CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***    ***

elNémo ID: 2409191743171092467

Job options:

ID        	=	 2409191743171092467
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   PRO A  46     -52.823  71.892 -29.980  1.00115.82           N  
ANISOU    1  N   PRO A  46    11451  18564  13992   2392  -1965   -978       N  
ATOM      2  CA  PRO A  46     -51.931  72.146 -31.118  1.00105.67           C  
ANISOU    2  CA  PRO A  46    10322  17275  12551   2534  -1999   -899       C  
ATOM      3  C   PRO A  46     -50.592  72.699 -30.641  1.00 98.92           C  
ANISOU    3  C   PRO A  46     9703  16190  11693   2492  -1868   -704       C  
ATOM      4  O   PRO A  46     -50.405  73.917 -30.638  1.00 95.12           O  
ANISOU    4  O   PRO A  46     9332  15670  11139   2650  -1814   -563       O  
ATOM      5  CB  PRO A  46     -52.681  73.220 -31.922  1.00 75.41           C  
ANISOU    5  CB  PRO A  46     6456  13621   8575   2826  -2072   -877       C  
ATOM      6  CG  PRO A  46     -54.075  73.268 -31.342  1.00 87.15           C  
ANISOU    6  CG  PRO A  46     7726  15241  10147   2821  -2107   -993       C  
ATOM      7  CD  PRO A  46     -53.923  72.868 -29.916  1.00 93.17           C  
ANISOU    7  CD  PRO A  46     8478  15831  11090   2570  -1993   -979       C  
ATOM      8  N   PHE A  47     -49.675  71.818 -30.246  1.00 69.14           N  
ANISOU    8  N   PHE A  47     6004  12268   7999   2285  -1816   -701       N  
ATOM      9  CA  PHE A  47     -48.422  72.241 -29.624  1.00 55.16           C  
ANISOU    9  CA  PHE A  47     4433  10277   6249   2214  -1689   -538       C  
ATOM     10  C   PHE A  47     -47.610  73.177 -30.509  1.00 78.66           C  
ANISOU   10  C   PHE A  47     7587  13223   9079   2406  -1672   -400       C  
ATOM     11  O   PHE A  47     -47.343  72.866 -31.669  1.00 75.79           O  
ANISOU   11  O   PHE A  47     7252  12935   8611   2496  -1745   -431       O  
ATOM     12  CB  PHE A  47     -47.576  71.037 -29.209  1.00 67.25           C  
ANISOU   12  CB  PHE A  47     6004  11675   7871   1980  -1653   -572       C  
ATOM     13  CG  PHE A  47     -46.694  71.302 -28.019  1.00 47.90           C  
ANISOU   13  CG  PHE A  47     3681   9014   5504   1848  -1519   -449       C  
ATOM     14  CD1 PHE A  47     -47.233  71.372 -26.744  1.00 48.09           C  
ANISOU   14  CD1 PHE A  47     3634   8991   5648   1740  -1456   -456       C  
ATOM     15  CD2 PHE A  47     -45.328  71.482 -28.173  1.00 62.97           C  
ANISOU   15  CD2 PHE A  47     5777  10778   7371   1835  -1457   -334       C  
ATOM     16  CE1 PHE A  47     -46.433  71.617 -25.651  1.00 55.82           C  
ANISOU   16  CE1 PHE A  47     4727   9789   6695   1629  -1341   -352       C  
ATOM     17  CE2 PHE A  47     -44.520  71.725 -27.079  1.00 45.26           C  
ANISOU   17  CE2 PHE A  47     3640   8355   5203   1718  -1342   -235       C  
ATOM     18  CZ  PHE A  47     -45.073  71.793 -25.817  1.00 61.51           C  
ANISOU   18  CZ  PHE A  47     5626  10373   7371   1618  -1287   -245       C  
ATOM     19  N   PRO A  48     -47.214  74.329 -29.949  1.00 81.78           N  
ANISOU   19  N   PRO A  48     8102  13501   9469   2467  -1566   -249       N  
ATOM     20  CA  PRO A  48     -46.523  75.433 -30.625  1.00 71.15           C  
ANISOU   20  CA  PRO A  48     6928  12107   8000   2658  -1518   -102       C  
ATOM     21  C   PRO A  48     -45.014  75.245 -30.721  1.00 71.03           C  
ANISOU   21  C   PRO A  48     7091  11915   7981   2569  -1443    -13       C  
ATOM     22  O   PRO A  48     -44.285  76.236 -30.710  1.00 70.68           O  
ANISOU   22  O   PRO A  48     7200  11757   7898   2652  -1348    127       O  
ATOM     23  CB  PRO A  48     -46.820  76.639 -29.719  1.00 60.57           C  
ANISOU   23  CB  PRO A  48     5617  10700   6699   2715  -1422      2       C  
ATOM     24  CG  PRO A  48     -47.826  76.157 -28.703  1.00 66.06           C  
ANISOU   24  CG  PRO A  48     6134  11444   7521   2580  -1441   -103       C  
ATOM     25  CD  PRO A  48     -47.591  74.696 -28.579  1.00 68.25           C  
ANISOU   25  CD  PRO A  48     6347  11709   7876   2368  -1484   -220       C  
ATOM     26  N   TRP A  49     -44.550  74.004 -30.807  1.00 63.25           N  
ANISOU   26  N   TRP A  49     6086  10906   7041   2403  -1479    -96       N  
ATOM     27  CA  TRP A  49     -43.116  73.750 -30.923  1.00 72.36           C  
ANISOU   27  CA  TRP A  49     7399  11901   8192   2318  -1413    -22       C  
ATOM     28  C   TRP A  49     -42.823  72.316 -31.350  1.00 87.42           C  
ANISOU   28  C   TRP A  49     9264  13833  10120   2184  -1482   -135       C  
ATOM     29  O   TRP A  49     -43.291  71.368 -30.724  1.00 79.28           O  
ANISOU   29  O   TRP A  49     8113  12818   9191   2021  -1510   -242       O  
ATOM     30  CB  TRP A  49     -42.401  74.058 -29.605  1.00 56.50           C  
ANISOU   30  CB  TRP A  49     5469   9702   6295   2169  -1287     65       C  
ATOM     31  CG  TRP A  49     -40.923  74.056 -29.753  1.00 58.15           C  
ANISOU   31  CG  TRP A  49     5845   9755   6492   2117  -1213    153       C  
ATOM     32  CD1 TRP A  49     -40.063  73.054 -29.411  1.00 57.18           C  
ANISOU   32  CD1 TRP A  49     5755   9534   6436   1931  -1195    125       C  
ATOM     33  CD2 TRP A  49     -40.124  75.097 -30.320  1.00 79.34           C  
ANISOU   33  CD2 TRP A  49     8685  12366   9093   2259  -1142    282       C  
ATOM     34  CE2 TRP A  49     -38.783  74.664 -30.278  1.00 79.89           C  
ANISOU   34  CE2 TRP A  49     8868  12296   9190   2141  -1086    319       C  
ATOM     35  CE3 TRP A  49     -40.412  76.357 -30.854  1.00 69.90           C  
ANISOU   35  CE3 TRP A  49     7548  11206   7806   2479  -1114    370       C  
ATOM     36  NE1 TRP A  49     -38.773  73.413 -29.718  1.00 70.51           N  
ANISOU   36  NE1 TRP A  49     7602  11098   8090   1945  -1123    223       N  
ATOM     37  CZ2 TRP A  49     -37.730  75.446 -30.748  1.00 53.35           C  
ANISOU   37  CZ2 TRP A  49     5667   8830   5775   2226  -1002    435       C  
ATOM     38  CZ3 TRP A  49     -39.366  77.132 -31.320  1.00 75.09           C  
ANISOU   38  CZ3 TRP A  49     8375  11750   8407   2566  -1023    492       C  
ATOM     39  CH2 TRP A  49     -38.042  76.673 -31.264  1.00 59.79           C  
ANISOU   39  CH2 TRP A  49     6539   9674   6506   2436   -968    520       C  
ATOM     40  N   ASN A  50     -42.033  72.159 -32.405  1.00 83.18           N  
ANISOU   40  N   ASN A  50     8829  13289   9488   2254  -1501   -108       N  
ATOM     41  CA  ASN A  50     -41.774  70.829 -32.938  1.00 63.11           C  
ANISOU   41  CA  ASN A  50     6249  10779   6952   2149  -1571   -216       C  
ATOM     42  C   ASN A  50     -40.296  70.442 -32.990  1.00 70.96           C  
ANISOU   42  C   ASN A  50     7395  11608   7957   2047  -1500   -147       C  
ATOM     43  O   ASN A  50     -39.868  69.735 -33.905  1.00 86.71           O  
ANISOU   43  O   ASN A  50     9416  13634   9896   2054  -1552   -192       O  
ATOM     44  CB  ASN A  50     -42.415  70.675 -34.324  1.00 84.75           C  
ANISOU   44  CB  ASN A  50     8925  13712   9562   2324  -1696   -301       C  
ATOM     45  CG  ASN A  50     -41.862  71.654 -35.331  1.00140.18           C  
ANISOU   45  CG  ASN A  50    16094  20735  16435   2544  -1675   -182       C  
ATOM     46  ND2 ASN A  50     -42.689  72.066 -36.284  1.00150.12           N  
ANISOU   46  ND2 ASN A  50    17298  22173  17568   2759  -1766   -219       N  
ATOM     47  OD1 ASN A  50     -40.701  72.035 -35.254  1.00159.81           O  
ANISOU   47  OD1 ASN A  50    18740  23062  18917   2524  -1575    -61       O  
ATOM     48  N   LYS A  51     -39.518  70.892 -32.009  1.00 39.65           N  
ANISOU   48  N   LYS A  51     3525   7475   4066   1954  -1385    -44       N  
ATOM     49  CA  LYS A  51     -38.105  70.530 -31.953  1.00 57.60           C  
ANISOU   49  CA  LYS A  51     5930   9593   6360   1851  -1316     15       C  
ATOM     50  C   LYS A  51     -37.702  70.032 -30.575  1.00 59.71           C  
ANISOU   50  C   LYS A  51     6193   9730   6764   1638  -1248     15       C  
ATOM     51  O   LYS A  51     -38.170  70.550 -29.562  1.00 51.13           O  
ANISOU   51  O   LYS A  51     5066   8617   5743   1607  -1204     39       O  
ATOM     52  CB  LYS A  51     -37.220  71.714 -32.334  1.00 50.58           C  
ANISOU   52  CB  LYS A  51     5201   8615   5400   1980  -1231    158       C  
ATOM     53  CG  LYS A  51     -37.734  72.544 -33.493  1.00 81.63           C  
ANISOU   53  CG  LYS A  51     9154  12668   9195   2225  -1273    189       C  
ATOM     54  CD  LYS A  51     -36.694  73.566 -33.911  1.00 96.57           C  
ANISOU   54  CD  LYS A  51    11221  14446  11024   2336  -1171    332       C  
ATOM     55  CE  LYS A  51     -37.268  74.589 -34.872  1.00 92.95           C  
ANISOU   55  CE  LYS A  51    10796  14090  10430   2596  -1187    387       C  
ATOM     56  NZ  LYS A  51     -36.205  75.493 -35.387  1.00106.81           N1+
ANISOU   56  NZ  LYS A  51    12732  15726  12125   2704  -1077    523       N1+
ATOM     57  N   ILE A  52     -36.824  69.032 -30.545  1.00 58.23           N  
ANISOU   57  N   ILE A  52     6049   9462   6614   1503  -1236     -8       N  
ATOM     58  CA  ILE A  52     -36.312  68.490 -29.292  1.00 60.62           C  
ANISOU   58  CA  ILE A  52     6364   9638   7032   1313  -1170     -3       C  
ATOM     59  C   ILE A  52     -35.549  69.569 -28.526  1.00 58.86           C  
ANISOU   59  C   ILE A  52     6247   9286   6833   1319  -1063    119       C  
ATOM     60  O   ILE A  52     -35.606  69.637 -27.294  1.00 48.65           O  
ANISOU   60  O   ILE A  52     4934   7926   5626   1217  -1010    132       O  
ATOM     61  CB  ILE A  52     -35.391  67.272 -29.543  1.00 58.80           C  
ANISOU   61  CB  ILE A  52     6179   9343   6820   1194  -1174    -38       C  
ATOM     62  CG1 ILE A  52     -36.147  66.170 -30.294  1.00 89.31           C  
ANISOU   62  CG1 ILE A  52     9934  13332  10669   1180  -1278   -170       C  
ATOM     63  CG2 ILE A  52     -34.841  66.726 -28.230  1.00 37.53           C  
ANISOU   63  CG2 ILE A  52     3504   6521   4234   1015  -1104    -26       C  
ATOM     64  CD1 ILE A  52     -36.744  65.100 -29.391  1.00 95.36           C  
ANISOU   64  CD1 ILE A  52    10591  14097  11545   1014  -1286   -265       C  
ATOM     65  N   ARG A  53     -34.841  70.417 -29.268  1.00 54.76           N  
ANISOU   65  N   ARG A  53     5837   8733   6236   1442  -1028    206       N  
ATOM     66  CA  ARG A  53     -34.111  71.535 -28.679  1.00 60.12           C  
ANISOU   66  CA  ARG A  53     6615   9293   6935   1462   -923    316       C  
ATOM     67  C   ARG A  53     -35.048  72.704 -28.389  1.00 64.69           C  
ANISOU   67  C   ARG A  53     7156   9922   7501   1581   -908    356       C  
ATOM     68  O   ARG A  53     -35.960  72.982 -29.167  1.00 64.09           O  
ANISOU   68  O   ARG A  53     7027   9972   7351   1722   -971    333       O  
ATOM     69  CB  ARG A  53     -32.989  71.987 -29.608  1.00 41.48           C  
ANISOU   69  CB  ARG A  53     4387   6869   4503   1548   -880    392       C  
ATOM     70  CG  ARG A  53     -31.850  70.999 -29.715  1.00 52.96           C  
ANISOU   70  CG  ARG A  53     5895   8244   5982   1424   -870    372       C  
ATOM     71  CD  ARG A  53     -31.094  70.910 -28.411  1.00 48.07           C  
ANISOU   71  CD  ARG A  53     5302   7497   5464   1271   -796    394       C  
ATOM     72  NE  ARG A  53     -30.271  72.090 -28.173  1.00 38.53           N  
ANISOU   72  NE  ARG A  53     4191   6187   4263   1319   -699    492       N  
ATOM     73  CZ  ARG A  53     -29.013  72.207 -28.583  1.00 48.54           C  
ANISOU   73  CZ  ARG A  53     5559   7365   5518   1317   -645    538       C  
ATOM     74  NH1 ARG A  53     -28.441  71.216 -29.255  1.00 59.24           N1+
ANISOU   74  NH1 ARG A  53     6935   8723   6850   1273   -681    500       N1+
ATOM     75  NH2 ARG A  53     -28.328  73.310 -28.322  1.00 48.76           N  
ANISOU   75  NH2 ARG A  53     5665   7297   5563   1358   -551    618       N  
ATOM     76  N   LEU A  54     -34.817  73.383 -27.268  1.00 51.50           N  
ANISOU   76  N   LEU A  54     5511   8155   5901   1530   -825    411       N  
ATOM     77  CA  LEU A  54     -35.668  74.490 -26.852  1.00 57.48           C  
ANISOU   77  CA  LEU A  54     6236   8944   6662   1630   -798    451       C  
ATOM     78  C   LEU A  54     -35.426  75.726 -27.705  1.00 52.61           C  
ANISOU   78  C   LEU A  54     5717   8315   5957   1821   -751    548       C  
ATOM     79  O   LEU A  54     -34.326  75.925 -28.215  1.00 48.98           O  
ANISOU   79  O   LEU A  54     5371   7770   5468   1840   -699    605       O  
ATOM     80  CB  LEU A  54     -35.429  74.844 -25.379  1.00 49.82           C  
ANISOU   80  CB  LEU A  54     5269   7867   5793   1518   -718    480       C  
ATOM     81  CG  LEU A  54     -35.853  73.843 -24.305  1.00 44.83           C  
ANISOU   81  CG  LEU A  54     4541   7240   5250   1349   -744    400       C  
ATOM     82  CD1 LEU A  54     -35.437  74.341 -22.940  1.00 32.14           C  
ANISOU   82  CD1 LEU A  54     2965   5522   3726   1265   -657    443       C  
ATOM     83  CD2 LEU A  54     -37.351  73.592 -24.351  1.00 36.21           C  
ANISOU   83  CD2 LEU A  54     3309   6288   4159   1386   -818    326       C  
ATOM     84  N   PRO A  55     -36.461  76.565 -27.853  1.00 41.89           N  
ANISOU   84  N   PRO A  55     4316   7041   4559   1969   -762    568       N  
ATOM     85  CA  PRO A  55     -36.306  77.855 -28.530  1.00 36.79           C  
ANISOU   85  CA  PRO A  55     3773   6372   3836   2163   -697    673       C  
ATOM     86  C   PRO A  55     -35.157  78.616 -27.891  1.00 38.90           C  
ANISOU   86  C   PRO A  55     4158   6458   4163   2113   -565    763       C  
ATOM     87  O   PRO A  55     -34.960  78.528 -26.685  1.00 48.07           O  
ANISOU   87  O   PRO A  55     5292   7545   5426   1971   -527    749       O  
ATOM     88  CB  PRO A  55     -37.629  78.563 -28.240  1.00 23.03           C  
ANISOU   88  CB  PRO A  55     1944   4722   2083   2276   -714    672       C  
ATOM     89  CG  PRO A  55     -38.605  77.466 -27.994  1.00 64.11           C  
ANISOU   89  CG  PRO A  55     6987  10053   7318   2184   -828    546       C  
ATOM     90  CD  PRO A  55     -37.830  76.359 -27.345  1.00 61.03           C  
ANISOU   90  CD  PRO A  55     6593   9580   7015   1961   -826    495       C  
ATOM     91  N   GLU A  56     -34.403  79.350 -28.694  1.00 69.36           N  
ANISOU   91  N   GLU A  56     8145  10247   7960   2231   -493    850       N  
ATOM     92  CA  GLU A  56     -33.210  80.014 -28.198  1.00 54.30           C  
ANISOU   92  CA  GLU A  56     6350   8166   6116   2179   -365    923       C  
ATOM     93  C   GLU A  56     -33.446  81.484 -27.875  1.00 57.82           C  
ANISOU   93  C   GLU A  56     6854   8542   6574   2302   -254   1013       C  
ATOM     94  O   GLU A  56     -32.531  82.188 -27.462  1.00 58.60           O  
ANISOU   94  O   GLU A  56     7047   8490   6729   2267   -130   1068       O  
ATOM     95  CB  GLU A  56     -32.072  79.855 -29.207  1.00 45.78           C  
ANISOU   95  CB  GLU A  56     5385   7026   4984   2206   -332    960       C  
ATOM     96  CG  GLU A  56     -32.530  79.895 -30.654  1.00101.96           C  
ANISOU   96  CG  GLU A  56    12528  14250  11960   2394   -384    977       C  
ATOM     97  CD  GLU A  56     -31.509  79.305 -31.609  1.00142.25           C  
ANISOU   97  CD  GLU A  56    17711  19323  17015   2383   -386    979       C  
ATOM     98  OE1 GLU A  56     -30.432  78.878 -31.142  1.00140.27           O  
ANISOU   98  OE1 GLU A  56    17490  18964  16840   2229   -346    969       O  
ATOM     99  OE2 GLU A  56     -31.785  79.265 -32.825  1.00156.14           O1-
ANISOU   99  OE2 GLU A  56    19501  21171  18656   2536   -429    990       O1-
ATOM    100  N   TYR A  57     -34.680  81.942 -28.047  1.00 52.12           N  
ANISOU  100  N   TYR A  57     6074   7928   5801   2439   -291   1018       N  
ATOM    101  CA  TYR A  57     -34.983  83.364 -27.888  1.00 51.43           C  
ANISOU  101  CA  TYR A  57     6052   7780   5708   2579   -179   1106       C  
ATOM    102  C   TYR A  57     -35.641  83.738 -26.556  1.00 55.58           C  
ANISOU  102  C   TYR A  57     6502   8290   6325   2501   -149   1081       C  
ATOM    103  O   TYR A  57     -35.942  84.906 -26.318  1.00 54.95           O  
ANISOU  103  O   TYR A  57     6474   8158   6248   2600    -48   1143       O  
ATOM    104  CB  TYR A  57     -35.816  83.875 -29.069  1.00 56.55           C  
ANISOU  104  CB  TYR A  57     6719   8544   6223   2827   -212   1151       C  
ATOM    105  CG  TYR A  57     -37.032  83.036 -29.395  1.00 63.88           C  
ANISOU  105  CG  TYR A  57     7500   9677   7093   2855   -373   1056       C  
ATOM    106  CD1 TYR A  57     -38.151  83.049 -28.574  1.00 75.91           C  
ANISOU  106  CD1 TYR A  57     8895  11282   8666   2831   -419   1005       C  
ATOM    107  CD2 TYR A  57     -37.070  82.248 -30.538  1.00 49.13           C  
ANISOU  107  CD2 TYR A  57     5620   7922   5126   2909   -473   1011       C  
ATOM    108  CE1 TYR A  57     -39.268  82.292 -28.874  1.00 87.32           C  
ANISOU  108  CE1 TYR A  57    10196  12912  10069   2853   -560    908       C  
ATOM    109  CE2 TYR A  57     -38.184  81.487 -30.847  1.00 74.13           C  
ANISOU  109  CE2 TYR A  57     8643  11275   8246   2933   -618    910       C  
ATOM    110  CZ  TYR A  57     -39.281  81.515 -30.010  1.00 96.85           C  
ANISOU  110  CZ  TYR A  57    11388  14229  11181   2903   -660    857       C  
ATOM    111  OH  TYR A  57     -40.394  80.765 -30.307  1.00 95.87           O  
ANISOU  111  OH  TYR A  57    11114  14291  11023   2923   -799    747       O  
ATOM    112  N   VAL A  58     -35.868  82.748 -25.697  1.00 49.65           N  
ANISOU  112  N   VAL A  58     5636   7582   5648   2328   -229    991       N  
ATOM    113  CA  VAL A  58     -36.324  83.005 -24.335  1.00 34.62           C  
ANISOU  113  CA  VAL A  58     3670   5647   3839   2229   -192    965       C  
ATOM    114  C   VAL A  58     -35.321  82.404 -23.360  1.00 55.58           C  
ANISOU  114  C   VAL A  58     6334   8195   6590   2015   -164    926       C  
ATOM    115  O   VAL A  58     -35.079  81.196 -23.372  1.00 58.15           O  
ANISOU  115  O   VAL A  58     6605   8561   6928   1901   -252    863       O  
ATOM    116  CB  VAL A  58     -37.718  82.422 -24.060  1.00 40.83           C  
ANISOU  116  CB  VAL A  58     4297   6590   4627   2230   -307    890       C  
ATOM    117  CG1 VAL A  58     -38.088  82.634 -22.605  1.00 35.96           C  
ANISOU  117  CG1 VAL A  58     3625   5928   4111   2116   -259    866       C  
ATOM    118  CG2 VAL A  58     -38.750  83.064 -24.968  1.00 39.63           C  
ANISOU  118  CG2 VAL A  58     4124   6556   4376   2453   -339    922       C  
ATOM    119  N   ILE A  59     -34.746  83.257 -22.516  1.00 46.85           N  
ANISOU  119  N   ILE A  59     5297   6954   5550   1966    -40    961       N  
ATOM    120  CA  ILE A  59     -33.566  82.902 -21.737  1.00 39.50           C  
ANISOU  120  CA  ILE A  59     4402   5909   4696   1793      5    935       C  
ATOM    121  C   ILE A  59     -33.750  83.063 -20.224  1.00 50.89           C  
ANISOU  121  C   ILE A  59     5799   7308   6229   1674     44    899       C  
ATOM    122  O   ILE A  59     -34.125  84.132 -19.751  1.00 52.09           O  
ANISOU  122  O   ILE A  59     5974   7415   6403   1731    130    933       O  
ATOM    123  CB  ILE A  59     -32.349  83.735 -22.194  1.00 45.53           C  
ANISOU  123  CB  ILE A  59     5307   6534   5458   1829    128    998       C  
ATOM    124  CG1 ILE A  59     -32.028  83.456 -23.663  1.00 69.04           C  
ANISOU  124  CG1 ILE A  59     8339   9548   8346   1934     92   1033       C  
ATOM    125  CG2 ILE A  59     -31.139  83.463 -21.322  1.00 41.70           C  
ANISOU  125  CG2 ILE A  59     4849   5939   5058   1656    176    961       C  
ATOM    126  CD1 ILE A  59     -32.769  84.357 -24.636  1.00 80.94           C  
ANISOU  126  CD1 ILE A  59     9891  11100   9764   2152    120   1105       C  
ATOM    127  N   PRO A  60     -33.457  81.995 -19.463  1.00 33.24           N  
ANISOU  127  N   PRO A  60     3506   5081   4043   1513    -13    833       N  
ATOM    128  CA  PRO A  60     -33.539  81.982 -18.002  1.00 36.63           C  
ANISOU  128  CA  PRO A  60     3897   5471   4550   1394     18    794       C  
ATOM    129  C   PRO A  60     -32.365  82.725 -17.389  1.00 44.18           C  
ANISOU  129  C   PRO A  60     4945   6285   5557   1335    133    809       C  
ATOM    130  O   PRO A  60     -31.282  82.772 -17.968  1.00 63.45           O  
ANISOU  130  O   PRO A  60     7462   8659   7989   1329    166    826       O  
ATOM    131  CB  PRO A  60     -33.415  80.495 -17.652  1.00 40.37           C  
ANISOU  131  CB  PRO A  60     4302   5996   5042   1259    -78    726       C  
ATOM    132  CG  PRO A  60     -33.367  79.758 -18.954  1.00 50.45           C  
ANISOU  132  CG  PRO A  60     5572   7344   6254   1308   -162    724       C  
ATOM    133  CD  PRO A  60     -32.916  80.731 -19.979  1.00 56.45           C  
ANISOU  133  CD  PRO A  60     6429   8057   6962   1440   -101    794       C  
ATOM    134  N   VAL A  61     -32.578  83.281 -16.207  1.00 26.27           N  
ANISOU  134  N   VAL A  61     2664   3973   3345   1289    193    794       N  
ATOM    135  CA  VAL A  61     -31.566  84.083 -15.549  1.00 51.26           C  
ANISOU  135  CA  VAL A  61     5905   7009   6564   1236    305    794       C  
ATOM    136  C   VAL A  61     -31.384  83.587 -14.126  1.00 45.97           C  
ANISOU  136  C   VAL A  61     5190   6327   5949   1096    293    730       C  
ATOM    137  O   VAL A  61     -30.263  83.507 -13.616  1.00 44.21           O  
ANISOU  137  O   VAL A  61     5005   6031   5761   1004    326    697       O  
ATOM    138  CB  VAL A  61     -31.970  85.570 -15.536  1.00 44.12           C  
ANISOU  138  CB  VAL A  61     5052   6044   5668   1345    419    845       C  
ATOM    139  CG1 VAL A  61     -31.130  86.349 -14.546  1.00 15.57           C  
ANISOU  139  CG1 VAL A  61     1487   2304   2123   1267    531    820       C  
ATOM    140  CG2 VAL A  61     -31.853  86.161 -16.930  1.00 49.96           C  
ANISOU  140  CG2 VAL A  61     5866   6766   6350   1488    458    916       C  
ATOM    141  N   HIS A  62     -32.500  83.246 -13.495  1.00 32.69           N  
ANISOU  141  N   HIS A  62     3426   4721   4272   1087    246    711       N  
ATOM    142  CA  HIS A  62     -32.478  82.803 -12.113  1.00 48.52           C  
ANISOU  142  CA  HIS A  62     5393   6720   6321    971    241    657       C  
ATOM    143  C   HIS A  62     -33.701  81.975 -11.721  1.00 44.39           C  
ANISOU  143  C   HIS A  62     4771   6300   5795    953    166    633       C  
ATOM    144  O   HIS A  62     -34.843  82.387 -11.934  1.00 30.33           O  
ANISOU  144  O   HIS A  62     2944   4575   4004   1037    163    654       O  
ATOM    145  CB  HIS A  62     -32.345  84.007 -11.187  1.00 33.69           C  
ANISOU  145  CB  HIS A  62     3555   4758   4488    972    350    657       C  
ATOM    146  CG  HIS A  62     -32.287  83.645  -9.739  1.00 34.19           C  
ANISOU  146  CG  HIS A  62     3589   4815   4588    866    351    602       C  
ATOM    147  CD2 HIS A  62     -33.176  83.826  -8.738  1.00 13.68           C  
ANISOU  147  CD2 HIS A  62      946   2240   2011    857    368    588       C  
ATOM    148  ND1 HIS A  62     -31.197  83.012  -9.177  1.00 30.38           N  
ANISOU  148  ND1 HIS A  62     3125   4300   4118    761    336    555       N  
ATOM    149  CE1 HIS A  62     -31.422  82.819  -7.890  1.00 46.98           C  
ANISOU  149  CE1 HIS A  62     5201   6409   6242    698    341    516       C  
ATOM    150  NE2 HIS A  62     -32.614  83.306  -7.596  1.00 39.06           N  
ANISOU  150  NE2 HIS A  62     4160   5435   5246    751    363    536       N  
ATOM    151  N   TYR A  63     -33.441  80.805 -11.144  1.00 30.02           N  
ANISOU  151  N   TYR A  63     2918   4501   3986    843    111    587       N  
ATOM    152  CA  TYR A  63     -34.492  79.947 -10.618  1.00 43.74           C  
ANISOU  152  CA  TYR A  63     4566   6318   5735    803     59    556       C  
ATOM    153  C   TYR A  63     -34.628  80.103  -9.109  1.00 41.26           C  
ANISOU  153  C   TYR A  63     4246   5971   5462    737    110    531       C  
ATOM    154  O   TYR A  63     -33.633  80.148  -8.385  1.00 32.10           O  
ANISOU  154  O   TYR A  63     3139   4743   4313    673    145    512       O  
ATOM    155  CB  TYR A  63     -34.199  78.480 -10.913  1.00 14.77           C  
ANISOU  155  CB  TYR A  63      869   2690   2053    727    -23    523       C  
ATOM    156  CG  TYR A  63     -34.201  78.084 -12.368  1.00 43.08           C  
ANISOU  156  CG  TYR A  63     4446   6326   5595    783    -89    535       C  
ATOM    157  CD1 TYR A  63     -33.045  78.181 -13.136  1.00 23.45           C  
ANISOU  157  CD1 TYR A  63     2036   3791   3083    795    -86    556       C  
ATOM    158  CD2 TYR A  63     -35.344  77.587 -12.967  1.00 13.72           C  
ANISOU  158  CD2 TYR A  63      640   2709   1863    822   -155    519       C  
ATOM    159  CE1 TYR A  63     -33.035  77.803 -14.461  1.00 48.95           C  
ANISOU  159  CE1 TYR A  63     5263   7069   6266    850   -146    568       C  
ATOM    160  CE2 TYR A  63     -35.345  77.209 -14.298  1.00 16.39           C  
ANISOU  160  CE2 TYR A  63      970   3103   2155    878   -221    522       C  
ATOM    161  CZ  TYR A  63     -34.187  77.320 -15.037  1.00 32.98           C  
ANISOU  161  CZ  TYR A  63     3156   5151   4223    895   -216    550       C  
ATOM    162  OH  TYR A  63     -34.178  76.943 -16.357  1.00 55.13           O  
ANISOU  162  OH  TYR A  63     5959   8012   6976    955   -279    555       O  
ATOM    163  N   ASP A  64     -35.868  80.168  -8.638  1.00 56.77           N  
ANISOU  163  N   ASP A  64     6141   7987   7444    757    114    525       N  
ATOM    164  CA  ASP A  64     -36.151  80.109  -7.211  1.00 49.07           C  
ANISOU  164  CA  ASP A  64     5151   6992   6501    694    155    499       C  
ATOM    165  C   ASP A  64     -36.955  78.845  -6.941  1.00 37.05           C  
ANISOU  165  C   ASP A  64     3547   5539   4990    635    104    466       C  
ATOM    166  O   ASP A  64     -38.156  78.798  -7.208  1.00 51.44           O  
ANISOU  166  O   ASP A  64     5289   7432   6825    675     85    463       O  
ATOM    167  CB  ASP A  64     -36.936  81.341  -6.767  1.00 76.08           C  
ANISOU  167  CB  ASP A  64     8564  10401   9941    765    225    520       C  
ATOM    168  CG  ASP A  64     -37.007  81.470  -5.262  1.00 96.86           C  
ANISOU  168  CG  ASP A  64    11203  12997  12601    705    281    495       C  
ATOM    169  OD1 ASP A  64     -37.922  80.879  -4.652  1.00 91.35           O  
ANISOU  169  OD1 ASP A  64    10440  12347  11922    675    271    477       O  
ATOM    170  OD2 ASP A  64     -36.142  82.166  -4.691  1.00107.75           O1-
ANISOU  170  OD2 ASP A  64    12653  14301  13987    689    338    489       O1-
ATOM    171  N   LEU A  65     -36.291  77.817  -6.418  1.00 33.79           N  
ANISOU  171  N   LEU A  65     3156   5106   4578    541     86    439       N  
ATOM    172  CA  LEU A  65     -36.931  76.514  -6.244  1.00 41.74           C  
ANISOU  172  CA  LEU A  65     4097   6164   5599    478     47    407       C  
ATOM    173  C   LEU A  65     -37.386  76.268  -4.817  1.00 43.49           C  
ANISOU  173  C   LEU A  65     4307   6369   5848    423    101    390       C  
ATOM    174  O   LEU A  65     -36.587  76.334  -3.884  1.00 41.27           O  
ANISOU  174  O   LEU A  65     4093   6031   5557    386    138    387       O  
ATOM    175  CB  LEU A  65     -35.979  75.388  -6.651  1.00 29.53           C  
ANISOU  175  CB  LEU A  65     2584   4606   4031    415     -2    393       C  
ATOM    176  CG  LEU A  65     -35.348  75.445  -8.040  1.00 42.60           C  
ANISOU  176  CG  LEU A  65     4263   6271   5654    458    -55    408       C  
ATOM    177  CD1 LEU A  65     -34.646  74.134  -8.327  1.00 29.09           C  
ANISOU  177  CD1 LEU A  65     2568   4557   3928    387   -104    387       C  
ATOM    178  CD2 LEU A  65     -36.394  75.748  -9.105  1.00 22.13           C  
ANISOU  178  CD2 LEU A  65     1599   3754   3056    539    -93    414       C  
ATOM    179  N   LEU A  66     -38.673  75.979  -4.657  1.00 46.02           N  
ANISOU  179  N   LEU A  66     4541   6743   6202    423    106    373       N  
ATOM    180  CA  LEU A  66     -39.187  75.458  -3.395  1.00 28.89           C  
ANISOU  180  CA  LEU A  66     2354   4561   4060    363    158    354       C  
ATOM    181  C   LEU A  66     -39.707  74.042  -3.600  1.00 48.99           C  
ANISOU  181  C   LEU A  66     4838   7145   6631    296    130    319       C  
ATOM    182  O   LEU A  66     -40.701  73.829  -4.301  1.00 45.85           O  
ANISOU  182  O   LEU A  66     4344   6815   6261    312     99    296       O  
ATOM    183  CB  LEU A  66     -40.316  76.330  -2.850  1.00 30.80           C  
ANISOU  183  CB  LEU A  66     2545   4823   4333    410    211    360       C  
ATOM    184  CG  LEU A  66     -41.016  75.722  -1.623  1.00 33.72           C  
ANISOU  184  CG  LEU A  66     2887   5186   4737    351    270    339       C  
ATOM    185  CD1 LEU A  66     -40.105  75.747  -0.403  1.00 58.79           C  
ANISOU  185  CD1 LEU A  66     6162   8289   7885    315    321    348       C  
ATOM    186  CD2 LEU A  66     -42.319  76.425  -1.318  1.00 35.29           C  
ANISOU  186  CD2 LEU A  66     3011   5423   4976    397    312    338       C  
ATOM    187  N   ILE A  67     -39.033  73.072  -2.996  1.00 22.37           N  
ANISOU  187  N   ILE A  67     1521   3731   3250    223    144    311       N  
ATOM    188  CA  ILE A  67     -39.510  71.701  -3.060  1.00 36.69           C  
ANISOU  188  CA  ILE A  67     3285   5561   5092    152    139    278       C  
ATOM    189  C   ILE A  67     -39.858  71.164  -1.682  1.00 46.39           C  
ANISOU  189  C   ILE A  67     4532   6752   6344     99    222    273       C  
ATOM    190  O   ILE A  67     -39.066  71.240  -0.742  1.00 56.65           O  
