ANISOU  404  C   ASP A 148     5223   8494   5318   1623   2085    428       C  
ATOM    405  O   ASP A 148      -5.918   3.292  52.871  1.00 53.02           O  
ANISOU  405  O   ASP A 148     5589   9015   5542   1752   2213    289       O  
ATOM    406  CB  ASP A 148      -6.679   0.505  51.481  1.00 57.74           C  
ANISOU  406  CB  ASP A 148     5812   9519   6609   1074   2001   1132       C  
ATOM    407  CG  ASP A 148      -7.663  -0.152  50.519  1.00 62.29           C  
ANISOU  407  CG  ASP A 148     6133  10023   7511    773   1867   1424       C  
ATOM    408  OD1 ASP A 148      -8.239   0.556  49.665  1.00 62.69           O  
ANISOU  408  OD1 ASP A 148     5983  10050   7785    872   1842   1312       O  
ATOM    409  OD2 ASP A 148      -7.879  -1.380  50.638  1.00 65.19           O1-
ANISOU  409  OD2 ASP A 148     6524  10347   7900    412   1754   1787       O1-
ATOM    410  N   SER A 149      -4.053   2.296  52.098  1.00 49.81           N  
ANISOU  410  N   SER A 149     5488   8237   5202   1555   1875    336       N  
ATOM    411  CA  SER A 149      -3.158   2.889  53.094  1.00 52.52           C  
ANISOU  411  CA  SER A 149     6090   8681   5184   1688   1893    121       C  
ATOM    412  C   SER A 149      -1.840   3.368  52.452  1.00 46.93           C  
ANISOU  412  C   SER A 149     5607   7675   4549   1673   1610   -110       C  
ATOM    413  O   SER A 149      -1.285   2.711  51.576  1.00 43.67           O  
ANISOU  413  O   SER A 149     5190   7045   4359   1549   1415    -11       O  
ATOM    414  CB  SER A 149      -2.878   1.886  54.211  1.00 59.08           C  
ANISOU  414  CB  SER A 149     6984   9737   5726   1560   1936    393       C  
ATOM    415  OG  SER A 149      -4.082   1.274  54.651  1.00 65.22           O  
ANISOU  415  OG  SER A 149     7507  10806   6466   1475   2171    704       O  
ATOM    416  N   THR A 150      -1.335   4.509  52.909  1.00 46.46           N  
ANISOU  416  N   THR A 150     5759   7616   4277   1787   1579   -409       N  
ATOM    417  CA  THR A 150      -0.141   5.112  52.324  1.00 45.26           C  
ANISOU  417  CA  THR A 150     5776   7251   4171   1717   1309   -591       C  
ATOM    418  C   THR A 150       1.128   4.311  52.565  1.00 43.41           C  
ANISOU  418  C   THR A 150     5582   7079   3832   1574   1116   -433       C  
ATOM    419  O   THR A 150       1.567   4.174  53.709  1.00 45.25           O  
ANISOU  419  O   THR A 150     5935   7523   3733   1558   1110   -396       O  
ATOM    420  CB  THR A 150       0.070   6.543  52.853  1.00 49.95           C  
ANISOU  420  CB  THR A 150     6652   7791   4534   1805   1269   -927       C  
ATOM    421  CG2 THR A 150       1.287   7.180  52.208  1.00 51.03           C  
ANISOU  421  CG2 THR A 150     6933   7735   4721   1636    957  -1049       C  
ATOM    422  OG1 THR A 150      -1.084   7.332  52.541  1.00 51.44           O  
ANISOU  422  OG1 THR A 150     6798   7816   4932   1924   1378  -1037       O  
ATOM    423  N   PRO A 151       1.745   3.817  51.472  1.00 37.09           N  
ANISOU  423  N   PRO A 151     4684   6117   3290   1501    955   -341       N  
ATOM    424  CA  PRO A 151       3.008   3.084  51.542  1.00 37.02           C  
ANISOU  424  CA  PRO A 151     4664   6183   3217   1457    777   -189       C  
ATOM    425  C   PRO A 151       4.151   3.950  52.063  1.00 41.95           C  
ANISOU  425  C   PRO A 151     5386   6958   3597   1370    590   -314       C  
ATOM    426  O   PRO A 151       4.153   5.163  51.828  1.00 44.82           O  
ANISOU  426  O   PRO A 151     5854   7231   3946   1299    529   -545       O  
ATOM    427  CB  PRO A 151       3.246   2.654  50.093  1.00 34.04           C  
ANISOU  427  CB  PRO A 151     4179   5604   3153   1468    699   -148       C  
ATOM    428  CG  PRO A 151       2.450   3.548  49.281  1.00 34.67           C  
ANISOU  428  CG  PRO A 151     4246   5516   3411   1442    750   -325       C  
ATOM    429  CD  PRO A 151       1.253   3.924  50.088  1.00 33.95           C  
ANISOU  429  CD  PRO A 151     4180   5485   3235   1496    941   -375       C  
ATOM    430  N   PRO A 152       5.111   3.325  52.767  1.00 41.11           N  
ANISOU  430  N   PRO A 152     5258   7065   3298   1354    461   -136       N  
ATOM    431  CA  PRO A 152       6.258   3.998  53.399  1.00 45.43           C  
ANISOU  431  CA  PRO A 152     5861   7827   3573   1209    226   -181       C  
ATOM    432  C   PRO A 152       7.115   4.747  52.393  1.00 43.97           C  
ANISOU  432  C   PRO A 152     5562   7615   3530   1071     40   -256       C  
ATOM    433  O   PRO A 152       7.146   4.383  51.214  1.00 38.56           O  
ANISOU  433  O   PRO A 152     4704   6821   3127   1149     87   -203       O  
ATOM    434  CB  PRO A 152       7.072   2.845  54.003  1.00 45.56           C  
ANISOU  434  CB  PRO A 152     5766   8073   3471   1280    121    126       C  
ATOM    435  CG  PRO A 152       6.148   1.671  54.030  1.00 46.45           C  
ANISOU  435  CG  PRO A 152     5890   8047   3712   1438    323    299       C  
ATOM    436  CD  PRO A 152       5.209   1.860  52.870  1.00 40.76           C  
ANISOU  436  CD  PRO A 152     5133   7038   3315   1468    481    158       C  
ATOM    437  N   PRO A 153       7.787   5.803  52.852  1.00 46.51           N  
ANISOU  437  N   PRO A 153     6008   8037   3627    832   -182   -372       N  
ATOM    438  CA  PRO A 153       8.717   6.556  52.012  1.00 46.55           C  
ANISOU  438  CA  PRO A 153     5886   8083   3718    600   -404   -371       C  
ATOM    439  C   PRO A 153       9.815   5.651  51.475  1.00 45.15           C  
ANISOU  439  C   PRO A 153     5305   8210   3639    674   -472    -75       C  
ATOM    440  O   PRO A 153      10.201   4.694  52.150  1.00 40.44           O  
ANISOU  440  O   PRO A 153     4600   7829   2938    830   -483    124       O  
ATOM    441  CB  PRO A 153       9.275   7.612  52.968  1.00 55.21           C  
ANISOU  441  CB  PRO A 153     7241   9263   4472    284   -687   -487       C  
ATOM    442  CG  PRO A 153       8.213   7.766  54.015  1.00 56.46           C  
ANISOU  442  CG  PRO A 153     7771   9271   4412    430   -520   -705       C  
ATOM    443  CD  PRO A 153       7.654   6.388  54.196  1.00 52.83           C  
ANISOU  443  CD  PRO A 153     7123   8907   4042    733   -250   -514       C  
ATOM    444  N   GLY A 154      10.294   5.928  50.267  1.00 43.42           N  
ANISOU  444  N   GLY A 154     4871   8021   3605    602   -504    -32       N  
ATOM    445  CA  GLY A 154      11.281   5.063  49.658  1.00 41.82           C  
ANISOU  445  CA  GLY A 154     4269   8139   3481    773   -503    224       C  
ATOM    446  C   GLY A 154      10.625   4.025  48.778  1.00 42.26           C  
ANISOU  446  C   GLY A 154     4308   7970   3780   1140   -240    217       C  
ATOM    447  O   GLY A 154      11.315   3.305  48.051  1.00 47.33           O  
ANISOU  447  O   GLY A 154     4689   8798   4496   1369   -189    365       O  
ATOM    448  N   THR A 155       9.299   3.927  48.857  1.00 36.46           N  
ANISOU  448  N   THR A 155     3853   6853   3146   1205    -81     52       N  
ATOM    449  CA  THR A 155       8.571   3.028  47.965  1.00 39.55           C  
ANISOU  449  CA  THR A 155     4279   6984   3763   1451    108     41       C  
ATOM    450  C   THR A 155       8.824   3.407  46.499  1.00 38.80           C  
ANISOU  450  C   THR A 155     4062   6876   3806   1418    128    -10       C  
ATOM    451  O   THR A 155       8.940   4.585  46.164  1.00 36.76           O  
ANISOU  451  O   THR A 155     3797   6639   3531   1147     37    -92       O  
ATOM    452  CB  THR A 155       7.044   3.058  48.211  1.00 36.97           C  
ANISOU  452  CB  THR A 155     4199   6320   3530   1437    248    -92       C  
ATOM    453  CG2 THR A 155       6.310   2.120  47.240  1.00 31.88           C  
ANISOU  453  CG2 THR A 155     3597   5406   3112   1600    372    -72       C  
ATOM    454  OG1 THR A 155       6.754   2.662  49.557  1.00 40.48           O  
ANISOU  454  OG1 THR A 155     4751   6826   3803   1465    271    -20       O  
ATOM    455  N   ARG A 156       8.912   2.405  45.634  1.00 39.39           N  
ANISOU  455  N   ARG A 156     5450   5640   3879    210   -960    136       N  
ATOM    456  CA  ARG A 156       9.146   2.637  44.214  1.00 39.43           C  
ANISOU  456  CA  ARG A 156     5392   5539   4052     60   -850    132       C  
ATOM    457  C   ARG A 156       8.091   1.906  43.374  1.00 36.86           C  
ANISOU  457  C   ARG A 156     4896   5299   3811    275   -697    277       C  
ATOM    458  O   ARG A 156       7.485   0.925  43.836  1.00 28.11           O  
ANISOU  458  O   ARG A 156     3599   4350   2732    456   -702    389       O  
ATOM    459  CB  ARG A 156      10.586   2.241  43.823  1.00 31.85           C  
ANISOU  459  CB  ARG A 156     4142   4649   3309   -252   -949     89       C  
ATOM    460  CG  ARG A 156      11.628   3.287  44.286  1.00 34.75           C  
ANISOU  460  CG  ARG A 156     4701   4892   3611   -551  -1090    -64       C  
ATOM    461  CD  ARG A 156      13.036   2.750  44.598  1.00 35.89           C  
ANISOU  461  CD  ARG A 156     4514   5224   3899   -814  -1266    -73       C  
ATOM    462  NE  ARG A 156      13.579   1.781  43.643  1.00 41.68           N  
ANISOU  462  NE  ARG A 156     4851   6098   4887   -852  -1189     49       N  
ATOM    463  CZ  ARG A 156      14.438   2.081  42.665  1.00 42.67           C  
ANISOU  463  CZ  ARG A 156     4862   6175   5177  -1079  -1140     62       C  
ATOM    464  NH1 ARG A 156      14.833   3.331  42.477  1.00 37.04           N1+
ANISOU  464  NH1 ARG A 156     4386   5256   4431  -1317  -1156    -30       N1+
ATOM    465  NH2 ARG A 156      14.896   1.126  41.867  1.00 33.66           N  
ANISOU  465  NH2 ARG A 156     3383   5173   4233  -1056  -1056    178       N  
ATOM    466  N   VAL A 157       7.832   2.449  42.178  1.00 37.44           N  
ANISOU  466  N   VAL A 157     5053   5264   3908    258   -562    282       N  
ATOM    467  CA  VAL A 157       6.817   1.945  41.243  1.00 36.17           C  
ANISOU  467  CA  VAL A 157     4761   5193   3789    434   -435    395       C  
ATOM    468  C   VAL A 157       7.453   1.535  39.923  1.00 34.05           C  
ANISOU  468  C   VAL A 157     4277   4949   3713    275   -393    371       C  
ATOM    469  O   VAL A 157       7.915   2.393  39.168  1.00 34.86           O  
ANISOU  469  O   VAL A 157     4515   4924   3807    165   -321    328       O  
ATOM    470  CB  VAL A 157       5.723   3.020  40.915  1.00 32.86           C  
ANISOU  470  CB  VAL A 157     4654   4674   3157    644   -281    457       C  
ATOM    471  CG1 VAL A 157       4.616   2.430  40.034  1.00 31.33           C  
ANISOU  471  CG1 VAL A 157     4273   4646   2984    823   -187    590       C  
ATOM    472  CG2 VAL A 157       5.139   3.656  42.183  1.00 31.46           C  
ANISOU  472  CG2 VAL A 157     4780   4431   2743    837   -284    477       C  
ATOM    473  N   ARG A 158       7.445   0.240  39.619  1.00 32.05           N  
ANISOU  473  N   ARG A 158     3711   4843   3625    282   -418    407       N  
ATOM    474  CA  ARG A 158       8.078  -0.263  38.397  1.00 28.67           C  
ANISOU  474  CA  ARG A 158     3094   4442   3357    166   -373    375       C  
ATOM    475  C   ARG A 158       7.047  -0.703  37.352  1.00 31.86           C  
ANISOU  475  C   ARG A 158     3427   4929   3749    301   -290    411       C  
ATOM    476  O   ARG A 158       6.001  -1.260  37.697  1.00 35.06           O  
ANISOU  476  O   ARG A 158     3766   5425   4130    439   -308    477       O  
ATOM    477  CB  ARG A 158       9.007  -1.424  38.735  1.00 30.04           C  
ANISOU  477  CB  ARG A 158     2991   4697   3724     64   -451    368       C  
ATOM    478  CG  ARG A 158       9.865  -1.940  37.574  1.00 31.76           C  
ANISOU  478  CG  ARG A 158     3035   4936   4097    -37   -390    341       C  
ATOM    479  CD  ARG A 158      10.771  -3.074  38.057  1.00 32.09           C  
ANISOU  479  CD  ARG A 158     2821   5059   4313    -89   -443    369       C  
ATOM    480  NE  ARG A 158      11.483  -2.716  39.288  1.00 32.22           N  
ANISOU  480  NE  ARG A 158     2836   5105   4301   -181   -560    387       N  
ATOM    481  CZ  ARG A 158      12.649  -2.078  39.314  1.00 34.39           C  
ANISOU  481  CZ  ARG A 158     3094   5377   4596   -372   -604    373       C  
ATOM    482  NH1 ARG A 158      13.236  -1.733  38.175  1.00 34.46           N1+
ANISOU  482  NH1 ARG A 158     3081   5345   4669   -467   -510    370       N1+
ATOM    483  NH2 ARG A 158      13.233  -1.791  40.474  1.00 35.81           N  
ANISOU  483  NH2 ARG A 158     3267   5613   4728   -470   -745    372       N  
ATOM    484  N   ALA A 159       7.335  -0.432  36.081  1.00 32.57           N  
ANISOU  484  N   ALA A 159     3522   5009   3846    260   -205    377       N  
ATOM    485  CA  ALA A 159       6.498  -0.904  34.972  1.00 34.01           C  
ANISOU  485  CA  ALA A 159     3619   5304   3997    365   -153    383       C  
ATOM    486  C   ALA A 159       7.320  -1.787  34.037  1.00 33.44           C  
ANISOU  486  C   ALA A 159     3368   5264   4073    273   -139    305       C  
ATOM    487  O   ALA A 159       8.453  -1.446  33.676  1.00 29.24           O  
ANISOU  487  O   ALA A 159     2842   4669   3597    170    -91    286       O  
ATOM    488  CB  ALA A 159       5.883   0.276  34.188  1.00 31.50           C  
ANISOU  488  CB  ALA A 159     3503   4985   3481    483    -35    432       C  
ATOM    489  N   MET A 160       6.740  -2.910  33.626  1.00 34.56           N  
ANISOU  489  N   MET A 160     3360   5497   4275    311   -174    266       N  
ATOM    490  CA  MET A 160       7.460  -3.854  32.775  1.00 32.83           C  
ANISOU  490  CA  MET A 160     3014   5284   4178    257   -149    176       C  
ATOM    491  C   MET A 160       6.520  -4.489  31.758  1.00 33.48           C  
ANISOU  491  C   MET A 160     3053   5468   4199    318   -163     99       C  
ATOM    492  O   MET A 160       5.342  -4.726  32.046  1.00 32.73           O  
ANISOU  492  O   MET A 160     2922   5447   4065    358   -232    128       O  
ATOM    493  CB  MET A 160       8.139  -4.932  33.624  1.00 29.16           C  
ANISOU  493  CB  MET A 160     2396   4766   3920    190   -196    176       C  
ATOM    494  CG  MET A 160       8.919  -5.957  32.816  1.00 29.42           C  
ANISOU  494  CG  MET A 160     2324   4778   4075    173   -139     98       C  
ATOM    495  SD  MET A 160       9.545  -7.302  33.835  1.00 46.50           S  
ANISOU  495  SD  MET A 160     4313   6880   6474    150   -158    139       S  
ATOM    496  CE  MET A 160      10.577  -6.398  35.002  1.00 23.67           C  
ANISOU  496  CE  MET A 160     1399   4014   3582     80   -195    260       C  
ATOM    497  N   ALA A 161       7.028  -4.729  30.552  1.00 35.26           N  
ANISOU  497  N   ALA A 161     3280   5717   4400    328    -99      8       N  
ATOM    498  CA  ALA A 161       6.195  -5.335  29.512  1.00 32.17           C  
ANISOU  498  CA  ALA A 161     2869   5438   3918    371   -136   -104       C  
ATOM    499  C   ALA A 161       6.559  -6.791  29.265  1.00 30.48           C  
ANISOU  499  C   ALA A 161     2572   5146   3864    312   -160   -242       C  
ATOM    500  O   ALA A 161       7.715  -7.173  29.383  1.00 30.21           O  
ANISOU  500  O   ALA A 161     2515   5006   3958    297    -86   -244       O  
ATOM    501  CB  ALA A 161       6.297  -4.545  28.229  1.00 30.47           C  
ANISOU  501  CB  ALA A 161     2754   5329   3495    472    -44   -119       C  
ATOM    502  N   ILE A 162       5.546  -7.610  29.002  1.00 29.25           N  
ANISOU  502  N   ILE A 162     2367   5037   3708    274   -263   -340       N  
ATOM    503  CA  ILE A 162       5.743  -8.985  28.567  1.00 30.52           C  
ANISOU  503  CA  ILE A 162     2510   5092   3996    214   -279   -509       C  
ATOM    504  C   ILE A 162       4.688  -9.283  27.507  1.00 35.88           C  
ANISOU  504  C   ILE A 162     3209   5909   4514    189   -386   -667       C  
ATOM    505  O   ILE A 162       3.650  -8.617  27.462  1.00 38.14           O  
ANISOU  505  O   ILE A 162     3455   6384   4652    204   -467   -594       O  
ATOM    506  CB  ILE A 162       5.639 -10.015  29.711  1.00 31.61           C  
ANISOU  506  CB  ILE A 162     2543   5070   4398    123   -317   -469       C  
ATOM    507  CG1 ILE A 162       4.243  -9.995  30.326  1.00 33.49           C  
ANISOU  507  CG1 ILE A 162     2683   5398   4646     60   -442   -387       C  
ATOM    508  CG2 ILE A 162       6.670  -9.749  30.788  1.00 29.44           C  
ANISOU  508  CG2 ILE A 162     2226   4710   4249    155   -235   -312       C  
ATOM    509  CD1 ILE A 162       3.959 -11.215  31.147  1.00 35.83           C  
ANISOU  509  CD1 ILE A 162     2872   5538   5205    -37   -474   -367       C  
ATOM    510  N   TYR A 163       4.963 -10.265  26.653  1.00 36.49           N  
ANISOU  510  N   TYR A 163     3356   5907   4603    164   -386   -878       N  
ATOM    511  CA  TYR A 163       4.013 -10.732  25.645  1.00 37.40           C  
ANISOU  511  CA  TYR A 163     3500   6144   4566    102   -523  -1079       C  
ATOM    512  C   TYR A 163       2.916 -11.572  26.298  1.00 43.51           C  
ANISOU  512  C   TYR A 163     4146   6870   5518    -95   -681  -1097       C  
ATOM    513  O   TYR A 163       3.196 -12.393  27.189  1.00 41.15           O  
ANISOU  513  O   TYR A 163     3804   6335   5496   -175   -646  -1061       O  
ATOM    514  CB  TYR A 163       4.724 -11.550  24.558  1.00 39.17           C  
ANISOU  514  CB  TYR A 163     3888   6261   4733    146   -465  -1326       C  
ATOM    515  CG  TYR A 163       5.576 -10.726  23.606  1.00 44.64           C  
ANISOU  515  CG  TYR A 163     4692   7075   5192    356   -321  -1309       C  
ATOM    516  CD1 TYR A 163       4.996  -9.801  22.737  1.00 46.44           C  
ANISOU  516  CD1 TYR A 163     4939   7590   5116    453   -363  -1300       C  
ATOM    517  CD2 TYR A 163       6.962 -10.875  23.571  1.00 46.98           C  
ANISOU  517  CD2 TYR A 163     5056   7220   5573    475   -126  -1269       C  
ATOM    518  CE1 TYR A 163       5.770  -9.047  21.864  1.00 49.23           C  
ANISOU  518  CE1 TYR A 163     5388   8049   5269    660   -205  -1253       C  
ATOM    519  CE2 TYR A 163       7.745 -10.122  22.704  1.00 48.77           C  
ANISOU  519  CE2 TYR A 163     5358   7564   5607    667     23  -1215       C  
ATOM    520  CZ  TYR A 163       7.144  -9.215  21.855  1.00 50.78           C  
ANISOU  520  CZ  TYR A 163     5643   8077   5574    757    -12  -1209       C  
ATOM    521  OH  TYR A 163       7.921  -8.477  20.997  1.00 51.99           O  
ANISOU  521  OH  TYR A 163     5866   8340   5550    960    160  -1126       O  
ATOM    522  N   LYS A 164       1.671 -11.344  25.869  1.00 46.19           N  
ANISOU  522  N   LYS A 164     4399   7451   5698   -163   -845  -1119       N  
ATOM    523  CA  LYS A 164       0.509 -11.985  26.480  1.00 47.75           C  
ANISOU  523  CA  LYS A 164     4422   7661   6058   -360  -1000  -1078       C  
ATOM    524  C   LYS A 164       0.390 -13.485  26.184  1.00 50.72           C  
ANISOU  524  C   LYS A 164     4840   7809   6623   -580  -1088  -1331       C  
ATOM    525  O   LYS A 164       0.015 -14.274  27.059  1.00 49.72           O  
ANISOU  525  O   LYS A 164     4604   7506   6783   -736  -1117  -1263       O  
ATOM    526  CB  LYS A 164      -0.776 -11.299  26.020  1.00 48.63           C  
ANISOU  526  CB  LYS A 164     4400   8150   5928   -365  -1152  -1006       C  
ATOM    527  CG  LYS A 164      -2.026 -11.917  26.625  1.00 46.70           C  
ANISOU  527  CG  LYS A 164     3926   7966   5853   -576  -1315   -920       C  
ATOM    528  CD  LYS A 164      -3.282 -11.277  26.087  1.00 46.57           C  
ANISOU  528  CD  LYS A 164     3742   8375   5578   -569  -1467   -829       C  
ATOM    529  CE  LYS A 164      -4.523 -11.850  26.743  1.00 45.70           C  
ANISOU  529  CE  LYS A 164     3413   8282   5667   -762  -1588   -667       C  
ATOM    530  NZ  LYS A 164      -5.747 -11.298  26.096  1.00 46.65           N1+
ANISOU  530  NZ  LYS A 164     3466   8699   5559   -722  -1679   -548       N1+
ATOM    531  N   GLN A 165       0.682 -13.873  24.947  1.00 51.28           N  
ANISOU  531  N   GLN A 165     5086   7872   6525   -584  -1122  -1619       N  
ATOM    532  CA  GLN A 165       0.570 -15.272  24.542  1.00 51.85           C  
ANISOU  532  CA  GLN A 165     5265   7694   6740   -793  -1205  -1907       C  
ATOM    533  C   GLN A 165       1.705 -16.051  25.173  1.00 50.60           C  
ANISOU  533  C   GLN A 165     5231   7134   6860   -737   -998  -1900       C  
ATOM    534  O   GLN A 165       2.840 -15.581  25.207  1.00 42.24           O  
ANISOU  534  O   GLN A 165     4261   6039   5750   -510   -808  -1816       O  
ATOM    535  CB  GLN A 165       0.592 -15.397  23.015  1.00 47.78           C  
ANISOU  535  CB  GLN A 165     4944   7303   5907   -771  -1295  -2232       C  
ATOM    536  CG  GLN A 165      -0.453 -14.535  22.353  1.00 48.61           C  
ANISOU  536  CG  GLN A 165     4909   7869   5693   -774  -1484  -2204       C  
ATOM    537  CD  GLN A 165      -0.227 -14.349  20.868  1.00 71.55           C  
ANISOU  537  CD  GLN A 165     8007  10967   8212   -643  -1524  -2460       C  
ATOM    538  NE2 GLN A 165      -0.778 -15.245  20.060  1.00 78.28           N  
ANISOU  538  NE2 GLN A 165     8951  11819   8974   -851  -1733  -2797       N  
ATOM    539  OE1 GLN A 165       0.423 -13.394  20.451  1.00 69.57           O  
ANISOU  539  OE1 GLN A 165     7826  10868   7739   -361  -1370  -2353       O  
ATOM    540  N   SER A 166       1.386 -17.239  25.676  1.00 54.03           N  
ANISOU  540  N   SER A 166     5654   7279   7596   -946  -1029  -1965       N  
ATOM    541  CA  SER A 166       2.337 -18.048  26.433  1.00 53.96           C  
ANISOU  541  CA  SER A 166     5728   6894   7880   -881   -818  -1901       C  
ATOM    542  C   SER A 166       3.548 -18.487  25.607  1.00 55.87           C  
ANISOU  542  C   SER A 166     6261   6941   8027   -704   -648  -2109       C  
ATOM    543  O   SER A 166       4.640 -18.655  26.154  1.00 58.88           O  
ANISOU  543  O   SER A 166     6679   7151   8542   -523   -427  -1969       O  
