CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.
elNémo will be down on october 27th, due to electrical maintenance.
Sorry for the inconvenience.


***    ***

elNémo ID: 20100716312152524

Job options:

ID        	=	 20100716312152524
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   LEU A 241      -4.606 -22.018  37.754  1.00 47.73      A    N  
ANISOU    1  N   LEU A 241     7329   6049   4757    -95   -537    -64  A    N  
ATOM      2  CA  LEU A 241      -4.342 -22.244  36.296  1.00 48.81      A    C  
ANISOU    2  CA  LEU A 241     7393   6215   4935    -71   -521    -79  A    C  
ATOM      3  C   LEU A 241      -5.604 -22.706  35.518  1.00 49.75      A    C  
ANISOU    3  C   LEU A 241     7502   6360   5040    -80   -474    -77  A    C  
ATOM      4  O   LEU A 241      -5.965 -22.037  34.533  1.00 45.74      A    O  
ANISOU    4  O   LEU A 241     6946   5890   4542    -72   -431    -82  A    O  
ATOM      5  CB  LEU A 241      -3.202 -23.213  36.042  1.00 49.08      A    C  
ANISOU    5  CB  LEU A 241     7411   6227   5008    -43   -577    -94  A    C  
ATOM      6  CG  LEU A 241      -1.772 -22.689  36.040  1.00 50.12      A    C  
ANISOU    6  CG  LEU A 241     7503   6357   5182    -21   -612   -103  A    C  
ATOM      7  CD1 LEU A 241      -0.831 -23.835  35.717  1.00 51.16      A    C  
ANISOU    7  CD1 LEU A 241     7615   6471   5351     12   -662   -121  A    C  
ATOM      8  CD2 LEU A 241      -1.573 -21.558  35.054  1.00 48.94      A    C  
ANISOU    8  CD2 LEU A 241     7284   6255   5054    -15   -567   -106  A    C  
ATOM      9  N   ASP A 242      -6.255 -23.819  35.915  1.00 48.55      A    N  
ANISOU    9  N   ASP A 242     7394   6185   4866    -99   -488    -67  A    N  
ATOM     10  CA  ASP A 242      -7.599 -24.171  35.318  1.00 50.42      A    C  
ANISOU   10  CA  ASP A 242     7623   6445   5088   -118   -446    -58  A    C  
ATOM     11  C   ASP A 242      -8.677 -23.322  36.003  1.00 51.09      A    C  
ANISOU   11  C   ASP A 242     7725   6553   5135   -145   -396    -40  A    C  
ATOM     12  O   ASP A 242      -9.405 -23.778  36.876  1.00 50.51      A    O  
ANISOU   12  O   ASP A 242     7696   6468   5025   -176   -391    -19  A    O  
ATOM     13  CB  ASP A 242      -7.943 -25.685  35.385  1.00 49.59      A    C  
ANISOU   13  CB  ASP A 242     7555   6308   4977   -135   -482    -50  A    C  
ATOM     14  CG  ASP A 242      -9.372 -26.021  34.836  1.00 50.77      A    C  
ANISOU   14  CG  ASP A 242     7695   6481   5114   -163   -444    -36  A    C  
ATOM     15  OD1 ASP A 242      -9.980 -25.157  34.157  1.00 47.54      A    O  
ANISOU   15  OD1 ASP A 242     7240   6113   4708   -159   -393    -39  A    O  
ATOM     16  OD2 ASP A 242      -9.904 -27.155  35.090  1.00 50.02      A    O1-
ANISOU   16  OD2 ASP A 242     7639   6359   5007   -192   -469    -20  A    O1-
ATOM     17  N   ASP A 243      -8.761 -22.069  35.609  1.00 49.75      A    N  
ANISOU   17  N   ASP A 243     7517   6414   4970   -132   -358    -47  A    N  
ATOM     18  CA  ASP A 243      -9.676 -21.168  36.267  1.00 49.67      A    C  
ANISOU   18  CA  ASP A 243     7523   6423   4925   -145   -314    -36  A    C  
ATOM     19  C   ASP A 243     -10.102 -20.213  35.169  1.00 48.25      A    C  
ANISOU   19  C   ASP A 243     7286   6282   4764   -128   -273    -45  A    C  
ATOM     20  O   ASP A 243      -9.306 -19.411  34.671  1.00 47.51      A    O  
ANISOU   20  O   ASP A 243     7166   6192   4693   -108   -281    -57  A    O  
ATOM     21  CB  ASP A 243      -8.964 -20.468  37.426  1.00 49.77      A    C  
ANISOU   21  CB  ASP A 243     7580   6411   4917   -141   -336    -36  A    C  
ATOM     22  CG  ASP A 243      -9.764 -19.335  38.030  1.00 52.82      A    C  
ANISOU   22  CG  ASP A 243     7983   6817   5267   -142   -291    -34  A    C  
ATOM     23  OD1 ASP A 243     -10.997 -19.219  37.778  1.00 52.70      A    O  
ANISOU   23  OD1 ASP A 243     7948   6836   5238   -149   -239    -27  A    O  
ATOM     24  OD2 ASP A 243      -9.132 -18.543  38.771  1.00 54.47      A    O1-
ANISOU   24  OD2 ASP A 243     8226   7007   5463   -133   -311    -39  A    O1-
ATOM     25  N   ILE A 244     -11.361 -20.306  34.785  1.00 45.65      A    N  
ANISOU   25  N   ILE A 244     6938   5981   4426   -140   -233    -37  A    N  
ATOM     26  CA  ILE A 244     -11.798 -19.577  33.631  1.00 46.59      A    C  
ANISOU   26  CA  ILE A 244     7005   6131   4565   -125   -204    -46  A    C  
ATOM     27  C   ILE A 244     -12.030 -18.099  33.924  1.00 45.45      A    C  
ANISOU   27  C   ILE A 244     6858   6001   4408   -110   -176    -50  A    C  
ATOM     28  O   ILE A 244     -12.087 -17.286  33.005  1.00 46.21      A    O  
ANISOU   28  O   ILE A 244     6919   6116   4523    -94   -163    -58  A    O  
ATOM     29  CB  ILE A 244     -13.006 -20.251  32.982  1.00 48.40      A    C  
ANISOU   29  CB  ILE A 244     7210   6382   4798   -141   -183    -37  A    C  
ATOM     30  CG1 ILE A 244     -13.354 -19.540  31.679  1.00 49.93      A    C  
ANISOU   30  CG1 ILE A 244     7357   6608   5006   -125   -151    -43  A    C  
ATOM     31  CG2 ILE A 244     -14.201 -20.267  33.928  1.00 49.65      A    C  
ANISOU   31  CG2 ILE A 244     7394   6544   4924   -171   -161    -15  A    C  
ATOM     32  CD1 ILE A 244     -14.312 -20.291  30.816  1.00 50.26      A    C  
ANISOU   32  CD1 ILE A 244     7366   6658   5070   -126   -159    -46  A    C  
ATOM     33  N   THR A 245     -12.103 -17.727  35.197  1.00 45.16      A    N  
ANISOU   33  N   THR A 245     6866   5953   4338   -114   -171    -46  A    N  
ATOM     34  CA  THR A 245     -12.268 -16.314  35.561  1.00 43.65      A    C  
ANISOU   34  CA  THR A 245     6684   5768   4131    -95   -152    -54  A    C  
ATOM     35  C   THR A 245     -11.052 -15.503  35.096  1.00 41.78      A    C  
ANISOU   35  C   THR A 245     6438   5514   3921    -80   -185    -64  A    C  
ATOM     36  O   THR A 245     -11.104 -14.285  34.978  1.00 41.93      A    O  
ANISOU   36  O   THR A 245     6455   5536   3940    -65   -178    -71  A    O  
ATOM     37  CB  THR A 245     -12.481 -16.176  37.075  1.00 44.16      A    C  
ANISOU   37  CB  THR A 245     6810   5819   4147    -99   -145    -50  A    C  
ATOM     38  CG2 THR A 245     -13.701 -16.995  37.523  1.00 43.49      A    C  
ANISOU   38  CG2 THR A 245     6728   5759   4035   -121   -105    -34  A    C  
ATOM     39  OG1 THR A 245     -11.319 -16.644  37.763  1.00 46.58      A    O  
ANISOU   39  OG1 THR A 245     7159   6086   4450   -109   -195    -48  A    O  
ATOM     40  N   ARG A 246      -9.968 -16.213  34.796  1.00 40.54      A    N  
ANISOU   40  N   ARG A 246     6273   5341   3790    -86   -223    -64  A    N  
ATOM     41  CA  ARG A 246      -8.688 -15.593  34.494  1.00 40.04      A    C  
ANISOU   41  CA  ARG A 246     6196   5263   3754    -78   -257    -69  A    C  
ATOM     42  C   ARG A 246      -8.555 -15.162  33.049  1.00 39.74      A    C  
ANISOU   42  C   ARG A 246     6100   5250   3746    -69   -243    -72  A    C  
ATOM     43  O   ARG A 246      -7.718 -14.330  32.741  1.00 39.13      A    O  
ANISOU   43  O   ARG A 246     6008   5169   3687    -67   -260    -71  A    O  
ATOM     44  CB  ARG A 246      -7.540 -16.533  34.852  1.00 39.34      A    C  
ANISOU   44  CB  ARG A 246     6117   5149   3681    -82   -304    -69  A    C  
ATOM     45  CG  ARG A 246      -7.322 -16.642  36.342  1.00 39.37      A    C  
ANISOU   45  CG  ARG A 246     6186   5117   3655    -91   -333    -65  A    C  
ATOM     46  CD  ARG A 246      -6.197 -17.587  36.744  1.00 38.27      A    C  
ANISOU   46  CD  ARG A 246     6059   4947   3533    -93   -389    -64  A    C  
ATOM     47  NE  ARG A 246      -4.934 -16.950  36.486  1.00 38.80      A    N  
ANISOU   47  NE  ARG A 246     6097   5006   3637    -86   -424    -68  A    N  
ATOM     48  CZ  ARG A 246      -3.748 -17.524  36.649  1.00 39.82      A    C  
ANISOU   48  CZ  ARG A 246     6217   5114   3797    -81   -476    -70  A    C  
ATOM     49  NH1 ARG A 246      -3.629 -18.790  37.118  1.00 40.16      A    N1+
ANISOU   49  NH1 ARG A 246     6289   5134   3835    -81   -505    -71  A    N1+
ATOM     50  NH2 ARG A 246      -2.668 -16.822  36.339  1.00 39.35      A    N  
ANISOU   50  NH2 ARG A 246     6120   5056   3775    -78   -501    -69  A    N  
ATOM     51  N   LEU A 247      -9.392 -15.733  32.181  1.00 39.25      A    N  
ANISOU   51  N   LEU A 247     6010   5213   3687    -68   -216    -72  A    N  
ATOM     52  CA  LEU A 247      -9.529 -15.296  30.808  1.00 37.03      A    C  
ANISOU   52  CA  LEU A 247     5686   4958   3425    -61   -198    -74  A    C  
ATOM     53  C   LEU A 247     -10.459 -14.120  30.713  1.00 34.83      A    C  
ANISOU   53  C   LEU A 247     5408   4690   3134    -55   -172    -73  A    C  
ATOM     54  O   LEU A 247     -11.544 -14.158  31.235  1.00 32.06      A    O  
ANISOU   54  O   LEU A 247     5071   4345   2763    -54   -150    -73  A    O  
ATOM     55  CB  LEU A 247     -10.100 -16.424  29.904  1.00 36.87      A    C  
ANISOU   55  CB  LEU A 247     5643   4954   3411    -61   -187    -77  A    C  
ATOM     56  CG  LEU A 247      -9.399 -17.769  29.958  1.00 36.55      A    C  
ANISOU   56  CG  LEU A 247     5608   4899   3380    -60   -215    -82  A    C  
ATOM     57  CD1 LEU A 247      -9.975 -18.697  28.920  1.00 36.40      A    C  
ANISOU   57  CD1 LEU A 247     5571   4892   3365    -58   -209    -88  A    C  
ATOM     58  CD2 LEU A 247      -7.913 -17.600  29.778  1.00 36.55      A    C  
ANISOU   58  CD2 LEU A 247     5590   4893   3401    -49   -239    -88  A    C  
ATOM     59  N   ASN A 248     -10.039 -13.124  29.932  1.00 35.53      A    N  
ANISOU   59  N   ASN A 248     5478   4785   3237    -50   -175    -71  A    N  
ATOM     60  CA  ASN A 248     -10.908 -11.986  29.497  1.00 34.28      A    C  
ANISOU   60  CA  ASN A 248     5316   4635   3072    -41   -157    -71  A    C  
ATOM     61  C   ASN A 248     -11.328 -12.150  28.105  1.00 35.18      A    C  
ANISOU   61  C   ASN A 248     5394   4774   3197    -39   -143    -69  A    C  
ATOM     62  O   ASN A 248     -10.628 -11.691  27.248  1.00 37.31      A    O  
ANISOU   62  O   ASN A 248     5648   5049   3479    -42   -150    -63  A    O  
ATOM     63  CB  ASN A 248     -10.121 -10.693  29.507  1.00 33.49      A    C  
ANISOU   63  CB  ASN A 248     5227   4519   2979    -43   -179    -65  A    C  
ATOM     64  CG  ASN A 248     -10.979  -9.503  29.337  1.00 33.03      A    C  
ANISOU   64  CG  ASN A 248     5181   4458   2911    -29   -171    -67  A    C  
ATOM     65  ND2 ASN A 248     -10.385  -8.441  28.851  1.00 33.16      A    N  
ANISOU   65  ND2 ASN A 248     5199   4463   2938    -36   -191    -58  A    N  
ATOM     66  OD1 ASN A 248     -12.160  -9.505  29.682  1.00 33.25      A    O  
ANISOU   66  OD1 ASN A 248     5215   4493   2924    -13   -148    -76  A    O  
ATOM     67  N   ILE A 249     -12.465 -12.805  27.876  1.00 37.09      A    N  
ANISOU   67  N   ILE A 249     5626   5031   3435    -36   -123    -72  A    N  
ATOM     68  CA  ILE A 249     -13.033 -13.059  26.566  1.00 36.16      A    C  
ANISOU   68  CA  ILE A 249     5480   4933   3325    -34   -115    -72  A    C  
ATOM     69  C   ILE A 249     -14.096 -12.008  26.235  1.00 36.37      A    C  
ANISOU   69  C   ILE A 249     5500   4967   3350    -21   -104    -71  A    C  
ATOM     70  O   ILE A 249     -15.115 -11.916  26.904  1.00 38.88      A    O  
ANISOU   70  O   ILE A 249     5820   5289   3661    -13    -90    -74  A    O  
ATOM     71  CB  ILE A 249     -13.677 -14.463  26.538  1.00 37.52      A    C  
ANISOU   71  CB  ILE A 249     5644   5112   3497    -42   -111    -73  A    C  
ATOM     72  CG1 ILE A 249     -12.590 -15.547  26.593  1.00 37.65      A    C  
ANISOU   72  CG1 ILE A 249     5667   5118   3518    -47   -130    -77  A    C  
ATOM     73  CG2 ILE A 249     -14.483 -14.656  25.260  1.00 38.28      A    C  
ANISOU   73  CG2 ILE A 249     5718   5226   3601    -39   -108    -74  A    C  
ATOM     74  CD1 ILE A 249     -13.111 -16.929  26.944  1.00 37.91      A    C  
ANISOU   74  CD1 ILE A 249     5708   5145   3548    -59   -136    -77  A    C  
ATOM     75  N   ILE A 250     -13.885 -11.221  25.197  1.00 35.81      A    N  
ANISOU   75  N   ILE A 250     5422   4898   3283    -18   -112    -67  A    N  
ATOM     76  CA  ILE A 250     -14.772 -10.096  24.917  1.00 35.12      A    C  
ANISOU   76  CA  ILE A 250     5336   4811   3197     -3   -111    -67  A    C  
ATOM     77  C   ILE A 250     -15.229 -10.070  23.446  1.00 36.13      A    C  
ANISOU   77  C   ILE A 250     5445   4950   3329     -2   -116    -62  A    C  
ATOM     78  O   ILE A 250     -14.549 -10.590  22.569  1.00 36.91      A    O  
ANISOU   78  O   ILE A 250     5538   5057   3426    -14   -120    -58  A    O  
ATOM     79  CB  ILE A 250     -14.093  -8.791  25.301  1.00 34.20      A    C  
ANISOU   79  CB  ILE A 250     5246   4671   3077      0   -128    -63  A    C  
ATOM     80  CG1 ILE A 250     -12.796  -8.642  24.565  1.00 33.81      A    C  
ANISOU   80  CG1 ILE A 250     5193   4619   3031    -21   -141    -50  A    C  
ATOM     81  CG2 ILE A 250     -13.794  -8.758  26.809  1.00 34.49      A    C  
ANISOU   81  CG2 ILE A 250     5310   4691   3104      2   -128    -70  A    C  
ATOM     82  CD1 ILE A 250     -12.128  -7.310  24.813  1.00 34.62      A    C  
ANISOU   82  CD1 ILE A 250     5321   4697   3134    -27   -164    -40  A    C  
ATOM     83  N   VAL A 251     -16.381  -9.460  23.197  1.00 37.56      A    N  
ANISOU   83  N   VAL A 251     5620   5134   3515     13   -118    -64  A    N  
ATOM     84  CA  VAL A 251     -16.924  -9.368  21.874  1.00 39.22      A    C  
ANISOU   84  CA  VAL A 251     5820   5352   3730     15   -130    -60  A    C  
ATOM     85  C   VAL A 251     -16.319  -8.191  21.153  1.00 39.14      A    C  
ANISOU   85  C   VAL A 251     5830   5328   3712     13   -148    -49  A    C  
ATOM     86  O   VAL A 251     -16.242  -7.085  21.697  1.00 37.29      A    O  
ANISOU   86  O   VAL A 251     5615   5073   3477     22   -157    -48  A    O  
ATOM     87  CB  VAL A 251     -18.432  -9.219  21.848  1.00 41.00      A    C  
ANISOU   87  CB  VAL A 251     6024   5586   3968     34   -130    -65  A    C  
ATOM     88  CG1 VAL A 251     -19.085 -10.228  22.776  1.00 41.93      A    C  
ANISOU   88  CG1 VAL A 251     6119   5719   4092     31   -109    -70  A    C  
ATOM     89  CG2 VAL A 251     -18.832  -7.847  22.278  1.00 43.58      A    C  
ANISOU   89  CG2 VAL A 251     6364   5898   4297     60   -137    -70  A    C  
ATOM     90  N   GLY A 252     -15.869  -8.465  19.938  1.00 38.45      A    N  
ANISOU   90  N   GLY A 252     5743   5249   3616      0   -153    -40  A    N  
ATOM     91  CA  GLY A 252     -15.471  -7.415  19.021  1.00 41.32      A    C  
ANISOU   91  CA  GLY A 252     6127   5603   3969     -8   -170    -24  A    C  
ATOM     92  C   GLY A 252     -16.183  -7.487  17.674  1.00 40.69      A    C  
ANISOU   92  C   GLY A 252     6049   5529   3881     -5   -184    -20  A    C  
ATOM     93  O   GLY A 252     -16.745  -8.507  17.291  1.00 43.65      A    O  
ANISOU   93  O   GLY A 252     6409   5918   4258     -1   -181    -30  A    O  
ATOM     94  N   TYR A 253     -16.157  -6.375  16.971  1.00 41.23      A    N  
ANISOU   94  N   TYR A 253     6141   5583   3940     -9   -206     -5  A    N  
ATOM     95  CA  TYR A 253     -16.678  -6.250  15.595  1.00 39.20      A    C  
ANISOU   95  CA  TYR A 253     5898   5327   3668     -9   -226      2  A    C  
ATOM     96  C   TYR A 253     -15.494  -6.228  14.673  1.00 39.08      A    C  
ANISOU   96  C   TYR A 253     5901   5325   3623    -37   -215     21  A    C  
ATOM     97  O   TYR A 253     -14.626  -5.357  14.811  1.00 35.34      A    O  
ANISOU   97  O   TYR A 253     5441   4843   3143    -56   -215     40  A    O  
ATOM     98  CB  TYR A 253     -17.372  -4.915  15.436  1.00 40.01      A    C  
ANISOU   98  CB  TYR A 253     6024   5401   3777      2   -262     10  A    C  
ATOM     99  CG  TYR A 253     -18.066  -4.711  14.119  1.00 42.02      A    C  
ANISOU   99  CG  TYR A 253     6297   5649   4019      5   -292     18  A    C  
ATOM    100  CD1 TYR A 253     -19.003  -5.626  13.661  1.00 43.53      A    C  
ANISOU  100  CD1 TYR A 253     6469   5852   4218     17   -300      5  A    C  
ATOM    101  CD2 TYR A 253     -17.823  -3.576  13.342  1.00 43.14      A    C  
ANISOU  101  CD2 TYR A 253     6480   5769   4142     -7   -321     41  A    C  
ATOM    102  CE1 TYR A 253     -19.661  -5.436  12.455  1.00 43.98      A    C  
ANISOU  102  CE1 TYR A 253     6547   5900   4263     19   -336     13  A    C  
ATOM    103  CE2 TYR A 253     -18.496  -3.361  12.159  1.00 43.21      A    C  
ANISOU  103  CE2 TYR A 253     6513   5768   4137     -4   -356     50  A    C  
ATOM    104  CZ  TYR A 253     -19.412  -4.303  11.716  1.00 43.59      A    C  
ANISOU  104  CZ  TYR A 253     6541   5829   4192     10   -363     34  A    C  
ATOM    105  OH  TYR A 253     -20.068  -4.166  10.522  1.00 43.63      A    O  
ANISOU  105  OH  TYR A 253     6573   5822   4182     12   -403     42  A    O  
ATOM    106  N   VAL A 254     -15.457  -7.184  13.736  1.00 40.26      A    N  
ANISOU  106  N   VAL A 254     6049   5494   3751    -38   -205     17  A    N  
ATOM    107  CA  VAL A 254     -14.388  -7.235  12.738  1.00 43.05      A    C  
ANISOU  107  CA  VAL A 254     6417   5868   4068    -59   -187     33  A    C  
ATOM    108  C   VAL A 254     -14.570  -6.098  11.706  1.00 46.73      A    C  
ANISOU  108  C   VAL A 254     6923   6321   4510    -73   -213     59  A    C  
ATOM    109  O   VAL A 254     -15.434  -6.173  10.830  1.00 50.74      A    O  
ANISOU  109  O   VAL A 254     7452   6821   5003    -64   -238     56  A    O  
ATOM    110  CB  VAL A 254     -14.393  -8.598  12.009  1.00 42.83      A    C  
ANISOU  110  CB  VAL A 254     6388   5864   4021    -48   -174     15  A    C  
ATOM    111  CG1 VAL A 254     -13.310  -8.627  10.968  1.00 42.10      A    C  
ANISOU  111  CG1 VAL A 254     6311   5799   3886    -63   -148     28  A    C  
ATOM    112  CG2 VAL A 254     -14.227  -9.762  13.009  1.00 44.20      A    C  
ANISOU  112  CG2 VAL A 254     6530   6044   4218    -36   -156     -8  A    C  
ATOM    113  N   GLU A 255     -13.781  -5.039  11.818  1.00 47.84      A    N  
ANISOU  113  N   GLU A 255     7075   6454   4645    -98   -212     85  A    N  
ATOM    114  CA  GLU A 255     -13.834  -3.951  10.842  1.00 48.35      A    C  
ANISOU  114  CA  GLU A 255     7182   6503   4683   -119   -238    115  A    C  
ATOM    115  C   GLU A 255     -13.274  -4.280   9.453  1.00 49.88      A    C  
ANISOU  115  C   GLU A 255     7398   6728   4825   -138   -217    132  A    C  
ATOM    116  O   GLU A 255     -13.864  -3.882   8.464  1.00 51.69      A    O  
ANISOU  116  O   GLU A 255     7668   6944   5028   -141   -245    144  A    O  
ATOM    117  CB  GLU A 255     -13.086  -2.768  11.401  1.00 46.75      A    C  
ANISOU  117  CB  GLU A 255     6989   6281   4490   -147   -248    142  A    C  
ATOM    118  CG  GLU A 255     -13.860  -2.123  12.528  1.00 45.10      A    C  
ANISOU  118  CG  GLU A 255     6782   6032   4320   -123   -282    127  A    C  
ATOM    119  CD  GLU A 255     -13.222  -0.853  12.983  1.00 44.22      A    C  
ANISOU  119  CD  GLU A 255     6694   5890   4215   -150   -305    154  A    C  
ATOM    120  OE1 GLU A 255     -12.068  -0.607  12.570  1.00 41.75      A    O  
ANISOU  120  OE1 GLU A 255     6384   5595   3884   -193   -289    186  A    O  
ATOM    121  OE2 GLU A 255     -13.870  -0.134  13.777  1.00 46.22      A    O1-
ANISOU  121  OE2 GLU A 255     6962   6104   4493   -127   -340    141  A    O1-
ATOM    122  N   GLU A 256     -12.137  -4.977   9.396  1.00 49.98      A    N  
ANISOU  122  N   GLU A 256     7384   6781   4823   -149   -168    132  A    N  
ATOM    123  CA  GLU A 256     -11.375  -5.224   8.151  1.00 51.19      A    C  
ANISOU  123  CA  GLU A 256     7554   6974   4923   -166   -135    149  A    C  
ATOM    124  C   GLU A 256     -10.708  -6.593   8.136  1.00 52.83      A    C  
ANISOU  124  C   GLU A 256     7727   7223   5121   -145    -88    121  A    C  
ATOM    125  O   GLU A 256     -10.133  -7.012   9.144  1.00 53.27      A    O  
ANISOU  125  O   GLU A 256     7740   7288   5212   -139    -69    109  A    O  
ATOM    126  CB  GLU A 256     -10.253  -4.211   7.947  1.00 51.72      A    C  
ANISOU  126  CB  GLU A 256     7621   7054   4973   -214   -117    194  A    C  
ATOM    127  CG  GLU A 256     -10.646  -2.908   7.284  1.00 56.01      A    C  
ANISOU  127  CG  GLU A 256     8220   7566   5495   -244   -158    232  A    C  
ATOM    128  CD  GLU A 256      -9.450  -1.989   7.024  1.00 60.16      A    C  
ANISOU  128  CD  GLU A 256     8746   8109   6001   -301   -138    283  A    C  
ATOM    129  OE1 GLU A 256      -8.509  -2.364   6.254  1.00 60.77      A    O  
ANISOU  129  OE1 GLU A 256     8809   8240   6037   -320    -85    299  A    O  
ATOM    130  OE2 GLU A 256      -9.442  -0.886   7.613  1.00 62.97      A    O1-
ANISOU  130  OE2 GLU A 256     9115   8425   6385   -326   -177    306  A    O1-
ATOM    131  N   VAL A 257     -10.771  -7.263   6.978  1.00 52.45      A    N  
ANISOU  131  N   VAL A 257     7705   7198   5024   -132    -73    112  A    N  
ATOM    132  CA  VAL A 257      -9.970  -8.436   6.686  1.00 50.68      A    C  
ANISOU  132  CA  VAL A 257     7460   7017   4778   -110    -26     89  A    C  
ATOM    133  C   VAL A 257      -8.961  -8.082   5.612  1.00 52.97      A    C  
ANISOU  133  C   VAL A 257     7761   7353   5010   -133     18    117  A    C  
ATOM    134  O   VAL A 257      -9.321  -7.551   4.572  1.00 55.18      A    O  
ANISOU  134  O   VAL A 257     8092   7629   5243   -148      7    138  A    O  
ATOM    135  CB  VAL A 257     -10.829  -9.577   6.150  1.00 50.30      A    C  
ANISOU  135  CB  VAL A 257     7440   6959   4711    -72    -45     51  A    C  
ATOM    136  CG1 VAL A 257     -10.029 -10.869   6.095  1.00 51.42      A    C  
ANISOU  136  CG1 VAL A 257     7560   7137   4840    -40     -4     19  A    C  
ATOM    137  CG2 VAL A 257     -12.037  -9.740   7.027  1.00 51.56      A    C  
ANISOU  137  CG2 VAL A 257     7593   7074   4922    -59    -94     33  A    C  
ATOM    138  N   GLU A 258      -7.702  -8.402   5.864  1.00 55.00      A    N  
ANISOU  138  N   GLU A 258     7969   7656   5271   -134     70    119  A    N  
ATOM    139  CA  GLU A 258      -6.605  -8.188   4.932  1.00 56.09      A    C  
ANISOU  139  CA  GLU A 258     8101   7851   5358   -154    127    145  A    C  
ATOM    140  C   GLU A 258      -5.784  -9.474   4.971  1.00 57.54      A    C  
ANISOU  140  C   GLU A 258     8243   8080   5537   -110    175    107  A    C  
ATOM    141  O   GLU A 258      -5.896 -10.215   5.946  1.00 59.30      A    O  
ANISOU  141  O   GLU A 258     8436   8284   5809    -82    159     74  A    O  
ATOM    142  CB  GLU A 258      -5.807  -6.943   5.350  1.00 57.71      A    C  
ANISOU  142  CB  GLU A 258     8276   8064   5586   -212    135    197  A    C  
ATOM    143  CG  GLU A 258      -4.347  -6.943   4.939  1.00 59.15      A    C  
ANISOU  143  CG  GLU A 258     8410   8318   5746   -232    204    221  A    C  
ATOM    144  CD  GLU A 258      -3.779  -5.557   4.694  1.00 61.48      A    C  
ANISOU  144  CD  GLU A 258     8705   8621   6031   -303    208    287  A    C  
ATOM    145  OE1 GLU A 258      -4.450  -4.558   5.074  1.00 58.07      A    O  
ANISOU  145  OE1 GLU A 258     8308   8131   5622   -334    150    311  A    O  
ATOM    146  OE2 GLU A 258      -2.665  -5.489   4.083  1.00 58.47      A    O1-
ANISOU  146  OE2 GLU A 258     8290   8307   5619   -326    270    315  A    O1-
ATOM    147  N   ILE A 259      -5.045  -9.790   3.898  1.00 60.35      A    N  
ANISOU  147  N   ILE A 259     8603   8494   5832   -100    231    109  A    N  
ATOM    148  CA  ILE A 259      -4.159 -10.979   3.856  1.00 62.07      A    C  
ANISOU  148  CA  ILE A 259     8780   8761   6043    -51    281     70  A    C  
ATOM    149  C   ILE A 259      -2.792 -10.510   4.296  1.00 63.27      A    C  
ANISOU  149  C   ILE A 259     8853   8963   6223    -80    329    101  A    C  
ATOM    150  O   ILE A 259      -2.490  -9.324   4.228  1.00 63.97      A    O  
ANISOU  150  O   ILE A 259     8933   9058   6311   -139    334    155  A    O  
ATOM    151  CB  ILE A 259      -4.144 -11.688   2.465  1.00 66.73      A    C  
ANISOU  151  CB  ILE A 259     9419   9386   6549    -12    316     46  A    C  
ATOM    152  CG1 ILE A 259      -5.414 -12.515   2.296  1.00 68.34      A    C  
ANISOU  152  CG1 ILE A 259     9687   9534   6743     26    259      3  A    C  
ATOM    153  CG2 ILE A 259      -2.963 -12.652   2.283  1.00 68.71      A    C  
ANISOU  153  CG2 ILE A 259     9620   9701   6783     36    382     15  A    C  
ATOM    154  CD1 ILE A 259      -5.785 -12.806   0.856  1.00 73.85      A    C  
ANISOU  154  CD1 ILE A 259    10463  10244   7353     47    266     -8  A    C  
ATOM    155  N   HIS A 260      -1.989 -11.439   4.802  1.00 66.93      A    N  
ANISOU  155  N   HIS A 260     9258   9456   6715    -39    357     68  A    N  
ATOM    156  CA  HIS A 260      -0.703 -11.124   5.415  1.00 68.16      A    C  
ANISOU  156  CA  HIS A 260     9327   9654   6913    -61    391     93  A    C  
ATOM    157  C   HIS A 260       0.340 -11.259   4.299  1.00 73.50      A    C  
ANISOU  157  C   HIS A 260     9975  10419   7533    -51    474    103  A    C  
ATOM    158  O   HIS A 260       0.391 -12.312   3.652  1.00 81.00      A    O  
ANISOU  158  O   HIS A 260    10942  11394   8439     11    503     56  A    O  
ATOM    159  CB  HIS A 260      -0.469 -12.107   6.588  1.00 65.19      A    C  
ANISOU  159  CB  HIS A 260     8908   9258   6601    -17    369     49  A    C  
ATOM    160  CG  HIS A 260       0.631 -11.718   7.538  1.00 63.41      A    C  
ANISOU  160  CG  HIS A 260     8599   9054   6439    -44    377     74  A    C  
ATOM    161  CD2 HIS A 260       0.693 -11.762   8.895  1.00 61.86      A    C  