ANISOU  190  O   ILE A  67     5921   7996   7607     92    259    294       O  
ATOM    191  CB  ILE A  67     -38.493  70.769  -3.690  1.00 33.01           C  
ANISOU  191  CB  ILE A  67     2867   5077   4596    113     88    273       C  
ATOM    192  CG1 ILE A  67     -37.191  70.838  -2.918  1.00 39.14           C  
ANISOU  192  CG1 ILE A  67     3758   5787   5326    103    110    299       C  
ATOM    193  CG2 ILE A  67     -38.249  71.139  -5.137  1.00 41.56           C  
ANISOU  193  CG2 ILE A  67     3929   6203   5659    164      8    275       C  
ATOM    194  CD1 ILE A  67     -36.261  69.747  -3.290  1.00 97.64           C  
ANISOU  194  CD1 ILE A  67    11215  13175  12709     58     75    294       C  
ATOM    195  N   HIS A  68     -41.061  70.612  -1.584  1.00 45.67           N  
ANISOU  195  N   HIS A  68     4351   6691   6310     65    252    241       N  
ATOM    196  CA  HIS A  68     -41.553  70.018  -0.358  1.00 48.75           C  
ANISOU  196  CA  HIS A  68     4750   7043   6730     14    344    236       C  
ATOM    197  C   HIS A  68     -41.827  68.537  -0.598  1.00 42.78           C  
ANISOU  197  C   HIS A  68     3961   6281   6013    -68    356    199       C  
ATOM    198  O   HIS A  68     -42.831  68.175  -1.211  1.00 48.04           O  
ANISOU  198  O   HIS A  68     4515   6999   6740    -92    345    151       O  
ATOM    199  CB  HIS A  68     -42.834  70.728   0.068  1.00 46.34           C  
ANISOU  199  CB  HIS A  68     4362   6771   6474     42    393    226       C  
ATOM    200  CG  HIS A  68     -43.452  70.164   1.308  1.00 59.48           C  
ANISOU  200  CG  HIS A  68     6030   8396   8174     -7    498    221       C  
ATOM    201  CD2 HIS A  68     -43.920  68.925   1.588  1.00 75.14           C  
ANISOU  201  CD2 HIS A  68     7989  10358  10204    -84    554    192       C  
ATOM    202  ND1 HIS A  68     -43.644  70.912   2.449  1.00 61.06           N  
ANISOU  202  ND1 HIS A  68     6270   8568   8363     24    569    247       N  
ATOM    203  CE1 HIS A  68     -44.207  70.159   3.377  1.00 50.41           C  
ANISOU  203  CE1 HIS A  68     4921   7184   7047    -26    662    240       C  
ATOM    204  NE2 HIS A  68     -44.385  68.948   2.881  1.00 57.40           N  
ANISOU  204  NE2 HIS A  68     5769   8068   7971    -93    660    207       N  
ATOM    205  N   ALA A  69     -40.931  67.682  -0.117  1.00 50.31           N  
ANISOU  205  N   ALA A  69     5009   7173   6931   -107    381    216       N  
ATOM    206  CA  ALA A  69     -41.059  66.240  -0.339  1.00 61.39           C  
ANISOU  206  CA  ALA A  69     6400   8556   8369   -185    402    185       C  
ATOM    207  C   ALA A  69     -41.439  65.472   0.926  1.00 54.29           C  
ANISOU  207  C   ALA A  69     5541   7594   7494   -232    523    192       C  
ATOM    208  O   ALA A  69     -40.917  65.734   2.012  1.00 54.06           O  
ANISOU  208  O   ALA A  69     5607   7518   7413   -203    573    235       O  
ATOM    209  CB  ALA A  69     -39.777  65.684  -0.923  1.00 34.84           C  
ANISOU  209  CB  ALA A  69     3116   5170   4951   -192    342    199       C  
ATOM    210  N   ASN A  70     -42.348  64.516   0.769  1.00 50.66           N  
ANISOU  210  N   ASN A  70     5006   7131   7111   -302    574    145       N  
ATOM    211  CA  ASN A  70     -42.782  63.673   1.872  1.00 42.77           C  
ANISOU  211  CA  ASN A  70     4042   6062   6145   -352    705    149       C  
ATOM    212  C   ASN A  70     -42.165  62.278   1.750  1.00 65.13           C  
ANISOU  212  C   ASN A  70     6943   8833   8972   -410    734    147       C  
ATOM    213  O   ASN A  70     -42.498  61.519   0.839  1.00 59.39           O  
ANISOU  213  O   ASN A  70     6144   8122   8301   -469    711     92       O  
ATOM    214  CB  ASN A  70     -44.310  63.581   1.888  1.00 52.62           C  
ANISOU  214  CB  ASN A  70     5156   7338   7499   -397    767     92       C  
ATOM    215  CG  ASN A  70     -44.863  63.198   3.247  1.00 74.05           C  
ANISOU  215  CG  ASN A  70     7910   9982  10242   -423    918    111       C  
ATOM    216  ND2 ASN A  70     -45.366  64.186   3.977  1.00 92.02           N  
ANISOU  216  ND2 ASN A  70    10174  12274  12516   -374    951    132       N  
ATOM    217  OD1 ASN A  70     -44.844  62.035   3.633  1.00 48.65           O  
ANISOU  217  OD1 ASN A  70     4740   6694   7050   -482   1009    108       O  
ATOM    218  N   LEU A  71     -41.252  61.952   2.658  1.00 49.90           N  
ANISOU  218  N   LEU A  71     5153   6838   6971   -387    783    204       N  
ATOM    219  CA  LEU A  71     -40.556  60.669   2.609  1.00 50.36           C  
ANISOU  219  CA  LEU A  71     5292   6833   7009   -425    814    213       C  
ATOM    220  C   LEU A  71     -41.366  59.580   3.297  1.00 55.92           C  
ANISOU  220  C   LEU A  71     6001   7464   7781   -491    964    200       C  
ATOM    221  O   LEU A  71     -40.827  58.555   3.711  1.00 53.67           O  
ANISOU  221  O   LEU A  71     5819   7105   7470   -506   1034    227       O  
ATOM    222  CB  LEU A  71     -39.172  60.778   3.249  1.00 62.35           C  
ANISOU  222  CB  LEU A  71     6957   8320   8412   -358    795    277       C  
ATOM    223  CG  LEU A  71     -38.296  61.925   2.752  1.00 39.72           C  
ANISOU  223  CG  LEU A  71     4098   5513   5481   -293    668    290       C  
ATOM    224  CD1 LEU A  71     -36.870  61.750   3.251  1.00 46.30           C  
ANISOU  224  CD1 LEU A  71     5064   6316   6212   -243    649    334       C  
ATOM    225  CD2 LEU A  71     -38.330  62.000   1.235  1.00 62.54           C  
ANISOU  225  CD2 LEU A  71     6897   8457   8406   -318    562    248       C  
ATOM    226  N   THR A  72     -42.665  59.819   3.427  1.00 64.89           N  
ANISOU  226  N   THR A  72     7028   8621   9007   -526   1020    158       N  
ATOM    227  CA  THR A  72     -43.577  58.833   3.983  1.00 34.56           C  
ANISOU  227  CA  THR A  72     3169   4710   5252   -600   1172    132       C  
ATOM    228  C   THR A  72     -44.580  58.458   2.908  1.00 46.37           C  
ANISOU  228  C   THR A  72     4502   6252   6867   -684   1150     34       C  
ATOM    229  O   THR A  72     -44.745  57.287   2.576  1.00 63.06           O  
ANISOU  229  O   THR A  72     6603   8316   9040   -763   1209    -10       O  
ATOM    230  CB  THR A  72     -44.327  59.391   5.205  1.00 58.54           C  
ANISOU  230  CB  THR A  72     6213   7728   8303   -573   1279    159       C  
ATOM    231  CG2 THR A  72     -45.191  58.314   5.848  1.00 34.48           C  
ANISOU  231  CG2 THR A  72     3163   4592   5344   -649   1457    139       C  
ATOM    232  OG1 THR A  72     -43.384  59.880   6.166  1.00 64.36           O  
ANISOU  232  OG1 THR A  72     7092   8440   8921   -485   1281    240       O  
ATOM    233  N   THR A  73     -45.236  59.472   2.355  1.00 55.78           N  
ANISOU  233  N   THR A  73     5567   7541   8088   -660   1065     -5       N  
ATOM    234  CA  THR A  73     -46.220  59.284   1.297  1.00 39.08           C  
ANISOU  234  CA  THR A  73     3280   5496   6074   -720   1023   -107       C  
ATOM    235  C   THR A  73     -45.540  59.270  -0.071  1.00 55.74           C  
ANISOU  235  C   THR A  73     5366   7668   8145   -708    871   -134       C  
ATOM    236  O   THR A  73     -46.163  58.961  -1.086  1.00 66.43           O  
ANISOU  236  O   THR A  73     6590   9083   9566   -754    820   -223       O  
ATOM    237  CB  THR A  73     -47.270  60.401   1.334  1.00 57.06           C  
ANISOU  237  CB  THR A  73     5431   7856   8392   -684   1000   -135       C  
ATOM    238  CG2 THR A  73     -47.752  60.611   2.763  1.00 31.46           C  
ANISOU  238  CG2 THR A  73     2237   4552   5164   -676   1141    -91       C  
ATOM    239  OG1 THR A  73     -46.694  61.620   0.845  1.00 70.99           O  
ANISOU  239  OG1 THR A  73     7207   9696  10072   -588    864    -96       O  
ATOM    240  N   LEU A  74     -44.257  59.613  -0.082  1.00 54.91           N  
ANISOU  240  N   LEU A  74     5384   7549   7929   -643    801    -59       N  
ATOM    241  CA  LEU A  74     -43.446  59.525  -1.286  1.00 68.37           C  
ANISOU  241  CA  LEU A  74     7094   9296   9589   -628    673    -71       C  
ATOM    242  C   LEU A  74     -43.974  60.404  -2.417  1.00 57.21           C  
ANISOU  242  C   LEU A  74     5547   8001   8189   -590    549   -122       C  
ATOM    243  O   LEU A  74     -44.035  59.981  -3.570  1.00 68.70           O  
ANISOU  243  O   LEU A  74     6933   9506   9665   -616    473   -184       O  
ATOM    244  CB  LEU A  74     -43.337  58.070  -1.746  1.00 65.63           C  
ANISOU  244  CB  LEU A  74     6753   8898   9287   -717    712   -120       C  
ATOM    245  CG  LEU A  74     -42.780  57.099  -0.703  1.00 49.45           C  
ANISOU  245  CG  LEU A  74     4845   6725   7218   -745    842    -65       C  
ATOM    246  CD1 LEU A  74     -42.421  55.775  -1.351  1.00 62.89           C  
ANISOU  246  CD1 LEU A  74     6569   8378   8947   -817    858   -104       C  
ATOM    247  CD2 LEU A  74     -41.564  57.696  -0.011  1.00 74.80           C  
ANISOU  247  CD2 LEU A  74     8202   9911  10306   -655    815     36       C  
ATOM    248  N   THR A  75     -44.358  61.628  -2.076  1.00 47.88           N  
ANISOU  248  N   THR A  75     4335   6866   6991   -522    531    -95       N  
ATOM    249  CA  THR A  75     -44.807  62.590  -3.072  1.00 46.36           C  
ANISOU  249  CA  THR A  75     4034   6784   6796   -462    419   -127       C  
ATOM    250  C   THR A  75     -44.221  63.950  -2.737  1.00 53.37           C  
ANISOU  250  C   THR A  75     4992   7681   7603   -361    379    -48       C  
ATOM    251  O   THR A  75     -43.815  64.191  -1.603  1.00 55.56           O  
ANISOU  251  O   THR A  75     5369   7895   7849   -347    449     12       O  
ATOM    252  CB  THR A  75     -46.328  62.707  -3.087  1.00 46.76           C  
ANISOU  252  CB  THR A  75     3926   6897   6944   -486    453   -203       C  
ATOM    253  CG2 THR A  75     -46.954  61.351  -3.320  1.00 48.94           C  
ANISOU  253  CG2 THR A  75     4125   7155   7315   -598    511   -294       C  
ATOM    254  OG1 THR A  75     -46.776  63.214  -1.827  1.00 50.06           O  
ANISOU  254  OG1 THR A  75     4367   7275   7377   -472    553   -162       O  
ATOM    255  N   PHE A  76     -44.171  64.838  -3.722  1.00 68.31           N  
ANISOU  255  N   PHE A  76     6838   9654   9461   -288    271    -51       N  
ATOM    256  CA  PHE A  76     -43.588  66.154  -3.497  1.00 39.94           C  
ANISOU  256  CA  PHE A  76     3313   6064   5798   -195    240     19       C  
ATOM    257  C   PHE A  76     -44.262  67.265  -4.296  1.00 45.09           C  
ANISOU  257  C   PHE A  76     3870   6812   6450   -111    169      5       C  
ATOM    258  O   PHE A  76     -44.640  67.086  -5.458  1.00 50.33           O  
ANISOU  258  O   PHE A  76     4445   7553   7126    -99     91    -47       O  
ATOM    259  CB  PHE A  76     -42.082  66.133  -3.763  1.00 30.71           C  
ANISOU  259  CB  PHE A  76     2270   4851   4548   -175    191     70       C  
ATOM    260  CG  PHE A  76     -41.717  65.898  -5.201  1.00 47.82           C  
ANISOU  260  CG  PHE A  76     4408   7068   6692   -162     88     43       C  
ATOM    261  CD1 PHE A  76     -41.585  64.616  -5.695  1.00 55.43           C  
ANISOU  261  CD1 PHE A  76     5361   8020   7678   -235     79     -1       C  
ATOM    262  CD2 PHE A  76     -41.486  66.966  -6.057  1.00 56.28           C  
ANISOU  262  CD2 PHE A  76     5471   8195   7719    -72      7     64       C  
ATOM    263  CE1 PHE A  76     -41.238  64.399  -7.015  1.00 50.28           C  
ANISOU  263  CE1 PHE A  76     4685   7416   7001   -219    -17    -28       C  
ATOM    264  CE2 PHE A  76     -41.137  66.754  -7.381  1.00 46.88           C  
ANISOU  264  CE2 PHE A  76     4261   7050   6499    -51    -84     43       C  
ATOM    265  CZ  PHE A  76     -41.014  65.469  -7.858  1.00 44.51           C  
ANISOU  265  CZ  PHE A  76     3947   6744   6219   -125   -100     -5       C  
ATOM    266  N   TRP A  77     -44.409  68.414  -3.648  1.00 52.82           N  
ANISOU  266  N   TRP A  77     4871   7787   7412    -47    199     50       N  
ATOM    267  CA  TRP A  77     -45.006  69.584  -4.263  1.00 62.41           C  
ANISOU  267  CA  TRP A  77     6014   9081   8619     48    148     51       C  
ATOM    268  C   TRP A  77     -43.917  70.621  -4.473  1.00 50.51           C  
ANISOU  268  C   TRP A  77     4614   7547   7032    127    110    120       C  
ATOM    269  O   TRP A  77     -42.949  70.676  -3.718  1.00 31.34           O  
ANISOU  269  O   TRP A  77     2300   5039   4568    110    148    164       O  
ATOM    270  CB  TRP A  77     -46.091  70.156  -3.351  1.00 55.39           C  
ANISOU  270  CB  TRP A  77     5064   8201   7778     62    224     47       C  
ATOM    271  CG  TRP A  77     -47.065  69.127  -2.860  1.00 95.83           C  
ANISOU  271  CG  TRP A  77    10100  13324  12988    -29    293    -16       C  
ATOM    272  CD1 TRP A  77     -48.305  68.864  -3.369  1.00 96.34           C  
ANISOU  272  CD1 TRP A  77    10008  13472  13123    -42    279    -96       C  
ATOM    273  CD2 TRP A  77     -46.881  68.222  -1.762  1.00137.04           C  
ANISOU  273  CD2 TRP A  77    15383  18452  18233   -118    394     -9       C  
ATOM    274  CE2 TRP A  77     -48.051  67.442  -1.662  1.00131.68           C  
ANISOU  274  CE2 TRP A  77    14584  17798  17650   -188    449    -84       C  
ATOM    275  CE3 TRP A  77     -45.840  67.995  -0.854  1.00129.04           C  
ANISOU  275  CE3 TRP A  77    14517  17343  17169   -139    447     51       C  
ATOM    276  NE1 TRP A  77     -48.904  67.853  -2.653  1.00 99.96           N  
ANISOU  276  NE1 TRP A  77    10427  13892  13662   -144    373   -142       N  
ATOM    277  CZ2 TRP A  77     -48.210  66.453  -0.690  1.00126.03           C  
ANISOU  277  CZ2 TRP A  77    13901  17000  16983   -279    566    -92       C  
ATOM    278  CZ3 TRP A  77     -46.000  67.010   0.112  1.00 91.49           C  
ANISOU  278  CZ3 TRP A  77     9795  12516  12451   -217    553     45       C  
ATOM    279  CH2 TRP A  77     -47.175  66.255   0.185  1.00104.66           C  
ANISOU  279  CH2 TRP A  77    11352  14199  14217   -287    617    -22       C  
ATOM    280  N   GLY A  78     -44.068  71.448  -5.496  1.00 50.93           N  
ANISOU  280  N   GLY A  78     4629   7666   7056    218     40    125       N  
ATOM    281  CA  GLY A  78     -43.067  72.462  -5.755  1.00 23.43           C  
ANISOU  281  CA  GLY A  78     1245   4150   3507    292     18    188       C  
ATOM    282  C   GLY A  78     -43.620  73.775  -6.260  1.00 51.03           C  
ANISOU  282  C   GLY A  78     4703   7699   6986    409      0    210       C  
ATOM    283  O   GLY A  78     -44.635  73.825  -6.959  1.00 50.35           O  
ANISOU  283  O   GLY A  78     4506   7705   6919    455    -42    173       O  
ATOM    284  N   THR A  79     -42.940  74.851  -5.893  1.00 34.64           N  
ANISOU  284  N   THR A  79     2720   5565   4875    461     34    268       N  
ATOM    285  CA  THR A  79     -43.227  76.153  -6.465  1.00 59.80           C  
ANISOU  285  CA  THR A  79     5902   8784   8037    582     25    302       C  
ATOM    286  C   THR A  79     -41.924  76.733  -6.964  1.00 66.23           C  
ANISOU  286  C   THR A  79     6830   9539   8795    620     12    350       C  
ATOM    287  O   THR A  79     -41.125  77.244  -6.176  1.00 74.22           O  
ANISOU  287  O   THR A  79     7933  10468   9798    602     68    379       O  
ATOM    288  CB  THR A  79     -43.828  77.117  -5.436  1.00 68.18           C  
ANISOU  288  CB  THR A  79     6961   9822   9123    615    104    323       C  
ATOM    289  CG2 THR A  79     -43.941  78.501  -6.037  1.00 48.62           C  
ANISOU  289  CG2 THR A  79     4502   7359   6613    745    106    368       C  
ATOM    290  OG1 THR A  79     -45.130  76.662  -5.053  1.00 78.58           O  
ANISOU  290  OG1 THR A  79     8161  11200  10496    590    120    277       O  
ATOM    291  N   THR A  80     -41.692  76.635  -8.267  1.00 37.87           N  
ANISOU  291  N   THR A  80     3231   5992   5165    671    -58    352       N  
ATOM    292  CA  THR A  80     -40.480  77.205  -8.838  1.00 66.95           C  
ANISOU  292  CA  THR A  80     7021   9618   8800    712    -62    397       C  
ATOM    293  C   THR A  80     -40.789  78.467  -9.632  1.00 44.73           C  
ANISOU  293  C   THR A  80     4214   6829   5953    851    -58    440       C  
ATOM    294  O   THR A  80     -41.756  78.523 -10.395  1.00 34.75           O  
ANISOU  294  O   THR A  80     2867   5659   4678    929   -105    427       O  
ATOM    295  CB  THR A  80     -39.698  76.190  -9.699  1.00 55.17           C  
ANISOU  295  CB  THR A  80     5549   8132   7280    668   -130    380       C  
ATOM    296  CG2 THR A  80     -39.863  74.783  -9.144  1.00 64.92           C  
ANISOU  296  CG2 THR A  80     6741   9375   8552    548   -143    328       C  
ATOM    297  OG1 THR A  80     -40.154  76.239 -11.056  1.00 52.83           O  
ANISOU  297  OG1 THR A  80     5203   7921   6949    755   -200    375       O  
ATOM    298  N   LYS A  81     -39.966  79.486  -9.413  1.00 27.94           N  
ANISOU  298  N   LYS A  81     2189   4617   3812    885      4    488       N  
ATOM    299  CA  LYS A  81     -40.092  80.754 -10.105  1.00 42.36           C  
ANISOU  299  CA  LYS A  81     4049   6440   5606   1019     31    539       C  
ATOM    300  C   LYS A  81     -38.842  80.993 -10.941  1.00 45.58           C  
ANISOU  300  C   LYS A  81     4557   6789   5974   1043     31    573       C  
ATOM    301  O   LYS A  81     -37.722  80.916 -10.431  1.00 46.04           O  
ANISOU  301  O   LYS A  81     4689   6761   6044    965     65    572       O  
ATOM    302  CB  LYS A  81     -40.271  81.886  -9.096  1.00 41.19           C  
ANISOU  302  CB  LYS A  81     3935   6228   5486   1042    128    564       C  
ATOM    303  CG  LYS A  81     -41.437  81.684  -8.141  1.00 45.56           C  
ANISOU  303  CG  LYS A  81     4399   6828   6084   1012    143    532       C  
ATOM    304  CD  LYS A  81     -41.559  82.835  -7.158  1.00 51.24           C  
ANISOU  304  CD  LYS A  81     5161   7481   6827   1038    241    557       C  
ATOM    305  CE  LYS A  81     -42.797  82.680  -6.284  1.00 68.09           C  
ANISOU  305  CE  LYS A  81     7203   9665   9002   1021    259    529       C  
ATOM    306  NZ  LYS A  81     -42.920  83.757  -5.266  1.00 71.29           N1+
ANISOU  306  NZ  LYS A  81     7652  10005   9431   1042    356    550       N1+
ATOM    307  N   VAL A  82     -39.027  81.277 -12.227  1.00 38.51           N  
ANISOU  307  N   VAL A  82     3661   5942   5028   1155     -7    601       N  
ATOM    308  CA  VAL A  82     -37.892  81.541 -13.104  1.00 49.99           C  
ANISOU  308  CA  VAL A  82     5212   7339   6442   1189      2    638       C  
ATOM    309  C   VAL A  82     -37.943  82.950 -13.671  1.00 34.25           C  
ANISOU  309  C   VAL A  82     3284   5311   4420   1333     71    704       C  
ATOM    310  O   VAL A  82     -38.928  83.333 -14.292  1.00 49.36           O  
ANISOU  310  O   VAL A  82     5151   7304   6298   1455     48    723       O  
ATOM    311  CB  VAL A  82     -37.846  80.565 -14.281  1.00 26.10           C  
ANISOU  311  CB  VAL A  82     2154   4391   3371   1201    -98    619       C  
ATOM    312  CG1 VAL A  82     -36.456  80.567 -14.906  1.00 43.56           C  
ANISOU  312  CG1 VAL A  82     4469   6525   5555   1190    -83    646       C  
ATOM    313  CG2 VAL A  82     -38.240  79.173 -13.827  1.00 46.51           C  
ANISOU  313  CG2 VAL A  82     4649   7035   5988   1083   -167    549       C  
ATOM    314  N   GLU A  83     -36.876  83.711 -13.458  1.00 32.87           N  
ANISOU  314  N   GLU A  83     3216   5016   4259   1320    160    735       N  
ATOM    315  CA  GLU A  83     -36.724  85.010 -14.097  1.00 52.49           C  
ANISOU  315  CA  GLU A  83     5783   7444   6717   1451    244    801       C  
ATOM    316  C   GLU A  83     -36.200  84.831 -15.521  1.00 40.68           C  
ANISOU  316  C   GLU A  83     4337   5963   5158   1526    209    834       C  
ATOM    317  O   GLU A  83     -35.132  84.263 -15.725  1.00 29.34           O  
ANISOU  317  O   GLU A  83     2943   4482   3725   1447    195    819       O  
ATOM    318  CB  GLU A  83     -35.775  85.897 -13.294  1.00 28.10           C  
ANISOU  318  CB  GLU A  83     2784   4214   3678   1398    363    809       C  
ATOM    319  CG  GLU A  83     -36.326  86.320 -11.944  1.00 65.48           C  
ANISOU  319  CG  GLU A  83     7485   8929   8465   1353    413    784       C  
ATOM    320  CD  GLU A  83     -35.363  87.192 -11.159  1.00 92.38           C  
ANISOU  320  CD  GLU A  83    10976  12202  11921   1298    528    778       C  
ATOM    321  OE1 GLU A  83     -35.278  87.016  -9.927  1.00 72.90           O  
ANISOU  321  OE1 GLU A  83     8487   9715   9497   1198    541    730       O  
ATOM    322  OE2 GLU A  83     -34.690  88.049 -11.770  1.00111.47           O1-
ANISOU  322  OE2 GLU A  83    13483  14535  14335   1357    610    816       O1-
ATOM    323  N   ILE A  84     -36.956  85.310 -16.505  1.00 27.06           N  
ANISOU  323  N   ILE A  84     2606   4303   3371   1687    195    879       N  
ATOM    324  CA  ILE A  84     -36.595  85.115 -17.903  1.00 37.07           C  
ANISOU  324  CA  ILE A  84     3918   5601   4565   1777    155    911       C  
ATOM    325  C   ILE A  84     -36.513  86.420 -18.678  1.00 42.51           C  
ANISOU  325  C   ILE A  84     4711   6234   5209   1946    254    996       C  
ATOM    326  O   ILE A  84     -37.068  87.434 -18.268  1.00 49.38           O  
ANISOU  326  O   ILE A  84     5595   7074   6093   2020    333   1030       O  
ATOM    327  CB  ILE A  84     -37.601  84.212 -18.644  1.00 35.59           C  
ANISOU  327  CB  ILE A  84     3622   5578   4322   1832     18    876       C  
ATOM    328  CG1 ILE A  84     -38.994  84.836 -18.623  1.00 35.84           C  
ANISOU  328  CG1 ILE A  84     3585   5700   4333   1961     12    888       C  
ATOM    329  CG2 ILE A  84     -37.627  82.817 -18.051  1.00 19.63           C  
ANISOU  329  CG2 ILE A  84     1507   3606   2344   1667    -72    792       C  
ATOM    330  CD1 ILE A  84     -39.992  84.094 -19.468  1.00 28.52           C  
ANISOU  330  CD1 ILE A  84     2548   4942   3346   2037   -119    847       C  
ATOM    331  N   THR A  85     -35.826  86.372 -19.816  1.00 64.14           N  
ANISOU  331  N   THR A  85     7525   8954   7890   2011    254   1033       N  
ATOM    332  CA  THR A  85     -35.766  87.493 -20.740  1.00 42.57           C  
ANISOU  332  CA  THR A  85     4900   6176   5099   2190    346   1121       C  
ATOM    333  C   THR A  85     -36.015  86.997 -22.166  1.00 56.57           C  
ANISOU  333  C   THR A  85     6670   8058   6765   2318    253   1141       C  
ATOM    334  O   THR A  85     -35.532  85.935 -22.555  1.00 68.38           O  
ANISOU  334  O   THR A  85     8141   9593   8248   2239    166   1099       O  
ATOM    335  CB  THR A  85     -34.409  88.219 -20.657  1.00 58.65           C  
ANISOU  335  CB  THR A  85     7069   8033   7181   2145    491   1157       C  
ATOM    336  CG2 THR A  85     -33.305  87.375 -21.262  1.00 97.73           C  
ANISOU  336  CG2 THR A  85    12052  12961  12119   2068    451   1139       C  
ATOM    337  OG1 THR A  85     -34.480  89.462 -21.359  1.00 93.91           O  
ANISOU  337  OG1 THR A  85    11643  12435  11603   2321    610   1247       O  
ATOM    338  N   ALA A  86     -36.785  87.757 -22.938  1.00 61.57           N  
ANISOU  338  N   ALA A  86     7330   8746   7318   2523    271   1202       N  
ATOM    339  CA  ALA A  86     -37.048  87.413 -24.334  1.00 62.40           C  
ANISOU  339  CA  ALA A  86     7442   8962   7307   2673    187   1224       C  
ATOM    340  C   ALA A  86     -36.226  88.295 -25.265  1.00 60.53           C  
ANISOU  340  C   ALA A  86     7371   8614   7015   2803    311   1321       C  
ATOM    341  O   ALA A  86     -36.184  89.509 -25.100  1.00 65.22           O  
ANISOU  341  O   ALA A  86     8057   9104   7622   2889    453   1392       O  
ATOM    342  CB  ALA A  86     -38.534  87.540 -24.647  1.00 54.55           C  
ANISOU  342  CB  ALA A  86     6350   8131   6244   2830    103   1217       C  
ATOM    343  N   SER A  87     -35.566  87.681 -26.240  1.00 54.61           N  
ANISOU  343  N   SER A  87     6663   7878   6206   2817    266   1325       N  
ATOM    344  CA  SER A  87     -34.780  88.434 -27.208  1.00 43.91           C  
ANISOU  344  CA  SER A  87     5469   6422   4795   2945    386   1418       C  
ATOM    345  C   SER A  87     -35.634  88.754 -28.424  1.00 60.01           C  
ANISOU  345  C   SER A  87     7531   8583   6689   3200    343   1474       C  
ATOM    346  O   SER A  87     -35.333  89.670 -29.183  1.00 74.39           O  
ANISOU  346  O   SER A  87     9491  10327   8447   3364    462   1571       O  
ATOM    347  CB  SER A  87     -33.527  87.658 -27.615  1.00 48.14           C  
ANISOU  347  CB  SER A  87     6050   6897   5343   2828    375   1397       C  
ATOM    348  OG  SER A  87     -33.852  86.348 -28.047  1.00 76.93           O  
ANISOU  348  OG  SER A  87     9594  10695   8942   2790    199   1326       O  
ATOM    349  N   GLN A  88     -36.704  87.988 -28.599  1.00 63.54           N  
ANISOU  349  N   GLN A  88     7839   9221   7084   3235    175   1409       N  
ATOM    350  CA  GLN A  88     -37.668  88.231 -29.658  1.00 54.23           C  
ANISOU  350  CA  GLN A  88     6651   8191   5765   3481    108   1442       C  
ATOM    351  C   GLN A  88     -39.056  88.289 -29.054  1.00 72.02           C  
ANISOU  351  C   GLN A  88     8761  10576   8028   3517     29   1393       C  
ATOM    352  O   GLN A  88     -39.339  87.594 -28.082  1.00 74.50           O  
ANISOU  352  O   GLN A  88     8948  10922   8437   3334    -40   1304       O  
ATOM    353  CB  GLN A  88     -37.632  87.112 -30.697  1.00 58.34           C  
ANISOU  353  CB  GLN A  88     7127   8846   6195   3506    -42   1390       C  
ATOM    354  CG  GLN A  88     -36.327  86.986 -31.454  1.00 84.98           C  
ANISOU  354  CG  GLN A  88    10638  12109   9542   3493     24   1438       C  
ATOM    355  CD  GLN A  88     -36.309  85.766 -32.347  1.00114.53           C  
ANISOU  355  CD  GLN A  88    14325  15988  13205   3481   -128   1366       C  
ATOM    356  NE2 GLN A  88     -35.174  85.077 -32.384  1.00115.85           N  
ANISOU  356  NE2 GLN A  88    14532  16068  13418   3324   -116   1343       N  
ATOM    357  OE1 GLN A  88     -37.306  85.440 -32.991  1.00117.88           O  
ANISOU  357  OE1 GLN A  88    14668  16596  13527   3606   -250   1321       O  
ATOM    358  N   PRO A  89     -39.938  89.112 -29.635  1.00 90.89           N  
ANISOU  358  N   PRO A  89    11172  13046  10317   3759     42   1453       N  
ATOM    359  CA  PRO A  89     -41.308  89.186 -29.122  1.00 91.27           C  
ANISOU  359  CA  PRO A  89    11075  13232  10370   3809    -36   1404       C  
ATOM    360  C   PRO A  89     -41.966  87.824 -29.262  1.00 85.73           C  
ANISOU  360  C   PRO A  89    10191  12722   9659   3730   -238   1274       C  
ATOM    361  O   PRO A  89     -41.738  87.156 -30.271  1.00100.75           O  
ANISOU  361  O   PRO A  89    12098  14706  11476   3779   -328   1250       O  
ATOM    362  CB  PRO A  89     -41.971  90.187 -30.065  1.00 50.60           C  
ANISOU  362  CB  PRO A  89     5997   8148   5079   4117      0   1495       C  
ATOM    363  CG  PRO A  89     -41.196  90.047 -31.340  1.00 75.00           C  
ANISOU  363  CG  PRO A  89     9210  11225   8061   4224      5   1546       C  
ATOM    364  CD  PRO A  89     -39.779  89.854 -30.897  1.00 74.57           C  
ANISOU  364  CD  PRO A  89     9248  10972   8112   4011    107   1558       C  
ATOM    365  N   THR A  90     -42.758  87.420 -28.276  1.00 65.05           N  
ANISOU  365  N   THR A  90     7419  10169   7128   3608   -300   1188       N  
ATOM    366  CA  THR A  90     -43.387  86.103 -28.289  1.00 75.71           C  
ANISOU  366  CA  THR A  90     8590  11685   8493   3507   -474   1055       C  
ATOM    367  C   THR A  90     -44.376  85.929 -27.141  1.00 68.34           C  
ANISOU  367  C   THR A  90     7501  10808   7658   3404   -507    979       C  
ATOM    368  O   THR A  90     -44.197  86.496 -26.066  1.00 50.62           O  
ANISOU  368  O   THR A  90     5290   8435   5506   3313   -396   1013       O  
ATOM    369  CB  THR A  90     -42.336  84.983 -28.208  1.00 69.80           C  
ANISOU  369  CB  THR A  90     7855  10867   7798   3287   -504   1000       C  
ATOM    370  CG2 THR A  90     -42.998  83.628 -28.139  1.00 43.53           C  
ANISOU  370  CG2 THR A  90     4354   7690   4494   3160   -656    854       C  
ATOM    371  OG1 THR A  90     -41.503  85.022 -29.371  1.00 76.09           O  
ANISOU  371  OG1 THR A  90     8783  11634   8495   3383   -486   1056       O  
ATOM    372  N   SER A  91     -45.416  85.138 -27.377  1.00 65.48           N  
ANISOU  372  N   SER A  91     6968  10636   7273   3412   -652    867       N  
ATOM    373  CA  SER A  91     -46.428  84.886 -26.359  1.00 67.16           C  
ANISOU  373  CA  SER A  91     7019  10917   7583   3318   -688    786       C  
ATOM    374  C   SER A  91     -46.468  83.420 -25.940  1.00 62.26           C  
ANISOU  374  C   SER A  91     6271  10342   7044   3085   -781    652       C  
ATOM    375  O   SER A  91     -47.409  82.981 -25.284  1.00 69.91           O  
ANISOU  375  O   SER A  91     7084  11396   8083   3008   -832    562       O  
ATOM    376  CB  SER A  91     -47.807  85.337 -26.845  1.00 56.14           C  
ANISOU  376  CB  SER A  91     5515   9709   6106   3532   -759    760       C  
ATOM    377  OG  SER A  91     -48.187  84.635 -28.017  1.00 98.95           O  
ANISOU  377  OG  SER A  91    10868  15307  11422   3622   -897    681       O  
ATOM    378  N   THR A  92     -45.449  82.663 -26.325  1.00 43.72           N  
ANISOU  378  N   THR A  92     3991   7931   4689   2975   -796    640       N  
ATOM    379  CA  THR A  92     -45.344  81.273 -25.899  1.00 59.58           C  
ANISOU  379  CA  THR A  92     5904   9954   6778   2748   -864    525       C  
ATOM    380  C   THR A  92     -43.986  81.013 -25.263  1.00 52.41           C  
ANISOU  380  C   THR A  92     5113   8857   5945   2567   -778    569       C  