ATOM    544  CB  SER A 166       1.629 -19.262  27.038  1.00 55.66           C  
ANISOU  544  CB  SER A 166     5884   6825   8438  -1147   -876  -1925       C  
ATOM    545  OG  SER A 166       1.029 -20.057  26.033  1.00 64.02           O  
ANISOU  545  OG  SER A 166     7094   7782   9449  -1381  -1039  -2274       O  
ATOM    546  N   GLN A 167       3.366 -18.684  24.304  1.00 57.61           N  
ANISOU  546  N   GLN A 167     6678   7209   8002   -736   -747  -2427       N  
ATOM    547  CA  GLN A 167       4.476 -19.122  23.458  1.00 62.18           C  
ANISOU  547  CA  GLN A 167     7556   7612   8457   -529   -569  -2623       C  
ATOM    548  C   GLN A 167       5.427 -17.972  23.083  1.00 56.12           C  
ANISOU  548  C   GLN A 167     6782   7100   7439   -218   -423  -2469       C  
ATOM    549  O   GLN A 167       6.347 -18.148  22.286  1.00 55.22           O  
ANISOU  549  O   GLN A 167     6886   6922   7174     -4   -266  -2587       O  
ATOM    550  CB  GLN A 167       3.955 -19.827  22.201  1.00 72.84           C  
ANISOU  550  CB  GLN A 167     9161   8900   9614   -664   -725  -3046       C  
ATOM    551  CG  GLN A 167       3.285 -18.954  21.148  1.00 81.30           C  
ANISOU  551  CG  GLN A 167    10204  10403  10284   -664   -934  -3173       C  
ATOM    552  CD  GLN A 167       1.782 -18.816  21.362  1.00 88.90           C  
ANISOU  552  CD  GLN A 167    10920  11585  11272   -985  -1238  -3167       C  
ATOM    553  NE2 GLN A 167       1.067 -18.452  20.298  1.00 91.23           N  
ANISOU  553  NE2 GLN A 167    11229  12214  11220  -1040  -1458  -3364       N  
ATOM    554  OE1 GLN A 167       1.265 -19.086  22.454  1.00 90.41           O  
ANISOU  554  OE1 GLN A 167    10902  11663  11786  -1173  -1270  -2977       O  
ATOM    555  N   HIS A 168       5.202 -16.796  23.655  1.00 51.55           N  
ANISOU  555  N   HIS A 168     5965   6800   6822   -190   -461  -2197       N  
ATOM    556  CA  HIS A 168       6.086 -15.667  23.406  1.00 49.36           C  
ANISOU  556  CA  HIS A 168     5669   6728   6357     60   -319  -2025       C  
ATOM    557  C   HIS A 168       6.625 -15.028  24.687  1.00 48.25           C  
ANISOU  557  C   HIS A 168     5331   6595   6409    111   -213  -1684       C  
ATOM    558  O   HIS A 168       7.406 -14.072  24.619  1.00 46.65           O  
ANISOU  558  O   HIS A 168     5095   6532   6099    274    -97  -1521       O  
ATOM    559  CB  HIS A 168       5.359 -14.604  22.587  1.00 43.17           C  
ANISOU  559  CB  HIS A 168     4848   6313   5243     84   -457  -2052       C  
ATOM    560  CG  HIS A 168       5.046 -15.033  21.191  1.00 50.22           C  
ANISOU  560  CG  HIS A 168     5944   7279   5858     97   -550  -2379       C  
ATOM    561  CD2 HIS A 168       3.876 -15.075  20.511  1.00 51.82           C  
ANISOU  561  CD2 HIS A 168     6140   7688   5861    -51   -793  -2572       C  
ATOM    562  ND1 HIS A 168       6.014 -15.494  20.327  1.00 50.93           N  
ANISOU  562  ND1 HIS A 168     6279   7248   5823    295   -389  -2542       N  
ATOM    563  CE1 HIS A 168       5.452 -15.801  19.170  1.00 55.48           C  
ANISOU  563  CE1 HIS A 168     7023   7937   6119    272   -532  -2848       C  
ATOM    564  NE2 HIS A 168       4.158 -15.554  19.254  1.00 54.70           N  
ANISOU  564  NE2 HIS A 168     6764   8049   5970     49   -792  -2876       N  
ATOM    565  N   MET A 169       6.242 -15.565  25.845  1.00 47.00           N  
ANISOU  565  N   MET A 169     4875   6465   6519    600   -202  -1126       N  
ATOM    566  CA  MET A 169       6.519 -14.879  27.108  1.00 46.66           C  
ANISOU  566  CA  MET A 169     4616   6538   6576    664    -18  -1003       C  
ATOM    567  C   MET A 169       8.009 -14.732  27.406  1.00 47.25           C  
ANISOU  567  C   MET A 169     4728   6651   6573    814    166  -1052       C  
ATOM    568  O   MET A 169       8.410 -13.714  27.971  1.00 47.30           O  
ANISOU  568  O   MET A 169     4646   6794   6531    820    298   -973       O  
ATOM    569  CB  MET A 169       5.848 -15.595  28.281  1.00 46.75           C  
ANISOU  569  CB  MET A 169     4499   6482   6781    551    -72   -866       C  
ATOM    570  CG  MET A 169       4.350 -15.386  28.353  1.00 51.50           C  
ANISOU  570  CG  MET A 169     4920   7166   7483    416   -192   -663       C  
ATOM    571  SD  MET A 169       3.668 -15.739  29.985  1.00 64.62           S  
ANISOU  571  SD  MET A 169     6357   8844   9352    356   -138   -430       S  
ATOM    572  CE  MET A 169       1.953 -15.946  29.578  1.00 59.68           C  
ANISOU  572  CE  MET A 169     5509   8335   8832    172   -368   -129       C  
ATOM    573  N   THR A 170       8.830 -15.710  27.007  1.00 46.67           N  
ANISOU  573  N   THR A 170     4810   6460   6464    929    184  -1141       N  
ATOM    574  CA  THR A 170      10.256 -15.666  27.341  1.00 44.54           C  
ANISOU  574  CA  THR A 170     4486   6292   6146   1086    366  -1068       C  
ATOM    575  C   THR A 170      11.026 -14.650  26.501  1.00 41.56           C  
ANISOU  575  C   THR A 170     4107   6106   5578   1186    460  -1073       C  
ATOM    576  O   THR A 170      12.103 -14.220  26.885  1.00 42.30           O  
ANISOU  576  O   THR A 170     4073   6383   5616   1228    576   -920       O  
ATOM    577  CB  THR A 170      10.930 -17.034  27.169  1.00 37.33           C  
ANISOU  577  CB  THR A 170     3728   5195   5259   1271    433  -1089       C  
ATOM    578  CG2 THR A 170      10.321 -18.048  28.096  1.00 37.80           C  
ANISOU  578  CG2 THR A 170     3785   5068   5510   1158    339  -1050       C  
ATOM    579  OG1 THR A 170      10.768 -17.472  25.821  1.00 40.97           O  
ANISOU  579  OG1 THR A 170     4510   5484   5573   1370    403  -1279       O  
ATOM    580  N   GLU A 171      10.459 -14.245  25.373  1.00 42.59           N  
ANISOU  580  N   GLU A 171     4359   6223   5601   1182    384  -1206       N  
ATOM    581  CA  GLU A 171      11.105 -13.267  24.511  1.00 44.37           C  
ANISOU  581  CA  GLU A 171     4583   6632   5645   1266    459  -1207       C  
ATOM    582  C   GLU A 171      10.982 -11.884  25.160  1.00 49.15           C  
ANISOU  582  C   GLU A 171     5042   7396   6238   1120    481  -1091       C  
ATOM    583  O   GLU A 171       9.918 -11.513  25.654  1.00 55.93           O  
ANISOU  583  O   GLU A 171     5869   8196   7184   1000    428  -1076       O  
ATOM    584  CB  GLU A 171      10.476 -13.304  23.112  1.00 44.57           C  
ANISOU  584  CB  GLU A 171     4806   6586   5542   1277    356  -1374       C  
ATOM    585  CG  GLU A 171      11.045 -12.323  22.094  1.00 49.60           C  
ANISOU  585  CG  GLU A 171     5449   7413   5985   1364    420  -1381       C  
ATOM    586  CD  GLU A 171      10.523 -12.591  20.667  1.00 55.95           C  
ANISOU  586  CD  GLU A 171     6503   8132   6624   1366    313  -1548       C  
ATOM    587  OE1 GLU A 171       9.923 -13.664  20.427  1.00 57.95           O  
ANISOU  587  OE1 GLU A 171     6991   8153   6874   1298    196  -1663       O  
ATOM    588  OE2 GLU A 171      10.724 -11.737  19.780  1.00 57.20           O1-
ANISOU  588  OE2 GLU A 171     6656   8448   6628   1398    329  -1553       O1-
ATOM    589  N   VAL A 172      12.079 -11.138  25.205  1.00 45.43           N  
ANISOU  589  N   VAL A 172     4506   7116   5639   1129    572   -969       N  
ATOM    590  CA  VAL A 172      12.053  -9.815  25.815  1.00 40.88           C  
ANISOU  590  CA  VAL A 172     3922   6624   4985    949    592   -868       C  
ATOM    591  C   VAL A 172      11.361  -8.801  24.897  1.00 41.37           C  
ANISOU  591  C   VAL A 172     4065   6690   4962    958    573   -947       C  
ATOM    592  O   VAL A 172      11.712  -8.673  23.723  1.00 44.17           O  
ANISOU  592  O   VAL A 172     4433   7139   5210   1061    559   -997       O  
ATOM    593  CB  VAL A 172      13.473  -9.302  26.140  1.00 36.79           C  
ANISOU  593  CB  VAL A 172     3332   6327   4319    857    638   -656       C  
ATOM    594  CG1 VAL A 172      13.408  -7.886  26.695  1.00 34.88           C  
ANISOU  594  CG1 VAL A 172     3227   6097   3927    609    637   -579       C  
ATOM    595  CG2 VAL A 172      14.149 -10.209  27.142  1.00 36.72           C  
ANISOU  595  CG2 VAL A 172     3191   6362   4399    826    655   -491       C  
ATOM    596  N   VAL A 173      10.357  -8.107  25.424  1.00 38.37           N  
ANISOU  596  N   VAL A 173     3741   6210   4628    883    599   -928       N  
ATOM    597  CA  VAL A 173       9.718  -7.025  24.685  1.00 38.25           C  
ANISOU  597  CA  VAL A 173     3786   6205   4542    915    622   -926       C  
ATOM    598  C   VAL A 173      10.636  -5.813  24.599  1.00 40.38           C  
ANISOU  598  C   VAL A 173     4178   6561   4602    828    683   -855       C  
ATOM    599  O   VAL A 173      11.023  -5.239  25.625  1.00 38.69           O  
ANISOU  599  O   VAL A 173     4111   6293   4295    670    752   -767       O  
ATOM    600  CB  VAL A 173       8.389  -6.590  25.327  1.00 38.19           C  
ANISOU  600  CB  VAL A 173     3801   6068   4643    933    707   -845       C  
ATOM    601  CG1 VAL A 173       7.766  -5.451  24.533  1.00 37.65           C  
ANISOU  601  CG1 VAL A 173     3771   6020   4513   1017    767   -779       C  
ATOM    602  CG2 VAL A 173       7.426  -7.788  25.475  1.00 36.77           C  
ANISOU  602  CG2 VAL A 173     3461   5840   4671    956    604   -844       C  
ATOM    603  N   ARG A 174      10.984  -5.432  23.370  1.00 45.62           N  
ANISOU  603  N   ARG A 174     4817   7356   5162    892    641   -880       N  
ATOM    604  CA  ARG A 174      11.843  -4.271  23.116  1.00 46.76           C  
ANISOU  604  CA  ARG A 174     5061   7607   5098    786    665   -783       C  
ATOM    605  C   ARG A 174      11.359  -3.520  21.880  1.00 41.29           C  
ANISOU  605  C   ARG A 174     4379   6959   4349    882    654   -809       C  
ATOM    606  O   ARG A 174      10.517  -4.019  21.146  1.00 38.38           O  
ANISOU  606  O   ARG A 174     3915   6585   4082   1009    601   -890       O  
ATOM    607  CB  ARG A 174      13.298  -4.686  22.930  1.00 49.94           C  
ANISOU  607  CB  ARG A 174     5340   8238   5399    748    621   -685       C  
ATOM    608  CG  ARG A 174      13.489  -5.762  21.881  1.00 53.40           C  
ANISOU  608  CG  ARG A 174     5634   8773   5882    984    606   -780       C  
ATOM    609  CD  ARG A 174      14.948  -5.883  21.455  1.00 61.87           C  
ANISOU  609  CD  ARG A 174     6571  10119   6818   1037    640   -603       C  
ATOM    610  NE  ARG A 174      15.818  -6.434  22.490  1.00 71.01           N  
ANISOU  610  NE  ARG A 174     7602  11367   8011    962    664   -401       N  
ATOM    611  CZ  ARG A 174      15.893  -7.728  22.796  1.00 75.95           C  
ANISOU  611  CZ  ARG A 174     8154  11929   8774   1132    722   -426       C  
ATOM    612  NH1 ARG A 174      15.121  -8.604  22.160  1.00 78.77           N1+
ANISOU  612  NH1 ARG A 174     8617  12091   9219   1345    742   -675       N1+
ATOM    613  NH2 ARG A 174      16.724  -8.144  23.750  1.00 73.98           N  
ANISOU  613  NH2 ARG A 174     7748  11802   8558   1055    743   -177       N  
ATOM    614  N   ARG A 175      11.864  -2.310  21.668  1.00 40.70           N  
ANISOU  614  N   ARG A 175     4438   6928   4099    779    680   -714       N  
ATOM    615  CA  ARG A 175      11.500  -1.546  20.474  1.00 39.91           C  
ANISOU  615  CA  ARG A 175     4335   6891   3940    866    669   -708       C  
ATOM    616  C   ARG A 175      12.076  -2.198  19.232  1.00 35.08           C  
ANISOU  616  C   ARG A 175     3539   6514   3275    966    572   -766       C  
ATOM    617  O   ARG A 175      13.150  -2.792  19.281  1.00 35.77           O  
ANISOU  617  O   ARG A 175     3543   6747   3302    961    560   -735       O  
ATOM    618  CB  ARG A 175      11.998  -0.109  20.574  1.00 39.76           C  
ANISOU  618  CB  ARG A 175     4549   6834   3723    707    714   -581       C  
ATOM    619  CG  ARG A 175      11.324   0.686  21.652  1.00 37.56           C  
ANISOU  619  CG  ARG A 175     4597   6244   3430    652    872   -538       C  
ATOM    620  CD  ARG A 175      11.994   2.024  21.769  1.00 40.12           C  
ANISOU  620  CD  ARG A 175     5268   6481   3495    429    892   -425       C  
ATOM    621  NE  ARG A 175      11.465   3.060  20.906  1.00 41.22           N  
ANISOU  621  NE  ARG A 175     5511   6554   3595    552    968   -372       N  
ATOM    622  CZ  ARG A 175      12.092   4.207  20.679  1.00 42.59           C  
ANISOU  622  CZ  ARG A 175     5962   6680   3538    359    948   -269       C  
ATOM    623  NH1 ARG A 175      13.279   4.438  21.225  1.00 38.18           N1+
ANISOU  623  NH1 ARG A 175     5581   6170   2754     -9    820   -184       N1+
ATOM    624  NH2 ARG A 175      11.536   5.120  19.901  1.00 43.63           N  
ANISOU  624  NH2 ARG A 175     6183   6734   3659    506   1037   -206       N  
ATOM    625  N   CYS A 176      11.355  -2.058  18.126  1.00 33.40           N  
ANISOU  625  N   CYS A 176     3280   6344   3068   1068    526   -811       N  
ATOM    626  CA  CYS A 176      11.767  -2.595  16.833  1.00 41.54           C  
ANISOU  626  CA  CYS A 176     4234   7560   3990   1163    454   -886       C  
ATOM    627  C   CYS A 176      13.005  -1.854  16.339  1.00 35.56           C  
ANISOU  627  C   CYS A 176     3458   7019   3036   1133    479   -766       C  
ATOM    628  O   CYS A 176      13.267  -0.730  16.760  1.00 36.34           O  
ANISOU  628  O   CYS A 176     3630   7103   3075    990    500   -628       O  
ATOM    629  CB  CYS A 176      10.626  -2.478  15.812  1.00 46.55           C  
ANISOU  629  CB  CYS A 176     4844   8202   4640   1195    362   -916       C  
ATOM    630  SG  CYS A 176      10.497  -0.857  15.071  1.00 45.17           S  
ANISOU  630  SG  CYS A 176     4669   8128   4364   1172    380   -754       S  
ATOM    631  N   PRO A 177      13.766  -2.474  15.438  1.00 35.68           N  
ANISOU  631  N   PRO A 177     3410   7221   2924   1263    489   -793       N  
ATOM    632  CA  PRO A 177      15.011  -1.853  14.971  1.00 44.08           C  
ANISOU  632  CA  PRO A 177     4388   8558   3803   1253    523   -602       C  
ATOM    633  C   PRO A 177      14.860  -0.410  14.490  1.00 36.55           C  
ANISOU  633  C   PRO A 177     3468   7662   2755   1116    467   -492       C  
ATOM    634  O   PRO A 177      15.709   0.424  14.787  1.00 41.13           O  
ANISOU  634  O   PRO A 177     4034   8364   3228    949    453   -280       O  
ATOM    635  CB  PRO A 177      15.433  -2.763  13.819  1.00 47.22           C  
ANISOU  635  CB  PRO A 177     4773   9097   4070   1501    590   -683       C  
ATOM    636  CG  PRO A 177      14.877  -4.106  14.201  1.00 49.33           C  
ANISOU  636  CG  PRO A 177     5150   9135   4460   1606    610   -886       C  
ATOM    637  CD  PRO A 177      13.565  -3.821  14.872  1.00 36.65           C  
ANISOU  637  CD  PRO A 177     3588   7297   3042   1431    492   -972       C  
ATOM    638  N   HIS A 178      13.796  -0.111  13.765  1.00 40.40           N  
ANISOU  638  N   HIS A 178     4006   8072   3273   1156    418   -592       N  
ATOM    639  CA  HIS A 178      13.600   1.249  13.286  1.00 41.49           C  
ANISOU  639  CA  HIS A 178     4182   8244   3338   1065    389   -464       C  
ATOM    640  C   HIS A 178      13.497   2.267  14.420  1.00 43.10           C  
ANISOU  640  C   HIS A 178     4560   8232   3583    891    434   -348       C  
ATOM    641  O   HIS A 178      14.242   3.244  14.447  1.00 43.61           O  
ANISOU  641  O   HIS A 178     4713   8358   3500    724    416   -181       O  
ATOM    642  CB  HIS A 178      12.360   1.312  12.403  1.00 37.20           C  
ANISOU  642  CB  HIS A 178     3620   7667   2849   1141    331   -529       C  
ATOM    643  CG  HIS A 178      11.828   2.690  12.200  1.00 37.57           C  
ANISOU  643  CG  HIS A 178     3714   7659   2902   1091    344   -367       C  
ATOM    644  CD2 HIS A 178      10.655   3.257  12.574  1.00 46.53           C  
ANISOU  644  CD2 HIS A 178     4895   8595   4191   1127    403   -280       C  
ATOM    645  ND1 HIS A 178      12.511   3.658  11.501  1.00 47.68           N  
ANISOU  645  ND1 HIS A 178     5000   9100   4015   1029    325   -232       N  
ATOM    646  CE1 HIS A 178      11.792   4.766  11.458  1.00 38.83           C  
ANISOU  646  CE1 HIS A 178     3966   7845   2944   1021    366    -96       C  
ATOM    647  NE2 HIS A 178      10.660   4.543  12.105  1.00 51.06           N  
ANISOU  647  NE2 HIS A 178     5536   9176   4689   1109    438   -110       N  
ATOM    648  N   HIS A 179      12.594   2.016  15.364  1.00 44.27           N  
ANISOU  648  N   HIS A 179     4802   8116   3902    914    496   -421       N  
ATOM    649  CA  HIS A 179      12.351   2.946  16.464  1.00 43.33           C  
ANISOU  649  CA  HIS A 179     4959   7720   3785    791    597   -337       C  
ATOM    650  C   HIS A 179      13.554   3.000  17.371  1.00 42.27           C  
ANISOU  650  C   HIS A 179     4943   7607   3512    541    562   -259       C  
ATOM    651  O   HIS A 179      13.941   4.067  17.837  1.00 42.06           O  
ANISOU  651  O   HIS A 179     5209   7450   3322    313    570   -133       O  
ATOM    652  CB  HIS A 179      11.088   2.554  17.261  1.00 42.96           C  
ANISOU  652  CB  HIS A 179     4956   7421   3946    923    708   -400       C  
ATOM    653  CG  HIS A 179       9.809   2.978  16.604  1.00 44.72           C  
ANISOU  653  CG  HIS A 179     5104   7602   4285   1110    767   -319       C  
ATOM    654  CD2 HIS A 179       9.373   4.197  16.210  1.00 44.59           C  
ANISOU  654  CD2 HIS A 179     5213   7500   4231   1176    869   -159       C  
ATOM    655  ND1 HIS A 179       8.800   2.093  16.298  1.00 36.32           N  
ANISOU  655  ND1 HIS A 179     3799   6603   3398   1235    712   -340       N  
ATOM    656  CE1 HIS A 179       7.805   2.747  15.724  1.00 37.64           C  
ANISOU  656  CE1 HIS A 179     3886   6780   3636   1359    762   -157       C  
ATOM    657  NE2 HIS A 179       8.128   4.023  15.662  1.00 43.90           N  
ANISOU  657  NE2 HIS A 179     4896   7472   4312   1362    883    -51       N  
ATOM    658  N   GLU A 180      14.156   1.843  17.597  1.00 35.46           N  
ANISOU  658  N   GLU A 180     3874   6907   2693    562    515   -300       N  
ATOM    659  CA  GLU A 180      15.362   1.763  18.395  1.00 42.08           C  
ANISOU  659  CA  GLU A 180     4717   7861   3411    318    457   -138       C  
ATOM    660  C   GLU A 180      16.379   2.764  17.881  1.00 47.92           C  
ANISOU  660  C   GLU A 180     5476   8814   3916     94    361    104       C  
ATOM    661  O   GLU A 180      17.120   3.366  18.652  1.00 53.10           O  
ANISOU  661  O   GLU A 180     6307   9466   4403   -263    276    306       O  
ATOM    662  CB  GLU A 180      15.914   0.337  18.349  1.00 43.05           C  
ANISOU  662  CB  GLU A 180     4539   8194   3624    480    458   -157       C  
ATOM    663  CG  GLU A 180      17.221   0.104  19.076  1.00 48.37           C  
ANISOU  663  CG  GLU A 180     5092   9087   4200    270    403    110       C  
ATOM    664  CD  GLU A 180      17.758  -1.299  18.828  1.00 58.75           C  
ANISOU  664  CD  GLU A 180     6105  10607   5611    546    475    131       C  
ATOM    665  OE1 GLU A 180      17.200  -2.020  17.968  1.00 57.72           O  
ANISOU  665  OE1 GLU A 180     5936  10430   5564    862    551    -92       O  
ATOM    666  OE2 GLU A 180      18.729  -1.688  19.507  1.00 69.10           O1-
ANISOU  666  OE2 GLU A 180     7249  12111   6894    434    459    395       O1-
ATOM    667  N   ARG A 181      16.380   2.957  16.565  1.00 52.58           N  
ANISOU  667  N   ARG A 181     4287  10848   4844  -1558     99  -1044       N  
ATOM    668  CA  ARG A 181      17.358   3.809  15.904  1.00 56.32           C  
ANISOU  668  CA  ARG A 181     4703  11701   4997  -1850    241  -1060       C  
ATOM    669  C   ARG A 181      16.828   5.242  15.719  1.00 54.78           C  
ANISOU  669  C   ARG A 181     4666  11467   4683  -2108    100   -414       C  
ATOM    670  O   ARG A 181      17.522   6.107  15.190  1.00 46.24           O  
ANISOU  670  O   ARG A 181     3603  10656   3310  -2411    142   -332       O  
ATOM    671  CB  ARG A 181      17.771   3.194  14.563  1.00 61.08           C  
ANISOU  671  CB  ARG A 181     5190  12901   5116  -2215    412  -1499       C  
ATOM    672  CG  ARG A 181      18.983   3.844  13.969  1.00 68.32           C  
ANISOU  672  CG  ARG A 181     6021  14165   5774  -2495    524  -1674       C  
ATOM    673  CD  ARG A 181      19.401   3.200  12.688  1.00 80.24           C  
ANISOU  673  CD  ARG A 181     7361  16151   6974  -2891    644  -2151       C  
ATOM    674  NE  ARG A 181      19.945   1.849  12.825  1.00 86.65           N  
ANISOU  674  NE  ARG A 181     7942  16909   8074  -2568    813  -2798       N  
ATOM    675  CZ  ARG A 181      21.244   1.558  12.762  1.00 91.64           C  
ANISOU  675  CZ  ARG A 181     8353  17617   8850  -2431   1000  -3257       C  
ATOM    676  NH1 ARG A 181      22.133   2.527  12.583  1.00 92.04           N1+
ANISOU  676  NH1 ARG A 181     8357  17857   8755  -2640   1064  -3157       N1+
ATOM    677  NH2 ARG A 181      21.656   0.302  12.885  1.00 94.12           N  
ANISOU  677  NH2 ARG A 181     8500  17798   9465  -2078   1111  -3790       N  
ATOM    678  N   CYS A 182      15.600   5.494  16.168  1.00 50.65           N  
ANISOU  678  N   CYS A 182     4246  10589   4408  -1984    -97     28       N  
ATOM    679  CA  CYS A 182      14.958   6.787  15.941  1.00 51.18           C  
ANISOU  679  CA  CYS A 182     4421  10602   4422  -2195   -275    644       C  
ATOM    680  C   CYS A 182      15.573   7.899  16.779  1.00 54.75           C  
ANISOU  680  C   CYS A 182     4923  10821   5059  -2107   -259    826       C  
ATOM    681  O   CYS A 182      16.198   7.651  17.814  1.00 57.71           O  
ANISOU  681  O   CYS A 182     5268  10945   5714  -1811   -146    566       O  
ATOM    682  CB  CYS A 182      13.466   6.698  16.258  1.00 49.30           C  
ANISOU  682  CB  CYS A 182     4211  10031   4490  -2021   -481   1020       C  
ATOM    683  SG  CYS A 182      12.467   6.222  14.840  1.00 71.56           S  
ANISOU  683  SG  CYS A 182     7063  13156   6971  -2393   -647   1209       S  