ANISOU  161  CD2 HIS A 260     8374   8817   6312    -49    332     68  A    C  
ATOM    162  ND1 HIS A 260       1.869 -11.285   7.118  1.00 61.25      A    N  
ANISOU  162  ND1 HIS A 260     8259   8851   6158    -69    436    108  A    N  
ATOM    163  CE1 HIS A 260       2.633 -11.049   8.170  1.00 62.56      A    C  
ANISOU  163  CE1 HIS A 260     8359   9018   6394    -90    421    123  A    C  
ATOM    164  NE2 HIS A 260       1.945 -11.330   9.263  1.00 60.12      A    N  
ANISOU  164  NE2 HIS A 260     8074   8638   6128    -77    357     98  A    N  
ATOM    165  N   PRO A 261       1.146 -10.192   4.041  1.00 75.28      A    N  
ANISOU  165  N   PRO A 261    10160  10688   7752   -114    511    163  A    N  
ATOM    166  CA  PRO A 261       2.126 -10.290   2.963  1.00 76.82      A    C  
ANISOU  166  CA  PRO A 261    10324  10976   7889   -109    598    177  A    C  
ATOM    167  C   PRO A 261       3.037 -11.493   3.097  1.00 78.09      A    C  
ANISOU  167  C   PRO A 261    10416  11190   8063    -36    645    127  A    C  
ATOM    168  O   PRO A 261       3.121 -12.283   2.159  1.00 80.67      A    O  
ANISOU  168  O   PRO A 261    10767  11557   8324     20    692     91  A    O  
ATOM    169  CB  PRO A 261       2.930  -8.985   3.081  1.00 78.89      A    C  
ANISOU  169  CB  PRO A 261    10532  11269   8172   -197    617    253  A    C  
ATOM    170  CG  PRO A 261       1.969  -8.019   3.676  1.00 78.18      A    C  
ANISOU  170  CG  PRO A 261    10497  11092   8112   -249    536    282  A    C  
ATOM    171  CD  PRO A 261       1.088  -8.823   4.594  1.00 75.68      A    C  
ANISOU  171  CD  PRO A 261    10206  10706   7840   -195    474    223  A    C  
ATOM    172  N   ASP A 262       3.690 -11.630   4.252  1.00 75.75      A    N  
ANISOU  172  N   ASP A 262    10041  10889   7849    -36    628    124  A    N  
ATOM    173  CA  ASP A 262       4.677 -12.685   4.493  1.00 75.74      A    C  
ANISOU  173  CA  ASP A 262     9963  10939   7874     30    667     81  A    C  
ATOM    174  C   ASP A 262       4.152 -13.941   5.181  1.00 73.89      A    C  
ANISOU  174  C   ASP A 262     9755  10647   7670    105    615     11  A    C  
ATOM    175  O   ASP A 262       4.873 -14.916   5.327  1.00 80.04      A    O  
ANISOU  175  O   ASP A 262    10485  11459   8465    170    639    -31  A    O  
ATOM    176  CB  ASP A 262       5.814 -12.113   5.328  1.00 81.10      A    C  
ANISOU  176  CB  ASP A 262    10535  11650   8627    -14    675    122  A    C  
ATOM    177  CG  ASP A 262       6.354 -10.815   4.756  1.00 85.89      A    C  
ANISOU  177  CG  ASP A 262    11113  12307   9213   -101    717    200  A    C  
ATOM    178  OD1 ASP A 262       6.376 -10.671   3.512  1.00 95.43      A    O  
ANISOU  178  OD1 ASP A 262    12349  13568  10340   -104    778    214  A    O  
ATOM    179  OD2 ASP A 262       6.745  -9.933   5.544  1.00 87.58      A    O1-
ANISOU  179  OD2 ASP A 262    11282  12505   9489   -169    685    249  A    O1-
ATOM    180  N   ALA A 263       2.911 -13.929   5.627  1.00 72.99      A    N  
ANISOU  180  N   ALA A 263     9717  10449   7565     95    544      0  A    N  
ATOM    181  CA  ALA A 263       2.331 -15.135   6.161  1.00 73.78      A    C  
ANISOU  181  CA  ALA A 263     9851  10495   7685    159    496    -60  A    C  
ATOM    182  C   ALA A 263       1.303 -15.610   5.163  1.00 75.39      A    C  
ANISOU  182  C   ALA A 263    10150  10677   7817    190    488    -90  A    C  
ATOM    183  O   ALA A 263       0.299 -14.945   4.905  1.00 78.62      A    O  
ANISOU  183  O   ALA A 263    10621  11045   8204    148    456    -66  A    O  
ATOM    184  CB  ALA A 263       1.717 -14.899   7.527  1.00 74.84      A    C  
ANISOU  184  CB  ALA A 263     9992  10553   7889    128    421    -53  A    C  
ATOM    185  N   ASP A 264       1.606 -16.757   4.577  1.00 74.47      A    N  
ANISOU  185  N   ASP A 264    10043  10587   7663    266    515   -143  A    N  
ATOM    186  CA  ASP A 264       0.732 -17.437   3.650  1.00 76.31      A    C  
ANISOU  186  CA  ASP A 264    10368  10795   7828    308    501   -181  A    C  
ATOM    187  C   ASP A 264      -0.688 -17.674   4.231  1.00 74.09      A    C  
ANISOU  187  C   ASP A 264    10157  10421   7573    295    413   -193  A    C  
ATOM    188  O   ASP A 264      -1.675 -17.327   3.576  1.00 72.25      A    O  
ANISOU  188  O   ASP A 264     9995  10159   7297    273    389   -183  A    O  
ATOM    189  CB  ASP A 264       1.402 -18.773   3.275  1.00 82.08      A    C  
ANISOU  189  CB  ASP A 264    11091  11559   8535    402    531   -245  A    C  
ATOM    190  CG  ASP A 264       0.862 -19.369   2.001  1.00 83.75      A    C  
ANISOU  190  CG  ASP A 264    11394  11771   8656    449    540   -281  A    C  
ATOM    191  OD1 ASP A 264      -0.099 -20.158   2.093  1.00 89.76      A    O  
ANISOU  191  OD1 ASP A 264    12227  12462   9414    476    473   -319  A    O  
ATOM    192  OD2 ASP A 264       1.417 -19.080   0.922  1.00 82.24      A    O1-
ANISOU  192  OD2 ASP A 264    11202  11651   8394    458    613   -272  A    O1-
ATOM    193  N   THR A 265      -0.777 -18.221   5.456  1.00 68.49      A    N  
ANISOU  193  N   THR A 265     9422   9665   6933    306    364   -213  A    N  
ATOM    194  CA  THR A 265      -2.061 -18.694   6.055  1.00 67.73      A    C  
ANISOU  194  CA  THR A 265     9384   9486   6863    303    286   -230  A    C  
ATOM    195  C   THR A 265      -2.812 -17.721   6.985  1.00 62.64      A    C  
ANISOU  195  C   THR A 265     8735   8796   6268    235    243   -188  A    C  
ATOM    196  O   THR A 265      -3.899 -18.037   7.465  1.00 63.67      A    O  
ANISOU  196  O   THR A 265     8906   8867   6419    229    185   -198  A    O  
ATOM    197  CB  THR A 265      -1.882 -20.018   6.878  1.00 70.51      A    C  
ANISOU  197  CB  THR A 265     9728   9805   7256    357    249   -279  A    C  
ATOM    198  CG2 THR A 265      -1.363 -21.172   5.993  1.00 69.99      A    C  
ANISOU  198  CG2 THR A 265     9685   9766   7141    438    274   -334  A    C  
ATOM    199  OG1 THR A 265      -0.989 -19.809   7.988  1.00 65.63      A    O  
ANISOU  199  OG1 THR A 265     9033   9200   6704    345    256   -265  A    O  
ATOM    200  N   LEU A 266      -2.245 -16.559   7.254  1.00 58.94      A    N  
ANISOU  200  N   LEU A 266     8218   8356   5819    185    270   -141  A    N  
ATOM    201  CA  LEU A 266      -2.862 -15.648   8.197  1.00 57.04      A    C  
ANISOU  201  CA  LEU A 266     7975   8071   5625    130    229   -107  A    C  
ATOM    202  C   LEU A 266      -3.617 -14.541   7.474  1.00 58.40      A    C  
ANISOU  202  C   LEU A 266     8190   8236   5762     84    224    -69  A    C  
ATOM    203  O   LEU A 266      -3.085 -13.908   6.551  1.00 56.76      A    O  
ANISOU  203  O   LEU A 266     7979   8074   5511     66    269    -42  A    O  
ATOM    204  CB  LEU A 266      -1.814 -14.997   9.143  1.00 56.91      A    C  
ANISOU  204  CB  LEU A 266     7884   8076   5663     99    243    -77  A    C  
ATOM    205  CG  LEU A 266      -0.762 -15.801   9.917  1.00 55.31      A    C  
ANISOU  205  CG  LEU A 266     7621   7890   5504    135    250   -102  A    C  
ATOM    206  CD1 LEU A 266       0.047 -14.864  10.792  1.00 55.96      A    C  
ANISOU  206  CD1 LEU A 266     7641   7983   5638     87    251    -61  A    C  
ATOM    207  CD2 LEU A 266      -1.370 -16.904  10.762  1.00 55.03      A    C  
ANISOU  207  CD2 LEU A 266     7612   7798   5497    170    198   -142  A    C  
ATOM    208  N   TYR A 267      -4.858 -14.297   7.901  1.00 59.92      A    N  
ANISOU  208  N   TYR A 267     8422   8370   5972     66    170    -66  A    N  
ATOM    209  CA  TYR A 267      -5.494 -12.999   7.651  1.00 58.85      A    C  
ANISOU  209  CA  TYR A 267     8313   8217   5828     17    153    -24  A    C  
ATOM    210  C   TYR A 267      -5.009 -12.030   8.733  1.00 58.30      A    C  
ANISOU  210  C   TYR A 267     8198   8141   5811    -24    148      8  A    C  
ATOM    211  O   TYR A 267      -4.702 -12.451   9.835  1.00 61.63      A    O  
ANISOU  211  O   TYR A 267     8584   8549   6280    -14    136     -5  A    O  
ATOM    212  CB  TYR A 267      -7.018 -13.101   7.714  1.00 57.60      A    C  
ANISOU  212  CB  TYR A 267     8207   8003   5675     18     97    -36  A    C  
ATOM    213  CG  TYR A 267      -7.695 -13.727   6.507  1.00 58.37      A    C  
ANISOU  213  CG  TYR A 267     8363   8096   5716     45     87    -58  A    C  
ATOM    214  CD1 TYR A 267      -7.540 -13.193   5.217  1.00 55.56      A    C  
ANISOU  214  CD1 TYR A 267     8043   7769   5296     34    112    -39  A    C  
ATOM    215  CD2 TYR A 267      -8.531 -14.825   6.671  1.00 57.31      A    C  
ANISOU  215  CD2 TYR A 267     8254   7926   5591     76     48    -96  A    C  
ATOM    216  CE1 TYR A 267      -8.189 -13.762   4.133  1.00 57.40      A    C  
ANISOU  216  CE1 TYR A 267     8339   7994   5476     60     96    -60  A    C  
ATOM    217  CE2 TYR A 267      -9.185 -15.402   5.606  1.00 57.86      A    C  
ANISOU  217  CE2 TYR A 267     8383   7986   5613     99     28   -116  A    C  
ATOM    218  CZ  TYR A 267      -9.013 -14.879   4.330  1.00 61.00      A    C  
ANISOU  218  CZ  TYR A 267     8819   8411   5946     93     51   -100  A    C  
ATOM    219  OH  TYR A 267      -9.686 -15.508   3.289  1.00 57.81      A    O  
ANISOU  219  OH  TYR A 267     8481   7991   5491    118     25   -124  A    O  
ATOM    220  N   CYS A 268      -4.925 -10.749   8.390  1.00 59.15      A    N  
ANISOU  220  N   CYS A 268     8314   8254   5907    -72    151     54  A    N  
ATOM    221  CA  CYS A 268      -4.694  -9.643   9.330  1.00 57.06      A    C  
ANISOU  221  CA  CYS A 268     8025   7967   5686   -116    131     88  A    C  
ATOM    222  C   CYS A 268      -6.009  -8.923   9.596  1.00 53.67      A    C  
ANISOU  222  C   CYS A 268     7644   7480   5267   -131     77     96  A    C  
ATOM    223  O   CYS A 268      -6.487  -8.199   8.707  1.00 53.05      A    O  
ANISOU  223  O   CYS A 268     7608   7396   5152   -151     69    119  A    O  
ATOM    224  CB  CYS A 268      -3.715  -8.632   8.730  1.00 58.03      A    C  
ANISOU  224  CB  CYS A 268     8128   8131   5790   -164    164    138  A    C  
ATOM    225  SG  CYS A 268      -1.966  -9.073   8.877  1.00 63.62      A    S  
ANISOU  225  SG  CYS A 268     8750   8909   6515   -162    223    143  A    S  
ATOM    226  N   LEU A 269      -6.568  -9.083  10.810  1.00 49.79      A    N  
ANISOU  226  N   LEU A 269     7147   6947   4822   -120     42     78  A    N  
ATOM    227  CA  LEU A 269      -7.880  -8.504  11.161  1.00 45.70      A    C  
ANISOU  227  CA  LEU A 269     6667   6379   4318   -123     -5     78  A    C  
ATOM    228  C   LEU A 269      -7.789  -7.255  11.955  1.00 43.70      A    C  
ANISOU  228  C   LEU A 269     6413   6097   4094   -156    -30    107  A    C  
ATOM    229  O   LEU A 269      -6.891  -7.094  12.749  1.00 42.72      A    O  
ANISOU  229  O   LEU A 269     6255   5978   3997   -170    -23    115  A    O  
ATOM    230  CB  LEU A 269      -8.740  -9.464  11.976  1.00 45.36      A    C  
ANISOU  230  CB  LEU A 269     6623   6309   4302    -89    -26     41  A    C  
ATOM    231  CG  LEU A 269      -9.314 -10.618  11.175  1.00 47.02      A    C  
ANISOU  231  CG  LEU A 269     6852   6526   4484    -57    -24     11  A    C  
ATOM    232  CD1 LEU A 269      -8.210 -11.473  10.536  1.00 46.32      A    C  
ANISOU  232  CD1 LEU A 269     6747   6483   4369    -40     17      0  A    C  
ATOM    233  CD2 LEU A 269     -10.250 -11.419  12.085  1.00 47.06      A    C  
ANISOU  233  CD2 LEU A 269     6855   6500   4522    -36    -52    -15  A    C  
ATOM    234  N   LYS A 270      -8.767  -6.379  11.758  1.00 44.74      A    N  
ANISOU  234  N   LYS A 270     6584   6192   4220   -164    -66    119  A    N  
ATOM    235  CA  LYS A 270      -8.900  -5.169  12.553  1.00 45.41      A    C  
ANISOU  235  CA  LYS A 270     6682   6239   4332   -185   -100    139  A    C  
ATOM    236  C   LYS A 270     -10.212  -5.315  13.308  1.00 42.55      A    C  
ANISOU  236  C   LYS A 270     6333   5839   3994   -152   -132    110  A    C  
ATOM    237  O   LYS A 270     -11.266  -5.478  12.704  1.00 40.50      A    O  
ANISOU  237  O   LYS A 270     6095   5570   3721   -133   -147     99  A    O  
ATOM    238  CB  LYS A 270      -8.858  -3.903  11.679  1.00 48.76      A    C  
ANISOU  238  CB  LYS A 270     7143   6652   4730   -222   -118    180  A    C  
ATOM    239  CG  LYS A 270      -7.478  -3.644  11.095  1.00 57.30      A    C  
ANISOU  239  CG  LYS A 270     8203   7775   5791   -265    -83    217  A    C  
ATOM    240  CD  LYS A 270      -7.448  -2.355  10.281  1.00 68.49      A    C  
ANISOU  240  CD  LYS A 270     9663   9177   7181   -309   -104    264  A    C  
ATOM    241  CE  LYS A 270      -6.128  -2.165   9.536  1.00 71.92      A    C  
ANISOU  241  CE  LYS A 270    10074   9663   7588   -356    -60    305  A    C  
ATOM    242  NZ  LYS A 270      -5.050  -1.831  10.510  1.00 74.13      A    N1+
ANISOU  242  NZ  LYS A 270    10308   9947   7910   -387    -59    324  A    N1+
ATOM    243  N   ILE A 271     -10.143  -5.311  14.631  1.00 40.27      A    N  
ANISOU  243  N   ILE A 271     6027   5531   3739   -145   -141     97  A    N  
ATOM    244  CA  ILE A 271     -11.303  -5.685  15.397  1.00 39.88      A    C  
ANISOU  244  CA  ILE A 271     5981   5460   3710   -112   -157     68  A    C  
ATOM    245  C   ILE A 271     -11.550  -4.685  16.517  1.00 39.47      A    C  
ANISOU  245  C   ILE A 271     5944   5370   3681   -111   -185     70  A    C  
ATOM    246  O   ILE A 271     -10.669  -4.387  17.290  1.00 42.29      A    O  
ANISOU  246  O   ILE A 271     6294   5720   4051   -127   -186     78  A    O  
ATOM    247  CB  ILE A 271     -11.176  -7.112  15.938  1.00 39.31      A    C  
ANISOU  247  CB  ILE A 271     5879   5408   3649    -92   -133     40  A    C  
ATOM    248  CG1 ILE A 271     -10.618  -8.081  14.870  1.00 39.05      A    C  
ANISOU  248  CG1 ILE A 271     5835   5411   3590    -91   -105     36  A    C  
ATOM    249  CG2 ILE A 271     -12.546  -7.576  16.358  1.00 40.94      A    C  
ANISOU  249  CG2 ILE A 271     6088   5598   3867    -65   -146     17  A    C  
ATOM    250  CD1 ILE A 271     -10.796  -9.545  15.241  1.00 38.20      A    C  
ANISOU  250  CD1 ILE A 271     5710   5312   3490    -65    -95      5  A    C  
ATOM    251  N   ASN A 272     -12.728  -4.096  16.522  1.00 39.13      A    N  
ANISOU  251  N   ASN A 272     5924   5301   3642    -90   -212     63  A    N  
ATOM    252  CA  ASN A 272     -13.128  -3.105  17.521  1.00 37.97      A    C  
ANISOU  252  CA  ASN A 272     5798   5115   3512    -78   -241     58  A    C  
ATOM    253  C   ASN A 272     -13.622  -3.883  18.722  1.00 38.42      A    C  
ANISOU  253  C   ASN A 272     5834   5177   3587    -49   -225     28  A    C  
ATOM    254  O   ASN A 272     -14.629  -4.629  18.617  1.00 37.68      A    O  
ANISOU  254  O   ASN A 272     5723   5096   3497    -26   -215      9  A    O  
ATOM    255  CB  ASN A 272     -14.264  -2.265  16.955  1.00 36.26      A    C  
ANISOU  255  CB  ASN A 272     5609   4874   3294    -58   -274     59  A    C  
ATOM    256  CG  ASN A 272     -14.922  -1.424  17.986  1.00 36.24      A    C  
ANISOU  256  CG  ASN A 272     5625   4835   3308    -28   -300     43  A    C  
ATOM    257  ND2 ASN A 272     -15.927  -0.691  17.559  1.00 36.32      A    N  
ANISOU  257  ND2 ASN A 272     5656   4822   3321     -4   -333     40  A    N  
ATOM    258  OD1 ASN A 272     -14.561  -1.448  19.187  1.00 36.27      A    O  
ANISOU  258  OD1 ASN A 272     5627   4831   3322    -23   -293     31  A    O  
ATOM    259  N   VAL A 273     -12.905  -3.759  19.838  1.00 38.00      A    N  
ANISOU  259  N   VAL A 273     5783   5112   3542    -56   -224     26  A    N  
ATOM    260  CA  VAL A 273     -13.263  -4.499  21.045  1.00 37.10      A    C  
ANISOU  260  CA  VAL A 273     5655   5000   3437    -33   -208      1  A    C  
ATOM    261  C   VAL A 273     -13.599  -3.502  22.173  1.00 37.90      A    C  
ANISOU  261  C   VAL A 273     5789   5066   3543    -13   -230     -8  A    C  
ATOM    262  O   VAL A 273     -13.518  -3.826  23.342  1.00 38.40      A    O  
ANISOU  262  O   VAL A 273     5855   5125   3608     -3   -221    -23  A    O  
ATOM    263  CB  VAL A 273     -12.167  -5.458  21.505  1.00 37.26      A    C  
ANISOU  263  CB  VAL A 273     5655   5038   3461    -51   -188      1  A    C  
ATOM    264  CG1 VAL A 273     -12.099  -6.692  20.656  1.00 38.45      A    C  
ANISOU  264  CG1 VAL A 273     5778   5224   3608    -54   -164     -1  A    C  
ATOM    265  CG2 VAL A 273     -10.839  -4.777  21.473  1.00 39.80      A    C  
ANISOU  265  CG2 VAL A 273     5984   5351   3786    -83   -203     24  A    C  
ATOM    266  N   GLY A 274     -13.991  -2.290  21.809  1.00 37.81      A    N  
ANISOU  266  N   GLY A 274     5808   5027   3530     -5   -261     -2  A    N  
ATOM    267  CA  GLY A 274     -14.538  -1.343  22.745  1.00 36.94      A    C  
ANISOU  267  CA  GLY A 274     5731   4882   3421     25   -284    -18  A    C  
ATOM    268  C   GLY A 274     -13.500  -0.385  23.188  1.00 37.68      A    C  
ANISOU  268  C   GLY A 274     5865   4938   3513      2   -319     -3  A    C  
ATOM    269  O   GLY A 274     -13.802   0.480  23.970  1.00 38.54      A    O  
ANISOU  269  O   GLY A 274     6014   5010   3619     28   -345    -17  A    O  
ATOM    270  N   GLU A 275     -12.280  -0.520  22.671  1.00 40.34      A    N  
ANISOU  270  N   GLU A 275     6191   5283   3851    -46   -321     25  A    N  
ATOM    271  CA  GLU A 275     -11.168   0.340  23.069  1.00 41.98      A    C  
ANISOU  271  CA  GLU A 275     6430   5458   4063    -79   -358     46  A    C  
ATOM    272  C   GLU A 275     -11.109   1.579  22.221  1.00 44.12      A    C  
ANISOU  272  C   GLU A 275     6735   5697   4331   -100   -399     73  A    C  
ATOM    273  O   GLU A 275     -11.933   1.780  21.352  1.00 42.80      A    O  
ANISOU  273  O   GLU A 275     6571   5532   4157    -85   -401     74  A    O  
ATOM    274  CB  GLU A 275      -9.843  -0.436  23.046  1.00 44.63      A    C  
ANISOU  274  CB  GLU A 275     6728   5822   4408   -121   -338     65  A    C  
ATOM    275  CG  GLU A 275      -9.838  -1.644  23.990  1.00 45.84      A    C  
ANISOU  275  CG  GLU A 275     6855   5996   4563   -101   -308     39  A    C  
ATOM    276  CD  GLU A 275      -8.529  -2.434  23.958  1.00 49.26      A    C  
ANISOU  276  CD  GLU A 275     7249   6456   5009   -135   -294     55  A    C  
ATOM    277  OE1 GLU A 275      -7.749  -2.272  22.976  1.00 50.50      A    O  
ANISOU  277  OE1 GLU A 275     7383   6632   5170   -170   -291     84  A    O  
ATOM    278  OE2 GLU A 275      -8.286  -3.233  24.918  1.00 46.95      A    O1-
ANISOU  278  OE2 GLU A 275     6950   6168   4721   -124   -286     38  A    O1-
ATOM    279  N   GLU A 276     -10.186   2.473  22.550  1.00 51.72      A    N  
ANISOU  279  N   GLU A 276     7729   6622   5299   -136   -442     97  A    N  
ATOM    280  CA  GLU A 276     -10.086   3.757  21.851  1.00 56.18      A    C  
ANISOU  280  CA  GLU A 276     8338   7146   5860   -162   -492    127  A    C  
ATOM    281  C   GLU A 276      -9.729   3.532  20.394  1.00 55.16      A    C  
ANISOU  281  C   GLU A 276     8179   7055   5722   -204   -469    163  A    C  
ATOM    282  O   GLU A 276     -10.214   4.237  19.538  1.00 56.18      A    O  
ANISOU  282  O   GLU A 276     8339   7166   5841   -207   -494    179  A    O  
ATOM    283  CB  GLU A 276      -9.041   4.700  22.511  1.00 61.92      A    C  
ANISOU  283  CB  GLU A 276     9104   7825   6597   -203   -546    151  A    C  
ATOM    284  CG  GLU A 276      -7.567   4.436  22.142  1.00 65.14      A    C  
ANISOU  284  CG  GLU A 276     9469   8261   7017   -274   -537    195  A    C  
ATOM    285  CD  GLU A 276      -6.607   5.522  22.626  1.00 70.90      A    C  
ANISOU  285  CD  GLU A 276    10239   8939   7761   -323   -603    227  A    C  
ATOM    286  OE1 GLU A 276      -6.948   6.729  22.513  1.00 73.39      A    O  
ANISOU  286  OE1 GLU A 276    10619   9195   8070   -327   -661    237  A    O  
ATOM    287  OE2 GLU A 276      -5.494   5.165  23.085  1.00 68.31      A    O1-
ANISOU  287  OE2 GLU A 276     9876   8625   7451   -360   -601    243  A    O1-
ATOM    288  N   LYS A 277      -8.851   2.566  20.140  1.00 56.74      A    N  
ANISOU  288  N   LYS A 277     8325   7307   5926   -233   -425    176  A    N  
ATOM    289  CA  LYS A 277      -8.431   2.179  18.786  1.00 57.47      A    C  
ANISOU  289  CA  LYS A 277     8385   7446   6005   -268   -392    206  A    C  
ATOM    290  C   LYS A 277      -8.771   0.721  18.588  1.00 55.07      A    C  
ANISOU  290  C   LYS A 277     8033   7195   5696   -236   -335    177  A    C  
ATOM    291  O   LYS A 277      -8.694  -0.085  19.515  1.00 52.77      A    O  
ANISOU  291  O   LYS A 277     7716   6914   5417   -213   -316    150  A    O  
ATOM    292  CB  LYS A 277      -6.918   2.351  18.604  1.00 61.69      A    C  
ANISOU  292  CB  LYS A 277     8892   7998   6547   -332   -389    250  A    C  
ATOM    293  CG  LYS A 277      -6.483   3.769  18.250  1.00 68.30      A    C  
ANISOU  293  CG  LYS A 277     9774   8794   7383   -385   -443    296  A    C  
ATOM    294  CD  LYS A 277      -5.060   4.071  18.728  1.00 73.57      A    C  
ANISOU  294  CD  LYS A 277    10418   9460   8073   -444   -459    331  A    C  
ATOM    295  CE  LYS A 277      -4.626   5.481  18.318  1.00 77.23      A    C  
ANISOU  295  CE  LYS A 277    10928   9880   8536   -506   -516    384  A    C  
ATOM    296  NZ  LYS A 277      -3.500   6.041  19.128  1.00 76.27      A    N1+
ANISOU  296  NZ  LYS A 277    10804   9731   8445   -557   -560    413  A    N1+
ATOM    297  N   SER A 278      -9.142   0.377  17.372  1.00 54.83      A    N  
ANISOU  297  N   SER A 278     7994   7194   5644   -236   -311    184  A    N  
ATOM    298  CA  SER A 278      -9.487  -0.992  17.063  1.00 54.99      A    C  
ANISOU  298  CA  SER A 278     7976   7259   5658   -207   -265    158  A    C  
ATOM    299  C   SER A 278      -8.182  -1.802  17.041  1.00 50.08      A    C  
ANISOU  299  C   SER A 278     7306   6681   5040   -232   -227    168  A    C  
ATOM    300  O   SER A 278      -7.134  -1.279  16.696  1.00 47.23      A    O  
ANISOU  300  O   SER A 278     6936   6331   4678   -277   -228    204  A    O  
ATOM    301  CB  SER A 278     -10.233  -1.032  15.737  1.00 59.25      A    C  
ANISOU  301  CB  SER A 278     8530   7811   6171   -201   -261    163  A    C  
ATOM    302  OG  SER A 278     -10.569  -2.359  15.380  1.00 66.92      A    O  
ANISOU  302  OG  SER A 278     9471   8820   7134   -176   -223    138  A    O  
ATOM    303  N   ARG A 279      -8.225  -3.057  17.451  1.00 46.27      A    N  
ANISOU  303  N   ARG A 279     6790   6224   4565   -204   -197    137  A    N  
ATOM    304  CA  ARG A 279      -6.986  -3.823  17.560  1.00 46.55      A    C  
ANISOU  304  CA  ARG A 279     6779   6296   4609   -219   -167    141  A    C  
ATOM    305  C   ARG A 279      -6.660  -4.506  16.261  1.00 45.11      A    C  
ANISOU  305  C   ARG A 279     6574   6164   4401   -221   -127    147  A    C  
ATOM    306  O   ARG A 279      -7.523  -4.704  15.439  1.00 44.95      A    O  
ANISOU  306  O   ARG A 279     6574   6148   4357   -204   -121    139  A    O  
ATOM    307  CB  ARG A 279      -7.085  -4.920  18.625  1.00 47.58      A    C  
ANISOU  307  CB  ARG A 279     6891   6428   4758   -186   -159    106  A    C  
ATOM    308  CG  ARG A 279      -6.937  -4.495  20.069  1.00 50.12      A    C  
ANISOU  308  CG  ARG A 279     7226   6711   5103   -186   -191    100  A    C  
ATOM    309  CD  ARG A 279      -6.790  -5.735  20.980  1.00 49.59      A    C  
ANISOU  309  CD  ARG A 279     7139   6653   5050   -162   -178     71  A    C  
ATOM    310  NE  ARG A 279      -7.003  -5.400  22.388  1.00 50.63      A    N  
ANISOU  310  NE  ARG A 279     7298   6745   5193   -153   -207     59  A    N  
ATOM    311  CZ  ARG A 279      -6.856  -6.233  23.428  1.00 50.33      A    C  
ANISOU  311  CZ  ARG A 279     7256   6701   5163   -138   -207     39  A    C  
ATOM    312  NH1 ARG A 279      -6.470  -7.489  23.286  1.00 47.17      A    N1+
ANISOU  312  NH1 ARG A 279     6823   6329   4768   -128   -185     27  A    N1+
ATOM    313  NH2 ARG A 279      -7.115  -5.780  24.647  1.00 52.93      A    N  
ANISOU  313  NH2 ARG A 279     7621   6993   5494   -131   -233     30  A    N  
ATOM    314  N   ASP A 280      -5.396  -4.881  16.128  1.00 47.19      A    N  
ANISOU  314  N   ASP A 280     6793   6465   4671   -240    -99    160  A    N  
ATOM    315  CA  ASP A 280      -4.860  -5.677  15.041  1.00 47.65      A    C  
ANISOU  315  CA  ASP A 280     6821   6579   4704   -234    -52    160  A    C  
ATOM    316  C   ASP A 280      -4.656  -7.072  15.585  1.00 46.82      A    C  
ANISOU  316  C   ASP A 280     6684   6489   4614   -195    -35    121  A    C  
ATOM    317  O   ASP A 280      -3.877  -7.266  16.509  1.00 44.48      A    O  
ANISOU  317  O   ASP A 280     6357   6192   4350   -198    -42    119  A    O  
ATOM    318  CB  ASP A 280      -3.504  -5.123  14.602  1.00 49.85      A    C  
ANISOU  318  CB  ASP A 280     7063   6893   4983   -280    -32    202  A    C  
ATOM    319  CG  ASP A 280      -3.625  -3.803  13.812  1.00 53.02      A    C  
ANISOU  319  CG  ASP A 280     7500   7284   5361   -327    -46    247  A    C  
ATOM    320  OD1 ASP A 280      -4.326  -3.780  12.755  1.00 54.50      A    O  
ANISOU  320  OD1 ASP A 280     7722   7477   5507   -319    -36    248  A    O  
ATOM    321  OD2 ASP A 280      -2.990  -2.804  14.239  1.00 51.33      A    O1-
ANISOU  321  OD2 ASP A 280     7283   7052   5168   -373    -73    283  A    O1-
ATOM    322  N   ILE A 281      -5.370  -8.031  15.016  1.00 45.85      A    N  
ANISOU  322  N   ILE A 281     6574   6377   4469   -159    -20     92  A    N  
ATOM    323  CA  ILE A 281      -5.287  -9.417  15.417  1.00 44.50      A    C  