ATOM    381  O   THR A  92     -42.961  81.489 -25.745  1.00 82.03           O  
ANISOU  381  O   THR A  92     9013  12505   9649   2619   -714    657       O  
ATOM    382  CB  THR A  92     -45.557  80.283 -27.063  1.00 58.66           C  
ANISOU  382  CB  THR A  92     5722   9985   6581   2778   -997    429       C  
ATOM    383  CG2 THR A  92     -46.755  80.688 -27.907  1.00 76.30           C  
ANISOU  383  CG2 THR A  92     7864  12415   8713   3002  -1085    395       C  
ATOM    384  OG1 THR A  92     -44.384  80.251 -27.888  1.00105.10           O  
ANISOU  384  OG1 THR A  92    11753  15788  12391   2805   -973    491       O  
ATOM    385  N   ILE A  93     -43.989  80.257 -24.173  1.00 59.76           N  
ANISOU  385  N   ILE A  93     5972   9743   6991   2360   -774    505       N  
ATOM    386  CA  ILE A  93     -42.753  79.887 -23.505  1.00 49.87           C  
ANISOU  386  CA  ILE A  93     4812   8328   5807   2184   -706    532       C  
ATOM    387  C   ILE A  93     -42.638  78.368 -23.437  1.00 57.73           C  
ANISOU  387  C   ILE A  93     5734   9356   6845   2006   -782    424       C  
ATOM    388  O   ILE A  93     -43.349  77.715 -22.676  1.00 65.82           O  
ANISOU  388  O   ILE A  93     6639  10423   7948   1893   -809    344       O  
ATOM    389  CB  ILE A  93     -42.680  80.471 -22.080  1.00 46.60           C  
ANISOU  389  CB  ILE A  93     4411   7800   5496   2100   -604    571       C  
ATOM    390  CG1 ILE A  93     -43.000  81.967 -22.095  1.00 38.75           C  
ANISOU  390  CG1 ILE A  93     3477   6780   4466   2275   -522    663       C  
ATOM    391  CG2 ILE A  93     -41.308  80.229 -21.472  1.00 38.11           C  
ANISOU  391  CG2 ILE A  93     3441   6562   4476   1949   -534    603       C  
ATOM    392  CD1 ILE A  93     -42.938  82.595 -20.738  1.00 51.07           C  
ANISOU  392  CD1 ILE A  93     5064   8224   6115   2190   -412    693       C  
ATOM    393  N   ILE A  94     -41.746  77.808 -24.247  1.00 42.85           N  
ANISOU  393  N   ILE A  94     3924   7447   4910   1985   -809    424       N  
ATOM    394  CA  ILE A  94     -41.500  76.373 -24.222  1.00 38.59           C  
ANISOU  394  CA  ILE A  94     3335   6918   4408   1819   -868    331       C  
ATOM    395  C   ILE A  94     -40.360  76.035 -23.266  1.00 44.67           C  
ANISOU  395  C   ILE A  94     4187   7526   5257   1645   -791    361       C  
ATOM    396  O   ILE A  94     -39.290  76.639 -23.319  1.00 40.22           O  
ANISOU  396  O   ILE A  94     3753   6850   4677   1665   -720    447       O  
ATOM    397  CB  ILE A  94     -41.174  75.821 -25.621  1.00 52.35           C  
ANISOU  397  CB  ILE A  94     5106   8730   6055   1884   -945    302       C  
ATOM    398  CG1 ILE A  94     -42.426  75.819 -26.502  1.00 46.04           C  
ANISOU  398  CG1 ILE A  94     4188   8120   5183   2031  -1048    232       C  
ATOM    399  CG2 ILE A  94     -40.604  74.414 -25.525  1.00 42.80           C  
ANISOU  399  CG2 ILE A  94     3884   7486   4893   1702   -977    227       C  
ATOM    400  CD1 ILE A  94     -42.757  77.164 -27.090  1.00 80.16           C  
ANISOU  400  CD1 ILE A  94     8560  12485   9411   2262  -1026    319       C  
ATOM    401  N   LEU A  95     -40.607  75.072 -22.383  1.00 50.41           N  
ANISOU  401  N   LEU A  95     4836   8245   6071   1479   -801    288       N  
ATOM    402  CA  LEU A  95     -39.577  74.561 -21.487  1.00 61.81           C  
ANISOU  402  CA  LEU A  95     6349   9555   7582   1316   -742    303       C  
ATOM    403  C   LEU A  95     -39.806  73.089 -21.150  1.00 58.70           C  
ANISOU  403  C   LEU A  95     5875   9184   7246   1159   -786    204       C  
ATOM    404  O   LEU A  95     -40.732  72.464 -21.663  1.00 57.67           O  
ANISOU  404  O   LEU A  95     5634   9170   7109   1171   -862    118       O  
ATOM    405  CB  LEU A  95     -39.469  75.414 -20.216  1.00 67.42           C  
ANISOU  405  CB  LEU A  95     7088  10172   8356   1290   -649    362       C  
ATOM    406  CG  LEU A  95     -40.724  76.052 -19.621  1.00 54.57           C  
ANISOU  406  CG  LEU A  95     5362   8608   6763   1347   -638    353       C  
ATOM    407  CD1 LEU A  95     -41.811  75.016 -19.379  1.00 94.15           C  
ANISOU  407  CD1 LEU A  95    10229  13720  11825   1267   -699    245       C  
ATOM    408  CD2 LEU A  95     -40.366  76.767 -18.331  1.00 26.67           C  
ANISOU  408  CD2 LEU A  95     1877   4962   3294   1300   -538    409       C  
ATOM    409  N   HIS A  96     -38.957  72.545 -20.282  1.00 19.32           N  
ANISOU  409  N   HIS A  96      944   4084   2315   1018   -735    214       N  
ATOM    410  CA  HIS A  96     -38.946  71.112 -20.005  1.00 39.93           C  
ANISOU  410  CA  HIS A  96     3509   6690   4974    873   -761    136       C  
ATOM    411  C   HIS A  96     -39.734  70.722 -18.756  1.00 33.59           C  
ANISOU  411  C   HIS A  96     2616   5883   4263    773   -729     93       C  
ATOM    412  O   HIS A  96     -39.615  71.361 -17.710  1.00 60.91           O  
ANISOU  412  O   HIS A  96     6105   9277   7761    757   -660    143       O  
ATOM    413  CB  HIS A  96     -37.506  70.619 -19.858  1.00 20.54           C  
ANISOU  413  CB  HIS A  96     1172   4117   2516    786   -726    171       C  
ATOM    414  CG  HIS A  96     -36.734  70.583 -21.140  1.00 40.01           C  
ANISOU  414  CG  HIS A  96     3712   6587   4902    851   -761    190       C  
ATOM    415  CD2 HIS A  96     -35.587  71.200 -21.508  1.00 39.00           C  
ANISOU  415  CD2 HIS A  96     3704   6383   4731    897   -722    265       C  
ATOM    416  ND1 HIS A  96     -37.112  69.806 -22.215  1.00 49.22           N  
ANISOU  416  ND1 HIS A  96     4827   7844   6029    872   -841    121       N  
ATOM    417  CE1 HIS A  96     -36.240  69.960 -23.195  1.00 48.89           C  
ANISOU  417  CE1 HIS A  96     4877   7783   5918    934   -850    159       C  
ATOM    418  NE2 HIS A  96     -35.304  70.799 -22.791  1.00 55.42           N  
ANISOU  418  NE2 HIS A  96     5807   8506   6743    948   -776    247       N  
ATOM    419  N   SER A  97     -40.528  69.663 -18.876  1.00 40.38           N  
ANISOU  419  N   SER A  97     3367   6815   5162    706   -775     -5       N  
ATOM    420  CA  SER A  97     -41.166  69.033 -17.726  1.00 30.80           C  
ANISOU  420  CA  SER A  97     2073   5585   4044    589   -735    -54       C  
ATOM    421  C   SER A  97     -41.433  67.564 -18.007  1.00 52.35           C  
ANISOU  421  C   SER A  97     4731   8344   6814    483   -772   -155       C  
ATOM    422  O   SER A  97     -41.767  67.190 -19.131  1.00 40.20           O  
ANISOU  422  O   SER A  97     3138   6897   5238    525   -850   -220       O  
ATOM    423  CB  SER A  97     -42.472  69.728 -17.368  1.00 35.47           C  
ANISOU  423  CB  SER A  97     2549   6259   4670    650   -731    -76       C  
ATOM    424  OG  SER A  97     -43.240  68.944 -16.469  1.00 41.31           O  
ANISOU  424  OG  SER A  97     3189   7001   5506    535   -698   -145       O  
ATOM    425  N   HIS A  98     -41.297  66.731 -16.984  1.00 52.72           N  
ANISOU  425  N   HIS A  98     4779   8316   6937    350   -712   -171       N  
ATOM    426  CA  HIS A  98     -41.473  65.296 -17.167  1.00 37.92           C  
ANISOU  426  CA  HIS A  98     2847   6450   5111    239   -728   -263       C  
ATOM    427  C   HIS A  98     -42.044  64.630 -15.917  1.00 35.08           C  
ANISOU  427  C   HIS A  98     2423   6047   4857    117   -651   -300       C  
ATOM    428  O   HIS A  98     -41.398  64.587 -14.868  1.00 68.34           O  
ANISOU  428  O   HIS A  98     6718  10156   9092     62   -575   -236       O  
ATOM    429  CB  HIS A  98     -40.143  64.659 -17.572  1.00 48.48           C  
ANISOU  429  CB  HIS A  98     4307   7708   6404    201   -734   -231       C  
ATOM    430  CG  HIS A  98     -40.236  63.194 -17.855  1.00 65.40           C  
ANISOU  430  CG  HIS A  98     6403   9854   8592     94   -749   -321       C  
ATOM    431  CD2 HIS A  98     -39.608  62.137 -17.291  1.00 48.32           C  
ANISOU  431  CD2 HIS A  98     4290   7599   6471    -21   -698   -323       C  
ATOM    432  ND1 HIS A  98     -41.051  62.678 -18.840  1.00 62.55           N  
ANISOU  432  ND1 HIS A  98     5928   9602   8235    103   -821   -430       N  
ATOM    433  CE1 HIS A  98     -40.925  61.364 -18.867  1.00 71.90           C  
ANISOU  433  CE1 HIS A  98     7094  10755   9470    -11   -810   -497       C  
ATOM    434  NE2 HIS A  98     -40.056  61.009 -17.937  1.00 66.60           N  
ANISOU  434  NE2 HIS A  98     6524   9959   8821    -86   -733   -429       N  
ATOM    435  N   HIS A  99     -43.260  64.113 -16.042  1.00 45.15           N  
ANISOU  435  N   HIS A  99     3548   7407   6201     80   -666   -407       N  
ATOM    436  CA  HIS A  99     -43.950  63.468 -14.925  1.00 55.55           C  
ANISOU  436  CA  HIS A  99     4789   8689   7629    -36   -581   -452       C  
ATOM    437  C   HIS A  99     -44.254  64.450 -13.800  1.00 63.20           C  
ANISOU  437  C   HIS A  99     5769   9627   8619     -4   -511   -382       C  
ATOM    438  O   HIS A  99     -44.153  64.106 -12.619  1.00 57.15           O  
ANISOU  438  O   HIS A  99     5048   8765   7903    -87   -412   -356       O  
ATOM    439  CB  HIS A  99     -43.136  62.289 -14.383  1.00 68.92           C  
ANISOU  439  CB  HIS A  99     6565  10266   9357   -162   -516   -444       C  
ATOM    440  CG  HIS A  99     -43.117  61.100 -15.291  1.00 68.16           C  
ANISOU  440  CG  HIS A  99     6423  10197   9277   -226   -562   -538       C  
ATOM    441  CD2 HIS A  99     -42.265  60.050 -15.365  1.00 61.11           C  
ANISOU  441  CD2 HIS A  99     5612   9223   8384   -306   -540   -538       C  
ATOM    442  ND1 HIS A  99     -44.070  60.889 -16.264  1.00 71.89           N  
ANISOU  442  ND1 HIS A  99     6758  10792   9764   -207   -637   -654       N  
ATOM    443  CE1 HIS A  99     -43.802  59.767 -16.905  1.00 62.52           C  
ANISOU  443  CE1 HIS A  99     5564   9599   8591   -278   -661   -726       C  
ATOM    444  NE2 HIS A  99     -42.711  59.237 -16.379  1.00 75.67           N  
ANISOU  444  NE2 HIS A  99     7362  11140  10250   -340   -601   -654       N  
ATOM    445  N   LEU A 100     -44.623  65.672 -14.170  1.00 49.33           N  
ANISOU  445  N   LEU A 100     3991   7940   6811    123   -554   -351       N  
ATOM    446  CA  LEU A 100     -45.006  66.681 -13.190  1.00 39.45           C  
ANISOU  446  CA  LEU A 100     2740   6669   5578    165   -492   -292       C  
ATOM    447  C   LEU A 100     -46.416  67.177 -13.477  1.00 56.37           C  
ANISOU  447  C   LEU A 100     4727   8939   7752    230   -525   -358       C  
ATOM    448  O   LEU A 100     -46.740  67.523 -14.611  1.00 61.33           O  
ANISOU  448  O   LEU A 100     5306   9673   8325    329   -616   -391       O  
ATOM    449  CB  LEU A 100     -44.020  67.854 -13.194  1.00 41.15           C  
ANISOU  449  CB  LEU A 100     3092   6834   5709    264   -493   -175       C  
ATOM    450  CG  LEU A 100     -42.625  67.630 -12.605  1.00 37.15           C  
ANISOU  450  CG  LEU A 100     2739   6199   5178    208   -445   -100       C  
ATOM    451  CD1 LEU A 100     -41.759  68.872 -12.774  1.00 50.01           C  
ANISOU  451  CD1 LEU A 100     4479   7793   6731    311   -450     -4       C  
ATOM    452  CD2 LEU A 100     -42.725  67.245 -11.140  1.00 53.81           C  
ANISOU  452  CD2 LEU A 100     4872   8223   7350    112   -340    -90       C  
ATOM    453  N   GLN A 101     -47.252  67.202 -12.445  1.00 44.82           N  
ANISOU  453  N   GLN A 101     3200   7461   6367    180   -445   -379       N  
ATOM    454  CA  GLN A 101     -48.624  67.675 -12.582  1.00 52.43           C  
ANISOU  454  CA  GLN A 101     4009   8543   7370    238   -466   -445       C  
ATOM    455  C   GLN A 101     -48.701  69.162 -12.271  1.00 54.39           C  
ANISOU  455  C   GLN A 101     4299   8796   7569    366   -451   -353       C  
ATOM    456  O   GLN A 101     -48.700  69.561 -11.109  1.00 56.39           O  
ANISOU  456  O   GLN A 101     4603   8969   7853    339   -358   -298       O  
ATOM    457  CB  GLN A 101     -49.562  66.891 -11.660  1.00 90.58           C  
ANISOU  457  CB  GLN A 101     8739  13356  12322    114   -378   -524       C  
ATOM    458  CG  GLN A 101     -49.698  65.420 -12.020  1.00131.47           C  
ANISOU  458  CG  GLN A 101    13851  18537  17564    -12   -382   -634       C  
ATOM    459  CD  GLN A 101     -50.263  65.213 -13.411  1.00156.25           C  
ANISOU  459  CD  GLN A 101    16856  21826  20686     40   -505   -743       C  
ATOM    460  NE2 GLN A 101     -49.761  64.199 -14.109  1.00163.50           N  
ANISOU  460  NE2 GLN A 101    17787  22736  21598    -25   -546   -797       N  
ATOM    461  OE1 GLN A 101     -51.142  65.952 -13.854  1.00155.52           O  
ANISOU  461  OE1 GLN A 101    16651  21860  20582    144   -564   -780       O  
ATOM    462  N   ILE A 102     -48.760  69.978 -13.319  1.00 43.90           N  
ANISOU  462  N   ILE A 102     2958   7561   6163    510   -539   -337       N  
ATOM    463  CA  ILE A 102     -48.773  71.426 -13.159  1.00 38.65           C  
ANISOU  463  CA  ILE A 102     2345   6895   5444    644   -523   -245       C  
ATOM    464  C   ILE A 102     -50.110  71.909 -12.616  1.00 40.94           C  
ANISOU  464  C   ILE A 102     2507   7255   5794    677   -490   -284       C  
ATOM    465  O   ILE A 102     -51.102  71.950 -13.340  1.00 50.70           O  
ANISOU  465  O   ILE A 102     3601   8630   7032    747   -560   -363       O  
ATOM    466  CB  ILE A 102     -48.494  72.161 -14.490  1.00 70.61           C  
ANISOU  466  CB  ILE A 102     6425  11020   9385    802   -615   -213       C  
ATOM    467  CG1 ILE A 102     -47.187  71.677 -15.124  1.00 39.99           C  
ANISOU  467  CG1 ILE A 102     2676   7074   5444    772   -646   -179       C  
ATOM    468  CG2 ILE A 102     -48.474  73.673 -14.267  1.00 38.15           C  
ANISOU  468  CG2 ILE A 102     2378   6891   5227    939   -578   -112       C  
ATOM    469  CD1 ILE A 102     -45.962  71.977 -14.296  1.00 48.57           C  
ANISOU  469  CD1 ILE A 102     3922   8009   6525    724   -567    -77       C  
ATOM    470  N   SER A 103     -50.131  72.277 -11.340  1.00 70.31           N  
ANISOU  470  N   SER A 103     6276  10883   9558    631   -386   -233       N  
ATOM    471  CA  SER A 103     -51.330  72.829 -10.727  1.00 37.60           C  
ANISOU  471  CA  SER A 103     2027   6792   5469    666   -341   -257       C  
ATOM    472  C   SER A 103     -51.649  74.188 -11.320  1.00 53.84           C  
ANISOU  472  C   SER A 103     4079   8924   7455    850   -384   -207       C  
ATOM    473  O   SER A 103     -52.798  74.488 -11.632  1.00 55.15           O  
ANISOU  473  O   SER A 103     4106   9212   7638    927   -418   -264       O  
ATOM    474  CB  SER A 103     -51.142  72.992  -9.217  1.00 55.81           C  
ANISOU  474  CB  SER A 103     4411   8971   7824    587   -216   -201       C  
ATOM    475  OG  SER A 103     -50.928  71.747  -8.576  1.00106.85           O  
ANISOU  475  OG  SER A 103    10883  15362  14353    428   -162   -242       O  
ATOM    476  N   ARG A 104     -50.621  75.009 -11.481  1.00 73.69           N  
ANISOU  476  N   ARG A 104     6746  11364   9889    923   -376   -100       N  
ATOM    477  CA  ARG A 104     -50.841  76.422 -11.731  1.00 69.72           C  
ANISOU  477  CA  ARG A 104     6273  10891   9327   1089   -373    -30       C  
ATOM    478  C   ARG A 104     -49.597  77.116 -12.286  1.00 65.84           C  
ANISOU  478  C   ARG A 104     5946  10326   8744   1165   -379     69       C  
ATOM    479  O   ARG A 104     -48.482  76.877 -11.822  1.00 72.12           O  
ANISOU  479  O   ARG A 104     6864  11000   9538   1077   -336    113       O  
ATOM    480  CB  ARG A 104     -51.282  77.087 -10.423  1.00 65.62           C  
ANISOU  480  CB  ARG A 104     5763  10310   8862   1073   -267      6       C  
ATOM    481  CG  ARG A 104     -51.599  78.554 -10.530  1.00 64.68           C  
ANISOU  481  CG  ARG A 104     5672  10210   8694   1237   -245     77       C  
ATOM    482  CD  ARG A 104     -52.609  78.795 -11.624  1.00120.84           C  
ANISOU  482  CD  ARG A 104    12653  17489  15772   1379   -336     27       C  
ATOM    483  NE  ARG A 104     -52.998  80.197 -11.703  1.00160.50           N  
ANISOU  483  NE  ARG A 104    17701  22532  20748   1548   -307     97       N  
ATOM    484  CZ  ARG A 104     -53.720  80.713 -12.691  1.00165.97           C  
ANISOU  484  CZ  ARG A 104    18318  23360  21383   1717   -378     83       C  
ATOM    485  NH1 ARG A 104     -54.126  79.939 -13.689  1.00144.59           N1+
ANISOU  485  NH1 ARG A 104    15496  20787  18656   1736   -490     -6       N1+
ATOM    486  NH2 ARG A 104     -54.032  82.001 -12.684  1.00174.72           N  
ANISOU  486  NH2 ARG A 104    19465  24472  22450   1873   -337    157       N  
ATOM    487  N   ALA A 105     -49.796  77.972 -13.285  1.00 38.78           N  
ANISOU  487  N   ALA A 105     2520   6976   5240   1335   -430    101       N  
ATOM    488  CA  ALA A 105     -48.705  78.754 -13.856  1.00 43.33           C  
ANISOU  488  CA  ALA A 105     3251   7480   5732   1424   -420    197       C  
ATOM    489  C   ALA A 105     -49.174  80.160 -14.200  1.00 52.44           C  
ANISOU  489  C   ALA A 105     4424   8671   6831   1613   -399    263       C  
ATOM    490  O   ALA A 105     -50.259  80.350 -14.752  1.00 74.96           O  
ANISOU  490  O   ALA A 105     7158  11659   9663   1725   -456    221       O  
ATOM    491  CB  ALA A 105     -48.130  78.072 -15.085  1.00 31.76           C  
ANISOU  491  CB  ALA A 105     1800   6060   4206   1437   -513    173       C  
ATOM    492  N   THR A 106     -48.342  81.142 -13.874  1.00 56.93           N  
ANISOU  492  N   THR A 106     5141   9116   7374   1650   -315    360       N  
ATOM    493  CA  THR A 106     -48.689  82.540 -14.071  1.00 66.77           C  
ANISOU  493  CA  THR A 106     6429  10365   8574   1822   -268    433       C  
ATOM    494  C   THR A 106     -47.459  83.345 -14.482  1.00 58.54           C  
ANISOU  494  C   THR A 106     5563   9206   7473   1882   -213    530       C  
ATOM    495  O   THR A 106     -46.326  82.890 -14.322  1.00 56.78           O  
ANISOU  495  O   THR A 106     5428   8886   7261   1770   -196    540       O  
ATOM    496  CB  THR A 106     -49.276  83.136 -12.785  1.00 57.79           C  
ANISOU  496  CB  THR A 106     5272   9181   7505   1794   -175    445       C  
ATOM    497  CG2 THR A 106     -50.561  82.417 -12.409  1.00 67.77           C  
ANISOU  497  CG2 THR A 106     6357  10562   8833   1745   -218    349       C  
ATOM    498  OG1 THR A 106     -48.330  82.982 -11.720  1.00 80.61           O  
ANISOU  498  OG1 THR A 106     8259  11925  10444   1645    -97    466       O  
ATOM    499  N   LEU A 107     -47.690  84.544 -15.008  1.00 59.85           N  
ANISOU  499  N   LEU A 107     5780   9380   7579   2062   -177    600       N  
ATOM    500  CA  LEU A 107     -46.613  85.411 -15.472  1.00 50.66           C  
ANISOU  500  CA  LEU A 107     4782   8103   6362   2136   -108    693       C  
ATOM    501  C   LEU A 107     -46.610  86.733 -14.708  1.00 49.32           C  
ANISOU  501  C   LEU A 107     4696   7829   6216   2189     22    763       C  
ATOM    502  O   LEU A 107     -47.610  87.446 -14.688  1.00 74.16           O  
ANISOU  502  O   LEU A 107     7791  11035   9349   2315     39    779       O  
ATOM    503  CB  LEU A 107     -46.759  85.671 -16.973  1.00 44.68           C  
ANISOU  503  CB  LEU A 107     4039   7439   5499   2321   -171    723       C  
ATOM    504  CG  LEU A 107     -45.756  86.607 -17.647  1.00 47.66           C  
ANISOU  504  CG  LEU A 107     4589   7708   5813   2427    -93    824       C  
ATOM    505  CD1 LEU A 107     -44.334  86.145 -17.407  1.00 47.88           C  
ANISOU  505  CD1 LEU A 107     4717   7602   5873   2271    -59    830       C  
ATOM    506  CD2 LEU A 107     -46.049  86.696 -19.134  1.00 43.84           C  
ANISOU  506  CD2 LEU A 107     4103   7338   5215   2616   -169    845       C  
ATOM    507  N   ARG A 108     -45.481  87.056 -14.082  1.00 59.43           N  
ANISOU  507  N   ARG A 108     6099   8952   7530   2094    114    798       N  
ATOM    508  CA  ARG A 108     -45.358  88.275 -13.288  1.00 56.45           C  
ANISOU  508  CA  ARG A 108     5806   8460   7184   2123    245    853       C  
ATOM    509  C   ARG A 108     -44.395  89.278 -13.916  1.00 54.31           C  
ANISOU  509  C   ARG A 108     5692   8074   6870   2215    335    936       C  
ATOM    510  O   ARG A 108     -43.405  88.894 -14.533  1.00 45.63           O  
ANISOU  510  O   ARG A 108     4659   6934   5746   2179    316    943       O  
ATOM    511  CB  ARG A 108     -44.886  87.942 -11.870  1.00 54.12           C  
ANISOU  511  CB  ARG A 108     5519   8071   6973   1936    295    814       C  
ATOM    512  CG  ARG A 108     -45.712  86.879 -11.169  1.00 53.28           C  
ANISOU  512  CG  ARG A 108     5273   8055   6916   1828    226    735       C  
ATOM    513  CD  ARG A 108     -45.304  86.750  -9.709  1.00 61.03           C  
ANISOU  513  CD  ARG A 108     6281   8939   7968   1675    294    710       C  
ATOM    514  NE  ARG A 108     -46.207  85.884  -8.956  1.00 78.51           N  
ANISOU  514  NE  ARG A 108     8370  11226  10232   1587    256    644       N  
ATOM    515  CZ  ARG A 108     -45.958  85.432  -7.731  1.00 97.39           C  
ANISOU  515  CZ  ARG A 108    10767  13559  12678   1447    293    612       C  
ATOM    516  NH1 ARG A 108     -44.826  85.758  -7.122  1.00110.52           N1+
ANISOU  516  NH1 ARG A 108    12545  15099  14349   1380    359    631       N1+
ATOM    517  NH2 ARG A 108     -46.834  84.647  -7.118  1.00 74.99           N  
ANISOU  517  NH2 ARG A 108     7819  10787   9887   1378    269    556       N  
ATOM    518  N   LYS A 109     -44.690  90.566 -13.747  1.00 91.57           N  
ANISOU  518  N   LYS A 109    10472  12735  11584   2332    441    997       N  
ATOM    519  CA  LYS A 109     -43.808  91.635 -14.224  1.00 75.38           C  
ANISOU  519  CA  LYS A 109     8579  10554   9508   2416    557   1076       C  
ATOM    520  C   LYS A 109     -43.897  92.879 -13.342  1.00 76.85           C  
ANISOU  520  C   LYS A 109     8832  10626   9742   2440    702   1112       C  
ATOM    521  O   LYS A 109     -44.943  93.521 -13.258  1.00 98.85           O  
ANISOU  521  O   LYS A 109    11580  13463  12514   2564    725   1138       O  
ATOM    522  CB  LYS A 109     -44.127  91.995 -15.677  1.00 57.44           C  
ANISOU  522  CB  LYS A 109     6336   8354   7134   2624    529   1138       C  
ATOM    523  CG  LYS A 109     -45.576  92.371 -15.917  1.00 83.29           C  
ANISOU  523  CG  LYS A 109     9520  11761  10365   2792    492   1149       C  
ATOM    524  CD  LYS A 109     -45.835  92.670 -17.385  1.00103.11           C  
ANISOU  524  CD  LYS A 109    12063  14353  12760   3009    456   1207       C  
ATOM    525  CE  LYS A 109     -47.306  92.969 -17.627  1.00118.04           C  
ANISOU  525  CE  LYS A 109    13848  16400  14603   3182    403   1207       C  
ATOM    526  NZ  LYS A 109     -47.619  93.094 -19.076  1.00111.73           N1+
ANISOU  526  NZ  LYS A 109    13063  15711  13678   3399    341   1249       N1+
ATOM    527  N   GLY A 110     -42.789  93.211 -12.686  1.00 95.55           N  
ANISOU  527  N   GLY A 110    11295  12841  12166   2323    798   1108       N  
ATOM    528  CA  GLY A 110     -42.737  94.352 -11.791  1.00105.50           C  
ANISOU  528  CA  GLY A 110    12624  13982  13481   2324    940   1128       C  
ATOM    529  C   GLY A 110     -42.093  94.019 -10.458  1.00119.09           C  
ANISOU  529  C   GLY A 110    14339  15626  15283   2124    964   1058       C  
ATOM    530  O   GLY A 110     -42.754  93.548  -9.533  1.00116.79           O  
ANISOU  530  O   GLY A 110    13955  15394  15025   2050    921   1009       O  
TER     531      GLY A 110 
ATOM    532  N   ARG A 114     -47.253  98.283  -9.190  1.00101.43           N  
ANISOU  532  N   ARG A 114    12018  13484  13036   2736   1259   1231       N  
ATOM    533  CA  ARG A 114     -45.990  98.012  -9.846  1.00104.92           C  
ANISOU  533  CA  ARG A 114    12549  13854  13464   2680   1258   1238       C  
ATOM    534  C   ARG A 114     -45.845  96.533 -10.078  1.00126.75           C  
ANISOU  534  C   ARG A 114    15213  16729  16216   2566   1098   1176       C  
ATOM    535  O   ARG A 114     -44.810  96.025 -10.513  1.00117.20           O  
ANISOU  535  O   ARG A 114    14052  15480  14999   2488   1071   1165       O  
ATOM    536  CB  ARG A 114     -44.871  98.457  -8.955  0.00 91.19           C  
ANISOU  536  CB  ARG A 114    10908  11943  11798   2536   1373   1210       C  
ATOM    537  CG  ARG A 114     -43.598  97.900  -9.396  0.00109.14           C  
ANISOU  537  CG  ARG A 114    13236  14162  14071   2434   1348   1190       C  
ATOM    538  CD  ARG A 114     -42.580  98.246  -8.414  0.00133.44           C  
ANISOU  538  CD  ARG A 114    16383  17094  17224   2285   1445   1143       C  
ATOM    539  NE  ARG A 114     -41.621  99.096  -9.068  0.00169.63           N  
ANISOU  539  NE  ARG A 114    21104  21539  21810   2332   1567   1188       N  
ATOM    540  CZ  ARG A 114     -40.809  98.658 -10.011  0.00197.02           C  
ANISOU  540  CZ  ARG A 114    24613  24999  25248   2327   1532   1202       C  
ATOM    541  NH1 ARG A 114     -40.853  97.388 -10.382  0.00207.76           N1+
ANISOU  541  NH1 ARG A 114    25886  26483  26572   2275   1375   1173       N1+
ATOM    542  NH2 ARG A 114     -39.953  99.484 -10.577  0.00203.37           N  
ANISOU  542  NH2 ARG A 114    25544  25666  26060   2371   1662   1243       N  
ATOM    543  N   LEU A 115     -46.906  95.830  -9.764  1.00141.68           N  
ANISOU  543  N   LEU A 115    16962  18760  18111   2554    997   1132       N  
ATOM    544  CA  LEU A 115     -46.874  94.410  -9.899  1.00128.40           C  
ANISOU  544  CA  LEU A 115    15179  17181  16427   2441    856   1066       C  
ATOM    545  C   LEU A 115     -48.090  94.005 -10.682  1.00120.88           C  
ANISOU  545  C   LEU A 115    14102  16407  15421   2569    746   1061       C  
ATOM    546  O   LEU A 115     -49.158  94.598 -10.553  1.00127.34           O  
ANISOU  546  O   LEU A 115    14868  17284  16233   2687    768   1080       O  
ATOM    547  CB  LEU A 115     -46.862  93.771  -8.525  1.00137.52           C  
ANISOU  547  CB  LEU A 115    16274  18319  17658   2254    848    993       C  
ATOM    548  CG  LEU A 115     -46.956  92.258  -8.566  1.00116.36           C  
ANISOU  548  CG  LEU A 115    13484  15744  14984   2135    712    923       C  
ATOM    549  CD1 LEU A 115     -45.942  91.714  -9.545  1.00 80.81           C  
ANISOU  549  CD1 LEU A 115     9036  11229  10440   2113    657    930       C  
ATOM    550  CD2 LEU A 115     -46.736  91.694  -7.182  1.00136.22           C  
ANISOU  550  CD2 LEU A 115    15975  18215  17568   1955    728    863       C  
ATOM    551  N   SER A 116     -47.912  93.002 -11.520  1.00119.65           N  
ANISOU  551  N   SER A 116    13895  16340  15225   2548    627   1032       N  
ATOM    552  CA  SER A 116     -48.985  92.526 -12.353  1.00117.77           C  
ANISOU  552  CA  SER A 116    13531  16283  14935   2663    509   1010       C  
ATOM    553  C   SER A 116     -48.766  91.057 -12.614  1.00110.57           C  
ANISOU  553  C   SER A 116    12532  15451  14029   2532    380    933       C  
ATOM    554  O   SER A 116     -47.639  90.619 -12.839  1.00106.30           O  
ANISOU  554  O   SER A 116    12068  14836  13485   2439    374    934       O  
ATOM    555  CB  SER A 116     -49.007  93.298 -13.667  1.00114.78           C  
ANISOU  555  CB  SER A 116    13226  15927  14456   2884    521   1090       C  
ATOM    556  OG  SER A 116     -49.262  94.668 -13.445  1.00112.47           O  
ANISOU  556  OG  SER A 116    13018  15557  14158   3016    651   1165       O  
ATOM    557  N   GLU A 117     -49.847  90.295 -12.570  1.00105.78           N  
ANISOU  557  N   GLU A 117    11763  14993  13436   2522    282    862       N  
ATOM    558  CA  GLU A 117     -49.765  88.871 -12.825  1.00 83.51           C  
ANISOU  558  CA  GLU A 117     8849  12253  10627   2399    164    781       C  
ATOM    559  C   GLU A 117     -50.912  88.454 -13.727  1.00 77.40           C  
ANISOU  559  C   GLU A 117     7927  11673   9807   2518     46    732       C  
ATOM    560  O   GLU A 117     -51.948  89.114 -13.774  1.00 95.51           O  
ANISOU  560  O   GLU A 117    10157  14047  12086   2657     54    742       O  
ATOM    561  CB  GLU A 117     -49.794  88.090 -11.513  1.00 72.41           C  
ANISOU  561  CB  GLU A 117     7385  10810   9318   2194    178    715       C  
ATOM    562  CG  GLU A 117     -49.169  86.717 -11.607  1.00116.76           C  
ANISOU  562  CG  GLU A 117    12976  16435  14954   2035    100    653       C  
ATOM    563  CD  GLU A 117     -49.139  86.001 -10.273  1.00139.46           C  
ANISOU  563  CD  GLU A 117    15814  19258  17916   1847    131    600       C  
ATOM    564  OE1 GLU A 117     -48.884  84.783 -10.255  1.00135.26           O  
ANISOU  564  OE1 GLU A 117    15237  18748  17408   1718     69    541       O  
ATOM    565  OE2 GLU A 117     -49.374  86.649  -9.237  1.00147.77           O1-
ANISOU  565  OE2 GLU A 117    16888  20246  19011   1831    221    619       O1-
ATOM    566  N   GLU A 118     -50.716  87.362 -14.449  1.00 70.56           N  
ANISOU  566  N   GLU A 118     7005  10885   8919   2465    -65    673       N  
ATOM    567  CA  GLU A 118     -51.701  86.888 -15.405  1.00 73.79           C  
ANISOU  567  CA  GLU A 118     7272  11485   9280   2573   -188    610       C  
ATOM    568  C   GLU A 118     -51.521  85.394 -15.618  1.00 61.07           C  
ANISOU  568  C   GLU A 118     5573   9932   7698   2419   -291    512       C  
ATOM    569  O   GLU A 118     -50.396  84.904 -15.657  1.00 73.92           O  
ANISOU  569  O   GLU A 118     7296  11464   9329   2308   -284    526       O  
ATOM    570  CB  GLU A 118     -51.551  87.633 -16.733  1.00 93.55           C  
ANISOU  570  CB  GLU A 118     9852  14032  11660   2794   -210    681       C  
ATOM    571  CG  GLU A 118     -51.956  89.096 -16.675  1.00120.75           C  
ANISOU  571  CG  GLU A 118    13367  17446  15068   2980   -114    773       C  