ATOM    684  N   SER A 183      15.408   9.133  16.322  1.00 57.22           N  
ANISOU  684  N   SER A 183     5337  11204   5201  -2408   -412   1295       N  
ATOM    685  CA  SER A 183      15.902  10.275  17.072  1.00 59.61           C  
ANISOU  685  CA  SER A 183     5736  11252   5663  -2384   -424   1512       C  
ATOM    686  C   SER A 183      14.771  10.848  17.904  1.00 59.85           C  
ANISOU  686  C   SER A 183     5807  10795   6140  -2138   -549   1983       C  
ATOM    687  O   SER A 183      14.326  11.972  17.657  1.00 64.72           O  
ANISOU  687  O   SER A 183     6553  11249   6786  -2276   -736   2461       O  
ATOM    688  CB  SER A 183      16.461  11.341  16.133  1.00 64.08           C  
ANISOU  688  CB  SER A 183     6423  12089   5837  -2858   -557   1704       C  
ATOM    689  OG  SER A 183      17.713  10.941  15.616  1.00 68.13           O  
ANISOU  689  OG  SER A 183     6865  13014   6007  -3053   -372   1224       O  
ATOM    690  N   ASP A 184      14.300  10.077  18.881  1.00 51.79           N  
ANISOU  690  N   ASP A 184     4701   9478   5499  -1744   -456   1813       N  
ATOM    691  CA  ASP A 184      13.182  10.519  19.694  1.00 50.23           C  
ANISOU  691  CA  ASP A 184     4544   8794   5748  -1452   -508   2183       C  
ATOM    692  C   ASP A 184      13.511  10.446  21.175  1.00 46.01           C  
ANISOU  692  C   ASP A 184     4154   7809   5521  -1124   -317   1971       C  
ATOM    693  O   ASP A 184      12.618  10.477  22.026  1.00 45.08           O  
ANISOU  693  O   ASP A 184     4110   7251   5767   -811   -264   2086       O  
ATOM    694  CB  ASP A 184      11.923   9.703  19.369  1.00 50.92           C  
ANISOU  694  CB  ASP A 184     4451   8915   5981  -1322   -634   2249       C  
ATOM    695  CG  ASP A 184      12.098   8.210  19.614  1.00 52.52           C  
ANISOU  695  CG  ASP A 184     4644   9163   6148  -1161   -517   1694       C  
ATOM    696  OD1 ASP A 184      13.110   7.790  20.226  1.00 50.40           O  
ANISOU  696  OD1 ASP A 184     4418   8862   5870  -1074   -369   1298       O  
ATOM    697  OD2 ASP A 184      11.208   7.451  19.174  1.00 54.05           O1-
ANISOU  697  OD2 ASP A 184     4797   9402   6340  -1141   -606   1681       O1-
ATOM    698  N   SER A 185      14.798  10.322  21.470  1.00 43.37           N  
ANISOU  698  N   SER A 185     3841   7608   5028  -1231   -215   1654       N  
ATOM    699  CA  SER A 185      15.250  10.277  22.842  1.00 44.12           C  
ANISOU  699  CA  SER A 185     4116   7298   5351  -1012   -101   1477       C  
ATOM    700  C   SER A 185      14.858  11.553  23.599  1.00 44.40           C  
ANISOU  700  C   SER A 185     4490   6807   5574   -938    -52   1850       C  
ATOM    701  O   SER A 185      14.864  12.650  23.041  1.00 31.96           O  
ANISOU  701  O   SER A 185     3027   5241   3874  -1138   -120   2195       O  
ATOM    702  CB  SER A 185      16.758  10.068  22.891  1.00 44.64           C  
ANISOU  702  CB  SER A 185     4085   7653   5223  -1187    -64   1141       C  
ATOM    703  OG  SER A 185      17.221  10.122  24.228  1.00 48.15           O  
ANISOU  703  OG  SER A 185     4742   7687   5866  -1039    -29   1039       O  
ATOM    704  N   ASP A 186      14.501  11.388  24.872  1.00 37.52           N  
ANISOU  704  N   ASP A 186     3825   5447   4985   -670     69   1769       N  
ATOM    705  CA  ASP A 186      14.211  12.518  25.746  1.00 37.64           C  
ANISOU  705  CA  ASP A 186     4221   4907   5174   -586    189   2019       C  
ATOM    706  C   ASP A 186      15.412  12.769  26.643  1.00 46.41           C  
ANISOU  706  C   ASP A 186     5614   5857   6164   -741    226   1850       C  
ATOM    707  O   ASP A 186      15.349  13.569  27.577  1.00 51.98           O  
ANISOU  707  O   ASP A 186     6738   6081   6931   -679    334   1848       O  
ATOM    708  CB  ASP A 186      12.966  12.270  26.580  1.00 38.38           C  
ANISOU  708  CB  ASP A 186     4390   4568   5624   -251    356   2038       C  
ATOM    709  CG  ASP A 186      13.100  11.073  27.507  1.00 41.97           C  
ANISOU  709  CG  ASP A 186     4883   4936   6127   -160    420   1663       C  
ATOM    710  OD1 ASP A 186      14.018  10.242  27.335  1.00 41.63           O  
ANISOU  710  OD1 ASP A 186     4714   5199   5905   -274    283   1382       O  
ATOM    711  OD2 ASP A 186      12.256  10.960  28.419  1.00 48.75           O1-
ANISOU  711  OD2 ASP A 186     5902   5404   7216     24    611   1647       O1-
ATOM    712  N   GLY A 187      16.481  12.014  26.403  1.00 45.43           N  
ANISOU  712  N   GLY A 187     5260   6144   5855   -891    124   1551       N  
ATOM    713  CA  GLY A 187      17.716  12.167  27.149  1.00 45.99           C  
ANISOU  713  CA  GLY A 187     5489   6156   5828  -1068     84   1403       C  
ATOM    714  C   GLY A 187      17.806  11.269  28.366  1.00 40.86           C  
ANISOU  714  C   GLY A 187     4981   5194   5351   -892     66   1136       C  
ATOM    715  O   GLY A 187      18.844  11.203  29.008  1.00 36.25           O  
ANISOU  715  O   GLY A 187     4483   4576   4715  -1031    -44   1003       O  
ATOM    716  N   LEU A 188      16.736  10.544  28.666  1.00 39.28           N  
ANISOU  716  N   LEU A 188     4796   4785   5342   -628    137   1071       N  
ATOM    717  CA  LEU A 188      16.748   9.702  29.851  1.00 40.19           C  
ANISOU  717  CA  LEU A 188     5133   4564   5575   -527    100    851       C  
ATOM    718  C   LEU A 188      16.554   8.242  29.500  1.00 40.90           C  
ANISOU  718  C   LEU A 188     4920   4884   5735   -359    -27    570       C  
ATOM    719  O   LEU A 188      17.266   7.382  30.024  1.00 43.98           O  
ANISOU  719  O   LEU A 188     5322   5231   6156   -338   -220    315       O  
ATOM    720  CB  LEU A 188      15.677  10.153  30.852  1.00 36.54           C  
ANISOU  720  CB  LEU A 188     5102   3535   5249   -438    338    995       C  
ATOM    721  CG  LEU A 188      15.886  11.587  31.347  1.00 36.84           C  
ANISOU  721  CG  LEU A 188     5481   3386   5131   -575    352   1106       C  
ATOM    722  CD1 LEU A 188      14.747  12.008  32.270  1.00 38.59           C  
ANISOU  722  CD1 LEU A 188     5820   3417   5427   -413    432   1013       C  
ATOM    723  CD2 LEU A 188      17.267  11.765  32.019  1.00 31.72           C  
ANISOU  723  CD2 LEU A 188     4910   2707   4435   -724    287   1035       C  
ATOM    724  N   ALA A 189      15.623   7.962  28.592  1.00 35.82           N  
ANISOU  724  N   ALA A 189     4020   4469   5119   -254     35    627       N  
ATOM    725  CA  ALA A 189      15.287   6.580  28.279  1.00 34.58           C  
ANISOU  725  CA  ALA A 189     3662   4470   5006   -125    -75    371       C  
ATOM    726  C   ALA A 189      16.297   5.936  27.330  1.00 37.44           C  
ANISOU  726  C   ALA A 189     3663   5319   5243   -155   -227     88       C  
ATOM    727  O   ALA A 189      16.747   6.558  26.363  1.00 39.49           O  
ANISOU  727  O   ALA A 189     3695   5975   5336   -305   -185    163       O  
ATOM    728  CB  ALA A 189      13.901   6.499  27.689  1.00 35.14           C  
ANISOU  728  CB  ALA A 189     3600   4611   5139    -54     24    547       C  
ATOM    729  N   PRO A 190      16.670   4.680  27.627  1.00 34.42           N  
ANISOU  729  N   PRO A 190     3253   4885   4941    -24   -398   -254       N  
ATOM    730  CA  PRO A 190      17.482   3.858  26.735  1.00 34.06           C  
ANISOU  730  CA  PRO A 190     2849   5253   4840     30   -498   -611       C  
ATOM    731  C   PRO A 190      16.732   3.690  25.430  1.00 37.75           C  
ANISOU  731  C   PRO A 190     3103   6103   5138    -37   -398   -586       C  
ATOM    732  O   PRO A 190      15.504   3.557  25.464  1.00 37.00           O  
ANISOU  732  O   PRO A 190     3136   5852   5071    -24   -371   -400       O  
ATOM    733  CB  PRO A 190      17.604   2.521  27.485  1.00 29.22           C  
ANISOU  733  CB  PRO A 190     2381   4313   4408    234   -728   -912       C  
ATOM    734  CG  PRO A 190      17.334   2.846  28.882  1.00 25.65           C  
ANISOU  734  CG  PRO A 190     2360   3332   4053    197   -777   -710       C  
ATOM    735  CD  PRO A 190      16.318   3.950  28.853  1.00 28.51           C  
ANISOU  735  CD  PRO A 190     2852   3642   4340     71   -507   -332       C  
ATOM    736  N   PRO A 191      17.452   3.707  24.299  1.00 40.18           N  
ANISOU  736  N   PRO A 191     3180   6839   5245   -142   -322   -733       N  
ATOM    737  CA  PRO A 191      16.862   3.640  22.950  1.00 42.21           C  
ANISOU  737  CA  PRO A 191     3360   7426   5251   -294   -234   -680       C  
ATOM    738  C   PRO A 191      15.999   2.399  22.688  1.00 41.38           C  
ANISOU  738  C   PRO A 191     3288   7278   5155   -200   -317   -859       C  
ATOM    739  O   PRO A 191      15.035   2.512  21.932  1.00 28.07           O  
ANISOU  739  O   PRO A 191     1590   5753   3324   -353   -312   -652       O  
ATOM    740  CB  PRO A 191      18.087   3.633  22.031  1.00 45.10           C  
ANISOU  740  CB  PRO A 191     3558   8182   5397   -403   -120   -947       C  
ATOM    741  CG  PRO A 191      19.205   4.211  22.866  1.00 43.79           C  
ANISOU  741  CG  PRO A 191     3369   7899   5372   -371   -132   -947       C  
ATOM    742  CD  PRO A 191      18.918   3.790  24.270  1.00 37.38           C  
ANISOU  742  CD  PRO A 191     2705   6621   4875   -147   -304   -942       C  
ATOM    743  N   GLN A 192      16.333   1.257  23.296  1.00 39.80           N  
ANISOU  743  N   GLN A 192     3145   6854   5124     23   -434  -1216       N  
ATOM    744  CA  GLN A 192      15.575   0.019  23.098  1.00 41.51           C  
ANISOU  744  CA  GLN A 192     3429   7003   5340     85   -555  -1430       C  
ATOM    745  C   GLN A 192      14.275  -0.071  23.907  1.00 38.21           C  
ANISOU  745  C   GLN A 192     3211   6251   5057     78   -661  -1157       C  
ATOM    746  O   GLN A 192      13.394  -0.876  23.571  1.00 26.33           O  
ANISOU  746  O   GLN A 192     1788   4736   3479     12   -740  -1192       O  
ATOM    747  CB  GLN A 192      16.404  -1.214  23.445  1.00 51.09           C  
ANISOU  747  CB  GLN A 192     4671   8027   6713    346   -696  -1931       C  
ATOM    748  CG  GLN A 192      17.585  -1.490  22.570  1.00 62.89           C  
ANISOU  748  CG  GLN A 192     5897   9878   8120    406   -571  -2347       C  
ATOM    749  CD  GLN A 192      18.223  -2.821  22.915  1.00 72.81           C  
ANISOU  749  CD  GLN A 192     7147  10887   9631    741   -768  -2874       C  
ATOM    750  NE2 GLN A 192      18.534  -3.023  24.198  1.00 72.04           N  
ANISOU  750  NE2 GLN A 192     7255  10287   9831    939   -999  -2810       N  
ATOM    751  OE1 GLN A 192      18.417  -3.670  22.038  1.00 80.38           O  
ANISOU  751  OE1 GLN A 192     7936  12087  10519    807   -743  -3351       O  
ATOM    752  N   HIS A 193      14.165   0.722  24.975  1.00 34.36           N  
ANISOU  752  N   HIS A 193     2874   5446   4736    116   -618   -880       N  
ATOM    753  CA  HIS A 193      13.048   0.581  25.917  1.00 35.01           C  
ANISOU  753  CA  HIS A 193     3219   5132   4951    114   -624   -665       C  
ATOM    754  C   HIS A 193      11.671   1.008  25.359  1.00 30.17           C  
ANISOU  754  C   HIS A 193     2479   4684   4302    -23   -522   -310       C  
ATOM    755  O   HIS A 193      11.471   2.159  24.916  1.00 27.80           O  
ANISOU  755  O   HIS A 193     2013   4559   3989    -81   -403      5       O  
ATOM    756  CB  HIS A 193      13.344   1.378  27.190  1.00 33.15           C  
ANISOU  756  CB  HIS A 193     3214   4517   4865    156   -550   -502       C  
ATOM    757  CG  HIS A 193      14.194   0.644  28.173  1.00 39.13           C  
ANISOU  757  CG  HIS A 193     4225   4925   5719    253   -754   -769       C  
ATOM    758  CD2 HIS A 193      15.173  -0.271  27.993  1.00 43.25           C  
ANISOU  758  CD2 HIS A 193     4682   5476   6276    387   -981  -1136       C  
ATOM    759  ND1 HIS A 193      14.054   0.794  29.534  1.00 38.19           N  
ANISOU  759  ND1 HIS A 193     4490   4336   5686    210   -764   -661       N  
ATOM    760  CE1 HIS A 193      14.923   0.019  30.153  1.00 38.37           C  
ANISOU  760  CE1 HIS A 193     4692   4109   5777    283  -1050   -903       C  
ATOM    761  NE2 HIS A 193      15.613  -0.640  29.241  1.00 42.65           N  
ANISOU  761  NE2 HIS A 193     4937   4935   6332    432  -1192  -1196       N  
ATOM    762  N   LEU A 194      10.720   0.079  25.405  1.00 24.27           N  
ANISOU  762  N   LEU A 194     1809   3858   3555    -87   -607   -339       N  
ATOM    763  CA  LEU A 194       9.343   0.378  24.972  1.00 27.23           C  
ANISOU  763  CA  LEU A 194     2003   4387   3955   -219   -554     10       C  
ATOM    764  C   LEU A 194       8.633   1.390  25.871  1.00 25.61           C  
ANISOU  764  C   LEU A 194     1805   3926   3999   -150   -336    348       C  
ATOM    765  O   LEU A 194       8.052   2.340  25.382  1.00 26.65           O  
ANISOU  765  O   LEU A 194     1692   4214   4219   -150   -257    689       O  
ATOM    766  CB  LEU A 194       8.516  -0.895  24.926  1.00 24.92           C  
ANISOU  766  CB  LEU A 194     1805   4064   3600   -356   -701   -108       C  
ATOM    767  CG  LEU A 194       7.030  -0.708  24.619  1.00 30.78           C  
ANISOU  767  CG  LEU A 194     2312   4969   4415   -517   -677    259       C  
ATOM    768  CD1 LEU A 194       6.818  -0.042  23.249  1.00 33.21           C  
ANISOU  768  CD1 LEU A 194     2292   5721   4607   -624   -748    515       C  
ATOM    769  CD2 LEU A 194       6.304  -2.044  24.701  1.00 27.61           C  
ANISOU  769  CD2 LEU A 194     2061   4515   3916   -718   -838    119       C  
ATOM    770  N   ILE A 195       8.693   1.201  27.185  1.00 30.70           N  
ANISOU  770  N   ILE A 195     3598   5679   2388   -611   -799    174       N  
ATOM    771  CA  ILE A 195       7.946   2.061  28.095  1.00 31.38           C  
ANISOU  771  CA  ILE A 195     3612   5623   2689   -439   -907    250       C  
ATOM    772  C   ILE A 195       8.807   3.168  28.718  1.00 32.17           C  
ANISOU  772  C   ILE A 195     3904   5446   2873   -445   -793    447       C  
ATOM    773  O   ILE A 195       9.830   2.904  29.341  1.00 31.27           O  
ANISOU  773  O   ILE A 195     3788   5236   2858   -605   -593    423       O  
ATOM    774  CB  ILE A 195       7.284   1.238  29.246  1.00 39.50           C  
ANISOU  774  CB  ILE A 195     4338   6670   4000   -472   -837     35       C  
ATOM    775  CG1 ILE A 195       6.582  -0.003  28.692  1.00 33.43           C  
ANISOU  775  CG1 ILE A 195     3365   6110   3227   -566   -913   -192       C  
ATOM    776  CG2 ILE A 195       6.298   2.106  30.070  1.00 25.51           C  
ANISOU  776  CG2 ILE A 195     2434   4846   2413   -265   -916     27       C  
ATOM    777  CD1 ILE A 195       5.971  -0.858  29.760  1.00 29.12           C  
ANISOU  777  CD1 ILE A 195     2578   5521   2965   -670   -781   -340       C  
ATOM    778  N   ARG A 196       8.369   4.410  28.538  1.00 35.26           N  
ANISOU  778  N   ARG A 196     4453   5685   3258   -258   -962    626       N  
ATOM    779  CA  ARG A 196       8.983   5.573  29.177  1.00 31.51           C  
ANISOU  779  CA  ARG A 196     4167   4875   2931   -258   -900    768       C  
ATOM    780  C   ARG A 196       8.020   6.205  30.180  1.00 33.33           C  
ANISOU  780  C   ARG A 196     4276   4964   3425     -2  -1006    637       C  
ATOM    781  O   ARG A 196       6.815   5.929  30.145  1.00 33.61           O  
ANISOU  781  O   ARG A 196     4079   5174   3516    202  -1150    501       O  
ATOM    782  CB  ARG A 196       9.369   6.629  28.134  1.00 31.53           C  
ANISOU  782  CB  ARG A 196     4534   4701   2747   -264   -984   1107       C  
ATOM    783  CG  ARG A 196      10.395   6.194  27.110  1.00 32.15           C  
ANISOU  783  CG  ARG A 196     4757   4945   2514   -542   -794   1236       C  
ATOM    784  CD  ARG A 196      10.742   7.343  26.165  1.00 36.57           C  
ANISOU  784  CD  ARG A 196     5733   5309   2853   -601   -832   1640       C  
ATOM    785  NE  ARG A 196      11.559   6.877  25.048  1.00 38.25           N  
ANISOU  785  NE  ARG A 196     6078   5787   2668   -865   -607   1742       N  
ATOM    786  CZ  ARG A 196      11.988   7.650  24.063  1.00 42.80           C  
ANISOU  786  CZ  ARG A 196     6979   6255   3029   -948   -511   2031       C  
ATOM    787  NH1 ARG A 196      11.685   8.943  24.050  1.00 51.22           N1+
ANISOU  787  NH1 ARG A 196     8341   6933   4187   -835   -686   2354       N1+
ATOM    788  NH2 ARG A 196      12.721   7.129  23.093  1.00 44.72           N  
ANISOU  788  NH2 ARG A 196     7240   6754   2996  -1121   -225   1973       N  
ATOM    789  N   VAL A 197       8.554   7.043  31.070  1.00 34.76           N  
ANISOU  789  N   VAL A 197     4580   4848   3778    -23   -926    627       N  
ATOM    790  CA  VAL A 197       7.740   7.941  31.894  1.00 37.13           C  
ANISOU  790  CA  VAL A 197     4845   4948   4313    255  -1014    482       C  
ATOM    791  C   VAL A 197       8.165   9.379  31.614  1.00 40.19           C  
ANISOU  791  C   VAL A 197     5589   4872   4808    320  -1127    689       C  
ATOM    792  O   VAL A 197       9.361   9.675  31.621  1.00 33.39           O  
ANISOU  792  O   VAL A 197     4932   3823   3931     34  -1008    813       O  
ATOM    793  CB  VAL A 197       7.894   7.665  33.414  1.00 30.19           C  
ANISOU  793  CB  VAL A 197     3828   4108   3535    175   -817    195       C  
ATOM    794  CG1 VAL A 197       7.133   8.717  34.238  1.00 31.66           C  
ANISOU  794  CG1 VAL A 197     4008   4082   3938    469   -859    -22       C  
ATOM    795  CG2 VAL A 197       7.441   6.249  33.769  1.00 26.40           C  
ANISOU  795  CG2 VAL A 197     3050   4014   2967     76   -689     50       C  
ATOM    796  N   GLU A 198       7.216  10.277  31.364  1.00 40.51           N  
ANISOU  796  N   GLU A 198     5691   4696   5004    687  -1365    728       N  
ATOM    797  CA  GLU A 198       7.593  11.664  31.091  1.00 48.11           C  
ANISOU  797  CA  GLU A 198     7054   5108   6117    750  -1496    962       C  
ATOM    798  C   GLU A 198       7.290  12.568  32.280  1.00 51.66           C  
ANISOU  798  C   GLU A 198     7503   5202   6925    968  -1492    645       C  
ATOM    799  O   GLU A 198       6.451  12.237  33.135  1.00 51.80           O  
ANISOU  799  O   GLU A 198     7188   5447   7045   1185  -1430    268       O  
ATOM    800  CB  GLU A 198       6.880  12.213  29.860  1.00 56.94           C  
ANISOU  800  CB  GLU A 198     8367   6101   7169   1043  -1836   1303       C  
ATOM    801  CG  GLU A 198       5.388  12.271  30.018  1.00 64.28           C  
ANISOU  801  CG  GLU A 198     8976   7146   8301   1550  -2090   1079       C  
ATOM    802  CD  GLU A 198       4.731  13.038  28.909  1.00 76.29           C  
ANISOU  802  CD  GLU A 198    10731   8440   9816   1912  -2530   1435       C  
ATOM    803  OE1 GLU A 198       5.467  13.613  28.078  1.00 82.42           O  
ANISOU  803  OE1 GLU A 198    12004   8913  10400   1737  -2599   1896       O  
ATOM    804  OE2 GLU A 198       3.484  13.060  28.862  1.00 80.41           O1-
ANISOU  804  OE2 GLU A 198    10932   9101  10520   2364  -2810   1267       O1-
ATOM    805  N   GLY A 199       8.015  13.684  32.355  1.00 52.27           N  
ANISOU  805  N   GLY A 199     7951   4726   7182    863  -1520    769       N  
ATOM    806  CA  GLY A 199       7.761  14.701  33.360  1.00 52.38           C  
ANISOU  806  CA  GLY A 199     8045   4300   7558   1085  -1554    441       C  
ATOM    807  C   GLY A 199       8.135  14.302  34.765  1.00 48.82           C  
ANISOU  807  C   GLY A 199     7403   4058   7089    908  -1310    -23       C  
ATOM    808  O   GLY A 199       7.436  14.655  35.711  1.00 52.02           O  
ANISOU  808  O   GLY A 199     7687   4417   7663   1195  -1281   -445       O  
ATOM    809  N   ASN A 200       9.211  13.525  34.883  1.00 45.88           N  
ANISOU  809  N   ASN A 200     6991   3953   6486    460  -1141     48       N  
ATOM    810  CA  ASN A 200       9.759  13.083  36.163  1.00 41.45           C  
ANISOU  810  CA  ASN A 200     6306   3605   5839    249   -977   -308       C  
ATOM    811  C   ASN A 200      11.283  12.929  36.075  1.00 41.81           C  
ANISOU  811  C   ASN A 200     6446   3611   5828   -234   -922   -155       C  
ATOM    812  O   ASN A 200      11.799  11.945  35.524  1.00 36.03           O  
ANISOU  812  O   ASN A 200     5571   3220   4901   -445   -837     57       O  
ATOM    813  CB  ASN A 200       9.093  11.778  36.607  1.00 38.50           C  
ANISOU  813  CB  ASN A 200     5582   3830   5217    319   -837   -456       C  
ATOM    814  CG  ASN A 200       9.353  11.458  38.071  1.00 39.79           C  
ANISOU  814  CG  ASN A 200     5683   4196   5241    203   -699   -824       C  
ATOM    815  ND2 ASN A 200       8.368  10.847  38.724  1.00 41.12           N  
ANISOU  815  ND2 ASN A 200     5619   4729   5274    373   -552  -1046       N  
ATOM    816  OD1 ASN A 200      10.404  11.805  38.624  1.00 39.16           O  
ANISOU  816  OD1 ASN A 200     5762   3951   5164    -48   -731   -913       O  
ATOM    817  N   LEU A 201      11.997  13.907  36.628  1.00 45.37           N  
ANISOU  817  N   LEU A 201     7104   3641   6494   -405   -973   -313       N  
ATOM    818  CA  LEU A 201      13.458  13.949  36.546  1.00 45.44           C  
ANISOU  818  CA  LEU A 201     7143   3571   6551   -883   -940   -208       C  
ATOM    819  C   LEU A 201      14.129  12.854  37.384  1.00 43.44           C  
ANISOU  819  C   LEU A 201     6615   3807   6082  -1073   -889   -404       C  
ATOM    820  O   LEU A 201      15.332  12.641  37.287  1.00 43.03           O  
ANISOU  820  O   LEU A 201     6462   3813   6075  -1429   -875   -334       O  
ATOM    821  CB  LEU A 201      13.973  15.317  36.999  1.00 50.24           C  
ANISOU  821  CB  LEU A 201     8024   3567   7500  -1040  -1044   -390       C  
ATOM    822  CG  LEU A 201      14.358  16.356  35.939  1.00 58.13           C  
ANISOU  822  CG  LEU A 201     9336   3980   8772  -1229  -1067     -3       C  
ATOM    823  CD1 LEU A 201      15.316  17.382  36.522  1.00 63.42           C  