ANISOU  323  CA  ILE A 281     6383   6215   4307   -121     -9     55  A    C  
ATOM    324  C   ILE A 281      -5.072 -10.251  14.140  1.00 46.03      A    C  
ANISOU  324  C   ILE A 281     6572   6452   4465    -98     27     42  A    C  
ATOM    325  O   ILE A 281      -5.863 -10.151  13.191  1.00 42.93      A    O  
ANISOU  325  O   ILE A 281     6214   6058   4038    -94     28     42  A    O  
ATOM    326  CB  ILE A 281      -6.604  -9.867  16.128  1.00 42.62      A    C  
ANISOU  326  CB  ILE A 281     6177   5937   4079    -97    -38     28  A    C  
ATOM    327  CG1 ILE A 281      -6.757  -9.217  17.516  1.00 43.64      A    C  
ANISOU  327  CG1 ILE A 281     6313   6027   4239   -109    -68     33  A    C  
ATOM    328  CG2 ILE A 281      -6.680 -11.374  16.302  1.00 41.34      A    C  
ANISOU  328  CG2 ILE A 281     6007   5781   3920    -61    -31     -6  A    C  
ATOM    329  CD1 ILE A 281      -8.169  -9.275  18.102  1.00 40.97      A    C  
ANISOU  329  CD1 ILE A 281     6006   5655   3903    -92    -90     16  A    C  
ATOM    330  N   CYS A 282      -4.035 -11.089  14.134  1.00 49.59      A    N  
ANISOU  330  N   CYS A 282     6980   6936   4922    -78     53     28  A    N  
ATOM    331  CA  CYS A 282      -3.894 -12.148  13.104  1.00 55.22      A    C  
ANISOU  331  CA  CYS A 282     7694   7684   5600    -40     85      1  A    C  
ATOM    332  C   CYS A 282      -4.789 -13.404  13.341  1.00 56.11      A    C  
ANISOU  332  C   CYS A 282     7837   7768   5713      0     61    -40  A    C  
ATOM    333  O   CYS A 282      -5.161 -13.721  14.469  1.00 52.08      A    O  
ANISOU  333  O   CYS A 282     7329   7222   5236      3     30    -52  A    O  
ATOM    334  CB  CYS A 282      -2.425 -12.578  12.976  1.00 58.29      A    C  
ANISOU  334  CB  CYS A 282     8024   8125   5998    -27    122      0  A    C  
ATOM    335  SG  CYS A 282      -1.355 -11.337  12.179  1.00 66.74      A    S  
ANISOU  335  SG  CYS A 282     9056   9249   7052    -76    165     52  A    S  
ATOM    336  N   SER A 283      -5.125 -14.113  12.259  1.00 58.71      A    N  
ANISOU  336  N   SER A 283     8193   8112   6002     29     74    -62  A    N  
ATOM    337  CA  SER A 283      -5.856 -15.375  12.358  1.00 56.14      A    C  
ANISOU  337  CA  SER A 283     7897   7759   5674     65     49   -100  A    C  
ATOM    338  C   SER A 283      -5.437 -16.335  11.256  1.00 58.30      A    C  
ANISOU  338  C   SER A 283     8181   8062   5906    107     74   -129  A    C  
ATOM    339  O   SER A 283      -5.263 -15.940  10.088  1.00 56.87      A    O  
ANISOU  339  O   SER A 283     8012   7914   5679    106    104   -120  A    O  
ATOM    340  CB  SER A 283      -7.353 -15.134  12.260  1.00 57.29      A    C  
ANISOU  340  CB  SER A 283     8086   7865   5813     51     14    -96  A    C  
ATOM    341  OG  SER A 283      -8.060 -16.333  12.522  1.00 59.49      A    O  
ANISOU  341  OG  SER A 283     8387   8115   6099     75    -15   -127  A    O  
ATOM    342  N   GLY A 284      -5.331 -17.606  11.629  1.00 57.10      A    N  
ANISOU  342  N   GLY A 284     8032   7895   5766    146     57   -166  A    N  
ATOM    343  CA  GLY A 284      -4.931 -18.664  10.730  1.00 58.99      A    C  
ANISOU  343  CA  GLY A 284     8288   8155   5970    198     72   -203  A    C  
ATOM    344  C   GLY A 284      -6.122 -19.331  10.096  1.00 62.56      A    C  
ANISOU  344  C   GLY A 284     8805   8571   6391    211     36   -224  A    C  
ATOM    345  O   GLY A 284      -6.197 -20.546  10.046  1.00 66.79      A    O  
ANISOU  345  O   GLY A 284     9366   9087   6922    250     13   -261  A    O  
ATOM    346  N   LEU A 285      -7.062 -18.538   9.603  1.00 66.22      A    N  
ANISOU  346  N   LEU A 285     9297   9024   6836    178     26   -200  A    N  
ATOM    347  CA  LEU A 285      -8.202 -19.061   8.848  1.00 63.53      A    C  
ANISOU  347  CA  LEU A 285     9018   8654   6466    187    -10   -216  A    C  
ATOM    348  C   LEU A 285      -8.073 -18.810   7.342  1.00 61.76      A    C  
ANISOU  348  C   LEU A 285     8830   8461   6175    201     15   -218  A    C  
ATOM    349  O   LEU A 285      -9.056 -18.965   6.637  1.00 64.64      A    O  
ANISOU  349  O   LEU A 285     9247   8800   6512    199    -18   -223  A    O  
ATOM    350  CB  LEU A 285      -9.489 -18.377   9.322  1.00 62.37      A    C  
ANISOU  350  CB  LEU A 285     8879   8469   6346    144    -48   -190  A    C  
ATOM    351  CG  LEU A 285      -9.888 -18.535  10.787  1.00 60.66      A    C  
ANISOU  351  CG  LEU A 285     8637   8222   6189    126    -75   -185  A    C  
ATOM    352  CD1 LEU A 285     -10.597 -17.282  11.297  1.00 60.10      A    C  
ANISOU  352  CD1 LEU A 285     8551   8140   6141     85    -82   -150  A    C  
ATOM    353  CD2 LEU A 285     -10.760 -19.770  10.982  1.00 59.88      A    C  
ANISOU  353  CD2 LEU A 285     8569   8081   6100    138   -123   -209  A    C  
ATOM    354  N   ARG A 286      -6.905 -18.427   6.827  1.00 62.83      A    N  
ANISOU  354  N   ARG A 286     8939   8652   6282    211     74   -211  A    N  
ATOM    355  CA  ARG A 286      -6.812 -18.073   5.376  1.00 64.37      A    C  
ANISOU  355  CA  ARG A 286     9172   8879   6403    218    105   -206  A    C  
ATOM    356  C   ARG A 286      -7.143 -19.247   4.426  1.00 63.08      A    C  
ANISOU  356  C   ARG A 286     9075   8704   6187    269     86   -252  A    C  
ATOM    357  O   ARG A 286      -7.835 -19.060   3.435  1.00 63.03      A    O  
ANISOU  357  O   ARG A 286     9128   8687   6131    264     70   -249  A    O  
ATOM    358  CB  ARG A 286      -5.453 -17.446   5.023  1.00 63.04      A    C  
ANISOU  358  CB  ARG A 286     8956   8781   6213    215    179   -186  A    C  
ATOM    359  N   LEU A 287      -6.718 -20.459   4.764  1.00 65.80      A    N  
ANISOU  359  N   LEU A 287     9415   9039   6544    318     78   -295  A    N  
ATOM    360  CA  LEU A 287      -6.972 -21.637   3.899  1.00 68.96      A    C  
ANISOU  360  CA  LEU A 287     9885   9421   6894    373     54   -344  A    C  
ATOM    361  C   LEU A 287      -8.326 -22.303   4.098  1.00 68.38      A    C  
ANISOU  361  C   LEU A 287     9866   9275   6840    362    -29   -356  A    C  
ATOM    362  O   LEU A 287      -8.676 -23.189   3.320  1.00 71.83      A    O  
ANISOU  362  O   LEU A 287    10370   9687   7234    399    -62   -392  A    O  
ATOM    363  CB  LEU A 287      -5.903 -22.720   4.094  1.00 71.37      A    C  
ANISOU  363  CB  LEU A 287    10170   9745   7200    438     75   -389  A    C  
ATOM    364  CG  LEU A 287      -4.495 -22.446   3.550  1.00 76.18      A    C  
ANISOU  364  CG  LEU A 287    10735  10435   7774    471    161   -393  A    C  
ATOM    365  CD1 LEU A 287      -3.568 -23.569   3.996  1.00 78.55      A    C  
ANISOU  365  CD1 LEU A 287    11006  10741   8095    539    167   -440  A    C  
ATOM    366  CD2 LEU A 287      -4.467 -22.291   2.027  1.00 78.56      A    C  
ANISOU  366  CD2 LEU A 287    11093  10773   7982    494    198   -401  A    C  
ATOM    367  N   LYS A 288      -9.081 -21.927   5.128  1.00 64.52      A    N  
ANISOU  367  N   LYS A 288     9349   8751   6414    314    -66   -328  A    N  
ATOM    368  CA  LYS A 288     -10.389 -22.554   5.343  1.00 60.63      A    C  
ANISOU  368  CA  LYS A 288     8896   8195   5944    299   -142   -334  A    C  
ATOM    369  C   LYS A 288     -11.558 -21.594   5.321  1.00 58.01      A    C  
ANISOU  369  C   LYS A 288     8567   7845   5629    245   -170   -296  A    C  
ATOM    370  O   LYS A 288     -12.704 -22.035   5.421  1.00 58.65      A    O  
ANISOU  370  O   LYS A 288     8673   7879   5730    229   -232   -297  A    O  
ATOM    371  CB  LYS A 288     -10.390 -23.381   6.628  1.00 61.22      A    C  
ANISOU  371  CB  LYS A 288     8944   8236   6079    299   -172   -345  A    C  
ATOM    372  CG  LYS A 288      -9.538 -24.632   6.508  1.00 64.75      A    C  
ANISOU  372  CG  LYS A 288     9411   8680   6509    360   -174   -393  A    C  
ATOM    373  CD  LYS A 288      -9.457 -25.421   7.796  1.00 65.72      A    C  
ANISOU  373  CD  LYS A 288     9512   8767   6689    359   -206   -400  A    C  
ATOM    374  CE  LYS A 288      -8.912 -26.825   7.569  1.00 68.03      A    C  
ANISOU  374  CE  LYS A 288     9847   9037   6964    421   -233   -452  A    C  
ATOM    375  NZ  LYS A 288      -8.906 -27.610   8.836  1.00 71.71      A    N1+
ANISOU  375  NZ  LYS A 288    10300   9460   7484    414   -274   -455  A    N1+
ATOM    376  N   LYS A 289     -11.296 -20.301   5.138  1.00 55.74      A    N  
ANISOU  376  N   LYS A 289     8253   7593   5332    219   -129   -262  A    N  
ATOM    377  CA  LYS A 289     -12.372 -19.308   5.163  1.00 53.12      A    C  
ANISOU  377  CA  LYS A 289     7921   7242   5019    174   -157   -226  A    C  
ATOM    378  C   LYS A 289     -12.113 -18.172   4.227  1.00 50.06      A    C  
ANISOU  378  C   LYS A 289     7549   6887   4585    161   -125   -200  A    C  
ATOM    379  O   LYS A 289     -10.986 -17.730   4.124  1.00 49.82      A    O  
ANISOU  379  O   LYS A 289     7493   6902   4534    165    -66   -191  A    O  
ATOM    380  CB  LYS A 289     -12.497 -18.715   6.575  1.00 53.80      A    C  
ANISOU  380  CB  LYS A 289     7944   7322   5174    142   -153   -201  A    C  
ATOM    381  CG  LYS A 289     -13.125 -19.634   7.611  1.00 52.31      A    C  
ANISOU  381  CG  LYS A 289     7742   7094   5036    138   -194   -214  A    C  
ATOM    382  CD  LYS A 289     -14.623 -19.704   7.475  1.00 51.07      A    C  
ANISOU  382  CD  LYS A 289     7606   6900   4898    116   -254   -205  A    C  
ATOM    383  CE  LYS A 289     -15.115 -21.119   7.679  1.00 49.78      A    C  
ANISOU  383  CE  LYS A 289     7465   6698   4747    125   -303   -230  A    C  
ATOM    384  NZ  LYS A 289     -16.597 -21.068   7.657  1.00 49.61      A    N1+
ANISOU  384  NZ  LYS A 289     7448   6645   4754     95   -359   -215  A    N1+
ATOM    385  N   ASN A 290     -13.165 -17.659   3.591  1.00 51.07      A    N  
ANISOU  385  N   ASN A 290     7715   6989   4698    140   -167   -184  A    N  
ATOM    386  CA  ASN A 290     -13.051 -16.446   2.748  1.00 52.96      A    C  
ANISOU  386  CA  ASN A 290     7976   7251   4895    119   -147   -152  A    C  
ATOM    387  C   ASN A 290     -13.203 -15.152   3.582  1.00 55.21      A    C  
ANISOU  387  C   ASN A 290     8212   7534   5229     79   -141   -112  A    C  
ATOM    388  O   ASN A 290     -13.734 -15.181   4.689  1.00 54.24      A    O  
ANISOU  388  O   ASN A 290     8049   7388   5170     68   -164   -111  A    O  
ATOM    389  CB  ASN A 290     -14.108 -16.464   1.635  1.00 52.49      A    C  
ANISOU  389  CB  ASN A 290     7986   7159   4795    118   -203   -154  A    C  
ATOM    390  CG  ASN A 290     -14.152 -17.788   0.832  1.00 51.55      A    C  
ANISOU  390  CG  ASN A 290     7928   7028   4628    159   -226   -197  A    C  
ATOM    391  ND2 ASN A 290     -15.324 -18.407   0.812  1.00 51.97      A    N  
ANISOU  391  ND2 ASN A 290     8008   7031   4706    157   -301   -210  A    N  
ATOM    392  OD1 ASN A 290     -13.179 -18.210   0.206  1.00 47.86      A    O  
ANISOU  392  OD1 ASN A 290     7485   6596   4103    192   -180   -218  A    O  
ATOM    393  N   SER A 291     -12.778 -14.017   3.046  1.00 59.04      A    N  
ANISOU  393  N   SER A 291     8707   8043   5683     56   -114    -79  A    N  
ATOM    394  CA  SER A 291     -12.810 -12.748   3.793  1.00 61.31      A    C  
ANISOU  394  CA  SER A 291     8956   8325   6012     20   -112    -42  A    C  
ATOM    395  C   SER A 291     -14.204 -12.321   4.234  1.00 63.48      A    C  
ANISOU  395  C   SER A 291     9231   8552   6333      7   -175    -35  A    C  
ATOM    396  O   SER A 291     -14.417 -11.899   5.377  1.00 65.15      A    O  
ANISOU  396  O   SER A 291     9398   8751   6603     -3   -181    -27  A    O  
ATOM    397  CB  SER A 291     -12.220 -11.610   2.951  1.00 66.21      A    C  
ANISOU  397  CB  SER A 291     9601   8972   6583     -7    -84     -5  A    C  
ATOM    398  OG  SER A 291     -13.170 -11.119   2.012  1.00 70.66      A    O  
ANISOU  398  OG  SER A 291    10225   9507   7113    -16   -132      8  A    O  
ATOM    399  N   GLU A 292     -15.155 -12.375   3.314  1.00 65.48      A    N  
ANISOU  399  N   GLU A 292     9536   8782   6561     11   -223    -37  A    N  
ATOM    400  CA  GLU A 292     -16.523 -11.973   3.636  1.00 64.51      A    C  
ANISOU  400  CA  GLU A 292     9408   8618   6485      3   -285    -31  A    C  
ATOM    401  C   GLU A 292     -17.154 -12.887   4.714  1.00 59.51      A    C  
ANISOU  401  C   GLU A 292     8729   7967   5914     14   -304    -54  A    C  
ATOM    402  O   GLU A 292     -18.205 -12.548   5.278  1.00 64.99      A    O  
ANISOU  402  O   GLU A 292     9397   8637   6658      8   -342    -48  A    O  
ATOM    403  CB  GLU A 292     -17.376 -11.886   2.358  1.00 66.50      A    C  
ANISOU  403  CB  GLU A 292     9725   8846   6696      5   -340    -28  A    C  
ATOM    404  CG  GLU A 292     -17.796 -13.222   1.747  1.00 73.91      A    C  
ANISOU  404  CG  GLU A 292    10698   9771   7611     27   -371    -60  A    C  
ATOM    405  CD  GLU A 292     -16.738 -13.913   0.867  1.00 79.53      A    C  
ANISOU  405  CD  GLU A 292    11456  10514   8248     47   -328    -78  A    C  
ATOM    406  OE1 GLU A 292     -15.933 -13.257   0.157  1.00 76.18      A    O  
ANISOU  406  OE1 GLU A 292    11060  10118   7764     40   -287    -60  A    O  
ATOM    407  OE2 GLU A 292     -16.749 -15.159   0.861  1.00 87.55      A    O1-
ANISOU  407  OE2 GLU A 292    12482  11523   9260     71   -337   -112  A    O1-
ATOM    408  N   ASP A 293     -16.511 -14.016   5.014  1.00 53.55      A    N  
ANISOU  408  N   ASP A 293     7963   7226   5155     30   -277    -79  A    N  
ATOM    409  CA  ASP A 293     -16.950 -14.916   6.088  1.00 53.30      A    C  
ANISOU  409  CA  ASP A 293     7893   7180   5177     35   -291    -97  A    C  
ATOM    410  C   ASP A 293     -16.663 -14.383   7.494  1.00 53.96      A    C  
ANISOU  410  C   ASP A 293     7918   7271   5311     23   -262    -85  A    C  
ATOM    411  O   ASP A 293     -17.281 -14.802   8.474  1.00 53.43      A    O  
ANISOU  411  O   ASP A 293     7818   7190   5292     19   -277    -90  A    O  
ATOM    412  CB  ASP A 293     -16.238 -16.246   5.957  1.00 52.73      A    C  
ANISOU  412  CB  ASP A 293     7836   7117   5082     58   -276   -128  A    C  
ATOM    413  CG  ASP A 293     -16.691 -16.998   4.781  1.00 53.16      A    C  
ANISOU  413  CG  ASP A 293     7950   7153   5093     74   -315   -147  A    C  
ATOM    414  OD1 ASP A 293     -17.923 -17.024   4.590  1.00 49.88      A    O  
ANISOU  414  OD1 ASP A 293     7545   6707   4699     62   -374   -142  A    O  
ATOM    415  OD2 ASP A 293     -15.831 -17.528   4.044  1.00 57.76      A    O1-
ANISOU  415  OD2 ASP A 293     8569   7754   5621     99   -290   -167  A    O1-
ATOM    416  N   LEU A 294     -15.698 -13.475   7.548  1.00 51.08      A    N  
ANISOU  416  N   LEU A 294     7546   6929   4932     15   -221    -67  A    N  
ATOM    417  CA  LEU A 294     -15.212 -12.877   8.735  1.00 49.54      A    C  
ANISOU  417  CA  LEU A 294     7308   6741   4773      4   -195    -56  A    C  
ATOM    418  C   LEU A 294     -15.604 -11.390   8.827  1.00 50.18      A    C  
ANISOU  418  C   LEU A 294     7388   6810   4866    -13   -208    -27  A    C  
ATOM    419  O   LEU A 294     -15.823 -10.863   9.949  1.00 48.35      A    O  
ANISOU  419  O   LEU A 294     7126   6568   4676    -18   -208    -22  A    O  
ATOM    420  CB  LEU A 294     -13.681 -12.978   8.722  1.00 48.79      A    C  
ANISOU  420  CB  LEU A 294     7202   6679   4654      6   -143    -56  A    C  
ATOM    421  CG  LEU A 294     -12.987 -14.335   8.591  1.00 47.91      A    C  
ANISOU  421  CG  LEU A 294     7091   6584   4526     32   -124    -86  A    C  
ATOM    422  CD1 LEU A 294     -11.469 -14.192   8.577  1.00 46.92      A    C  
ANISOU  422  CD1 LEU A 294     6944   6498   4384     34    -71    -81  A    C  
ATOM    423  CD2 LEU A 294     -13.379 -15.213   9.759  1.00 48.44      A    C  
ANISOU  423  CD2 LEU A 294     7134   6630   4641     38   -142   -103  A    C  
ATOM    424  N   LEU A 295     -15.665 -10.715   7.669  1.00 46.72      A    N  
ANISOU  424  N   LEU A 295     6991   6372   4388    -21   -220    -11  A    N  
ATOM    425  CA  LEU A 295     -15.816  -9.277   7.651  1.00 46.08      A    C  
ANISOU  425  CA  LEU A 295     6920   6278   4311    -38   -234     17  A    C  
ATOM    426  C   LEU A 295     -17.105  -8.877   8.352  1.00 45.00      A    C  
ANISOU  426  C   LEU A 295     6764   6109   4224    -29   -276     14  A    C  
ATOM    427  O   LEU A 295     -18.129  -9.528   8.232  1.00 47.98      A    O  
ANISOU  427  O   LEU A 295     7138   6474   4618    -16   -307     -1  A    O  
ATOM    428  CB  LEU A 295     -15.784  -8.719   6.200  1.00 47.10      A    C  
ANISOU  428  CB  LEU A 295     7105   6407   4383    -49   -248     37  A    C  
ATOM    429  CG  LEU A 295     -15.685  -7.192   6.076  1.00 45.86      A    C  
ANISOU  429  CG  LEU A 295     6968   6235   4222    -74   -261     73  A    C  
ATOM    430  CD1 LEU A 295     -14.350  -6.671   6.566  1.00 45.64      A    C  
ANISOU  430  CD1 LEU A 295     6919   6231   4191    -98   -215     93  A    C  
ATOM    431  CD2 LEU A 295     -15.904  -6.706   4.663  1.00 48.29      A    C  
ANISOU  431  CD2 LEU A 295     7338   6535   4474    -85   -287     93  A    C  
ATOM    432  N   HIS A 296     -17.058  -7.810   9.127  1.00 43.35      A    N  
ANISOU  432  N   HIS A 296     6540   5887   4040    -36   -277     28  A    N  
ATOM    433  CA  HIS A 296     -18.290  -7.290   9.715  1.00 42.00      A    C  
ANISOU  433  CA  HIS A 296     6354   5691   3914    -20   -314     24  A    C  
ATOM    434  C   HIS A 296     -19.063  -8.292  10.588  1.00 40.25      A    C  
ANISOU  434  C   HIS A 296     6088   5472   3731     -4   -312      0  A    C  
ATOM    435  O   HIS A 296     -20.240  -8.129  10.844  1.00 37.43      A    O  
ANISOU  435  O   HIS A 296     5711   5101   3407     10   -342     -5  A    O  
ATOM    436  CB  HIS A 296     -19.163  -6.661   8.624  1.00 41.29      A    C  
ANISOU  436  CB  HIS A 296     6301   5577   3809    -17   -365     35  A    C  
ATOM    437  CG  HIS A 296     -18.581  -5.391   8.088  1.00 42.79      A    C  
ANISOU  437  CG  HIS A 296     6533   5755   3970    -35   -374     64  A    C  
ATOM    438  CD2 HIS A 296     -17.605  -4.586   8.587  1.00 43.13      A    C  
ANISOU  438  CD2 HIS A 296     6578   5798   4009    -55   -350     83  A    C  
ATOM    439  ND1 HIS A 296     -18.973  -4.822   6.888  1.00 41.65      A    N  
ANISOU  439  ND1 HIS A 296     6438   5591   3793    -42   -415     82  A    N  
ATOM    440  CE1 HIS A 296     -18.272  -3.726   6.681  1.00 42.09      A    C  
ANISOU  440  CE1 HIS A 296     6527   5637   3826    -65   -414    111  A    C  
ATOM    441  NE2 HIS A 296     -17.441  -3.550   7.698  1.00 43.90      A    N  
ANISOU  441  NE2 HIS A 296     6726   5878   4074    -75   -376    113  A    N  
ATOM    442  N   LYS A 297     -18.365  -9.307  11.083  1.00 42.34      A    N  
ANISOU  442  N   LYS A 297     6335   5756   3994     -7   -277    -12  A    N  
ATOM    443  CA  LYS A 297     -18.903 -10.181  12.133  1.00 42.39      A    C  
ANISOU  443  CA  LYS A 297     6302   5765   4037      0   -271    -29  A    C  
ATOM    444  C   LYS A 297     -18.546  -9.643  13.522  1.00 42.19      A    C  
ANISOU  444  C   LYS A 297     6253   5740   4037      0   -245    -28  A    C  
ATOM    445  O   LYS A 297     -17.566  -8.892  13.708  1.00 43.04      A    O  
ANISOU  445  O   LYS A 297     6373   5848   4132     -7   -229    -17  A    O  
ATOM    446  CB  LYS A 297     -18.360 -11.606  12.008  1.00 43.25      A    C  
ANISOU  446  CB  LYS A 297     6412   5887   4132     -3   -255    -44  A    C  
ATOM    447  CG  LYS A 297     -18.717 -12.312  10.720  1.00 45.14      A    C  
ANISOU  447  CG  LYS A 297     6683   6123   4345     -1   -283    -51  A    C  
ATOM    448  CD  LYS A 297     -20.204 -12.518  10.554  1.00 45.82      A    C  
ANISOU  448  CD  LYS A 297     6757   6193   4459      1   -329    -52  A    C  
ATOM    449  CE  LYS A 297     -20.481 -13.039   9.146  1.00 50.13      A    C  
ANISOU  449  CE  LYS A 297     7346   6729   4972      2   -366    -57  A    C  
ATOM    450  NZ  LYS A 297     -19.708 -14.294   8.831  1.00 49.82      A    N1+
ANISOU  450  NZ  LYS A 297     7330   6696   4902      5   -352    -75  A    N1+
ATOM    451  N   TYR A 298     -19.379 -10.054  14.472  1.00 41.83      A    N  
ANISOU  451  N   TYR A 298     6173   5694   4023      9   -245    -38  A    N  
ATOM    452  CA  TYR A 298     -19.173  -9.873  15.908  1.00 41.56      A    C  
ANISOU  452  CA  TYR A 298     6119   5662   4009     12   -219    -42  A    C  
ATOM    453  C   TYR A 298     -18.490 -11.150  16.366  1.00 40.68      A    C  
ANISOU  453  C   TYR A 298     6001   5562   3893      1   -197    -51  A    C  
ATOM    454  O   TYR A 298     -19.046 -12.240  16.215  1.00 40.56      A    O  
ANISOU  454  O   TYR A 298     5975   5550   3884     -2   -206    -58  A    O  
ATOM    455  CB  TYR A 298     -20.530  -9.631  16.649  1.00 40.09      A    C  
ANISOU  455  CB  TYR A 298     5900   5475   3855     29   -226    -48  A    C  
ATOM    456  CG  TYR A 298     -21.028  -8.202  16.517  1.00 40.25      A    C  
ANISOU  456  CG  TYR A 298     5928   5480   3883     50   -247    -44  A    C  
ATOM    457  CD1 TYR A 298     -20.634  -7.220  17.408  1.00 41.78      A    C  
ANISOU  457  CD1 TYR A 298     6133   5663   4077     62   -236    -45  A    C  
ATOM    458  CD2 TYR A 298     -21.865  -7.830  15.477  1.00 41.24      A    C  
ANISOU  458  CD2 TYR A 298     6058   5597   4014     59   -285    -40  A    C  
ATOM    459  CE1 TYR A 298     -21.073  -5.906  17.278  1.00 42.26      A    C  
ANISOU  459  CE1 TYR A 298     6208   5702   4144     85   -261    -44  A    C  
ATOM    460  CE2 TYR A 298     -22.299  -6.530  15.321  1.00 41.60      A    C  
ANISOU  460  CE2 TYR A 298     6115   5622   4066     81   -311    -37  A    C  
ATOM    461  CZ  TYR A 298     -21.897  -5.569  16.224  1.00 43.15      A    C  
ANISOU  461  CZ  TYR A 298     6324   5807   4264     95   -299    -39  A    C  
ATOM    462  OH  TYR A 298     -22.354  -4.280  16.080  1.00 43.94      A    O  
ANISOU  462  OH  TYR A 298     6441   5880   4370    121   -332    -39  A    O  
ATOM    463  N   VAL A 299     -17.279 -11.033  16.912  1.00 40.85      A    N  
ANISOU  463  N   VAL A 299     6030   5586   3905     -4   -175    -49  A    N  
ATOM    464  CA  VAL A 299     -16.524 -12.239  17.251  1.00 40.41      A    C  
ANISOU  464  CA  VAL A 299     5971   5537   3844    -11   -160    -59  A    C  
ATOM    465  C   VAL A 299     -16.190 -12.193  18.722  1.00 41.26      A    C  
ANISOU  465  C   VAL A 299     6069   5641   3966    -12   -144    -60  A    C  
ATOM    466  O   VAL A 299     -16.455 -11.164  19.385  1.00 39.30      A    O  
ANISOU  466  O   VAL A 299     5821   5385   3726     -7   -142    -56  A    O  
ATOM    467  CB  VAL A 299     -15.275 -12.392  16.386  1.00 40.50      A    C  
ANISOU  467  CB  VAL A 299     5998   5560   3831    -14   -150    -58  A    C  
ATOM    468  CG1 VAL A 299     -15.688 -12.591  14.950  1.00 41.65      A    C  
ANISOU  468  CG1 VAL A 299     6161   5709   3954    -10   -166    -58  A    C  
ATOM    469  CG2 VAL A 299     -14.377 -11.173  16.497  1.00 40.63      A    C  
ANISOU  469  CG2 VAL A 299     6018   5576   3840    -22   -140    -42  A    C  
ATOM    470  N   LEU A 300     -15.668 -13.326  19.223  1.00 41.45      A    N  
ANISOU  470  N   LEU A 300     6091   5666   3991    -17   -137    -69  A    N  
ATOM    471  CA  LEU A 300     -15.199 -13.447  20.610  1.00 41.23      A    C  
ANISOU  471  CA  LEU A 300     6062   5632   3971    -21   -126    -70  A    C  
ATOM    472  C   LEU A 300     -13.705 -13.397  20.681  1.00 39.71      A    C  
ANISOU  472  C   LEU A 300     5874   5440   3772    -23   -120    -70  A    C  
ATOM    473  O   LEU A 300     -13.027 -14.305  20.225  1.00 42.07      A    O  
ANISOU  473  O   LEU A 300     6173   5745   4066    -20   -121    -78  A    O  
ATOM    474  CB  LEU A 300     -15.674 -14.748  21.222  1.00 40.96      A    C  
ANISOU  474  CB  LEU A 300     6024   5594   3943    -28   -128    -76  A    C  
ATOM    475  CG  LEU A 300     -17.214 -14.841  21.342  1.00 42.23      A    C  
ANISOU  475  CG  LEU A 300     6168   5760   4117    -32   -131    -72  A    C  
ATOM    476  CD1 LEU A 300     -17.578 -15.787  22.496  1.00 42.79      A    C  
ANISOU  476  CD1 LEU A 300     6236   5827   4193    -47   -126    -69  A    C  
ATOM    477  CD2 LEU A 300     -17.925 -13.502  21.539  1.00 40.26      A    C  
ANISOU  477  CD2 LEU A 300     5908   5514   3873    -19   -124    -67  A    C  
ATOM    478  N   VAL A 301     -13.188 -12.321  21.254  1.00 37.68      A    N  
ANISOU  478  N   VAL A 301     5622   5176   3517    -26   -117    -61  A    N  
ATOM    479  CA  VAL A 301     -11.737 -12.147  21.368  1.00 36.05      A    C  
ANISOU  479  CA  VAL A 301     5412   4971   3311    -33   -116    -57  A    C  
ATOM    480  C   VAL A 301     -11.250 -12.446  22.768  1.00 35.08      A    C  
ANISOU  480  C   VAL A 301     5295   4833   3197    -35   -121    -61  A    C  
ATOM    481  O   VAL A 301     -11.742 -11.830  23.715  1.00 33.93      A    O  
ANISOU  481  O   VAL A 301     5164   4672   3053    -35   -124    -59  A    O  
ATOM    482  CB  VAL A 301     -11.335 -10.685  21.014  1.00 35.63      A    C  
ANISOU  482  CB  VAL A 301     5365   4915   3255    -43   -120    -39  A    C  
ATOM    483  CG1 VAL A 301      -9.834 -10.497  21.138  1.00 35.69      A    C  
ANISOU  483  CG1 VAL A 301     5362   4929   3269    -56   -119    -29  A    C  
ATOM    484  CG2 VAL A 301     -11.792 -10.352  19.600  1.00 35.67      A    C  
ANISOU  484  CG2 VAL A 301     5373   4933   3246    -42   -118    -32  A    C  
ATOM    485  N   LEU A 302     -10.281 -13.358  22.890  1.00 35.17      A    N  
ANISOU  485  N   LEU A 302     5299   4849   3215    -34   -123    -67  A    N  