ATOM    572  CD  GLU A 118     -53.264  89.355 -17.378  1.00159.60           C  
ANISOU  572  CD  GLU A 118    18160  22557  19924   3182   -193    747       C  
ATOM    573  OE1 GLU A 118     -53.697  88.475 -18.149  1.00175.62           O  
ANISOU  573  OE1 GLU A 118    20068  24741  21918   3199   -327    663       O  
ATOM    574  OE2 GLU A 118     -53.855  90.434 -17.168  1.00165.25           O1-
ANISOU  574  OE2 GLU A 118    18895  23270  20622   3326   -122    805       O1-
ATOM    575  N   PRO A 119     -52.632  84.662 -15.756  1.00 65.38           N  
ANISOU  575  N   PRO A 119     5936  10635   8270   2411   -382    408       N  
ATOM    576  CA  PRO A 119     -52.578  83.206 -15.892  1.00 81.56           C  
ANISOU  576  CA  PRO A 119     7890  12738  10361   2256   -469    302       C  
ATOM    577  C   PRO A 119     -51.949  82.814 -17.214  1.00 78.28           C  
ANISOU  577  C   PRO A 119     7518  12369   9854   2317   -558    302       C  
ATOM    578  O   PRO A 119     -52.063  83.555 -18.191  1.00 68.58           O  
ANISOU  578  O   PRO A 119     6327  11204   8525   2516   -587    351       O  
ATOM    579  CB  PRO A 119     -54.057  82.796 -15.892  1.00 75.60           C  
ANISOU  579  CB  PRO A 119     6922  12155   9647   2281   -538    192       C  
ATOM    580  CG  PRO A 119     -54.803  83.983 -15.376  1.00 72.43           C  
ANISOU  580  CG  PRO A 119     6512  11758   9248   2405   -466    245       C  
ATOM    581  CD  PRO A 119     -54.011  85.165 -15.819  1.00 62.37           C  
ANISOU  581  CD  PRO A 119     5422  10393   7884   2551   -406    377       C  
ATOM    582  N   LEU A 120     -51.288  81.663 -17.241  1.00 64.77           N  
ANISOU  582  N   LEU A 120     5810  10624   8175   2156   -596    250       N  
ATOM    583  CA  LEU A 120     -50.744  81.130 -18.480  1.00 61.06           C  
ANISOU  583  CA  LEU A 120     5367  10207   7626   2198   -687    234       C  
ATOM    584  C   LEU A 120     -51.438  79.822 -18.830  1.00 53.52           C  
ANISOU  584  C   LEU A 120     4239   9391   6707   2115   -798     90       C  
ATOM    585  O   LEU A 120     -51.525  78.920 -17.997  1.00 66.79           O  
ANISOU  585  O   LEU A 120     5855  11032   8488   1928   -779     23       O  
ATOM    586  CB  LEU A 120     -49.236  80.891 -18.354  1.00 56.78           C  
ANISOU  586  CB  LEU A 120     4988   9502   7083   2086   -636    296       C  
ATOM    587  CG  LEU A 120     -48.311  82.089 -18.133  1.00 50.92           C  
ANISOU  587  CG  LEU A 120     4430   8609   6308   2149   -524    427       C  
ATOM    588  CD1 LEU A 120     -46.884  81.609 -17.905  1.00 55.69           C  
ANISOU  588  CD1 LEU A 120     5159   9069   6932   2006   -486    456       C  
ATOM    589  CD2 LEU A 120     -48.375  83.057 -19.302  1.00 50.21           C  
ANISOU  589  CD2 LEU A 120     4403   8573   6102   2382   -538    497       C  
ATOM    590  N   GLN A 121     -51.944  79.729 -20.056  1.00 55.89           N  
ANISOU  590  N   GLN A 121     4470   9847   6919   2253   -906     39       N  
ATOM    591  CA  GLN A 121     -52.469  78.472 -20.565  1.00 68.88           C  
ANISOU  591  CA  GLN A 121     5970  11619   8584   2173  -1013   -108       C  
ATOM    592  C   GLN A 121     -51.323  77.462 -20.552  1.00 76.24           C  
ANISOU  592  C   GLN A 121     6993  12437   9539   1997  -1007   -115       C  
ATOM    593  O   GLN A 121     -50.176  77.817 -20.839  1.00 69.07           O  
ANISOU  593  O   GLN A 121     6253  11420   8572   2021   -970    -15       O  
ATOM    594  CB  GLN A 121     -53.009  78.658 -21.985  1.00 82.68           C  
ANISOU  594  CB  GLN A 121     7659  13548  10208   2375  -1131   -150       C  
ATOM    595  CG  GLN A 121     -53.720  77.442 -22.561  1.00110.99           C  
ANISOU  595  CG  GLN A 121    11068  17290  13813   2312  -1250   -323       C  
ATOM    596  CD  GLN A 121     -55.155  77.328 -22.091  1.00141.44           C  
ANISOU  596  CD  GLN A 121    14711  21278  17750   2307  -1276   -437       C  
ATOM    597  NE2 GLN A 121     -55.801  76.217 -22.425  1.00136.47           N  
ANISOU  597  NE2 GLN A 121    13913  20771  17168   2221  -1364   -603       N  
ATOM    598  OE1 GLN A 121     -55.679  78.231 -21.441  1.00161.18           O  
ANISOU  598  OE1 GLN A 121    17197  23769  20275   2379  -1215   -380       O  
ATOM    599  N   VAL A 122     -51.619  76.212 -20.206  1.00 55.89           N  
ANISOU  599  N   VAL A 122     4305   9879   7050   1821  -1033   -233       N  
ATOM    600  CA  VAL A 122     -50.573  75.196 -20.096  1.00 59.51           C  
ANISOU  600  CA  VAL A 122     4848  10226   7539   1650  -1018   -242       C  
ATOM    601  C   VAL A 122     -50.813  73.997 -21.010  1.00 61.11           C  
ANISOU  601  C   VAL A 122     4952  10538   7730   1603  -1124   -374       C  
ATOM    602  O   VAL A 122     -51.811  73.288 -20.874  1.00 66.51           O  
ANISOU  602  O   VAL A 122     5463  11320   8486   1536  -1162   -505       O  
ATOM    603  CB  VAL A 122     -50.413  74.709 -18.642  1.00 52.66           C  
ANISOU  603  CB  VAL A 122     3982   9229   6797   1454   -920   -241       C  
ATOM    604  CG1 VAL A 122     -49.560  73.458 -18.591  1.00 27.07           C  
ANISOU  604  CG1 VAL A 122      791   5904   3591   1282   -919   -278       C  
ATOM    605  CG2 VAL A 122     -49.816  75.805 -17.775  1.00 46.85           C  
ANISOU  605  CG2 VAL A 122     3380   8358   6064   1483   -813   -105       C  
ATOM    606  N   LEU A 123     -49.891  73.775 -21.940  1.00 50.41           N  
ANISOU  606  N   LEU A 123     3705   9162   6288   1635  -1165   -346       N  
ATOM    607  CA  LEU A 123     -49.980  72.646 -22.856  1.00 50.69           C  
ANISOU  607  CA  LEU A 123     3666   9290   6305   1592  -1262   -467       C  
ATOM    608  C   LEU A 123     -48.798  71.702 -22.655  1.00 64.17           C  
ANISOU  608  C   LEU A 123     5483  10854   8044   1423  -1225   -452       C  
ATOM    609  O   LEU A 123     -47.661  72.147 -22.511  1.00 57.16           O  
ANISOU  609  O   LEU A 123     4764   9834   7118   1426  -1164   -331       O  
ATOM    610  CB  LEU A 123     -50.003  73.137 -24.304  1.00 43.22           C  
ANISOU  610  CB  LEU A 123     2740   8469   5211   1799  -1358   -460       C  
ATOM    611  CG  LEU A 123     -50.931  74.298 -24.657  1.00 54.54           C  
ANISOU  611  CG  LEU A 123     4114  10033   6575   2018  -1391   -437       C  
ATOM    612  CD1 LEU A 123     -50.772  74.666 -26.125  1.00 56.31           C  
ANISOU  612  CD1 LEU A 123     4387  10368   6642   2222  -1479   -422       C  
ATOM    613  CD2 LEU A 123     -52.380  73.965 -24.337  1.00 56.10           C  
ANISOU  613  CD2 LEU A 123     4087  10376   6851   1996  -1438   -577       C  
ATOM    614  N   GLU A 124     -49.060  70.399 -22.653  1.00 50.75           N  
ANISOU  614  N   GLU A 124     3685   9182   6416   1279  -1257   -578       N  
ATOM    615  CA  GLU A 124     -47.981  69.429 -22.502  1.00 60.77           C  
ANISOU  615  CA  GLU A 124     5053  10323   7713   1126  -1223   -569       C  
ATOM    616  C   GLU A 124     -47.712  68.648 -23.785  1.00 42.40           C  
ANISOU  616  C   GLU A 124     2718   8071   5319   1145  -1318   -647       C  
ATOM    617  O   GLU A 124     -48.630  68.336 -24.543  1.00 60.98           O  
ANISOU  617  O   GLU A 124     4927  10586   7656   1201  -1412   -770       O  
ATOM    618  CB  GLU A 124     -48.253  68.467 -21.338  1.00 52.46           C  
ANISOU  618  CB  GLU A 124     3932   9197   6803    924  -1154   -632       C  
ATOM    619  CG  GLU A 124     -49.437  67.536 -21.549  1.00 91.96           C  
ANISOU  619  CG  GLU A 124     8732  14326  11881    858  -1208   -806       C  
ATOM    620  CD  GLU A 124     -49.607  66.537 -20.416  1.00101.21           C  
ANISOU  620  CD  GLU A 124     9855  15405  13197    654  -1120   -860       C  
ATOM    621  OE1 GLU A 124     -48.666  66.376 -19.610  1.00 96.63           O  
ANISOU  621  OE1 GLU A 124     9409  14665  12641    562  -1033   -767       O  
ATOM    622  OE2 GLU A 124     -50.684  65.908 -20.336  1.00 73.70           O1-
ANISOU  622  OE2 GLU A 124     6195  12008   9801    588  -1135   -999       O1-
ATOM    623  N   HIS A 125     -46.438  68.357 -24.024  1.00 63.76           N  
ANISOU  623  N   HIS A 125     5577  10664   7985   1104  -1295   -577       N  
ATOM    624  CA  HIS A 125     -46.023  67.465 -25.099  1.00 61.64           C  
ANISOU  624  CA  HIS A 125     5317  10436   7666   1091  -1367   -647       C  
ATOM    625  C   HIS A 125     -45.073  66.430 -24.512  1.00 68.38           C  
ANISOU  625  C   HIS A 125     6253  11139   8590    906  -1303   -636       C  
ATOM    626  O   HIS A 125     -43.852  66.561 -24.624  1.00 50.61           O  
ANISOU  626  O   HIS A 125     4161   8777   6291    906  -1267   -537       O  
ATOM    627  CB  HIS A 125     -45.323  68.231 -26.218  1.00 65.55           C  
ANISOU  627  CB  HIS A 125     5935  10952   8018   1264  -1407   -561       C  
ATOM    628  CG  HIS A 125     -45.029  67.394 -27.423  1.00 74.31           C  
ANISOU  628  CG  HIS A 125     7042  12129   9065   1276  -1491   -639       C  
ATOM    629  CD2 HIS A 125     -44.619  66.108 -27.534  1.00 63.10           C  
ANISOU  629  CD2 HIS A 125     5616  10668   7692   1132  -1501   -716       C  
ATOM    630  ND1 HIS A 125     -45.177  67.861 -28.711  1.00100.03           N  
ANISOU  630  ND1 HIS A 125    10303  15512  12192   1462  -1578   -647       N  
ATOM    631  CE1 HIS A 125     -44.859  66.903 -29.564  1.00 89.59           C  
ANISOU  631  CE1 HIS A 125     8975  14225  10839   1428  -1640   -728       C  
ATOM    632  NE2 HIS A 125     -44.517  65.828 -28.875  1.00 65.04           N  
ANISOU  632  NE2 HIS A 125     5859  11015   7839   1226  -1594   -771       N  
ATOM    633  N   PRO A 126     -45.639  65.398 -23.875  1.00 60.10           N  
ANISOU  633  N   PRO A 126     5094  10085   7658    751  -1283   -741       N  
ATOM    634  CA  PRO A 126     -44.905  64.366 -23.135  1.00 57.75           C  
ANISOU  634  CA  PRO A 126     4858   9644   7439    572  -1209   -736       C  
ATOM    635  C   PRO A 126     -43.812  63.700 -23.968  1.00 59.12           C  
ANISOU  635  C   PRO A 126     5139   9772   7552    554  -1238   -726       C  
ATOM    636  O   PRO A 126     -42.738  63.404 -23.443  1.00 63.82           O  
ANISOU  636  O   PRO A 126     5863  10226   8161    474  -1170   -647       O  
ATOM    637  CB  PRO A 126     -45.999  63.353 -22.784  1.00 50.82           C  
ANISOU  637  CB  PRO A 126     3804   8825   6680    448  -1210   -888       C  
ATOM    638  CG  PRO A 126     -47.246  64.166 -22.734  1.00 44.58           C  
ANISOU  638  CG  PRO A 126     2877   8163   5898    544  -1242   -930       C  
ATOM    639  CD  PRO A 126     -47.094  65.181 -23.827  1.00 40.16           C  
ANISOU  639  CD  PRO A 126     2366   7697   5198    744  -1325   -877       C  
ATOM    640  N   ARG A 127     -44.087  63.468 -25.245  1.00 55.77           N  
ANISOU  640  N   ARG A 127     4658   9471   7059    634  -1339   -808       N  
ATOM    641  CA  ARG A 127     -43.092  62.887 -26.134  1.00 57.39           C  
ANISOU  641  CA  ARG A 127     4963   9644   7200    633  -1370   -801       C  
ATOM    642  C   ARG A 127     -41.780  63.650 -26.039  1.00 70.06           C  
ANISOU  642  C   ARG A 127     6760  11124   8735    687  -1314   -637       C  
ATOM    643  O   ARG A 127     -40.720  63.072 -25.801  1.00 80.83           O  
ANISOU  643  O   ARG A 127     8233  12366  10114    597  -1265   -591       O  
ATOM    644  CB  ARG A 127     -43.595  62.913 -27.572  0.00 94.92           C  
ANISOU  644  CB  ARG A 127     9641  14564  11859    763  -1491   -891       C  
ATOM    645  CG  ARG A 127     -43.757  61.545 -28.174  0.00123.38           C  
ANISOU  645  CG  ARG A 127    13164  18216  15498    666  -1544  -1038       C  
ATOM    646  CD  ARG A 127     -44.625  61.590 -29.409  0.00135.37           C  
ANISOU  646  CD  ARG A 127    14557  19935  16943    792  -1672  -1162       C  
ATOM    647  NE  ARG A 127     -44.963  60.239 -29.831  0.00132.52           N  
ANISOU  647  NE  ARG A 127    14087  19625  16641    677  -1718  -1330       N  
ATOM    648  CZ  ARG A 127     -44.292  59.558 -30.749  0.00121.45           C  
ANISOU  648  CZ  ARG A 127    12741  18222  15182    674  -1762  -1363       C  
ATOM    649  NH1 ARG A 127     -43.253  60.107 -31.361  0.00 93.54           N1+
ANISOU  649  NH1 ARG A 127     9370  14642  11530    785  -1765  -1238       N1+
ATOM    650  NH2 ARG A 127     -44.665  58.329 -31.058  0.00131.60           N  
ANISOU  650  NH2 ARG A 127    13918  19551  16534    560  -1796  -1525       N  
ATOM    651  N   GLN A 128     -41.866  64.963 -26.219  1.00 72.67           N  
ANISOU  651  N   GLN A 128     7129  11488   8993    837  -1317   -552       N  
ATOM    652  CA  GLN A 128     -40.693  65.819 -26.235  1.00 54.74           C  
ANISOU  652  CA  GLN A 128     5029   9111   6658    902  -1262   -407       C  
ATOM    653  C   GLN A 128     -40.269  66.193 -24.821  1.00 49.11           C  
ANISOU  653  C   GLN A 128     4379   8262   6018    815  -1157   -319       C  
ATOM    654  O   GLN A 128     -39.239  66.835 -24.627  1.00 49.94           O  
ANISOU  654  O   GLN A 128     4619   8263   6092    839  -1099   -208       O  
ATOM    655  CB  GLN A 128     -40.975  67.079 -27.062  1.00 37.30           C  
ANISOU  655  CB  GLN A 128     2838   6993   4342   1106  -1301   -354       C  
ATOM    656  CG  GLN A 128     -41.358  66.787 -28.512  1.00 68.61           C  
ANISOU  656  CG  GLN A 128     6750  11105   8214   1218  -1411   -436       C  
ATOM    657  CD  GLN A 128     -41.684  68.040 -29.310  1.00 90.13           C  
ANISOU  657  CD  GLN A 128     9497  13925  10824   1438  -1446   -379       C  
ATOM    658  NE2 GLN A 128     -42.302  67.856 -30.472  1.00 82.81           N  
ANISOU  658  NE2 GLN A 128     8493  13157   9813   1555  -1552   -465       N  
ATOM    659  OE1 GLN A 128     -41.380  69.157 -28.891  1.00108.30           O  
ANISOU  659  OE1 GLN A 128    11884  16157  13108   1507  -1376   -260       O  
ATOM    660  N   GLU A 129     -41.066  65.779 -23.840  1.00 51.50           N  
ANISOU  660  N   GLU A 129     4579   8567   6421    714  -1131   -376       N  
ATOM    661  CA  GLU A 129     -40.833  66.145 -22.448  1.00 41.32           C  
ANISOU  661  CA  GLU A 129     3334   7167   5199    642  -1036   -303       C  
ATOM    662  C   GLU A 129     -40.816  67.664 -22.306  1.00 40.27           C  
ANISOU  662  C   GLU A 129     3253   7030   5018    772  -1007   -202       C  
ATOM    663  O   GLU A 129     -39.949  68.231 -21.637  1.00 49.95           O  
ANISOU  663  O   GLU A 129     4590   8141   6246    758   -934   -104       O  
ATOM    664  CB  GLU A 129     -39.520  65.540 -21.935  1.00 31.29           C  
ANISOU  664  CB  GLU A 129     2191   5750   3949    532   -974   -248       C  
ATOM    665  CG  GLU A 129     -39.417  64.030 -22.109  1.00 57.46           C  
ANISOU  665  CG  GLU A 129     5471   9054   7306    410   -993   -337       C  
ATOM    666  CD  GLU A 129     -38.164  63.443 -21.480  1.00 73.65           C  
ANISOU  666  CD  GLU A 129     7644  10963   9377    310   -928   -278       C  
ATOM    667  OE1 GLU A 129     -37.215  64.209 -21.204  1.00 81.25           O  
ANISOU  667  OE1 GLU A 129     8725  11846  10302    349   -885   -175       O  
ATOM    668  OE2 GLU A 129     -38.128  62.211 -21.260  1.00 50.47           O1-
ANISOU  668  OE2 GLU A 129     4682   7996   6496    194   -917   -339       O1-
ATOM    669  N   GLN A 130     -41.784  68.315 -22.944  1.00 32.03           N  
ANISOU  669  N   GLN A 130     2124   6116   3931    903  -1065   -231       N  
ATOM    670  CA  GLN A 130     -41.854  69.774 -22.967  1.00 48.24           C  
ANISOU  670  CA  GLN A 130     4223   8176   5930   1049  -1041   -138       C  
ATOM    671  C   GLN A 130     -43.219  70.311 -22.529  1.00 50.87           C  
ANISOU  671  C   GLN A 130     4423   8605   6300   1102  -1051   -175       C  
ATOM    672  O   GLN A 130     -44.225  69.607 -22.597  1.00 56.53           O  
ANISOU  672  O   GLN A 130     4994   9422   7061   1062  -1103   -290       O  
ATOM    673  CB  GLN A 130     -41.533  70.289 -24.373  1.00 35.46           C  
ANISOU  673  CB  GLN A 130     2664   6619   4190   1209  -1096   -107       C  
ATOM    674  CG  GLN A 130     -40.104  70.050 -24.821  1.00 44.91           C  
ANISOU  674  CG  GLN A 130     4008   7712   5344   1182  -1071    -47       C  
ATOM    675  CD  GLN A 130     -39.847  70.551 -26.227  1.00 44.64           C  
ANISOU  675  CD  GLN A 130     4031   7741   5188   1347  -1119    -17       C  
ATOM    676  NE2 GLN A 130     -38.578  70.694 -26.582  1.00 38.09           N  
ANISOU  676  NE2 GLN A 130     3342   6812   4320   1351  -1076     59       N  
ATOM    677  OE1 GLN A 130     -40.782  70.803 -26.987  1.00 43.94           O  
ANISOU  677  OE1 GLN A 130     3859   7795   5041   1475  -1192    -64       O  
ATOM    678  N   ILE A 131     -43.241  71.561 -22.073  1.00 55.39           N  
ANISOU  678  N   ILE A 131     5043   9143   6859   1191   -995    -82       N  
ATOM    679  CA  ILE A 131     -44.490  72.273 -21.834  1.00 42.45           C  
ANISOU  679  CA  ILE A 131     3292   7603   5235   1281  -1006   -102       C  
ATOM    680  C   ILE A 131     -44.489  73.540 -22.666  1.00 59.81           C  
ANISOU  680  C   ILE A 131     5550   9849   7327   1489  -1019    -22       C  
ATOM    681  O   ILE A 131     -43.435  74.013 -23.094  1.00 54.99           O  
ANISOU  681  O   ILE A 131     5082   9158   6654   1541   -988     67       O  
ATOM    682  CB  ILE A 131     -44.657  72.743 -20.375  1.00 30.80           C  
ANISOU  682  CB  ILE A 131     1816   6040   3847   1212   -911    -56       C  
ATOM    683  CG1 ILE A 131     -44.180  71.699 -19.377  1.00 56.61           C  
ANISOU  683  CG1 ILE A 131     5098   9203   7207   1014   -860    -83       C  
ATOM    684  CG2 ILE A 131     -46.105  73.111 -20.089  1.00104.04           C  
ANISOU  684  CG2 ILE A 131    10940  15429  13159   1270   -929   -111       C  
ATOM    685  CD1 ILE A 131     -44.210  72.222 -17.963  1.00 67.73           C  
ANISOU  685  CD1 ILE A 131     6527  10522   8687    960   -764    -29       C  
ATOM    686  N   ALA A 132     -45.681  74.093 -22.874  1.00 56.93           N  
ANISOU  686  N   ALA A 132     5073   9614   6944   1611  -1060    -55       N  
ATOM    687  CA  ALA A 132     -45.836  75.416 -23.458  1.00 51.88           C  
ANISOU  687  CA  ALA A 132     4486   9015   6211   1822  -1055     30       C  
ATOM    688  C   ALA A 132     -46.692  76.264 -22.528  1.00 62.69           C  
ANISOU  688  C   ALA A 132     5793  10392   7635   1862  -1002     56       C  
ATOM    689  O   ALA A 132     -47.743  75.826 -22.059  1.00 69.16           O  
ANISOU  689  O   ALA A 132     6459  11295   8522   1808  -1031    -37       O  
ATOM    690  CB  ALA A 132     -46.472  75.322 -24.831  1.00 66.87           C  
ANISOU  690  CB  ALA A 132     6314  11087   8006   1978  -1169    -33       C  
ATOM    691  N   LEU A 133     -46.224  77.476 -22.250  1.00 64.98           N  
ANISOU  691  N   LEU A 133     6200  10589   7900   1952   -916    179       N  
ATOM    692  CA  LEU A 133     -46.966  78.415 -21.425  1.00 49.36           C  
ANISOU  692  CA  LEU A 133     4181   8610   5964   2010   -857    216       C  
ATOM    693  C   LEU A 133     -47.471  79.540 -22.314  1.00 55.39           C  
ANISOU  693  C   LEU A 133     4960   9464   6623   2255   -876    272       C  
ATOM    694  O   LEU A 133     -46.685  80.322 -22.843  1.00 62.31           O  
ANISOU  694  O   LEU A 133     5980  10268   7425   2365   -829    375       O  
ATOM    695  CB  LEU A 133     -46.070  78.975 -20.323  1.00 35.79           C  
ANISOU  695  CB  LEU A 133     2583   6709   4307   1925   -733    310       C  
ATOM    696  CG  LEU A 133     -45.283  77.938 -19.519  1.00 37.73           C  
ANISOU  696  CG  LEU A 133     2854   6848   4633   1704   -707    277       C  
ATOM    697  CD1 LEU A 133     -44.246  78.610 -18.638  1.00 53.27           C  
ANISOU  697  CD1 LEU A 133     4955   8647   6637   1654   -594    372       C  
ATOM    698  CD2 LEU A 133     -46.215  77.073 -18.689  1.00 30.41           C  
ANISOU  698  CD2 LEU A 133     1779   5974   3802   1575   -724    177       C  
ATOM    699  N   LEU A 134     -48.784  79.611 -22.488  1.00 53.04           N  
ANISOU  699  N   LEU A 134     4513   9324   6317   2347   -940    202       N  
ATOM    700  CA  LEU A 134     -49.374  80.621 -23.358  1.00 58.29           C  
ANISOU  700  CA  LEU A 134     5180  10096   6872   2598   -968    247       C  
ATOM    701  C   LEU A 134     -49.764  81.880 -22.593  1.00 69.11           C  
ANISOU  701  C   LEU A 134     6577  11412   8268   2690   -870    335       C  
ATOM    702  O   LEU A 134     -50.507  81.823 -21.611  1.00 53.30           O  
ANISOU  702  O   LEU A 134     4468   9422   6360   2612   -847    291       O  
ATOM    703  CB  LEU A 134     -50.585  80.052 -24.093  1.00 62.13           C  
ANISOU  703  CB  LEU A 134     5485  10803   7320   2675  -1102    116       C  
ATOM    704  CG  LEU A 134     -50.300  78.829 -24.961  1.00 76.69           C  
ANISOU  704  CG  LEU A 134     7292  12716   9130   2604  -1206     16       C  
ATOM    705  CD1 LEU A 134     -51.522  78.467 -25.781  1.00 82.21           C  
ANISOU  705  CD1 LEU A 134     7811  13646   9778   2716  -1340   -115       C  
ATOM    706  CD2 LEU A 134     -49.108  79.092 -25.866  1.00 77.31           C  
ANISOU  706  CD2 LEU A 134     7553  12719   9103   2682  -1190    111       C  
ATOM    707  N   ALA A 135     -49.256  83.017 -23.052  1.00 62.14           N  
ANISOU  707  N   ALA A 135     5842  10465   7304   2857   -804    461       N  
ATOM    708  CA  ALA A 135     -49.555  84.296 -22.424  1.00 50.17           C  
ANISOU  708  CA  ALA A 135     4381   8882   5800   2953   -694    550       C  
ATOM    709  C   ALA A 135     -50.626  85.021 -23.218  1.00 62.71           C  
ANISOU  709  C   ALA A 135     5908  10631   7288   3208   -745    558       C  
ATOM    710  O   ALA A 135     -50.762  84.802 -24.423  1.00 73.29           O  
ANISOU  710  O   ALA A 135     7230  12096   8521   3346   -842    536       O  
ATOM    711  CB  ALA A 135     -48.302  85.147 -22.334  1.00 56.18           C  
ANISOU  711  CB  ALA A 135     5354   9447   6543   2964   -562    680       C  
ATOM    712  N   PRO A 136     -51.403  85.878 -22.538  1.00 85.04           N  
ANISOU  712  N   PRO A 136     8703  13461  10147   3278   -681    588       N  
ATOM    713  CA  PRO A 136     -52.396  86.735 -23.194  1.00 72.37           C  
ANISOU  713  CA  PRO A 136     7057  11996   8446   3540   -710    613       C  
ATOM    714  C   PRO A 136     -51.740  87.641 -24.230  1.00 91.22           C  
ANISOU  714  C   PRO A 136     9625  14336  10699   3751   -661    738       C  
ATOM    715  O   PRO A 136     -52.114  87.620 -25.404  1.00 88.82           O  
ANISOU  715  O   PRO A 136     9294  14181  10272   3941   -756    725       O  
ATOM    716  CB  PRO A 136     -52.941  87.574 -22.039  1.00 50.06           C  
ANISOU  716  CB  PRO A 136     4220   9102   5697   3531   -602    651       C  
ATOM    717  CG  PRO A 136     -52.729  86.734 -20.832  1.00 73.68           C  
ANISOU  717  CG  PRO A 136     7153  12010   8833   3254   -579    582       C  
ATOM    718  CD  PRO A 136     -51.448  85.998 -21.070  1.00 80.85           C  
ANISOU  718  CD  PRO A 136     8159  12813   9745   3110   -584    588       C  
ATOM    719  N   GLU A 137     -50.760  88.420 -23.787  1.00 90.51           N  
ANISOU  719  N   GLU A 137     9718  14038  10633   3717   -510    854       N  
ATOM    720  CA  GLU A 137     -50.056  89.357 -24.653  1.00 74.69           C  
ANISOU  720  CA  GLU A 137     7905  11953   8521   3901   -429    983       C  
ATOM    721  C   GLU A 137     -48.626  88.882 -24.876  1.00 82.64           C  
ANISOU  721  C   GLU A 137     9040  12819   9541   3763   -395   1010       C  
ATOM    722  O   GLU A 137     -48.104  88.098 -24.085  1.00108.47           O  
ANISOU  722  O   GLU A 137    12281  16014  12920   3521   -396    953       O  
ATOM    723  CB  GLU A 137     -50.045  90.743 -24.009  1.00103.88           C  
ANISOU  723  CB  GLU A 137    11717  15511  12241   3983   -261   1095       C  
ATOM    724  CG  GLU A 137     -51.362  91.129 -23.350  1.00134.78           C  
ANISOU  724  CG  GLU A 137    15496  19523  16189   4044   -272   1060       C  
ATOM    725  CD  GLU A 137     -51.243  92.371 -22.486  1.00150.91           C  
ANISOU  725  CD  GLU A 137    17653  21403  18283   4067    -97   1158       C  
ATOM    726  OE1 GLU A 137     -50.119  92.900 -22.354  1.00158.70           O  
ANISOU  726  OE1 GLU A 137    18816  22196  19288   4020     33   1243       O  
ATOM    727  OE2 GLU A 137     -52.275  92.816 -21.936  1.00140.04           O1-
ANISOU  727  OE2 GLU A 137    16185  20091  16932   4131    -88   1144       O1-
ATOM    728  N   PRO A 138     -47.988  89.354 -25.957  1.00 86.06           N  
ANISOU  728  N   PRO A 138     9620  13218   9862   3923   -360   1097       N  
ATOM    729  CA  PRO A 138     -46.580  89.049 -26.244  1.00 77.00           C  
ANISOU  729  CA  PRO A 138     8609  11927   8721   3814   -311   1135       C  
ATOM    730  C   PRO A 138     -45.647  89.627 -25.181  1.00 64.50           C  
ANISOU  730  C   PRO A 138     7145  10114   7250   3661   -146   1196       C  
ATOM    731  O   PRO A 138     -46.028  90.558 -24.469  1.00 82.10           O  
ANISOU  731  O   PRO A 138     9396  12280   9519   3700    -45   1241       O  
ATOM    732  CB  PRO A 138     -46.335  89.751 -27.585  1.00 79.32           C  
ANISOU  732  CB  PRO A 138     9040  12234   8863   4071   -280   1235       C  
ATOM    733  CG  PRO A 138     -47.411  90.788 -27.676  1.00 91.41           C  
ANISOU  733  CG  PRO A 138    10556  13844  10331   4303   -250   1285       C  
ATOM    734  CD  PRO A 138     -48.598  90.166 -27.020  1.00 68.16           C  
ANISOU  734  CD  PRO A 138     7393  11057   7447   4228   -370   1164       C  
ATOM    735  N   LEU A 139     -44.440  89.081 -25.076  1.00 55.20           N  
ANISOU  735  N   LEU A 139     6038   8816   6120   3490   -120   1190       N  
ATOM    736  CA  LEU A 139     -43.478  89.566 -24.095  1.00 65.17           C  
ANISOU  736  CA  LEU A 139     7405   9870   7486   3338     27   1231       C  
ATOM    737  C   LEU A 139     -42.669  90.722 -24.670  1.00 73.79           C  
ANISOU  737  C   LEU A 139     8694  10815   8529   3473    182   1354       C  
ATOM    738  O   LEU A 139     -42.286  90.700 -25.838  1.00 88.01           O  
ANISOU  738  O   LEU A 139    10573  12637  10231   3597    168   1398       O  
ATOM    739  CB  LEU A 139     -42.539  88.443 -23.645  1.00 49.55           C  
ANISOU  739  CB  LEU A 139     5407   7833   5588   3091    -14   1162       C  
ATOM    740  CG  LEU A 139     -43.130  87.105 -23.196  1.00 46.69           C  
ANISOU  740  CG  LEU A 139     4868   7597   5275   2939   -159   1039       C  
ATOM    741  CD1 LEU A 139     -42.079  86.318 -22.435  1.00 38.27           C  
ANISOU  741  CD1 LEU A 139     3819   6418   4303   2696   -144    998       C  
ATOM    742  CD2 LEU A 139     -44.374  87.283 -22.341  1.00 57.11           C  
ANISOU  742  CD2 LEU A 139     6059   8996   6644   2941   -177    996       C  
ATOM    743  N   LEU A 140     -42.409  91.733 -23.849  1.00 70.60           N  
ANISOU  743  N   LEU A 140     8372  10258   8195   3449    336   1408       N  
ATOM    744  CA  LEU A 140     -41.600  92.863 -24.281  1.00 53.15           C  
ANISOU  744  CA  LEU A 140     6350   7883   5959   3554    509   1518       C  
ATOM    745  C   LEU A 140     -40.117  92.525 -24.242  1.00 74.94           C  
ANISOU  745  C   LEU A 140     9202  10494   8776   3388    568   1514       C  
ATOM    746  O   LEU A 140     -39.576  92.168 -23.196  1.00 96.91           O  
ANISOU  746  O   LEU A 140    11952  13197  11671   3172    584   1456       O  
ATOM    747  CB  LEU A 140     -41.879  94.089 -23.415  1.00 59.11           C  
ANISOU  747  CB  LEU A 140     7158   8526   6775   3587    660   1568       C  
ATOM    748  CG  LEU A 140     -43.345  94.515 -23.386  1.00 78.90           C  
ANISOU  748  CG  LEU A 140     9576  11171   9230   3758    615   1576       C  
ATOM    749  CD1 LEU A 140     -43.500  95.849 -22.667  1.00 83.22           C  
ANISOU  749  CD1 LEU A 140    10207  11585   9828   3812    789   1642       C  
ATOM    750  CD2 LEU A 140     -43.893  94.587 -24.803  1.00 55.21           C  
ANISOU  750  CD2 LEU A 140     6593   8310   6076   4014    546   1625       C  
ATOM    751  N   VAL A 141     -39.470  92.644 -25.394  1.00 64.95           N  
ANISOU  751  N   VAL A 141     8051   9198   7430   3497    601   1575       N  
ATOM    752  CA  VAL A 141     -38.055  92.327 -25.529  1.00 64.65           C  
ANISOU  752  CA  VAL A 141     8101   9028   7435   3361    657   1574       C  
ATOM    753  C   VAL A 141     -37.190  93.093 -24.528  1.00 59.79           C  
ANISOU  753  C   VAL A 141     7568   8206   6943   3226    828   1586       C  
ATOM    754  O   VAL A 141     -37.315  94.308 -24.388  1.00 66.78           O  
ANISOU  754  O   VAL A 141     8545   8991   7838   3330    978   1656       O  
ATOM    755  CB  VAL A 141     -37.556  92.625 -26.956  1.00 50.66           C  
ANISOU  755  CB  VAL A 141     6465   7233   5551   3539    705   1660       C  
ATOM    756  CG1 VAL A 141     -36.079  92.289 -27.089  1.00 31.64           C  
ANISOU  756  CG1 VAL A 141     4141   4687   3195   3393    768   1654       C  
ATOM    757  CG2 VAL A 141     -38.384  91.859 -27.980  1.00 62.90           C  
ANISOU  757  CG2 VAL A 141     7932   8997   6971   3679    528   1637       C  
ATOM    758  N   GLY A 142     -36.313  92.372 -23.833  1.00 60.02           N  
ANISOU  758  N   GLY A 142     7564   8175   7065   2997    806   1513       N  
ATOM    759  CA  GLY A 142     -35.365  92.986 -22.921  1.00 56.57           C  
ANISOU  759  CA  GLY A 142     7196   7553   6744   2856    955   1506       C  
ATOM    760  C   GLY A 142     -35.915  93.172 -21.522  1.00 74.19           C  
ANISOU  760  C   GLY A 142     9344   9781   9064   2749    960   1452       C  
ATOM    761  O   GLY A 142     -35.159  93.308 -20.560  1.00 61.72           O  
ANISOU  761  O   GLY A 142     7778   8085   7587   2585   1032   1408       O  
ATOM    762  N   LEU A 143     -37.238  93.179 -21.413  1.00 69.55           N  