ANISOU  823  CD1 LEU A 201    10174   4134   9788  -1602  -1130   -223       C  
ATOM    824  CD2 LEU A 201      14.948  15.726  34.678  1.00 57.91           C  
ANISOU  824  CD2 LEU A 201     9234   4215   8555  -1501   -911    491       C  
ATOM    825  N   ARG A 202      13.348  12.139  38.181  1.00 41.84           N  
ANISOU  825  N   ARG A 202     6279   3962   5657   -836   -862   -626       N  
ATOM    826  CA  ARG A 202      13.898  11.085  39.016  1.00 42.42           C  
ANISOU  826  CA  ARG A 202     6167   4456   5495   -979   -856   -746       C  
ATOM    827  C   ARG A 202      13.612   9.704  38.444  1.00 37.58           C  
ANISOU  827  C   ARG A 202     5339   4249   4690   -930   -750   -504       C  
ATOM    828  O   ARG A 202      13.755   8.694  39.131  1.00 33.28           O  
ANISOU  828  O   ARG A 202     4671   4031   3943   -964   -745   -559       O  
ATOM    829  CB  ARG A 202      13.337  11.220  40.427  1.00 48.45           C  
ANISOU  829  CB  ARG A 202     6997   5331   6081   -826   -871  -1151       C  
ATOM    830  CG  ARG A 202      13.582  12.612  40.987  1.00 58.81           C  
ANISOU  830  CG  ARG A 202     8544   6199   7603   -858   -986  -1481       C  
ATOM    831  CD  ARG A 202      12.577  12.964  42.048  1.00 65.26           C  
ANISOU  831  CD  ARG A 202     9453   7075   8266   -574   -917  -1912       C  
ATOM    832  NE  ARG A 202      12.843  12.333  43.324  1.00 68.58           N  
ANISOU  832  NE  ARG A 202     9868   7908   8279   -675   -929  -2161       N  
ATOM    833  CZ  ARG A 202      11.896  12.058  44.212  1.00 72.55           C  
ANISOU  833  CZ  ARG A 202    10380   8724   8461   -471   -754  -2424       C  
ATOM    834  NH1 ARG A 202      10.625  12.333  43.931  1.00 70.05           N1+
ANISOU  834  NH1 ARG A 202     9986   8367   8263   -140   -553  -2511       N1+
ATOM    835  NH2 ARG A 202      12.219  11.492  45.369  1.00 76.39           N  
ANISOU  835  NH2 ARG A 202    10939   9590   8496   -602   -781  -2588       N  
ATOM    836  N   VAL A 203      13.253   9.669  37.165  1.00 29.87           N  
ANISOU  836  N   VAL A 203     4354   3224   3770   -865   -693   -228       N  
ATOM    837  CA  VAL A 203      12.975   8.418  36.484  1.00 26.86           C  
ANISOU  837  CA  VAL A 203     3788   3182   3233   -834   -609    -50       C  
ATOM    838  C   VAL A 203      14.250   7.591  36.327  1.00 26.74           C  
ANISOU  838  C   VAL A 203     3625   3329   3207  -1094   -581     34       C  
ATOM    839  O   VAL A 203      15.336   8.121  36.077  1.00 28.24           O  
ANISOU  839  O   VAL A 203     3824   3361   3544  -1324   -588     80       O  
ATOM    840  CB  VAL A 203      12.321   8.669  35.083  1.00 27.40           C  
ANISOU  840  CB  VAL A 203     3921   3180   3311   -705   -605    197       C  
ATOM    841  CG1 VAL A 203      13.275   9.356  34.116  1.00 29.31           C  
ANISOU  841  CG1 VAL A 203     4323   3178   3634   -933   -585    446       C  
ATOM    842  CG2 VAL A 203      11.857   7.383  34.502  1.00 30.13           C  
ANISOU  842  CG2 VAL A 203     4076   3883   3490   -658   -547    271       C  
ATOM    843  N   GLU A 204      14.107   6.280  36.456  1.00 25.40           N  
ANISOU  843  N   GLU A 204     3290   3454   2907  -1057   -544     42       N  
ATOM    844  CA  GLU A 204      15.251   5.380  36.404  1.00 28.91           C  
ANISOU  844  CA  GLU A 204     3559   4036   3392  -1215   -548     78       C  
ATOM    845  C   GLU A 204      14.934   4.179  35.517  1.00 29.43           C  
ANISOU  845  C   GLU A 204     3499   4290   3392  -1155   -445    179       C  
ATOM    846  O   GLU A 204      13.839   3.623  35.595  1.00 24.31           O  
ANISOU  846  O   GLU A 204     2858   3744   2636  -1021   -424    169       O  
ATOM    847  CB  GLU A 204      15.637   4.948  37.825  1.00 26.44           C  
ANISOU  847  CB  GLU A 204     3220   3812   3014  -1228   -694    -59       C  
ATOM    848  CG  GLU A 204      16.530   3.705  37.932  1.00 27.99           C  
ANISOU  848  CG  GLU A 204     3219   4158   3256  -1267   -766    -10       C  
ATOM    849  CD  GLU A 204      16.829   3.323  39.400  1.00 30.63           C  
ANISOU  849  CD  GLU A 204     3609   4577   3453  -1250   -987    -82       C  
ATOM    850  OE1 GLU A 204      17.166   4.236  40.192  1.00 29.62           O  
ANISOU  850  OE1 GLU A 204     3574   4393   3288  -1324  -1128   -236       O  
ATOM    851  OE2 GLU A 204      16.693   2.129  39.767  1.00 23.18           O1-
ANISOU  851  OE2 GLU A 204     2655   3736   2415  -1173  -1033     20       O1-
ATOM    852  N   TYR A 205      15.874   3.812  34.642  1.00 32.03           N  
ANISOU  852  N   TYR A 205     3696   4671   3804  -1273   -360    234       N  
ATOM    853  CA  TYR A 205      15.670   2.690  33.716  1.00 30.78           C  
ANISOU  853  CA  TYR A 205     3435   4675   3584  -1222   -256    253       C  
ATOM    854  C   TYR A 205      16.640   1.542  33.974  1.00 30.65           C  
ANISOU  854  C   TYR A 205     3197   4732   3715  -1234   -271    167       C  
ATOM    855  O   TYR A 205      17.816   1.769  34.290  1.00 31.16           O  
ANISOU  855  O   TYR A 205     3111   4777   3951  -1330   -308    122       O  
ATOM    856  CB  TYR A 205      15.794   3.159  32.269  1.00 30.67           C  
ANISOU  856  CB  TYR A 205     3482   4694   3478  -1302   -101    354       C  
ATOM    857  CG  TYR A 205      14.711   4.120  31.852  1.00 30.05           C  
ANISOU  857  CG  TYR A 205     3639   4520   3256  -1212   -157    483       C  
ATOM    858  CD1 TYR A 205      14.865   5.490  32.036  1.00 32.46           C  
ANISOU  858  CD1 TYR A 205     4123   4578   3634  -1274   -195    585       C  
ATOM    859  CD2 TYR A 205      13.527   3.657  31.281  1.00 27.59           C  
ANISOU  859  CD2 TYR A 205     3358   4338   2785  -1053   -210    484       C  
ATOM    860  CE1 TYR A 205      13.872   6.378  31.657  1.00 33.59           C  
ANISOU  860  CE1 TYR A 205     4489   4571   3704  -1125   -293    712       C  
ATOM    861  CE2 TYR A 205      12.521   4.533  30.903  1.00 27.63           C  
ANISOU  861  CE2 TYR A 205     3530   4264   2703   -909   -328    595       C  
ATOM    862  CZ  TYR A 205      12.699   5.892  31.090  1.00 31.23           C  
ANISOU  862  CZ  TYR A 205     4182   4441   3243   -917   -374    722       C  
ATOM    863  OH  TYR A 205      11.710   6.773  30.706  1.00 32.25           O  
ANISOU  863  OH  TYR A 205     4485   4429   3339   -711   -535    843       O  
ATOM    864  N   LEU A 206      16.136   0.316  33.807  1.00 30.98           N  
ANISOU  864  N   LEU A 206     3200   4834   3737  -1132   -263    130       N  
ATOM    865  CA  LEU A 206      16.884  -0.909  34.117  1.00 30.90           C  
ANISOU  865  CA  LEU A 206     3023   4806   3912  -1071   -325     59       C  
ATOM    866  C   LEU A 206      16.972  -1.897  32.950  1.00 34.10           C  
ANISOU  866  C   LEU A 206     3320   5265   4373  -1026   -177    -68       C  
ATOM    867  O   LEU A 206      15.968  -2.176  32.263  1.00 38.34           O  
ANISOU  867  O   LEU A 206     3960   5850   4758  -1020   -111    -96       O  
ATOM    868  CB  LEU A 206      16.246  -1.646  35.312  1.00 25.33           C  
ANISOU  868  CB  LEU A 206     2433   4020   3172   -999   -485    132       C  
ATOM    869  CG  LEU A 206      16.976  -2.926  35.740  1.00 29.62           C  
ANISOU  869  CG  LEU A 206     2877   4452   3926   -899   -623    131       C  
ATOM    870  CD1 LEU A 206      18.374  -2.589  36.391  1.00 22.92           C  
ANISOU  870  CD1 LEU A 206     1859   3607   3241   -869   -820    113       C  
ATOM    871  CD2 LEU A 206      16.148  -3.809  36.662  1.00 27.78           C  
ANISOU  871  CD2 LEU A 206     2838   4105   3611   -880   -717    275       C  
ATOM    872  N   ASP A 207      18.179  -2.394  32.710  1.00 30.88           N  
ANISOU  872  N   ASP A 207     2673   4866   4193   -989   -136   -195       N  
ATOM    873  CA  ASP A 207      18.365  -3.620  31.947  1.00 29.55           C  
ANISOU  873  CA  ASP A 207     2387   4685   4155   -881    -38   -393       C  
ATOM    874  C   ASP A 207      18.778  -4.690  32.940  1.00 34.03           C  
ANISOU  874  C   ASP A 207     2878   5033   5019   -711   -274   -387       C  
ATOM    875  O   ASP A 207      19.905  -4.671  33.431  1.00 37.81           O  
ANISOU  875  O   ASP A 207     3131   5497   5738   -632   -391   -413       O  
ATOM    876  CB  ASP A 207      19.447  -3.477  30.865  1.00 30.61           C  
ANISOU  876  CB  ASP A 207     2274   4999   4359   -920    229   -593       C  
ATOM    877  CG  ASP A 207      19.063  -2.520  29.755  1.00 32.55           C  
ANISOU  877  CG  ASP A 207     2674   5451   4244  -1103    470   -539       C  
ATOM    878  OD1 ASP A 207      17.875  -2.173  29.623  1.00 31.84           O  
ANISOU  878  OD1 ASP A 207     2855   5357   3886  -1130    395   -405       O  
ATOM    879  OD2 ASP A 207      19.962  -2.125  28.997  1.00 37.45           O1-
ANISOU  879  OD2 ASP A 207     3133   6247   4850  -1219    736   -622       O1-
ATOM    880  N   ASP A 208      17.899  -5.639  33.219  1.00 32.54           N  
ANISOU  880  N   ASP A 208     2866   4661   4835   -661   -363   -343       N  
ATOM    881  CA  ASP A 208      18.210  -6.667  34.196  1.00 32.71           C  
ANISOU  881  CA  ASP A 208     2914   4407   5107   -513   -610   -245       C  
ATOM    882  C   ASP A 208      19.430  -7.469  33.758  1.00 36.26           C  
ANISOU  882  C   ASP A 208     3075   4749   5953   -290   -630   -477       C  
ATOM    883  O   ASP A 208      19.474  -7.998  32.654  1.00 34.69           O  
ANISOU  883  O   ASP A 208     2777   4555   5850   -244   -423   -763       O  
ATOM    884  CB  ASP A 208      17.016  -7.588  34.376  1.00 37.54           C  
ANISOU  884  CB  ASP A 208     3773   4806   5684   -571   -628   -161       C  
ATOM    885  CG  ASP A 208      17.173  -8.529  35.561  1.00 46.27           C  
ANISOU  885  CG  ASP A 208     5033   5587   6962   -475   -891     78       C  
ATOM    886  OD1 ASP A 208      17.904  -9.543  35.427  1.00 50.72           O  
ANISOU  886  OD1 ASP A 208     5508   5872   7889   -269  -1011    -15       O  
ATOM    887  OD2 ASP A 208      16.561  -8.260  36.625  1.00 46.55           O1-
ANISOU  887  OD2 ASP A 208     5294   5637   6755   -595   -975    359       O1-
ATOM    888  N   ARG A 209      20.441  -7.544  34.614  1.00 42.85           N  
ANISOU  888  N   ARG A 209     3750   5510   7020   -130   -893   -397       N  
ATOM    889  CA  ARG A 209      21.675  -8.212  34.206  1.00 49.84           C  
ANISOU  889  CA  ARG A 209     4257   6325   8355    132   -921   -662       C  
ATOM    890  C   ARG A 209      21.478  -9.714  33.974  1.00 49.78           C  
ANISOU  890  C   ARG A 209     4339   5921   8655    356   -984   -776       C  
ATOM    891  O   ARG A 209      22.287 -10.343  33.299  1.00 55.26           O  
ANISOU  891  O   ARG A 209     4726   6547   9724    591   -899  -1116       O  
ATOM    892  CB  ARG A 209      22.801  -7.975  35.219  1.00 55.57           C  
ANISOU  892  CB  ARG A 209     4739   7070   9307    285  -1279   -562       C  
ATOM    893  CG  ARG A 209      22.479  -8.314  36.652  1.00 58.77           C  
ANISOU  893  CG  ARG A 209     5473   7251   9604    352  -1716   -180       C  
ATOM    894  CD  ARG A 209      23.709  -8.128  37.501  1.00 62.51           C  
ANISOU  894  CD  ARG A 209     5656   7788  10308    540  -2130   -149       C  
ATOM    895  NE  ARG A 209      24.826  -8.905  36.977  1.00 67.92           N  
ANISOU  895  NE  ARG A 209     5906   8370  11531    869  -2164   -433       N  
ATOM    896  CZ  ARG A 209      26.011  -8.995  37.568  1.00 71.07           C  
ANISOU  896  CZ  ARG A 209     6111   8802  12091   1057  -2414   -452       C  
ATOM    897  NH1 ARG A 209      26.222  -8.365  38.716  1.00 70.26           N1+
ANISOU  897  NH1 ARG A 209     6164   8835  11698    964  -2713   -221       N1+
ATOM    898  NH2 ARG A 209      26.977  -9.722  37.021  1.00 74.28           N  
ANISOU  898  NH2 ARG A 209     6161   9121  12939   1340  -2363   -734       N  
ATOM    899  N   ASN A 210      20.398 -10.285  34.497  1.00 44.69           N  
ANISOU  899  N   ASN A 210     4099   5002   7881    266  -1097   -526       N  
ATOM    900  CA  ASN A 210      20.201 -11.722  34.354  1.00 47.01           C  
ANISOU  900  CA  ASN A 210     4522   4819   8520    433  -1182   -606       C  
ATOM    901  C   ASN A 210      19.055 -12.108  33.423  1.00 47.03           C  
ANISOU  901  C   ASN A 210     4707   4772   8391    220   -911   -805       C  
ATOM    902  O   ASN A 210      19.136 -13.119  32.726  1.00 47.98           O  
ANISOU  902  O   ASN A 210     4797   4603   8830    355   -854  -1125       O  
ATOM    903  CB  ASN A 210      19.986 -12.344  35.723  1.00 47.90           C  
ANISOU  903  CB  ASN A 210     4964   4552   8685    486  -1561   -146       C  
ATOM    904  CG  ASN A 210      21.239 -12.305  36.564  1.00 50.71           C  
ANISOU  904  CG  ASN A 210     5126   4875   9265    794  -1949     -9       C  
ATOM    905  ND2 ASN A 210      22.264 -13.007  36.117  1.00 52.37           N  
ANISOU  905  ND2 ASN A 210     5007   4883  10008   1167  -2050   -300       N  
ATOM    906  OD1 ASN A 210      21.289 -11.643  37.600  1.00 51.77           O  
ANISOU  906  OD1 ASN A 210     5382   5185   9102    712  -2170    312       O  
ATOM    907  N   THR A 211      18.008 -11.292  33.381  1.00 43.86           N  
ANISOU  907  N   THR A 211     4464   4656   7546    -92   -765   -669       N  
ATOM    908  CA  THR A 211      16.867 -11.599  32.535  1.00 43.83           C  
ANISOU  908  CA  THR A 211     4586   4659   7410   -302   -580   -860       C  
ATOM    909  C   THR A 211      16.846 -10.789  31.257  1.00 38.84           C  
ANISOU  909  C   THR A 211     3796   4473   6488   -375   -314  -1168       C  
ATOM    910  O   THR A 211      16.137 -11.135  30.320  1.00 37.26           O  
ANISOU  910  O   THR A 211     3650   4315   6191   -484   -197  -1437       O  
ATOM    911  CB  THR A 211      15.555 -11.335  33.266  1.00 47.23           C  
ANISOU  911  CB  THR A 211     5263   5112   7572   -587   -605   -533       C  
ATOM    912  CG2 THR A 211      15.529 -12.063  34.592  1.00 50.88           C  
ANISOU  912  CG2 THR A 211     5958   5178   8197   -578   -826   -147       C  
ATOM    913  OG1 THR A 211      15.446  -9.928  33.510  1.00 45.12           O  
ANISOU  913  OG1 THR A 211     4949   5265   6930   -671   -546   -381       O  
ATOM    914  N   PHE A 212      17.611  -9.702  31.238  1.00 35.72           N  
ANISOU  914  N   PHE A 212     3229   4405   5938   -343   -239  -1112       N  
ATOM    915  CA  PHE A 212      17.691  -8.813  30.082  1.00 35.30           C  
ANISOU  915  CA  PHE A 212     3082   4768   5563   -442     25  -1300       C  
ATOM    916  C   PHE A 212      16.397  -8.057  29.806  1.00 31.68           C  
ANISOU  916  C   PHE A 212     2828   4522   4686   -666     50  -1160       C  
ATOM    917  O   PHE A 212      16.274  -7.379  28.785  1.00 34.41           O  
ANISOU  917  O   PHE A 212     3183   5179   4711   -749    217  -1264       O  
ATOM    918  CB  PHE A 212      18.107  -9.598  28.845  1.00 42.85           C  
ANISOU  918  CB  PHE A 212     3919   5746   6617   -338    230  -1776       C  
ATOM    919  CG  PHE A 212      19.241 -10.515  29.098  1.00 44.96           C  
ANISOU  919  CG  PHE A 212     3954   5737   7393    -49    182  -1979       C  
ATOM    920  CD1 PHE A 212      20.498 -10.013  29.363  1.00 45.83           C  
ANISOU  920  CD1 PHE A 212     3742   5994   7676     78    224  -1966       C  
ATOM    921  CD2 PHE A 212      19.051 -11.882  29.096  1.00 49.31           C  
ANISOU  921  CD2 PHE A 212     4584   5844   8306    102     66  -2192       C  
ATOM    922  CE1 PHE A 212      21.563 -10.860  29.610  1.00 50.32           C  
ANISOU  922  CE1 PHE A 212     4024   6319   8777    406    130  -2175       C  
ATOM    923  CE2 PHE A 212      20.110 -12.734  29.342  1.00 54.35           C  
ANISOU  923  CE2 PHE A 212     5004   6168   9478    441    -25  -2379       C  
ATOM    924  CZ  PHE A 212      21.367 -12.218  29.601  1.00 53.74           C  
ANISOU  924  CZ  PHE A 212     4559   6286   9573    619     -5  -2373       C  
ATOM    925  N   ARG A 213      15.429  -8.178  30.707  1.00 32.04           N  
ANISOU  925  N   ARG A 213     3031   4412   4730   -756   -114   -919       N  
ATOM    926  CA  ARG A 213      14.183  -7.443  30.573  1.00 30.93           C  
ANISOU  926  CA  ARG A 213     3000   4476   4275   -918   -114   -807       C  
ATOM    927  C   ARG A 213      14.323  -5.947  30.919  1.00 32.23           C  
ANISOU  927  C   ARG A 213     3178   4861   4205   -940   -100   -573       C  
ATOM    928  O   ARG A 213      15.140  -5.536  31.757  1.00 26.95           O  
ANISOU  928  O   ARG A 213     2472   4137   3630   -891   -149   -422       O  
ATOM    929  CB  ARG A 213      13.096  -8.102  31.436  1.00 26.19           C  
ANISOU  929  CB  ARG A 213     2501   3664   3786  -1035   -223   -670       C  
ATOM    930  CG  ARG A 213      12.812  -9.525  30.951  1.00 31.09           C  
ANISOU  930  CG  ARG A 213     3138   4010   4664  -1077   -239   -925       C  
ATOM    931  CD  ARG A 213      11.535 -10.081  31.496  1.00 28.84           C  
ANISOU  931  CD  ARG A 213     2922   3576   4459  -1300   -284   -826       C  
ATOM    932  NE  ARG A 213      11.249 -11.434  31.021  1.00 35.65           N  
ANISOU  932  NE  ARG A 213     3816   4108   5621  -1392   -312  -1089       N  
ATOM    933  CZ  ARG A 213      10.532 -11.722  29.930  1.00 40.30           C  
ANISOU  933  CZ  ARG A 213     4337   4816   6161  -1511   -315  -1449       C  
ATOM    934  NH1 ARG A 213      10.039 -10.748  29.168  1.00 39.65           N1+
ANISOU  934  NH1 ARG A 213     4161   5194   5711  -1518   -315  -1541       N1+
ATOM    935  NH2 ARG A 213      10.307 -12.991  29.595  1.00 43.88           N  
ANISOU  935  NH2 ARG A 213     4836   4899   6937  -1620   -355  -1724       N  
ATOM    936  N   HIS A 214      13.513  -5.130  30.255  1.00 31.69           N  
ANISOU  936  N   HIS A 214     4653   4230   3157   -224   -128    295       N  
ATOM    937  CA  HIS A 214      13.535  -3.707  30.506  1.00 28.76           C  
ANISOU  937  CA  HIS A 214     4218   3767   2943     10   -218    392       C  
ATOM    938  C   HIS A 214      12.458  -3.369  31.516  1.00 32.95           C  
ANISOU  938  C   HIS A 214     4526   4519   3474     -6   -370    178       C  
ATOM    939  O   HIS A 214      11.489  -4.106  31.683  1.00 34.93           O  
ANISOU  939  O   HIS A 214     4657   5063   3551   -154   -424    -62       O  
ATOM    940  CB  HIS A 214      13.340  -2.933  29.222  1.00 29.48           C  
ANISOU  940  CB  HIS A 214     4429   3884   2887    302   -245    525       C  
ATOM    941  CG  HIS A 214      14.322  -3.305  28.160  1.00 35.25           C  
ANISOU  941  CG  HIS A 214     5402   4400   3592    302    -69    718       C  
ATOM    942  CD2 HIS A 214      15.423  -4.091  28.204  1.00 33.85           C  
ANISOU  942  CD2 HIS A 214     5318   3997   3545    111    111    802       C  
ATOM    943  ND1 HIS A 214      14.200  -2.891  26.851  1.00 37.93           N  
ANISOU  943  ND1 HIS A 214     5929   4754   3727    541    -56    842       N  
ATOM    944  CE1 HIS A 214      15.198  -3.382  26.144  1.00 36.57           C  
ANISOU  944  CE1 HIS A 214     5961   4350   3583    462    143    991       C  
ATOM    945  NE2 HIS A 214      15.947  -4.128  26.937  1.00 32.88           N  
ANISOU  945  NE2 HIS A 214     5422   3745   3326    205    246    964       N  
ATOM    946  N   SER A 215      12.672  -2.293  32.251  1.00 30.85           N  
ANISOU  946  N   SER A 215     4210   4094   3417    104   -400    238       N  
ATOM    947  CA  SER A 215      11.649  -1.794  33.142  1.00 25.20           C  
ANISOU  947  CA  SER A 215     3300   3563   2711    133   -529     54       C  
ATOM    948  C   SER A 215      11.950  -0.342  33.452  1.00 26.68           C  
ANISOU  948  C   SER A 215     3519   3528   3090    346   -523    183       C  
ATOM    949  O   SER A 215      13.086   0.104  33.265  1.00 28.00           O  
ANISOU  949  O   SER A 215     3834   3377   3427    366   -392    371       O  
ATOM    950  CB  SER A 215      11.582  -2.649  34.416  1.00 27.78           C  
ANISOU  950  CB  SER A 215     3546   3911   3096   -167   -504   -123       C  
ATOM    951  OG  SER A 215      12.831  -2.703  35.106  1.00 26.92           O  
ANISOU  951  OG  SER A 215     3530   3501   3197   -263   -416      4       O  
ATOM    952  N   VAL A 216      10.940   0.396  33.913  1.00 28.30           N  
ANISOU  952  N   VAL A 216     3587   3893   3272    494   -630     63       N  
ATOM    953  CA  VAL A 216      11.132   1.786  34.320  1.00 26.53           C  
ANISOU  953  CA  VAL A 216     3423   3433   3223    681   -585    162       C  
ATOM    954  C   VAL A 216      10.458   2.011  35.673  1.00 29.97           C  
ANISOU  954  C   VAL A 216     3673   3962   3752    580   -653    -41       C  
ATOM    955  O   VAL A 216       9.295   1.634  35.895  1.00 26.86           O  
ANISOU  955  O   VAL A 216     3085   3904   3217    575   -769   -251       O  
ATOM    956  CB  VAL A 216      10.597   2.812  33.287  1.00 31.43           C  
ANISOU  956  CB  VAL A 216     4167   4082   3693   1113   -601    290       C  
ATOM    957  CG1 VAL A 216       9.142   2.534  32.889  1.00 27.71           C  
ANISOU  957  CG1 VAL A 216     3491   4097   2939   1304   -806    110       C  
ATOM    958  CG2 VAL A 216      10.740   4.214  33.839  1.00 26.85           C  
ANISOU  958  CG2 VAL A 216     3694   3216   3291   1280   -494    369       C  
ATOM    959  N   VAL A 217      11.214   2.638  36.567  1.00 31.62           N  
ANISOU  959  N   VAL A 217     3935   3879   4199    480   -562     -1       N  
ATOM    960  CA  VAL A 217      10.812   2.804  37.946  1.00 29.41           C  
ANISOU  960  CA  VAL A 217     3527   3628   4021    337   -600   -180       C  
ATOM    961  C   VAL A 217      10.930   4.298  38.317  1.00 28.68           C  
ANISOU  961  C   VAL A 217     3519   3286   4093    499   -509   -120       C  
ATOM    962  O   VAL A 217      11.812   5.009  37.806  1.00 25.19           O  
ANISOU  962  O   VAL A 217     3258   2553   3759    576   -364     51       O  