ATOM    486  CA  LEU A 302      -9.439 -13.501  24.099  1.00 34.49      A    C  
ANISOU  486  CA  LEU A 302     5218   4746   3138    -39   -136    -67  A    C  
ATOM    487  C   LEU A 302      -8.488 -12.306  24.180  1.00 34.42      A    C  
ANISOU  487  C   LEU A 302     5205   4735   3138    -51   -143    -53  A    C  
ATOM    488  O   LEU A 302      -7.363 -12.328  23.670  1.00 34.13      A    O  
ANISOU  488  O   LEU A 302     5143   4714   3110    -55   -142    -47  A    O  
ATOM    489  CB  LEU A 302      -8.647 -14.829  24.110  1.00 34.33      A    C  
ANISOU  489  CB  LEU A 302     5188   4728   3125    -30   -143    -80  A    C  
ATOM    490  CG  LEU A 302      -7.698 -15.040  25.299  1.00 34.42      A    C  
ANISOU  490  CG  LEU A 302     5206   4721   3150    -33   -165    -80  A    C  
ATOM    491  CD1 LEU A 302      -8.455 -14.953  26.603  1.00 34.26      A    C  
ANISOU  491  CD1 LEU A 302     5221   4676   3121    -41   -173    -78  A    C  
ATOM    492  CD2 LEU A 302      -6.971 -16.392  25.281  1.00 34.81      A    C  
ANISOU  492  CD2 LEU A 302     5248   4769   3209    -17   -179    -95  A    C  
ATOM    493  N   ALA A 303      -8.936 -11.266  24.873  1.00 34.05      A    N  
ANISOU  493  N   ALA A 303     5181   4669   3087    -56   -151    -46  A    N  
ATOM    494  CA  ALA A 303      -8.238  -9.970  24.912  1.00 33.54      A    C  
ANISOU  494  CA  ALA A 303     5120   4593   3028    -72   -166    -29  A    C  
ATOM    495  C   ALA A 303      -6.938  -9.863  25.686  1.00 33.74      A    C  
ANISOU  495  C   ALA A 303     5142   4605   3070    -86   -190    -22  A    C  
ATOM    496  O   ALA A 303      -6.126  -8.986  25.412  1.00 32.26      A    O  
ANISOU  496  O   ALA A 303     4945   4417   2895   -106   -203     -3  A    O  
ATOM    497  CB  ALA A 303      -9.212  -8.927  25.430  1.00 33.97      A    C  
ANISOU  497  CB  ALA A 303     5208   4625   3072    -66   -174    -30  A    C  
ATOM    498  N   ASN A 304      -6.705 -10.749  26.652  1.00 36.42      A    N  
ANISOU  498  N   ASN A 304     5490   4933   3414    -79   -201    -34  A    N  
ATOM    499  CA  ASN A 304      -5.601 -10.552  27.609  1.00 37.26      A    C  
ANISOU  499  CA  ASN A 304     5602   5017   3536    -91   -234    -28  A    C  
ATOM    500  C   ASN A 304      -4.331 -11.329  27.386  1.00 40.15      A    C  
ANISOU  500  C   ASN A 304     5927   5399   3927    -93   -242    -27  A    C  
ATOM    501  O   ASN A 304      -3.416 -11.316  28.236  1.00 40.49      A    O  
ANISOU  501  O   ASN A 304     5972   5424   3988   -101   -276    -23  A    O  
ATOM    502  CB  ASN A 304      -6.072 -10.703  29.047  1.00 38.28      A    C  
ANISOU  502  CB  ASN A 304     5779   5114   3649    -84   -251    -39  A    C  
ATOM    503  CG  ASN A 304      -6.525 -12.114  29.418  1.00 37.37      A    C  
ANISOU  503  CG  ASN A 304     5670   5002   3525    -71   -241    -54  A    C  
ATOM    504  ND2 ASN A 304      -6.407 -12.423  30.694  1.00 36.22      A    N  
ANISOU  504  ND2 ASN A 304     5562   4829   3370    -71   -263    -58  A    N  
ATOM    505  OD1 ASN A 304      -6.987 -12.907  28.586  1.00 39.57      A    O  
ANISOU  505  OD1 ASN A 304     5927   5305   3803    -62   -217    -60  A    O  
ATOM    506  N   LEU A 305      -4.243 -11.980  26.233  1.00 41.59      A    N  
ANISOU  506  N   LEU A 305     6073   5617   4111    -82   -214    -31  A    N  
ATOM    507  CA  LEU A 305      -2.973 -12.421  25.727  1.00 41.77      A    C  
ANISOU  507  CA  LEU A 305     6045   5666   4158    -80   -214    -28  A    C  
ATOM    508  C   LEU A 305      -2.181 -11.154  25.486  1.00 44.11      A    C  
ANISOU  508  C   LEU A 305     6319   5969   4470   -111   -222      0  A    C  
ATOM    509  O   LEU A 305      -2.788 -10.103  25.242  1.00 46.17      A    O  
ANISOU  509  O   LEU A 305     6604   6221   4716   -127   -219     13  A    O  
ATOM    510  CB  LEU A 305      -3.188 -13.113  24.414  1.00 41.85      A    C  
ANISOU  510  CB  LEU A 305     6030   5712   4155    -61   -177    -39  A    C  
ATOM    511  CG  LEU A 305      -3.997 -14.398  24.443  1.00 43.10      A    C  
ANISOU  511  CG  LEU A 305     6211   5864   4300    -34   -173    -64  A    C  
ATOM    512  CD1 LEU A 305      -4.416 -14.769  23.025  1.00 45.70      A    C  
ANISOU  512  CD1 LEU A 305     6528   6224   4610    -19   -141    -72  A    C  
ATOM    513  CD2 LEU A 305      -3.143 -15.522  24.997  1.00 44.40      A    C  
ANISOU  513  CD2 LEU A 305     6364   6021   4485    -14   -196    -80  A    C  
ATOM    514  N   LYS A 306      -0.850 -11.248  25.510  1.00 45.86      A    N  
ANISOU  514  N   LYS A 306     6494   6206   4722   -119   -235      9  A    N  
ATOM    515  CA  LYS A 306       0.023 -10.101  25.213  1.00 48.98      A    C  
ANISOU  515  CA  LYS A 306     6858   6612   5137   -157   -243     42  A    C  
ATOM    516  C   LYS A 306       0.244  -9.939  23.723  1.00 48.62      A    C  
ANISOU  516  C   LYS A 306     6769   6619   5083   -163   -197     56  A    C  
ATOM    517  O   LYS A 306       0.262 -10.935  22.978  1.00 46.46      A    O  
ANISOU  517  O   LYS A 306     6470   6381   4800   -132   -162     37  A    O  
ATOM    518  CB  LYS A 306       1.419 -10.244  25.871  1.00 54.22      A    C  
ANISOU  518  CB  LYS A 306     7479   7276   5845   -168   -279     52  A    C  
ATOM    519  CG  LYS A 306       1.443 -10.187  27.397  1.00 55.06      A    C  
ANISOU  519  CG  LYS A 306     7632   7326   5960   -171   -336     45  A    C  
ATOM    520  CD  LYS A 306       2.626  -9.412  27.989  1.00 57.11      A    C  
ANISOU  520  CD  LYS A 306     7868   7570   6260   -208   -386     72  A    C  
ATOM    521  CE  LYS A 306       3.132 -10.044  29.278  1.00 57.26      A    C  
ANISOU  521  CE  LYS A 306     7903   7552   6298   -195   -439     58  A    C  
ATOM    522  NZ  LYS A 306       3.965 -11.250  28.996  1.00 57.68      A    N1+
ANISOU  522  NZ  LYS A 306     7893   7640   6382   -166   -431     44  A    N1+
ATOM    523  N   GLU A 307       0.406  -8.675  23.308  1.00 50.79      A    N  
ANISOU  523  N   GLU A 307     7044   6897   5358   -203   -199     90  A    N  
ATOM    524  CA  GLU A 307       0.775  -8.320  21.942  1.00 53.83      A    C  
ANISOU  524  CA  GLU A 307     7389   7331   5732   -221   -158    114  A    C  
ATOM    525  C   GLU A 307       2.021  -9.111  21.550  1.00 58.22      A    C  
ANISOU  525  C   GLU A 307     7868   7940   6312   -210   -133    113  A    C  
ATOM    526  O   GLU A 307       2.970  -9.242  22.355  1.00 58.42      A    O  
ANISOU  526  O   GLU A 307     7859   7959   6378   -216   -164    117  A    O  
ATOM    527  CB  GLU A 307       1.068  -6.813  21.801  1.00 56.17      A    C  
ANISOU  527  CB  GLU A 307     7692   7614   6034   -278   -179    158  A    C  
ATOM    528  CG  GLU A 307       1.362  -6.392  20.347  1.00 59.34      A    C  
ANISOU  528  CG  GLU A 307     8062   8068   6416   -303   -134    189  A    C  
ATOM    529  CD  GLU A 307       1.165  -4.891  20.043  1.00 61.46      A    C  
ANISOU  529  CD  GLU A 307     8364   8311   6674   -356   -157    231  A    C  
ATOM    530  OE1 GLU A 307       1.924  -4.026  20.563  1.00 60.07      A    O  
ANISOU  530  OE1 GLU A 307     8178   8115   6528   -403   -197    264  A    O  
ATOM    531  OE2 GLU A 307       0.269  -4.567  19.242  1.00 62.42      A    O1-
ANISOU  531  OE2 GLU A 307     8526   8431   6758   -353   -140    232  A    O1-
ATOM    532  N   LYS A 308       1.985  -9.653  20.335  1.00 58.62      A    N  
ANISOU  532  N   LYS A 308     7894   8040   6337   -188    -79    104  A    N  
ATOM    533  CA  LYS A 308       3.096 -10.362  19.693  1.00 62.08      A    C  
ANISOU  533  CA  LYS A 308     8257   8541   6789   -169    -41    100  A    C  
ATOM    534  C   LYS A 308       3.388  -9.740  18.303  1.00 60.40      A    C  
ANISOU  534  C   LYS A 308     8016   8384   6548   -195     10    132  A    C  
ATOM    535  O   LYS A 308       2.584  -8.942  17.813  1.00 56.88      A    O  
ANISOU  535  O   LYS A 308     7619   7923   6069   -221     13    150  A    O  
ATOM    536  CB  LYS A 308       2.726 -11.831  19.551  1.00 64.91      A    C  
ANISOU  536  CB  LYS A 308     8625   8904   7132   -104    -26     51  A    C  
ATOM    537  CG  LYS A 308       3.003 -12.619  20.801  1.00 66.83      A    C  
ANISOU  537  CG  LYS A 308     8869   9112   7411    -79    -71     26  A    C  
ATOM    538  CD  LYS A 308       2.739 -14.091  20.560  1.00 69.56      A    C  
ANISOU  538  CD  LYS A 308     9223   9462   7742    -17    -59    -19  A    C  
ATOM    539  CE  LYS A 308       1.278 -14.417  20.792  1.00 74.93      A    C  
ANISOU  539  CE  LYS A 308     9982  10097   8391     -7    -73    -39  A    C  
ATOM    540  NZ  LYS A 308       1.051 -15.880  20.635  1.00 77.60      A    N1+
ANISOU  540  NZ  LYS A 308    10333  10431   8718     45    -72    -80  A    N1+
ATOM    541  N   SER A 309       4.509 -10.065  17.686  1.00 59.63      A    N  
ANISOU  541  N   SER A 309     7840   8352   6461   -189     52    140  A    N  
ATOM    542  CA  SER A 309       4.804  -9.521  16.374  1.00 61.63      A    C  
ANISOU  542  CA  SER A 309     8065   8666   6681   -216    109    173  A    C  
ATOM    543  C   SER A 309       5.106 -10.635  15.438  1.00 63.57      A    C  
ANISOU  543  C   SER A 309     8278   8976   6899   -158    172    140  A    C  
ATOM    544  O   SER A 309       6.204 -11.066  15.390  1.00 68.06      A    O  
ANISOU  544  O   SER A 309     8766   9601   7492   -143    203    140  A    O  
ATOM    545  CB  SER A 309       6.014  -8.588  16.438  1.00 60.92      A    C  
ANISOU  545  CB  SER A 309     7910   8606   6630   -283    106    230  A    C  
ATOM    546  OG  SER A 309       6.131  -7.710  15.334  1.00 58.06      A    O  
ANISOU  546  OG  SER A 309     7534   8293   6231   -326    155    274  A    O  
ATOM    547  N   LEU A 310       4.152 -11.065  14.635  1.00 65.23      A    N  
ANISOU  547  N   LEU A 310     8551   9176   7057   -122    189    110  A    N  
ATOM    548  CA  LEU A 310       4.374 -12.151  13.698  1.00 67.44      A    C  
ANISOU  548  CA  LEU A 310     8815   9505   7300    -61    241     72  A    C  
ATOM    549  C   LEU A 310       4.618 -11.666  12.314  1.00 67.30      A    C  
ANISOU  549  C   LEU A 310     8779   9557   7235    -84    308    104  A    C  
ATOM    550  O   LEU A 310       3.845 -10.902  11.794  1.00 63.93      A    O  
ANISOU  550  O   LEU A 310     8400   9115   6773   -129    307    136  A    O  
ATOM    551  CB  LEU A 310       3.134 -12.957  13.583  1.00 69.05      A    C  
ANISOU  551  CB  LEU A 310     9099   9665   7470    -16    222     27  A    C  
ATOM    552  CG  LEU A 310       2.728 -13.669  14.824  1.00 76.41      A    C  
ANISOU  552  CG  LEU A 310    10041  10550   8439     26    175    -14  A    C  
ATOM    553  CD1 LEU A 310       1.388 -14.353  14.691  1.00 78.36      A    C  
ANISOU  553  CD1 LEU A 310    10270  10757   8744    -11    124      8  A    C  
ATOM    554  CD2 LEU A 310       3.834 -14.622  15.215  1.00 77.74      A    C  
ANISOU  554  CD2 LEU A 310    10292  10667   8576     49    149    -44  A    C  
ATOM    555  N   ARG A 311       5.771 -12.010  11.773  1.00 67.00      A    N  
ANISOU  555  N   ARG A 311     8669   9593   7195    -50    364     94  A    N  
ATOM    556  CA  ARG A 311       6.169 -11.702  10.409  1.00 65.26      A    C  
ANISOU  556  CA  ARG A 311     8414   9453   6926    -66    440    123  A    C  
ATOM    557  C   ARG A 311       5.949 -10.290   9.993  1.00 61.78      A    C  
ANISOU  557  C   ARG A 311     8004   9007   6461   -151    440    186  A    C  
ATOM    558  O   ARG A 311       5.370 -10.038   9.006  1.00 61.66      A    O  
ANISOU  558  O   ARG A 311     8050   8996   6380   -156    463    191  A    O  
ATOM    559  CB  ARG A 311       5.613 -12.703   9.415  1.00 67.04      A    C  
ANISOU  559  CB  ARG A 311     8685   9705   7081      2    484     75  A    C  
ATOM    560  CG  ARG A 311       6.304 -14.050   9.469  1.00 72.76      A    C  
ANISOU  560  CG  ARG A 311     9368  10455   7823     90    499     15  A    C  
ATOM    561  CD  ARG A 311       5.827 -14.881   8.294  1.00 81.03      A    C  
ANISOU  561  CD  ARG A 311    10455  11540   8793    155    552    -26  A    C  
ATOM    562  NE  ARG A 311       6.343 -16.240   8.079  1.00 85.90      A    N  
ANISOU  562  NE  ARG A 311    11026  12188   9424    244    571    -84  A    N  
ATOM    563  CZ  ARG A 311       5.711 -17.361   8.420  1.00 88.80      A    C  
ANISOU  563  CZ  ARG A 311    11445  12506   9785    315    532   -146  A    C  
ATOM    564  NH1 ARG A 311       4.587 -17.337   9.091  1.00 81.47      A    N1+
ANISOU  564  NH1 ARG A 311    10614  11500   8841    307    475   -160  A    N1+
ATOM    565  NH2 ARG A 311       6.234 -18.516   8.129  1.00 94.83      A    N  
ANISOU  565  NH2 ARG A 311    12164  13302  10565    395    549   -195  A    N  
ATOM    566  N   GLY A 312       6.336  -9.372  10.821  1.00 60.91      A    N  
ANISOU  566  N   GLY A 312     7857   8883   6402   -219    408    236  A    N  
ATOM    567  CA  GLY A 312       6.223  -7.980  10.558  1.00 59.58      A    C  
ANISOU  567  CA  GLY A 312     7722   8702   6213   -302    399    299  A    C  
ATOM    568  C   GLY A 312       4.913  -7.473  11.039  1.00 60.51      A    C  
ANISOU  568  C   GLY A 312     7934   8724   6333   -320    325    296  A    C  
ATOM    569  O   GLY A 312       4.787  -6.330  11.358  1.00 62.52      A    O  
ANISOU  569  O   GLY A 312     8204   8943   6608   -387    284    343  A    O  
ATOM    570  N   ARG A 313       3.980  -8.370  11.284  1.00 62.34      A    N  
ANISOU  570  N   ARG A 313     8226   8913   6547   -261    304    241  A    N  
ATOM    571  CA  ARG A 313       2.657  -7.945  11.730  1.00 66.36      A    C  
ANISOU  571  CA  ARG A 313     8821   9338   7052   -272    242    237  A    C  
ATOM    572  C   ARG A 313       2.256  -8.133  13.193  1.00 63.85      A    C  
ANISOU  572  C   ARG A 313     8517   8955   6786   -253    180    208  A    C  
ATOM    573  O   ARG A 313       2.287  -9.217  13.706  1.00 64.19      A    O  
ANISOU  573  O   ARG A 313     8548   8995   6846   -198    177    161  A    O  
ATOM    574  CB  ARG A 313       1.595  -8.572  10.866  1.00 64.62      A    C  
ANISOU  574  CB  ARG A 313     8671   9108   6771   -234    254    207  A    C  
ATOM    575  CG  ARG A 313       1.662  -8.122   9.441  1.00 67.27      A    C  
ANISOU  575  CG  ARG A 313     9020   9496   7044   -259    305    239  A    C  
ATOM    576  CD  ARG A 313       1.530  -6.626   9.275  1.00 66.13      A    C  
ANISOU  576  CD  ARG A 313     8897   9335   6893   -339    286    304  A    C  
ATOM    577  NE  ARG A 313       1.702  -6.285   7.882  1.00 66.27      A    N  
ANISOU  577  NE  ARG A 313     8941   9398   6839   -357    334    331  A    N  
ATOM    578  CZ  ARG A 313       0.721  -6.016   7.040  1.00 69.28      A    C  
ANISOU  578  CZ  ARG A 313     9403   9754   7166   -344    323    321  A    C  
ATOM    579  NH1 ARG A 313      -0.531  -6.013   7.448  1.00 69.11      A    N1+
ANISOU  579  NH1 ARG A 313     9436   9662   7157   -313    266    286  A    N1+
ATOM    580  NH2 ARG A 313       0.996  -5.729   5.792  1.00 67.39      A    N  
ANISOU  580  NH2 ARG A 313     9188   9560   6857   -362    369    347  A    N  
ATOM    581  N   LYS A 314       1.822  -7.044  13.822  1.00 65.21      A    N  
ANISOU  581  N   LYS A 314     8724   9071   6979   -299    127    236  A    N  
ATOM    582  CA  LYS A 314       1.394  -7.087  15.229  1.00 61.76      A    C  
ANISOU  582  CA  LYS A 314     8311   8570   6584   -288     68    215  A    C  
ATOM    583  C   LYS A 314       0.075  -7.820  15.342  1.00 54.42      A    C  
ANISOU  583  C   LYS A 314     7440   7603   5632   -238     55    169  A    C  
ATOM    584  O   LYS A 314      -0.760  -7.725  14.445  1.00 55.93      A    O  
ANISOU  584  O   LYS A 314     7674   7796   5781   -231     69    167  A    O  
ATOM    585  CB  LYS A 314       1.238  -5.674  15.821  1.00 64.53      A    C  
ANISOU  585  CB  LYS A 314     8694   8869   6952   -345     15    254  A    C  
ATOM    586  CG  LYS A 314       2.502  -4.803  15.831  1.00 67.40      A    C  
ANISOU  586  CG  LYS A 314     9006   9257   7345   -409     12    308  A    C  
ATOM    587  CD  LYS A 314       3.610  -5.367  16.716  1.00 67.87      A    C  
ANISOU  587  CD  LYS A 314     8995   9333   7459   -402      3    300  A    C  
ATOM    588  CE  LYS A 314       4.797  -4.422  16.829  1.00 66.89      A    C  
ANISOU  588  CE  LYS A 314     8818   9226   7372   -472    -11    358  A    C  
ATOM    589  NZ  LYS A 314       5.723  -4.574  15.675  1.00 67.14      A    N1+
ANISOU  589  NZ  LYS A 314     8774   9345   7389   -490     58    386  A    N1+
ATOM    590  N   SER A 315      -0.081  -8.546  16.446  1.00 48.50      A    N  
ANISOU  590  N   SER A 315     6691   6822   4912   -206     27    135  A    N  
ATOM    591  CA  SER A 315      -1.278  -9.322  16.769  1.00 45.81      A    C  
ANISOU  591  CA  SER A 315     6398   6446   4559   -164     12     94  A    C  
ATOM    592  C   SER A 315      -1.574  -9.324  18.307  1.00 44.10      A    C  
ANISOU  592  C   SER A 315     6202   6176   4378   -161    -36     81  A    C  
ATOM    593  O   SER A 315      -0.843  -9.918  19.079  1.00 43.62      A    O  
ANISOU  593  O   SER A 315     6110   6115   4347   -149    -47     69  A    O  
ATOM    594  CB  SER A 315      -1.071 -10.748  16.298  1.00 44.35      A    C  
ANISOU  594  CB  SER A 315     6192   6296   4363   -113     43     57  A    C  
ATOM    595  OG  SER A 315      -2.232 -11.497  16.547  1.00 44.14      A    O  
ANISOU  595  OG  SER A 315     6211   6234   4325    -81     25     23  A    O  
ATOM    596  N   HIS A 316      -2.641  -8.679  18.733  1.00 41.87      A    N  
ANISOU  596  N   HIS A 316     5971   5849   4087   -169    -64     82  A    N  
ATOM    597  CA  HIS A 316      -2.943  -8.484  20.149  1.00 42.15      A    C  
ANISOU  597  CA  HIS A 316     6032   5835   4146   -169   -105     74  A    C  
ATOM    598  C   HIS A 316      -4.297  -9.071  20.519  1.00 41.11      A    C  
ANISOU  598  C   HIS A 316     5941   5677   3999   -136   -111     43  A    C  
ATOM    599  O   HIS A 316      -5.299  -8.391  20.424  1.00 40.11      A    O  
ANISOU  599  O   HIS A 316     5851   5528   3858   -139   -120     46  A    O  
ATOM    600  CB  HIS A 316      -2.931  -6.986  20.462  1.00 43.71      A    C  
ANISOU  600  CB  HIS A 316     6255   6001   4349   -208   -137    105  A    C  
ATOM    601  CG  HIS A 316      -3.134  -6.676  21.903  1.00 48.62      A    C  
ANISOU  601  CG  HIS A 316     6909   6574   4989   -207   -180     96  A    C  
ATOM    602  CD2 HIS A 316      -2.991  -7.448  23.008  1.00 47.04      A    C  
ANISOU  602  CD2 HIS A 316     6710   6358   4805   -187   -195     74  A    C  
ATOM    603  ND1 HIS A 316      -3.558  -5.437  22.349  1.00 52.17      A    N  
ANISOU  603  ND1 HIS A 316     7404   6981   5437   -225   -215    110  A    N  
ATOM    604  CE1 HIS A 316      -3.647  -5.458  23.664  1.00 48.26      A    C  
ANISOU  604  CE1 HIS A 316     6934   6447   4952   -215   -246     95  A    C  
ATOM    605  NE2 HIS A 316      -3.326  -6.668  24.082  1.00 47.69      A    N  
ANISOU  605  NE2 HIS A 316     6837   6391   4889   -194   -234     74  A    N  
ATOM    606  N   GLY A 317      -4.301 -10.329  20.947  1.00 42.02      A    N  
ANISOU  606  N   GLY A 317     6048   5794   4120   -107   -108     15  A    N  
ATOM    607  CA  GLY A 317      -5.523 -11.091  21.238  1.00 44.20      A    C  
ANISOU  607  CA  GLY A 317     6356   6053   4385    -82   -110    -10  A    C  
ATOM    608  C   GLY A 317      -5.682 -12.234  20.225  1.00 45.05      A    C  
ANISOU  608  C   GLY A 317     6453   6188   4475    -56    -86    -29  A    C  
ATOM    609  O   GLY A 317      -4.774 -12.500  19.456  1.00 45.24      A    O  
ANISOU  609  O   GLY A 317     6446   6246   4497    -51    -66    -27  A    O  
ATOM    610  N   MET A 318      -6.813 -12.934  20.229  1.00 45.28      A    N  
ANISOU  610  N   MET A 318     6507   6203   4493    -39    -90    -47  A    N  
ATOM    611  CA  MET A 318      -7.082 -13.955  19.195  1.00 43.44      A    C  
ANISOU  611  CA  MET A 318     6275   5989   4241    -16    -76    -66  A    C  
ATOM    612  C   MET A 318      -8.589 -14.244  19.122  1.00 40.22      A    C  
ANISOU  612  C   MET A 318     5897   5562   3822    -12    -87    -75  A    C  
ATOM    613  O   MET A 318      -9.309 -14.076  20.081  1.00 38.44      A    O  
ANISOU  613  O   MET A 318     5684   5313   3608    -19   -101    -73  A    O  
ATOM    614  CB  MET A 318      -6.261 -15.245  19.415  1.00 45.06      A    C  
ANISOU  614  CB  MET A 318     6464   6200   4456      8    -78    -88  A    C  
ATOM    615  CG  MET A 318      -6.972 -16.334  20.210  1.00 49.60      A    C  
ANISOU  615  CG  MET A 318     7063   6743   5037     19   -102   -107  A    C  
ATOM    616  SD  MET A 318      -5.982 -17.713  20.865  1.00 55.51      A    S  
ANISOU  616  SD  MET A 318     7803   7482   5804     46   -122   -130  A    S  
ATOM    617  CE  MET A 318      -5.577 -18.579  19.341  1.00 56.64      A    C  
ANISOU  617  CE  MET A 318     7938   7655   5925     84   -103   -155  A    C  
ATOM    618  N   VAL A 319      -9.045 -14.715  17.968  1.00 38.54      A    N  
ANISOU  618  N   VAL A 319     5694   5361   3588      0    -81    -84  A    N  
ATOM    619  CA  VAL A 319     -10.458 -14.886  17.702  1.00 37.56      A    C  
ANISOU  619  CA  VAL A 319     5591   5222   3456      0    -95    -88  A    C  
ATOM    620  C   VAL A 319     -10.780 -16.340  17.920  1.00 38.18      A    C  
ANISOU  620  C   VAL A 319     5680   5288   3539     14   -111   -109  A    C  
ATOM    621  O   VAL A 319      -9.984 -17.203  17.540  1.00 37.04      A    O  
ANISOU  621  O   VAL A 319     5534   5152   3387     33   -108   -126  A    O  
ATOM    622  CB  VAL A 319     -10.845 -14.429  16.278  1.00 36.27      A    C  
ANISOU  622  CB  VAL A 319     5440   5072   3265      0    -90    -82  A    C  
ATOM    623  CG1 VAL A 319     -12.294 -14.763  16.005  1.00 36.10      A    C  
ANISOU  623  CG1 VAL A 319     5437   5034   3243      1   -113    -87  A    C  
ATOM    624  CG2 VAL A 319     -10.582 -12.943  16.114  1.00 35.45      A    C  
ANISOU  624  CG2 VAL A 319     5334   4975   3159    -18    -82    -56  A    C  
ATOM    625  N   LEU A 320     -11.927 -16.597  18.564  1.00 39.24      A    N  
ANISOU  625  N   LEU A 320     5822   5401   3684      4   -128   -108  A    N  
ATOM    626  CA  LEU A 320     -12.186 -17.927  19.102  1.00 41.80      A    C  
ANISOU  626  CA  LEU A 320     6157   5706   4016      6   -147   -121  A    C  
ATOM    627  C   LEU A 320     -13.072 -18.684  18.122  1.00 41.74      A    C  
ANISOU  627  C   LEU A 320     6167   5693   3998     10   -167   -131  A    C  
ATOM    628  O   LEU A 320     -13.966 -18.069  17.543  1.00 43.52      A    O  
ANISOU  628  O   LEU A 320     6391   5923   4219      3   -169   -121  A    O  
ATOM    629  CB  LEU A 320     -12.845 -17.871  20.491  1.00 41.26      A    C  
ANISOU  629  CB  LEU A 320     6088   5622   3966    -11   -151   -111  A    C  
ATOM    630  CG  LEU A 320     -12.221 -17.317  21.795  1.00 42.07      A    C  
ANISOU  630  CG  LEU A 320     6189   5716   4079    -17   -147   -106  A    C  
ATOM    631  CD1 LEU A 320     -13.121 -17.242  23.017  1.00 42.72      A    C  
ANISOU  631  CD1 LEU A 320     6267   5800   4164     -3   -149   -115  A    C  
ATOM    632  CD2 LEU A 320     -10.998 -18.091  22.162  1.00 42.60      A    C  
ANISOU  632  CD2 LEU A 320     6250   5788   4148    -25   -133    -92  A    C  
ATOM    633  N   CYS A 321     -12.827 -19.994  17.965  1.00 42.45      A    N  
ANISOU  633  N   CYS A 321     6275   5769   4084     23   -187   -149  A    N  
ATOM    634  CA  CYS A 321     -13.537 -20.842  16.984  1.00 44.30      A    C  
ANISOU  634  CA  CYS A 321     6535   5991   4305     28   -215   -161  A    C  
ATOM    635  C   CYS A 321     -13.823 -22.246  17.462  1.00 45.58      A    C  
ANISOU  635  C   CYS A 321     6720   6121   4477     23   -252   -171  A    C  
ATOM    636  O   CYS A 321     -13.131 -22.794  18.312  1.00 47.05      A    O  
ANISOU  636  O   CYS A 321     6908   6295   4672     28   -255   -176  A    O  
ATOM    637  CB  CYS A 321     -12.713 -21.063  15.715  1.00 44.95      A    C  
ANISOU  637  CB  CYS A 321     6634   6088   4356     61   -208   -182  A    C  
ATOM    638  SG  CYS A 321     -12.073 -19.619  14.878  1.00 45.26      A    S  
ANISOU  638  SG  CYS A 321     6656   6167   4373     67   -166   -171  A    S  
ATOM    639  N   GLY A 322     -14.820 -22.829  16.827  1.00 47.32      A    N  
ANISOU  639  N   GLY A 322     6960   6324   4693     13   -284   -172  A    N  
ATOM    640  CA  GLY A 322     -15.134 -24.226  16.973  1.00 49.57      A    C  
ANISOU  640  CA  GLY A 322     7276   6574   4984      7   -330   -181  A    C  
ATOM    641  C   GLY A 322     -14.492 -24.998  15.842  1.00 51.91      A    C  
ANISOU  641  C   GLY A 322     7611   6859   5251     47   -350   -214  A    C  
ATOM    642  O   GLY A 322     -14.376 -24.493  14.700  1.00 46.57      A    O  
ANISOU  642  O   GLY A 322     6941   6203   4549     67   -337   -224  A    O  
ATOM    643  N   SER A 323     -14.041 -26.205  16.184  1.00 52.28      A    N  
ANISOU  643  N   SER A 323     7688   6875   5301     60   -382   -231  A    N  
ATOM    644  CA  SER A 323     -13.390 -27.077  15.237  1.00 53.92      A    C  
ANISOU  644  CA  SER A 323     7938   7068   5481    106   -405   -269  A    C  
ATOM    645  C   SER A 323     -13.943 -28.482  15.354  1.00 56.35      A    C  
ANISOU  645  C   SER A 323     8295   7320   5795     95   -473   -277  A    C  
ATOM    646  O   SER A 323     -14.037 -29.036  16.464  1.00 55.83      A    O  
ANISOU  646  O   SER A 323     8230   7227   5753     69   -495   -262  A    O  
ATOM    647  CB  SER A 323     -11.897 -27.097  15.502  1.00 53.92      A    C  
ANISOU  647  CB  SER A 323     7924   7085   5476    150   -376   -290  A    C  