ANISOU  762  N   LEU A 143     8666   9325   8434   2847    882   1452       N  
ATOM    763  CA  LEU A 143     -37.901  93.348 -20.128  1.00 62.79           C  
ANISOU  763  CA  LEU A 143     7726   8478   7653   2764    883   1406       C  
ATOM    764  C   LEU A 143     -37.870  92.054 -19.324  1.00 58.98           C  
ANISOU  764  C   LEU A 143     7114   8071   7225   2561    749   1302       C  
ATOM    765  O   LEU A 143     -38.179  90.987 -19.851  1.00 88.77           O  
ANISOU  765  O   LEU A 143    10804  11976  10950   2555    603   1265       O  
ATOM    766  CB  LEU A 143     -39.347  93.796 -20.339  1.00 76.91           C  
ANISOU  766  CB  LEU A 143     9459  10386   9376   2948    849   1441       C  
ATOM    767  CG  LEU A 143     -40.202  93.987 -19.087  1.00 84.13           C  
ANISOU  767  CG  LEU A 143    10280  11327  10359   2886    848   1398       C  
ATOM    768  CD1 LEU A 143     -39.615  95.065 -18.197  1.00 76.44           C  
ANISOU  768  CD1 LEU A 143     9404  10169   9473   2826   1026   1418       C  
ATOM    769  CD2 LEU A 143     -41.630  94.332 -19.463  1.00 82.99           C  
ANISOU  769  CD2 LEU A 143    10070  11321  10141   3081    800   1429       C  
ATOM    770  N   PRO A 144     -37.490  92.143 -18.039  1.00 67.39           N  
ANISOU  770  N   PRO A 144     8166   9050   8391   2398    801   1252       N  
ATOM    771  CA  PRO A 144     -37.460  90.972 -17.158  1.00 65.61           C  
ANISOU  771  CA  PRO A 144     7829   8883   8217   2212    691   1159       C  
ATOM    772  C   PRO A 144     -38.844  90.559 -16.667  1.00 58.44           C  
ANISOU  772  C   PRO A 144     6786   8115   7305   2228    595   1123       C  
ATOM    773  O   PRO A 144     -39.540  91.350 -16.029  1.00 58.20           O  
ANISOU  773  O   PRO A 144     6744   8069   7299   2276    659   1138       O  
ATOM    774  CB  PRO A 144     -36.623  91.457 -15.973  1.00 54.56           C  
ANISOU  774  CB  PRO A 144     6478   7339   6915   2070    802   1128       C  
ATOM    775  CG  PRO A 144     -36.888  92.909 -15.920  1.00 28.09           C  
ANISOU  775  CG  PRO A 144     3207   3894   3570   2190    949   1190       C  
ATOM    776  CD  PRO A 144     -36.950  93.337 -17.365  1.00 66.60           C  
ANISOU  776  CD  PRO A 144     8163   8783   8360   2378    975   1276       C  
ATOM    777  N   TYR A 145     -39.230  89.324 -16.969  1.00 71.99           N  
ANISOU  777  N   TYR A 145     8398   9962   8992   2185    449   1072       N  
ATOM    778  CA  TYR A 145     -40.445  88.740 -16.428  1.00 49.94           C  
ANISOU  778  CA  TYR A 145     5464   7298   6214   2163    357   1018       C  
ATOM    779  C   TYR A 145     -40.093  87.667 -15.411  1.00 63.79           C  
ANISOU  779  C   TYR A 145     7154   9045   8037   1954    306    938       C  
ATOM    780  O   TYR A 145     -38.922  87.374 -15.173  1.00 70.68           O  
ANISOU  780  O   TYR A 145     8089   9825   8940   1839    332    924       O  
ATOM    781  CB  TYR A 145     -41.290  88.104 -17.531  1.00 50.53           C  
ANISOU  781  CB  TYR A 145     5453   7538   6208   2274    228   1006       C  
ATOM    782  CG  TYR A 145     -41.903  89.074 -18.509  1.00 60.68           C  
ANISOU  782  CG  TYR A 145     6780   8868   7409   2506    257   1079       C  
ATOM    783  CD1 TYR A 145     -42.311  88.652 -19.762  1.00 81.60           C  
ANISOU  783  CD1 TYR A 145     9394  11647   9964   2634    155   1081       C  
ATOM    784  CD2 TYR A 145     -42.079  90.407 -18.180  1.00109.20           C  
ANISOU  784  CD2 TYR A 145    13000  14927  13564   2605    388   1146       C  
ATOM    785  CE1 TYR A 145     -42.874  89.527 -20.660  1.00 95.59           C  
ANISOU  785  CE1 TYR A 145    11208  13468  11646   2862    179   1150       C  
ATOM    786  CE2 TYR A 145     -42.643  91.292 -19.076  1.00117.42           C  
ANISOU  786  CE2 TYR A 145    14087  16006  14520   2830    421   1220       C  
ATOM    787  CZ  TYR A 145     -43.039  90.845 -20.317  1.00 88.46           C  
ANISOU  787  CZ  TYR A 145    10386  12474  10752   2963    314   1224       C  
ATOM    788  OH  TYR A 145     -43.603  91.717 -21.220  1.00 82.23           O  
ANISOU  788  OH  TYR A 145     9646  11731   9866   3205    344   1300       O  
ATOM    789  N   THR A 146     -41.122  87.078 -14.817  1.00 71.09           N  
ANISOU  789  N   THR A 146     7954  10069   8988   1913    238    884       N  
ATOM    790  CA  THR A 146     -40.954  85.925 -13.949  1.00 52.55           C  
ANISOU  790  CA  THR A 146     5539   7733   6695   1732    184    810       C  
ATOM    791  C   THR A 146     -42.107  84.954 -14.175  1.00 61.37           C  
ANISOU  791  C   THR A 146     6511   9004   7804   1733     68    752       C  
ATOM    792  O   THR A 146     -43.270  85.351 -14.194  1.00 46.51           O  
ANISOU  792  O   THR A 146     4554   7204   5914   1830     59    752       O  
ATOM    793  CB  THR A 146     -40.884  86.333 -12.467  1.00 33.54           C  
ANISOU  793  CB  THR A 146     3143   5239   4360   1636    269    795       C  
ATOM    794  CG2 THR A 146     -40.587  85.125 -11.599  1.00 46.70           C  
ANISOU  794  CG2 THR A 146     4761   6909   6074   1460    222    728       C  
ATOM    795  OG1 THR A 146     -39.847  87.304 -12.287  1.00 71.12           O  
ANISOU  795  OG1 THR A 146     8031   9860   9134   1638    381    837       O  
ATOM    796  N   VAL A 147     -41.774  83.683 -14.383  1.00 55.22           N  
ANISOU  796  N   VAL A 147     5690   8263   7028   1628    -16    699       N  
ATOM    797  CA  VAL A 147     -42.780  82.633 -14.498  1.00 37.94           C  
ANISOU  797  CA  VAL A 147     3359   6207   4848   1597   -118    626       C  
ATOM    798  C   VAL A 147     -42.865  81.910 -13.170  1.00 39.69           C  
ANISOU  798  C   VAL A 147     3533   6399   5150   1432   -100    573       C  
ATOM    799  O   VAL A 147     -41.846  81.477 -12.631  1.00 50.92           O  
ANISOU  799  O   VAL A 147     5021   7731   6597   1312    -75    569       O  
ATOM    800  CB  VAL A 147     -42.428  81.609 -15.595  1.00 43.98           C  
ANISOU  800  CB  VAL A 147     4105   7037   5568   1585   -219    594       C  
ATOM    801  CG1 VAL A 147     -43.465  80.494 -15.631  1.00 45.69           C  
ANISOU  801  CG1 VAL A 147     4168   7383   5809   1534   -314    503       C  
ATOM    802  CG2 VAL A 147     -42.327  82.285 -16.955  1.00 35.26           C  
ANISOU  802  CG2 VAL A 147     3056   5968   4373   1760   -236    648       C  
ATOM    803  N   VAL A 148     -44.075  81.792 -12.637  1.00 45.22           N  
ANISOU  803  N   VAL A 148     4121   7174   5888   1431   -110    533       N  
ATOM    804  CA  VAL A 148     -44.276  81.054 -11.397  1.00 63.91           C  
ANISOU  804  CA  VAL A 148     6439   9516   8328   1283    -88    483       C  
ATOM    805  C   VAL A 148     -45.096  79.810 -11.679  1.00 61.02           C  
ANISOU  805  C   VAL A 148     5937   9262   7985   1227   -174    401       C  
ATOM    806  O   VAL A 148     -46.212  79.898 -12.191  1.00 66.17           O  
ANISOU  806  O   VAL A 148     6480  10030   8631   1313   -220    369       O  
ATOM    807  CB  VAL A 148     -44.992  81.893 -10.329  1.00 54.00           C  
ANISOU  807  CB  VAL A 148     5166   8237   7115   1303     -6    498       C  
ATOM    808  CG1 VAL A 148     -44.903  81.198  -8.982  1.00 46.37           C  
ANISOU  808  CG1 VAL A 148     4189   7217   6214   1150     35    461       C  
ATOM    809  CG2 VAL A 148     -44.380  83.281 -10.251  1.00 48.21           C  
ANISOU  809  CG2 VAL A 148     4554   7407   6357   1387     80    575       C  
ATOM    810  N   ILE A 149     -44.536  78.651 -11.349  1.00 52.62           N  
ANISOU  810  N   ILE A 149     4880   8165   6951   1086   -191    361       N  
ATOM    811  CA  ILE A 149     -45.206  77.392 -11.631  1.00 50.94           C  
ANISOU  811  CA  ILE A 149     4546   8041   6767   1018   -261    276       C  
ATOM    812  C   ILE A 149     -45.386  76.545 -10.383  1.00 54.57           C  
ANISOU  812  C   ILE A 149     4974   8455   7303    869   -212    234       C  
ATOM    813  O   ILE A 149     -44.436  76.308  -9.634  1.00 53.76           O  
ANISOU  813  O   ILE A 149     4968   8249   7209    782   -163    260       O  
ATOM    814  CB  ILE A 149     -44.436  76.578 -12.673  1.00 44.16           C  
ANISOU  814  CB  ILE A 149     3716   7196   5866    996   -337    259       C  
ATOM    815  CG1 ILE A 149     -44.036  77.468 -13.847  1.00 60.83           C  
ANISOU  815  CG1 ILE A 149     5892   9328   7893   1145   -368    316       C  
ATOM    816  CG2 ILE A 149     -45.280  75.417 -13.152  1.00 42.43           C  
ANISOU  816  CG2 ILE A 149     3359   7086   5675    949   -413    162       C  
ATOM    817  CD1 ILE A 149     -43.193  76.765 -14.885  1.00 50.31           C  
ANISOU  817  CD1 ILE A 149     4603   8002   6513   1133   -435    308       C  
ATOM    818  N   HIS A 150     -46.620  76.102 -10.160  1.00 37.67           N  
ANISOU  818  N   HIS A 150     2699   6396   5217    847   -220    168       N  
ATOM    819  CA  HIS A 150     -46.920  75.166  -9.086  1.00 40.53           C  
ANISOU  819  CA  HIS A 150     3022   6723   5655    708   -169    121       C  
ATOM    820  C   HIS A 150     -47.146  73.794  -9.692  1.00 37.49           C  
ANISOU  820  C   HIS A 150     2553   6395   5297    627   -231     37       C  
ATOM    821  O   HIS A 150     -47.867  73.654 -10.676  1.00 57.95           O  
ANISOU  821  O   HIS A 150     5036   9102   7881    685   -308    -20       O  
ATOM    822  CB  HIS A 150     -48.165  75.605  -8.321  1.00 41.99           C  
ANISOU  822  CB  HIS A 150     3111   6945   5897    727   -115    100       C  
ATOM    823  CG  HIS A 150     -48.072  76.989  -7.759  1.00 60.63           C  
ANISOU  823  CG  HIS A 150     5545   9256   8234    813    -52    176       C  
ATOM    824  CD2 HIS A 150     -48.534  78.175  -8.227  1.00 58.52           C  
ANISOU  824  CD2 HIS A 150     5265   9039   7933    957    -60    212       C  
ATOM    825  ND1 HIS A 150     -47.447  77.268  -6.562  1.00 49.84           N  
ANISOU  825  ND1 HIS A 150     4282   7776   6879    756     36    221       N  
ATOM    826  CE1 HIS A 150     -47.523  78.564  -6.320  1.00 45.94           C  
ANISOU  826  CE1 HIS A 150     3832   7259   6364    852     80    276       C  
ATOM    827  NE2 HIS A 150     -48.177  79.137  -7.314  1.00 57.48           N  
ANISOU  827  NE2 HIS A 150     5228   8814   7799    975     28    276       N  
ATOM    828  N   TYR A 151     -46.526  72.781  -9.103  1.00 39.69           N  
ANISOU  828  N   TYR A 151     2882   6594   5605    499   -197     25       N  
ATOM    829  CA  TYR A 151     -46.606  71.428  -9.637  1.00 65.69           C  
ANISOU  829  CA  TYR A 151     6113   9919   8925    411   -242    -53       C  
ATOM    830  C   TYR A 151     -46.529  70.403  -8.516  1.00 67.73           C  
ANISOU  830  C   TYR A 151     6391  10095   9250    269   -159    -74       C  
ATOM    831  O   TYR A 151     -46.199  70.732  -7.372  1.00 27.48           O  
ANISOU  831  O   TYR A 151     1373   4909   4157    245    -76    -20       O  
ATOM    832  CB  TYR A 151     -45.462  71.182 -10.621  1.00 46.16           C  
ANISOU  832  CB  TYR A 151     3726   7431   6382    428   -311    -29       C  
ATOM    833  CG  TYR A 151     -44.106  71.319  -9.974  1.00 43.64           C  
ANISOU  833  CG  TYR A 151     3564   6986   6030    393   -261     49       C  
ATOM    834  CD1 TYR A 151     -43.498  72.559  -9.857  1.00 50.84           C  
ANISOU  834  CD1 TYR A 151     4570   7855   6893    478   -240    129       C  
ATOM    835  CD2 TYR A 151     -43.447  70.215  -9.457  1.00 37.72           C  
ANISOU  835  CD2 TYR A 151     2868   6161   5301    276   -230     38       C  
ATOM    836  CE1 TYR A 151     -42.267  72.694  -9.256  1.00 43.51           C  
ANISOU  836  CE1 TYR A 151     3772   6821   5939    443   -198    185       C  
ATOM    837  CE2 TYR A 151     -42.210  70.343  -8.853  1.00 44.31           C  
ANISOU  837  CE2 TYR A 151     3839   6895   6102    252   -191    102       C  
ATOM    838  CZ  TYR A 151     -41.625  71.582  -8.755  1.00 34.00           C  
ANISOU  838  CZ  TYR A 151     2613   5556   4751    333   -178    169       C  
ATOM    839  OH  TYR A 151     -40.395  71.719  -8.158  1.00 44.74           O  
ANISOU  839  OH  TYR A 151     4095   6823   6081    307   -143    217       O  
ATOM    840  N   ALA A 152     -46.824  69.154  -8.853  1.00 46.28           N  
ANISOU  840  N   ALA A 152     3602   7402   6579    180   -177   -155       N  
ATOM    841  CA  ALA A 152     -46.743  68.068  -7.887  1.00 43.69           C  
ANISOU  841  CA  ALA A 152     3300   6989   6313     48    -90   -175       C  
ATOM    842  C   ALA A 152     -46.316  66.786  -8.587  1.00 40.85           C  
ANISOU  842  C   ALA A 152     2937   6623   5960    -31   -129   -230       C  
ATOM    843  O   ALA A 152     -46.523  66.631  -9.788  1.00 50.56           O  
ANISOU  843  O   ALA A 152     4095   7943   7174      3   -222   -285       O  
ATOM    844  CB  ALA A 152     -48.081  67.887  -7.187  1.00 28.08           C  
ANISOU  844  CB  ALA A 152     1201   5041   4429      4    -19   -236       C  
ATOM    845  N   GLY A 153     -45.716  65.871  -7.834  1.00 47.71           N  
ANISOU  845  N   GLY A 153     3889   7389   6849   -130    -56   -215       N  
ATOM    846  CA  GLY A 153     -45.237  64.627  -8.408  1.00 58.57           C  
ANISOU  846  CA  GLY A 153     5279   8742   8232   -207    -79   -260       C  
ATOM    847  C   GLY A 153     -44.871  63.571  -7.382  1.00 54.84           C  
ANISOU  847  C   GLY A 153     4883   8155   7798   -316     29   -249       C  
ATOM    848  O   GLY A 153     -44.839  63.833  -6.181  1.00 69.12           O  
ANISOU  848  O   GLY A 153     6753   9897   9614   -324    119   -196       O  
ATOM    849  N   ASN A 154     -44.596  62.367  -7.872  1.00 51.61           N  
ANISOU  849  N   ASN A 154     4476   7724   7410   -393     23   -299       N  
ATOM    850  CA  ASN A 154     -44.248  61.238  -7.024  1.00 55.39           C  
ANISOU  850  CA  ASN A 154     5031   8090   7923   -491    129   -291       C  
ATOM    851  C   ASN A 154     -42.748  60.957  -7.119  1.00 43.62           C  
ANISOU  851  C   ASN A 154     3693   6532   6350   -480    104   -220       C  
ATOM    852  O   ASN A 154     -42.209  60.852  -8.218  1.00 46.67           O  
ANISOU  852  O   ASN A 154     4082   6957   6694   -457     10   -234       O  
ATOM    853  CB  ASN A 154     -45.072  59.998  -7.440  1.00 42.01           C  
ANISOU  853  CB  ASN A 154     3228   6409   6325   -596    161   -406       C  
ATOM    854  CG  ASN A 154     -46.566  60.112  -7.059  1.00 66.72           C  
ANISOU  854  CG  ASN A 154     6208   9586   9555   -628    219   -482       C  
ATOM    855  ND2 ASN A 154     -47.472  59.817  -8.003  1.00 65.50           N  
ANISOU  855  ND2 ASN A 154     5895   9531   9461   -652    163   -601       N  
ATOM    856  OD1 ASN A 154     -46.882  60.439  -5.918  1.00 52.71           O  
ANISOU  856  OD1 ASN A 154     4461   7761   7803   -630    315   -438       O  
ATOM    857  N   LEU A 155     -42.066  60.871  -5.979  1.00 37.20           N  
ANISOU  857  N   LEU A 155     3004   5623   5508   -487    185   -146       N  
ATOM    858  CA  LEU A 155     -40.635  60.561  -5.980  1.00 22.48           C  
ANISOU  858  CA  LEU A 155     1278   3697   3566   -475    166    -84       C  
ATOM    859  C   LEU A 155     -40.367  59.395  -6.915  1.00 47.21           C  
ANISOU  859  C   LEU A 155     4400   6823   6714   -535    134   -138       C  
ATOM    860  O   LEU A 155     -41.066  58.385  -6.877  1.00 41.91           O  
ANISOU  860  O   LEU A 155     3673   6131   6120   -619    197   -204       O  
ATOM    861  CB  LEU A 155     -40.127  60.207  -4.575  1.00 58.97           C  
ANISOU  861  CB  LEU A 155     6019   8217   8169   -493    275    -22       C  
ATOM    862  CG  LEU A 155     -39.723  61.337  -3.622  1.00 44.86           C  
ANISOU  862  CG  LEU A 155     4302   6417   6325   -420    290     51       C  
ATOM    863  CD1 LEU A 155     -40.924  62.188  -3.290  1.00 70.99           C  
ANISOU  863  CD1 LEU A 155     7514   9775   9683   -400    315     32       C  
ATOM    864  CD2 LEU A 155     -39.104  60.788  -2.344  1.00 44.00           C  
ANISOU  864  CD2 LEU A 155     4319   6216   6184   -432    387    104       C  
ATOM    865  N   SER A 156     -39.358  59.548  -7.761  1.00 55.18           N  
ANISOU  865  N   SER A 156     5463   7849   7654   -492     43   -113       N  
ATOM    866  CA  SER A 156     -38.973  58.500  -8.690  1.00 37.83           C  
ANISOU  866  CA  SER A 156     3268   5646   5459   -539      6   -158       C  
ATOM    867  C   SER A 156     -38.672  57.193  -7.951  1.00 56.54           C  
ANISOU  867  C   SER A 156     5715   7910   7857   -620    113   -154       C  
ATOM    868  O   SER A 156     -38.063  57.197  -6.879  1.00 50.57           O  
ANISOU  868  O   SER A 156     5067   7081   7066   -606    181    -82       O  
ATOM    869  CB  SER A 156     -37.745  58.946  -9.483  1.00 34.62           C  
ANISOU  869  CB  SER A 156     2937   5255   4964   -472    -90   -110       C  
ATOM    870  OG  SER A 156     -37.399  58.009 -10.486  1.00 52.43           O  
ANISOU  870  OG  SER A 156     5190   7514   7217   -509   -134   -156       O  
ATOM    871  N   GLU A 157     -39.112  56.075  -8.520  1.00 49.71           N  
ANISOU  871  N   GLU A 157     4796   7038   7054   -701    132   -234       N  
ATOM    872  CA  GLU A 157     -38.751  54.767  -7.987  1.00 65.53           C  
ANISOU  872  CA  GLU A 157     6883   8934   9083   -774    236   -230       C  
ATOM    873  C   GLU A 157     -37.788  54.104  -8.964  1.00 61.08           C  
ANISOU  873  C   GLU A 157     6371   8360   8474   -779    170   -237       C  
ATOM    874  O   GLU A 157     -37.626  52.885  -8.978  1.00 42.40           O  
ANISOU  874  O   GLU A 157     4045   5924   6142   -848    235   -263       O  
ATOM    875  CB  GLU A 157     -39.993  53.896  -7.761  1.00 45.20           C  
ANISOU  875  CB  GLU A 157     4214   6334   6626   -876    338   -320       C  
ATOM    876  CG  GLU A 157     -40.980  54.444  -6.725  1.00 62.12           C  
ANISOU  876  CG  GLU A 157     6306   8477   8820   -878    421   -314       C  
ATOM    877  CD  GLU A 157     -40.366  54.601  -5.344  1.00108.96           C  
ANISOU  877  CD  GLU A 157    12379  14322  14701   -840    512   -207       C  
ATOM    878  OE1 GLU A 157     -39.568  53.728  -4.943  1.00114.99           O  
ANISOU  878  OE1 GLU A 157    13264  14993  15435   -857    577   -164       O  
ATOM    879  OE2 GLU A 157     -40.686  55.597  -4.658  1.00126.36           O1-
ANISOU  879  OE2 GLU A 157    14571  16551  16889   -788    520   -167       O1-
ATOM    880  N   THR A 158     -37.140  54.930  -9.777  1.00 68.78           N  
ANISOU  880  N   THR A 158     7353   9402   9377   -703     48   -210       N  
ATOM    881  CA  THR A 158     -36.306  54.431 -10.861  1.00 49.00           C  
ANISOU  881  CA  THR A 158     4884   6905   6830   -700    -27   -223       C  
ATOM    882  C   THR A 158     -34.861  54.924 -10.783  1.00 46.77           C  
ANISOU  882  C   THR A 158     4725   6598   6449   -625    -71   -129       C  
ATOM    883  O   THR A 158     -34.108  54.803 -11.747  1.00 59.18           O  
ANISOU  883  O   THR A 158     6323   8187   7974   -602   -146   -130       O  
ATOM    884  CB  THR A 158     -36.900  54.816 -12.232  1.00 63.33           C  
ANISOU  884  CB  THR A 158     6576   8833   8652   -680   -140   -301       C  
ATOM    885  CG2 THR A 158     -36.622  56.279 -12.554  1.00 42.02           C  
ANISOU  885  CG2 THR A 158     3876   6207   5884   -571   -230   -247       C  
ATOM    886  OG1 THR A 158     -36.331  53.984 -13.251  1.00121.97           O  
ANISOU  886  OG1 THR A 158    14024  16257  16060   -704   -187   -339       O  
ATOM    887  N   PHE A 159     -34.482  55.487  -9.640  1.00 48.71           N  
ANISOU  887  N   PHE A 159     5042   6804   6662   -586    -22    -54       N  
ATOM    888  CA  PHE A 159     -33.095  55.896  -9.405  1.00 39.32           C  
ANISOU  888  CA  PHE A 159     3966   5588   5386   -522    -52     25       C  
ATOM    889  C   PHE A 159     -32.583  56.946 -10.392  1.00 39.62           C  
ANISOU  889  C   PHE A 159     3987   5694   5372   -451   -164     38       C  
ATOM    890  O   PHE A 159     -31.403  56.967 -10.754  1.00 52.30           O  
ANISOU  890  O   PHE A 159     5667   7285   6919   -417   -206     74       O  
ATOM    891  CB  PHE A 159     -32.189  54.669  -9.382  1.00 49.75           C  
ANISOU  891  CB  PHE A 159     5383   6834   6685   -553    -16     39       C  
ATOM    892  CG  PHE A 159     -32.570  53.678  -8.332  1.00 52.22           C  
ANISOU  892  CG  PHE A 159     5738   7066   7039   -608    110     41       C  
ATOM    893  CD1 PHE A 159     -32.025  53.754  -7.065  1.00 53.70           C  
ANISOU  893  CD1 PHE A 159     6023   7200   7182   -570    177    111       C  
ATOM    894  CD2 PHE A 159     -33.498  52.690  -8.601  1.00 54.99           C  
ANISOU  894  CD2 PHE A 159     6029   7394   7472   -694    169    -30       C  
ATOM    895  CE1 PHE A 159     -32.381  52.852  -6.090  1.00 72.20           C  
ANISOU  895  CE1 PHE A 159     8416   9463   9554   -609    304    121       C  
ATOM    896  CE2 PHE A 159     -33.861  51.782  -7.629  1.00 66.68           C  
ANISOU  896  CE2 PHE A 159     7554   8787   8995   -745    303    -24       C  
ATOM    897  CZ  PHE A 159     -33.302  51.864  -6.372  1.00 77.26           C  
ANISOU  897  CZ  PHE A 159     9003  10070  10283   -697    373     57       C  
ATOM    898  N   HIS A 160     -33.488  57.821 -10.806  1.00 54.49           N  
ANISOU  898  N   HIS A 160     5773   7653   7279   -424   -206     10       N  
ATOM    899  CA  HIS A 160     -33.150  58.935 -11.673  1.00 50.37           C  
ANISOU  899  CA  HIS A 160     5237   7193   6710   -345   -296     28       C  
ATOM    900  C   HIS A 160     -34.142  60.039 -11.370  1.00 60.86           C  
ANISOU  900  C   HIS A 160     6489   8574   8062   -306   -294     26       C  
ATOM    901  O   HIS A 160     -35.284  59.757 -11.016  1.00 58.54           O  
ANISOU  901  O   HIS A 160     6115   8296   7830   -349   -253    -20       O  
ATOM    902  CB  HIS A 160     -33.254  58.517 -13.138  1.00 36.17           C  
ANISOU  902  CB  HIS A 160     3388   5448   4906   -347   -374    -26       C  
ATOM    903  CG  HIS A 160     -32.295  59.229 -14.035  1.00 61.03           C  
ANISOU  903  CG  HIS A 160     6584   8620   7986   -272   -450     13       C  
ATOM    904  CD2 HIS A 160     -32.495  60.170 -14.985  1.00 63.35           C  
ANISOU  904  CD2 HIS A 160     6853   8974   8241   -194   -511     13       C  
ATOM    905  ND1 HIS A 160     -30.939  58.984 -14.013  1.00 83.66           N  
ANISOU  905  ND1 HIS A 160     9554  11429  10804   -264   -450     59       N  
ATOM    906  CE1 HIS A 160     -30.344  59.748 -14.910  1.00 92.53           C  
ANISOU  906  CE1 HIS A 160    10716  12571  11870   -193   -500     84       C  
ATOM    907  NE2 HIS A 160     -31.265  60.478 -15.514  1.00 83.86           N  
ANISOU  907  NE2 HIS A 160     9553  11539  10773   -147   -531     61       N  
ATOM    908  N   GLY A 161     -33.710  61.289 -11.498  1.00 48.84           N  
ANISOU  908  N   GLY A 161     4990   7074   6494   -226   -330     73       N  
ATOM    909  CA  GLY A 161     -34.561  62.418 -11.166  1.00 23.73           C  
ANISOU  909  CA  GLY A 161     1750   3936   3331   -179   -322     80       C  
ATOM    910  C   GLY A 161     -34.545  62.674  -9.674  1.00 37.15           C  
ANISOU  910  C   GLY A 161     3493   5580   5043   -193   -239    117       C  
ATOM    911  O   GLY A 161     -33.489  62.617  -9.044  1.00 48.11           O  
ANISOU  911  O   GLY A 161     4977   6909   6393   -192   -214    160       O  
ATOM    912  N   PHE A 162     -35.716  62.958  -9.110  1.00 36.17           N  
ANISOU  912  N   PHE A 162     3296   5481   4968   -202   -198     96       N  
ATOM    913  CA  PHE A 162     -35.870  63.103  -7.664  1.00 26.21           C  
ANISOU  913  CA  PHE A 162     2069   4168   3720   -218   -111    124       C  
ATOM    914  C   PHE A 162     -36.375  61.773  -7.118  1.00 45.13           C  
ANISOU  914  C   PHE A 162     4455   6524   6168   -305    -38     90       C  
ATOM    915  O   PHE A 162     -37.579  61.527  -7.072  1.00 44.71           O  
ANISOU  915  O   PHE A 162     4308   6499   6182   -341     -7     40       O  
ATOM    916  CB  PHE A 162     -36.847  64.238  -7.351  1.00 42.19           C  
ANISOU  916  CB  PHE A 162     4023   6237   5769   -172    -98    125       C  
ATOM    917  CG  PHE A 162     -37.091  64.453  -5.884  1.00 44.25           C  
ANISOU  917  CG  PHE A 162     4317   6451   6043   -183     -8    151       C  
ATOM    918  CD1 PHE A 162     -36.186  65.147  -5.106  1.00 43.12           C  
ANISOU  918  CD1 PHE A 162     4266   6267   5850   -144     11    203       C  
ATOM    919  CD2 PHE A 162     -38.243  63.976  -5.289  1.00 79.64           C  
ANISOU  919  CD2 PHE A 162     8734  10935  10592   -232     61    117       C  
ATOM    920  CE1 PHE A 162     -36.417  65.357  -3.763  1.00 22.33           C  
ANISOU  920  CE1 PHE A 162     1665   3599   3222   -147     91    224       C  
ATOM    921  CE2 PHE A 162     -38.479  64.180  -3.948  1.00 79.08           C  
ANISOU  921  CE2 PHE A 162     8697  10820  10528   -236    148    144       C  
ATOM    922  CZ  PHE A 162     -37.560  64.873  -3.186  1.00 64.54           C  
ANISOU  922  CZ  PHE A 162     6953   8942   8626   -190    160    199       C  
ATOM    923  N   TYR A 163     -35.449  60.911  -6.712  1.00 48.02           N  
ANISOU  923  N   TYR A 163     4918   6823   6507   -335     -6    114       N  
ATOM    924  CA  TYR A 163     -35.790  59.515  -6.475  1.00 35.08           C  
ANISOU  924  CA  TYR A 163     3280   5136   4913   -416     61     81       C  
ATOM    925  C   TYR A 163     -35.695  59.037  -5.025  1.00 46.09           C  
ANISOU  925  C   TYR A 163     4755   6453   6306   -436    173    118       C  
ATOM    926  O   TYR A 163     -34.862  59.505  -4.247  1.00 40.21           O  
ANISOU  926  O   TYR A 163     4098   5680   5499   -386    184    174       O  
ATOM    927  CB  TYR A 163     -34.957  58.607  -7.387  1.00 33.16           C  
ANISOU  927  CB  TYR A 163     3078   4877   4646   -439     15     68       C  
ATOM    928  CG  TYR A 163     -33.471  58.649  -7.121  1.00 29.21           C  
ANISOU  928  CG  TYR A 163     2700   4334   4066   -398     -2    129       C  
ATOM    929  CD1 TYR A 163     -32.865  57.690  -6.327  1.00 39.43           C  
ANISOU  929  CD1 TYR A 163     4089   5552   5341   -422     68    157       C  
ATOM    930  CD2 TYR A 163     -32.672  59.640  -7.670  1.00 42.62           C  
ANISOU  930  CD2 TYR A 163     4418   6067   5710   -332    -83    157       C  
ATOM    931  CE1 TYR A 163     -31.505  57.713  -6.082  1.00 53.44           C  
ANISOU  931  CE1 TYR A 163     5966   7299   7041   -378     48    205       C  
ATOM    932  CE2 TYR A 163     -31.310  59.675  -7.431  1.00 44.58           C  
ANISOU  932  CE2 TYR A 163     4765   6280   5893   -299    -97    202       C  
ATOM    933  CZ  TYR A 163     -30.732  58.706  -6.635  1.00 64.81           C  
ANISOU  933  CZ  TYR A 163     7411   8779   8434   -321    -37    223       C  
ATOM    934  OH  TYR A 163     -29.377  58.727  -6.384  1.00 59.25           O  
ANISOU  934  OH  TYR A 163     6798   8051   7664   -281    -56    259       O  
ATOM    935  N   LYS A 164     -36.567  58.089  -4.688  1.00 56.75           N  
ANISOU  935  N   LYS A 164     6069   7767   7725   -507    260     80       N  
ATOM    936  CA  LYS A 164     -36.547  57.422  -3.394  1.00 51.13           C  
ANISOU  936  CA  LYS A 164     5441   6972   7015   -528    384    114       C  
ATOM    937  C   LYS A 164     -35.463  56.348  -3.343  1.00 54.59           C  
ANISOU  937  C   LYS A 164     5994   7342   7407   -538    406    143       C  
ATOM    938  O   LYS A 164     -35.241  55.628  -4.316  1.00 38.69           O  
ANISOU  938  O   LYS A 164     3964   5328   5408   -576    367    107       O  
ATOM    939  CB  LYS A 164     -37.899  56.766  -3.119  1.00 54.56           C  
ANISOU  939  CB  LYS A 164     5795   7385   7551   -606    483     59       C  
ATOM    940  CG  LYS A 164     -37.983  56.078  -1.767  1.00 52.44           C  
ANISOU  940  CG  LYS A 164     5616   7023   7287   -623    629     98       C  
ATOM    941  CD  LYS A 164     -38.914  54.871  -1.802  1.00 83.73           C  
ANISOU  941  CD  LYS A 164     9531  10931  11353   -723    739     37       C  
ATOM    942  CE  LYS A 164     -38.174  53.610  -2.234  1.00102.32           C  
ANISOU  942  CE  LYS A 164    11961  13221  13696   -761    759     34       C  
ATOM    943  NZ  LYS A 164     -38.968  52.375  -1.976  1.00106.65           N1+
ANISOU  943  NZ  LYS A 164    12495  13686  14341   -856    903    -13       N1+
ATOM    944  N   SER A 165     -34.801  56.247  -2.194  1.00 55.44           N  
ANISOU  944  N   SER A 165     6216   7395   7453   -496    468    205       N  
ATOM    945  CA  SER A 165     -33.801  55.216  -1.959  1.00 38.40           C  
ANISOU  945  CA  SER A 165     4176   5171   5244   -490    503    240       C  
ATOM    946  C   SER A 165     -33.890  54.785  -0.496  1.00 38.10           C  
ANISOU  946  C   SER A 165     4231   5062   5183   -470    633    287       C  
ATOM    947  O   SER A 165     -34.275  55.581   0.361  1.00 77.80           O  
ANISOU  947  O   SER A 165     9254  10105  10200   -435    661    308       O  
ATOM    948  CB  SER A 165     -32.405  55.745  -2.287  1.00 44.57           C  
ANISOU  948  CB  SER A 165     5017   5983   5933   -421    399    274       C  
ATOM    949  OG  SER A 165     -31.449  54.703  -2.269  1.00 64.11           O  
ANISOU  949  OG  SER A 165     7591   8405   8363   -415    419    299       O  
ATOM    950  N   THR A 166     -33.546  53.535  -0.207  1.00 32.96           N  
ANISOU  950  N   THR A 166     3669   4331   4522   -488    718    307       N  
ATOM    951  CA  THR A 166     -33.715  53.003   1.145  1.00 45.87           C  
ANISOU  951  CA  THR A 166     5402   5891   6136   -464    859    355       C  
ATOM    952  C   THR A 166     -32.451  52.379   1.731  1.00 36.90           C  
ANISOU  952  C   THR A 166     4416   4710   4893   -390    881    419       C  