ATOM    963  CB  VAL A 217      11.684   1.893  38.895  1.00 39.67           C  
ANISOU  963  CB  VAL A 217     4819   4839   5415      3   -581   -237       C  
ATOM    964  CG1 VAL A 217      13.174   2.155  38.693  1.00 36.61           C  
ANISOU  964  CG1 VAL A 217     4546   4164   5202    -47   -475    -72       C  
ATOM    965  CG2 VAL A 217      11.328   2.098  40.347  1.00 43.06           C  
ANISOU  965  CG2 VAL A 217     5166   5274   5922   -135   -611   -414       C  
ATOM    966  N   VAL A 218       9.998   4.766  39.155  1.00 28.00           N  
ANISOU  966  N   VAL A 218     3320   3302   4015    544   -555   -276       N  
ATOM    967  CA  VAL A 218       9.996   6.121  39.689  1.00 29.20           C  
ANISOU  967  CA  VAL A 218     3564   3214   4315    667   -443   -258       C  
ATOM    968  C   VAL A 218       9.672   6.039  41.167  1.00 30.79           C  
ANISOU  968  C   VAL A 218     3638   3457   4604    437   -477   -472       C  
ATOM    969  O   VAL A 218       9.045   5.075  41.590  1.00 26.47           O  
ANISOU  969  O   VAL A 218     2934   3172   3953    292   -586   -634       O  
ATOM    970  CB  VAL A 218       8.958   7.025  39.003  1.00 35.00           C  
ANISOU  970  CB  VAL A 218     4340   4036   4922   1107   -443   -203       C  
ATOM    971  CG1 VAL A 218       9.313   7.246  37.518  1.00 40.70           C  
ANISOU  971  CG1 VAL A 218     5271   4672   5520   1388   -385     34       C  
ATOM    972  CG2 VAL A 218       7.546   6.454  39.177  1.00 32.87           C  
ANISOU  972  CG2 VAL A 218     3790   4218   4483   1183   -627   -416       C  
ATOM    973  N   PRO A 219      10.091   7.042  41.967  1.00 38.75           N  
ANISOU  973  N   PRO A 219     4740   4192   5790    380   -354   -491       N  
ATOM    974  CA  PRO A 219       9.685   7.069  43.385  1.00 37.26           C  
ANISOU  974  CA  PRO A 219     4460   4040   5658    190   -380   -700       C  
ATOM    975  C   PRO A 219       8.157   7.145  43.525  1.00 42.76           C  
ANISOU  975  C   PRO A 219     5011   4996   6239    377   -441   -836       C  
ATOM    976  O   PRO A 219       7.537   7.946  42.807  1.00 45.36           O  
ANISOU  976  O   PRO A 219     5371   5341   6521    734   -405   -755       O  
ATOM    977  CB  PRO A 219      10.310   8.368  43.917  1.00 37.58           C  
ANISOU  977  CB  PRO A 219     4656   3732   5890    160   -201   -687       C  
ATOM    978  CG  PRO A 219      11.388   8.725  42.936  1.00 40.40           C  
ANISOU  978  CG  PRO A 219     5170   3856   6323    202    -71   -499       C  
ATOM    979  CD  PRO A 219      10.897   8.223  41.599  1.00 41.37           C  
ANISOU  979  CD  PRO A 219     5294   4159   6266    472   -147   -347       C  
ATOM    980  N   TYR A 220       7.557   6.366  44.427  1.00 38.24           N  
ANISOU  980  N   TYR A 220     4295   4622   5611    167   -512  -1048       N  
ATOM    981  CA  TYR A 220       6.125   6.512  44.693  1.00 34.71           C  
ANISOU  981  CA  TYR A 220     3670   4426   5092    302   -533  -1234       C  
ATOM    982  C   TYR A 220       5.854   7.870  45.319  1.00 37.08           C  
ANISOU  982  C   TYR A 220     4047   4519   5521    457   -413  -1250       C  
ATOM    983  O   TYR A 220       6.588   8.289  46.213  1.00 37.36           O  
ANISOU  983  O   TYR A 220     4226   4279   5689    252   -324  -1261       O  
ATOM    984  CB  TYR A 220       5.606   5.408  45.616  1.00 31.41           C  
ANISOU  984  CB  TYR A 220     3132   4200   4600    -13   -559  -1481       C  
ATOM    985  CG  TYR A 220       4.191   5.678  46.093  1.00 33.74           C  
ANISOU  985  CG  TYR A 220     3226   4724   4869     73   -533  -1723       C  
ATOM    986  CD1 TYR A 220       3.099   5.426  45.261  1.00 31.94           C  
ANISOU  986  CD1 TYR A 220     2741   4882   4513    273   -607  -1839       C  
ATOM    987  CD2 TYR A 220       3.947   6.209  47.358  1.00 27.06           C  
ANISOU  987  CD2 TYR A 220     2425   3733   4122    -39   -434  -1857       C  
ATOM    988  CE1 TYR A 220       1.813   5.675  45.671  1.00 33.74           C  
ANISOU  988  CE1 TYR A 220     2725   5367   4727    364   -582  -2093       C  
ATOM    989  CE2 TYR A 220       2.660   6.469  47.780  1.00 33.61           C  
ANISOU  989  CE2 TYR A 220     3056   4770   4942     46   -385  -2088       C  
ATOM    990  CZ  TYR A 220       1.594   6.191  46.937  1.00 36.51           C  
ANISOU  990  CZ  TYR A 220     3131   5542   5198    249   -459  -2212       C  
ATOM    991  OH  TYR A 220       0.305   6.438  47.340  1.00 37.61           O  
ANISOU  991  OH  TYR A 220     3013   5941   5338    342   -412  -2480       O  
ATOM    992  N   GLU A 221       4.824   8.570  44.851  1.00 41.65           N  
ANISOU  992  N   GLU A 221     4538   5240   6047    832   -406  -1261       N  
ATOM    993  CA  GLU A 221       4.437   9.817  45.503  1.00 47.47           C  
ANISOU  993  CA  GLU A 221     5365   5778   6892   1001   -259  -1292       C  
ATOM    994  C   GLU A 221       3.037   9.652  46.095  1.00 48.83           C  
ANISOU  994  C   GLU A 221     5266   6273   7014   1058   -294  -1556       C  
ATOM    995  O   GLU A 221       2.123   9.172  45.424  1.00 48.26           O  
ANISOU  995  O   GLU A 221     4935   6603   6800   1248   -420  -1650       O  
ATOM    996  CB  GLU A 221       4.474  10.987  44.505  1.00 55.52           C  
ANISOU  996  CB  GLU A 221     6583   6616   7895   1472   -157  -1056       C  
ATOM    997  CG  GLU A 221       5.811  11.158  43.773  1.00 62.55           C  
ANISOU  997  CG  GLU A 221     7745   7188   8833   1416    -72   -813       C  
ATOM    998  CD  GLU A 221       5.758  12.182  42.636  1.00 72.06           C  
ANISOU  998  CD  GLU A 221     9203   8216   9960   1914     59   -570       C  
ATOM    999  OE1 GLU A 221       6.823  12.507  42.059  1.00 73.46           O  
ANISOU  999  OE1 GLU A 221     9651   8068  10191   1873    207   -383       O  
ATOM   1000  OE2 GLU A 221       4.650  12.651  42.307  1.00 78.18           O1-
ANISOU 1000  OE2 GLU A 221     9916   9185  10606   2366     25   -573       O1-
ATOM   1001  N   PRO A 222       2.862  10.047  47.364  1.00 45.70           N  
ANISOU 1001  N   PRO A 222     4912   5720   6730    875   -173  -1708       N  
ATOM   1002  CA  PRO A 222       1.510  10.009  47.928  1.00 46.06           C  
ANISOU 1002  CA  PRO A 222     4703   6047   6750    943   -159  -1972       C  
ATOM   1003  C   PRO A 222       0.600  11.026  47.256  1.00 49.21           C  
ANISOU 1003  C   PRO A 222     5014   6572   7113   1511   -138  -1922       C  
ATOM   1004  O   PRO A 222       1.092  12.045  46.777  1.00 53.35           O  
ANISOU 1004  O   PRO A 222     5804   6795   7670   1804    -41  -1679       O  
ATOM   1005  CB  PRO A 222       1.736  10.372  49.404  1.00 45.24           C  
ANISOU 1005  CB  PRO A 222     4759   5655   6776    639     -2  -2096       C  
ATOM   1006  CG  PRO A 222       3.198  10.142  49.651  1.00 40.07           C  
ANISOU 1006  CG  PRO A 222     4357   4697   6169    322     -9  -1957       C  
ATOM   1007  CD  PRO A 222       3.871  10.450  48.354  1.00 38.46           C  
ANISOU 1007  CD  PRO A 222     4248   4409   5955    568    -50  -1687       C  
ATOM   1008  N   PRO A 223      -0.707  10.749  47.195  1.00 49.89           N  
ANISOU 1008  N   PRO A 223     4735   7104   7118   1681   -211  -2161       N  
ATOM   1009  CA  PRO A 223      -1.672  11.733  46.698  1.00 55.20           C  
ANISOU 1009  CA  PRO A 223     5286   7949   7737   2284   -204  -2145       C  
ATOM   1010  C   PRO A 223      -1.690  12.893  47.664  1.00 60.28           C  
ANISOU 1010  C   PRO A 223     6165   8200   8537   2355     40  -2126       C  
ATOM   1011  O   PRO A 223      -1.348  12.655  48.829  1.00 58.12           O  
ANISOU 1011  O   PRO A 223     5985   7710   8386   1883    152  -2256       O  
ATOM   1012  CB  PRO A 223      -3.007  10.983  46.716  1.00 46.92           C  
ANISOU 1012  CB  PRO A 223     3771   7478   6578   2238   -325  -2466       C  
ATOM   1013  CG  PRO A 223      -2.643   9.554  46.686  1.00 49.53           C  
ANISOU 1013  CG  PRO A 223     3955   7988   6876   1773   -413  -2635       C  
ATOM   1014  CD  PRO A 223      -1.351   9.456  47.474  1.00 47.27           C  
ANISOU 1014  CD  PRO A 223     4076   7170   6716   1341   -293  -2472       C  
ATOM   1015  N   GLU A 224      -2.000  14.111  47.235  1.00 67.15           N  
ANISOU 1015  N   GLU A 224     7195   8936   9384   2902    143  -1948       N  
ATOM   1016  CA  GLU A 224      -2.236  15.149  48.237  1.00 71.93           C  
ANISOU 1016  CA  GLU A 224     7988   9213  10130   2953    408  -1988       C  
ATOM   1017  C   GLU A 224      -3.535  14.771  48.969  1.00 75.70           C  
ANISOU 1017  C   GLU A 224     8073  10087  10603   2847    378  -2292       C  
ATOM   1018  O   GLU A 224      -4.324  13.984  48.448  1.00 79.08           O  
ANISOU 1018  O   GLU A 224     8132  11026  10890   2854    165  -2410       O  
ATOM   1019  CB  GLU A 224      -2.313  16.533  47.611  1.00 77.03           C  
ANISOU 1019  CB  GLU A 224     8969   9575  10725   3455    582  -1655       C  
ATOM   1020  CG  GLU A 224      -3.349  16.683  46.544  1.00 84.95           C  
ANISOU 1020  CG  GLU A 224     9767  10995  11516   3900    406  -1535       C  
ATOM   1021  CD  GLU A 224      -3.427  18.107  46.057  1.00 92.95           C  
ANISOU 1021  CD  GLU A 224    11144  11681  12489   4339    593  -1248       C  
ATOM   1022  OE1 GLU A 224      -2.711  18.966  46.624  1.00 92.08           O  
ANISOU 1022  OE1 GLU A 224    11426  11019  12541   4238    885  -1167       O  
ATOM   1023  OE2 GLU A 224      -4.202  18.365  45.113  1.00 99.05           O1-
ANISOU 1023  OE2 GLU A 224    11829  12761  13044   4755    443  -1136       O1-
ATOM   1024  N   VAL A 225      -3.779  15.334  50.152  1.00 75.88           N  
ANISOU 1024  N   VAL A 225     8193   9871  10768   2720    606  -2431       N  
ATOM   1025  CA  VAL A 225      -4.902  14.899  50.997  1.00 73.34           C  
ANISOU 1025  CA  VAL A 225     7538   9865  10462   2520    619  -2742       C  
ATOM   1026  C   VAL A 225      -6.273  15.110  50.319  1.00 75.88           C  
ANISOU 1026  C   VAL A 225     7539  10646  10648   2954    509  -2739       C  
ATOM   1027  O   VAL A 225      -7.275  14.492  50.698  1.00 75.10           O  
ANISOU 1027  O   VAL A 225     7089  10910  10535   2786    468  -3024       O  
ATOM   1028  CB  VAL A 225      -4.819  15.603  52.377  1.00 74.84           C  
ANISOU 1028  CB  VAL A 225     7980   9641  10814   2315    913  -2843       C  
ATOM   1029  CG1 VAL A 225      -5.846  15.057  53.366  1.00 74.95           C  
ANISOU 1029  CG1 VAL A 225     7708   9918  10851   2015    958  -3168       C  
ATOM   1030  CG2 VAL A 225      -3.434  15.421  52.947  1.00 71.26           C  
ANISOU 1030  CG2 VAL A 225     7868   8740  10469   1858    987  -2830       C  
ATOM   1031  N   GLY A 226      -6.296  15.940  49.276  1.00 80.93           N  
ANISOU 1031  N   GLY A 226     8311  11262  11178   3474    458  -2431       N  
ATOM   1032  CA  GLY A 226      -7.510  16.223  48.518  1.00 86.75           C  
ANISOU 1032  CA  GLY A 226     8784  12419  11757   3915    319  -2414       C  
ATOM   1033  C   GLY A 226      -7.736  15.406  47.251  1.00 86.34           C  
ANISOU 1033  C   GLY A 226     8490  12848  11466   3993    -15  -2412       C  
ATOM   1034  O   GLY A 226      -8.700  15.624  46.515  1.00 89.86           O  
ANISOU 1034  O   GLY A 226     8734  13680  11730   4364   -172  -2421       O  
ATOM   1035  N   SER A 227      -6.824  14.480  46.983  1.00 82.94           N  
ANISOU 1035  N   SER A 227     8104  12390  11021   3650   -118  -2411       N  
ATOM   1036  CA  SER A 227      -6.924  13.591  45.830  1.00 83.06           C  
ANISOU 1036  CA  SER A 227     7932  12818  10810   3641   -399  -2433       C  
ATOM   1037  C   SER A 227      -6.941  12.150  46.341  1.00 76.67           C  
ANISOU 1037  C   SER A 227     6852  12243  10035   3035   -462  -2783       C  
ATOM   1038  O   SER A 227      -6.576  11.892  47.492  1.00 73.36           O  
ANISOU 1038  O   SER A 227     6479  11584   9810   2641   -294  -2930       O  
ATOM   1039  CB  SER A 227      -5.784  13.829  44.827  1.00 87.26           C  
ANISOU 1039  CB  SER A 227     8824  13067  11263   3823   -435  -2068       C  
ATOM   1040  OG  SER A 227      -4.511  13.472  45.342  1.00 87.17           O  
ANISOU 1040  OG  SER A 227     9031  12660  11428   3456   -323  -2021       O  
ATOM   1041  N   ASP A 228      -7.429  11.225  45.520  1.00 76.91           N  
ANISOU 1041  N   ASP A 228     6637  12728   9858   2944   -669  -2944       N  
ATOM   1042  CA  ASP A 228      -7.583   9.841  45.961  1.00 73.86           C  
ANISOU 1042  CA  ASP A 228     6047  12542   9474   2357   -670  -3299       C  
ATOM   1043  C   ASP A 228      -6.559   8.860  45.390  1.00 69.99           C  
ANISOU 1043  C   ASP A 228     5695  11975   8923   2072   -733  -3216       C  
ATOM   1044  O   ASP A 228      -6.418   7.738  45.877  1.00 66.87           O  
ANISOU 1044  O   ASP A 228     5262  11594   8552   1560   -656  -3449       O  
ATOM   1045  CB  ASP A 228      -8.977   9.342  45.554  1.00 77.45           C  
ANISOU 1045  CB  ASP A 228     6136  13558   9733   2364   -783  -3644       C  
ATOM   1046  CG  ASP A 228     -10.107  10.118  46.206  1.00 81.54           C  
ANISOU 1046  CG  ASP A 228     6447  14214  10319   2576   -718  -3801       C  
ATOM   1047  OD1 ASP A 228      -9.855  11.227  46.729  1.00 81.14           O  
ANISOU 1047  OD1 ASP A 228     6575  13827  10426   2850   -594  -3568       O  
ATOM   1048  OD2 ASP A 228     -11.257   9.616  46.178  1.00 84.17           O1-
ANISOU 1048  OD2 ASP A 228     6450  14987  10545   2471   -763  -4175       O1-
ATOM   1049  N   CYS A 229      -5.838   9.290  44.366  1.00 50.90           N  
ANISOU 1049  N   CYS A 229     7410   5084   6846   1573    759   -762       N  
ATOM   1050  CA  CYS A 229      -4.871   8.430  43.691  1.00 45.60           C  
ANISOU 1050  CA  CYS A 229     6431   4723   6173   1320    515   -764       C  
ATOM   1051  C   CYS A 229      -3.626   9.183  43.254  1.00 42.16           C  
ANISOU 1051  C   CYS A 229     6092   4260   5667    970    303   -899       C  
ATOM   1052  O   CYS A 229      -3.548  10.412  43.346  1.00 44.96           O  
ANISOU 1052  O   CYS A 229     6744   4327   6012    893    334   -990       O  
ATOM   1053  CB  CYS A 229      -5.518   7.761  42.483  1.00 30.51           C  
ANISOU 1053  CB  CYS A 229     4144   2941   4509   1368    516   -535       C  
ATOM   1054  SG  CYS A 229      -6.028   8.961  41.273  1.00 39.90           S  
ANISOU 1054  SG  CYS A 229     5351   3916   5892   1336    546   -382       S  
ATOM   1055  N   THR A 230      -2.644   8.426  42.804  1.00 31.75           N  
ANISOU 1055  N   THR A 230     4520   3228   4315    763    108   -899       N  
ATOM   1056  CA  THR A 230      -1.440   9.004  42.227  1.00 37.21           C  
ANISOU 1056  CA  THR A 230     5210   3945   4984    428    -93   -961       C  
ATOM   1057  C   THR A 230      -1.416   8.708  40.725  1.00 34.10           C  
ANISOU 1057  C   THR A 230     4507   3674   4774    359   -141   -773       C  
ATOM   1058  O   THR A 230      -1.773   7.601  40.307  1.00 31.01           O  
ANISOU 1058  O   THR A 230     3850   3488   4443    473   -117   -671       O  
ATOM   1059  CB  THR A 230      -0.174   8.453  42.897  1.00 35.18           C  
ANISOU 1059  CB  THR A 230     4898   3949   4518    237   -279  -1082       C  
ATOM   1060  CG2 THR A 230       1.091   9.074  42.271  1.00 33.45           C  
ANISOU 1060  CG2 THR A 230     4633   3765   4310   -125   -486  -1105       C  
ATOM   1061  OG1 THR A 230      -0.224   8.730  44.302  1.00 35.67           O  
ANISOU 1061  OG1 THR A 230     5262   3934   4356    305   -250  -1265       O  
ATOM   1062  N   THR A 231      -1.046   9.696  39.913  1.00 33.55           N  
ANISOU 1062  N   THR A 231     4487   3469   4793    180   -195   -729       N  
ATOM   1063  CA  THR A 231      -1.031   9.488  38.465  1.00 36.93           C  
ANISOU 1063  CA  THR A 231     4647   4034   5352    134   -233   -541       C  
ATOM   1064  C   THR A 231       0.393   9.463  37.889  1.00 39.55           C  
ANISOU 1064  C   THR A 231     4841   4547   5642   -157   -407   -536       C  
ATOM   1065  O   THR A 231       1.178  10.395  38.081  1.00 41.95           O  
ANISOU 1065  O   THR A 231     5294   4710   5934   -378   -484   -598       O  
ATOM   1066  CB  THR A 231      -1.824  10.575  37.711  1.00 35.13           C  
ANISOU 1066  CB  THR A 231     4505   3558   5285    209   -123   -389       C  
ATOM   1067  CG2 THR A 231      -1.831  10.267  36.222  1.00 35.62           C  
ANISOU 1067  CG2 THR A 231     4280   3829   5424    179   -176   -191       C  
ATOM   1068  OG1 THR A 231      -3.171  10.614  38.183  1.00 33.07           O  
ANISOU 1068  OG1 THR A 231     4333   3144   5087    501     59   -341       O  
ATOM   1069  N   ILE A 232       0.704   8.399  37.162  1.00 27.84           N  
ANISOU 1069  N   ILE A 232     3071   3359   4149   -155   -453   -454       N  
ATOM   1070  CA  ILE A 232       1.962   8.295  36.453  1.00 35.80           C  
ANISOU 1070  CA  ILE A 232     3910   4561   5133   -375   -571   -392       C  
ATOM   1071  C   ILE A 232       1.677   8.364  34.953  1.00 38.97           C  
ANISOU 1071  C   ILE A 232     4157   5033   5616   -347   -540   -213       C  
ATOM   1072  O   ILE A 232       0.805   7.646  34.443  1.00 35.76           O  
ANISOU 1072  O   ILE A 232     3637   4722   5227   -173   -481   -169       O  
ATOM   1073  CB  ILE A 232       2.693   6.982  36.820  1.00 36.82           C  
ANISOU 1073  CB  ILE A 232     3847   4985   5157   -375   -618   -431       C  
ATOM   1074  CG1 ILE A 232       3.129   7.017  38.288  1.00 38.27           C  
ANISOU 1074  CG1 ILE A 232     4170   5154   5217   -425   -679   -577       C  
ATOM   1075  CG2 ILE A 232       3.919   6.759  35.947  1.00 26.57           C  
ANISOU 1075  CG2 ILE A 232     2337   3911   3849   -547   -693   -317       C  
ATOM   1076  CD1 ILE A 232       3.768   5.728  38.754  1.00 39.45           C  
ANISOU 1076  CD1 ILE A 232     4123   5597   5271   -380   -699   -570       C  
ATOM   1077  N   HIS A 233       2.414   9.221  34.252  1.00 41.02           N  
ANISOU 1077  N   HIS A 233     4406   5258   5920   -527   -585   -104       N  
ATOM   1078  CA  HIS A 233       2.203   9.425  32.822  1.00 40.18           C  
ANISOU 1078  CA  HIS A 233     4172   5237   5859   -494   -551     93       C  
ATOM   1079  C   HIS A 233       3.125   8.554  31.986  1.00 39.02           C  
ANISOU 1079  C   HIS A 233     3788   5413   5623   -557   -591    162       C  
ATOM   1080  O   HIS A 233       4.291   8.891  31.792  1.00 44.46           O  
ANISOU 1080  O   HIS A 233     4413   6164   6317   -742   -640    237       O  
ATOM   1081  CB  HIS A 233       2.432  10.884  32.464  1.00 42.97           C  
ANISOU 1081  CB  HIS A 233     4645   5352   6329   -621   -532    221       C  
ATOM   1082  CG  HIS A 233       1.501  11.821  33.157  1.00 48.65           C  
ANISOU 1082  CG  HIS A 233     5626   5712   7148   -531   -443    173       C  
ATOM   1083  CD2 HIS A 233       1.717  12.724  34.141  1.00 55.03           C  
ANISOU 1083  CD2 HIS A 233     6696   6204   8008   -648   -435     40       C  
ATOM   1084  ND1 HIS A 233       0.155  11.883  32.866  1.00 49.25           N  
ANISOU 1084  ND1 HIS A 233     5717   5720   7274   -283   -333    266       N  
ATOM   1085  CE1 HIS A 233      -0.416  12.799  33.626  1.00 52.55           C  
ANISOU 1085  CE1 HIS A 233     6394   5786   7786   -220   -228    219       C  
ATOM   1086  NE2 HIS A 233       0.510  13.321  34.411  1.00 59.00           N  
ANISOU 1086  NE2 HIS A 233     7390   6432   8594   -441   -285     58       N  
ATOM   1087  N   TYR A 234       2.609   7.432  31.501  1.00 31.81           N  
ANISOU 1087  N   TYR A 234     2749   4697   4641   -406   -560    138       N  
ATOM   1088  CA  TYR A 234       3.415   6.531  30.701  1.00 30.85           C  
ANISOU 1088  CA  TYR A 234     2444   4856   4421   -428   -555    180       C  
ATOM   1089  C   TYR A 234       3.363   6.842  29.215  1.00 37.34           C  
ANISOU 1089  C   TYR A 234     3189   5807   5192   -411   -533    352       C  
ATOM   1090  O   TYR A 234       2.393   7.438  28.724  1.00 40.90           O  
ANISOU 1090  O   TYR A 234     3688   6180   5670   -333   -527    432       O  
ATOM   1091  CB  TYR A 234       2.984   5.088  30.927  1.00 24.12           C  
ANISOU 1091  CB  TYR A 234     1521   4127   3518   -290   -516     39       C  
ATOM   1092  CG  TYR A 234       3.312   4.568  32.305  1.00 37.06           C  
ANISOU 1092  CG  TYR A 234     3185   5724   5171   -288   -516    -83       C  
ATOM   1093  CD1 TYR A 234       4.631   4.281  32.664  1.00 34.93           C  
ANISOU 1093  CD1 TYR A 234     2823   5590   4859   -393   -536    -55       C  
ATOM   1094  CD2 TYR A 234       2.305   4.314  33.237  1.00 35.17           C  
ANISOU 1094  CD2 TYR A 234     3037   5346   4981   -163   -488   -193       C  
ATOM   1095  CE1 TYR A 234       4.945   3.782  33.924  1.00 36.85           C  
ANISOU 1095  CE1 TYR A 234     3068   5847   5085   -378   -548   -136       C  
ATOM   1096  CE2 TYR A 234       2.610   3.806  34.508  1.00 36.11           C  
ANISOU 1096  CE2 TYR A 234     3179   5462   5081   -135   -478   -282       C  
ATOM   1097  CZ  TYR A 234       3.933   3.546  34.848  1.00 38.17           C  
ANISOU 1097  CZ  TYR A 234     3350   5876   5275   -245   -517   -256       C  
ATOM   1098  OH  TYR A 234       4.247   3.046  36.101  1.00 38.77           O  
ANISOU 1098  OH  TYR A 234     3429   5996   5304   -207   -519   -314       O  
ATOM   1099  N   ASN A 235       4.422   6.410  28.497  1.00  0.00           N  
ATOM   1100  CA  ASN A 235       4.508   6.498  27.042  1.00  0.00           C  
ATOM   1101  C   ASN A 235       4.994   5.196  26.449  1.00  0.00           C  
ATOM   1102  O   ASN A 235       6.075   4.693  26.809  1.00  0.00           O  
ATOM   1103  CB  ASN A 235       5.453   7.669  26.647  1.00  0.00           C  
ATOM   1104  CG  ASN A 235       4.875   9.086  26.736  1.00  0.00           C  
ATOM   1105  ND2 ASN A 235       5.697  10.101  26.752  1.00  0.00           N  