ATOM    648  OG  SER A 323     -11.252 -26.140  14.689  1.00 56.59      A    O  
ANISOU  648  OG  SER A 323     8239   7471   5792    175   -325   -296  A    O  
ATOM    649  N   PHE A 324     -14.317 -29.060  14.219  1.00 56.61      A    N  
ANISOU  649  N   PHE A 324     8373   7332   5804    112   -512   -298  A    N  
ATOM    650  CA  PHE A 324     -14.717 -30.487  14.184  1.00 59.74      A    C  
ANISOU  650  CA  PHE A 324     8828   7668   6202    107   -587   -310  A    C  
ATOM    651  C   PHE A 324     -14.322 -31.075  12.840  1.00 59.94      A    C  
ANISOU  651  C   PHE A 324     8910   7677   6184    164   -613   -355  A    C  
ATOM    652  O   PHE A 324     -14.603 -30.475  11.803  1.00 58.11      A    O  
ANISOU  652  O   PHE A 324     8682   7470   5926    173   -597   -360  A    O  
ATOM    653  CB  PHE A 324     -16.231 -30.669  14.421  1.00 58.79      A    C  
ANISOU  653  CB  PHE A 324     8707   7522   6108     39   -630   -273  A    C  
ATOM    654  CG  PHE A 324     -16.677 -32.115  14.477  1.00 59.49      A    C  
ANISOU  654  CG  PHE A 324     8855   7544   6202     21   -714   -278  A    C  
ATOM    655  CD1 PHE A 324     -16.486 -32.877  15.633  1.00 58.87      A    C  
ANISOU  655  CD1 PHE A 324     8787   7433   6146      0   -738   -265  A    C  
ATOM    656  CD2 PHE A 324     -17.311 -32.712  13.380  1.00 59.89      A    C  
ANISOU  656  CD2 PHE A 324     8959   7560   6237     23   -775   -292  A    C  
ATOM    657  CE1 PHE A 324     -16.910 -34.191  15.692  1.00 60.38      A    C  
ANISOU  657  CE1 PHE A 324     9037   7558   6343    -23   -821   -265  A    C  
ATOM    658  CE2 PHE A 324     -17.731 -34.035  13.432  1.00 58.42      A    C  
ANISOU  658  CE2 PHE A 324     8831   7305   6057      2   -861   -295  A    C  
ATOM    659  CZ  PHE A 324     -17.533 -34.776  14.578  1.00 59.56      A    C  
ANISOU  659  CZ  PHE A 324     8985   7418   6225    -21   -884   -280  A    C  
ATOM    660  N   GLY A 325     -13.673 -32.241  12.876  1.00 63.31      A    N  
ANISOU  660  N   GLY A 325     9386   8064   6602    203   -654   -389  A    N  
ATOM    661  CA  GLY A 325     -13.134 -32.875  11.685  1.00 64.88      A    C  
ANISOU  661  CA  GLY A 325     9645   8249   6756    271   -676   -440  A    C  
ATOM    662  C   GLY A 325     -12.259 -31.871  10.969  1.00 65.10      A    C  
ANISOU  662  C   GLY A 325     9638   8346   6752    317   -595   -456  A    C  
ATOM    663  O   GLY A 325     -11.279 -31.411  11.516  1.00 69.04      A    O  
ANISOU  663  O   GLY A 325    10087   8882   7261    338   -541   -457  A    O  
ATOM    664  N   GLU A 326     -12.640 -31.491   9.764  1.00 65.43      A    N  
ANISOU  664  N   GLU A 326     9704   8403   6753    328   -589   -465  A    N  
ATOM    665  CA  GLU A 326     -11.847 -30.547   8.978  1.00 67.20      A    C  
ANISOU  665  CA  GLU A 326     9901   8692   6939    366   -513   -476  A    C  
ATOM    666  C   GLU A 326     -12.478 -29.143   8.965  1.00 62.28      A    C  
ANISOU  666  C   GLU A 326     9227   8108   6325    313   -472   -430  A    C  
ATOM    667  O   GLU A 326     -11.842 -28.184   8.531  1.00 60.89      A    O  
ANISOU  667  O   GLU A 326     9019   7987   6126    329   -406   -427  A    O  
ATOM    668  CB  GLU A 326     -11.638 -31.120   7.566  1.00 67.24      A    C  
ANISOU  668  CB  GLU A 326     9980   8689   6880    427   -530   -523  A    C  
ATOM    669  CG  GLU A 326     -11.167 -32.578   7.623  1.00 70.42      A    C  
ANISOU  669  CG  GLU A 326    10441   9040   7275    481   -586   -571  A    C  
ATOM    670  CD  GLU A 326     -11.176 -33.306   6.286  1.00 76.52      A    C  
ANISOU  670  CD  GLU A 326    11303   9787   7982    540   -622   -620  A    C  
ATOM    671  OE1 GLU A 326     -11.879 -32.849   5.336  1.00 76.45      A    O  
ANISOU  671  OE1 GLU A 326    11324   9784   7937    523   -627   -612  A    O  
ATOM    672  OE2 GLU A 326     -10.489 -34.362   6.192  1.00 77.53      A    O1-
ANISOU  672  OE2 GLU A 326    11476   9885   8093    606   -650   -670  A    O1-
ATOM    673  N   GLN A 327     -13.703 -29.026   9.482  1.00 61.08      A    N  
ANISOU  673  N   GLN A 327     9066   7929   6211    250   -510   -395  A    N  
ATOM    674  CA  GLN A 327     -14.421 -27.732   9.556  1.00 59.20      A    C  
ANISOU  674  CA  GLN A 327     8781   7722   5989    203   -481   -353  A    C  
ATOM    675  C   GLN A 327     -13.926 -26.867  10.712  1.00 58.87      A    C  
ANISOU  675  C   GLN A 327     8669   7716   5983    183   -425   -326  A    C  
ATOM    676  O   GLN A 327     -13.633 -27.385  11.819  1.00 57.48      A    O  
ANISOU  676  O   GLN A 327     8478   7523   5839    175   -432   -324  A    O  
ATOM    677  CB  GLN A 327     -15.921 -27.943   9.774  1.00 59.48      A    C  
ANISOU  677  CB  GLN A 327     8821   7720   6057    146   -540   -325  A    C  
ATOM    678  CG  GLN A 327     -16.669 -28.690   8.675  1.00 61.61      A    C  
ANISOU  678  CG  GLN A 327     9159   7947   6300    150   -610   -343  A    C  
ATOM    679  CD  GLN A 327     -18.081 -29.080   9.098  1.00 60.70      A    C  
ANISOU  679  CD  GLN A 327     9039   7793   6230     88   -675   -311  A    C  
ATOM    680  NE2 GLN A 327     -18.226 -30.289   9.637  1.00 62.48      A    N  
ANISOU  680  NE2 GLN A 327     9292   7970   6475     75   -730   -316  A    N  
ATOM    681  OE1 GLN A 327     -19.023 -28.310   8.947  1.00 57.35      A    O  
ANISOU  681  OE1 GLN A 327     8583   7382   5824     52   -678   -282  A    O  
ATOM    682  N   ILE A 328     -13.855 -25.554  10.483  1.00 55.09      A    N  
ANISOU  682  N   ILE A 328     8153   7280   5498    172   -375   -305  A    N  
ATOM    683  CA  ILE A 328     -13.670 -24.622  11.602  1.00 55.03      A    C  
ANISOU  683  CA  ILE A 328     8084   7297   5526    144   -334   -275  A    C  
ATOM    684  C   ILE A 328     -14.641 -23.464  11.424  1.00 53.78      A    C  
ANISOU  684  C   ILE A 328     7904   7152   5377    108   -328   -243  A    C  
ATOM    685  O   ILE A 328     -14.721 -22.916  10.340  1.00 62.92      A    O  
ANISOU  685  O   ILE A 328     9080   8325   6501    117   -320   -244  A    O  
ATOM    686  CB  ILE A 328     -12.194 -24.161  11.738  1.00 56.37      A    C  
ANISOU  686  CB  ILE A 328     8225   7507   5686    175   -277   -284  A    C  
ATOM    687  CG1 ILE A 328     -11.968 -23.284  12.994  1.00 55.91      A    C  
ANISOU  687  CG1 ILE A 328     8111   7464   5666    145   -246   -255  A    C  
ATOM    688  CG2 ILE A 328     -11.723 -23.446  10.478  1.00 59.72      A    C  
ANISOU  688  CG2 ILE A 328     8657   7971   6063    197   -239   -289  A    C  
ATOM    689  CD1 ILE A 328     -10.544 -22.773  13.137  1.00 55.25      A    C  
ANISOU  689  CD1 ILE A 328     7994   7419   5578    168   -197   -258  A    C  
ATOM    690  N   GLU A 329     -15.418 -23.123  12.447  1.00 48.75      A    N  
ANISOU  690  N   GLU A 329     7233   6507   4781     69   -333   -216  A    N  
ATOM    691  CA  GLU A 329     -16.326 -21.978  12.378  1.00 46.34      A    C  
ANISOU  691  CA  GLU A 329     6901   6215   4489     42   -327   -189  A    C  
ATOM    692  C   GLU A 329     -16.078 -21.032  13.544  1.00 46.22      A    C  
ANISOU  692  C   GLU A 329     6839   6220   4502     27   -287   -168  A    C  
ATOM    693  O   GLU A 329     -15.551 -21.439  14.586  1.00 49.76      A    O  
ANISOU  693  O   GLU A 329     7274   6663   4966     25   -276   -169  A    O  
ATOM    694  CB  GLU A 329     -17.797 -22.406  12.408  1.00 46.17      A    C  
ANISOU  694  CB  GLU A 329     6880   6166   4493     11   -377   -176  A    C  
ATOM    695  CG  GLU A 329     -18.231 -23.421  11.356  1.00 48.02      A    C  
ANISOU  695  CG  GLU A 329     7168   6370   4707     19   -433   -194  A    C  
ATOM    696  CD  GLU A 329     -18.193 -22.881   9.905  1.00 49.52      A    C  
ANISOU  696  CD  GLU A 329     7392   6570   4853     40   -437   -204  A    C  
ATOM    697  OE1 GLU A 329     -18.422 -21.659   9.678  1.00 48.78      A    O  
ANISOU  697  OE1 GLU A 329     7276   6499   4759     34   -414   -185  A    O  
ATOM    698  OE2 GLU A 329     -17.946 -23.702   8.986  1.00 49.40      A    O1-
ANISOU  698  OE2 GLU A 329     7432   6536   4801     65   -466   -230  A    O1-
ATOM    699  N   LEU A 330     -16.445 -19.770  13.369  1.00 43.10      A    N  
ANISOU  699  N   LEU A 330     6424   5842   4108     18   -270   -149  A    N  
ATOM    700  CA  LEU A 330     -16.331 -18.801  14.435  1.00 42.45      A    C  
ANISOU  700  CA  LEU A 330     6305   5772   4049      6   -239   -131  A    C  
ATOM    701  C   LEU A 330     -17.376 -19.076  15.508  1.00 41.32      A    C  
ANISOU  701  C   LEU A 330     6139   5616   3942    -18   -253   -119  A    C  
ATOM    702  O   LEU A 330     -18.467 -19.556  15.208  1.00 41.56      A    O  
ANISOU  702  O   LEU A 330     6171   5635   3985    -31   -286   -115  A    O  
ATOM    703  CB  LEU A 330     -16.646 -17.404  13.910  1.00 42.33      A    C  
ANISOU  703  CB  LEU A 330     6282   5770   4028      3   -229   -115  A    C  
ATOM    704  CG  LEU A 330     -15.817 -16.751  12.870  1.00 40.80      A    C  
ANISOU  704  CG  LEU A 330     6109   5595   3799     16   -211   -115  A    C  
ATOM    705  CD1 LEU A 330     -16.546 -15.486  12.506  1.00 42.65      A    C  
ANISOU  705  CD1 LEU A 330     6340   5829   4035      7   -219    -96  A    C  
ATOM    706  CD2 LEU A 330     -14.484 -16.392  13.416  1.00 40.22      A    C  
ANISOU  706  CD2 LEU A 330     6019   5539   3722     20   -172   -113  A    C  
ATOM    707  N   LEU A 331     -17.063 -18.707  16.746  1.00 41.49      A    N  
ANISOU  707  N   LEU A 331     6139   5644   3981    -24   -227   -110  A    N  
ATOM    708  CA  LEU A 331     -18.086 -18.663  17.833  1.00 40.80      A    C  
ANISOU  708  CA  LEU A 331     6025   5555   3922    -46   -226    -95  A    C  
ATOM    709  C   LEU A 331     -18.800 -17.368  17.610  1.00 39.01      A    C  
ANISOU  709  C   LEU A 331     5777   5341   3703    -43   -218    -84  A    C  
ATOM    710  O   LEU A 331     -18.183 -16.409  17.174  1.00 42.49      A    O  
ANISOU  710  O   LEU A 331     6224   5789   4128    -29   -205    -84  A    O  
ATOM    711  CB  LEU A 331     -17.455 -18.714  19.229  1.00 40.22      A    C  
ANISOU  711  CB  LEU A 331     5946   5481   3854    -51   -203    -92  A    C  
ATOM    712  CG  LEU A 331     -16.534 -19.914  19.495  1.00 40.81      A    C  
ANISOU  712  CG  LEU A 331     6044   5538   3922    -48   -215   -105  A    C  
ATOM    713  CD1 LEU A 331     -15.946 -19.837  20.892  1.00 39.95      A    C  
ANISOU  713  CD1 LEU A 331     5932   5426   3818    -54   -197   -100  A    C  
ATOM    714  CD2 LEU A 331     -17.244 -21.267  19.255  1.00 41.59      A    C  
ANISOU  714  CD2 LEU A 331     6160   5616   4026    -65   -253   -106  A    C  
ATOM    715  N   ALA A 332     -20.100 -17.361  17.808  1.00 37.78      A    N  
ANISOU  715  N   ALA A 332     5596   5188   3571    -56   -230    -73  A    N  
ATOM    716  CA  ALA A 332     -20.906 -16.195  17.494  1.00 38.65      A    C  
ANISOU  716  CA  ALA A 332     5684   5307   3691    -46   -231    -66  A    C  
ATOM    717  C   ALA A 332     -21.784 -15.776  18.694  1.00 39.07      A    C  
ANISOU  717  C   ALA A 332     5698   5374   3771    -50   -210    -56  A    C  
ATOM    718  O   ALA A 332     -22.450 -16.640  19.318  1.00 38.22      A    O  
ANISOU  718  O   ALA A 332     5569   5271   3680    -71   -210    -47  A    O  
ATOM    719  CB  ALA A 332     -21.788 -16.478  16.269  1.00 38.88      A    C  
ANISOU  719  CB  ALA A 332     5716   5329   3726    -50   -273    -64  A    C  
ATOM    720  N   PRO A 333     -21.787 -14.463  19.012  1.00 39.75      A    N  
ANISOU  720  N   PRO A 333     5776   5467   3857    -29   -191    -56  A    N  
ATOM    721  CA  PRO A 333     -22.733 -13.900  19.978  1.00 41.64      A    C  
ANISOU  721  CA  PRO A 333     5979   5723   4118    -20   -171    -52  A    C  
ATOM    722  C   PRO A 333     -23.999 -13.641  19.297  1.00 42.82      A    C  
ANISOU  722  C   PRO A 333     6096   5880   4294    -14   -195    -47  A    C  
ATOM    723  O   PRO A 333     -23.953 -13.222  18.193  1.00 48.26      A    O  
ANISOU  723  O   PRO A 333     6801   6557   4977     -5   -224    -49  A    O  
ATOM    724  CB  PRO A 333     -22.130 -12.534  20.337  1.00 41.31      A    C  
ANISOU  724  CB  PRO A 333     5955   5675   4063      5   -154    -58  A    C  
ATOM    725  CG  PRO A 333     -21.250 -12.198  19.184  1.00 40.96      A    C  
ANISOU  725  CG  PRO A 333     5946   5616   4000      6   -175    -59  A    C  
ATOM    726  CD  PRO A 333     -20.696 -13.520  18.720  1.00 39.88      A    C  
ANISOU  726  CD  PRO A 333     5823   5477   3852    -13   -183    -61  A    C  
ATOM    727  N   PRO A 334     -25.142 -13.872  19.946  1.00 45.89      A    N  
ANISOU  727  N   PRO A 334     6435   6290   4710    -20   -184    -39  A    N  
ATOM    728  CA  PRO A 334     -26.357 -13.412  19.294  1.00 46.95      A    C  
ANISOU  728  CA  PRO A 334     6529   6432   4874     -7   -211    -36  A    C  
ATOM    729  C   PRO A 334     -26.272 -11.928  19.016  1.00 47.37      A    C  
ANISOU  729  C   PRO A 334     6596   6478   4924     33   -215    -46  A    C  
ATOM    730  O   PRO A 334     -25.444 -11.233  19.574  1.00 50.31      A    O  
ANISOU  730  O   PRO A 334     6997   6842   5273     49   -191    -55  A    O  
ATOM    731  CB  PRO A 334     -27.443 -13.706  20.317  1.00 48.02      A    C  
ANISOU  731  CB  PRO A 334     6604   6603   5039    -14   -182    -26  A    C  
ATOM    732  CG  PRO A 334     -26.876 -14.809  21.141  1.00 49.24      A    C  
ANISOU  732  CG  PRO A 334     6775   6758   5177    -49   -158    -17  A    C  
ATOM    733  CD  PRO A 334     -25.412 -14.525  21.235  1.00 46.51      A    C  
ANISOU  733  CD  PRO A 334     6490   6388   4793    -38   -149    -31  A    C  
ATOM    734  N   ASP A 335     -27.104 -11.441  18.129  1.00 49.21      A    N  
ANISOU  734  N   ASP A 335     6810   6707   5179     49   -253    -45  A    N  
ATOM    735  CA  ASP A 335     -26.959 -10.065  17.686  1.00 50.48      A    C  
ANISOU  735  CA  ASP A 335     6995   6850   5333     84   -270    -54  A    C  
ATOM    736  C   ASP A 335     -27.387  -9.193  18.842  1.00 48.82      A    C  
ANISOU  736  C   ASP A 335     6757   6656   5135    120   -236    -64  A    C  
ATOM    737  O   ASP A 335     -28.054  -9.688  19.740  1.00 50.73      A    O  
ANISOU  737  O   ASP A 335     6950   6929   5396    117   -203    -63  A    O  
ATOM    738  CB  ASP A 335     -27.786  -9.814  16.416  1.00 51.44      A    C  
ANISOU  738  CB  ASP A 335     7108   6960   5474     92   -327    -50  A    C  
ATOM    739  CG  ASP A 335     -27.276 -10.613  15.212  1.00 50.57      A    C  
ANISOU  739  CG  ASP A 335     7042   6831   5341     61   -362    -43  A    C  
ATOM    740  OD1 ASP A 335     -26.074 -10.490  14.883  1.00 45.07      A    O  
ANISOU  740  OD1 ASP A 335     6400   6119   4603     54   -353    -44  A    O  
ATOM    741  OD2 ASP A 335     -28.099 -11.341  14.598  1.00 51.65      A    O1-
ANISOU  741  OD2 ASP A 335     7155   6968   5499     45   -399    -36  A    O1-
ATOM    742  N   GLY A 336     -26.954  -7.933  18.845  1.00 48.60      A    N  
ANISOU  742  N   GLY A 336     6764   6606   5093    152   -242    -74  A    N  
ATOM    743  CA  GLY A 336     -27.330  -6.950  19.895  1.00 48.97      A    C  
ANISOU  743  CA  GLY A 336     6798   6661   5147    197   -216    -90  A    C  
ATOM    744  C   GLY A 336     -26.282  -6.725  20.973  1.00 47.60      A    C  
ANISOU  744  C   GLY A 336     6664   6480   4940    196   -179    -97  A    C  
ATOM    745  O   GLY A 336     -26.394  -5.840  21.803  1.00 50.39      A    O  
ANISOU  745  O   GLY A 336     7024   6830   5288    234   -163   -112  A    O  
ATOM    746  N   VAL A 337     -25.250  -7.543  20.947  1.00 45.72      A    N  
ANISOU  746  N   VAL A 337     6454   6237   4679    155   -169    -87  A    N  
ATOM    747  CA  VAL A 337     -24.148  -7.441  21.866  1.00 42.69      A    C  
ANISOU  747  CA  VAL A 337     6110   5844   4267    148   -142    -91  A    C  
ATOM    748  C   VAL A 337     -23.334  -6.170  21.607  1.00 42.91      A    C  
ANISOU  748  C   VAL A 337     6190   5836   4278    163   -167    -94  A    C  
ATOM    749  O   VAL A 337     -23.425  -5.592  20.560  1.00 43.56      A    O  
ANISOU  749  O   VAL A 337     6285   5899   4364    168   -204    -88  A    O  
ATOM    750  CB  VAL A 337     -23.291  -8.684  21.712  1.00 41.56      A    C  
ANISOU  750  CB  VAL A 337     5977   5703   4109    103   -135    -79  A    C  
ATOM    751  CG1 VAL A 337     -24.101  -9.905  22.185  1.00 41.33      A    C  
ANISOU  751  CG1 VAL A 337     5904   5704   4096     84   -113    -74  A    C  
ATOM    752  CG2 VAL A 337     -22.831  -8.848  20.248  1.00 41.76      A    C  
ANISOU  752  CG2 VAL A 337     6024   5713   4130     84   -171    -70  A    C  
ATOM    753  N   ASN A 338     -22.588  -5.706  22.593  1.00 43.34      A    N  
ANISOU  753  N   ASN A 338     6276   5876   4312    170   -151   -101  A    N  
ATOM    754  CA  ASN A 338     -21.803  -4.503  22.467  1.00 43.94      A    C  
ANISOU  754  CA  ASN A 338     6404   5915   4374    178   -179   -101  A    C  
ATOM    755  C   ASN A 338     -20.361  -4.887  22.411  1.00 42.59      A    C  
ANISOU  755  C   ASN A 338     6263   5734   4184    137   -177    -87  A    C  
ATOM    756  O   ASN A 338     -19.960  -5.834  23.039  1.00 40.31      A    O  
ANISOU  756  O   ASN A 338     5964   5461   3889    118   -150    -87  A    O  
ATOM    757  CB  ASN A 338     -21.977  -3.608  23.685  1.00 46.27      A    C  
ANISOU  757  CB  ASN A 338     6720   6197   4662    218   -169   -121  A    C  
ATOM    758  CG  ASN A 338     -23.377  -3.101  23.820  1.00 49.70      A    C  
ANISOU  758  CG  ASN A 338     7123   6644   5116    269   -168   -139  A    C  
ATOM    759  ND2 ASN A 338     -23.906  -2.581  22.724  1.00 49.59      A    N  
ANISOU  759  ND2 ASN A 338     7102   6618   5120    282   -207   -135  A    N  
ATOM    760  OD1 ASN A 338     -23.981  -3.150  24.907  1.00 54.69      A    O  
ANISOU  760  OD1 ASN A 338     7736   7297   5745    300   -132   -157  A    O  
ATOM    761  N   VAL A 339     -19.591  -4.122  21.663  1.00 42.36      A    N  
ANISOU  761  N   VAL A 339     6267   5679   4146    123   -207    -74  A    N  
ATOM    762  CA  VAL A 339     -18.182  -4.289  21.603  1.00 42.77      A    C  
ANISOU  762  CA  VAL A 339     6342   5724   4184     87   -206    -59  A    C  
ATOM    763  C   VAL A 339     -17.745  -4.056  23.014  1.00 44.15      A    C  
ANISOU  763  C   VAL A 339     6535   5886   4352     95   -195    -70  A    C  
ATOM    764  O   VAL A 339     -18.189  -3.102  23.640  1.00 47.50      A    O  
ANISOU  764  O   VAL A 339     6982   6289   4775    127   -207    -83  A    O  
ATOM    765  CB  VAL A 339     -17.477  -3.242  20.657  1.00 43.52      A    C  
ANISOU  765  CB  VAL A 339     6472   5792   4269     69   -242    -38  A    C  
ATOM    766  CG1 VAL A 339     -17.690  -3.611  19.185  1.00 45.26      A    C  
ANISOU  766  CG1 VAL A 339     6683   6027   4486     54   -250    -25  A    C  
ATOM    767  CG2 VAL A 339     -17.920  -1.798  20.910  1.00 42.76      A    C  
ANISOU  767  CG2 VAL A 339     6411   5657   4176     98   -277    -44  A    C  
ATOM    768  N   GLY A 340     -16.894  -4.922  23.524  1.00 43.83      A    N  
ANISOU  768  N   GLY A 340     6490   5856   4305     71   -176    -67  A    N  
ATOM    769  CA  GLY A 340     -16.317  -4.697  24.822  1.00 42.67      A    C  
ANISOU  769  CA  GLY A 340     6370   5693   4149     73   -174    -74  A    C  
ATOM    770  C   GLY A 340     -16.980  -5.532  25.900  1.00 42.29      A    C  
ANISOU  770  C   GLY A 340     6306   5664   4095     88   -140    -90  A    C  
ATOM    771  O   GLY A 340     -16.389  -5.696  26.901  1.00 41.84      A    O  
ANISOU  771  O   GLY A 340     6271   5599   4027     83   -136    -94  A    O  
ATOM    772  N   GLU A 341     -18.185  -6.079  25.734  1.00 40.18      A    N  
ANISOU  772  N   GLU A 341     6003   5425   3837    103   -119    -97  A    N  
ATOM    773  CA  GLU A 341     -18.727  -6.857  26.857  1.00 38.18      A    C  
ANISOU  773  CA  GLU A 341     5738   5193   3576    110    -84   -106  A    C  
ATOM    774  C   GLU A 341     -18.050  -8.212  27.125  1.00 38.00      A    C  
ANISOU  774  C   GLU A 341     5710   5180   3548     74    -72    -96  A    C  
ATOM    775  O   GLU A 341     -17.752  -9.028  26.217  1.00 38.77      A    O  
ANISOU  775  O   GLU A 341     5788   5286   3657     50    -79    -86  A    O  
ATOM    776  CB  GLU A 341     -20.215  -7.047  26.731  1.00 39.67      A    C  
ANISOU  776  CB  GLU A 341     5883   5411   3777    132    -63   -112  A    C  
ATOM    777  CG  GLU A 341     -20.602  -8.149  25.786  1.00 42.50      A    C  
ANISOU  777  CG  GLU A 341     6200   5792   4154    105    -62    -99  A    C  
ATOM    778  CD  GLU A 341     -22.076  -8.358  25.719  1.00 44.72      A    C  
ANISOU  778  CD  GLU A 341     6432   6104   4454    122    -46   -101  A    C  
ATOM    779  OE1 GLU A 341     -22.767  -7.518  25.096  1.00 44.49      A    O  
ANISOU  779  OE1 GLU A 341     6390   6073   4441    150    -63   -107  A    O  
ATOM    780  OE2 GLU A 341     -22.517  -9.371  26.323  1.00 49.70      A    O1-
ANISOU  780  OE2 GLU A 341     7038   6759   5084    104    -18    -95  A    O1-
ATOM    781  N   ARG A 342     -17.829  -8.472  28.406  1.00 38.25      A    N  
ANISOU  781  N   ARG A 342     5763   5208   3561     74    -57   -101  A    N  
ATOM    782  CA  ARG A 342     -17.095  -9.662  28.863  1.00 36.60      A    C  
ANISOU  782  CA  ARG A 342     5561   4999   3345     43    -54    -93  A    C  
ATOM    783  C   ARG A 342     -18.079 -10.827  28.792  1.00 36.23      A    C  
ANISOU  783  C   ARG A 342     5477   4982   3304     31    -30    -87  A    C  
ATOM    784  O   ARG A 342     -19.211 -10.695  29.251  1.00 33.77      A    O  
ANISOU  784  O   ARG A 342     5148   4692   2988     47     -3    -91  A    O  
ATOM    785  CB  ARG A 342     -16.533  -9.413  30.289  1.00 36.90      A    C  
ANISOU  785  CB  ARG A 342     5646   5018   3357     48    -53   -100  A    C  
ATOM    786  CG  ARG A 342     -15.306 -10.240  30.637  1.00 36.94      A    C  
ANISOU  786  CG  ARG A 342     5669   5007   3359     19    -72    -92  A    C  
ATOM    787  CD  ARG A 342     -15.153 -10.503  32.113  1.00 37.53      A    C  
ANISOU  787  CD  ARG A 342     5785   5070   3404     18    -66    -95  A    C  
ATOM    788  NE  ARG A 342     -14.414 -11.743  32.352  1.00 37.77      A    N  
ANISOU  788  NE  ARG A 342     5820   5094   3436     -9    -78    -86  A    N  
ATOM    789  CZ  ARG A 342     -13.958 -12.145  33.541  1.00 36.77      A    C  
ANISOU  789  CZ  ARG A 342     5734   4949   3285    -18    -86    -85  A    C  
ATOM    790  NH1 ARG A 342     -14.179 -11.391  34.630  1.00 36.43      A    N1+
ANISOU  790  NH1 ARG A 342     5735   4895   3210      0    -79    -94  A    N1+
ATOM    791  NH2 ARG A 342     -13.271 -13.294  33.634  1.00 35.34      A    N  
ANISOU  791  NH2 ARG A 342     5556   4758   3110    -41   -106    -76  A    N  
ATOM    792  N   ILE A 343     -17.666 -11.918  28.135  1.00 36.98      A    N  
ANISOU  792  N   ILE A 343     5560   5080   3411      4    -42    -78  A    N  
ATOM    793  CA  ILE A 343     -18.470 -13.126  28.005  1.00 38.72      A    C  
ANISOU  793  CA  ILE A 343     5752   5320   3639    -15    -31    -69  A    C  
ATOM    794  C   ILE A 343     -18.082 -14.061  29.152  1.00 42.22      A    C  
ANISOU  794  C   ILE A 343     6221   5756   4064    -36    -24    -63  A    C  
ATOM    795  O   ILE A 343     -16.881 -14.363  29.361  1.00 40.71      A    O  
ANISOU  795  O   ILE A 343     6059   5541   3867    -44    -45    -64  A    O  
ATOM    796  CB  ILE A 343     -18.153 -13.833  26.679  1.00 40.75      A    C  
ANISOU  796  CB  ILE A 343     5995   5574   3913    -29    -56    -65  A    C  
ATOM    797  CG1 ILE A 343     -18.405 -12.905  25.445  1.00 40.63      A    C  
ANISOU  797  CG1 ILE A 343     5965   5562   3910    -12    -68    -69  A    C  
ATOM    798  CG2 ILE A 343     -18.869 -15.170  26.580  1.00 40.06      A    C  
ANISOU  798  CG2 ILE A 343     5889   5497   3834    -54    -56    -55  A    C  
ATOM    799  CD1 ILE A 343     -19.787 -12.274  25.379  1.00 41.49      A    C  
ANISOU  799  CD1 ILE A 343     6044   5688   4030      6    -56    -69  A    C  
ATOM    800  N   ILE A 344     -19.087 -14.507  29.904  1.00 45.67      A    N  
ANISOU  800  N   ILE A 344     6647   6214   4492    -46      2    -54  A    N  
ATOM    801  CA  ILE A 344     -18.890 -15.173  31.195  1.00 50.98      A    C  
ANISOU  801  CA  ILE A 344     7350   6880   5137    -65     14    -46  A    C  
ATOM    802  C   ILE A 344     -19.646 -16.485  31.184  1.00 53.61      A    C  
ANISOU  802  C   ILE A 344     7662   7228   5477   -102     19    -25  A    C  
ATOM    803  O   ILE A 344     -20.566 -16.625  30.409  1.00 64.36      A    O  
ANISOU  803  O   ILE A 344     8980   8612   6862   -106     23    -19  A    O  
ATOM    804  CB  ILE A 344     -19.435 -14.310  32.373  1.00 54.70      A    C  
ANISOU  804  CB  ILE A 344     7837   7367   5579    -42     52    -52  A    C  
ATOM    805  CG1 ILE A 344     -20.966 -14.174  32.324  1.00 57.08      A    C  
ANISOU  805  CG1 ILE A 344     8087   7712   5888    -34     92    -47  A    C  
ATOM    806  CG2 ILE A 344     -18.819 -12.916  32.384  1.00 54.44      A    C  
ANISOU  806  CG2 ILE A 344     7830   7314   5540     -5     40    -72  A    C  
ATOM    807  CD1 ILE A 344     -21.588 -13.622  33.607  1.00 58.30      A    C  
ANISOU  807  CD1 ILE A 344     8254   7889   6006    -13    139    -52  A    C  
ATOM    808  N   CYS A 345     -19.292 -17.431  32.040  1.00 54.59      A    N  
ANISOU  808  N   CYS A 345     7820   7339   5581   -130     14    -13  A    N  
ATOM    809  CA  CYS A 345     -20.084 -18.659  32.185  1.00 58.22      A    C  
ANISOU  809  CA  CYS A 345     8266   7811   6044   -172     18     11  A    C  
ATOM    810  C   CYS A 345     -21.277 -18.502  33.119  1.00 58.22      A    C  