ATOM    953  O   THR A 166     -31.474  52.133   1.022  1.00 59.37           O  
ANISOU  953  O   THR A 166     7290   7570   7697   -374    799    420       O  
ATOM    954  CB  THR A 166     -34.845  51.955   1.193  1.00 46.82           C  
ANISOU  954  CB  THR A 166     5491   5936   6363   -558    997    318       C  
ATOM    955  CG2 THR A 166     -36.177  52.593   0.853  1.00 48.41           C  
ANISOU  955  CG2 THR A 166     5541   6187   6666   -620    990    253       C  
ATOM    956  OG1 THR A 166     -34.578  50.916   0.244  1.00 60.99           O  
ANISOU  956  OG1 THR A 166     7286   7695   8190   -616    991    284       O  
ATOM    957  N   TYR A 167     -32.478  52.131   3.036  1.00 40.95           N  
ANISOU  957  N   TYR A 167     5027   5172   5359   -338    992    471       N  
ATOM    958  CA  TYR A 167     -31.422  51.366   3.696  1.00 60.57           C  
ANISOU  958  CA  TYR A 167     7662   7608   7742   -259   1037    533       C  
ATOM    959  C   TYR A 167     -31.922  50.813   5.023  1.00 59.03           C  
ANISOU  959  C   TYR A 167     7564   7334   7530   -226   1205    582       C  
ATOM    960  O   TYR A 167     -32.942  51.263   5.540  1.00 74.53           O  
ANISOU  960  O   TYR A 167     9478   9295   9546   -252   1269    571       O  
ATOM    961  CB  TYR A 167     -30.164  52.217   3.911  1.00 32.01           C  
ANISOU  961  CB  TYR A 167     4086   4068   4009   -157    914    557       C  
ATOM    962  CG  TYR A 167     -30.235  53.214   5.053  1.00 46.41           C  
ANISOU  962  CG  TYR A 167     5929   5932   5774    -83    919    579       C  
ATOM    963  CD1 TYR A 167     -30.841  54.451   4.887  1.00 49.12           C  
ANISOU  963  CD1 TYR A 167     6164   6337   6161   -107    857    544       C  
ATOM    964  CD2 TYR A 167     -29.666  52.927   6.288  1.00 52.76           C  
ANISOU  964  CD2 TYR A 167     6862   6715   6471     20    982    634       C  
ATOM    965  CE1 TYR A 167     -30.893  55.367   5.922  1.00 48.83           C  
ANISOU  965  CE1 TYR A 167     6147   6335   6073    -41    864    560       C  
ATOM    966  CE2 TYR A 167     -29.716  53.837   7.328  1.00 61.72           C  
ANISOU  966  CE2 TYR A 167     8013   7891   7547     90    983    647       C  
ATOM    967  CZ  TYR A 167     -30.329  55.054   7.138  1.00 54.71           C  
ANISOU  967  CZ  TYR A 167     7015   7059   6712     54    925    608       C  
ATOM    968  OH  TYR A 167     -30.378  55.967   8.167  1.00 57.35           O  
ANISOU  968  OH  TYR A 167     7369   7433   6991    122    928    616       O  
ATOM    969  N   ARG A 168     -31.208  49.833   5.568  1.00 54.15           N  
ANISOU  969  N   ARG A 168     7086   6651   6836   -163   1282    637       N  
ATOM    970  CA  ARG A 168     -31.565  49.282   6.874  1.00 72.55           C  
ANISOU  970  CA  ARG A 168     9531   8903   9130   -110   1450    696       C  
ATOM    971  C   ARG A 168     -30.451  49.417   7.910  1.00 59.12           C  
ANISOU  971  C   ARG A 168     7966   7229   7268     43   1433    762       C  
ATOM    972  O   ARG A 168     -29.296  49.084   7.646  1.00 73.28           O  
ANISOU  972  O   ARG A 168     9820   9042   8981    104   1363    780       O  
ATOM    973  CB  ARG A 168     -32.030  47.823   6.754  1.00 62.68           C  
ANISOU  973  CB  ARG A 168     8338   7526   7950   -174   1612    704       C  
ATOM    974  CG  ARG A 168     -33.469  47.685   6.282  1.00 62.86           C  
ANISOU  974  CG  ARG A 168     8239   7509   8135   -315   1690    638       C  
ATOM    975  CD  ARG A 168     -33.835  46.245   5.985  1.00 71.83           C  
ANISOU  975  CD  ARG A 168     9418   8520   9353   -392   1840    628       C  
ATOM    976  NE  ARG A 168     -35.067  46.154   5.205  1.00102.46           N  
ANISOU  976  NE  ARG A 168    13146  12387  13396   -540   1870    535       N  
ATOM    977  CZ  ARG A 168     -36.267  45.892   5.716  1.00 97.59           C  
ANISOU  977  CZ  ARG A 168    12499  11702  12879   -607   2027    514       C  
ATOM    978  NH1 ARG A 168     -36.408  45.683   7.018  1.00 53.04           N1+
ANISOU  978  NH1 ARG A 168     6978   5988   7187   -537   2178    588       N1+
ATOM    979  NH2 ARG A 168     -37.327  45.834   4.921  1.00 92.12           N  
ANISOU  979  NH2 ARG A 168    11651  11014  12335   -740   2035    415       N  
ATOM    980  N   THR A 169     -30.817  49.918   9.088  1.00 50.66           N  
ANISOU  980  N   THR A 169     6936   6164   6148    108   1496    793       N  
ATOM    981  CA  THR A 169     -29.886  50.069  10.200  1.00 67.51           C  
ANISOU  981  CA  THR A 169     9197   8331   8124    262   1489    848       C  
ATOM    982  C   THR A 169     -29.458  48.703  10.713  1.00 70.35           C  
ANISOU  982  C   THR A 169     9717   8597   8415    333   1621    917       C  
ATOM    983  O   THR A 169     -30.079  47.695  10.388  1.00 74.27           O  
ANISOU  983  O   THR A 169    10231   8988   8999    255   1748    924       O  
ATOM    984  CB  THR A 169     -30.534  50.841  11.364  1.00 63.40           C  
ANISOU  984  CB  THR A 169     8686   7828   7573    310   1547    864       C  
ATOM    985  CG2 THR A 169     -31.150  52.138  10.867  1.00 52.42           C  
ANISOU  985  CG2 THR A 169     7138   6513   6266    233   1444    799       C  
ATOM    986  OG1 THR A 169     -31.554  50.035  11.966  1.00 59.34           O  
ANISOU  986  OG1 THR A 169     8231   7202   7112    282   1746    901       O  
ATOM    987  N   LYS A 170     -28.398  48.667  11.515  1.00 81.59           N  
ANISOU  987  N   LYS A 170    11258  10061   9682    485   1593    964       N  
ATOM    988  CA  LYS A 170     -27.961  47.414  12.117  1.00 74.26           C  
ANISOU  988  CA  LYS A 170    10498   9048   8668    581   1723   1039       C  
ATOM    989  C   LYS A 170     -29.083  46.809  12.956  1.00 77.13           C  
ANISOU  989  C   LYS A 170    10939   9296   9072    570   1942   1087       C  
ATOM    990  O   LYS A 170     -29.197  45.589  13.072  1.00 90.48           O  
ANISOU  990  O   LYS A 170    12737  10869  10771    577   2096   1137       O  
ATOM    991  CB  LYS A 170     -26.699  47.614  12.962  1.00 60.07           C  
ANISOU  991  CB  LYS A 170     8806   7334   6683    765   1651   1075       C  
ATOM    992  CG  LYS A 170     -26.723  48.841  13.863  1.00 94.37           C  
ANISOU  992  CG  LYS A 170    13126  11777  10955    837   1586   1057       C  
ATOM    993  CD  LYS A 170     -25.463  48.911  14.719  1.00107.68           C  
ANISOU  993  CD  LYS A 170    14916  13546  12450   1025   1520   1082       C  
ATOM    994  CE  LYS A 170     -25.226  50.310  15.278  1.00102.28           C  
ANISOU  994  CE  LYS A 170    14168  12988  11706   1075   1397   1030       C  
ATOM    995  NZ  LYS A 170     -26.233  50.719  16.298  1.00 71.19           N1+
ANISOU  995  NZ  LYS A 170    10257   9026   7767   1092   1506   1052       N1+
ATOM    996  N   GLU A 171     -29.914  47.673  13.531  1.00 62.17           N  
ANISOU  996  N   GLU A 171     8988   7426   7206    552   1962   1071       N  
ATOM    997  CA  GLU A 171     -31.098  47.228  14.258  1.00 86.11           C  
ANISOU  997  CA  GLU A 171    12069  10350  10298    522   2169   1106       C  
ATOM    998  C   GLU A 171     -32.101  46.592  13.297  1.00 89.74           C  
ANISOU  998  C   GLU A 171    12436  10714  10945    344   2256   1062       C  
ATOM    999  O   GLU A 171     -33.087  45.983  13.718  1.00 74.41           O  
ANISOU  999  O   GLU A 171    10530   8660   9081    296   2449   1081       O  
ATOM   1000  CB  GLU A 171     -31.745  48.389  15.019  1.00 74.32           C  
ANISOU 1000  CB  GLU A 171    10522   8917   8797    539   2156   1091       C  
ATOM   1001  CG  GLU A 171     -30.873  48.984  16.116  1.00 89.57           C  
ANISOU 1001  CG  GLU A 171    12551  10937  10544    717   2092   1127       C  
ATOM   1002  CD  GLU A 171     -29.770  49.871  15.572  1.00123.40           C  
ANISOU 1002  CD  GLU A 171    16759  15360  14767    748   1861   1073       C  
ATOM   1003  OE1 GLU A 171     -30.065  50.749  14.733  1.00131.17           O  
ANISOU 1003  OE1 GLU A 171    17586  16401  15851    638   1744   1003       O  
ATOM   1004  OE2 GLU A 171     -28.607  49.696  15.991  1.00127.55           O1-
ANISOU 1004  OE2 GLU A 171    17381  15938  15145    885   1802   1100       O1-
ATOM   1005  N   GLY A 172     -31.844  46.747  12.001  1.00 92.83           N  
ANISOU 1005  N   GLY A 172    12707  11153  11411    248   2115    996       N  
ATOM   1006  CA  GLY A 172     -32.647  46.111  10.973  1.00 85.56           C  
ANISOU 1006  CA  GLY A 172    11693  10159  10656     86   2172    940       C  
ATOM   1007  C   GLY A 172     -33.844  46.914  10.499  1.00 90.28           C  
ANISOU 1007  C   GLY A 172    12113  10792  11396    -44   2142    862       C  
ATOM   1008  O   GLY A 172     -34.653  46.414   9.719  1.00 74.43           O  
ANISOU 1008  O   GLY A 172    10017   8731   9534   -180   2198    804       O  
ATOM   1009  N   GLU A 173     -33.966  48.155  10.960  1.00 92.23           N  
ANISOU 1009  N   GLU A 173    12306  11134  11603     -1   2055    854       N  
ATOM   1010  CA  GLU A 173     -35.093  48.991  10.551  1.00 90.21           C  
ANISOU 1010  CA  GLU A 173    11883  10919  11472   -109   2023    785       C  
ATOM   1011  C   GLU A 173     -34.835  49.691   9.213  1.00 90.39           C  
ANISOU 1011  C   GLU A 173    11758  11042  11543   -175   1824    712       C  
ATOM   1012  O   GLU A 173     -33.700  50.041   8.883  1.00 62.09           O  
ANISOU 1012  O   GLU A 173     8195   7528   7867   -111   1680    720       O  
ATOM   1013  CB  GLU A 173     -35.479  49.999  11.645  1.00106.10           C  
ANISOU 1013  CB  GLU A 173    13903  12977  13434    -39   2039    808       C  
ATOM   1014  CG  GLU A 173     -34.570  51.211  11.771  1.00106.37           C  
ANISOU 1014  CG  GLU A 173    13924  13137  13354     54   1856    807       C  
ATOM   1015  CD  GLU A 173     -35.094  52.214  12.782  1.00139.98           C  
ANISOU 1015  CD  GLU A 173    18175  17433  17579    106   1879    818       C  
ATOM   1016  OE1 GLU A 173     -35.400  53.360  12.385  1.00145.81           O  
ANISOU 1016  OE1 GLU A 173    18788  18254  18360     69   1767    767       O  
ATOM   1017  OE2 GLU A 173     -35.214  51.854  13.973  1.00147.62           O1-
ANISOU 1017  OE2 GLU A 173    19267  18345  18477    187   2015    878       O1-
ATOM   1018  N   LEU A 174     -35.906  49.886   8.450  1.00 99.44           N  
ANISOU 1018  N   LEU A 174    12753  12197  12832   -300   1821    638       N  
ATOM   1019  CA  LEU A 174     -35.823  50.406   7.091  1.00 65.39           C  
ANISOU 1019  CA  LEU A 174     8300   7968   8576   -368   1654    567       C  
ATOM   1020  C   LEU A 174     -36.047  51.915   7.023  1.00 62.31           C  
ANISOU 1020  C   LEU A 174     7805   7690   8180   -349   1526    540       C  
ATOM   1021  O   LEU A 174     -37.080  52.421   7.459  1.00 60.44           O  
ANISOU 1021  O   LEU A 174     7503   7458   8004   -376   1584    523       O  
ATOM   1022  CB  LEU A 174     -36.845  49.687   6.214  1.00 55.38           C  
ANISOU 1022  CB  LEU A 174     6924   6653   7464   -509   1718    491       C  
ATOM   1023  CG  LEU A 174     -37.219  50.309   4.871  1.00 72.08           C  
ANISOU 1023  CG  LEU A 174     8866   8861   9661   -588   1569    404       C  
ATOM   1024  CD1 LEU A 174     -36.737  49.431   3.732  1.00 43.24           C  
ANISOU 1024  CD1 LEU A 174     5205   5189   6036   -644   1524    366       C  
ATOM   1025  CD2 LEU A 174     -38.723  50.509   4.800  1.00 52.02           C  
ANISOU 1025  CD2 LEU A 174     6188   6322   7257   -682   1638    335       C  
ATOM   1026  N   ARG A 175     -35.073  52.630   6.465  1.00 71.01           N  
ANISOU 1026  N   ARG A 175     8891   8877   9212   -302   1358    537       N  
ATOM   1027  CA  ARG A 175     -35.135  54.085   6.385  1.00 55.32           C  
ANISOU 1027  CA  ARG A 175     6819   6988   7211   -275   1240    516       C  
ATOM   1028  C   ARG A 175     -35.240  54.543   4.934  1.00 61.87           C  
ANISOU 1028  C   ARG A 175     7514   7885   8108   -340   1105    452       C  
ATOM   1029  O   ARG A 175     -34.763  53.866   4.025  1.00 64.76           O  
ANISOU 1029  O   ARG A 175     7879   8241   8485   -374   1061    434       O  
ATOM   1030  CB  ARG A 175     -33.896  54.706   7.032  1.00 40.19           C  
ANISOU 1030  CB  ARG A 175     4997   5118   5154   -156   1163    560       C  
ATOM   1031  CG  ARG A 175     -33.473  54.058   8.339  1.00 41.07           C  
ANISOU 1031  CG  ARG A 175     5265   5171   5168    -68   1276    627       C  
ATOM   1032  CD  ARG A 175     -33.962  54.837   9.549  1.00 52.59           C  
ANISOU 1032  CD  ARG A 175     6746   6645   6592    -11   1333    648       C  
ATOM   1033  NE  ARG A 175     -32.871  55.541  10.217  1.00 74.30           N  
ANISOU 1033  NE  ARG A 175     9566   9459   9208    105   1250    670       N  
ATOM   1034  CZ  ARG A 175     -32.890  55.916  11.493  1.00 98.01           C  
ANISOU 1034  CZ  ARG A 175    12644  12467  12129    192   1307    701       C  
ATOM   1035  NH1 ARG A 175     -33.947  55.650  12.252  1.00 75.74           N1+
ANISOU 1035  NH1 ARG A 175     9845   9585   9347    178   1454    725       N1+
ATOM   1036  NH2 ARG A 175     -31.849  56.552  12.013  1.00113.17           N  
ANISOU 1036  NH2 ARG A 175    14615  14454  13930    293   1219    704       N  
ATOM   1037  N   ILE A 176     -35.857  55.703   4.731  1.00 69.38           N  
ANISOU 1037  N   ILE A 176     8358   8906   9097   -348   1042    421       N  
ATOM   1038  CA  ILE A 176     -36.017  56.282   3.401  1.00 55.11           C  
ANISOU 1038  CA  ILE A 176     6426   7171   7343   -390    916    365       C  
ATOM   1039  C   ILE A 176     -35.219  57.576   3.248  1.00 61.54           C  
ANISOU 1039  C   ILE A 176     7236   8062   8085   -318    786    377       C  
ATOM   1040  O   ILE A 176     -35.166  58.396   4.172  1.00 50.33           O  
ANISOU 1040  O   ILE A 176     5847   6657   6618   -259    799    403       O  
ATOM   1041  CB  ILE A 176     -37.500  56.605   3.111  1.00 48.24           C  
ANISOU 1041  CB  ILE A 176     5417   6324   6588   -458    948    310       C  
ATOM   1042  CG1 ILE A 176     -38.334  55.325   3.045  1.00 49.38           C  
ANISOU 1042  CG1 ILE A 176     5539   6396   6827   -549   1072    275       C  
ATOM   1043  CG2 ILE A 176     -37.641  57.391   1.820  1.00 55.58           C  
ANISOU 1043  CG2 ILE A 176     6224   7342   7550   -472    809    259       C  
ATOM   1044  CD1 ILE A 176     -39.826  55.582   3.007  1.00 85.94           C  
ANISOU 1044  CD1 ILE A 176    10036  11045  11573   -612   1127    217       C  
ATOM   1045  N   LEU A 177     -34.597  57.754   2.084  1.00 44.10           N  
ANISOU 1045  N   LEU A 177     4990   5896   5870   -324    668    355       N  
ATOM   1046  CA  LEU A 177     -34.035  59.052   1.716  1.00 49.91           C  
ANISOU 1046  CA  LEU A 177     5698   6702   6565   -272    553    353       C  
ATOM   1047  C   LEU A 177     -34.498  59.489   0.333  1.00 34.53           C  
ANISOU 1047  C   LEU A 177     3631   4810   4678   -310    464    307       C  
ATOM   1048  O   LEU A 177     -34.920  58.668  -0.479  1.00 45.81           O  
ANISOU 1048  O   LEU A 177     5011   6231   6164   -371    466    271       O  
ATOM   1049  CB  LEU A 177     -32.505  59.054   1.786  1.00 31.81           C  
ANISOU 1049  CB  LEU A 177     3500   4412   4175   -213    491    382       C  
ATOM   1050  CG  LEU A 177     -31.719  58.097   0.892  1.00 63.42           C  
ANISOU 1050  CG  LEU A 177     7534   8397   8167   -235    449    378       C  
ATOM   1051  CD1 LEU A 177     -30.440  58.763   0.408  1.00 45.59           C  
ANISOU 1051  CD1 LEU A 177     5298   6181   5844   -185    339    382       C  
ATOM   1052  CD2 LEU A 177     -31.413  56.797   1.625  1.00 59.65           C  
ANISOU 1052  CD2 LEU A 177     7162   7847   7655   -231    545    411       C  
ATOM   1053  N   ALA A 178     -34.433  60.792   0.085  1.00 44.50           N  
ANISOU 1053  N   ALA A 178     4850   6129   5928   -267    392    304       N  
ATOM   1054  CA  ALA A 178     -34.706  61.354  -1.232  1.00 34.72           C  
ANISOU 1054  CA  ALA A 178     3516   4950   4725   -275    300    270       C  
ATOM   1055  C   ALA A 178     -33.424  61.973  -1.784  1.00 46.58           C  
ANISOU 1055  C   ALA A 178     5062   6473   6163   -225    207    288       C  
ATOM   1056  O   ALA A 178     -32.690  62.651  -1.062  1.00 48.48           O  
ANISOU 1056  O   ALA A 178     5364   6709   6348   -174    205    314       O  
ATOM   1057  CB  ALA A 178     -35.801  62.393  -1.144  1.00 43.30           C  
ANISOU 1057  CB  ALA A 178     4513   6081   5858   -262    305    255       C  
ATOM   1058  N   SER A 179     -33.153  61.738  -3.063  1.00 47.11           N  
ANISOU 1058  N   SER A 179     5096   6564   6238   -240    134    267       N  
ATOM   1059  CA  SER A 179     -31.900  62.182  -3.663  1.00 40.07           C  
ANISOU 1059  CA  SER A 179     4250   5684   5291   -199     56    282       C  
ATOM   1060  C   SER A 179     -32.093  62.617  -5.112  1.00 47.31           C  
ANISOU 1060  C   SER A 179     5095   6652   6230   -193    -25    259       C  
ATOM   1061  O   SER A 179     -33.162  62.420  -5.692  1.00 46.53           O  
ANISOU 1061  O   SER A 179     4911   6586   6184   -221    -30    225       O  
ATOM   1062  CB  SER A 179     -30.856  61.064  -3.575  1.00 54.80           C  
ANISOU 1062  CB  SER A 179     6201   7506   7114   -213     62    296       C  
ATOM   1063  OG  SER A 179     -29.657  61.413  -4.247  1.00 78.47           O  
ANISOU 1063  OG  SER A 179     9233  10516  10066   -180    -12    303       O  
ATOM   1064  N   THR A 180     -31.057  63.213  -5.693  1.00 43.08           N  
ANISOU 1064  N   THR A 180     4593   6124   5650   -152    -86    274       N  
ATOM   1065  CA  THR A 180     -31.131  63.687  -7.070  1.00 27.72           C  
ANISOU 1065  CA  THR A 180     2596   4223   3711   -130   -157    261       C  
ATOM   1066  C   THR A 180     -30.130  63.006  -8.004  1.00 51.56           C  
ANISOU 1066  C   THR A 180     5657   7233   6700   -139   -209    259       C  
ATOM   1067  O   THR A 180     -29.025  62.615  -7.607  1.00 42.43           O  
ANISOU 1067  O   THR A 180     4578   6038   5505   -139   -202    277       O  
ATOM   1068  CB  THR A 180     -30.928  65.217  -7.161  1.00 49.61           C  
ANISOU 1068  CB  THR A 180     5366   7015   6469    -65   -177    281       C  
ATOM   1069  CG2 THR A 180     -32.103  65.963  -6.528  1.00 27.70           C  
ANISOU 1069  CG2 THR A 180     2533   4261   3729    -51   -136    278       C  
ATOM   1070  OG1 THR A 180     -29.717  65.581  -6.487  1.00 46.62           O  
ANISOU 1070  OG1 THR A 180     5066   6599   6048    -45   -165    302       O  
ATOM   1071  N   GLN A 181     -30.542  62.860  -9.254  1.00 40.76           N  
ANISOU 1071  N   GLN A 181     4234   5906   5348   -140   -262    234       N  
ATOM   1072  CA  GLN A 181     -29.650  62.432 -10.313  1.00 44.49           C  
ANISOU 1072  CA  GLN A 181     4739   6377   5788   -135   -317    233       C  
ATOM   1073  C   GLN A 181     -30.219  62.987 -11.602  1.00 58.93           C  
ANISOU 1073  C   GLN A 181     6503   8268   7622    -97   -377    215       C  
ATOM   1074  O   GLN A 181     -31.196  62.451 -12.132  1.00 29.88           O  
ANISOU 1074  O   GLN A 181     2750   4630   3974   -122   -395    172       O  
ATOM   1075  CB  GLN A 181     -29.562  60.908 -10.379  1.00 42.27           C  
ANISOU 1075  CB  GLN A 181     4477   6067   5517   -199   -303    210       C  
ATOM   1076  CG  GLN A 181     -28.663  60.407 -11.495  1.00 37.48           C  
ANISOU 1076  CG  GLN A 181     3903   5459   4878   -196   -358    206       C  
ATOM   1077  CD  GLN A 181     -27.246  60.915 -11.359  1.00 41.24           C  
ANISOU 1077  CD  GLN A 181     4458   5906   5304   -154   -370    246       C  
ATOM   1078  NE2 GLN A 181     -26.575  60.502 -10.295  1.00 72.63           N  
ANISOU 1078  NE2 GLN A 181     8499   9837   9262   -166   -327    265       N  
ATOM   1079  OE1 GLN A 181     -26.763  61.680 -12.191  1.00 49.28           O  
ANISOU 1079  OE1 GLN A 181     5498   6931   6293   -109   -401    257       O  
ATOM   1080  N   PHE A 182     -29.617  64.069 -12.092  1.00 40.66           N  
ANISOU 1080  N   PHE A 182     4236   5947   5266    -33   -391    245       N  
ATOM   1081  CA  PHE A 182     -30.186  64.817 -13.207  1.00 46.54           C  
ANISOU 1081  CA  PHE A 182     4947   6739   5996     25   -426    239       C  
ATOM   1082  C   PHE A 182     -29.501  64.580 -14.548  1.00 46.05           C  
ANISOU 1082  C   PHE A 182     4930   6676   5890     49   -466    238       C  
ATOM   1083  O   PHE A 182     -30.147  64.655 -15.593  1.00 33.81           O  
ANISOU 1083  O   PHE A 182     3336   5181   4328     84   -507    215       O  
ATOM   1084  CB  PHE A 182     -30.200  66.316 -12.904  1.00 44.89           C  
ANISOU 1084  CB  PHE A 182     4746   6528   5781     90   -402    275       C  
ATOM   1085  CG  PHE A 182     -31.194  66.713 -11.861  1.00 37.96           C  
ANISOU 1085  CG  PHE A 182     3804   5671   4948     85   -369    271       C  
ATOM   1086  CD1 PHE A 182     -30.997  67.851 -11.100  1.00 53.90           C  
ANISOU 1086  CD1 PHE A 182     5842   7668   6971    120   -330    302       C  
ATOM   1087  CD2 PHE A 182     -32.325  65.949 -11.637  1.00 49.52           C  
ANISOU 1087  CD2 PHE A 182     5185   7175   6457     41   -369    231       C  
ATOM   1088  CE1 PHE A 182     -31.909  68.221 -10.141  1.00 41.26           C  
ANISOU 1088  CE1 PHE A 182     4187   6082   5408    118   -291    298       C  
ATOM   1089  CE2 PHE A 182     -33.243  66.317 -10.674  1.00 44.55           C  
ANISOU 1089  CE2 PHE A 182     4499   6558   5869     35   -326    227       C  
ATOM   1090  CZ  PHE A 182     -33.033  67.453  -9.928  1.00 26.71           C  
ANISOU 1090  CZ  PHE A 182     2273   4273   3603     76   -286    264       C  
ATOM   1091  N   GLU A 183     -28.199  64.319 -14.531  1.00 34.02           N  
ANISOU 1091  N   GLU A 183     3490   5097   4341     35   -455    259       N  
ATOM   1092  CA  GLU A 183     -27.493  64.091 -15.783  1.00 46.38           C  
ANISOU 1092  CA  GLU A 183     5098   6656   5868     56   -483    258       C  
ATOM   1093  C   GLU A 183     -28.115  62.897 -16.480  1.00 23.69           C  
ANISOU 1093  C   GLU A 183     2181   3821   3001     22   -524    212       C  
ATOM   1094  O   GLU A 183     -28.254  61.835 -15.882  1.00 51.70           O  
ANISOU 1094  O   GLU A 183     5713   7355   6578    -44   -516    189       O  
ATOM   1095  CB  GLU A 183     -26.000  63.852 -15.560  1.00 51.27           C  
ANISOU 1095  CB  GLU A 183     5804   7209   6467     38   -460    280       C  
ATOM   1096  CG  GLU A 183     -25.195  63.748 -16.853  1.00 62.81           C  
ANISOU 1096  CG  GLU A 183     7311   8660   7895     64   -479    283       C  
ATOM   1097  CD  GLU A 183     -23.703  63.619 -16.616  1.00116.57           C  
ANISOU 1097  CD  GLU A 183    14193  15406  14691     48   -452    300       C  
ATOM   1098  OE1 GLU A 183     -23.280  63.607 -15.443  1.00159.64           O  
ANISOU 1098  OE1 GLU A 183    19665  20833  20158     23   -424    306       O  
ATOM   1099  OE2 GLU A 183     -22.949  63.529 -17.607  1.00138.19           O1-
ANISOU 1099  OE2 GLU A 183    16968  18130  17408     66   -460    303       O1-
ATOM   1100  N   PRO A 184     -28.498  63.073 -17.755  1.00 55.22           N  
ANISOU 1100  N   PRO A 184     6149   7865   6969     69   -568    193       N  
ATOM   1101  CA  PRO A 184     -28.315  64.304 -18.530  1.00 44.54           C  
ANISOU 1101  CA  PRO A 184     4818   6528   5578    157   -573    225       C  
ATOM   1102  C   PRO A 184     -29.569  65.175 -18.569  1.00 44.86           C  
ANISOU 1102  C   PRO A 184     4782   6637   5625    215   -587    219       C  
ATOM   1103  O   PRO A 184     -29.475  66.383 -18.794  1.00 63.39           O  
ANISOU 1103  O   PRO A 184     7148   8987   7952    290   -573    259       O  
ATOM   1104  CB  PRO A 184     -28.068  63.778 -19.950  1.00 26.88           C  
ANISOU 1104  CB  PRO A 184     2595   4317   3300    183   -618    203       C  
ATOM   1105  CG  PRO A 184     -28.321  62.262 -19.888  1.00 38.31           C  
ANISOU 1105  CG  PRO A 184     4012   5771   4773    103   -641    150       C  
ATOM   1106  CD  PRO A 184     -29.029  62.003 -18.604  1.00 31.67           C  
ANISOU 1106  CD  PRO A 184     3120   4926   3987     44   -615    136       C  
ATOM   1107  N   THR A 185     -30.726  64.559 -18.335  1.00 49.48           N  
ANISOU 1107  N   THR A 185     5279   7277   6246    180   -611    167       N  
ATOM   1108  CA  THR A 185     -32.000  65.144 -18.725  1.00 31.71           C  
ANISOU 1108  CA  THR A 185     2939   5115   3996    241   -644    142       C  
ATOM   1109  C   THR A 185     -33.099  64.910 -17.683  1.00 46.98           C  
ANISOU 1109  C   THR A 185     4782   7073   5995    189   -626    108       C  
ATOM   1110  O   THR A 185     -34.276  64.768 -18.019  1.00 45.89           O  
ANISOU 1110  O   THR A 185     4543   7018   5876    202   -663     52       O  
ATOM   1111  CB  THR A 185     -32.413  64.554 -20.097  1.00 61.74           C  
ANISOU 1111  CB  THR A 185     6699   8994   7765    271   -714     86       C  
ATOM   1112  CG2 THR A 185     -33.733  65.104 -20.568  1.00 94.22           C  
ANISOU 1112  CG2 THR A 185    10713  13216  11872    345   -759     50       C  
ATOM   1113  OG1 THR A 185     -31.407  64.868 -21.065  1.00 44.25           O  
ANISOU 1113  OG1 THR A 185     4570   6755   5488    329   -722    124       O  
ATOM   1114  N   ALA A 186     -32.718  64.895 -16.410  1.00 33.24           N  
ANISOU 1114  N   ALA A 186     3074   5265   4289    134   -569    137       N  
ATOM   1115  CA  ALA A 186     -33.666  64.533 -15.357  1.00 36.69           C  
ANISOU 1115  CA  ALA A 186     3434   5715   4793     76   -539    107       C  
ATOM   1116  C   ALA A 186     -34.128  65.684 -14.465  1.00 51.29           C  
ANISOU 1116  C   ALA A 186     5263   7564   6661    115   -498    142       C  
ATOM   1117  O   ALA A 186     -35.041  65.511 -13.661  1.00 62.18           O  
ANISOU 1117  O   ALA A 186     6568   8962   8097     77   -469    116       O  
ATOM   1118  CB  ALA A 186     -33.109  63.403 -14.512  1.00 57.81           C  
ANISOU 1118  CB  ALA A 186     6143   8324   7499    -20   -501    102       C  
ATOM   1119  N   ALA A 187     -33.503  66.850 -14.595  1.00 39.34           N  
ANISOU 1119  N   ALA A 187     3813   6028   5108    187   -487    199       N  
ATOM   1120  CA  ALA A 187     -33.900  68.000 -13.785  1.00 21.90           C  
ANISOU 1120  CA  ALA A 187     1587   3814   2918    229   -446    232       C  
ATOM   1121  C   ALA A 187     -35.370  68.317 -14.013  1.00 37.61           C  
ANISOU 1121  C   ALA A 187     3466   5892   4932    270   -466    198       C  
ATOM   1122  O   ALA A 187     -36.081  68.741 -13.101  1.00 43.37           O  
ANISOU 1122  O   ALA A 187     4146   6628   5704    267   -427    200       O  
ATOM   1123  CB  ALA A 187     -33.040  69.206 -14.113  1.00 49.45           C  
ANISOU 1123  CB  ALA A 187     5154   7269   6366    304   -431    289       C  
ATOM   1124  N   ARG A 188     -35.819  68.092 -15.241  1.00 15.76           N  
ANISOU 1124  N   ARG A 188      656   3195   2136    312   -529    163       N  
ATOM   1125  CA  ARG A 188     -37.190  68.378 -15.635  1.00 29.01           C  
ANISOU 1125  CA  ARG A 188     2221   4975   3828    366   -563    121       C  
ATOM   1126  C   ARG A 188     -38.170  67.478 -14.893  1.00 39.16           C  
ANISOU 1126  C   ARG A 188     3403   6285   5190    275   -547     54       C  
ATOM   1127  O   ARG A 188     -39.384  67.680 -14.953  1.00 37.85           O  
ANISOU 1127  O   ARG A 188     3126   6200   5054    303   -563     10       O  
ATOM   1128  CB  ARG A 188     -37.329  68.171 -17.140  1.00 42.11           C  
ANISOU 1128  CB  ARG A 188     3859   6709   5431    429   -641     88       C  
ATOM   1129  CG  ARG A 188     -36.930  66.773 -17.579  1.00 45.64           C  
ANISOU 1129  CG  ARG A 188     4313   7146   5882    343   -671     34       C  
ATOM   1130  CD  ARG A 188     -36.823  66.662 -19.077  1.00 47.93           C  
ANISOU 1130  CD  ARG A 188     4606   7501   6105    414   -744     10       C  
ATOM   1131  NE  ARG A 188     -35.634  67.338 -19.577  1.00 48.62           N  
ANISOU 1131  NE  ARG A 188     4815   7530   6127    476   -730     87       N  
ATOM   1132  CZ  ARG A 188     -35.333  67.447 -20.863  1.00 24.78           C  
ANISOU 1132  CZ  ARG A 188     1827   4551   3038    555   -777     88       C  
ATOM   1133  NH1 ARG A 188     -36.134  66.916 -21.777  1.00 67.82           N1+
ANISOU 1133  NH1 ARG A 188     7194  10106   8468    585   -851     13       N1+
ATOM   1134  NH2 ARG A 188     -34.227  68.076 -21.234  1.00 53.51           N  
ANISOU 1134  NH2 ARG A 188     5576   8126   6629    604   -749    160       N  
ATOM   1135  N   MET A 189     -37.631  66.475 -14.204  1.00 42.91           N  
ANISOU 1135  N   MET A 189     3913   6691   5699    169   -511     46       N  
ATOM   1136  CA  MET A 189     -38.435  65.554 -13.411  1.00 44.43           C  
ANISOU 1136  CA  MET A 189     4022   6888   5973     73   -473    -11       C  
ATOM   1137  C   MET A 189     -38.667  66.085 -11.995  1.00 47.06           C  
ANISOU 1137  C   MET A 189     4360   7175   6346     57   -392     27       C  
ATOM   1138  O   MET A 189     -39.660  65.752 -11.358  1.00 41.83           O  
ANISOU 1138  O   MET A 189     3621   6526   5745      9   -348    -15       O  
ATOM   1139  CB  MET A 189     -37.764  64.180 -13.343  1.00 40.45           C  
ANISOU 1139  CB  MET A 189     3557   6327   5484    -26   -462    -35       C  
ATOM   1140  CG  MET A 189     -37.959  63.309 -14.571  1.00 55.63           C  
ANISOU 1140  CG  MET A 189     5436   8303   7398    -42   -529   -107       C  
ATOM   1141  SD  MET A 189     -37.185  61.692 -14.363  1.00 52.09           S  
ANISOU 1141  SD  MET A 189     5037   7777   6978   -162   -499   -130       S  
ATOM   1142  CE  MET A 189     -37.814  61.225 -12.753  1.00205.29           C  
ANISOU 1142  CE  MET A 189    24421  27116  26464   -253   -383   -136       C  
ATOM   1143  N   ALA A 190     -37.740  66.905 -11.509  1.00 31.75           N  