ATOM   1106  OD1 ASN A 235       3.672   9.298  26.770  1.00  0.00           O  
ATOM   1107  N   TYR A 236       4.293   4.713  25.420  1.00 31.25           N  
ANISOU 1107  N   TYR A 236     2111   5850   3913   -241   -386    491       N  
ATOM   1108  CA  TYR A 236       4.712   3.546  24.643  1.00 30.21           C  
ANISOU 1108  CA  TYR A 236     1935   5943   3601   -167   -298    410       C  
ATOM   1109  C   TYR A 236       5.322   4.052  23.356  1.00 35.37           C  
ANISOU 1109  C   TYR A 236     2546   6797   4095   -153   -239    626       C  
ATOM   1110  O   TYR A 236       4.720   4.902  22.693  1.00 31.46           O  
ANISOU 1110  O   TYR A 236     2071   6329   3554   -140   -294    764       O  
ATOM   1111  CB  TYR A 236       3.543   2.604  24.364  1.00 29.89           C  
ANISOU 1111  CB  TYR A 236     1943   5936   3475    -84   -336    191       C  
ATOM   1112  CG  TYR A 236       3.022   1.976  25.638  1.00 28.03           C  
ANISOU 1112  CG  TYR A 236     1728   5512   3412    -77   -352      9       C  
ATOM   1113  CD1 TYR A 236       2.118   2.652  26.452  1.00 29.30           C  
ANISOU 1113  CD1 TYR A 236     1925   5480   3728    -85   -437     19       C  
ATOM   1114  CD2 TYR A 236       3.466   0.727  26.047  1.00 26.50           C  
ANISOU 1114  CD2 TYR A 236     1516   5322   3229    -35   -249   -143       C  
ATOM   1115  CE1 TYR A 236       1.667   2.096  27.641  1.00 32.20           C  
ANISOU 1115  CE1 TYR A 236     2310   5689   4237    -53   -428   -119       C  
ATOM   1116  CE2 TYR A 236       3.022   0.155  27.225  1.00 27.00           C  
ANISOU 1116  CE2 TYR A 236     1620   5187   3452     -9   -237   -264       C  
ATOM   1117  CZ  TYR A 236       2.129   0.843  28.026  1.00 30.36           C  
ANISOU 1117  CZ  TYR A 236     2100   5426   4009    -18   -326   -246       C  
ATOM   1118  OH  TYR A 236       1.683   0.268  29.205  1.00 25.56           O  
ANISOU 1118  OH  TYR A 236     1552   4623   3535     30   -289   -328       O  
ATOM   1119  N   MET A 237       6.534   3.566  23.043  1.00 31.17           N  
ANISOU 1119  N   MET A 237     1943   6410   3491   -136   -105    694       N  
ATOM   1120  CA  MET A 237       7.397   4.167  22.018  1.00 41.67           C  
ANISOU 1120  CA  MET A 237     3202   7916   4715   -126    -11    967       C  
ATOM   1121  C   MET A 237       7.540   3.332  20.749  1.00 43.83           C  
ANISOU 1121  C   MET A 237     3512   8455   4687     24    117    928       C  
ATOM   1122  O   MET A 237       8.444   3.540  19.938  1.00 36.89           O  
ANISOU 1122  O   MET A 237     2569   7754   3692     76    255   1149       O  
ATOM   1123  CB  MET A 237       8.796   4.428  22.601  1.00 42.93           C  
ANISOU 1123  CB  MET A 237     3219   8056   5035   -225     60   1150       C  
ATOM   1124  CG  MET A 237       8.770   5.389  23.760  1.00 33.03           C  
ANISOU 1124  CG  MET A 237     1957   6552   4040   -406    -78   1184       C  
ATOM   1125  SD  MET A 237       8.023   6.929  23.192  1.00 43.49           S  
ANISOU 1125  SD  MET A 237     3354   7749   5423   -455   -149   1371       S  
ATOM   1126  CE  MET A 237       9.228   7.441  21.951  1.00 37.21           C  
ANISOU 1126  CE  MET A 237     2406   7175   4557   -451      4   1748       C  
ATOM   1127  N   CYS A 238       6.610   2.415  20.561  1.00 44.22           N  
ANISOU 1127  N   CYS A 238     3674   8526   4603     88     74    646       N  
ATOM   1128  CA  CYS A 238       6.674   1.482  19.452  1.00 45.98           C  
ANISOU 1128  CA  CYS A 238     3985   8966   4518    211    186    519       C  
ATOM   1129  C   CYS A 238       5.247   1.009  19.197  1.00 36.17           C  
ANISOU 1129  C   CYS A 238     2854   7725   3162    201     25    249       C  
ATOM   1130  O   CYS A 238       4.468   0.849  20.150  1.00 34.21           O  
ANISOU 1130  O   CYS A 238     2601   7276   3122    132    -92    104       O  
ATOM   1131  CB  CYS A 238       7.612   0.334  19.837  1.00 36.05           C  
ANISOU 1131  CB  CYS A 238     2722   7682   3295    279    387    410       C  
ATOM   1132  SG  CYS A 238       8.575  -0.442  18.580  1.00 54.27           S  
ANISOU 1132  SG  CYS A 238     5097  10236   5286    462    668    437       S  
ATOM   1133  N   ASN A 239       4.862   0.856  17.939  1.00 44.39           N  
ANISOU 1133  N   ASN A 239     3982   9009   3875    261      4    205       N  
ATOM   1134  CA  ASN A 239       3.499   0.377  17.631  1.00 47.76           C  
ANISOU 1134  CA  ASN A 239     4487   9480   4180    216   -185    -49       C  
ATOM   1135  C   ASN A 239       3.326  -1.143  17.738  1.00 47.54           C  
ANISOU 1135  C   ASN A 239     4583   9372   4107    207   -126   -440       C  
ATOM   1136  O   ASN A 239       4.282  -1.912  17.581  1.00 49.95           O  
ANISOU 1136  O   ASN A 239     4965   9677   4338    291    100   -520       O  
ATOM   1137  CB  ASN A 239       3.042   0.828  16.232  1.00 54.37           C  
ANISOU 1137  CB  ASN A 239     5363  10648   4647    262   -279     48       C  
ATOM   1138  CG  ASN A 239       2.342   2.186  16.244  1.00 57.38           C  
ANISOU 1138  CG  ASN A 239     5620  11056   5127    241   -441    352       C  
ATOM   1139  ND2 ASN A 239       1.343   2.329  17.112  1.00 64.82           N  
ANISOU 1139  ND2 ASN A 239     6502  11802   6326    162   -596    289       N  
ATOM   1140  OD1 ASN A 239       2.673   3.078  15.469  1.00 53.95           O  
ANISOU 1140  OD1 ASN A 239     5145  10809   4544    314   -402    656       O  
ATOM   1141  N   SER A 240       2.103  -1.560  18.045  1.00 43.88           N  
ANISOU 1141  N   SER A 240     4127   8820   3725    110   -309   -657       N  
ATOM   1142  CA  SER A 240       1.738  -2.969  18.030  1.00 45.97           C  
ANISOU 1142  CA  SER A 240     4515   8993   3958     66   -279  -1038       C  
ATOM   1143  C   SER A 240       1.966  -3.570  16.661  1.00 48.43           C  
ANISOU 1143  C   SER A 240     5011   9545   3846    105   -220  -1220       C  
ATOM   1144  O   SER A 240       2.269  -4.750  16.549  1.00 54.75           O  
ANISOU 1144  O   SER A 240     5967  10243   4591    122    -60  -1507       O  
ATOM   1145  CB  SER A 240       0.263  -3.164  18.407  1.00 49.00           C  
ANISOU 1145  CB  SER A 240     4839   9292   4487    -70   -523  -1190       C  
ATOM   1146  OG  SER A 240       0.010  -2.812  19.747  1.00 36.31           O  
ANISOU 1146  OG  SER A 240     3100   7434   3261    -82   -537  -1073       O  
ATOM   1147  N   SER A 241       1.825  -2.760  15.617  1.00 46.26           N  
ANISOU 1147  N   SER A 241     4734   9583   3259    134   -328  -1048       N  
ATOM   1148  CA  SER A 241       1.928  -3.273  14.253  1.00 49.37           C  
ANISOU 1148  CA  SER A 241     5326  10255   3177    175   -299  -1229       C  
ATOM   1149  C   SER A 241       3.351  -3.216  13.694  1.00 58.81           C  
ANISOU 1149  C   SER A 241     6606  11562   4176    368     13  -1070       C  
ATOM   1150  O   SER A 241       3.597  -3.664  12.572  1.00 64.05           O  
ANISOU 1150  O   SER A 241     7468  12451   4419    447    102  -1213       O  
ATOM   1151  CB  SER A 241       0.994  -2.497  13.342  1.00 51.62           C  
ANISOU 1151  CB  SER A 241     5559  10881   3175    126   -580  -1110       C  
ATOM   1152  OG  SER A 241       1.449  -1.167  13.211  1.00 74.66           O  
ANISOU 1152  OG  SER A 241     8332  13928   6107    237   -543   -654       O  
ATOM   1153  N   CYS A 242       4.285  -2.680  14.476  1.00 56.58           N  
ANISOU 1153  N   CYS A 242     6174  11132   4190    442    181   -774       N  
ATOM   1154  CA  CYS A 242       5.682  -2.562  14.040  1.00 56.95           C  
ANISOU 1154  CA  CYS A 242     6235  11286   4116    621    485   -550       C  
ATOM   1155  C   CYS A 242       6.282  -3.902  13.671  1.00 51.37           C  
ANISOU 1155  C   CYS A 242     5748  10534   3234    735    759   -842       C  
ATOM   1156  O   CYS A 242       6.466  -4.761  14.528  1.00 70.70           O  
ANISOU 1156  O   CYS A 242     8210  12705   5948    723    876  -1016       O  
ATOM   1157  CB  CYS A 242       6.549  -1.932  15.136  1.00 52.99           C  
ANISOU 1157  CB  CYS A 242     5512  10599   4023    625    586   -231       C  
ATOM   1158  SG  CYS A 242       6.501  -0.144  15.238  1.00 45.22           S  
ANISOU 1158  SG  CYS A 242     4310   9689   3183    567    429    230       S  
ATOM   1159  N   MET A 243       6.617  -4.068  12.403  1.00 55.15           N  
ANISOU 1159  N   MET A 243     6409  11283   3263    869    890   -876       N  
ATOM   1160  CA  MET A 243       7.314  -5.264  11.966  1.00 60.55           C  
ANISOU 1160  CA  MET A 243     7343  11799   3862    994   1182  -1093       C  
ATOM   1161  C   MET A 243       8.730  -5.254  12.541  1.00 59.80           C  
ANISOU 1161  C   MET A 243     7107  11565   4051   1152   1504   -777       C  
ATOM   1162  O   MET A 243       9.406  -4.227  12.541  1.00 55.93           O  
ANISOU 1162  O   MET A 243     6405  11209   3638   1207   1535   -354       O  
ATOM   1163  CB  MET A 243       7.312  -5.340  10.443  1.00 69.34           C  
ANISOU 1163  CB  MET A 243     8710  13098   4539   1070   1200  -1151       C  
ATOM   1164  CG  MET A 243       7.879  -4.108   9.765  1.00 73.00           C  
ANISOU 1164  CG  MET A 243     9027  13838   4872   1189   1224   -688       C  
ATOM   1165  SD  MET A 243       7.311  -3.942   8.063  1.00 88.11           S  
ANISOU 1165  SD  MET A 243    11179  16047   6253   1214   1086   -770       S  
ATOM   1166  CE  MET A 243       5.594  -3.627   8.422  1.00 99.54           C  
ANISOU 1166  CE  MET A 243    12522  17575   7724    948    604   -958       C  
ATOM   1167  N   GLY A 244       9.169  -6.387  13.068  1.00 60.70           N  
ANISOU 1167  N   GLY A 244     7318  11380   4364   1205   1729   -956       N  
ATOM   1168  CA  GLY A 244      10.501  -6.463  13.640  1.00 59.67           C  
ANISOU 1168  CA  GLY A 244     7036  11098   4538   1334   2000   -638       C  
ATOM   1169  C   GLY A 244      10.506  -6.160  15.125  1.00 57.70           C  
ANISOU 1169  C   GLY A 244     6497  10718   4707   1236   1897   -496       C  
ATOM   1170  O   GLY A 244      11.552  -6.166  15.779  1.00 56.55           O  
ANISOU 1170  O   GLY A 244     6189  10441   4858   1290   2039   -221       O  
ATOM   1171  N   GLY A 245       9.328  -5.892  15.668  1.00 55.89           N  
ANISOU 1171  N   GLY A 245     6203  10528   4504   1073   1629   -686       N  
ATOM   1172  CA  GLY A 245       9.216  -5.652  17.087  1.00 51.49           C  
ANISOU 1172  CA  GLY A 245     5417   9795   4353    963   1511   -588       C  
ATOM   1173  C   GLY A 245       8.203  -6.585  17.707  1.00 50.58           C  
ANISOU 1173  C   GLY A 245     5411   9416   4391    859   1411   -968       C  
ATOM   1174  O   GLY A 245       8.337  -7.815  17.636  1.00 48.89           O  
ANISOU 1174  O   GLY A 245     5363   9047   4164    951   1639  -1217       O  
ATOM   1175  N   MET A 246       7.180  -5.990  18.310  1.00 50.25           N  
ANISOU 1175  N   MET A 246     5275   9304   4512    674   1091   -995       N  
ATOM   1176  CA  MET A 246       6.064  -6.741  18.852  1.00 48.66           C  
ANISOU 1176  CA  MET A 246     5145   8877   4468    555    962  -1317       C  
ATOM   1177  C   MET A 246       5.422  -7.511  17.709  1.00 51.97           C  
ANISOU 1177  C   MET A 246     5827   9349   4572    522    949  -1685       C  
ATOM   1178  O   MET A 246       5.089  -8.690  17.858  1.00 53.19           O  
ANISOU 1178  O   MET A 246     6124   9281   4805    501   1049  -2003       O  
ATOM   1179  CB  MET A 246       5.059  -5.799  19.530  1.00 43.07           C  
ANISOU 1179  CB  MET A 246     4285   8137   3944    390    632  -1228       C  
ATOM   1180  CG  MET A 246       5.628  -5.108  20.759  1.00 35.71           C  
ANISOU 1180  CG  MET A 246     3142   7115   3312    397    632   -934       C  
ATOM   1181  SD  MET A 246       4.498  -4.086  21.737  1.00 44.73           S  
ANISOU 1181  SD  MET A 246     4153   8149   4693    246    319   -851       S  
ATOM   1182  CE  MET A 246       4.516  -2.526  20.844  1.00 33.74           C  
ANISOU 1182  CE  MET A 246     2716   6998   3105    211    166   -576       C  
ATOM   1183  N   ASN A 247       5.331  -6.854  16.553  1.00 53.74           N  
ANISOU 1183  N   ASN A 247     6120   9868   4431    524    846  -1632       N  
ATOM   1184  CA  ASN A 247       4.827  -7.475  15.337  1.00 61.97           C  
ANISOU 1184  CA  ASN A 247     7429  11039   5079    493    814  -1972       C  
ATOM   1185  C   ASN A 247       3.450  -8.111  15.513  1.00 61.51           C  
ANISOU 1185  C   ASN A 247     7435  10830   5104    270    563  -2339       C  
ATOM   1186  O   ASN A 247       3.275  -9.320  15.343  1.00 53.09           O  
ANISOU 1186  O   ASN A 247     6581   9577   4013    233    679  -2715       O  
ATOM   1187  CB  ASN A 247       5.824  -8.516  14.842  1.00 71.95           C  
ANISOU 1187  CB  ASN A 247     8923  12236   6180    685   1212  -2125       C  
ATOM   1188  CG  ASN A 247       5.455  -9.075  13.491  1.00 81.02           C  
ANISOU 1188  CG  ASN A 247    10405  13446   6933    652   1178  -2416       C  
ATOM   1189  ND2 ASN A 247       5.954 -10.268  13.197  1.00 84.17           N  
ANISOU 1189  ND2 ASN A 247    11088  13571   7324    747   1473  -2620       N  
ATOM   1190  OD1 ASN A 247       4.709  -8.455  12.728  1.00 84.81           O  
ANISOU 1190  OD1 ASN A 247    10898  14189   7135    540    887  -2432       O  
ATOM   1191  N   ARG A 248       2.489  -7.269  15.883  1.00 59.19           N  
ANISOU 1191  N   ARG A 248     6945  10601   4941    124    235  -2206       N  
ATOM   1192  CA  ARG A 248       1.079  -7.638  16.029  1.00 61.26           C  
ANISOU 1192  CA  ARG A 248     7191  10787   5300    -99    -53  -2460       C  
ATOM   1193  C   ARG A 248       0.812  -8.599  17.193  1.00 60.34           C  
ANISOU 1193  C   ARG A 248     7040  10269   5616   -158     44  -2631       C  
ATOM   1194  O   ARG A 248      -0.331  -9.019  17.400  1.00 61.29           O  
ANISOU 1194  O   ARG A 248     7126  10284   5877   -348   -161  -2833       O  
ATOM   1195  CB  ARG A 248       0.550  -8.207  14.705  1.00 67.91           C  
ANISOU 1195  CB  ARG A 248     8269  11832   5702   -207   -178  -2812       C  
ATOM   1196  CG  ARG A 248       0.603  -7.172  13.583  1.00 74.56           C  
ANISOU 1196  CG  ARG A 248     9107  13090   6132   -147   -317  -2577       C  
ATOM   1197  CD  ARG A 248      -0.039  -7.638  12.279  1.00 84.21           C  
ANISOU 1197  CD  ARG A 248    10553  14409   7035   -260   -483  -2784       C  
ATOM   1198  NE  ARG A 248       0.634  -8.824  11.751  1.00 90.77           N  
ANISOU 1198  NE  ARG A 248    11725  15051   7712   -198   -212  -3092       N  
ATOM   1199  CZ  ARG A 248       1.859  -8.825  11.229  1.00 93.94           C  
ANISOU 1199  CZ  ARG A 248    12287  15514   7890     36    105  -2993       C  
ATOM   1200  NH1 ARG A 248       2.568  -7.702  11.185  1.00 92.82           N1+
ANISOU 1200  NH1 ARG A 248    11971  15628   7667    211    182  -2592       N1+
ATOM   1201  NH2 ARG A 248       2.386  -9.956  10.774  1.00 97.40           N  
ANISOU 1201  NH2 ARG A 248    13062  15728   8217    102    366  -3265       N  
ATOM   1202  N   ARG A 249       1.848  -8.919  17.971  1.00 57.00           N  
ANISOU 1202  N   ARG A 249     6597   9642   5417      6    353  -2511       N  
ATOM   1203  CA  ARG A 249       1.663  -9.728  19.174  1.00 53.29           C  
ANISOU 1203  CA  ARG A 249     6062   8816   5369    -10    466  -2589       C  
ATOM   1204  C   ARG A 249       1.246  -8.865  20.362  1.00 46.13           C  
ANISOU 1204  C   ARG A 249     4889   7860   4778    -35    307  -2303       C  
ATOM   1205  O   ARG A 249       1.924  -7.896  20.710  1.00 42.52           O  
ANISOU 1205  O   ARG A 249     4308   7513   4336     63    324  -1983       O  
ATOM   1206  CB  ARG A 249       2.937 -10.499  19.526  1.00 44.17           C  
ANISOU 1206  CB  ARG A 249     4983   7489   4312    198    874  -2556       C  
ATOM   1207  CG  ARG A 249       3.293 -11.586  18.559  1.00 48.22           C  
ANISOU 1207  CG  ARG A 249     5797   7936   4587    249   1110  -2883       C  
ATOM   1208  CD  ARG A 249       4.673 -12.181  18.860  1.00 52.89           C  
ANISOU 1208  CD  ARG A 249     6429   8401   5266    513   1552  -2749       C  
ATOM   1209  NE  ARG A 249       5.754 -11.190  18.795  1.00 48.75           N  
ANISOU 1209  NE  ARG A 249     5754   8142   4627    676   1623  -2345       N  
ATOM   1210  CZ  ARG A 249       7.033 -11.450  19.065  1.00 52.46           C  
ANISOU 1210  CZ  ARG A 249     6200   8525   5206    891   1928  -2051       C  
ATOM   1211  NH1 ARG A 249       7.412 -12.682  19.396  1.00 48.67           N1+
ANISOU 1211  NH1 ARG A 249     5864   7702   4926   1010   2204  -2084       N1+
ATOM   1212  NH2 ARG A 249       7.941 -10.483  18.979  1.00 46.31           N  
ANISOU 1212  NH2 ARG A 249     5257   7985   4352    982   1947  -1681       N  
ATOM   1213  N   PRO A 250       0.132  -9.235  21.004  1.00 45.53           N  
ANISOU 1213  N   PRO A 250     4733   7601   4965   -169    165  -2420       N  
ATOM   1214  CA  PRO A 250      -0.360  -8.514  22.192  1.00 42.02           C  
ANISOU 1214  CA  PRO A 250     4067   7081   4819   -171     47  -2174       C  
ATOM   1215  C   PRO A 250       0.576  -8.592  23.421  1.00 41.38           C  
ANISOU 1215  C   PRO A 250     3905   6834   4982     -8    282  -1977       C  
ATOM   1216  O   PRO A 250       1.232  -9.618  23.658  1.00 38.78           O  
ANISOU 1216  O   PRO A 250     3650   6342   4745     85    547  -2072       O  
ATOM   1217  CB  PRO A 250      -1.704  -9.199  22.483  1.00 40.68           C  
ANISOU 1217  CB  PRO A 250     3848   6738   4869   -335    -93  -2375       C  
ATOM   1218  CG  PRO A 250      -1.592 -10.577  21.834  1.00 40.58           C  
ANISOU 1218  CG  PRO A 250     4043   6583   4791   -401     56  -2743       C  
ATOM   1219  CD  PRO A 250      -0.723 -10.376  20.622  1.00 42.52           C  
ANISOU 1219  CD  PRO A 250     4475   7068   4615   -334    121  -2797       C  
ATOM   1220  N   ILE A 251       0.621  -7.505  24.195  1.00 37.75           N  
ANISOU 1220  N   ILE A 251     3757   6711   3873    496    217     56       N  
ATOM   1221  CA  ILE A 251       1.460  -7.438  25.385  1.00 36.21           C  
ANISOU 1221  CA  ILE A 251     3550   6408   3799    551    271     58       C  
ATOM   1222  C   ILE A 251       0.691  -7.016  26.626  1.00 40.59           C  
ANISOU 1222  C   ILE A 251     4128   6749   4547    521    234    119       C  
ATOM   1223  O   ILE A 251      -0.384  -6.431  26.540  1.00 44.14           O  
ANISOU 1223  O   ILE A 251     4566   7160   5047    464    171    189       O  
ATOM   1224  CB  ILE A 251       2.665  -6.445  25.230  1.00 42.26           C  
ANISOU 1224  CB  ILE A 251     4217   7329   4509    520    326    184       C  
ATOM   1225  CG1 ILE A 251       2.187  -5.003  25.036  1.00 40.80           C  
ANISOU 1225  CG1 ILE A 251     4012   7134   4357    401    263    395       C  
ATOM   1226  CG2 ILE A 251       3.650  -6.878  24.128  1.00 38.64           C  
ANISOU 1226  CG2 ILE A 251     3694   7150   3838    551    394    102       C  
ATOM   1227  CD1 ILE A 251       3.323  -3.985  25.195  1.00 38.93           C  
ANISOU 1227  CD1 ILE A 251     3710   6981   4101    327    298    536       C  
ATOM   1228  N   LEU A 252       1.253  -7.345  27.788  1.00 42.72           N  
ANISOU 1228  N   LEU A 252     4420   6898   4914    569    270     78       N  
ATOM   1229  CA  LEU A 252       0.738  -6.876  29.069  1.00 37.42           C  
ANISOU 1229  CA  LEU A 252     3757   6061   4400    535    255    127       C  
ATOM   1230  C   LEU A 252       1.740  -5.914  29.693  1.00 38.90           C  
ANISOU 1230  C   LEU A 252     3888   6252   4639    534    289    225       C  
ATOM   1231  O   LEU A 252       2.944  -6.061  29.497  1.00 44.10           O  
ANISOU 1231  O   LEU A 252     4511   7016   5230    574    334    216       O  
ATOM   1232  CB  LEU A 252       0.508  -8.039  30.016  1.00 33.37           C  
ANISOU 1232  CB  LEU A 252     3337   5400   3941    553    252     16       C  
ATOM   1233  CG  LEU A 252      -0.311  -9.209  29.498  1.00 39.11           C  
ANISOU 1233  CG  LEU A 252     4153   6097   4610    531    210    -97       C  
ATOM   1234  CD1 LEU A 252      -0.467 -10.241  30.594  1.00 39.24           C  
ANISOU 1234  CD1 LEU A 252     4290   5937   4684    510    189   -167       C  
ATOM   1235  CD2 LEU A 252      -1.657  -8.770  28.962  1.00 45.62           C  
ANISOU 1235  CD2 LEU A 252     4930   6974   5430    443    164    -64       C  
ATOM   1236  N   THR A 253       1.254  -4.934  30.440  1.00 37.78           N  
ANISOU 1236  N   THR A 253     3731   6010   4612    489    263    303       N  
ATOM   1237  CA  THR A 253       2.134  -4.159  31.304  1.00 35.17           C  
ANISOU 1237  CA  THR A 253     3377   5639   4348    474    286    369       C  
ATOM   1238  C   THR A 253       1.918  -4.571  32.751  1.00 30.13           C  
ANISOU 1238  C   THR A 253     2777   4862   3807    485    300    300       C  
ATOM   1239  O   THR A 253       0.781  -4.662  33.226  1.00 26.31           O  
ANISOU 1239  O   THR A 253     2312   4300   3383    465    280    257       O  
ATOM   1240  CB  THR A 253       1.917  -2.661  31.180  1.00 35.73           C  
ANISOU 1240  CB  THR A 253     3427   5675   4474    414    233    500       C  
ATOM   1241  CG2 THR A 253       2.864  -1.931  32.135  1.00 31.15           C  
ANISOU 1241  CG2 THR A 253     2839   5040   3956    377    250    551       C  
ATOM   1242  OG1 THR A 253       2.175  -2.248  29.833  1.00 37.01           O  
ANISOU 1242  OG1 THR A 253     3569   5973   4520    370    208    597       O  
ATOM   1243  N   ILE A 254       3.015  -4.871  33.429  1.00 30.67           N  
ANISOU 1243  N   ILE A 254     2847   4933   3874    509    332    286       N  
ATOM   1244  CA  ILE A 254       2.971  -5.263  34.824  1.00 30.66           C  
ANISOU 1244  CA  ILE A 254     2893   4816   3938    504    336    241       C  
ATOM   1245  C   ILE A 254       3.465  -4.115  35.690  1.00 32.74           C  
ANISOU 1245  C   ILE A 254     3121   5048   4269    457    339    305       C  
ATOM   1246  O   ILE A 254       4.593  -3.654  35.522  1.00 31.59           O  