ANISOU  810  C   CYS A 345     8245   7850   6024   -182     71     28  A    C  
ATOM    811  O   CYS A 345     -21.457 -17.455  33.754  1.00 58.46      A    O  
ANISOU  811  O   CYS A 345     8280   7897   6033   -150    105     15  A    O  
ATOM    812  CB  CYS A 345     -19.204 -19.797  32.698  1.00 59.87      A    C  
ANISOU  812  CB  CYS A 345     8524   7983   6238   -201    -15     21  A    C  
ATOM    813  SG  CYS A 345     -17.829 -20.070  31.596  1.00 67.17      A    S  
ANISOU  813  SG  CYS A 345     9463   8870   7188   -183    -70      0  A    S  
ATOM    814  N   GLU A 346     -22.029 -19.571  33.276  1.00 59.90      A    N  
ANISOU  814  N   GLU A 346     8437   8079   6244   -228     76     56  A    N  
ATOM    815  CA  GLU A 346     -23.150 -19.584  34.185  1.00 58.66      A    C  
ANISOU  815  CA  GLU A 346     8257   7966   6065   -247    131     79  A    C  
ATOM    816  C   GLU A 346     -22.557 -19.800  35.570  1.00 60.46      A    C  
ANISOU  816  C   GLU A 346     8553   8177   6240   -259    142     86  A    C  
ATOM    817  O   GLU A 346     -21.645 -20.576  35.756  1.00 54.47      A    O  
ANISOU  817  O   GLU A 346     7849   7373   5473   -279     97     89  A    O  
ATOM    818  CB  GLU A 346     -24.184 -20.665  33.838  1.00 61.49      A    C  
ANISOU  818  CB  GLU A 346     8564   8349   6450   -300    132    114  A    C  
ATOM    819  CG  GLU A 346     -23.962 -21.460  32.566  1.00 64.31      A    C  
ANISOU  819  CG  GLU A 346     8924   8669   6841   -334     67    123  A    C  
ATOM    820  CD  GLU A 346     -25.183 -22.215  32.058  1.00 67.19      A    C  
ANISOU  820  CD  GLU A 346     9221   9060   7245   -371     61    149  A    C  
ATOM    821  OE1 GLU A 346     -25.087 -23.401  31.758  1.00 69.70      A    O  
ANISOU  821  OE1 GLU A 346     9474   9428   7580   -357    102    152  A    O  
ATOM    822  OE2 GLU A 346     -26.250 -21.636  31.938  1.00 64.73      A    O1-
ANISOU  822  OE2 GLU A 346     8922   8718   6952   -413     10    166  A    O1-
ATOM    823  N   ASN A 347     -23.091 -19.078  36.532  1.00 61.11      A    N  
ANISOU  823  N   ASN A 347     8636   8294   6285   -238    200     83  A    N  
ATOM    824  CA  ASN A 347     -22.639 -19.114  37.938  1.00 63.12      A    C  
ANISOU  824  CA  ASN A 347     8960   8540   6481   -243    219     88  A    C  
ATOM    825  C   ASN A 347     -21.226 -18.598  38.152  1.00 59.43      A    C  
ANISOU  825  C   ASN A 347     8560   8021   5998   -212    177     60  A    C  
ATOM    826  O   ASN A 347     -20.522 -19.053  39.054  1.00 58.45      A    O  
ANISOU  826  O   ASN A 347     8503   7866   5837   -230    159     68  A    O  
ATOM    827  CB  ASN A 347     -22.773 -20.533  38.508  1.00 65.31      A    C  
ANISOU  827  CB  ASN A 347     9263   8810   6739   -312    210    129  A    C  
ATOM    828  CG  ASN A 347     -24.127 -21.134  38.219  1.00 69.90      A    C  
ANISOU  828  CG  ASN A 347     9774   9440   7344   -354    243    163  A    C  
ATOM    829  ND2 ASN A 347     -24.180 -22.459  38.135  1.00 70.82      A    N  
ANISOU  829  ND2 ASN A 347     9901   9536   7469   -418    208    198  A    N  
ATOM    830  OD1 ASN A 347     -25.125 -20.406  38.055  1.00 73.23      A    O  
ANISOU  830  OD1 ASN A 347    10130   9916   7778   -329    294    158  A    O  
ATOM    831  N   MET A 348     -20.806 -17.665  37.309  1.00 55.25      A    N  
ANISOU  831  N   MET A 348     8013   7479   5499   -168    157     30  A    N  
ATOM    832  CA  MET A 348     -19.477 -17.104  37.423  1.00 52.34      A    C  
ANISOU  832  CA  MET A 348     7696   7064   5123   -142    115      7  A    C  
ATOM    833  C   MET A 348     -19.667 -15.751  38.077  1.00 49.47      A    C  
ANISOU  833  C   MET A 348     7352   6713   4729    -95    148    -15  A    C  
ATOM    834  O   MET A 348     -20.691 -15.089  37.896  1.00 48.33      A    O  
ANISOU  834  O   MET A 348     7163   6609   4589    -69    191    -23  A    O  
ATOM    835  CB  MET A 348     -18.793 -16.999  36.052  1.00 53.82      A    C  
ANISOU  835  CB  MET A 348     7856   7229   5362   -132     69     -5  A    C  
ATOM    836  CG  MET A 348     -17.412 -16.349  36.078  1.00 55.55      A    C  
ANISOU  836  CG  MET A 348     8116   7407   5581   -108     28    -26  A    C  
ATOM    837  SD  MET A 348     -16.547 -16.137  34.492  1.00 52.48      A    S  
ANISOU  837  SD  MET A 348     7693   7000   5245    -95    -15    -39  A    S  
ATOM    838  CE  MET A 348     -16.354 -17.859  34.035  1.00 55.31      A    C  
ANISOU  838  CE  MET A 348     8045   7346   5621   -134    -44    -22  A    C  
ATOM    839  N   ASP A 349     -18.676 -15.344  38.849  1.00 47.62      A    N  
ANISOU  839  N   ASP A 349     7186   6441   4464    -82    122    -28  A    N  
ATOM    840  CA  ASP A 349     -18.793 -14.141  39.607  1.00 47.31      A    C  
ANISOU  840  CA  ASP A 349     7182   6405   4388    -38    145    -51  A    C  
ATOM    841  C   ASP A 349     -18.181 -13.070  38.725  1.00 44.20      A    C  
ANISOU  841  C   ASP A 349     6777   5986   4030     -4    109    -75  A    C  
ATOM    842  O   ASP A 349     -17.030 -13.146  38.355  1.00 39.72      A    O  
ANISOU  842  O   ASP A 349     6227   5379   3485    -15     55    -76  A    O  
ATOM    843  CB  ASP A 349     -18.103 -14.286  40.987  1.00 49.44      A    C  
ANISOU  843  CB  ASP A 349     7540   6643   4599    -46    132    -50  A    C  
ATOM    844  CG  ASP A 349     -18.253 -13.020  41.876  1.00 53.64      A    C  
ANISOU  844  CG  ASP A 349     8123   7175   5082      3    155    -77  A    C  
ATOM    845  OD1 ASP A 349     -18.969 -12.062  41.470  1.00 57.55      A    O  
ANISOU  845  OD1 ASP A 349     8581   7695   5588     46    184    -98  A    O  
ATOM    846  OD2 ASP A 349     -17.638 -12.982  42.974  1.00 51.71      A    O1-
ANISOU  846  OD2 ASP A 349     7959   6899   4787      3    137    -81  A    O1-
ATOM    847  N   VAL A 350     -18.978 -12.076  38.362  1.00 44.74      A    N  
ANISOU  847  N   VAL A 350     6813   6079   4107     35    137    -92  A    N  
ATOM    848  CA  VAL A 350     -18.484 -11.031  37.490  1.00 46.94      A    C  
ANISOU  848  CA  VAL A 350     7084   6333   4418     63    100   -111  A    C  
ATOM    849  C   VAL A 350     -17.338 -10.209  38.131  1.00 46.80      A    C  
ANISOU  849  C   VAL A 350     7139   6264   4377     79     57   -127  A    C  
ATOM    850  O   VAL A 350     -16.512  -9.647  37.412  1.00 48.24      A    O  
ANISOU  850  O   VAL A 350     7321   6416   4591     80     11   -131  A    O  
ATOM    851  CB  VAL A 350     -19.658 -10.206  36.893  1.00 50.66      A    C  
ANISOU  851  CB  VAL A 350     7503   6838   4907    103    133   -125  A    C  
ATOM    852  CG1 VAL A 350     -20.540  -9.584  37.962  1.00 53.91      A    C  
ANISOU  852  CG1 VAL A 350     7934   7275   5272    145    184   -142  A    C  
ATOM    853  CG2 VAL A 350     -19.169  -9.176  35.875  1.00 52.67      A    C  
ANISOU  853  CG2 VAL A 350     7751   7064   5196    125     90   -138  A    C  
ATOM    854  N   ASN A 351     -17.222 -10.204  39.463  1.00 46.33      A    N  
ANISOU  854  N   ASN A 351     7144   6193   4263     84     66   -132  A    N  
ATOM    855  CA  ASN A 351     -16.121  -9.496  40.131  1.00 43.63      A    C  
ANISOU  855  CA  ASN A 351     6878   5798   3900     95     16   -145  A    C  
ATOM    856  C   ASN A 351     -14.823 -10.263  40.190  1.00 41.91      A    C  
ANISOU  856  C   ASN A 351     6682   5544   3697     53    -38   -129  A    C  
ATOM    857  O   ASN A 351     -13.837  -9.769  40.733  1.00 40.36      A    O  
ANISOU  857  O   ASN A 351     6543   5302   3489     56    -87   -136  A    O  
ATOM    858  CB  ASN A 351     -16.529  -9.113  41.548  1.00 44.92      A    C  
ANISOU  858  CB  ASN A 351     7111   5961   3992    123     44   -161  A    C  
ATOM    859  CG  ASN A 351     -17.738  -8.210  41.558  1.00 43.94      A    C  
ANISOU  859  CG  ASN A 351     6969   5872   3853    177     96   -185  A    C  
ATOM    860  ND2 ASN A 351     -18.673  -8.463  42.469  1.00 45.43      A    N  
ANISOU  860  ND2 ASN A 351     7170   6102   3989    193    160   -188  A    N  
ATOM    861  OD1 ASN A 351     -17.828  -7.305  40.749  1.00 40.50      A    O  
ANISOU  861  OD1 ASN A 351     6507   5427   3451    205     79   -199  A    O  
ATOM    862  N   LYS A 352     -14.799 -11.455  39.627  1.00 40.98      A    N  
ANISOU  862  N   LYS A 352     6519   5443   3608     18    -34   -107  A    N  
ATOM    863  CA  LYS A 352     -13.553 -12.164  39.527  1.00 43.02      A    C  
ANISOU  863  CA  LYS A 352     6788   5668   3889    -12    -89    -95  A    C  
ATOM    864  C   LYS A 352     -12.800 -11.747  38.250  1.00 42.49      A    C  
ANISOU  864  C   LYS A 352     6674   5590   3879    -12   -124    -97  A    C  
ATOM    865  O   LYS A 352     -12.958 -12.342  37.164  1.00 43.35      A    O  
ANISOU  865  O   LYS A 352     6724   5721   4025    -25   -115    -88  A    O  
ATOM    866  CB  LYS A 352     -13.774 -13.678  39.622  1.00 45.10      A    C  
ANISOU  866  CB  LYS A 352     7039   5945   4151    -48    -78    -74  A    C  
ATOM    867  CG  LYS A 352     -13.895 -14.115  41.073  1.00 48.58      A    C  
ANISOU  867  CG  LYS A 352     7550   6376   4531    -59    -69    -67  A    C  
ATOM    868  CD  LYS A 352     -14.272 -15.579  41.223  1.00 51.50      A    C  
ANISOU  868  CD  LYS A 352     7913   6759   4894    -99    -57    -41  A    C  
ATOM    869  CE  LYS A 352     -14.644 -15.870  42.670  1.00 55.05      A    C  
ANISOU  869  CE  LYS A 352     8433   7208   5274   -110    -34    -30  A    C  
ATOM    870  NZ  LYS A 352     -14.855 -17.326  42.914  1.00 56.70      A    N1+
ANISOU  870  NZ  LYS A 352     8649   7419   5473   -157    -35      0  A    N1+
ATOM    871  N   LEU A 353     -11.944 -10.751  38.386  1.00 40.15      A    N  
ANISOU  871  N   LEU A 353     6407   5259   3587     -2   -165   -106  A    N  
ATOM    872  CA  LEU A 353     -11.386 -10.126  37.216  1.00 40.07      A    C  
ANISOU  872  CA  LEU A 353     6354   5245   3624     -2   -189   -105  A    C  
ATOM    873  C   LEU A 353     -10.455 -11.098  36.469  1.00 40.10      A    C  
ANISOU  873  C   LEU A 353     6316   5250   3669    -29   -214    -91  A    C  
ATOM    874  O   LEU A 353      -9.966 -12.055  37.043  1.00 39.75      A    O  
ANISOU  874  O   LEU A 353     6290   5193   3619    -45   -232    -85  A    O  
ATOM    875  CB  LEU A 353     -10.652  -8.832  37.583  1.00 39.48      A    C  
ANISOU  875  CB  LEU A 353     6323   5129   3546      8   -234   -113  A    C  
ATOM    876  CG  LEU A 353     -11.466  -7.809  38.360  1.00 40.38      A    C  
ANISOU  876  CG  LEU A 353     6491   5235   3616     44   -217   -134  A    C  
ATOM    877  CD1 LEU A 353     -10.549  -6.678  38.758  1.00 40.68      A    C  
ANISOU  877  CD1 LEU A 353     6582   5221   3653     47   -278   -140  A    C  
ATOM    878  CD2 LEU A 353     -12.672  -7.292  37.593  1.00 40.49      A    C  
ANISOU  878  CD2 LEU A 353     6465   5283   3636     71   -172   -143  A    C  
ATOM    879  N   PRO A 354     -10.210 -10.830  35.173  1.00 39.68      A    N  
ANISOU  879  N   PRO A 354     6210   5211   3655    -32   -216    -87  A    N  
ATOM    880  CA  PRO A 354      -9.325 -11.674  34.431  1.00 39.66      A    C  
ANISOU  880  CA  PRO A 354     6167   5213   3687    -49   -235    -78  A    C  
ATOM    881  C   PRO A 354      -7.933 -11.145  34.666  1.00 39.02      A    C  
ANISOU  881  C   PRO A 354     6096   5102   3625    -59   -285    -73  A    C  
ATOM    882  O   PRO A 354      -7.779  -9.978  35.030  1.00 37.57      A    O  
ANISOU  882  O   PRO A 354     5943   4897   3434    -55   -305    -75  A    O  
ATOM    883  CB  PRO A 354      -9.748 -11.389  32.974  1.00 39.67      A    C  
ANISOU  883  CB  PRO A 354     6115   5245   3713    -45   -210    -76  A    C  
ATOM    884  CG  PRO A 354     -10.117  -9.923  33.017  1.00 39.15      A    C  
ANISOU  884  CG  PRO A 354     6068   5169   3637    -31   -211    -80  A    C  
ATOM    885  CD  PRO A 354     -10.558  -9.607  34.410  1.00 38.36      A    C  
ANISOU  885  CD  PRO A 354     6027   5049   3499    -17   -209    -91  A    C  
ATOM    886  N   ASP A 355      -6.929 -11.980  34.441  1.00 38.02      A    N  
ANISOU  886  N   ASP A 355     5944   4974   3526    -71   -310    -68  A    N  
ATOM    887  CA  ASP A 355      -5.542 -11.503  34.533  1.00 38.04      A    C  
ANISOU  887  CA  ASP A 355     5939   4954   3557    -83   -359    -60  A    C  
ATOM    888  C   ASP A 355      -5.301 -10.273  33.648  1.00 37.93      A    C  
ANISOU  888  C   ASP A 355     5898   4950   3564    -90   -359    -51  A    C  
ATOM    889  O   ASP A 355      -5.488 -10.323  32.450  1.00 39.74      A    O  
ANISOU  889  O   ASP A 355     6079   5210   3808    -89   -330    -47  A    O  
ATOM    890  CB  ASP A 355      -4.589 -12.607  34.102  1.00 37.51      A    C  
ANISOU  890  CB  ASP A 355     5829   4898   3524    -87   -376    -57  A    C  
ATOM    891  CG  ASP A 355      -4.656 -13.835  35.009  1.00 38.47      A    C  
ANISOU  891  CG  ASP A 355     5985   5002   3629    -84   -391    -63  A    C  
ATOM    892  OD1 ASP A 355      -5.575 -13.948  35.861  1.00 41.08      A    O  
ANISOU  892  OD1 ASP A 355     6367   5321   3918    -83   -376    -66  A    O  
ATOM    893  OD2 ASP A 355      -3.778 -14.702  34.894  1.00 38.78      A    O1-
ANISOU  893  OD2 ASP A 355     6000   5038   3696    -82   -418    -64  A    O1-
ATOM    894  N   LYS A 356      -4.879  -9.164  34.223  1.00 39.18      A    N  
ANISOU  894  N   LYS A 356     6090   5075   3720    -98   -396    -46  A    N  
ATOM    895  CA  LYS A 356      -4.354  -8.041  33.447  1.00 39.92      A    C  
ANISOU  895  CA  LYS A 356     6160   5169   3839   -115   -412    -30  A    C  
ATOM    896  C   LYS A 356      -3.651  -8.571  32.208  1.00 41.39      A    C  
ANISOU  896  C   LYS A 356     6268   5393   4062   -127   -396    -17  A    C  
ATOM    897  O   LYS A 356      -3.930  -8.120  31.098  1.00 43.64      A    O  
ANISOU  897  O   LYS A 356     6523   5704   4353   -131   -369     -9  A    O  
ATOM    898  CB  LYS A 356      -3.392  -7.167  34.294  1.00 40.59      A    C  
ANISOU  898  CB  LYS A 356     6280   5206   3932   -134   -477    -21  A    C  
ATOM    899  CG  LYS A 356      -3.202  -5.723  33.814  1.00 40.66      A    C  
ANISOU  899  CG  LYS A 356     6295   5199   3952   -153   -500     -5  A    C  
ATOM    900  CD  LYS A 356      -4.537  -4.999  33.774  1.00 41.12      A    C  
ANISOU  900  CD  LYS A 356     6397   5252   3975   -126   -473    -21  A    C  
ATOM    901  CE  LYS A 356      -4.563  -3.814  32.820  1.00 41.87      A    C  
ANISOU  901  CE  LYS A 356     6482   5343   4083   -141   -481     -4  A    C  
ATOM    902  NZ  LYS A 356      -5.882  -3.073  32.941  1.00 42.58      A    N1+
ANISOU  902  NZ  LYS A 356     6620   5418   4137   -105   -464    -24  A    N1+
ATOM    903  N   THR A 357      -2.763  -9.547  32.384  1.00 41.43      A    N  
ANISOU  903  N   THR A 357     6245   5405   4090   -130   -412    -17  A    N  
ATOM    904  CA  THR A 357      -2.068 -10.098  31.271  1.00 42.52      A    C  
ANISOU  904  CA  THR A 357     6311   5582   4260   -133   -394    -10  A    C  
ATOM    905  C   THR A 357      -1.640 -11.528  31.472  1.00 42.07      A    C  
ANISOU  905  C   THR A 357     6234   5533   4214   -116   -398    -23  A    C  
ATOM    906  O   THR A 357      -1.119 -11.880  32.536  1.00 41.68      A    O  
ANISOU  906  O   THR A 357     6211   5453   4170   -117   -440    -26  A    O  
ATOM    907  CB  THR A 357      -0.827  -9.263  30.997  1.00 48.06      A    C  
ANISOU  907  CB  THR A 357     6976   6286   4999   -163   -425     14  A    C  
ATOM    908  CG2 THR A 357      -0.266  -9.634  29.703  1.00 49.46      A    C  
ANISOU  908  CG2 THR A 357     7078   6513   5200   -165   -392     23  A    C  
ATOM    909  OG1 THR A 357      -1.184  -7.868  30.943  1.00 51.59      A    O  
ANISOU  909  OG1 THR A 357     7455   6713   5435   -182   -436     27  A    O  
ATOM    910  N   LEU A 358      -1.804 -12.337  30.413  1.00 41.00      A    N  
ANISOU  910  N   LEU A 358     6057   5437   4084   -100   -359    -30  A    N  
ATOM    911  CA  LEU A 358      -1.458 -13.729  30.438  1.00 39.08      A    C  
ANISOU  911  CA  LEU A 358     5797   5199   3851    -79   -363    -46  A    C  
ATOM    912  C   LEU A 358      -0.039 -13.895  30.020  1.00 41.65      A    C  
ANISOU  912  C   LEU A 358     6059   5546   4220    -78   -380    -40  A    C  
ATOM    913  O   LEU A 358       0.504 -13.079  29.322  1.00 42.92      A    O  
ANISOU  913  O   LEU A 358     6178   5732   4398    -95   -369    -23  A    O  
ATOM    914  CB  LEU A 358      -2.350 -14.518  29.517  1.00 39.12      A    C  
ANISOU  914  CB  LEU A 358     5794   5231   3838    -60   -320    -59  A    C  
ATOM    915  CG  LEU A 358      -3.847 -14.447  29.805  1.00 38.42      A    C  
ANISOU  915  CG  LEU A 358     5754   5131   3712    -61   -298    -64  A    C  
ATOM    916  CD1 LEU A 358      -4.606 -15.114  28.663  1.00 38.30      A    C  
ANISOU  916  CD1 LEU A 358     5719   5144   3686    -47   -261    -73  A    C  
ATOM    917  CD2 LEU A 358      -4.230 -15.108  31.125  1.00 37.99      A    C  
ANISOU  917  CD2 LEU A 358     5753   5041   3638    -60   -321    -70  A    C  
ATOM    918  N   SER A 359       0.570 -14.974  30.484  1.00 46.85      A    N  
ANISOU  918  N   SER A 359     6711   6193   4896    -58   -409    -53  A    N  
ATOM    919  CA  SER A 359       1.987 -15.306  30.238  1.00 51.03      A    C  
ANISOU  919  CA  SER A 359     7174   6741   5471    -48   -430    -52  A    C  
ATOM    920  C   SER A 359       2.345 -15.469  28.749  1.00 50.92      A    C  
ANISOU  920  C   SER A 359     7089   6786   5469    -32   -380    -55  A    C  
ATOM    921  O   SER A 359       1.469 -15.675  27.925  1.00 49.73      A    O  
ANISOU  921  O   SER A 359     6949   6655   5289    -21   -336    -64  A    O  
ATOM    922  CB  SER A 359       2.295 -16.620  31.022  1.00 53.83      A    C  
ANISOU  922  CB  SER A 359     7550   7066   5835    -20   -473    -73  A    C  
ATOM    923  OG  SER A 359       3.567 -17.204  30.745  1.00 56.59      A    O  
ANISOU  923  OG  SER A 359     7834   7435   6231      3   -493    -80  A    O  
ATOM    924  N   PHE A 360       3.629 -15.351  28.415  1.00 52.71      A    N  
ANISOU  924  N   PHE A 360     7244   7043   5739    -31   -388    -46  A    N  
ATOM    925  CA  PHE A 360       4.108 -15.682  27.080  1.00 55.91      A    C  
ANISOU  925  CA  PHE A 360     7580   7509   6153     -8   -338    -52  A    C  
ATOM    926  C   PHE A 360       4.374 -17.196  26.987  1.00 60.81      A    C  
ANISOU  926  C   PHE A 360     8191   8132   6782     47   -345    -88  A    C  
ATOM    927  O   PHE A 360       4.251 -17.797  25.922  1.00 62.52      A    O  
ANISOU  927  O   PHE A 360     8385   8385   6983     80   -302   -107  A    O  
ATOM    928  CB  PHE A 360       5.404 -14.941  26.754  1.00 56.23      A    C  
ANISOU  928  CB  PHE A 360     7538   7589   6237    -30   -338    -25  A    C  
ATOM    929  CG  PHE A 360       5.220 -13.532  26.268  1.00 54.53      A    C  
ANISOU  929  CG  PHE A 360     7318   7390   6011    -81   -314     10  A    C  
ATOM    930  CD1 PHE A 360       4.418 -13.248  25.190  1.00 54.16      A    C  
ANISOU  930  CD1 PHE A 360     7284   7370   5924    -83   -259     12  A    C  
ATOM    931  CD2 PHE A 360       5.925 -12.491  26.862  1.00 56.05      A    C  
ANISOU  931  CD2 PHE A 360     7493   7566   6235   -127   -355     43  A    C  
ATOM    932  CE1 PHE A 360       4.273 -11.945  24.738  1.00 55.72      A    C  
ANISOU  932  CE1 PHE A 360     7481   7576   6111   -130   -244     47  A    C  
ATOM    933  CE2 PHE A 360       5.790 -11.184  26.422  1.00 55.52      A    C  
ANISOU  933  CE2 PHE A 360     7427   7506   6159   -176   -342     78  A    C  
ATOM    934  CZ  PHE A 360       4.959 -10.905  25.355  1.00 54.90      A    C  
ANISOU  934  CZ  PHE A 360     7364   7454   6039   -177   -286     80  A    C  
ATOM    935  N   ASP A 361       4.800 -17.786  28.097  1.00 63.66      A    N  
ANISOU  935  N   ASP A 361     8570   8451   7165     58   -405    -97  A    N  
ATOM    936  CA  ASP A 361       5.017 -19.228  28.200  1.00 68.46      A    C  
ANISOU  936  CA  ASP A 361     9183   9045   7781    110   -428   -131  A    C  
ATOM    937  C   ASP A 361       3.676 -19.966  28.177  1.00 64.17      A    C  
ANISOU  937  C   ASP A 361     8718   8473   7190    119   -418   -148  A    C  
ATOM    938  O   ASP A 361       2.898 -19.863  29.131  1.00 65.21      A    O  
ANISOU  938  O   ASP A 361     8918   8558   7299     93   -443   -140  A    O  
ATOM    939  CB  ASP A 361       5.754 -19.559  29.518  1.00 70.59      A    C  
ANISOU  939  CB  ASP A 361     9466   9268   8086    112   -505   -131  A    C  
ATOM    940  CG  ASP A 361       6.232 -21.022  29.590  1.00 76.55      A    C  
ANISOU  940  CG  ASP A 361    10216  10009   8860    170   -538   -165  A    C  
ATOM    941  OD1 ASP A 361       6.356 -21.668  28.521  1.00 85.84      A    O  
ANISOU  941  OD1 ASP A 361    11355  11224  10035    213   -500   -189  A    O  
ATOM    942  OD2 ASP A 361       6.501 -21.526  30.710  1.00 75.41      A    O1-
ANISOU  942  OD2 ASP A 361    10109   9811   8729    174   -607   -169  A    O1-
ATOM    943  N   LYS A 362       3.428 -20.725  27.115  1.00 62.22      A    N  
ANISOU  943  N   LYS A 362     8459   8252   6927    157   -382   -172  A    N  
ATOM    944  CA  LYS A 362       2.180 -21.467  26.946  1.00 61.70      A    C  
ANISOU  944  CA  LYS A 362     8460   8162   6821    163   -375   -187  A    C  
ATOM    945  C   LYS A 362       1.847 -22.219  28.213  1.00 62.74      A    C  
ANISOU  945  C   LYS A 362     8657   8230   6949    159   -434   -191  A    C  
ATOM    946  O   LYS A 362       0.720 -22.173  28.704  1.00 58.74      A    O  
ANISOU  946  O   LYS A 362     8211   7695   6410    129   -434   -181  A    O  
ATOM    947  CB  LYS A 362       2.310 -22.520  25.858  1.00 63.95      A    C  
ANISOU  947  CB  LYS A 362     8728   8469   7099    217   -356   -221  A    C  
ATOM    948  CG  LYS A 362       2.633 -22.054  24.442  1.00 66.63      A    C  
ANISOU  948  CG  LYS A 362     9009   8875   7432    232   -294   -224  A    C  
ATOM    949  CD  LYS A 362       2.686 -23.263  23.482  1.00 67.01      A    C  
ANISOU  949  CD  LYS A 362     9059   8935   7465    294   -283   -264  A    C  
ATOM    950  CE  LYS A 362       3.664 -24.341  23.979  1.00 68.42      A    C  
ANISOU  950  CE  LYS A 362     9222   9093   7679    346   -332   -293  A    C  
ATOM    951  NZ  LYS A 362       3.864 -25.518  23.096  1.00 67.30      A    N1+
ANISOU  951  NZ  LYS A 362     9083   8960   7526    416   -329   -338  A    N1+
ATOM    952  N   GLU A 363       2.849 -22.931  28.720  1.00 66.87      A    N  
ANISOU  952  N   GLU A 363     9165   8734   7506    189   -483   -205  A    N  
ATOM    953  CA  GLU A 363       2.705 -23.780  29.906  1.00 71.15      A    C  
ANISOU  953  CA  GLU A 363     9772   9213   8045    189   -548   -209  A    C  
ATOM    954  C   GLU A 363       2.268 -23.035  31.164  1.00 68.04      A    C  
ANISOU  954  C   GLU A 363     9430   8785   7636    138   -570   -180  A    C  
ATOM    955  O   GLU A 363       1.725 -23.649  32.077  1.00 74.74      A    O  
ANISOU  955  O   GLU A 363    10349   9584   8462    125   -607   -178  A    O  
ATOM    956  CB  GLU A 363       4.018 -24.541  30.189  1.00 76.32      A    C  
ANISOU  956  CB  GLU A 363    10393   9856   8747    235   -602   -229  A    C  
ATOM    957  CG  GLU A 363       4.370 -25.596  29.143  1.00 78.42      A    C  
ANISOU  957  CG  GLU A 363    10630  10143   9023    299   -593   -267  A    C  
ATOM    958  CD  GLU A 363       5.732 -26.228  29.377  1.00 84.99      A    C  
ANISOU  958  CD  GLU A 363    11416  10970   9906    352   -644   -289  A    C  
ATOM    959  OE1 GLU A 363       6.033 -26.673  30.510  1.00 86.14      A    O  
ANISOU  959  OE1 GLU A 363    11601  11060  10068    349   -716   -286  A    O  
ATOM    960  OE2 GLU A 363       6.518 -26.287  28.411  1.00 92.67      A    O1-
ANISOU  960  OE2 GLU A 363    12310  11995  10902    398   -611   -309  A    O1-
ATOM    961  N   LYS A 364       2.506 -21.728  31.223  1.00 65.23      A    N  
ANISOU  961  N   LYS A 364     9043   8452   7288    108   -550   -159  A    N  
ATOM    962  CA  LYS A 364       2.108 -20.918  32.375  1.00 63.02      A    C  
ANISOU  962  CA  LYS A 364     8815   8139   6988     65   -570   -135  A    C  
ATOM    963  C   LYS A 364       0.934 -19.999  32.063  1.00 62.53      A    C  
ANISOU  963  C   LYS A 364     8775   8095   6888     34   -515   -121  A    C  
ATOM    964  O   LYS A 364       0.697 -19.034  32.785  1.00 61.96      A    O  
ANISOU  964  O   LYS A 364     8731   8007   6801      3   -520   -104  A    O  
ATOM    965  CB  LYS A 364       3.288 -20.102  32.853  1.00 63.76      A    C  
ANISOU  965  CB  LYS A 364     8870   8232   7121     53   -605   -122  A    C  
ATOM    966  CG  LYS A 364       4.456 -20.996  33.200  1.00 68.73      A    C  
ANISOU  966  CG  LYS A 364     9474   8845   7795     87   -665   -136  A    C  
ATOM    967  CD  LYS A 364       5.416 -20.363  34.200  1.00 72.22      A    C  
ANISOU  967  CD  LYS A 364     9910   9260   8268     67   -727   -119  A    C  
ATOM    968  CE  LYS A 364       6.541 -21.347  34.529  1.00 72.51      A    C  
ANISOU  968  CE  LYS A 364     9918   9277   8352    106   -792   -136  A    C  
ATOM    969  NZ  LYS A 364       7.700 -20.650  35.145  1.00 74.06      A    N1+
ANISOU  969  NZ  LYS A 364    10076   9466   8598     90   -848   -119  A    N1+
ATOM    970  N   ASN A 365       0.197 -20.317  30.992  1.00 59.05      A    N  
ANISOU  970  N   ASN A 365     8322   7683   6430     46   -467   -131  A    N  
ATOM    971  CA  ASN A 365      -0.924 -19.524  30.522  1.00 53.95      A    C  
ANISOU  971  CA  ASN A 365     7688   7057   5753     23   -416   -120  A    C  
ATOM    972  C   ASN A 365      -2.186 -20.332  30.761  1.00 53.21      A    C  