ANISOU 1143  N   ALA A 190     2522   5174   4366     95   -364    100       N  
ATOM   1144  CA  ALA A 190     -37.839  67.464 -10.167  1.00 39.99           C  
ANISOU 1144  CA  ALA A 190     3596   6167   5432     86   -285    135       C  
ATOM   1145  C   ALA A 190     -38.496  68.845 -10.176  1.00 50.28           C  
ANISOU 1145  C   ALA A 190     4862   7513   6731    178   -282    159       C  
ATOM   1146  O   ALA A 190     -39.202  69.219  -9.236  1.00 33.75           O  
ANISOU 1146  O   ALA A 190     2737   5413   4674    172   -225    160       O  
ATOM   1147  CB  ALA A 190     -36.465  67.532  -9.514  1.00 21.76           C  
ANISOU 1147  CB  ALA A 190     1413   3770   3087     69   -252    188       C  
ATOM   1148  N   PHE A 191     -38.265  69.601 -11.244  1.00 40.02           N  
ANISOU 1148  N   PHE A 191     3571   6252   5385    269   -337    181       N  
ATOM   1149  CA  PHE A 191     -38.892  70.907 -11.400  1.00 39.30           C  
ANISOU 1149  CA  PHE A 191     3449   6201   5283    371   -333    207       C  
ATOM   1150  C   PHE A 191     -38.815  71.357 -12.844  1.00 31.85           C  
ANISOU 1150  C   PHE A 191     2502   5316   4282    470   -403    215       C  
ATOM   1151  O   PHE A 191     -37.848  71.048 -13.536  1.00 33.78           O  
ANISOU 1151  O   PHE A 191     2823   5531   4483    466   -432    229       O  
ATOM   1152  CB  PHE A 191     -38.206  71.938 -10.507  1.00 53.51           C  
ANISOU 1152  CB  PHE A 191     5340   7920   7071    393   -265    268       C  
ATOM   1153  CG  PHE A 191     -36.745  72.102 -10.792  1.00 36.60           C  
ANISOU 1153  CG  PHE A 191     3309   5711   4885    397   -269    307       C  
ATOM   1154  CD1 PHE A 191     -35.809  71.328 -10.129  1.00 38.99           C  
ANISOU 1154  CD1 PHE A 191     3675   5949   5190    311   -249    305       C  
ATOM   1155  CD2 PHE A 191     -36.306  73.027 -11.722  1.00 34.06           C  
ANISOU 1155  CD2 PHE A 191     3029   5393   4521    490   -288    346       C  
ATOM   1156  CE1 PHE A 191     -34.464  71.472 -10.389  1.00 54.90           C  
ANISOU 1156  CE1 PHE A 191     5782   7909   7170    314   -253    333       C  
ATOM   1157  CE2 PHE A 191     -34.963  73.175 -11.988  1.00 41.56           C  
ANISOU 1157  CE2 PHE A 191     4074   6278   5440    488   -282    376       C  
ATOM   1158  CZ  PHE A 191     -34.039  72.396 -11.320  1.00 43.13           C  
ANISOU 1158  CZ  PHE A 191     4324   6418   5644    397   -269    366       C  
ATOM   1159  N   PRO A 192     -39.835  72.093 -13.302  1.00 37.52           N  
ANISOU 1159  N   PRO A 192     3146   6116   4995    565   -425    209       N  
ATOM   1160  CA  PRO A 192     -39.850  72.630 -14.665  1.00 22.95           C  
ANISOU 1160  CA  PRO A 192     1309   4330   3081    682   -483    223       C  
ATOM   1161  C   PRO A 192     -38.639  73.518 -14.884  1.00 35.20           C  
ANISOU 1161  C   PRO A 192     2987   5801   4585    738   -451    302       C  
ATOM   1162  O   PRO A 192     -38.252  74.252 -13.974  1.00 52.91           O  
ANISOU 1162  O   PRO A 192     5281   7971   6851    733   -381    347       O  
ATOM   1163  CB  PRO A 192     -41.122  73.485 -14.692  1.00 37.22           C  
ANISOU 1163  CB  PRO A 192     3021   6222   4897    782   -486    217       C  
ATOM   1164  CG  PRO A 192     -41.973  72.943 -13.609  1.00 52.88           C  
ANISOU 1164  CG  PRO A 192     4913   8216   6962    691   -452    167       C  
ATOM   1165  CD  PRO A 192     -41.034  72.478 -12.543  1.00 43.96           C  
ANISOU 1165  CD  PRO A 192     3872   6969   5861    575   -388    189       C  
ATOM   1166  N   CYS A 193     -38.045  73.453 -16.069  1.00 49.10           N  
ANISOU 1166  N   CYS A 193     4800   7572   6282    789   -495    315       N  
ATOM   1167  CA  CYS A 193     -36.889  74.284 -16.369  1.00 43.24           C  
ANISOU 1167  CA  CYS A 193     4175   6753   5503    842   -457    386       C  
ATOM   1168  C   CYS A 193     -36.508  74.221 -17.839  1.00 38.77           C  
ANISOU 1168  C   CYS A 193     3649   6221   4861    919   -508    395       C  
ATOM   1169  O   CYS A 193     -37.063  73.437 -18.607  1.00 32.32           O  
ANISOU 1169  O   CYS A 193     2772   5489   4019    922   -580    340       O  
ATOM   1170  CB  CYS A 193     -35.696  73.880 -15.498  1.00 17.46           C  
ANISOU 1170  CB  CYS A 193      986   3381   2268    730   -412    397       C  
ATOM   1171  SG  CYS A 193     -35.322  72.110 -15.502  1.00 46.42           S  
ANISOU 1171  SG  CYS A 193     4647   7045   5945    593   -456    334       S  
ATOM   1172  N   PHE A 194     -35.567  75.074 -18.225  1.00 42.27           N  
ANISOU 1172  N   PHE A 194     4192   6596   5271    985   -466    463       N  
ATOM   1173  CA  PHE A 194     -34.966  75.005 -19.545  1.00 26.47           C  
ANISOU 1173  CA  PHE A 194     2252   4605   3200   1050   -497    481       C  
ATOM   1174  C   PHE A 194     -33.797  74.046 -19.418  1.00 22.43           C  
ANISOU 1174  C   PHE A 194     1797   4024   2701    928   -497    462       C  
ATOM   1175  O   PHE A 194     -32.674  74.452 -19.128  1.00 55.80           O  
ANISOU 1175  O   PHE A 194     6106   8154   6940    906   -440    504       O  
ATOM   1176  CB  PHE A 194     -34.515  76.398 -19.998  1.00 39.10           C  
ANISOU 1176  CB  PHE A 194     3934   6155   4766   1182   -436    565       C  
ATOM   1177  CG  PHE A 194     -35.648  77.389 -20.137  1.00 42.66           C  
ANISOU 1177  CG  PHE A 194     4340   6671   5199   1319   -428    592       C  
ATOM   1178  CD1 PHE A 194     -36.373  77.467 -21.315  1.00 57.61           C  
ANISOU 1178  CD1 PHE A 194     6204   8671   7015   1448   -488    588       C  
ATOM   1179  CD2 PHE A 194     -35.992  78.235 -19.090  1.00 43.78           C  
ANISOU 1179  CD2 PHE A 194     4475   6768   5393   1319   -357    615       C  
ATOM   1180  CE1 PHE A 194     -37.418  78.373 -21.450  1.00 59.96           C  
ANISOU 1180  CE1 PHE A 194     6458   9034   7288   1587   -484    612       C  
ATOM   1181  CE2 PHE A 194     -37.032  79.143 -19.218  1.00 32.10           C  
ANISOU 1181  CE2 PHE A 194     2959   5344   3892   1446   -342    639       C  
ATOM   1182  CZ  PHE A 194     -37.746  79.210 -20.401  1.00 44.37           C  
ANISOU 1182  CZ  PHE A 194     4476   7010   5372   1586   -410    641       C  
ATOM   1183  N   ASP A 195     -34.081  72.763 -19.612  1.00 54.52           N  
ANISOU 1183  N   ASP A 195     5811   8137   6767    850   -557    395       N  
ATOM   1184  CA  ASP A 195     -33.157  71.696 -19.238  1.00 49.87           C  
ANISOU 1184  CA  ASP A 195     5262   7484   6201    723   -553    370       C  
ATOM   1185  C   ASP A 195     -32.139  71.382 -20.327  1.00 40.80           C  
ANISOU 1185  C   ASP A 195     4190   6311   5001    740   -570    382       C  
ATOM   1186  O   ASP A 195     -32.027  70.242 -20.776  1.00 60.81           O  
ANISOU 1186  O   ASP A 195     6714   8867   7525    684   -615    334       O  
ATOM   1187  CB  ASP A 195     -33.932  70.431 -18.847  1.00 46.34           C  
ANISOU 1187  CB  ASP A 195     4729   7086   5793    627   -595    294       C  
ATOM   1188  CG  ASP A 195     -33.125  69.493 -17.969  1.00 55.74           C  
ANISOU 1188  CG  ASP A 195     5960   8197   7024    498   -566    281       C  
ATOM   1189  OD1 ASP A 195     -31.936  69.774 -17.717  1.00 85.97           O  
ANISOU 1189  OD1 ASP A 195     9876  11942  10846    481   -525    323       O  
ATOM   1190  OD2 ASP A 195     -33.683  68.468 -17.526  1.00 53.91           O1-
ANISOU 1190  OD2 ASP A 195     5667   7986   6831    417   -582    227       O1-
ATOM   1191  N   GLU A 196     -31.399  72.405 -20.744  1.00 45.33           N  
ANISOU 1191  N   GLU A 196     4842   6836   5546    820   -526    447       N  
ATOM   1192  CA  GLU A 196     -30.247  72.220 -21.623  1.00 20.43           C  
ANISOU 1192  CA  GLU A 196     1771   3638   2352    830   -521    467       C  
ATOM   1193  C   GLU A 196     -29.017  72.830 -20.953  1.00 36.86           C  
ANISOU 1193  C   GLU A 196     3928   5607   4470    796   -445    512       C  
ATOM   1194  O   GLU A 196     -29.130  73.809 -20.219  1.00 44.20           O  
ANISOU 1194  O   GLU A 196     4858   6503   5434    822   -394    544       O  
ATOM   1195  CB  GLU A 196     -30.511  72.828 -23.003  1.00 24.48           C  
ANISOU 1195  CB  GLU A 196     2307   4206   2789    977   -542    498       C  
ATOM   1196  CG  GLU A 196     -31.833  72.359 -23.606  1.00 20.72           C  
ANISOU 1196  CG  GLU A 196     1738   3858   2276   1027   -625    444       C  
ATOM   1197  CD  GLU A 196     -31.962  72.635 -25.089  1.00 54.90           C  
ANISOU 1197  CD  GLU A 196     6094   8254   6512   1168   -662    460       C  
ATOM   1198  OE1 GLU A 196     -32.945  72.153 -25.689  1.00 50.77           O  
ANISOU 1198  OE1 GLU A 196     5493   7846   5952   1211   -741    402       O  
ATOM   1199  OE2 GLU A 196     -31.088  73.326 -25.651  1.00 77.37           O1-
ANISOU 1199  OE2 GLU A 196     9037  11038   9322   1239   -611    526       O1-
ATOM   1200  N   PRO A 197     -27.837  72.239 -21.184  1.00 36.60           N  
ANISOU 1200  N   PRO A 197     3953   5519   4435    736   -438    506       N  
ATOM   1201  CA  PRO A 197     -26.664  72.640 -20.402  1.00 29.62           C  
ANISOU 1201  CA  PRO A 197     3121   4539   3594    686   -376    528       C  
ATOM   1202  C   PRO A 197     -26.193  74.050 -20.738  1.00 39.35           C  
ANISOU 1202  C   PRO A 197     4408   5716   4826    785   -309    592       C  
ATOM   1203  O   PRO A 197     -25.415  74.620 -19.977  1.00 34.20           O  
ANISOU 1203  O   PRO A 197     3782   4988   4224    757   -253    605       O  
ATOM   1204  CB  PRO A 197     -25.592  71.619 -20.810  1.00 26.99           C  
ANISOU 1204  CB  PRO A 197     2831   4176   3250    617   -392    504       C  
ATOM   1205  CG  PRO A 197     -26.317  70.532 -21.528  1.00 15.58           C  
ANISOU 1205  CG  PRO A 197     1348   2805   1768    608   -461    462       C  
ATOM   1206  CD  PRO A 197     -27.516  71.177 -22.148  1.00 45.53           C  
ANISOU 1206  CD  PRO A 197     5099   6675   5525    716   -487    475       C  
ATOM   1207  N   ALA A 198     -26.658  74.599 -21.856  1.00 31.05           N  
ANISOU 1207  N   ALA A 198     3376   4701   3721    906   -312    629       N  
ATOM   1208  CA  ALA A 198     -26.244  75.933 -22.287  1.00 39.10           C  
ANISOU 1208  CA  ALA A 198     4464   5657   4737   1016   -234    700       C  
ATOM   1209  C   ALA A 198     -27.024  77.037 -21.574  1.00 40.11           C  
ANISOU 1209  C   ALA A 198     4574   5772   4893   1060   -175    720       C  
ATOM   1210  O   ALA A 198     -26.561  78.176 -21.481  1.00 55.65           O  
ANISOU 1210  O   ALA A 198     6607   7655   6884   1100    -71    758       O  
ATOM   1211  CB  ALA A 198     -26.388  76.073 -23.791  1.00 43.54           C  
ANISOU 1211  CB  ALA A 198     5071   6257   5216   1136   -246    735       C  
ATOM   1212  N   PHE A 199     -28.209  76.692 -21.080  1.00 31.67           N  
ANISOU 1212  N   PHE A 199     3417   4787   3829   1051   -235    690       N  
ATOM   1213  CA  PHE A 199     -29.051  77.634 -20.358  1.00 40.31           C  
ANISOU 1213  CA  PHE A 199     4485   5881   4949   1090   -187    704       C  
ATOM   1214  C   PHE A 199     -28.648  77.713 -18.894  1.00 53.64           C  
ANISOU 1214  C   PHE A 199     6165   7504   6712    973   -139    674       C  
ATOM   1215  O   PHE A 199     -29.358  77.184 -18.037  1.00 54.79           O  
ANISOU 1215  O   PHE A 199     6237   7696   6884    911   -178    635       O  
ATOM   1216  CB  PHE A 199     -30.506  77.181 -20.402  1.00 26.68           C  
ANISOU 1216  CB  PHE A 199     2659   4277   3203   1124   -271    676       C  
ATOM   1217  CG  PHE A 199     -31.168  77.346 -21.732  1.00 25.95           C  
ANISOU 1217  CG  PHE A 199     2562   4268   3029   1264   -316    699       C  
ATOM   1218  CD1 PHE A 199     -31.590  78.591 -22.163  1.00 46.13           C  
ANISOU 1218  CD1 PHE A 199     5156   6818   5552   1410   -260    761       C  
ATOM   1219  CD2 PHE A 199     -31.418  76.245 -22.534  1.00 59.25           C  
ANISOU 1219  CD2 PHE A 199     6746   8569   7196   1244   -403    650       C  
ATOM   1220  CE1 PHE A 199     -32.226  78.741 -23.382  1.00 23.99           C  
ANISOU 1220  CE1 PHE A 199     2349   4102   2662   1557   -306    783       C  
ATOM   1221  CE2 PHE A 199     -32.052  76.389 -23.757  1.00 61.99           C  
ANISOU 1221  CE2 PHE A 199     7089   9006   7460   1378   -448    659       C  
ATOM   1222  CZ  PHE A 199     -32.456  77.639 -24.180  1.00 32.18           C  
ANISOU 1222  CZ  PHE A 199     3348   5235   3645   1539   -403    727       C  
ATOM   1223  N   LYS A 200     -27.526  78.362 -18.599  1.00 20.45           N  
ANISOU 1223  N   LYS A 200     2033   3194   2542    944    -51    686       N  
ATOM   1224  CA  LYS A 200     -27.065  78.436 -17.216  1.00 30.47           C  
ANISOU 1224  CA  LYS A 200     3294   4409   3874    839    -11    647       C  
ATOM   1225  C   LYS A 200     -27.789  79.533 -16.447  1.00 37.54           C  
ANISOU 1225  C   LYS A 200     4178   5284   4800    875     56    659       C  
ATOM   1226  O   LYS A 200     -28.289  80.494 -17.035  1.00 38.51           O  
ANISOU 1226  O   LYS A 200     4328   5400   4904    985    104    707       O  
ATOM   1227  CB  LYS A 200     -25.562  78.667 -17.134  1.00 11.19           C  
ANISOU 1227  CB  LYS A 200      917   1870   1462    786     51    637       C  
ATOM   1228  CG  LYS A 200     -24.697  77.546 -17.651  1.00 10.67           C  
ANISOU 1228  CG  LYS A 200      862   1815   1376    733     -9    617       C  
ATOM   1229  CD  LYS A 200     -23.278  77.754 -17.162  1.00 36.78           C  
ANISOU 1229  CD  LYS A 200     4210   5035   4728    660     52    587       C  
ATOM   1230  CE  LYS A 200     -22.354  76.690 -17.691  1.00 44.30           C  
ANISOU 1230  CE  LYS A 200     5177   5995   5662    614     -1    570       C  
ATOM   1231  NZ  LYS A 200     -21.018  76.701 -17.032  1.00 55.25           N1+
ANISOU 1231  NZ  LYS A 200     6583   7317   7093    533     40    524       N1+
ATOM   1232  N   ALA A 201     -27.842  79.379 -15.128  1.00 26.14           N  
ANISOU 1232  N   ALA A 201     2700   3832   3400    788     62    617       N  
ATOM   1233  CA  ALA A 201     -28.513  80.341 -14.275  1.00 21.96           C  
ANISOU 1233  CA  ALA A 201     2157   3283   2902    811    125    621       C  
ATOM   1234  C   ALA A 201     -28.125  80.172 -12.812  1.00 27.95           C  
ANISOU 1234  C   ALA A 201     2902   4012   3707    705    143    568       C  
ATOM   1235  O   ALA A 201     -27.346  79.288 -12.456  1.00 39.00           O  
ANISOU 1235  O   ALA A 201     4299   5409   5108    621    105    530       O  
ATOM   1236  CB  ALA A 201     -30.016  80.225 -14.429  1.00 12.50           C  
ANISOU 1236  CB  ALA A 201      892   2177   1681    874     76    637       C  
ATOM   1237  N   SER A 202     -28.678  81.037 -11.972  1.00 34.26           N  
ANISOU 1237  N   SER A 202     3693   4791   4536    720    203    567       N  
ATOM   1238  CA  SER A 202     -28.465  80.967 -10.543  1.00 38.68           C  
ANISOU 1238  CA  SER A 202     4238   5331   5130    636    221    517       C  
ATOM   1239  C   SER A 202     -29.672  80.289  -9.911  1.00 22.75           C  
ANISOU 1239  C   SER A 202     2148   3391   3104    621    168    508       C  
ATOM   1240  O   SER A 202     -30.773  80.372 -10.444  1.00 26.72           O  
ANISOU 1240  O   SER A 202     2612   3949   3592    688    147    539       O  
ATOM   1241  CB  SER A 202     -28.289  82.372  -9.983  1.00 36.04           C  
ANISOU 1241  CB  SER A 202     3941   4917   4835    659    329    513       C  
ATOM   1242  OG  SER A 202     -27.999  82.311  -8.601  1.00103.64           O  
ANISOU 1242  OG  SER A 202    12490  13464  13422    581    343    456       O  
ATOM   1243  N   PHE A 203     -29.460  79.614  -8.784  1.00 23.71           N  
ANISOU 1243  N   PHE A 203     2253   3520   3237    537    151    465       N  
ATOM   1244  CA  PHE A 203     -30.526  78.859  -8.127  1.00 39.54           C  
ANISOU 1244  CA  PHE A 203     4195   5588   5239    511    112    454       C  
ATOM   1245  C   PHE A 203     -30.643  79.164  -6.636  1.00 52.72           C  
ANISOU 1245  C   PHE A 203     5864   7236   6932    472    160    424       C  
ATOM   1246  O   PHE A 203     -29.701  78.938  -5.869  1.00 28.79           O  
ANISOU 1246  O   PHE A 203     2866   4174   3900    414    168    387       O  
ATOM   1247  CB  PHE A 203     -30.312  77.346  -8.300  1.00 33.00           C  
ANISOU 1247  CB  PHE A 203     3346   4802   4390    450     36    436       C  
ATOM   1248  CG  PHE A 203     -30.372  76.880  -9.722  1.00 27.86           C  
ANISOU 1248  CG  PHE A 203     2685   4187   3713    486    -21    458       C  
ATOM   1249  CD1 PHE A 203     -31.573  76.503 -10.292  1.00 28.17           C  
ANISOU 1249  CD1 PHE A 203     2659   4300   3745    521    -65    467       C  
ATOM   1250  CD2 PHE A 203     -29.225  76.812 -10.489  1.00 35.31           C  
ANISOU 1250  CD2 PHE A 203     3681   5096   4640    485    -31    464       C  
ATOM   1251  CE1 PHE A 203     -31.629  76.071 -11.599  1.00 19.89           C  
ANISOU 1251  CE1 PHE A 203     1599   3292   2665    559   -123    479       C  
ATOM   1252  CE2 PHE A 203     -29.277  76.385 -11.802  1.00 44.30           C  
ANISOU 1252  CE2 PHE A 203     4815   6269   5749    523    -82    484       C  
ATOM   1253  CZ  PHE A 203     -30.481  76.015 -12.357  1.00 37.36           C  
ANISOU 1253  CZ  PHE A 203     3873   5467   4856    562   -131    490       C  
ATOM   1254  N   SER A 204     -31.805  79.671  -6.230  1.00 26.50           N  
ANISOU 1254  N   SER A 204     2506   3938   3626    509    189    437       N  
ATOM   1255  CA  SER A 204     -32.144  79.748  -4.814  1.00 36.82           C  
ANISOU 1255  CA  SER A 204     3803   5239   4948    473    226    410       C  
ATOM   1256  C   SER A 204     -33.032  78.562  -4.425  1.00 51.89           C  
ANISOU 1256  C   SER A 204     5654   7210   6853    435    183    404       C  
ATOM   1257  O   SER A 204     -34.231  78.539  -4.724  1.00 42.23           O  
ANISOU 1257  O   SER A 204     4370   6035   5641    469    174    421       O  
ATOM   1258  CB  SER A 204     -32.831  81.069  -4.485  1.00 34.74           C  
ANISOU 1258  CB  SER A 204     3538   4952   4709    533    298    426       C  
ATOM   1259  OG  SER A 204     -31.907  82.142  -4.523  1.00 86.70           O  
ANISOU 1259  OG  SER A 204    10180  11459  11304    548    359    418       O  
ATOM   1260  N   ILE A 205     -32.435  77.573  -3.765  1.00 51.98           N  
ANISOU 1260  N   ILE A 205     5683   7218   6848    366    162    376       N  
ATOM   1261  CA  ILE A 205     -33.147  76.341  -3.440  1.00 42.51           C  
ANISOU 1261  CA  ILE A 205     4442   6063   5649    324    134    370       C  
ATOM   1262  C   ILE A 205     -33.608  76.265  -1.994  1.00 33.44           C  
ANISOU 1262  C   ILE A 205     3292   4908   4505    298    183    355       C  
ATOM   1263  O   ILE A 205     -32.817  76.438  -1.069  1.00 32.20           O  
ANISOU 1263  O   ILE A 205     3188   4717   4329    280    209    334       O  
ATOM   1264  CB  ILE A 205     -32.292  75.108  -3.752  1.00 40.37           C  
ANISOU 1264  CB  ILE A 205     4195   5793   5352    272     82    358       C  
ATOM   1265  CG1 ILE A 205     -32.030  75.029  -5.256  1.00 46.34           C  
ANISOU 1265  CG1 ILE A 205     4942   6564   6100    298     30    374       C  
ATOM   1266  CG2 ILE A 205     -32.992  73.852  -3.265  1.00 13.45           C  
ANISOU 1266  CG2 ILE A 205      751   2412   1947    223     75    349       C  
ATOM   1267  CD1 ILE A 205     -31.111  73.917  -5.660  1.00 21.59           C  
ANISOU 1267  CD1 ILE A 205     1837   3426   2941    252    -19    364       C  
ATOM   1268  N   LYS A 206     -34.899  75.997  -1.820  1.00 34.82           N  
ANISOU 1268  N   LYS A 206     3404   5120   4706    300    196    361       N  
ATOM   1269  CA  LYS A 206     -35.506  75.854  -0.501  1.00 48.51           C  
ANISOU 1269  CA  LYS A 206     5133   6849   6447    279    251    351       C  
ATOM   1270  C   LYS A 206     -36.139  74.474  -0.326  1.00 48.69           C  
ANISOU 1270  C   LYS A 206     5119   6899   6482    227    244    344       C  
ATOM   1271  O   LYS A 206     -37.033  74.088  -1.082  1.00 42.37           O  
ANISOU 1271  O   LYS A 206     4244   6140   5712    226    220    343       O  
ATOM   1272  CB  LYS A 206     -36.567  76.931  -0.293  1.00 45.21           C  
ANISOU 1272  CB  LYS A 206     4673   6443   6062    330    298    362       C  
ATOM   1273  CG  LYS A 206     -36.007  78.327  -0.140  1.00 41.92           C  
ANISOU 1273  CG  LYS A 206     4304   5984   5639    377    333    365       C  
ATOM   1274  CD  LYS A 206     -37.092  79.361  -0.346  1.00 51.51           C  
ANISOU 1274  CD  LYS A 206     5472   7215   6885    442    369    386       C  
ATOM   1275  CE  LYS A 206     -37.266  79.656  -1.818  1.00 56.32           C  
ANISOU 1275  CE  LYS A 206     6051   7852   7497    497    326    411       C  
ATOM   1276  NZ  LYS A 206     -35.998  80.196  -2.379  1.00 69.76           N1+
ANISOU 1276  NZ  LYS A 206     7823   9504   9179    510    320    416       N1+
ATOM   1277  N   ILE A 207     -35.673  73.737   0.676  1.00 31.94           N  
ANISOU 1277  N   ILE A 207     3050   4752   4335    187    270    335       N  
ATOM   1278  CA  ILE A 207     -36.200  72.406   0.953  1.00 39.95           C  
ANISOU 1278  CA  ILE A 207     4045   5773   5362    135    284    331       C  
ATOM   1279  C   ILE A 207     -36.996  72.383   2.245  1.00 39.35           C  
ANISOU 1279  C   ILE A 207     3968   5685   5297    129    365    332       C  
ATOM   1280  O   ILE A 207     -36.477  72.735   3.305  1.00 44.63           O  
ANISOU 1280  O   ILE A 207     4703   6327   5928    145    401    332       O  
ATOM   1281  CB  ILE A 207     -35.075  71.378   1.127  1.00 28.30           C  
ANISOU 1281  CB  ILE A 207     2640   4272   3841    101    264    328       C  
ATOM   1282  CG1 ILE A 207     -33.955  71.617   0.112  1.00 39.38           C  
ANISOU 1282  CG1 ILE A 207     4069   5675   5221    114    194    327       C  
ATOM   1283  CG2 ILE A 207     -35.630  69.981   1.030  1.00 27.00           C  
ANISOU 1283  CG2 ILE A 207     2451   4110   3699     48    277    325       C  
ATOM   1284  CD1 ILE A 207     -34.328  71.302  -1.294  1.00 23.79           C  
ANISOU 1284  CD1 ILE A 207     2035   3732   3274    108    140    328       C  
ATOM   1285  N   ARG A 208     -38.251  71.963   2.161  1.00 38.83           N  
ANISOU 1285  N   ARG A 208     3826   5643   5284    108    394    326       N  
ATOM   1286  CA  ARG A 208     -39.051  71.759   3.360  1.00 38.01           C  
ANISOU 1286  CA  ARG A 208     3721   5523   5198     95    481    328       C  
ATOM   1287  C   ARG A 208     -38.960  70.299   3.798  1.00 51.28           C  
ANISOU 1287  C   ARG A 208     5436   7176   6873     39    517    327       C  
ATOM   1288  O   ARG A 208     -39.095  69.384   2.986  1.00 78.06           O  
ANISOU 1288  O   ARG A 208     8790  10578  10293     -4    489    313       O  
ATOM   1289  CB  ARG A 208     -40.499  72.196   3.132  1.00 16.19           C  
ANISOU 1289  CB  ARG A 208      852   2799   2502    105    507    318       C  
ATOM   1290  CG  ARG A 208     -40.654  73.698   3.023  1.00 37.32           C  
ANISOU 1290  CG  ARG A 208     3513   5491   5177    173    500    328       C  
ATOM   1291  CD  ARG A 208     -41.933  74.174   3.673  1.00 31.27           C  
ANISOU 1291  CD  ARG A 208     2686   4739   4456    190    570    325       C  
ATOM   1292  NE  ARG A 208     -43.043  74.266   2.728  1.00 62.13           N  
ANISOU 1292  NE  ARG A 208     6475   8709   8423    203    543    309       N  
ATOM   1293  CZ  ARG A 208     -43.580  75.411   2.324  1.00 61.63           C  
ANISOU 1293  CZ  ARG A 208     6364   8680   8374    271    532    316       C  
ATOM   1294  NH1 ARG A 208     -43.113  76.563   2.785  1.00 44.52           N1+
ANISOU 1294  NH1 ARG A 208     4261   6480   6174    323    555    339       N1+
ATOM   1295  NH2 ARG A 208     -44.588  75.404   1.464  1.00 69.13           N  
ANISOU 1295  NH2 ARG A 208     7201   9697   9369    291    501    296       N  
ATOM   1296  N   ARG A 209     -38.720  70.094   5.089  1.00 30.85           N  
ANISOU 1296  N   ARG A 209     2925   4550   4245     45    585    340       N  
ATOM   1297  CA  ARG A 209     -38.394  68.775   5.613  1.00 50.01           C  
ANISOU 1297  CA  ARG A 209     5416   6939   6648     10    627    350       C  
ATOM   1298  C   ARG A 209     -38.901  68.574   7.040  1.00 45.72           C  
ANISOU 1298  C   ARG A 209     4919   6361   6090     19    736    366       C  
ATOM   1299  O   ARG A 209     -39.266  69.530   7.719  1.00 46.92           O  
ANISOU 1299  O   ARG A 209     5070   6521   6238     57    769    368       O  
ATOM   1300  CB  ARG A 209     -36.880  68.592   5.602  1.00 22.42           C  
ANISOU 1300  CB  ARG A 209     2013   3432   3073     31    571    357       C  
ATOM   1301  CG  ARG A 209     -36.152  69.633   6.424  1.00 31.64           C  
ANISOU 1301  CG  ARG A 209     3242   4601   4180     88    566    356       C  
ATOM   1302  CD  ARG A 209     -34.726  69.223   6.674  1.00 23.33           C  
ANISOU 1302  CD  ARG A 209     2279   3538   3047    108    528    355       C  
ATOM   1303  NE  ARG A 209     -34.456  69.065   8.096  1.00 63.30           N  
ANISOU 1303  NE  ARG A 209     7426   8586   8041    146    587    362       N  
ATOM   1304  CZ  ARG A 209     -34.124  70.068   8.900  1.00 62.60           C  
ANISOU 1304  CZ  ARG A 209     7367   8508   7911    194    591    344       C  
ATOM   1305  NH1 ARG A 209     -34.031  71.291   8.412  1.00 29.00           N1+
ANISOU 1305  NH1 ARG A 209     3065   4270   3683    203    550    320       N1+
ATOM   1306  NH2 ARG A 209     -33.890  69.849  10.187  1.00 73.08           N  
ANISOU 1306  NH2 ARG A 209     8773   9829   9167    237    642    347       N  
ATOM   1307  N   GLU A 210     -38.922  67.319   7.482  1.00 60.54           N  
ANISOU 1307  N   GLU A 210     6844   8198   7961    -13    799    378       N  
ATOM   1308  CA  GLU A 210     -39.206  66.999   8.874  1.00 38.04           C  
ANISOU 1308  CA  GLU A 210     4066   5308   5080      7    910    402       C  
ATOM   1309  C   GLU A 210     -37.965  67.277   9.706  1.00 60.96           C  
ANISOU 1309  C   GLU A 210     7086   8207   7871     73    888    417       C  
ATOM   1310  O   GLU A 210     -36.861  67.366   9.170  1.00 69.16           O  
ANISOU 1310  O   GLU A 210     8150   9263   8864     87    799    409       O  
ATOM   1311  CB  GLU A 210     -39.617  65.531   9.034  1.00 56.54           C  
ANISOU 1311  CB  GLU A 210     6430   7599   7453    -45    997    413       C  
ATOM   1312  CG  GLU A 210     -41.098  65.264   8.829  1.00 43.39           C  
ANISOU 1312  CG  GLU A 210     4659   5928   5900   -106   1072    391       C  
ATOM   1313  CD  GLU A 210     -41.452  63.795   8.920  1.00 81.29           C  
ANISOU 1313  CD  GLU A 210     9478  10666  10741   -167   1167    393       C  
ATOM   1314  OE1 GLU A 210     -41.142  63.185   9.964  1.00108.97           O  
ANISOU 1314  OE1 GLU A 210    13099  14115  14190   -140   1259    432       O  
ATOM   1315  OE2 GLU A 210     -42.047  63.258   7.962  1.00 72.14           O1-
ANISOU 1315  OE2 GLU A 210     8224   9517   9670   -237   1156    353       O1-
ATOM   1316  N   PRO A 211     -38.145  67.426  11.023  1.00 51.57           N  
ANISOU 1316  N   PRO A 211     5962   6998   6633    117    970    434       N  
ATOM   1317  CA  PRO A 211     -37.023  67.693  11.924  1.00 47.08           C  
ANISOU 1317  CA  PRO A 211     5500   6437   5951    189    951    438       C  
ATOM   1318  C   PRO A 211     -36.090  66.492  12.074  1.00 54.64           C  
ANISOU 1318  C   PRO A 211     6551   7371   6838    204    950    459       C  
ATOM   1319  O   PRO A 211     -34.956  66.653  12.521  1.00 57.24           O  
ANISOU 1319  O   PRO A 211     6954   7723   7072    264    902    451       O  
ATOM   1320  CB  PRO A 211     -37.715  67.995  13.256  1.00 38.80           C  
ANISOU 1320  CB  PRO A 211     4492   5372   4879    230   1056    453       C  
ATOM   1321  CG  PRO A 211     -39.104  68.408  12.882  1.00 34.86           C  
ANISOU 1321  CG  PRO A 211     3884   4871   4490    182   1099    447       C  
ATOM   1322  CD  PRO A 211     -39.442  67.566  11.704  1.00 56.11           C  
ANISOU 1322  CD  PRO A 211     6503   7554   7261    108   1078    442       C  
ATOM   1323  N   ARG A 212     -36.559  65.307  11.701  1.00 51.33           N  
ANISOU 1323  N   ARG A 212     6126   6910   6466    152   1004    480       N  
ATOM   1324  CA  ARG A 212     -35.757  64.093  11.841  1.00 52.58           C  
ANISOU 1324  CA  ARG A 212     6379   7037   6562    168   1019    506       C  
ATOM   1325  C   ARG A 212     -34.808  63.913  10.659  1.00 68.95           C  
ANISOU 1325  C   ARG A 212     8429   9135   8635    145    902    486       C  
ATOM   1326  O   ARG A 212     -33.967  63.013  10.659  1.00 72.45           O  
ANISOU 1326  O   ARG A 212     8946   9560   9020    165    894    504       O  
ATOM   1327  CB  ARG A 212     -36.654  62.866  11.981  1.00 53.83           C  
ANISOU 1327  CB  ARG A 212     6549   7127   6776    120   1144    534       C  
ATOM   1328  CG  ARG A 212     -37.402  62.492  10.712  1.00 52.17           C  
ANISOU 1328  CG  ARG A 212     6223   6909   6689     20   1129    507       C  
ATOM   1329  CD  ARG A 212     -38.536  61.522  10.997  1.00 65.80           C  
ANISOU 1329  CD  ARG A 212     7940   8569   8493    -37   1272    518       C  
ATOM   1330  NE  ARG A 212     -39.332  61.247   9.806  1.00 74.59           N  
ANISOU 1330  NE  ARG A 212     8924   9688   9728   -133   1253    474       N  
ATOM   1331  CZ  ARG A 212     -39.328  60.089   9.155  1.00 65.44           C  
ANISOU 1331  CZ  ARG A 212     7761   8489   8614   -194   1276    464       C  
ATOM   1332  NH1 ARG A 212     -38.574  59.087   9.583  1.00 69.36           N1+
ANISOU 1332  NH1 ARG A 212     8381   8929   9044   -168   1327    503       N1+
ATOM   1333  NH2 ARG A 212     -40.086  59.929   8.076  1.00 62.51           N  
ANISOU 1333  NH2 ARG A 212     7263   8137   8352   -278   1250    412       N  