ANISOU 1246  O   ILE A 254     2925   4981   4096    450    348    363       O  
ATOM   1247  CB  ILE A 254       3.836  -6.502  35.075  1.00 29.69           C  
ANISOU 1247  CB  ILE A 254     2816   4695   3769    581    338    176       C  
ATOM   1248  CG1 ILE A 254       3.412  -7.628  34.137  1.00 28.07           C  
ANISOU 1248  CG1 ILE A 254     2672   4499   3496    633    320     92       C  
ATOM   1249  CG2 ILE A 254       3.769  -6.936  36.573  1.00 26.74           C  
ANISOU 1249  CG2 ILE A 254     2517   4195   3446    552    321    155       C  
ATOM   1250  CD1 ILE A 254       4.307  -8.839  34.220  1.00 29.51           C  
ANISOU 1250  CD1 ILE A 254     2914   4661   3638    752    296      8       C  
ATOM   1251  N   ILE A 255       2.622  -3.669  36.618  1.00 34.71           N  
ANISOU 1251  N   ILE A 255     3391   5201   4596    416    332    282       N  
ATOM   1252  CA  ILE A 255       2.987  -2.606  37.548  1.00 38.32           C  
ANISOU 1252  CA  ILE A 255     3837   5605   5117    373    326    310       C  
ATOM   1253  C   ILE A 255       3.211  -3.214  38.927  1.00 37.38           C  
ANISOU 1253  C   ILE A 255     3759   5448   4998    351    345    255       C  
ATOM   1254  O   ILE A 255       2.293  -3.827  39.499  1.00 37.01           O  
ANISOU 1254  O   ILE A 255     3747   5368   4946    328    357    190       O  
ATOM   1255  CB  ILE A 255       1.894  -1.488  37.702  1.00 29.74           C  
ANISOU 1255  CB  ILE A 255     2740   4442   4119    364    295    294       C  
ATOM   1256  CG1 ILE A 255       1.386  -0.942  36.352  1.00 26.91           C  
ANISOU 1256  CG1 ILE A 255     2361   4101   3763    391    246    357       C  
ATOM   1257  CG2 ILE A 255       2.434  -0.344  38.556  1.00 22.12           C  
ANISOU 1257  CG2 ILE A 255     1787   3401   3216    325    275    311       C  
ATOM   1258  CD1 ILE A 255       2.380  -0.127  35.609  1.00 23.00           C  
ANISOU 1258  CD1 ILE A 255     1869   3629   3242    348    211    484       C  
ATOM   1259  N   THR A 256       4.419  -3.044  39.463  1.00 31.24           N  
ANISOU 1259  N   THR A 256     2970   4692   4207    338    341    291       N  
ATOM   1260  CA  THR A 256       4.722  -3.565  40.788  1.00 29.35           C  
ANISOU 1260  CA  THR A 256     2775   4422   3953    312    338    258       C  
ATOM   1261  C   THR A 256       5.017  -2.440  41.747  1.00 32.83           C  
ANISOU 1261  C   THR A 256     3203   4836   4434    241    332    261       C  
ATOM   1262  O   THR A 256       5.596  -1.405  41.377  1.00 32.62           O  
ANISOU 1262  O   THR A 256     3136   4819   4437    214    315    313       O  
ATOM   1263  CB  THR A 256       5.913  -4.505  40.825  1.00 28.64           C  
ANISOU 1263  CB  THR A 256     2688   4386   3808    373    314    277       C  
ATOM   1264  CG2 THR A 256       5.560  -5.844  40.206  1.00 27.33           C  
ANISOU 1264  CG2 THR A 256     2583   4198   3602    450    300    239       C  
ATOM   1265  OG1 THR A 256       7.010  -3.903  40.136  1.00 35.28           O  
ANISOU 1265  OG1 THR A 256     3432   5337   4638    391    315    332       O  
ATOM   1266  N   LEU A 257       4.556  -2.641  42.973  1.00 36.37           N  
ANISOU 1266  N   LEU A 257     3698   5250   4870    191    341    202       N  
ATOM   1267  CA  LEU A 257       4.846  -1.740  44.069  1.00 36.50           C  
ANISOU 1267  CA  LEU A 257     3718   5247   4902    122    334    174       C  
ATOM   1268  C   LEU A 257       5.975  -2.354  44.918  1.00 34.26           C  
ANISOU 1268  C   LEU A 257     3455   5009   4552     95    302    211       C  
ATOM   1269  O   LEU A 257       5.856  -3.484  45.401  1.00 34.87           O  
ANISOU 1269  O   LEU A 257     3592   5089   4569     96    291    211       O  
ATOM   1270  CB  LEU A 257       3.582  -1.524  44.885  1.00 34.07           C  
ANISOU 1270  CB  LEU A 257     3427   4920   4597     83    371     65       C  
ATOM   1271  CG  LEU A 257       3.445  -0.186  45.578  1.00 37.07           C  
ANISOU 1271  CG  LEU A 257     3800   5256   5028     55    367    -13       C  
ATOM   1272  CD1 LEU A 257       3.462   0.936  44.545  1.00 32.50           C  
ANISOU 1272  CD1 LEU A 257     3204   4594   4550    109    323     21       C  
ATOM   1273  CD2 LEU A 257       2.137  -0.201  46.335  1.00 40.13           C  
ANISOU 1273  CD2 LEU A 257     4171   5684   5393     40    420   -151       C  
ATOM   1274  N   GLU A 258       7.077  -1.634  45.093  1.00 30.79           N  
ANISOU 1274  N   GLU A 258     2974   4604   4122     62    270    252       N  
ATOM   1275  CA  GLU A 258       8.200  -2.190  45.856  1.00 32.29           C  
ANISOU 1275  CA  GLU A 258     3158   4862   4250     52    222    289       C  
ATOM   1276  C   GLU A 258       8.843  -1.190  46.846  1.00 32.49           C  
ANISOU 1276  C   GLU A 258     3173   4905   4268    -59    191    278       C  
ATOM   1277  O   GLU A 258       8.749   0.029  46.662  1.00 33.47           O  
ANISOU 1277  O   GLU A 258     3287   4982   4448   -120    196    261       O  
ATOM   1278  CB  GLU A 258       9.276  -2.746  44.890  1.00 30.70           C  
ANISOU 1278  CB  GLU A 258     2872   4760   4034    147    198    353       C  
ATOM   1279  CG  GLU A 258       9.733  -1.759  43.833  1.00 31.84           C  
ANISOU 1279  CG  GLU A 258     2922   4967   4208    118    217    399       C  
ATOM   1280  CD  GLU A 258      10.758  -2.338  42.843  1.00 32.11           C  
ANISOU 1280  CD  GLU A 258     2839   5163   4198    208    215    438       C  
ATOM   1281  OE1 GLU A 258      10.375  -3.154  41.962  1.00 34.03           O  
ANISOU 1281  OE1 GLU A 258     3091   5411   4428    319    239    415       O  
ATOM   1282  OE2 GLU A 258      11.950  -1.953  42.955  1.00 25.32           O1-
ANISOU 1282  OE2 GLU A 258     1868   4445   3306    162    191    477       O1-
ATOM   1283  N   ASP A 259       9.469  -1.704  47.910  1.00 32.87           N  
ANISOU 1283  N   ASP A 259     3240   5004   4244    -89    143    289       N  
ATOM   1284  CA  ASP A 259      10.142  -0.827  48.880  1.00 34.13           C  
ANISOU 1284  CA  ASP A 259     3389   5199   4379   -206    103    273       C  
ATOM   1285  C   ASP A 259      11.525  -0.410  48.374  1.00 35.83           C  
ANISOU 1285  C   ASP A 259     3486   5525   4603   -223     55    348       C  
ATOM   1286  O   ASP A 259      11.957  -0.844  47.302  1.00 39.87           O  
ANISOU 1286  O   ASP A 259     3913   6107   5128   -133     64    402       O  
ATOM   1287  CB  ASP A 259      10.273  -1.495  50.258  1.00 35.41           C  
ANISOU 1287  CB  ASP A 259     3618   5399   4439   -254     56    264       C  
ATOM   1288  CG  ASP A 259      11.142  -2.768  50.241  1.00 43.35           C  
ANISOU 1288  CG  ASP A 259     4605   6471   5395   -154    -25    353       C  
ATOM   1289  OD1 ASP A 259      11.960  -2.965  49.321  1.00 44.47           O  
ANISOU 1289  OD1 ASP A 259     4642   6680   5574    -53    -45    399       O  
ATOM   1290  OD2 ASP A 259      11.042  -3.572  51.193  1.00 46.55           O1-
ANISOU 1290  OD2 ASP A 259     5103   6871   5715   -176    -79    372       O1-
ATOM   1291  N   SER A 260      12.235   0.379  49.177  1.00 34.31           N  
ANISOU 1291  N   SER A 260     3277   5375   4385   -351      6    341       N  
ATOM   1292  CA  SER A 260      13.540   0.931  48.793  1.00 39.29           C  
ANISOU 1292  CA  SER A 260     3779   6140   5010   -423    -40    410       C  
ATOM   1293  C   SER A 260      14.612  -0.143  48.542  1.00 40.97           C  
ANISOU 1293  C   SER A 260     3854   6543   5169   -307    -82    472       C  
ATOM   1294  O   SER A 260      15.629   0.133  47.910  1.00 38.27           O  
ANISOU 1294  O   SER A 260     3358   6370   4815   -336    -96    524       O  
ATOM   1295  CB  SER A 260      14.047   1.903  49.864  1.00 42.85           C  
ANISOU 1295  CB  SER A 260     4254   6596   5430   -602   -101    378       C  
ATOM   1296  OG  SER A 260      14.096   1.284  51.137  1.00 43.97           O  
ANISOU 1296  OG  SER A 260     4443   6774   5489   -600   -144    343       O  
ATOM   1297  N   SER A 261      14.389  -1.351  49.056  1.00 44.39           N  
ANISOU 1297  N   SER A 261     4344   6956   5565   -180   -113    462       N  
ATOM   1298  CA  SER A 261      15.310  -2.470  48.856  1.00 45.09           C  
ANISOU 1298  CA  SER A 261     4331   7181   5620    -15   -180    498       C  
ATOM   1299  C   SER A 261      14.869  -3.373  47.704  1.00 47.30           C  
ANISOU 1299  C   SER A 261     4617   7421   5936    166   -134    487       C  
ATOM   1300  O   SER A 261      15.513  -4.386  47.448  1.00 50.99           O  
ANISOU 1300  O   SER A 261     5020   7967   6385    345   -193    487       O  
ATOM   1301  CB  SER A 261      15.400  -3.336  50.119  1.00 49.65           C  
ANISOU 1301  CB  SER A 261     5004   7728   6131     22   -284    510       C  
ATOM   1302  OG  SER A 261      15.993  -2.658  51.204  1.00 55.44           O  
ANISOU 1302  OG  SER A 261     5715   8541   6808   -130   -347    517       O  
ATOM   1303  N   GLY A 262      13.771  -3.028  47.023  1.00 44.93           N  
ANISOU 1303  N   GLY A 262     4394   6993   5683    135    -42    464       N  
ATOM   1304  CA  GLY A 262      13.301  -3.809  45.886  1.00 37.67           C  
ANISOU 1304  CA  GLY A 262     3485   6041   4787    282      1    446       C  
ATOM   1305  C   GLY A 262      12.355  -4.961  46.225  1.00 35.60           C  
ANISOU 1305  C   GLY A 262     3394   5613   4521    362    -21    421       C  
ATOM   1306  O   GLY A 262      12.012  -5.755  45.352  1.00 35.25           O  
ANISOU 1306  O   GLY A 262     3376   5528   4489    486     -7    396       O  
ATOM   1307  N   ASN A 263      11.940  -5.070  47.488  1.00 38.97           N  
ANISOU 1307  N   ASN A 263     3941   5954   4913    271    -61    427       N  
ATOM   1308  CA  ASN A 263      11.002  -6.125  47.911  1.00 37.87           C  
ANISOU 1308  CA  ASN A 263     3976   5670   4745    283    -87    425       C  
ATOM   1309  C   ASN A 263       9.553  -5.844  47.441  1.00 34.36           C  
ANISOU 1309  C   ASN A 263     3590   5134   4330    211     18    378       C  
ATOM   1310  O   ASN A 263       9.081  -4.708  47.524  1.00 30.06           O  
ANISOU 1310  O   ASN A 263     3006   4602   3813    110     89    342       O  
ATOM   1311  CB  ASN A 263      11.036  -6.287  49.441  1.00 36.92           C  
ANISOU 1311  CB  ASN A 263     3955   5531   4542    171   -159    457       C  
ATOM   1312  CG  ASN A 263      12.420  -6.688  49.963  1.00 42.25           C  
ANISOU 1312  CG  ASN A 263     4576   6294   5182    257   -292    510       C  
ATOM   1313  ND2 ASN A 263      13.010  -5.830  50.797  1.00 40.88           N  
ANISOU 1313  ND2 ASN A 263     4335   6226   4970    142   -311    518       N  
ATOM   1314  OD1 ASN A 263      12.936  -7.763  49.642  1.00 43.14           O  
ANISOU 1314  OD1 ASN A 263     4711   6380   5303    432   -390    534       O  
ATOM   1315  N   LEU A 264       8.842  -6.883  47.000  1.00 32.54           N  
ANISOU 1315  N   LEU A 264     3461   4809   4095    264     10    372       N  
ATOM   1316  CA  LEU A 264       7.487  -6.730  46.448  1.00 33.60           C  
ANISOU 1316  CA  LEU A 264     3624   4890   4254    206     97    326       C  
ATOM   1317  C   LEU A 264       6.428  -6.338  47.497  1.00 35.52           C  
ANISOU 1317  C   LEU A 264     3921   5123   4451     36    146    293       C  
ATOM   1318  O   LEU A 264       6.321  -6.958  48.555  1.00 40.57           O  
ANISOU 1318  O   LEU A 264     4666   5744   5004    -55     98    323       O  
ATOM   1319  CB  LEU A 264       7.056  -8.035  45.771  1.00 33.87           C  
ANISOU 1319  CB  LEU A 264     3761   4829   4279    282     58    325       C  
ATOM   1320  CG  LEU A 264       5.673  -8.068  45.109  1.00 34.06           C  
ANISOU 1320  CG  LEU A 264     3806   4817   4316    221    130    280       C  
ATOM   1321  CD1 LEU A 264       5.623  -7.148  43.870  1.00 33.47           C  
ANISOU 1321  CD1 LEU A 264     3596   4812   4308    288    202    249       C  
ATOM   1322  CD2 LEU A 264       5.263  -9.497  44.771  1.00 33.58           C  
ANISOU 1322  CD2 LEU A 264     3895   4639   4224    244     63    284       C  
ATOM   1323  N   LEU A 265       5.672  -5.285  47.200  1.00 31.84           N  
ANISOU 1323  N   LEU A 265     3380   4683   4034     -3    232    228       N  
ATOM   1324  CA  LEU A 265       4.618  -4.780  48.084  1.00 30.04           C  
ANISOU 1324  CA  LEU A 265     3160   4486   3768   -129    294    152       C  
ATOM   1325  C   LEU A 265       3.243  -4.923  47.440  1.00 35.09           C  
ANISOU 1325  C   LEU A 265     3779   5126   4428   -139    357     94       C  
ATOM   1326  O   LEU A 265       2.236  -5.083  48.131  1.00 32.55           O  
ANISOU 1326  O   LEU A 265     3468   4861   4038   -252    404     36       O  
ATOM   1327  CB  LEU A 265       4.858  -3.319  48.455  1.00 27.67           C  
ANISOU 1327  CB  LEU A 265     2787   4214   3514   -147    322     89       C  
ATOM   1328  CG  LEU A 265       6.157  -2.986  49.170  1.00 29.77           C  
ANISOU 1328  CG  LEU A 265     3053   4507   3752   -174    260    131       C  
ATOM   1329  CD1 LEU A 265       6.226  -1.481  49.456  1.00 23.88           C  
ANISOU 1329  CD1 LEU A 265     2260   3754   3058   -213    279     52       C  
ATOM   1330  CD2 LEU A 265       6.277  -3.808  50.433  1.00 24.38           C  
ANISOU 1330  CD2 LEU A 265     2460   3863   2941   -269    219    158       C  
ATOM   1331  N   GLY A 266       3.205  -4.813  46.113  1.00 40.91           N  
ANISOU 1331  N   GLY A 266     4467   5831   5246    -32    360    106       N  
ATOM   1332  CA  GLY A 266       1.968  -4.991  45.365  1.00 42.23           C  
ANISOU 1332  CA  GLY A 266     4604   6008   5432    -31    400     60       C  
ATOM   1333  C   GLY A 266       2.190  -5.207  43.870  1.00 38.93           C  
ANISOU 1333  C   GLY A 266     4166   5559   5067     82    378    100       C  
ATOM   1334  O   GLY A 266       3.209  -4.785  43.311  1.00 34.01           O  
ANISOU 1334  O   GLY A 266     3510   4933   4481    163    355    148       O  
ATOM   1335  N   ARG A 267       1.224  -5.847  43.218  1.00 35.68           N  
ANISOU 1335  N   ARG A 267     3765   5152   4641     68    387     77       N  
ATOM   1336  CA  ARG A 267       1.320  -6.082  41.790  1.00 39.33           C  
ANISOU 1336  CA  ARG A 267     4211   5603   5129    162    367     99       C  
ATOM   1337  C   ARG A 267      -0.039  -6.082  41.131  1.00 36.38           C  
ANISOU 1337  C   ARG A 267     3789   5271   4764    135    388     49       C  
ATOM   1338  O   ARG A 267      -0.994  -6.644  41.670  1.00 30.58           O  
ANISOU 1338  O   ARG A 267     3073   4564   3981     24    404      7       O  
ATOM   1339  CB  ARG A 267       2.028  -7.413  41.500  1.00 41.42           C  
ANISOU 1339  CB  ARG A 267     4585   5809   5345    206    311    130       C  
ATOM   1340  CG  ARG A 267       2.287  -7.666  40.015  1.00 38.28           C  
ANISOU 1340  CG  ARG A 267     4165   5428   4952    316    298    126       C  
ATOM   1341  CD  ARG A 267       2.656  -9.122  39.743  1.00 37.72           C  
ANISOU 1341  CD  ARG A 267     4222   5276   4833    369    233    108       C  
ATOM   1342  NE  ARG A 267       3.921  -9.513  40.370  1.00 35.54           N  
ANISOU 1342  NE  ARG A 267     3989   4965   4550    451    181    134       N  
ATOM   1343  CZ  ARG A 267       4.052 -10.521  41.231  1.00 37.66           C  
ANISOU 1343  CZ  ARG A 267     4406   5115   4788    425    103    149       C  
ATOM   1344  NH1 ARG A 267       2.988 -11.228  41.584  1.00 41.62           N1+
ANISOU 1344  NH1 ARG A 267     5033   5528   5253    283     78    148       N1+
ATOM   1345  NH2 ARG A 267       5.239 -10.820  41.751  1.00 37.64           N  
ANISOU 1345  NH2 ARG A 267     4427   5091   4785    527     36    174       N  
ATOM   1346  N   ASN A 268      -0.109  -5.418  39.978  1.00 34.86           N  
ANISOU 1346  N   ASN A 268     3527   5101   4619    219    380     62       N  
ATOM   1347  CA  ASN A 268      -1.289  -5.413  39.120  1.00 31.25           C  
ANISOU 1347  CA  ASN A 268     3013   4694   4167    218    376     27       C  
ATOM   1348  C   ASN A 268      -0.864  -5.364  37.674  1.00 33.56           C  
ANISOU 1348  C   ASN A 268     3299   4999   4453    301    344     76       C  
ATOM   1349  O   ASN A 268       0.265  -4.964  37.369  1.00 37.33           O  
ANISOU 1349  O   ASN A 268     3779   5470   4934    356    338    136       O  
ATOM   1350  CB  ASN A 268      -2.202  -4.237  39.431  1.00 34.06           C  
ANISOU 1350  CB  ASN A 268     3258   5093   4591    233    389    -27       C  
ATOM   1351  CG  ASN A 268      -3.209  -4.565  40.507  1.00 36.61           C  
ANISOU 1351  CG  ASN A 268     3543   5491   4878    130    435   -119       C  
ATOM   1352  ND2 ASN A 268      -3.061  -3.952  41.682  1.00 34.28           N  
ANISOU 1352  ND2 ASN A 268     3230   5202   4595    111    470   -166       N  
ATOM   1353  OD1 ASN A 268      -4.139  -5.336  40.269  1.00 39.40           O  
ANISOU 1353  OD1 ASN A 268     3874   5916   5178     51    439   -153       O  
ATOM   1354  N   SER A 269      -1.754  -5.751  36.771  1.00 33.12           N  
ANISOU 1354  N   SER A 269     3223   4990   4371    293    323     51       N  
ATOM   1355  CA  SER A 269      -1.403  -5.746  35.352  1.00 30.79           C  
ANISOU 1355  CA  SER A 269     2925   4736   4040    357    293     92       C  
ATOM   1356  C   SER A 269      -2.581  -5.439  34.444  1.00 34.42           C  
ANISOU 1356  C   SER A 269     3314   5265   4498    355    254     82       C  
ATOM   1357  O   SER A 269      -3.737  -5.585  34.852  1.00 33.87           O  
ANISOU 1357  O   SER A 269     3196   5228   4446    301    253     20       O  
ATOM   1358  CB  SER A 269      -0.793  -7.094  34.976  1.00 32.18           C  
ANISOU 1358  CB  SER A 269     3202   4891   4135    368    287     62       C  
ATOM   1359  OG  SER A 269      -1.678  -8.149  35.308  1.00 37.74           O  
ANISOU 1359  OG  SER A 269     3974   5556   4809    278    271     -2       O  
ATOM   1360  N   PHE A 270      -2.272  -4.998  33.220  1.00 36.53           N  
ANISOU 1360  N   PHE A 270     3564   5582   4732    405    220    145       N  
ATOM   1361  CA  PHE A 270      -3.280  -4.758  32.173  1.00 34.10           C  
ANISOU 1361  CA  PHE A 270     3200   5353   4404    411    159    153       C  
ATOM   1362  C   PHE A 270      -2.693  -4.993  30.776  1.00 37.36           C  
ANISOU 1362  C   PHE A 270     3643   5846   4704    426    138    201       C  
ATOM   1363  O   PHE A 270      -1.501  -4.777  30.546  1.00 40.30           O  
ANISOU 1363  O   PHE A 270     4040   6235   5038    448    166    257       O  
ATOM   1364  CB  PHE A 270      -3.842  -3.336  32.261  1.00 31.12           C  
ANISOU 1364  CB  PHE A 270     2744   4956   4125    463    102    203       C  
ATOM   1365  CG  PHE A 270      -2.793  -2.260  32.143  1.00 31.25           C  
ANISOU 1365  CG  PHE A 270     2792   4910   4170    493     84    316       C  
ATOM   1366  CD1 PHE A 270      -2.070  -1.849  33.262  1.00 29.79           C  
ANISOU 1366  CD1 PHE A 270     2631   4637   4050    488    127    313       C  
ATOM   1367  CD2 PHE A 270      -2.524  -1.657  30.909  1.00 29.70           C  
ANISOU 1367  CD2 PHE A 270     2608   4756   3918    496     16    435       C  
ATOM   1368  CE1 PHE A 270      -1.093  -0.856  33.164  1.00 27.95           C  
ANISOU 1368  CE1 PHE A 270     2431   4350   3836    479    102    420       C  
ATOM   1369  CE2 PHE A 270      -1.559  -0.665  30.800  1.00 29.45           C  
ANISOU 1369  CE2 PHE A 270     2617   4677   3898    475     -8    558       C  
ATOM   1370  CZ  PHE A 270      -0.848  -0.258  31.931  1.00 31.81           C  
ANISOU 1370  CZ  PHE A 270     2936   4878   4271    462     34    548       C  
ATOM   1371  N   GLU A 271      -3.538  -5.431  29.847  1.00 34.14           N  
ANISOU 1371  N   GLU A 271     3221   5520   4229    404     90    171       N  
ATOM   1372  CA  GLU A 271      -3.126  -5.619  28.465  1.00 30.51           C  
ANISOU 1372  CA  GLU A 271     2784   5170   3638    409     67    203       C  
ATOM   1373  C   GLU A 271      -3.015  -4.283  27.753  1.00 26.55           C  
ANISOU 1373  C   GLU A 271     2239   4717   3132    424      6    350       C  
ATOM   1374  O   GLU A 271      -3.681  -3.328  28.120  1.00 31.79           O  
ANISOU 1374  O   GLU A 271     2857   5318   3904    449    -55    402       O  
ATOM   1375  CB  GLU A 271      -4.095  -6.547  27.737  1.00 26.73           C  
ANISOU 1375  CB  GLU A 271     2317   4762   3077    362     23    116       C  
ATOM   1376  CG  GLU A 271      -3.733  -6.753  26.270  1.00 37.01           C  
ANISOU 1376  CG  GLU A 271     3642   6202   4217    362     -1    128       C  
ATOM   1377  CD  GLU A 271      -4.531  -7.837  25.627  1.00 37.50           C  
ANISOU 1377  CD  GLU A 271     3743   6318   4188    306    -42     13       C  
ATOM   1378  OE1 GLU A 271      -4.937  -8.749  26.365  1.00 33.93           O  
ANISOU 1378  OE1 GLU A 271     3343   5768   3780    260    -30    -88       O  
ATOM   1379  OE2 GLU A 271      -4.804  -7.751  24.407  1.00 44.33           O1-
ANISOU 1379  OE2 GLU A 271     4593   7323   4928    285    -97     33       O1-
ATOM   1380  N   VAL A 272      -2.130  -4.204  26.766  1.00 33.02           N  
ANISOU 1380  N   VAL A 272     3079   5648   3820    408     18    413       N  
ATOM   1381  CA  VAL A 272      -1.942  -2.986  25.985  1.00 33.52           C  
ANISOU 1381  CA  VAL A 272     3131   5763   3844    377    -54    584       C  
ATOM   1382  C   VAL A 272      -1.992  -3.251  24.487  1.00 34.49           C  
ANISOU 1382  C   VAL A 272     3259   6075   3772    330    -90    616       C  
ATOM   1383  O   VAL A 272      -1.563  -4.308  24.007  1.00 29.77           O  
ANISOU 1383  O   VAL A 272     2673   5593   3044    329    -20    502       O  
ATOM   1384  CB  VAL A 272      -0.586  -2.299  26.305  1.00 42.82           C  
ANISOU 1384  CB  VAL A 272     4318   6932   5019    342     -2    682       C  
ATOM   1385  CG1 VAL A 272      -0.519  -0.918  25.680  1.00 44.01           C  
ANISOU 1385  CG1 VAL A 272     4490   7078   5152    275   -106    884       C  