ANISOU  972  C   ASN A 365     7650   6943   5625     18   -410   -125  A    C  
ATOM    973  O   ASN A 365      -2.386 -21.377  30.130  1.00 54.29      A    O  
ANISOU  973  O   ASN A 365     7785   7082   5760     40   -408   -141  A    O  
ATOM    974  CB  ASN A 365      -0.748 -19.221  29.024  1.00 52.69      A    C  
ANISOU  974  CB  ASN A 365     7468   6949   5603     37   -370   -125  A    C  
ATOM    975  CG  ASN A 365      -1.887 -18.381  28.440  1.00 50.50      A    C  
ANISOU  975  CG  ASN A 365     7201   6689   5295     16   -324   -114  A    C  
ATOM    976  ND2 ASN A 365      -1.562 -17.609  27.413  1.00 48.51      A    N  
ANISOU  976  ND2 ASN A 365     6903   6477   5050     14   -291   -106  A    N  
ATOM    977  OD1 ASN A 365      -3.029 -18.411  28.910  1.00 45.06      A    O  
ANISOU  977  OD1 ASN A 365     6559   5981   4578      2   -319   -110  A    O  
ATOM    978  N   PRO A 366      -3.045 -19.865  31.680  1.00 51.06      A    N  
ANISOU  978  N   PRO A 366     7427   6649   5322     -9   -407   -110  A    N  
ATOM    979  CA  PRO A 366      -4.291 -20.531  31.951  1.00 50.66      A    C  
ANISOU  979  CA  PRO A 366     7421   6586   5239    -21   -396   -108  A    C  
ATOM    980  C   PRO A 366      -4.993 -21.058  30.718  1.00 50.86      A    C  
ANISOU  980  C   PRO A 366     7426   6637   5262    -10   -365   -118  A    C  
ATOM    981  O   PRO A 366      -5.452 -22.208  30.723  1.00 55.84      A    O  
ANISOU  981  O   PRO A 366     8082   7250   5885     -9   -380   -123  A    O  
ATOM    982  CB  PRO A 366      -5.110 -19.436  32.587  1.00 51.35      A    C  
ANISOU  982  CB  PRO A 366     7535   6675   5299    -45   -370    -93  A    C  
ATOM    983  CG  PRO A 366      -4.105 -18.709  33.406  1.00 53.62      A    C  
ANISOU  983  CG  PRO A 366     7830   6943   5597    -49   -404    -88  A    C  
ATOM    984  CD  PRO A 366      -2.855 -18.718  32.577  1.00 52.37      A    C  
ANISOU  984  CD  PRO A 366     7612   6802   5482    -30   -418    -96  A    C  
ATOM    985  N   PHE A 367      -5.063 -20.250  29.666  1.00 47.83      A    N  
ANISOU  985  N   PHE A 367     7000   6290   4884     -5   -328   -118  A    N  
ATOM    986  CA  PHE A 367      -5.814 -20.649  28.484  1.00 45.80      A    C  
ANISOU  986  CA  PHE A 367     6729   6054   4619      2   -301   -126  A    C  
ATOM    987  C   PHE A 367      -5.583 -22.105  28.011  1.00 45.04      A    C  
ANISOU  987  C   PHE A 367     6639   5945   4529     27   -326   -146  A    C  
ATOM    988  O   PHE A 367      -6.555 -22.837  27.780  1.00 43.27      A    O  
ANISOU  988  O   PHE A 367     6439   5710   4289     19   -327   -147  A    O  
ATOM    989  CB  PHE A 367      -5.595 -19.706  27.309  1.00 43.66      A    C  
ANISOU  989  CB  PHE A 367     6412   5822   4353     10   -266   -126  A    C  
ATOM    990  CG  PHE A 367      -6.356 -20.148  26.088  1.00 43.07      A    C  
ANISOU  990  CG  PHE A 367     6332   5766   4267     20   -244   -136  A    C  
ATOM    991  CD1 PHE A 367      -7.672 -19.796  25.925  1.00 41.51      A    C  
ANISOU  991  CD1 PHE A 367     6147   5572   4051      1   -225   -126  A    C  
ATOM    992  CD2 PHE A 367      -5.778 -21.015  25.172  1.00 41.97      A    C  
ANISOU  992  CD2 PHE A 367     6177   5636   4133     51   -250   -157  A    C  
ATOM    993  CE1 PHE A 367      -8.392 -20.247  24.838  1.00 42.33      A    C  
ANISOU  993  CE1 PHE A 367     6249   5687   4145      8   -215   -134  A    C  
ATOM    994  CE2 PHE A 367      -6.484 -21.463  24.089  1.00 40.76      A    C  
ANISOU  994  CE2 PHE A 367     6029   5493   3964     60   -237   -167  A    C  
ATOM    995  CZ  PHE A 367      -7.801 -21.099  23.932  1.00 41.76      A    C  
ANISOU  995  CZ  PHE A 367     6170   5620   4075     36   -223   -154  A    C  
ATOM    996  N   PHE A 368      -4.322 -22.516  27.904  1.00 45.32      A    N  
ANISOU  996  N   PHE A 368     6652   5978   4587     56   -349   -161  A    N  
ATOM    997  CA  PHE A 368      -3.975 -23.834  27.361  1.00 48.71      A    C  
ANISOU  997  CA  PHE A 368     7087   6395   5023     91   -375   -186  A    C  
ATOM    998  C   PHE A 368      -4.277 -24.967  28.336  1.00 50.44      A    C  
ANISOU  998  C   PHE A 368     7364   6563   5237     82   -424   -186  A    C  
ATOM    999  O   PHE A 368      -4.362 -26.138  27.920  1.00 49.17      A    O  
ANISOU  999  O   PHE A 368     7225   6381   5075    104   -451   -204  A    O  
ATOM   1000  CB  PHE A 368      -2.498 -23.919  26.955  1.00 51.62      A    C  
ANISOU 1000  CB  PHE A 368     7407   6782   5421    133   -383   -205  A    C  
ATOM   1001  CG  PHE A 368      -2.080 -22.858  26.004  1.00 52.49      A    C  
ANISOU 1001  CG  PHE A 368     7461   6945   5537    137   -335   -201  A    C  
ATOM   1002  CD1 PHE A 368      -2.275 -23.017  24.646  1.00 54.40      A    C  
ANISOU 1002  CD1 PHE A 368     7685   7220   5764    160   -301   -216  A    C  
ATOM   1003  CD2 PHE A 368      -1.552 -21.665  26.469  1.00 53.73      A    C  
ANISOU 1003  CD2 PHE A 368     7588   7116   5708    113   -326   -180  A    C  
ATOM   1004  CE1 PHE A 368      -1.928 -22.008  23.755  1.00 55.54      A    C  
ANISOU 1004  CE1 PHE A 368     7782   7414   5907    157   -255   -208  A    C  
ATOM   1005  CE2 PHE A 368      -1.181 -20.659  25.580  1.00 56.09      A    C  
ANISOU 1005  CE2 PHE A 368     7838   7462   6010    109   -284   -170  A    C  
ATOM   1006  CZ  PHE A 368      -1.373 -20.831  24.221  1.00 55.59      A    C  
ANISOU 1006  CZ  PHE A 368     7756   7434   5929    130   -246   -183  A    C  
ATOM   1007  N   HIS A 369      -4.435 -24.626  29.614  1.00 49.33      A    N  
ANISOU 1007  N   HIS A 369     7254   6400   5090     51   -439   -164  A    N  
ATOM   1008  CA  HIS A 369      -4.798 -25.605  30.627  1.00 50.34      A    C  
ANISOU 1008  CA  HIS A 369     7442   6479   5204     32   -483   -156  A    C  
ATOM   1009  C   HIS A 369      -6.303 -25.745  30.665  1.00 48.94      A    C  
ANISOU 1009  C   HIS A 369     7294   6301   4998     -5   -459   -137  A    C  
ATOM   1010  O   HIS A 369      -6.856 -26.807  30.946  1.00 48.77      A    O  
ANISOU 1010  O   HIS A 369     7317   6247   4965    -22   -489   -131  A    O  
ATOM   1011  CB  HIS A 369      -4.290 -25.149  32.000  1.00 53.79      A    C  
ANISOU 1011  CB  HIS A 369     7903   6893   5639     15   -507   -141  A    C  
ATOM   1012  CG  HIS A 369      -2.822 -25.368  32.219  1.00 54.84      A    C  
ANISOU 1012  CG  HIS A 369     8017   7011   5806     49   -553   -156  A    C  
ATOM   1013  CD2 HIS A 369      -1.753 -24.576  31.966  1.00 55.95      A    C  
ANISOU 1013  CD2 HIS A 369     8103   7178   5977     69   -548   -163  A    C  
ATOM   1014  ND1 HIS A 369      -2.318 -26.521  32.798  1.00 59.82      A    N  
ANISOU 1014  ND1 HIS A 369     8687   7595   6446     63   -616   -164  A    N  
ATOM   1015  CE1 HIS A 369      -1.001 -26.427  32.891  1.00 58.66      A    C  
ANISOU 1015  CE1 HIS A 369     8505   7447   6335     96   -648   -178  A    C  
ATOM   1016  NE2 HIS A 369      -0.632 -25.257  32.392  1.00 57.84      A    N  
ANISOU 1016  NE2 HIS A 369     8341   7389   6246     97   -606   -176  A    N  
ATOM   1017  N   ILE A 370      -6.960 -24.628  30.399  1.00 47.47      A    N  
ANISOU 1017  N   ILE A 370     7082   6151   4802    -22   -408   -126  A    N  
ATOM   1018  CA  ILE A 370      -8.403 -24.554  30.367  1.00 45.35      A    C  
ANISOU 1018  CA  ILE A 370     6825   5893   4511    -55   -379   -108  A    C  
ATOM   1019  C   ILE A 370      -8.961 -25.158  29.060  1.00 45.87      A    C  
ANISOU 1019  C   ILE A 370     6876   5969   4581    -45   -375   -120  A    C  
ATOM   1020  O   ILE A 370     -10.011 -25.834  29.069  1.00 45.07      A    O  
ANISOU 1020  O   ILE A 370     6797   5856   4469    -72   -381   -108  A    O  
ATOM   1021  CB  ILE A 370      -8.816 -23.072  30.440  1.00 45.20      A    C  
ANISOU 1021  CB  ILE A 370     6780   5908   4484    -64   -330    -98  A    C  
ATOM   1022  CG1 ILE A 370      -8.419 -22.470  31.814  1.00 45.62      A    C  
ANISOU 1022  CG1 ILE A 370     6860   5946   4525    -76   -338    -87  A    C  
ATOM   1023  CG2 ILE A 370     -10.293 -22.927  30.169  1.00 44.91      A    C  
ANISOU 1023  CG2 ILE A 370     6739   5891   4433    -89   -297    -84  A    C  
ATOM   1024  CD1 ILE A 370      -8.359 -20.943  31.893  1.00 44.94      A    C  
ANISOU 1024  CD1 ILE A 370     6754   5884   4437    -74   -306    -84  A    C  
ATOM   1025  N   GLN A 371      -8.236 -24.905  27.959  1.00 43.78      A    N  
ANISOU 1025  N   GLN A 371     6574   5726   4331     -8   -365   -143  A    N  
ATOM   1026  CA  GLN A 371      -8.657 -25.237  26.605  1.00 43.71      A    C  
ANISOU 1026  CA  GLN A 371     6553   5732   4321      7   -357   -157  A    C  
ATOM   1027  C   GLN A 371      -9.301 -26.605  26.461  1.00 42.33      A    C  
ANISOU 1027  C   GLN A 371     6418   5522   4141     -2   -396   -160  A    C  
ATOM   1028  O   GLN A 371     -10.401 -26.694  25.923  1.00 43.17      A    O  
ANISOU 1028  O   GLN A 371     6527   5635   4240    -23   -388   -151  A    O  
ATOM   1029  CB  GLN A 371      -7.480 -25.076  25.630  1.00 45.32      A    C  
ANISOU 1029  CB  GLN A 371     6723   5959   4537     54   -350   -184  A    C  
ATOM   1030  CG  GLN A 371      -7.817 -25.375  24.188  1.00 45.52      A    C  
ANISOU 1030  CG  GLN A 371     6741   6000   4553     75   -340   -201  A    C  
ATOM   1031  CD  GLN A 371      -6.816 -24.799  23.212  1.00 45.63      A    C  
ANISOU 1031  CD  GLN A 371     6713   6053   4569    113   -310   -219  A    C  
ATOM   1032  NE2 GLN A 371      -7.325 -24.263  22.105  1.00 44.24      A    N  
ANISOU 1032  NE2 GLN A 371     6523   5906   4377    113   -279   -219  A    N  
ATOM   1033  OE1 GLN A 371      -5.602 -24.834  23.439  1.00 45.63      A    O  
ANISOU 1033  OE1 GLN A 371     6692   6060   4586    140   -315   -230  A    O  
ATOM   1034  N   PRO A 372      -8.692 -27.665  27.017  1.00 42.21      A    N  
ANISOU 1034  N   PRO A 372     6439   5465   4131      8   -446   -168  A    N  
ATOM   1035  CA  PRO A 372      -9.302 -29.013  26.836  1.00 41.52      A    C  
ANISOU 1035  CA  PRO A 372     6398   5337   4039     -2   -493   -170  A    C  
ATOM   1036  C   PRO A 372     -10.719 -29.158  27.350  1.00 40.89      A    C  
ANISOU 1036  C   PRO A 372     6338   5249   3946    -64   -489   -134  A    C  
ATOM   1037  O   PRO A 372     -11.400 -30.087  26.993  1.00 42.16      A    O  
ANISOU 1037  O   PRO A 372     6528   5384   4105    -81   -523   -130  A    O  
ATOM   1038  CB  PRO A 372      -8.371 -29.936  27.624  1.00 42.11      A    C  
ANISOU 1038  CB  PRO A 372     6512   5366   4123     14   -549   -179  A    C  
ATOM   1039  CG  PRO A 372      -7.101 -29.154  27.790  1.00 43.08      A    C  
ANISOU 1039  CG  PRO A 372     6595   5513   4260     51   -531   -194  A    C  
ATOM   1040  CD  PRO A 372      -7.538 -27.720  27.929  1.00 42.24      A    C  
ANISOU 1040  CD  PRO A 372     6450   5452   4147     25   -470   -173  A    C  
ATOM   1041  N   HIS A 373     -11.160 -28.246  28.202  1.00 41.22      A    N  
ANISOU 1041  N   HIS A 373     6364   5315   3980    -95   -450   -108  A    N  
ATOM   1042  CA  HIS A 373     -12.495 -28.273  28.721  1.00 40.50      A    C  
ANISOU 1042  CA  HIS A 373     6280   5229   3877   -150   -435    -74  A    C  
ATOM   1043  C   HIS A 373     -13.390 -27.293  28.003  1.00 39.80      A    C  
ANISOU 1043  C   HIS A 373     6144   5187   3791   -156   -385    -69  A    C  
ATOM   1044  O   HIS A 373     -14.555 -27.188  28.348  1.00 37.99      A    O  
ANISOU 1044  O   HIS A 373     5906   4971   3556   -196   -366    -42  A    O  
ATOM   1045  CB  HIS A 373     -12.442 -27.892  30.204  1.00 43.76      A    C  
ANISOU 1045  CB  HIS A 373     6711   5640   4274   -176   -420    -50  A    C  
ATOM   1046  CG  HIS A 373     -11.521 -28.744  31.018  1.00 44.56      A    C  
ANISOU 1046  CG  HIS A 373     6863   5693   4373   -171   -473    -53  A    C  
ATOM   1047  CD2 HIS A 373     -10.383 -28.440  31.685  1.00 46.82      A    C  
ANISOU 1047  CD2 HIS A 373     7159   5968   4660   -146   -486    -64  A    C  
ATOM   1048  ND1 HIS A 373     -11.740 -30.092  31.224  1.00 45.65      A    N  
ANISOU 1048  ND1 HIS A 373     7051   5785   4508   -195   -527    -42  A    N  
ATOM   1049  CE1 HIS A 373     -10.768 -30.584  31.971  1.00 47.74      A    C  
ANISOU 1049  CE1 HIS A 373     7356   6010   4771   -181   -572    -48  A    C  
ATOM   1050  NE2 HIS A 373      -9.925 -29.606  32.256  1.00 48.56      A    N  
ANISOU 1050  NE2 HIS A 373     7434   6135   4879   -151   -548    -62  A    N  
ATOM   1051  N   LEU A 374     -12.851 -26.565  27.013  1.00 40.46      A    N  
ANISOU 1051  N   LEU A 374     6195   5296   3882   -115   -365    -93  A    N  
ATOM   1052  CA  LEU A 374     -13.663 -25.662  26.149  1.00 40.52      A    C  
ANISOU 1052  CA  LEU A 374     6162   5341   3892   -116   -328    -91  A    C  
ATOM   1053  C   LEU A 374     -14.265 -26.334  24.872  1.00 40.05      A    C  
ANISOU 1053  C   LEU A 374     6105   5274   3835   -114   -353   -100  A    C  
ATOM   1054  O   LEU A 374     -13.552 -26.559  23.863  1.00 36.57      A    O  
ANISOU 1054  O   LEU A 374     5670   4831   3394    -75   -367   -128  A    O  
ATOM   1055  CB  LEU A 374     -12.819 -24.439  25.734  1.00 41.03      A    C  
ANISOU 1055  CB  LEU A 374     6196   5436   3958    -81   -295   -106  A    C  
ATOM   1056  CG  LEU A 374     -12.303 -23.504  26.833  1.00 39.88      A    C  
ANISOU 1056  CG  LEU A 374     6044   5298   3808    -82   -272    -98  A    C  
ATOM   1057  CD1 LEU A 374     -11.541 -22.369  26.204  1.00 39.71      A    C  
ANISOU 1057  CD1 LEU A 374     5992   5302   3792    -54   -248   -110  A    C  
ATOM   1058  CD2 LEU A 374     -13.397 -22.929  27.675  1.00 39.95      A    C  
ANISOU 1058  CD2 LEU A 374     6050   5320   3808   -114   -244    -74  A    C  
ATOM   1059  N   LEU A 375     -15.584 -26.575  24.899  1.00 39.93      A    N  
ANISOU 1059  N   LEU A 375     6084   5261   3824   -155   -356    -77  A    N  
ATOM   1060  CA  LEU A 375     -16.272 -27.357  23.869  1.00 41.44      A    C  
ANISOU 1060  CA  LEU A 375     6287   5436   4022   -163   -393    -80  A    C  
ATOM   1061  C   LEU A 375     -17.536 -26.670  23.380  1.00 43.17      A    C  
ANISOU 1061  C   LEU A 375     6466   5686   4250   -185   -371    -63  A    C  
ATOM   1062  O   LEU A 375     -18.161 -25.873  24.108  1.00 44.10      A    O  
ANISOU 1062  O   LEU A 375     6549   5833   4370   -205   -331    -41  A    O  
ATOM   1063  CB  LEU A 375     -16.679 -28.752  24.408  1.00 41.85      A    C  
ANISOU 1063  CB  LEU A 375     6381   5444   4076   -203   -445    -63  A    C  
ATOM   1064  CG  LEU A 375     -15.550 -29.664  24.938  1.00 42.35      A    C  
ANISOU 1064  CG  LEU A 375     6493   5464   4133   -184   -483    -78  A    C  
ATOM   1065  CD1 LEU A 375     -16.151 -30.944  25.492  1.00 42.51      A    C  
ANISOU 1065  CD1 LEU A 375     6557   5438   4155   -234   -537    -52  A    C  
ATOM   1066  CD2 LEU A 375     -14.498 -29.990  23.866  1.00 41.82      A    C  
ANISOU 1066  CD2 LEU A 375     6443   5382   4062   -123   -508   -122  A    C  
ATOM   1067  N   VAL A 376     -17.933 -26.978  22.145  1.00 42.19      A    N  
ANISOU 1067  N   VAL A 376     6346   5555   4128   -178   -400    -74  A    N  
ATOM   1068  CA  VAL A 376     -19.304 -26.668  21.749  1.00 43.83      A    C  
ANISOU 1068  CA  VAL A 376     6521   5781   4352   -208   -399    -53  A    C  
ATOM   1069  C   VAL A 376     -20.085 -27.952  21.900  1.00 45.71      A    C  
ANISOU 1069  C   VAL A 376     6780   5984   4601   -256   -451    -32  A    C  
ATOM   1070  O   VAL A 376     -19.659 -28.984  21.380  1.00 45.31      A    O  
ANISOU 1070  O   VAL A 376     6779   5892   4544   -247   -503    -50  A    O  
ATOM   1071  CB  VAL A 376     -19.430 -26.064  20.316  1.00 43.02      A    C  
ANISOU 1071  CB  VAL A 376     6407   5691   4244   -178   -401    -73  A    C  
ATOM   1072  CG1 VAL A 376     -18.527 -24.854  20.173  1.00 41.44      A    C  
ANISOU 1072  CG1 VAL A 376     6193   5521   4031   -136   -354    -90  A    C  
ATOM   1073  CG2 VAL A 376     -19.064 -27.066  19.261  1.00 44.31      A    C  
ANISOU 1073  CG2 VAL A 376     6620   5818   4395   -159   -455    -98  A    C  
ATOM   1074  N   LYS A 377     -21.174 -27.894  22.676  1.00 48.13      A    N  
ANISOU 1074  N   LYS A 377     7051   6309   4924   -306   -435      4  A    N  
ATOM   1075  CA  LYS A 377     -22.068 -29.026  22.846  1.00 51.62      A    C  
ANISOU 1075  CA  LYS A 377     7505   6725   5382   -365   -482     34  A    C  
ATOM   1076  C   LYS A 377     -23.456 -28.554  22.465  1.00 52.34      A    C  
ANISOU 1076  C   LYS A 377     7535   6849   5500   -395   -474     58  A    C  
ATOM   1077  O   LYS A 377     -23.910 -27.521  22.974  1.00 55.50      A    O  
ANISOU 1077  O   LYS A 377     7882   7298   5907   -392   -416     70  A    O  
ATOM   1078  CB  LYS A 377     -22.022 -29.561  24.280  1.00 52.97      A    C  
ANISOU 1078  CB  LYS A 377     7690   6888   5546   -406   -472     64  A    C  
ATOM   1079  CG  LYS A 377     -20.641 -30.098  24.654  1.00 54.58      A    C  
ANISOU 1079  CG  LYS A 377     7955   7053   5728   -375   -492     39  A    C  
ATOM   1080  CD  LYS A 377     -20.538 -30.761  26.041  1.00 53.84      A    C  
ANISOU 1080  CD  LYS A 377     7892   6941   5624   -417   -496     69  A    C  
ATOM   1081  CE  LYS A 377     -20.338 -29.778  27.189  1.00 54.23      A    C  
ANISOU 1081  CE  LYS A 377     7916   7031   5658   -412   -426     79  A    C  
ATOM   1082  NZ  LYS A 377     -20.006 -30.437  28.509  1.00 55.08      A    N1+
ANISOU 1082  NZ  LYS A 377     8069   7114   5745   -445   -435    102  A    N1+
ATOM   1083  N   ASN A 378     -24.091 -29.297  21.546  1.00 52.89      A    N  
ANISOU 1083  N   ASN A 378     7617   6890   5586   -418   -537     63  A    N  
ATOM   1084  CA  ASN A 378     -25.331 -28.900  20.830  1.00 52.10      A    C  
ANISOU 1084  CA  ASN A 378     7464   6814   5517   -437   -548     79  A    C  
ATOM   1085  C   ASN A 378     -25.351 -27.441  20.341  1.00 52.16      A    C  
ANISOU 1085  C   ASN A 378     7428   6865   5523   -389   -500     59  A    C  
ATOM   1086  O   ASN A 378     -26.301 -26.695  20.566  1.00 51.34      A    O  
ANISOU 1086  O   ASN A 378     7259   6804   5444   -401   -469     80  A    O  
ATOM   1087  CB  ASN A 378     -26.559 -29.195  21.695  1.00 54.65      A    C  
ANISOU 1087  CB  ASN A 378     7733   7160   5869   -508   -539    130  A    C  
ATOM   1088  CG  ASN A 378     -26.702 -30.676  22.035  1.00 57.53      A    C  
ANISOU 1088  CG  ASN A 378     8143   7477   6239   -568   -600    157  A    C  
ATOM   1089  ND2 ASN A 378     -27.596 -30.955  22.967  1.00 61.26      A    N  
ANISOU 1089  ND2 ASN A 378     8571   7973   6729   -634   -582    206  A    N  
ATOM   1090  OD1 ASN A 378     -26.037 -31.565  21.459  1.00 57.94      A    O  
ANISOU 1090  OD1 ASN A 378     8268   7470   6276   -556   -664    134  A    O  
ATOM   1091  N   GLY A 379     -24.279 -27.029  19.678  1.00 52.97      A    N  
ANISOU 1091  N   GLY A 379     7569   6958   5598   -332   -495     21  A    N  
ATOM   1092  CA  GLY A 379     -24.238 -25.722  19.044  1.00 53.42      A    C  
ANISOU 1092  CA  GLY A 379     7599   7047   5651   -289   -462      4  A    C  
ATOM   1093  C   GLY A 379     -24.065 -24.568  20.013  1.00 52.96      A    C  
ANISOU 1093  C   GLY A 379     7500   7029   5590   -273   -391      9  A    C  
ATOM   1094  O   GLY A 379     -24.189 -23.399  19.633  1.00 57.08      A    O  
ANISOU 1094  O   GLY A 379     7996   7578   6114   -243   -364      0  A    O  
ATOM   1095  N   VAL A 380     -23.762 -24.874  21.266  1.00 50.62      A    N  
ANISOU 1095  N   VAL A 380     7208   6737   5288   -291   -363     22  A    N  
ATOM   1096  CA  VAL A 380     -23.485 -23.820  22.251  1.00 47.11      A    C  
ANISOU 1096  CA  VAL A 380     6739   6325   4834   -272   -299     22  A    C  
ATOM   1097  C   VAL A 380     -22.081 -23.987  22.783  1.00 44.92      A    C  
ANISOU 1097  C   VAL A 380     6509   6028   4529   -250   -289      4  A    C  
ATOM   1098  O   VAL A 380     -21.561 -25.092  22.827  1.00 46.92      A    O  
ANISOU 1098  O   VAL A 380     6805   6247   4775   -262   -324      1  A    O  
ATOM   1099  CB  VAL A 380     -24.474 -23.857  23.418  1.00 46.27      A    C  
ANISOU 1099  CB  VAL A 380     6590   6248   4743   -311   -267     56  A    C  
ATOM   1100  CG1 VAL A 380     -24.383 -22.572  24.213  1.00 47.37      A    C  
ANISOU 1100  CG1 VAL A 380     6703   6424   4872   -281   -204     51  A    C  
ATOM   1101  CG2 VAL A 380     -25.902 -24.021  22.919  1.00 47.02      A    C  
ANISOU 1101  CG2 VAL A 380     6631   6360   4873   -343   -287     79  A    C  
ATOM   1102  N   ALA A 381     -21.460 -22.890  23.168  1.00 43.29      A    N  
ANISOU 1102  N   ALA A 381     6295   5841   4309   -217   -246     -7  A    N  
ATOM   1103  CA  ALA A 381     -20.129 -22.930  23.747  1.00 44.09      A    C  
ANISOU 1103  CA  ALA A 381     6434   5928   4390   -198   -237    -21  A    C  
ATOM   1104  C   ALA A 381     -20.190 -23.148  25.256  1.00 43.79      A    C  
ANISOU 1104  C   ALA A 381     6401   5892   4343   -223   -214     -2  A    C  
ATOM   1105  O   ALA A 381     -20.967 -22.462  25.942  1.00 43.79      A    O  
ANISOU 1105  O   ALA A 381     6370   5923   4346   -232   -176     12  A    O  
ATOM   1106  CB  ALA A 381     -19.406 -21.618  23.456  1.00 43.30      A    C  
ANISOU 1106  CB  ALA A 381     6327   5844   4281   -157   -209    -40  A    C  
ATOM   1107  N   HIS A 382     -19.324 -24.032  25.759  1.00 44.00      A    N  
ANISOU 1107  N   HIS A 382     6472   5886   4358   -229   -237     -5  A    N  
ATOM   1108  CA  HIS A 382     -19.209 -24.368  27.211  1.00 44.62      A    C  
ANISOU 1108  CA  HIS A 382     6572   5959   4421   -254   -224     12  A    C  
ATOM   1109  C   HIS A 382     -17.796 -24.304  27.787  1.00 44.68      A    C  
ANISOU 1109  C   HIS A 382     6617   5945   4412   -229   -230     -4  A    C  
ATOM   1110  O   HIS A 382     -16.847 -24.804  27.171  1.00 40.92      A    O  
ANISOU 1110  O   HIS A 382     6164   5443   3939   -205   -264    -25  A    O  
ATOM   1111  CB  HIS A 382     -19.653 -25.813  27.479  1.00 44.77      A    C  
ANISOU 1111  CB  HIS A 382     6617   5950   4443   -302   -264     35  A    C  
ATOM   1112  CG  HIS A 382     -21.100 -26.060  27.224  1.00 45.97      A    C  
ANISOU 1112  CG  HIS A 382     6730   6121   4613   -343   -263     63  A    C  
ATOM   1113  CD2 HIS A 382     -22.076 -26.514  28.046  1.00 46.23      A    C  
ANISOU 1113  CD2 HIS A 382     6748   6168   4647   -397   -250    101  A    C  
ATOM   1114  ND1 HIS A 382     -21.699 -25.842  25.991  1.00 45.81      A    N  
ANISOU 1114  ND1 HIS A 382     6678   6110   4615   -334   -277     55  A    N  
ATOM   1115  CE1 HIS A 382     -22.984 -26.154  26.073  1.00 46.24      A    C  
ANISOU 1115  CE1 HIS A 382     6696   6183   4689   -379   -278     86  A    C  
ATOM   1116  NE2 HIS A 382     -23.236 -26.576  27.307  1.00 46.44      A    N  
ANISOU 1116  NE2 HIS A 382     6729   6214   4702   -419   -258    116  A    N  
ATOM   1117  N   TYR A 383     -17.675 -23.749  29.005  1.00 44.87      A    N  
ANISOU 1117  N   TYR A 383     6649   5979   4418   -233   -198      5  A    N  
ATOM   1118  CA  TYR A 383     -16.554 -24.127  29.883  1.00 47.16      A    C  
ANISOU 1118  CA  TYR A 383     6986   6239   4693   -228   -218      0  A    C  
ATOM   1119  C   TYR A 383     -17.067 -25.320  30.698  1.00 46.25      A    C  
ANISOU 1119  C   TYR A 383     6903   6102   4566   -276   -238     29  A    C  
ATOM   1120  O   TYR A 383     -18.010 -25.194  31.452  1.00 48.17      A    O  
ANISOU 1120  O   TYR A 383     7137   6369   4796   -308   -205     55  A    O  
ATOM   1121  CB  TYR A 383     -16.081 -22.953  30.772  1.00 49.06      A    C  
ANISOU 1121  CB  TYR A 383     7230   6493   4916   -209   -185     -4  A    C  
ATOM   1122  CG  TYR A 383     -15.062 -23.375  31.816  1.00 49.76      A    C  
ANISOU 1122  CG  TYR A 383     7368   6548   4987   -210   -210     -4  A    C  
ATOM   1123  CD1 TYR A 383     -13.755 -23.598  31.470  1.00 49.18      A    C  
ANISOU 1123  CD1 TYR A 383     7308   6448   4927   -182   -247    -25  A    C  
ATOM   1124  CD2 TYR A 383     -15.432 -23.576  33.143  1.00 50.18      A    C  
ANISOU 1124  CD2 TYR A 383     7455   6598   5011   -240   -198     18  A    C  
ATOM   1125  CE1 TYR A 383     -12.837 -24.020  32.397  1.00 50.44      A    C  
ANISOU 1125  CE1 TYR A 383     7512   6576   5077   -183   -279    -25  A    C  
ATOM   1126  CE2 TYR A 383     -14.521 -24.001  34.082  1.00 49.46      A    C  
ANISOU 1126  CE2 TYR A 383     7417   6472   4904   -243   -229     19  A    C  
ATOM   1127  CZ  TYR A 383     -13.216 -24.226  33.707  1.00 50.54      A    C  
ANISOU 1127  CZ  TYR A 383     7564   6578   5059   -213   -273     -2  A    C  
ATOM   1128  OH  TYR A 383     -12.258 -24.646  34.632  1.00 45.94      A    O  
ANISOU 1128  OH  TYR A 383     7031   5957   4465   -213   -313     -2  A    O  
ATOM   1129  N   LYS A 384     -16.502 -26.467  30.509  1.00 47.43      A    N  
ANISOU 1129  N   LYS A 384     7089   6209   4721   -281   -293     24  A    N  
ATOM   1130  CA  LYS A 384     -16.972 -27.622  31.222  1.00 49.39      A    C  
ANISOU 1130  CA  LYS A 384     7375   6428   4960   -332   -324     54  A    C  
ATOM   1131  C   LYS A 384     -18.435 -27.842  30.962  1.00 52.54      A    C  
ANISOU 1131  C   LYS A 384     7741   6852   5366   -381   -307     86  A    C  
ATOM   1132  O   LYS A 384     -18.798 -28.129  29.869  1.00 58.64      A    O  
ANISOU 1132  O   LYS A 384     8490   7627   6164   -380   -326     79  A    O  
ATOM   1133  CB  LYS A 384     -16.609 -27.574  32.679  1.00 48.25      A    C  
ANISOU 1133  CB  LYS A 384     7273   6274   4785   -349   -316     71  A    C  
ATOM   1134  CG  LYS A 384     -15.129 -27.622  32.871  1.00 46.31      A    C  
ANISOU 1134  CG  LYS A 384     7053   6003   4537   -303   -337     42  A    C  
ATOM   1135  CD  LYS A 384     -14.707 -27.603  34.298  1.00 44.64      A    C  
ANISOU 1135  CD  LYS A 384     6895   5770   4294   -322   -344     59  A    C  
ATOM   1136  CE  LYS A 384     -13.248 -27.855  34.359  1.00 44.97      A    C  
ANISOU 1136  CE  LYS A 384     6972   5767   4345   -288   -401     35  A    C  
ATOM   1137  NZ  LYS A 384     -12.622 -26.910  35.280  1.00 46.33      A    N1+
ANISOU 1137  NZ  LYS A 384     7169   5938   4496   -276   -391     33  A    N1+
ATOM   1138  N   ASP A 385     -19.262 -27.838  31.981  1.00 53.17      A    N  
ANISOU 1138  N   ASP A 385     7821   6954   5426   -425   -272    121  A    N  
ATOM   1139  CA  ASP A 385     -20.685 -27.973  31.794  1.00 54.21      A    C  
ANISOU 1139  CA  ASP A 385     7905   7122   5568   -471   -245    155  A    C  
ATOM   1140  C   ASP A 385     -21.437 -26.668  31.850  1.00 50.75      A    C  
ANISOU 1140  C   ASP A 385     7401   6746   5134   -449   -175    150  A    C  
ATOM   1141  O   ASP A 385     -22.619 -26.665  31.835  1.00 51.51      A    O  
ANISOU 1141  O   ASP A 385     7447   6878   5244   -481   -151    176  A    O  
ATOM   1142  CB  ASP A 385     -21.229 -28.847  32.874  1.00 54.83      A    C  
ANISOU 1142  CB  ASP A 385     8017   7192   5623   -538   -247    201  A    C  
ATOM   1143  CG  ASP A 385     -20.982 -30.265  32.628  1.00 58.87      A    C  
ANISOU 1143  CG  ASP A 385     8576   7644   6147   -575   -326    214  A    C  
ATOM   1144  OD1 ASP A 385     -20.791 -30.649  31.511  1.00 55.76      A    O  
ANISOU 1144  OD1 ASP A 385     8175   7228   5782   -551   -370    189  A    O  
ATOM   1145  OD2 ASP A 385     -21.001 -31.045  33.548  1.00 63.22      A    O1-
ANISOU 1145  OD2 ASP A 385     9176   8168   6675   -625   -348    248  A    O1-
ATOM   1146  N   ALA A 386     -20.728 -25.570  31.919  1.00 48.06      A    N  
ANISOU 1146  N   ALA A 386     7059   6415   4785   -394   -151    118  A    N  
ATOM   1147  CA  ALA A 386     -21.299 -24.258  32.099  1.00 48.64      A    C  
ANISOU 1147  CA  ALA A 386     7086   6539   4855   -367    -90    112  A    C  
ATOM   1148  C   ALA A 386     -21.202 -23.456  30.817  1.00 48.26      A    C  
ANISOU 1148  C   ALA A 386     7001   6499   4834   -323    -95     82  A    C  
ATOM   1149  O   ALA A 386     -20.117 -23.176  30.356  1.00 48.96      A    O  
ANISOU 1149  O   ALA A 386     7113   6564   4924   -287   -118     55  A    O  
ATOM   1150  CB  ALA A 386     -20.550 -23.523  33.216  1.00 49.94      A    C  
ANISOU 1150  CB  ALA A 386     7288   6702   4982   -342    -62    101  A    C  
ATOM   1151  N   LYS A 387     -22.345 -23.036  30.295  1.00 49.33      A    N  
ANISOU 1151  N   LYS A 387     7077   6671   4992   -326    -73     90  A    N  
ATOM   1152  CA  LYS A 387     -22.451 -22.307  29.026  1.00 47.50      A    C  
ANISOU 1152  CA  LYS A 387     6813   6448   4787   -290    -82     67  A    C  
ATOM   1153  C   LYS A 387     -21.897 -20.912  29.052  1.00 46.05      A    C  
ANISOU 1153  C   LYS A 387     6628   6274   4593   -238    -55     41  A    C  
ATOM   1154  O   LYS A 387     -21.948 -20.267  30.066  1.00 52.08      A    O  
ANISOU 1154  O   LYS A 387     7396   7055   5335   -227    -16     41  A    O  
ATOM   1155  CB  LYS A 387     -23.916 -22.202  28.638  1.00 48.09      A    C  
ANISOU 1155  CB  LYS A 387     6822   6559   4889   -309    -67     86  A    C  
ATOM   1156  CG  LYS A 387     -24.543 -23.562  28.388  1.00 49.47      A    C  
ANISOU 1156  CG  LYS A 387     6992   6720   5081   -366   -106    115  A    C  
ATOM   1157  CD  LYS A 387     -26.026 -23.433  28.179  1.00 51.47      A    C  
ANISOU 1157  CD  LYS A 387     7173   7017   5366   -390    -88    139  A    C  
ATOM   1158  CE  LYS A 387     -26.619 -24.749  27.713  1.00 53.08      A    C  
ANISOU 1158  CE  LYS A 387     7373   7200   5594   -450   -140    168  A    C  
ATOM   1159  NZ  LYS A 387     -27.694 -24.471  26.711  1.00 53.44      A    N1+
ANISOU 1159  NZ  LYS A 387     7354   7268   5683   -451   -157    173  A    N1+
ATOM   1160  N   TRP A 388     -21.398 -20.449  27.913  1.00 44.41      A    N  
ANISOU 1160  N   TRP A 388     6418   6056   4400   -207    -78     18  A    N  
ATOM   1161  CA  TRP A 388     -20.892 -19.109  27.765  1.00 42.03      A    C  
ANISOU 1161  CA  TRP A 388     6117   5760   4092   -163    -61     -2  A    C  
ATOM   1162  C   TRP A 388     -22.054 -18.210  27.523  1.00 42.84      A    C  
ANISOU 1162  C   TRP A 388     6170   5896   4210   -148    -36      0  A    C  
ATOM   1163  O   TRP A 388     -22.899 -18.529  26.666  1.00 40.85      A    O  
ANISOU 1163  O   TRP A 388     5883   5653   3983   -160    -52      6  A    O  
ATOM   1164  CB  TRP A 388     -20.000 -19.006  26.539  1.00 40.87      A    C  
ANISOU 1164  CB  TRP A 388     5983   5593   3953   -142    -94    -21  A    C  
ATOM   1165  CG  TRP A 388     -18.676 -19.689  26.636  1.00 40.04      A    C  
ANISOU 1165  CG  TRP A 388     5919   5456   3836   -142   -119    -30  A    C  
ATOM   1166  CD1 TRP A 388     -18.338 -20.742  27.432  1.00 39.69      A    C  
ANISOU 1166  CD1 TRP A 388     5905   5392   3783   -166   -132    -21  A    C  
ATOM   1167  CD2 TRP A 388     -17.523 -19.390  25.859  1.00 39.76      A    C  
ANISOU 1167  CD2 TRP A 388     5897   5408   3800   -116   -134    -49  A    C  
ATOM   1168  CE2 TRP A 388     -16.513 -20.292  26.239  1.00 39.29      A    C  
ANISOU 1168  CE2 TRP A 388     5869   5323   3733   -120   -157    -54  A    C  
ATOM   1169  CE3 TRP A 388     -17.251 -18.457  24.864  1.00 39.31      A    C  
ANISOU 1169  CE3 TRP A 388     5827   5360   3746    -92   -132    -60  A    C  
ATOM   1170  NE1 TRP A 388     -17.032 -21.110  27.198  1.00 39.50      A    N  
ANISOU 1170  NE1 TRP A 388     5910   5343   3755   -150   -159    -37  A    N  
ATOM   1171  CZ2 TRP A 388     -15.266 -20.288  25.664  1.00 39.15      A    C  
ANISOU 1171  CZ2 TRP A 388     5863   5296   3717    -97   -172    -71  A    C  
ATOM   1172  CZ3 TRP A 388     -16.007 -18.436  24.323  1.00 40.04      A    C  
ANISOU 1172  CZ3 TRP A 388     5934   5443   3834    -75   -144    -73  A    C  
ATOM   1173  CH2 TRP A 388     -15.020 -19.354  24.724  1.00 40.16      A    C  
ANISOU 1173  CH2 TRP A 388     5972   5439   3846    -76   -161    -80  A    C  
ATOM   1174  N   LEU A 389     -22.065 -17.054  28.213  1.00 42.06      A    N  
ANISOU 1174  N   LEU A 389     6072   5811   4097   -118     -2    -10  A    N  
ATOM   1175  CA  LEU A 389     -23.204 -16.127  28.162  1.00 42.18      A    C  
ANISOU 1175  CA  LEU A 389     6040   5859   4125    -94     24    -12  A    C  
ATOM   1176  C   LEU A 389     -22.839 -14.700  27.711  1.00 41.79      A    C  
ANISOU 1176  C   LEU A 389     6000   5802   4077    -47     20    -35  A    C  
ATOM   1177  O   LEU A 389     -21.807 -14.185  28.044  1.00 37.91      A    O  
ANISOU 1177  O   LEU A 389     5550   5288   3565    -33     16    -47  A    O  
ATOM   1178  CB  LEU A 389     -23.849 -16.067  29.541  1.00 43.90      A    C  
ANISOU 1178  CB  LEU A 389     6248   6106   4322    -97     73     -3  A    C  
ATOM   1179  CG  LEU A 389     -25.018 -16.973  29.875  1.00 45.37      A    C  
ANISOU 1179  CG  LEU A 389     6390   6327   4521   -136     94     24  A    C  
ATOM   1180  CD1 LEU A 389     -24.788 -18.437  29.517  1.00 46.27      A    C  
ANISOU 1180  CD1 LEU A 389     6517   6417   4643   -190     56     45  A    C  
ATOM   1181  CD2 LEU A 389     -25.366 -16.796  31.341  1.00 45.85      A    C  
ANISOU 1181  CD2 LEU A 389     6455   6416   4547   -135    151     31  A    C  
ATOM   1182  N   SER A 390     -23.727 -14.060  26.966  1.00 45.20      A    N  
ANISOU 1182  N   SER A 390     6391   6250   4533    -26     16    -39  A    N  
ATOM   1183  CA  SER A 390     -23.542 -12.681  26.522  1.00 47.43      A    C  
ANISOU 1183  CA  SER A 390     6682   6521   4816     15      7    -57  A    C  
ATOM   1184  C   SER A 390     -24.702 -11.940  27.098  1.00 48.20      A    C  
ANISOU 1184  C   SER A 390     6742   6649   4920     48     39    -63  A    C  
ATOM   1185  O   SER A 390     -25.566 -12.551  27.741  1.00 51.12      A    O  
ANISOU 1185  O   SER A 390     7074   7052   5294     33     70    -51  A    O  
ATOM   1186  CB  SER A 390     -23.653 -12.574  24.995  1.00 51.80      A    C  
ANISOU 1186  CB  SER A 390     7224   7063   5392     16    -33    -57  A    C  
ATOM   1187  OG  SER A 390     -25.035 -12.557  24.618  1.00 53.52      A    O  
ANISOU 1187  OG  SER A 390     7385   7307   5640     22    -33    -51  A    O  
ATOM   1188  N   SER A 391     -24.765 -10.644  26.808  1.00 46.80      A    N  
ANISOU 1188  N   SER A 391     6572   6462   4747     92     29    -80  A    N  
ATOM   1189  CA  SER A 391     -25.880  -9.808  27.251  1.00 46.20      A    C  
ANISOU 1189  CA  SER A 391     6460   6414   4681    136     55    -93  A    C  
ATOM   1190  C   SER A 391     -27.159 -10.175  26.564  1.00 46.73      A    C  
ANISOU 1190  C   SER A 391     6454   6511   4788    132     50    -82  A    C  
ATOM   1191  O   SER A 391     -28.221  -9.719  26.971  1.00 48.95      A    O  
ANISOU 1191  O   SER A 391     6688   6826   5084    165     77    -89  A    O  
ATOM   1192  CB  SER A 391     -25.595  -8.303  27.032  1.00 47.01      A    C  
ANISOU 1192  CB  SER A 391     6596   6488   4779    187     33   -116  A    C  
ATOM   1193  OG  SER A 391     -25.255  -7.947  25.693  1.00 42.00      A    O  
ANISOU 1193  OG  SER A 391     5973   5824   4160    183    -16   -112  A    O  
ATOM   1194  N   LYS A 392     -27.078 -10.974  25.498  1.00 47.74      A    N  
ANISOU 1194  N   LYS A 392     6573   6628   4935     94     12    -66  A    N  
ATOM   1195  CA  LYS A 392     -28.276 -11.352  24.756  1.00 46.85      A    C  
ANISOU 1195  CA  LYS A 392     6396   6539   4865     85     -4    -54  A    C  
ATOM   1196  C   LYS A 392     -28.399 -12.846  24.591  1.00 46.55      A    C  
ANISOU 1196  C   LYS A 392     6341   6508   4836     25    -12    -29  A    C  
ATOM   1197  O   LYS A 392     -29.109 -13.299  23.713  1.00 50.85      A    O  
ANISOU 1197  O   LYS A 392     6849   7057   5414      7    -46    -17  A    O  
ATOM   1198  CB  LYS A 392     -28.265 -10.693  23.392  1.00 48.25      A    C  
ANISOU 1198  CB  LYS A 392     6582   6688   5059    104    -58    -61  A    C  
ATOM   1199  CG  LYS A 392     -28.139  -9.188  23.445  1.00 49.43      A    C  
ANISOU 1199  CG  LYS A 392     6756   6822   5201    161    -63    -84  A    C  
ATOM   1200  CD  LYS A 392     -29.492  -8.533  23.352  1.00 52.40      A    C  
ANISOU 1200  CD  LYS A 392     7070   7224   5615    203    -64    -92  A    C  
ATOM   1201  CE  LYS A 392     -29.418  -7.079  23.793  1.00 55.25      A    C  
ANISOU 1201  CE  LYS A 392     7457   7570   5963    267    -60   -118  A    C  
ATOM   1202  NZ  LYS A 392     -30.482  -6.270  23.124  1.00 56.97      A    N1+
ANISOU 1202  NZ  LYS A 392     7633   7790   6220    313    -93   -129  A    N1+
ATOM   1203  N   GLY A 393     -27.706 -13.616  25.418  1.00 45.70      A    N  
ANISOU 1203  N   GLY A 393     6266   6396   4699     -5     10    -21  A    N  
ATOM   1204  CA  GLY A 393     -27.870 -15.052  25.443  1.00 43.99      A    C  
ANISOU 1204  CA  GLY A 393     6039   6183   4490    -62      1      3  A    C  
ATOM   1205  C   GLY A 393     -26.613 -15.831  25.098  1.00 42.79      A    C  
ANISOU 1205  C   GLY A 393     5951   5990   4316    -88    -28      3  A    C  
ATOM   1206  O   GLY A 393     -25.560 -15.268  24.795  1.00 40.80      A    O  
ANISOU 1206  O   GLY A 393     5747   5711   4044    -65    -40    -14  A    O  
ATOM   1207  N   GLU A 394     -26.776 -17.148  25.104  1.00 42.96      A    N  
ANISOU 1207  N   GLU A 394     5970   6008   4344   -138    -44     24  A    N  
ATOM   1208  CA  GLU A 394     -25.695 -18.086  24.949  1.00 43.95      A    C  
ANISOU 1208  CA  GLU A 394     6152   6096   4449   -162    -71     23  A    C  
ATOM   1209  C   GLU A 394     -24.925 -17.959  23.611  1.00 44.43      A    C  
ANISOU 1209  C   GLU A 394     6246   6124   4508   -144   -116      5  A    C  
ATOM   1210  O   GLU A 394     -25.464 -17.581  22.572  1.00 41.84      A    O  
ANISOU 1210  O   GLU A 394     5898   5797   4199   -132   -142      1  A    O  
ATOM   1211  CB  GLU A 394     -26.207 -19.520  25.132  1.00 47.00      A    C  
ANISOU 1211  CB  GLU A 394     6529   6481   4847   -219    -89     51  A    C  
ATOM   1212  CG  GLU A 394     -26.895 -20.084  23.880  1.00 49.64      A    C  
ANISOU 1212  CG  GLU A 394     6841   6805   5215   -239   -143     58  A    C  
ATOM   1213  CD  GLU A 394     -27.785 -21.290  24.126  1.00 50.75      A    C  
ANISOU 1213  CD  GLU A 394     6954   6952   5377   -299   -160     92  A    C  
ATOM   1214  OE1 GLU A 394     -27.473 -22.142  24.950  1.00 52.94      A    O  
ANISOU 1214  OE1 GLU A 394     7257   7219   5637   -334   -153    108  A    O  
ATOM   1215  OE2 GLU A 394     -28.816 -21.410  23.454  1.00 58.87      A    O1-
ANISOU 1215  OE2 GLU A 394     7933   7991   6441   -315   -187    106  A    O1-
ATOM   1216  N   ILE A 395     -23.631 -18.287  23.677  1.00 45.44      A    N  
ANISOU 1216  N   ILE A 395     6427   6225   4610   -142   -123     -5  A    N  
ATOM   1217  CA  ILE A 395     -22.741 -18.178  22.543  1.00 44.31      A    C  
ANISOU 1217  CA  ILE A 395     6318   6058   4457   -124   -153    -22  A    C  
ATOM   1218  C   ILE A 395     -22.968 -19.427  21.704  1.00 46.32      A    C  
ANISOU 1218  C   ILE A 395     6583   6294   4721   -150   -198    -18  A    C  
ATOM   1219  O   ILE A 395     -22.927 -20.562  22.229  1.00 47.28      A    O  
ANISOU 1219  O   ILE A 395     6718   6403   4841   -181   -209     -7  A    O  
ATOM   1220  CB  ILE A 395     -21.266 -18.077  23.004  1.00 43.36      A    C  
ANISOU 1220  CB  ILE A 395     6241   5922   4311   -111   -142    -35  A    C  
ATOM   1221  CG1 ILE A 395     -21.024 -16.793  23.817  1.00 41.30      A    C  
ANISOU 1221  CG1 ILE A 395     5978   5673   4040    -86   -107    -40  A    C  
ATOM   1222  CG2 ILE A 395     -20.316 -18.117  21.812  1.00 44.25      A    C  
ANISOU 1222  CG2 ILE A 395     6382   6017   4412    -95   -167    -51  A    C  
ATOM   1223  CD1 ILE A 395     -21.329 -15.491  23.102  1.00 41.54      A    C  
ANISOU 1223  CD1 ILE A 395     5995   5711   4078    -57   -107    -47  A    C  
ATOM   1224  N   THR A 396     -23.236 -19.206  20.414  1.00 47.02      A    N  
ANISOU 1224  N   THR A 396     6672   6378   4816   -138   -229    -25  A    N  
ATOM   1225  CA  THR A 396     -23.539 -20.287  19.457  1.00 47.35      A    C  
ANISOU 1225  CA  THR A 396     6729   6397   4863   -158   -280    -24  A    C  
ATOM   1226  C   THR A 396     -22.375 -20.591  18.478  1.00 46.06      A    C  
ANISOU 1226  C   THR A 396     6620   6209   4670   -136   -302    -47  A    C  
ATOM   1227  O   THR A 396     -21.468 -19.789  18.244  1.00 43.20      A    O  
ANISOU 1227  O   THR A 396     6274   5853   4287   -107   -280    -61  A    O  
ATOM   1228  CB  THR A 396     -24.866 -19.998  18.686  1.00 48.14      A    C  
ANISOU 1228  CB  THR A 396     6791   6507   4992   -165   -308    -13  A    C  
ATOM   1229  CG2 THR A 396     -26.015 -19.880  19.689  1.00 47.83      A    C  
ANISOU 1229  CG2 THR A 396     6689   6498   4985   -187   -283      9  A    C  
ATOM   1230  OG1 THR A 396     -24.766 -18.762  17.920  1.00 48.89      A    O  
ANISOU 1230  OG1 THR A 396     6886   6609   5081   -129   -305    -25  A    O  
ATOM   1231  N   CYS A 397     -22.406 -21.792  17.938  1.00 46.72      A    N  
ANISOU 1231  N   CYS A 397     6733   6266   4751   -152   -346    -51  A    N  
ATOM   1232  CA  CYS A 397     -21.449 -22.203  16.933  1.00 47.19      A    C  
ANISOU 1232  CA  CYS A 397     6843   6305   4780   -126   -367    -76  A    C  
ATOM   1233  C   CYS A 397     -22.206 -23.035  15.947  1.00 50.21      A    C  
ANISOU 1233  C   CYS A 397     7246   6663   5167   -141   -427    -77  A    C  
ATOM   1234  O   CYS A 397     -22.999 -23.894  16.381  1.00 51.60      A    O  
ANISOU 1234  O   CYS A 397     7412   6826   5368   -179   -456    -59  A    O  
ATOM   1235  CB  CYS A 397     -20.373 -23.062  17.541  1.00 46.37      A    C  
ANISOU 1235  CB  CYS A 397     6771   6184   4661   -122   -363    -88  A    C  
ATOM   1236  SG  CYS A 397     -19.038 -23.394  16.393  1.00 47.11      A    S  
ANISOU 1236  SG  CYS A 397     6917   6265   4716    -77   -374   -123  A    S  
ATOM   1237  N   PRO A 398     -21.988 -22.793  14.629  1.00 53.81      A    N  
ANISOU 1237  N   PRO A 398     7733   7113   5598   -115   -447    -94  A    N  
ATOM   1238  CA  PRO A 398     -22.782 -23.530  13.623  1.00 55.70      A    C  
ANISOU 1238  CA  PRO A 398     7998   7325   5840   -129   -513    -96  A    C  
ATOM   1239  C   PRO A 398     -22.527 -25.046  13.600  1.00 55.80      A    C  
ANISOU 1239  C   PRO A 398     8058   7297   5844   -139   -558   -107  A    C  
ATOM   1240  O   PRO A 398     -23.308 -25.783  12.993  1.00 55.06      A    O  
ANISOU 1240  O   PRO A 398     7985   7174   5760   -161   -621   -104  A    O  
ATOM   1241  CB  PRO A 398     -22.399 -22.861  12.289  1.00 54.90      A    C  
ANISOU 1241  CB  PRO A 398     7931   7227   5701    -93   -517   -114  A    C  
ATOM   1242  CG  PRO A 398     -21.883 -21.511  12.683  1.00 55.44      A    C  
ANISOU 1242  CG  PRO A 398     7969   7330   5766    -75   -456   -109  A    C  
ATOM   1243  CD  PRO A 398     -21.216 -21.692  14.016  1.00 53.60      A    C  
ANISOU 1243  CD  PRO A 398     7716   7107   5543    -80   -414   -107  A    C  
ATOM   1244  N   LEU A 399     -21.468 -25.497  14.260  1.00 54.40      A    N  
ANISOU 1244  N   LEU A 399     7900   7116   5654   -125   -534   -120  A    N  
ATOM   1245  CA  LEU A 399     -21.182 -26.921  14.375  1.00 58.61      A    C  
ANISOU 1245  CA  LEU A 399     8480   7606   6180   -131   -579   -132  A    C  
ATOM   1246  C   LEU A 399     -22.025 -27.509  15.498  1.00 60.23      A    C  
ANISOU 1246  C   LEU A 399     8657   7801   6425   -188   -595    -98  A    C  
ATOM   1247  O   LEU A 399     -22.416 -26.798  16.406  1.00 62.76      A    O  
ANISOU 1247  O   LEU A 399     8922   8154   6767   -208   -551    -73  A    O  
ATOM   1248  CB  LEU A 399     -19.700 -27.151  14.644  1.00 58.94      A    C  
ANISOU 1248  CB  LEU A 399     8551   7647   6195    -89   -550   -160  A    C  
ATOM   1249  CG  LEU A 399     -18.779 -26.317  13.758  1.00 62.78      A    C  
ANISOU 1249  CG  LEU A 399     9045   8161   6645    -39   -511   -185  A    C  
ATOM   1250  CD1 LEU A 399     -17.314 -26.460  14.180  1.00 60.49      A    C  
ANISOU 1250  CD1 LEU A 399     8764   7879   6338     -1   -475   -207  A    C  
ATOM   1251  CD2 LEU A 399     -19.026 -26.666  12.281  1.00 62.16      A    C  
ANISOU 1251  CD2 LEU A 399     9016   8063   6535    -19   -555   -206  A    C  
ATOM   1252  N   GLU A 400     -22.304 -28.807  15.435  1.00 66.79      A    N  
ANISOU 1252  N   GLU A 400     9529   8586   7262   -213   -659    -96  A    N  
ATOM   1253  CA  GLU A 400     -23.165 -29.453  16.431  1.00 71.15      A    C  
ANISOU 1253  CA  GLU A 400    10057   9126   7849   -277   -680    -57  A    C  
ATOM   1254  C   GLU A 400     -22.282 -29.744  17.638  1.00 68.36      A    C  
ANISOU 1254  C   GLU A 400     9714   8772   7488   -274   -647    -56  A    C  
ATOM   1255  O   GLU A 400     -22.536 -29.237  18.718  1.00 63.68      A    O  
ANISOU 1255  O   GLU A 400     9074   8210   6910   -299   -599    -30  A    O  
ATOM   1256  CB  GLU A 400     -23.865 -30.725  15.893  1.00 77.73      A    C  
ANISOU 1256  CB  GLU A 400    10934   9905   8694   -315   -771    -49  A    C  
ATOM   1257  CG  GLU A 400     -24.458 -30.653  14.452  1.00 79.26      A    C  
ANISOU 1257  CG  GLU A 400    11147  10084   8883   -304   -823    -63  A    C  
ATOM   1258  CD  GLU A 400     -25.714 -29.775  14.293  1.00 82.46      A    C  
ANISOU 1258  CD  GLU A 400    11479  10527   9325   -335   -814    -32  A    C  
ATOM   1259  OE1 GLU A 400     -26.091 -29.035  15.239  1.00 83.56      A    O  
ANISOU 1259  OE1 GLU A 400    11546  10712   9489   -355   -754     -5  A    O  
ATOM   1260  OE2 GLU A 400     -26.328 -29.817  13.199  1.00 79.73      A    O1-
ANISOU 1260  OE2 GLU A 400    11149  10163   8981   -337   -869    -37  A    O1-
ATOM   1261  N   GLN A 401     -21.225 -30.520  17.418  1.00 69.47      A    N  
ANISOU 1261  N   GLN A 401     9916   8874   7602   -239   -674    -88  A    N  
ATOM   1262  CA  GLN A 401     -20.169 -30.772  18.406  1.00 67.47      A    C  
ANISOU 1262  CA  GLN A 401     9679   8615   7339   -223   -650    -96  A    C  
ATOM   1263  C   GLN A 401     -18.886 -30.067  17.948  1.00 66.50      A    C  
ANISOU 1263  C   GLN A 401     9560   8517   7190   -153   -606   -135  A    C  
ATOM   1264  O   GLN A 401     -18.867 -29.499  16.851  1.00 66.29      A    O  
ANISOU 1264  O   GLN A 401     9531   8508   7148   -122   -597   -154  A    O  
ATOM   1265  CB  GLN A 401     -19.923 -32.277  18.561  1.00 70.06      A    C  
ANISOU 1265  CB  GLN A 401    10074   8879   7664   -234   -721   -102  A    C  
ATOM   1266  CG  GLN A 401     -21.137 -33.065  19.055  1.00 73.97      A    C  
ANISOU 1266  CG  GLN A 401    10569   9347   8186   -313   -770    -57  A    C  
ATOM   1267  CD  GLN A 401     -21.607 -32.638  20.455  1.00 78.47      A    C  
ANISOU 1267  CD  GLN A 401    11086   9952   8774   -364   -719    -12  A    C  
ATOM   1268  NE2 GLN A 401     -22.928 -32.740  20.696  1.00 76.42      A    N  
ANISOU 1268  NE2 GLN A 401    10788   9703   8543   -432   -730     32  A    N  
ATOM   1269  OE1 GLN A 401     -20.793 -32.215  21.309  1.00 77.20      A    O  
ANISOU 1269  OE1 GLN A 401    10919   9810   8602   -342   -671    -17  A    O  
ATOM   1270  N   GLY A 402     -17.836 -30.071  18.787  1.00 62.43      A    N  
ANISOU 1270  N   GLY A 402     9048   8004   6669   -131   -579   -144  A    N  
ATOM   1271  CA  GLY A 402     -16.559 -29.399  18.439  1.00 59.49      A    C  
ANISOU 1271  CA  GLY A 402     8668   7657   6275    -70   -536   -176  A    C  
ATOM   1272  C   GLY A 402     -15.682 -28.960  19.611  1.00 54.46      A    C  
ANISOU 1272  C   GLY A 402     8010   7037   5644    -63   -495   -171  A    C  
ATOM   1273  O   GLY A 402     -16.130 -28.969  20.738  1.00 54.85      A    O  
ANISOU 1273  O   GLY A 402     8047   7084   5708   -105   -490   -141  A    O  
ATOM   1274  N   THR A 403     -14.434 -28.593  19.312  1.00 51.84      A    N  
ANISOU 1274  N   THR A 403     7674   6723   5298    -11   -469   -199  A    N  
ATOM   1275  CA  THR A 403     -13.449 -28.099  20.272  1.00 50.95      A    C  
ANISOU 1275  CA  THR A 403     7539   6626   5191      0   -435   -198  A    C  
ATOM   1276  C   THR A 403     -13.004 -26.662  19.982  1.00 50.01      A    C  
ANISOU 1276  C   THR A 403     7375   6558   5068     17   -376   -197  A    C  
ATOM   1277  O   THR A 403     -12.940 -26.246  18.842  1.00 53.43      A    O  
ANISOU 1277  O   THR A 403     7802   7012   5486     41   -361   -211  A    O  
ATOM   1278  CB  THR A 403     -12.210 -28.998  20.255  1.00 52.02      A    C  
ANISOU 1278  CB  THR A 403     7706   6737   5323     47   -463   -231  A    C  
ATOM   1279  CG2 THR A 403     -12.585 -30.390  20.697  1.00 52.64      A    C  
ANISOU 1279  CG2 THR A 403     7836   6757   5407     27   -529   -228  A    C  
ATOM   1280  OG1 THR A 403     -11.668 -29.058  18.923  1.00 54.10      A    O  
ANISOU 1280  OG1 THR A 403     7976   7013   5566     99   -458   -266  A    O  
ATOM   1281  N   ILE A 404     -12.619 -25.929  21.020  1.00 51.23      A    N  
ANISOU 1281  N   ILE A 404     7503   6727   5232      6   -346   -181  A    N  
ATOM   1282  CA  ILE A 404     -12.496 -24.481  20.946  1.00 48.70      A    C  
ANISOU 1282  CA  ILE A 404     7144   6448   4912      7   -298   -171  A    C  
ATOM   1283  C   ILE A 404     -11.042 -24.127  20.914  1.00 49.76      A    C  
ANISOU 1283  C   ILE A 404     7263   6598   5045     42   -279   -187  A    C  
ATOM   1284  O   ILE A 404     -10.271 -24.588  21.744  1.00 52.10      A    O  
ANISOU 1284  O   ILE A 404     7565   6876   5351     50   -294   -192  A    O  
ATOM   1285  CB  ILE A 404     -13.196 -23.802  22.147  1.00 49.47      A    C  
ANISOU 1285  CB  ILE A 404     7225   6549   5019    -30   -279   -142  A    C  
ATOM   1286  CG1 ILE A 404     -14.701 -23.866  21.963  1.00 50.56      A    C  
ANISOU 1286  CG1 ILE A 404     7359   6687   5161    -62   -285   -123  A    C  
ATOM   1287  CG2 ILE A 404     -12.745 -22.352  22.355  1.00 49.70      A    C  
ANISOU 1287  CG2 ILE A 404     7224   6608   5049    -24   -238   -135  A    C  
ATOM   1288  CD1 ILE A 404     -15.503 -23.419  23.158  1.00 51.70      A    C  
ANISOU 1288  CD1 ILE A 404     7489   6839   5313    -97   -265    -96  A    C  
ATOM   1289  N   SER A 405     -10.674 -23.298  19.953  1.00 48.89      A    N  
ANISOU 1289  N   SER A 405     7130   6520   4923     60   -248   -193  A    N  
ATOM   1290  CA  SER A 405      -9.338 -22.809  19.835  1.00 49.52      A    C  
ANISOU 1290  CA  SER A 405     7185   6625   5005     87   -224   -202  A    C  
ATOM   1291  C   SER A 405      -9.405 -21.328  19.495  1.00 52.25      A    C  
ANISOU 1291  C   SER A 405     7502   7004   5346     72   -186   -182  A    C  
ATOM   1292  O   SER A 405     -10.511 -20.786  19.439  1.00 53.02      A    O  
ANISOU 1292  O   SER A 405     7604   7101   5441     48   -183   -166  A    O  
ATOM   1293  CB  SER A 405      -8.611 -23.582  18.750  1.00 51.07      A    C  
ANISOU 1293  CB  SER A 405     7389   6829   5184    132   -228   -233  A    C  
ATOM   1294  OG  SER A 405      -9.214 -23.376  17.463  1.00 55.91      A    O  
ANISOU 1294  OG  SER A 405     8013   7457   5770    136   -218   -237  A    O  
ATOM   1295  OXT SER A 405      -8.385 -20.651  19.280  1.00 55.21      A    O1-
ANISOU 1295  OXT SER A 405     7849   7405   5721     83   -161   -181  A    O1-
TER   
END



If you find results from this site helpful for your research, please cite one of our papers:

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