ATOM   1386  CG2 VAL A 272      -0.375  -2.190  27.795  1.00 39.97           C  
ANISOU 1386  CG2 VAL A 272     3959   6408   4820    381     43    629       C  
ATOM   1387  N   ARG A 273      -2.573  -2.298  23.766  1.00 34.54           N  
ANISOU 1387  N   ARG A 273     3263   6102   3758    301   -214    762       N  
ATOM   1388  CA  ARG A 273      -2.417  -2.194  22.317  1.00 34.24           C  
ANISOU 1388  CA  ARG A 273     3240   6259   3509    223   -262    855       C  
ATOM   1389  C   ARG A 273      -2.052  -0.752  21.949  1.00 33.61           C  
ANISOU 1389  C   ARG A 273     3201   6152   3418    149   -361   1097       C  
ATOM   1390  O   ARG A 273      -2.810   0.182  22.222  1.00 36.77           O  
ANISOU 1390  O   ARG A 273     3622   6388   3959    193   -498   1195       O  
ATOM   1391  CB  ARG A 273      -3.691  -2.637  21.586  1.00 35.39           C  
ANISOU 1391  CB  ARG A 273     3368   6476   3602    233   -360    805       C  
ATOM   1392  CG  ARG A 273      -3.720  -2.348  20.087  1.00 42.18           C  
ANISOU 1392  CG  ARG A 273     4249   7535   4240    145   -447    928       C  
ATOM   1393  CD  ARG A 273      -5.050  -2.815  19.492  1.00 48.51           C  
ANISOU 1393  CD  ARG A 273     5022   8405   5006    158   -556    864       C  
ATOM   1394  NE  ARG A 273      -5.311  -2.279  18.157  1.00 57.66           N  
ANISOU 1394  NE  ARG A 273     6203   9725   5978     81   -691   1022       N  
ATOM   1395  CZ  ARG A 273      -4.825  -2.782  17.023  1.00 62.25           C  
ANISOU 1395  CZ  ARG A 273     6811  10546   6294    -18   -652   1007       C  
ATOM   1396  NH1 ARG A 273      -4.044  -3.853  17.052  1.00 62.06           N1+
ANISOU 1396  NH1 ARG A 273     6790  10616   6175    -20   -485    816       N1+
ATOM   1397  NH2 ARG A 273      -5.130  -2.218  15.855  1.00 63.35           N  
ANISOU 1397  NH2 ARG A 273     6977  10837   6257   -105   -791   1174       N  
ATOM   1398  N   VAL A 274      -0.892  -0.580  21.326  1.00 35.22           N  
ANISOU 1398  N   VAL A 274     3416   6521   3446     34   -299   1188       N  
ATOM   1399  CA  VAL A 274      -0.459   0.720  20.826  1.00 38.64           C  
ANISOU 1399  CA  VAL A 274     3911   6953   3818    -98   -400   1443       C  
ATOM   1400  C   VAL A 274      -0.818   0.813  19.351  1.00 41.54           C  
ANISOU 1400  C   VAL A 274     4304   7521   3956   -196   -496   1561       C  
ATOM   1401  O   VAL A 274      -0.372   0.004  18.553  1.00 42.42           O  
ANISOU 1401  O   VAL A 274     4371   7900   3845   -251   -396   1476       O  
ATOM   1402  CB  VAL A 274       1.054   0.934  20.964  1.00 40.27           C  
ANISOU 1402  CB  VAL A 274     4095   7276   3930   -222   -279   1499       C  
ATOM   1403  CG1 VAL A 274       1.404   2.385  20.631  1.00 38.24           C  
ANISOU 1403  CG1 VAL A 274     3931   6956   3641   -394   -410   1786       C  
ATOM   1404  CG2 VAL A 274       1.528   0.559  22.356  1.00 34.36           C  
ANISOU 1404  CG2 VAL A 274     3303   6389   3364   -123   -165   1350       C  
ATOM   1405  N   CYS A 275      -1.628   1.793  18.988  1.00 39.62           N  
ANISOU 1405  N   CYS A 275     4139   7153   3764   -207   -701   1746       N  
ATOM   1406  CA  CYS A 275      -2.203   1.830  17.655  1.00 41.67           C  
ANISOU 1406  CA  CYS A 275     4427   7585   3822   -278   -825   1853       C  
ATOM   1407  C   CYS A 275      -2.616   3.230  17.269  1.00 44.62           C  
ANISOU 1407  C   CYS A 275     4923   7799   4230   -334  -1071   2140       C  
ATOM   1408  O   CYS A 275      -2.590   4.150  18.090  1.00 45.78           O  
ANISOU 1408  O   CYS A 275     5138   7669   4590   -287  -1154   2225       O  
ATOM   1409  CB  CYS A 275      -3.417   0.897  17.574  1.00 44.24           C  
ANISOU 1409  CB  CYS A 275     4682   7935   4190   -138   -849   1659       C  
ATOM   1410  SG  CYS A 275      -4.679   1.212  18.865  1.00 42.57           S  
ANISOU 1410  SG  CYS A 275     4429   7405   4339     80   -950   1566       S  
ATOM   1411  N   ALA A 276      -2.931   3.406  15.993  1.00 47.39           N  
ANISOU 1411  N   ALA A 276     5323   8325   4360   -443  -1200   2293       N  
ATOM   1412  CA  ALA A 276      -3.535   4.641  15.546  1.00 48.45           C  
ANISOU 1412  CA  ALA A 276     5592   8287   4531   -464  -1483   2567       C  
ATOM   1413  C   ALA A 276      -5.032   4.515  15.798  1.00 57.66           C  
ANISOU 1413  C   ALA A 276     6699   9314   5896   -222  -1632   2454       C  
ATOM   1414  O   ALA A 276      -5.643   3.469  15.519  1.00 59.65           O  
ANISOU 1414  O   ALA A 276     6835   9748   6082   -160  -1565   2263       O  
ATOM   1415  CB  ALA A 276      -3.243   4.893  14.096  1.00 51.31           C  
ANISOU 1415  CB  ALA A 276     6034   8908   4555   -698  -1573   2797       C  
ATOM   1416  N   CYS A 277      -5.615   5.562  16.359  1.00 56.18           N  
ANISOU 1416  N   CYS A 277     6583   8810   5953    -84  -1834   2552       N  
ATOM   1417  CA  CYS A 277      -7.046   5.571  16.671  1.00 57.91           C  
ANISOU 1417  CA  CYS A 277     6713   8916   6375    168  -1984   2436       C  
ATOM   1418  C   CYS A 277      -7.607   4.555  17.689  1.00 54.46           C  
ANISOU 1418  C   CYS A 277     6086   8517   6087    320  -1786   2101       C  
ATOM   1419  O   CYS A 277      -8.492   3.761  17.368  1.00 56.08           O  
ANISOU 1419  O   CYS A 277     6171   8923   6213    345  -1751   1956       O  
ATOM   1420  CB  CYS A 277      -7.841   5.448  15.368  1.00 57.02           C  
ANISOU 1420  CB  CYS A 277     6595   9001   6069    138  -2167   2543       C  
ATOM   1421  SG  CYS A 277      -9.486   6.049  15.530  1.00 82.39           S  
ANISOU 1421  SG  CYS A 277     9739  12045   9521    432  -2467   2528       S  
ATOM   1422  N   PRO A 278      -7.075   4.570  18.917  1.00 50.51           N  
ANISOU 1422  N   PRO A 278     3090   8954   7149     94   -783     56       N  
ATOM   1423  CA  PRO A 278      -7.555   3.737  20.025  1.00 49.51           C  
ANISOU 1423  CA  PRO A 278     3208   8780   6823     91  -1038   -141       C  
ATOM   1424  C   PRO A 278      -9.078   3.681  20.189  1.00 48.54           C  
ANISOU 1424  C   PRO A 278     3414   8640   6387    -28   -997   -303       C  
ATOM   1425  O   PRO A 278      -9.647   2.627  20.503  1.00 37.81           O  
ANISOU 1425  O   PRO A 278     2255   7332   4779     30  -1069   -498       O  
ATOM   1426  CB  PRO A 278      -6.896   4.362  21.265  1.00 52.53           C  
ANISOU 1426  CB  PRO A 278     3552   8946   7460    -96  -1381   -108       C  
ATOM   1427  CG  PRO A 278      -5.725   5.130  20.723  1.00 56.05           C  
ANISOU 1427  CG  PRO A 278     3602   9406   8287   -125  -1320     64       C  
ATOM   1428  CD  PRO A 278      -6.217   5.680  19.426  1.00 54.14           C  
ANISOU 1428  CD  PRO A 278     3319   9249   8004    -91   -932    157       C  
ATOM   1429  N   GLY A 279      -9.732   4.822  20.008  1.00 47.14           N  
ANISOU 1429  N   GLY A 279     3266   8405   6239   -183   -878   -208       N  
ATOM   1430  CA  GLY A 279     -11.175   4.878  20.140  1.00 43.95           C  
ANISOU 1430  CA  GLY A 279     3099   8037   5560   -268   -804   -270       C  
ATOM   1431  C   GLY A 279     -11.855   3.868  19.229  1.00 41.55           C  
ANISOU 1431  C   GLY A 279     2849   7984   4953   -194   -662   -369       C  
ATOM   1432  O   GLY A 279     -12.684   3.067  19.678  1.00 40.16           O  
ANISOU 1432  O   GLY A 279     2880   7816   4564   -272   -747   -524       O  
ATOM   1433  N   ARG A 280     -11.477   3.872  17.954  1.00 39.79           N  
ANISOU 1433  N   ARG A 280     2445   7977   4694    -66   -465   -295       N  
ATOM   1434  CA  ARG A 280     -12.087   2.949  17.006  1.00 45.16           C  
ANISOU 1434  CA  ARG A 280     3141   8995   5023    -27   -377   -448       C  
ATOM   1435  C   ARG A 280     -11.751   1.493  17.347  1.00 45.06           C  
ANISOU 1435  C   ARG A 280     3318   8888   4913     43   -502   -722       C  
ATOM   1436  O   ARG A 280     -12.636   0.626  17.362  1.00 43.23           O  
ANISOU 1436  O   ARG A 280     3405   8595   4424   -104   -536   -922       O  
ATOM   1437  CB  ARG A 280     -11.622   3.266  15.587  1.00 51.46           C  
ANISOU 1437  CB  ARG A 280     3758  10043   5753    160   -138   -311       C  
ATOM   1438  CG  ARG A 280     -12.206   2.383  14.493  1.00 59.91           C  
ANISOU 1438  CG  ARG A 280     4796  11586   6382    208    -61   -515       C  
ATOM   1439  CD  ARG A 280     -11.380   2.542  13.211  1.00 67.30           C  
ANISOU 1439  CD  ARG A 280     5592  12727   7251    514    193   -382       C  
ATOM   1440  NE  ARG A 280     -10.021   2.070  13.471  1.00 74.57           N  
ANISOU 1440  NE  ARG A 280     6403  13502   8430    774    244   -373       N  
ATOM   1441  CZ  ARG A 280      -8.933   2.474  12.823  1.00 82.89           C  
ANISOU 1441  CZ  ARG A 280     7334  14490   9669   1011    438   -110       C  
ATOM   1442  NH1 ARG A 280      -9.026   3.367  11.844  1.00 87.45           N1+
ANISOU 1442  NH1 ARG A 280     7898  15123  10207   1028    599    125       N1+
ATOM   1443  NH2 ARG A 280      -7.747   1.981  13.161  1.00 84.89           N  
ANISOU 1443  NH2 ARG A 280     7464  14627  10161   1242    468    -53       N  
ATOM   1444  N   ASP A 281     -10.484   1.232  17.647  1.00 39.10           N  
ANISOU 1444  N   ASP A 281     2474   7999   4384    262   -536   -683       N  
ATOM   1445  CA  ASP A 281     -10.060  -0.128  17.931  1.00 40.79           C  
ANISOU 1445  CA  ASP A 281     3005   7979   4515    438   -555   -860       C  
ATOM   1446  C   ASP A 281     -10.697  -0.672  19.221  1.00 39.52           C  
ANISOU 1446  C   ASP A 281     3207   7490   4318    272   -754   -986       C  
ATOM   1447  O   ASP A 281     -10.979  -1.869  19.329  1.00 40.74           O  
ANISOU 1447  O   ASP A 281     3764   7415   4301    298   -713  -1174       O  
ATOM   1448  CB  ASP A 281      -8.529  -0.193  17.995  1.00 44.09           C  
ANISOU 1448  CB  ASP A 281     3142   8416   5195    772   -530   -684       C  
ATOM   1449  CG  ASP A 281      -7.876  -0.009  16.623  1.00 50.65           C  
ANISOU 1449  CG  ASP A 281     3692   9545   6007   1033   -234   -547       C  
ATOM   1450  OD1 ASP A 281      -8.573   0.381  15.652  1.00 45.86           O  
ANISOU 1450  OD1 ASP A 281     3079   9158   5189    940    -82   -577       O  
ATOM   1451  OD2 ASP A 281      -6.658  -0.252  16.512  1.00 56.25           O1-
ANISOU 1451  OD2 ASP A 281     4165  10314   6896   1368   -136   -366       O1-
ATOM   1452  N   ARG A 282     -10.946   0.196  20.194  1.00 37.62           N  
ANISOU 1452  N   ARG A 282     2881   7191   4221    112   -935   -880       N  
ATOM   1453  CA  ARG A 282     -11.616  -0.267  21.389  1.00 41.51           C  
ANISOU 1453  CA  ARG A 282     3731   7405   4635      2  -1075   -959       C  
ATOM   1454  C   ARG A 282     -13.072  -0.664  21.102  1.00 40.74           C  
ANISOU 1454  C   ARG A 282     3864   7322   4293   -250   -973  -1060       C  
ATOM   1455  O   ARG A 282     -13.505  -1.760  21.465  1.00 42.13           O  
ANISOU 1455  O   ARG A 282     4395   7261   4352   -304   -961  -1190       O  
ATOM   1456  CB  ARG A 282     -11.581   0.781  22.485  1.00 39.88           C  
ANISOU 1456  CB  ARG A 282     3462   7123   4566    -83  -1270   -842       C  
ATOM   1457  CG  ARG A 282     -12.321   0.297  23.706  1.00 40.26           C  
ANISOU 1457  CG  ARG A 282     3912   6907   4477   -132  -1364   -892       C  
ATOM   1458  CD  ARG A 282     -12.357   1.313  24.812  1.00 43.18           C  
ANISOU 1458  CD  ARG A 282     4344   7173   4888   -184  -1539   -816       C  
ATOM   1459  NE  ARG A 282     -13.357   0.919  25.796  1.00 45.33           N  
ANISOU 1459  NE  ARG A 282     5010   7244   4968   -206  -1521   -817       N  
ATOM   1460  CZ  ARG A 282     -13.937   1.748  26.654  1.00 44.29           C  
ANISOU 1460  CZ  ARG A 282     5062   7013   4752   -244  -1545   -746       C  
ATOM   1461  NH1 ARG A 282     -13.657   3.044  26.636  1.00 40.59           N1+
ANISOU 1461  NH1 ARG A 282     4471   6575   4378   -308  -1594   -706       N1+
ATOM   1462  NH2 ARG A 282     -14.833   1.279  27.503  1.00 48.22           N  
ANISOU 1462  NH2 ARG A 282     5901   7352   5068   -209  -1471   -697       N  
ATOM   1463  N   ARG A 283     -13.833   0.217  20.463  1.00 34.80           N  
ANISOU 1463  N   ARG A 283     2888   6861   3474   -411   -892   -962       N  
ATOM   1464  CA  ARG A 283     -15.231  -0.103  20.136  1.00 41.39           C  
ANISOU 1464  CA  ARG A 283     3816   7834   4075   -676   -831   -997       C  
ATOM   1465  C   ARG A 283     -15.356  -1.383  19.303  1.00 45.59           C  
ANISOU 1465  C   ARG A 283     4574   8347   4401   -772   -784  -1251       C  
ATOM   1466  O   ARG A 283     -16.256  -2.197  19.520  1.00 47.04           O  
ANISOU 1466  O   ARG A 283     5006   8413   4456  -1037   -806  -1358       O  
ATOM   1467  CB  ARG A 283     -15.905   1.056  19.392  1.00 34.11           C  
ANISOU 1467  CB  ARG A 283     2575   7288   3097   -734   -710   -781       C  
ATOM   1468  CG  ARG A 283     -17.432   1.111  19.552  1.00 34.16           C  
ANISOU 1468  CG  ARG A 283     2626   7385   2968   -940   -635   -636       C  
ATOM   1469  CD  ARG A 283     -18.030   2.240  18.738  1.00 36.11           C  
ANISOU 1469  CD  ARG A 283     2630   7954   3137   -875   -445   -366       C  
ATOM   1470  NE  ARG A 283     -17.581   3.547  19.221  1.00 41.48           N  
ANISOU 1470  NE  ARG A 283     3235   8530   3996   -682   -376   -169       N  
ATOM   1471  CZ  ARG A 283     -17.939   4.716  18.689  1.00 43.71           C  
ANISOU 1471  CZ  ARG A 283     3391   8979   4236   -562   -203     96       C  
ATOM   1472  NH1 ARG A 283     -18.768   4.745  17.653  1.00 34.20           N1+
ANISOU 1472  NH1 ARG A 283     2112   8109   2774   -577   -119    218       N1+
ATOM   1473  NH2 ARG A 283     -17.464   5.857  19.189  1.00 32.18           N  
ANISOU 1473  NH2 ARG A 283     1898   7350   2978   -437   -142    236       N  
ATOM   1474  N   THR A 284     -14.446  -1.546  18.345  1.00 49.23           N  
ANISOU 1474  N   THR A 284     4974   8901   4829   -563   -697  -1339       N  
ATOM   1475  CA  THR A 284     -14.433  -2.703  17.456  1.00 49.71           C  
ANISOU 1475  CA  THR A 284     5347   8900   4640   -595   -613  -1619       C  
ATOM   1476  C   THR A 284     -14.102  -4.000  18.182  1.00 47.67           C  
ANISOU 1476  C   THR A 284     5575   8117   4420   -529   -598  -1795       C  
ATOM   1477  O   THR A 284     -14.713  -5.034  17.928  1.00 47.59           O  
ANISOU 1477  O   THR A 284     5966   7904   4214   -774   -569  -2041       O  
ATOM   1478  CB  THR A 284     -13.422  -2.491  16.318  1.00 54.90           C  
ANISOU 1478  CB  THR A 284     5847   9772   5240   -264   -453  -1613       C  
ATOM   1479  CG2 THR A 284     -13.283  -3.741  15.470  1.00 56.78           C  
ANISOU 1479  CG2 THR A 284     6545   9855   5174   -214   -326  -1937       C  
ATOM   1480  OG1 THR A 284     -13.883  -1.423  15.481  1.00 57.10           O  
ANISOU 1480  OG1 THR A 284     5739  10542   5413   -334   -422  -1451       O  
ATOM   1481  N   GLU A 285     -13.135  -3.953  19.088  1.00 49.03           N  
ANISOU 1481  N   GLU A 285     5722   8069   4838   -212   -620  -1659       N  
ATOM   1482  CA  GLU A 285     -12.755  -5.161  19.808  1.00 51.29           C  
ANISOU 1482  CA  GLU A 285     6457   7879   5151    -50   -567  -1752       C  
ATOM   1483  C   GLU A 285     -13.836  -5.533  20.835  1.00 50.33           C  
ANISOU 1483  C   GLU A 285     6590   7505   5029   -365   -650  -1753       C  
ATOM   1484  O   GLU A 285     -14.078  -6.716  21.095  1.00 47.08           O  
ANISOU 1484  O   GLU A 285     6654   6681   4552   -427   -548  -1893       O  
ATOM   1485  CB  GLU A 285     -11.386  -5.000  20.479  1.00 49.47           C  
ANISOU 1485  CB  GLU A 285     6053   7594   5150    410   -599  -1550       C  
ATOM   1486  CG  GLU A 285     -10.876  -6.325  21.051  1.00 54.75           C  
ANISOU 1486  CG  GLU A 285     7185   7812   5804    708   -476  -1593       C  
ATOM   1487  CD  GLU A 285      -9.441  -6.285  21.543  1.00 55.58           C  
ANISOU 1487  CD  GLU A 285     7053   7973   6093   1222   -502  -1348       C  
ATOM   1488  OE1 GLU A 285      -8.691  -5.355  21.159  1.00 53.50           O  
ANISOU 1488  OE1 GLU A 285     6265   8086   5977   1335   -575  -1185       O  
ATOM   1489  OE2 GLU A 285      -9.064  -7.206  22.312  1.00 58.05           O1-
ANISOU 1489  OE2 GLU A 285     7685   7965   6407   1512   -440  -1285       O1-
ATOM   1490  N   GLU A 286     -14.500  -4.518  21.386  1.00 45.42           N  
ANISOU 1490  N   GLU A 286     5676   7106   4476   -545   -784  -1571       N  
ATOM   1491  CA  GLU A 286     -15.575  -4.726  22.352  1.00 45.71           C  
ANISOU 1491  CA  GLU A 286     5887   6976   4505   -797   -815  -1492       C  
ATOM   1492  C   GLU A 286     -16.859  -5.206  21.692  1.00 54.06           C  
ANISOU 1492  C   GLU A 286     7017   8123   5400  -1276   -768  -1607       C  
ATOM   1493  O   GLU A 286     -17.746  -5.716  22.376  1.00 53.89           O  
ANISOU 1493  O   GLU A 286     7180   7907   5387  -1526   -741  -1546       O  
ATOM   1494  CB  GLU A 286     -15.864  -3.465  23.160  1.00 38.10           C  
ANISOU 1494  CB  GLU A 286     4646   6203   3627   -767   -919  -1244       C  
ATOM   1495  CG  GLU A 286     -14.919  -3.266  24.341  1.00 37.60           C  
ANISOU 1495  CG  GLU A 286     4669   5934   3683   -428  -1036  -1144       C  
ATOM   1496  CD  GLU A 286     -15.135  -1.939  25.018  1.00 35.50           C  
ANISOU 1496  CD  GLU A 286     4220   5815   3453   -417  -1139   -970       C  
ATOM   1497  OE1 GLU A 286     -16.038  -1.191  24.576  1.00 43.36           O  
ANISOU 1497  OE1 GLU A 286     5021   7055   4401   -612  -1058   -879       O  
ATOM   1498  OE2 GLU A 286     -14.416  -1.639  25.991  1.00 35.63           O1-
ANISOU 1498  OE2 GLU A 286     4314   5706   3518   -204  -1298   -918       O1-
ATOM   1499  N   GLU A 287     -16.987  -4.986  20.384  1.00 61.43           N  
ANISOU 1499  N   GLU A 287     7766   9400   6175  -1418   -772  -1737       N  
ATOM   1500  CA  GLU A 287     -18.182  -5.410  19.652  1.00 67.22           C  
ANISOU 1500  CA  GLU A 287     8514  10322   6702  -1926   -807  -1863       C  
ATOM   1501  C   GLU A 287     -18.324  -6.938  19.593  1.00 71.62           C  
ANISOU 1501  C   GLU A 287     9646  10381   7185  -2179   -743  -2165       C  
ATOM   1502  O   GLU A 287     -19.434  -7.452  19.540  1.00 74.44           O  
ANISOU 1502  O   GLU A 287    10075  10738   7472  -2702   -797  -2219       O  
ATOM   1503  CB  GLU A 287     -18.164  -4.810  18.247  1.00 71.36           C  
ANISOU 1503  CB  GLU A 287     8742  11356   7017  -1941   -838  -1925       C  
ATOM   1504  CG  GLU A 287     -19.390  -5.101  17.411  1.00 81.89           C  
ANISOU 1504  CG  GLU A 287    10014  12875   8224  -2321   -877  -1899       C  
ATOM   1505  CD  GLU A 287     -19.142  -4.884  15.926  1.00 91.39           C  
ANISOU 1505  CD  GLU A 287    11131  14398   9197  -2224   -867  -2003       C  
ATOM   1506  OE1 GLU A 287     -18.045  -4.386  15.568  1.00 91.46           O  
ANISOU 1506  OE1 GLU A 287    11063  14525   9164  -1848   -790  -2042       O  
ATOM   1507  OE2 GLU A 287     -20.043  -5.204  15.117  1.00 97.64           O1-
ANISOU 1507  OE2 GLU A 287    11909  15366   9824  -2527   -941  -2042       O1-
ATOM   1508  N   ASN A 288     -17.211  -7.636  19.614  1.00 74.64           N  
ANISOU 1508  N   ASN A 288    10432  10329   7598  -1810   -607  -2328       N  
ATOM   1509  CA  ASN A 288     -17.203  -9.084  19.603  1.00 79.66           C  
ANISOU 1509  CA  ASN A 288    11728  10347   8194  -1949   -463  -2582       C  
ATOM   1510  C   ASN A 288     -17.726  -9.727  20.862  1.00 76.72           C  
ANISOU 1510  C   ASN A 288    11502   9635   8015  -2150   -433  -2389       C  
ATOM   1511  O   ASN A 288     -17.608 -10.922  21.032  1.00 78.81           O  
ANISOU 1511  O   ASN A 288    12221   9452   8269  -2517   -337  -2545       O  
ATOM   1512  CB  ASN A 288     -15.780  -9.592  19.453  1.00 84.22           C  
ANISOU 1512  CB  ASN A 288    12666  10547   8788  -1349   -256  -2669       C  
ATOM   1513  CG  ASN A 288     -15.265  -9.473  18.046  1.00 90.88           C  
ANISOU 1513  CG  ASN A 288    13564  11587   9378  -1189   -182  -2912       C  
ATOM   1514  ND2 ASN A 288     -16.163  -9.456  17.082  1.00 96.23           N  
ANISOU 1514  ND2 ASN A 288    14610  12188   9766  -1639   -188  -3275       N  
ATOM   1515  OD1 ASN A 288     -14.068  -9.412  17.830  1.00 91.36           O  
ANISOU 1515  OD1 ASN A 288    13340  11879   9492   -679   -124  -2766       O  
ATOM   1516  N   LEU A 289     -18.268  -8.939  21.767  1.00 73.06           N  
ANISOU 1516  N   LEU A 289    10697   9345   7717  -1856   -489  -2050       N  
ATOM   1517  CA  LEU A 289     -18.713  -9.483  23.035  1.00 70.28           C  
ANISOU 1517  CA  LEU A 289    10374   8810   7518  -1850   -456  -1757       C  
ATOM   1518  C   LEU A 289     -20.218  -9.716  22.980  1.00 64.83           C  
ANISOU 1518  C   LEU A 289     9811   7898   6925  -1218   -426  -1620       C  
ATOM   1519  O   LEU A 289     -20.941  -8.795  22.480  1.00 66.50           O  
ANISOU 1519  O   LEU A 289    10345   7787   7134   -888   -314  -1738       O  
ATOM   1520  CB  LEU A 289     -18.314  -8.579  24.192  1.00 57.89           C  
ANISOU 1520  CB  LEU A 289     9202   6800   5992  -2301   -317  -1785       C  
ATOM   1521  CG  LEU A 289     -16.849  -8.372  24.552  1.00 58.69           C  
ANISOU 1521  CG  LEU A 289     9118   7137   6045  -3047   -391  -1820       C  
ATOM   1522  CD1 LEU A 289     -16.643  -7.345  25.621  1.00 56.41           C  
ANISOU 1522  CD1 LEU A 289     8242   7587   5605  -3191   -600  -1814       C  
ATOM   1523  CD2 LEU A 289     -16.240  -9.674  24.969  1.00 64.93           C  
ANISOU 1523  CD2 LEU A 289    10446   7436   6788  -3548   -307  -2165       C  
TER    1524      LEU A 289 
HETATM 1525 ZN    ZN A 401       8.710   0.208  16.282  1.00 40.65          ZN  
CONECT  630 1525
CONECT  655 1525
CONECT 1132 1525
CONECT 1158 1525
CONECT 1525  630  655 1132 1158
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.