ATOM   1334  N   HIS A 213     -34.953  64.767   9.650  1.00 59.88           N  
ANISOU 1334  N   HIS A 213     7179   8025   7548    109    818    454       N  
ATOM   1335  CA  HIS A 213     -34.102  64.705   8.472  1.00 32.96           C  
ANISOU 1335  CA  HIS A 213     3744   4639   4142     88    710    436       C  
ATOM   1336  C   HIS A 213     -33.195  65.918   8.384  1.00 59.28           C  
ANISOU 1336  C   HIS A 213     7073   8018   7432    133    619    408       C  
ATOM   1337  O   HIS A 213     -33.287  66.843   9.189  1.00 59.73           O  
ANISOU 1337  O   HIS A 213     7140   8091   7462    174    636    398       O  
ATOM   1338  CB  HIS A 213     -34.936  64.649   7.192  1.00 38.08           C  
ANISOU 1338  CB  HIS A 213     4279   5293   4895     15    684    417       C  
ATOM   1339  CG  HIS A 213     -35.826  63.451   7.092  1.00 51.52           C  
ANISOU 1339  CG  HIS A 213     5964   6951   6659    -45    769    425       C  
ATOM   1340  CD2 HIS A 213     -35.564  62.130   7.228  1.00 42.61           C  
ANISOU 1340  CD2 HIS A 213     4903   5773   5515    -63    822    445       C  
ATOM   1341  ND1 HIS A 213     -37.172  63.548   6.805  1.00 59.12           N  
ANISOU 1341  ND1 HIS A 213     6828   7916   7720    -97    814    406       N  
ATOM   1342  CE1 HIS A 213     -37.699  62.338   6.771  1.00 64.14           C  
ANISOU 1342  CE1 HIS A 213     7464   8504   8402   -152    893    407       C  
ATOM   1343  NE2 HIS A 213     -36.746  61.460   7.023  1.00 63.46           N  
ANISOU 1343  NE2 HIS A 213     7483   8381   8249   -133    904    434       N  
ATOM   1344  N   LEU A 214     -32.320  65.907   7.386  1.00 62.18           N  
ANISOU 1344  N   LEU A 214     7426   8403   7796    121    528    393       N  
ATOM   1345  CA  LEU A 214     -31.540  67.084   7.047  1.00 73.31           C  
ANISOU 1345  CA  LEU A 214     8816   9850   9191    146    448    361       C  
ATOM   1346  C   LEU A 214     -31.424  67.176   5.536  1.00 67.59           C  
ANISOU 1346  C   LEU A 214     8024   9135   8522    104    376    351       C  
ATOM   1347  O   LEU A 214     -31.266  66.165   4.853  1.00 69.80           O  
ANISOU 1347  O   LEU A 214     8307   9402   8813     71    359    362       O  
ATOM   1348  CB  LEU A 214     -30.154  67.037   7.693  1.00 31.79           C  
ANISOU 1348  CB  LEU A 214     3637   4606   3834    202    413    344       C  
ATOM   1349  CG  LEU A 214     -29.074  66.195   7.021  1.00 47.47           C  
ANISOU 1349  CG  LEU A 214     5655   6594   5790    198    354    345       C  
ATOM   1350  CD1 LEU A 214     -27.713  66.562   7.574  1.00 46.78           C  
ANISOU 1350  CD1 LEU A 214     5616   6539   5618    257    304    310       C  
ATOM   1351  CD2 LEU A 214     -29.353  64.720   7.204  1.00 77.13           C  
ANISOU 1351  CD2 LEU A 214     9462  10313   9532    186    411    385       C  
ATOM   1352  N   ALA A 215     -31.525  68.390   5.015  1.00 42.15           N  
ANISOU 1352  N   ALA A 215     4746   5933   5335    109    339    332       N  
ATOM   1353  CA  ALA A 215     -31.336  68.605   3.590  1.00 44.06           C  
ANISOU 1353  CA  ALA A 215     4935   6188   5619     86    271    325       C  
ATOM   1354  C   ALA A 215     -29.946  69.162   3.334  1.00 49.11           C  
ANISOU 1354  C   ALA A 215     5607   6836   6218    111    210    302       C  
ATOM   1355  O   ALA A 215     -29.489  70.059   4.046  1.00 32.76           O  
ANISOU 1355  O   ALA A 215     3559   4770   4120    145    217    278       O  
ATOM   1356  CB  ALA A 215     -32.393  69.563   3.052  1.00 39.54           C  
ANISOU 1356  CB  ALA A 215     4281   5631   5112     84    276    325       C  
ATOM   1357  N   ILE A 216     -29.263  68.610   2.337  1.00 21.25           N  
ANISOU 1357  N   ILE A 216     2079   3306   2687     93    155    303       N  
ATOM   1358  CA  ILE A 216     -28.056  69.244   1.821  1.00 35.15           C  
ANISOU 1358  CA  ILE A 216     3852   5073   4431    109    100    278       C  
ATOM   1359  C   ILE A 216     -28.248  69.510   0.337  1.00 37.53           C  
ANISOU 1359  C   ILE A 216     4101   5377   4782     91     59    287       C  
ATOM   1360  O   ILE A 216     -29.092  68.884  -0.293  1.00 26.36           O  
ANISOU 1360  O   ILE A 216     2648   3967   3399     65     57    306       O  
ATOM   1361  CB  ILE A 216     -26.773  68.429   2.098  1.00 25.04           C  
ANISOU 1361  CB  ILE A 216     2633   3793   3087    119     70    266       C  
ATOM   1362  CG1 ILE A 216     -26.797  67.076   1.389  1.00 53.34           C  
ANISOU 1362  CG1 ILE A 216     6227   7368   6673     88     53    293       C  
ATOM   1363  CG2 ILE A 216     -26.578  68.237   3.600  1.00 31.39           C  
ANISOU 1363  CG2 ILE A 216     3494   4604   3828    155    109    256       C  
ATOM   1364  CD1 ILE A 216     -25.651  66.151   1.820  1.00 17.68           C  
ANISOU 1364  CD1 ILE A 216     1780   2851   2088    109     36    289       C  
ATOM   1365  N   SER A 217     -27.499  70.466  -0.205  1.00 29.93           N  
ANISOU 1365  N   SER A 217     3135   4411   3825    108     31    269       N  
ATOM   1366  CA  SER A 217     -27.637  70.826  -1.611  1.00 19.41           C  
ANISOU 1366  CA  SER A 217     1765   3081   2530    107     -2    281       C  
ATOM   1367  C   SER A 217     -26.305  71.304  -2.172  1.00 17.82           C  
ANISOU 1367  C   SER A 217     1589   2865   2318    117    -32    261       C  
ATOM   1368  O   SER A 217     -25.255  71.066  -1.578  1.00 27.67           O  
ANISOU 1368  O   SER A 217     2876   4109   3528    116    -41    233       O  
ATOM   1369  CB  SER A 217     -28.718  71.897  -1.782  1.00 33.23           C  
ANISOU 1369  CB  SER A 217     3466   4836   4323    130     28    293       C  
ATOM   1370  OG  SER A 217     -29.170  71.973  -3.124  1.00 32.40           O  
ANISOU 1370  OG  SER A 217     3320   4746   4246    139     -3    313       O  
ATOM   1371  N   ASN A 218     -26.349  71.973  -3.319  1.00 36.90           N  
ANISOU 1371  N   ASN A 218     3983   5275   4764    131    -45    273       N  
ATOM   1372  CA  ASN A 218     -25.143  72.523  -3.935  1.00 26.57           C  
ANISOU 1372  CA  ASN A 218     2697   3943   3456    140    -59    255       C  
ATOM   1373  C   ASN A 218     -24.436  73.498  -3.010  1.00 37.34           C  
ANISOU 1373  C   ASN A 218     4080   5286   4820    148    -23    210       C  
ATOM   1374  O   ASN A 218     -23.238  73.374  -2.750  1.00 15.53           O  
ANISOU 1374  O   ASN A 218     1343   2519   2038    139    -37    171       O  
ATOM   1375  CB  ASN A 218     -25.485  73.236  -5.241  1.00 15.64           C  
ANISOU 1375  CB  ASN A 218     1291   2549   2102    167    -60    282       C  
ATOM   1376  CG  ASN A 218     -26.109  72.309  -6.262  1.00 44.93           C  
ANISOU 1376  CG  ASN A 218     4977   6289   5808    163   -105    313       C  
ATOM   1377  ND2 ASN A 218     -25.267  71.596  -6.997  1.00 38.70           N  
ANISOU 1377  ND2 ASN A 218     4209   5495   4999    148   -145    312       N  
ATOM   1378  OD1 ASN A 218     -27.334  72.235  -6.391  1.00 33.02           O  
ANISOU 1378  OD1 ASN A 218     3425   4808   4314    173   -104    331       O  
ATOM   1379  N   MET A 219     -25.186  74.475  -2.513  1.00 47.72           N  
ANISOU 1379  N   MET A 219     5379   6593   6160    167     25    209       N  
ATOM   1380  CA  MET A 219     -24.611  75.549  -1.716  1.00 43.47           C  
ANISOU 1380  CA  MET A 219     4854   6031   5631    175     67    160       C  
ATOM   1381  C   MET A 219     -24.818  75.321  -0.227  1.00 31.45           C  
ANISOU 1381  C   MET A 219     3343   4532   4076    173     82    132       C  
ATOM   1382  O   MET A 219     -25.620  74.478   0.169  1.00 62.37           O  
ANISOU 1382  O   MET A 219     7255   8471   7971    170     76    163       O  
ATOM   1383  CB  MET A 219     -25.206  76.895  -2.145  1.00 34.76           C  
ANISOU 1383  CB  MET A 219     3736   4896   4576    204    120    175       C  
ATOM   1384  CG  MET A 219     -24.914  77.259  -3.591  1.00 36.25           C  
ANISOU 1384  CG  MET A 219     3927   5057   4790    220    117    203       C  
ATOM   1385  SD  MET A 219     -23.162  77.511  -3.928  1.00 48.84           S  
ANISOU 1385  SD  MET A 219     5551   6613   6393    197    119    149       S  
ATOM   1386  CE  MET A 219     -23.066  79.299  -3.945  1.00 69.91           C  
ANISOU 1386  CE  MET A 219     8229   9214   9120    219    214    125       C  
ATOM   1387  N   PRO A 220     -24.083  76.071   0.608  1.00 37.48           N  
ANISOU 1387  N   PRO A 220     4120   5286   4835    176    105     70       N  
ATOM   1388  CA  PRO A 220     -24.208  75.993   2.066  1.00 30.04           C  
ANISOU 1388  CA  PRO A 220     3192   4369   3853    186    121     36       C  
ATOM   1389  C   PRO A 220     -25.595  76.403   2.554  1.00 39.39           C  
ANISOU 1389  C   PRO A 220     4363   5550   5054    202    169     70       C  
ATOM   1390  O   PRO A 220     -26.287  77.184   1.900  1.00 25.20           O  
ANISOU 1390  O   PRO A 220     2541   3728   3307    210    199     99       O  
ATOM   1391  CB  PRO A 220     -23.168  77.004   2.554  1.00  9.94           C  
ANISOU 1391  CB  PRO A 220      650   1810   1317    186    139    -49       C  
ATOM   1392  CG  PRO A 220     -22.185  77.094   1.464  1.00 16.83           C  
ANISOU 1392  CG  PRO A 220     1517   2660   2218    168    118    -63       C  
ATOM   1393  CD  PRO A 220     -22.991  76.974   0.208  1.00 41.15           C  
ANISOU 1393  CD  PRO A 220     4586   5719   5332    169    119     18       C  
ATOM   1394  N   LEU A 221     -25.996  75.865   3.698  1.00 29.23           N  
ANISOU 1394  N   LEU A 221     3094   4290   3723    212    180     69       N  
ATOM   1395  CA  LEU A 221     -27.272  76.223   4.297  1.00 50.83           C  
ANISOU 1395  CA  LEU A 221     5816   7024   6473    226    231     95       C  
ATOM   1396  C   LEU A 221     -27.176  77.608   4.931  1.00 53.02           C  
ANISOU 1396  C   LEU A 221     6095   7282   6770    243    278     45       C  
ATOM   1397  O   LEU A 221     -26.262  77.891   5.705  1.00 50.58           O  
ANISOU 1397  O   LEU A 221     5807   6982   6428    248    274    -23       O  
ATOM   1398  CB  LEU A 221     -27.681  75.183   5.342  1.00 37.80           C  
ANISOU 1398  CB  LEU A 221     4194   5400   4768    234    240    111       C  
ATOM   1399  CG  LEU A 221     -29.069  75.312   5.973  1.00 43.14           C  
ANISOU 1399  CG  LEU A 221     4856   6075   5459    244    299    144       C  
ATOM   1400  CD1 LEU A 221     -30.147  75.101   4.927  1.00 85.27           C  
ANISOU 1400  CD1 LEU A 221    10140  11405  10854    227    301    198       C  
ATOM   1401  CD2 LEU A 221     -29.226  74.324   7.110  1.00 20.68           C  
ANISOU 1401  CD2 LEU A 221     2057   3249   2554    258    319    152       C  
ATOM   1402  N   VAL A 222     -28.118  78.474   4.588  1.00 51.43           N  
ANISOU 1402  N   VAL A 222     5865   7056   6619    254    323     73       N  
ATOM   1403  CA  VAL A 222     -28.109  79.842   5.079  1.00 44.65           C  
ANISOU 1403  CA  VAL A 222     5009   6169   5789    270    378     30       C  
ATOM   1404  C   VAL A 222     -28.914  79.954   6.364  1.00 49.12           C  
ANISOU 1404  C   VAL A 222     5584   6750   6330    289    422     25       C  
ATOM   1405  O   VAL A 222     -28.423  80.458   7.374  1.00 47.30           O  
ANISOU 1405  O   VAL A 222     5377   6522   6073    297    442    -40       O  
ATOM   1406  CB  VAL A 222     -28.689  80.805   4.036  1.00 48.56           C  
ANISOU 1406  CB  VAL A 222     5478   6624   6349    285    414     67       C  
ATOM   1407  CG1 VAL A 222     -28.905  82.179   4.645  1.00 69.20           C  
ANISOU 1407  CG1 VAL A 222     8099   9202   8993    305    487     31       C  
ATOM   1408  CG2 VAL A 222     -27.775  80.879   2.828  1.00 45.50           C  
ANISOU 1408  CG2 VAL A 222     5093   6213   5983    272    386     65       C  
ATOM   1409  N   LYS A 223     -30.153  79.481   6.318  1.00 38.64           N  
ANISOU 1409  N   LYS A 223     4235   5435   5012    297    437     87       N  
ATOM   1410  CA  LYS A 223     -31.005  79.481   7.496  1.00 63.33           C  
ANISOU 1410  CA  LYS A 223     7370   8573   8117    315    485     91       C  
ATOM   1411  C   LYS A 223     -32.017  78.349   7.448  1.00 70.75           C  
ANISOU 1411  C   LYS A 223     8291   9536   9055    306    486    152       C  
ATOM   1412  O   LYS A 223     -32.473  77.949   6.376  1.00 69.77           O  
ANISOU 1412  O   LYS A 223     8127   9416   8968    292    461    194       O  
ATOM   1413  CB  LYS A 223     -31.749  80.806   7.623  1.00 43.58           C  
ANISOU 1413  CB  LYS A 223     4850   6045   5664    339    549     89       C  
ATOM   1414  CG  LYS A 223     -32.577  81.143   6.401  1.00 66.77           C  
ANISOU 1414  CG  LYS A 223     7738   8969   8661    349    554    146       C  
ATOM   1415  CD  LYS A 223     -33.614  82.204   6.701  1.00 60.79           C  
ANISOU 1415  CD  LYS A 223     6962   8194   7942    385    624    159       C  
ATOM   1416  CE  LYS A 223     -34.342  82.608   5.435  1.00 67.51           C  
ANISOU 1416  CE  LYS A 223     7767   9041   8844    412    624    212       C  
ATOM   1417  NZ  LYS A 223     -35.701  83.126   5.741  1.00 65.70           N1+
ANISOU 1417  NZ  LYS A 223     7501   8818   8644    449    679    242       N1+
ATOM   1418  N   SER A 224     -32.355  77.833   8.624  1.00 50.28           N  
ANISOU 1418  N   SER A 224     5728   6957   6419    317    518    151       N  
ATOM   1419  CA  SER A 224     -33.464  76.903   8.769  1.00 46.21           C  
ANISOU 1419  CA  SER A 224     5194   6451   5912    307    547    202       C  
ATOM   1420  C   SER A 224     -34.595  77.640   9.463  1.00 44.75           C  
ANISOU 1420  C   SER A 224     4990   6259   5754    330    620    210       C  
ATOM   1421  O   SER A 224     -34.383  78.321  10.467  1.00 66.90           O  
ANISOU 1421  O   SER A 224     7832   9060   8527    357    654    175       O  
ATOM   1422  CB  SER A 224     -33.049  75.676   9.584  1.00 56.67           C  
ANISOU 1422  CB  SER A 224     6576   7788   7167    307    547    204       C  
ATOM   1423  OG  SER A 224     -32.122  74.870   8.876  1.00 54.48           O  
ANISOU 1423  OG  SER A 224     6313   7517   6869    286    482    204       O  
ATOM   1424  N   VAL A 225     -35.799  77.516   8.923  1.00 53.06           N  
ANISOU 1424  N   VAL A 225     5980   7316   6865    320    643    251       N  
ATOM   1425  CA  VAL A 225     -36.944  78.214   9.477  1.00 45.38           C  
ANISOU 1425  CA  VAL A 225     4978   6339   5925    344    712    261       C  
ATOM   1426  C   VAL A 225     -38.091  77.258   9.752  1.00 42.70           C  
ANISOU 1426  C   VAL A 225     4605   6010   5608    325    757    295       C  
ATOM   1427  O   VAL A 225     -38.650  76.680   8.826  1.00 61.01           O  
ANISOU 1427  O   VAL A 225     6862   8344   7974    298    734    316       O  
ATOM   1428  CB  VAL A 225     -37.454  79.291   8.510  1.00 67.10           C  
ANISOU 1428  CB  VAL A 225     7669   9088   8738    364    708    271       C  
ATOM   1429  CG1 VAL A 225     -38.684  79.972   9.081  1.00 46.86           C  
ANISOU 1429  CG1 VAL A 225     5072   6524   6209    394    781    284       C  
ATOM   1430  CG2 VAL A 225     -36.360  80.302   8.217  1.00 56.68           C  
ANISOU 1430  CG2 VAL A 225     6383   7744   7408    380    684    237       C  
ATOM   1431  N   THR A 226     -38.439  77.094  11.024  1.00 54.73           N  
ANISOU 1431  N   THR A 226     6170   7525   7100    338    825    295       N  
ATOM   1432  CA  THR A 226     -39.643  76.359  11.380  1.00 58.93           C  
ANISOU 1432  CA  THR A 226     6667   8056   7665    321    892    324       C  
ATOM   1433  C   THR A 226     -40.823  77.033  10.684  1.00 47.67           C  
ANISOU 1433  C   THR A 226     5143   6647   6324    325    906    334       C  
ATOM   1434  O   THR A 226     -41.099  78.208  10.913  1.00 55.59           O  
ANISOU 1434  O   THR A 226     6136   7647   7338    363    930    327       O  
ATOM   1435  CB  THR A 226     -39.865  76.360  12.897  1.00 61.39           C  
ANISOU 1435  CB  THR A 226     7045   8353   7929    350    976    323       C  
ATOM   1436  CG2 THR A 226     -38.728  75.649  13.597  1.00 50.04           C  
ANISOU 1436  CG2 THR A 226     5706   6910   6397    362    959    313       C  
ATOM   1437  OG1 THR A 226     -39.911  77.713  13.362  1.00 98.62           O  
ANISOU 1437  OG1 THR A 226    11766  13066  12640    391    996    300       O  
ATOM   1438  N   VAL A 227     -41.504  76.290   9.821  1.00 47.65           N  
ANISOU 1438  N   VAL A 227     5064   6664   6377    289    890    347       N  
ATOM   1439  CA  VAL A 227     -42.509  76.872   8.942  1.00 50.71           C  
ANISOU 1439  CA  VAL A 227     5347   7082   6836    301    879    351       C  
ATOM   1440  C   VAL A 227     -43.911  76.501   9.394  1.00 67.04           C  
ANISOU 1440  C   VAL A 227     7348   9161   8962    286    958    355       C  
ATOM   1441  O   VAL A 227     -44.876  77.232   9.166  1.00 49.70           O  
ANISOU 1441  O   VAL A 227     5076   6991   6817    315    977    355       O  
ATOM   1442  CB  VAL A 227     -42.291  76.403   7.494  1.00 54.17           C  
ANISOU 1442  CB  VAL A 227     5733   7550   7299    278    793    349       C  
ATOM   1443  CG1 VAL A 227     -43.393  76.915   6.591  1.00 76.25           C  
ANISOU 1443  CG1 VAL A 227     8417  10392  10161    303    779    349       C  
ATOM   1444  CG2 VAL A 227     -40.947  76.888   7.006  1.00 83.99           C  
ANISOU 1444  CG2 VAL A 227     9572  11314  11028    296    725    345       C  
ATOM   1445  N   ALA A 228     -44.010  75.348  10.036  1.00 83.44           N  
ANISOU 1445  N   ALA A 228     9455  11216  11032    243   1008    359       N  
ATOM   1446  CA  ALA A 228     -45.263  74.882  10.595  1.00 44.40           C  
ANISOU 1446  CA  ALA A 228     4458   6269   6145    220   1102    360       C  
ATOM   1447  C   ALA A 228     -44.899  73.875  11.658  1.00 65.85           C  
ANISOU 1447  C   ALA A 228     7269   8938   8814    197   1172    374       C  
ATOM   1448  O   ALA A 228     -43.735  73.782  12.053  1.00 80.10           O  
ANISOU 1448  O   ALA A 228     9178  10722  10535    215   1143    381       O  
ATOM   1449  CB  ALA A 228     -46.124  74.246   9.522  1.00 31.72           C  
ANISOU 1449  CB  ALA A 228     2728   4701   4622    175   1077    341       C  
ATOM   1450  N   GLU A 229     -45.883  73.110  12.115  1.00 62.98           N  
ANISOU 1450  N   GLU A 229     6872   8557   8503    160   1267    376       N  
ATOM   1451  CA  GLU A 229     -45.647  72.164  13.196  1.00 66.14           C  
ANISOU 1451  CA  GLU A 229     7372   8903   8856    149   1356    398       C  
ATOM   1452  C   GLU A 229     -44.433  71.273  12.969  1.00 68.57           C  
ANISOU 1452  C   GLU A 229     7763   9191   9098    135   1303    407       C  
ATOM   1453  O   GLU A 229     -43.370  71.505  13.548  1.00 83.33           O  
ANISOU 1453  O   GLU A 229     9739  11052  10871    181   1277    417       O  
ATOM   1454  CB  GLU A 229     -46.897  71.328  13.476  1.00 91.79           C  
ANISOU 1454  CB  GLU A 229    10559  12127  12189     97   1471    395       C  
ATOM   1455  CG  GLU A 229     -47.774  71.938  14.546  1.00 94.83           C  
ANISOU 1455  CG  GLU A 229    10944  12499  12589    130   1578    405       C  
ATOM   1456  CD  GLU A 229     -46.960  72.483  15.708  1.00118.79           C  
ANISOU 1456  CD  GLU A 229    14116  15511  15509    201   1597    430       C  
ATOM   1457  OE1 GLU A 229     -45.853  71.964  15.962  1.00147.01           O  
ANISOU 1457  OE1 GLU A 229    17796  19064  18995    216   1568    445       O  
ATOM   1458  OE2 GLU A 229     -47.428  73.433  16.370  1.00120.06           O1-
ANISOU 1458  OE2 GLU A 229    14275  15677  15665    246   1640    432       O1-
ATOM   1459  N   GLY A 230     -44.588  70.255  12.133  1.00 47.26           N  
ANISOU 1459  N   GLY A 230     5015   6489   6452     73   1288    397       N  
ATOM   1460  CA  GLY A 230     -43.493  69.337  11.871  1.00 81.50           C  
ANISOU 1460  CA  GLY A 230     9429  10805  10733     58   1244    407       C  
ATOM   1461  C   GLY A 230     -42.697  69.696  10.631  1.00 74.59           C  
ANISOU 1461  C   GLY A 230     8521   9971   9848     57   1106    389       C  
ATOM   1462  O   GLY A 230     -42.100  68.822  10.009  1.00 71.48           O  
ANISOU 1462  O   GLY A 230     8145   9569   9446     24   1064    388       O  
ATOM   1463  N   LEU A 231     -42.682  70.980  10.277  1.00 40.34           N  
ANISOU 1463  N   LEU A 231     4141   5673   5513     96   1045    378       N  
ATOM   1464  CA  LEU A 231     -42.054  71.432   9.037  1.00 45.09           C  
ANISOU 1464  CA  LEU A 231     4706   6312   6115    100    927    363       C  
ATOM   1465  C   LEU A 231     -40.973  72.490   9.230  1.00 69.13           C  
ANISOU 1465  C   LEU A 231     7817   9361   9089    156    871    364       C  
ATOM   1466  O   LEU A 231     -41.182  73.499   9.908  1.00 74.59           O  
ANISOU 1466  O   LEU A 231     8521  10052   9768    198    904    363       O  
ATOM   1467  CB  LEU A 231     -43.100  71.969   8.058  1.00 26.19           C  
ANISOU 1467  CB  LEU A 231     2180   3965   3806     93    898    344       C  
ATOM   1468  CG  LEU A 231     -43.851  70.955   7.196  1.00 68.97           C  
ANISOU 1468  CG  LEU A 231     7504   9403   9299     30    894    320       C  
ATOM   1469  CD1 LEU A 231     -44.703  70.022   8.047  1.00114.22           C  
ANISOU 1469  CD1 LEU A 231    13229  15097  15075    -17   1012    317       C  
ATOM   1470  CD2 LEU A 231     -44.708  71.689   6.186  1.00 67.67           C  
ANISOU 1470  CD2 LEU A 231     7213   9303   9197     49    842    296       C  
ATOM   1471  N   ILE A 232     -39.820  72.253   8.608  1.00 53.18           N  
ANISOU 1471  N   ILE A 232     5836   7343   7027    152    791    360       N  
ATOM   1472  CA  ILE A 232     -38.734  73.224   8.578  1.00 43.69           C  
ANISOU 1472  CA  ILE A 232     4683   6146   5773    194    733    348       C  
ATOM   1473  C   ILE A 232     -38.374  73.548   7.136  1.00 37.54           C  
ANISOU 1473  C   ILE A 232     3853   5390   5022    187    645    340       C  
ATOM   1474  O   ILE A 232     -38.297  72.661   6.293  1.00 35.58           O  
ANISOU 1474  O   ILE A 232     3579   5149   4791    151    605    343       O  
ATOM   1475  CB  ILE A 232     -37.476  72.702   9.293  1.00 42.08           C  
ANISOU 1475  CB  ILE A 232     4585   5924   5481    207    722    344       C  
ATOM   1476  CG1 ILE A 232     -37.823  72.206  10.698  1.00 45.39           C  
ANISOU 1476  CG1 ILE A 232     5066   6321   5859    223    814    358       C  
ATOM   1477  CG2 ILE A 232     -36.416  73.789   9.366  1.00 32.73           C  
ANISOU 1477  CG2 ILE A 232     3437   4746   4252    245    672    315       C  
ATOM   1478  CD1 ILE A 232     -36.619  71.810  11.512  1.00 57.58           C  
ANISOU 1478  CD1 ILE A 232     6717   7858   7302    259    803    352       C  
ATOM   1479  N   GLU A 233     -38.162  74.826   6.854  1.00 61.13           N  
ANISOU 1479  N   GLU A 233     6830   8383   8012    226    621    332       N  
ATOM   1480  CA  GLU A 233     -37.769  75.249   5.519  1.00 58.08           C  
ANISOU 1480  CA  GLU A 233     6410   8013   7646    233    548    330       C  
ATOM   1481  C   GLU A 233     -36.297  75.608   5.506  1.00 56.06           C  
ANISOU 1481  C   GLU A 233     6225   7737   7337    244    506    312       C  
ATOM   1482  O   GLU A 233     -35.885  76.599   6.107  1.00 63.38           O  
ANISOU 1482  O   GLU A 233     7189   8648   8246    274    528    294       O  
ATOM   1483  CB  GLU A 233     -38.599  76.446   5.069  1.00 46.93           C  
ANISOU 1483  CB  GLU A 233     4935   6616   6279    275    560    336       C  
ATOM   1484  CG  GLU A 233     -38.388  76.859   3.632  1.00 55.79           C  
ANISOU 1484  CG  GLU A 233     6022   7757   7419    296    495    343       C  
ATOM   1485  CD  GLU A 233     -39.530  77.704   3.119  1.00 73.85           C  
ANISOU 1485  CD  GLU A 233     8233  10074   9753    344    510    356       C  
ATOM   1486  OE1 GLU A 233     -40.513  77.120   2.620  1.00 71.57           O  
ANISOU 1486  OE1 GLU A 233     7863   9829   9502    333    498    356       O  
ATOM   1487  OE2 GLU A 233     -39.457  78.949   3.224  1.00 66.87           O1-
ANISOU 1487  OE2 GLU A 233     7367   9170   8869    394    537    361       O1-
ATOM   1488  N   ASP A 234     -35.508  74.786   4.825  1.00 52.49           N  
ANISOU 1488  N   ASP A 234     5791   7288   6867    217    448    312       N  
ATOM   1489  CA  ASP A 234     -34.085  75.038   4.682  1.00 53.52           C  
ANISOU 1489  CA  ASP A 234     5976   7404   6954    223    404    290       C  
ATOM   1490  C   ASP A 234     -33.809  75.956   3.497  1.00 57.19           C  
ANISOU 1490  C   ASP A 234     6414   7867   7449    243    367    291       C  
ATOM   1491  O   ASP A 234     -34.268  75.697   2.382  1.00 35.88           O  
ANISOU 1491  O   ASP A 234     3665   5187   4781    239    334    311       O  
ATOM   1492  CB  ASP A 234     -33.315  73.721   4.546  1.00 55.96           C  
ANISOU 1492  CB  ASP A 234     6322   7714   7225    192    365    291       C  
ATOM   1493  CG  ASP A 234     -32.978  73.104   5.891  1.00 67.37           C  
ANISOU 1493  CG  ASP A 234     7834   9152   8612    197    402    284       C  
ATOM   1494  OD1 ASP A 234     -33.194  73.784   6.916  1.00 58.29           O  
ANISOU 1494  OD1 ASP A 234     6704   7998   7445    225    449    270       O  
ATOM   1495  OD2 ASP A 234     -32.494  71.950   5.929  1.00 55.54           O1-
ANISOU 1495  OD2 ASP A 234     6372   7651   7079    179    386    291       O1-
ATOM   1496  N   HIS A 235     -33.082  77.041   3.759  1.00 32.19           N  
ANISOU 1496  N   HIS A 235     3280   4676   4273    266    380    265       N  
ATOM   1497  CA  HIS A 235     -32.659  77.969   2.716  1.00 30.31           C  
ANISOU 1497  CA  HIS A 235     3034   4421   4061    288    362    265       C  
ATOM   1498  C   HIS A 235     -31.172  77.797   2.464  1.00 28.97           C  
ANISOU 1498  C   HIS A 235     2909   4235   3863    269    322    234       C  
ATOM   1499  O   HIS A 235     -30.355  77.975   3.364  1.00 40.07           O  
ANISOU 1499  O   HIS A 235     4356   5631   5239    264    333    190       O  
ATOM   1500  CB  HIS A 235     -32.930  79.417   3.126  1.00 26.17           C  
ANISOU 1500  CB  HIS A 235     2514   3869   3561    325    422    253       C  
ATOM   1501  CG  HIS A 235     -34.383  79.747   3.276  1.00 56.00           C  
ANISOU 1501  CG  HIS A 235     6243   7664   7372    354    464    283       C  
ATOM   1502  CD2 HIS A 235     -35.287  79.390   4.221  1.00 52.42           C  
ANISOU 1502  CD2 HIS A 235     5772   7228   6917    349    501    288       C  
ATOM   1503  ND1 HIS A 235     -35.060  80.548   2.382  1.00 73.83           N  
ANISOU 1503  ND1 HIS A 235     8462   9922   9667    399    475    313       N  
ATOM   1504  CE1 HIS A 235     -36.318  80.669   2.768  1.00 59.90           C  
ANISOU 1504  CE1 HIS A 235     6652   8181   7925    420    511    331       C  
ATOM   1505  NE2 HIS A 235     -36.481  79.974   3.880  1.00 52.63           N  
ANISOU 1505  NE2 HIS A 235     5743   7268   6986    385    530    315       N  
ATOM   1506  N   PHE A 236     -30.819  77.440   1.238  1.00 14.23           N  
ANISOU 1506  N   PHE A 236     1031   2371   2004    263    274    253       N  
ATOM   1507  CA  PHE A 236     -29.420  77.362   0.864  1.00 29.61           C  
ANISOU 1507  CA  PHE A 236     3015   4301   3934    247    241    224       C  
ATOM   1508  C   PHE A 236     -29.071  78.599   0.052  1.00 32.30           C  
ANISOU 1508  C   PHE A 236     3358   4604   4310    274    264    222       C  
ATOM   1509  O   PHE A 236     -29.941  79.213  -0.569  1.00 40.99           O  
ANISOU 1509  O   PHE A 236     4432   5702   5441    310    286    259       O  
ATOM   1510  CB  PHE A 236     -29.152  76.084   0.061  1.00 10.14           C  
ANISOU 1510  CB  PHE A 236      545   1857   1450    221    179    245       C  
ATOM   1511  CG  PHE A 236     -29.578  74.831   0.764  1.00 40.18           C  
ANISOU 1511  CG  PHE A 236     4352   5688   5227    196    171    254       C  
ATOM   1512  CD1 PHE A 236     -30.840  74.305   0.559  1.00 15.88           C  
ANISOU 1512  CD1 PHE A 236     1229   2633   2173    190    178    286       C  
ATOM   1513  CD2 PHE A 236     -28.721  74.187   1.640  1.00 38.79           C  
ANISOU 1513  CD2 PHE A 236     4223   5514   5002    183    162    227       C  
ATOM   1514  CE1 PHE A 236     -31.242  73.163   1.214  1.00 47.60           C  
ANISOU 1514  CE1 PHE A 236     5253   6662   6173    163    189    292       C  
ATOM   1515  CE2 PHE A 236     -29.118  73.039   2.295  1.00 37.90           C  
ANISOU 1515  CE2 PHE A 236     4124   5415   4860    168    170    242       C  
ATOM   1516  CZ  PHE A 236     -30.381  72.527   2.083  1.00 49.94           C  
ANISOU 1516  CZ  PHE A 236     5608   6950   6417    154    189    275       C  
ATOM   1517  N   ASP A 237     -27.801  78.974   0.070  1.00 13.76           N  
ANISOU 1517  N   ASP A 237     1042   2226   1959    260    265    177       N  
ATOM   1518  CA  ASP A 237     -27.358  80.163  -0.642  1.00 38.01           C  
ANISOU 1518  CA  ASP A 237     4125   5247   5070    281    305    170       C  
ATOM   1519  C   ASP A 237     -27.618  80.043  -2.149  1.00 51.87           C  
ANISOU 1519  C   ASP A 237     5869   7002   6839    307    282    228       C  
ATOM   1520  O   ASP A 237     -27.778  78.940  -2.685  1.00 33.99           O  
ANISOU 1520  O   ASP A 237     3588   4775   4550    295    221    255       O  
ATOM   1521  CB  ASP A 237     -25.875  80.422  -0.353  1.00 63.84           C  
ANISOU 1521  CB  ASP A 237     7424   8491   8341    250    309     99       C  
ATOM   1522  CG  ASP A 237     -25.370  81.714  -0.963  1.00113.25           C  
ANISOU 1522  CG  ASP A 237    13697  14682  14651    263    373     82       C  
ATOM   1523  OD1 ASP A 237     -26.181  82.487  -1.511  1.00118.07           O  
ANISOU 1523  OD1 ASP A 237    14305  15264  15290    306    420    130       O  
ATOM   1524  OD2 ASP A 237     -24.147  81.960  -0.890  1.00148.65           O1-
ANISOU 1524  OD2 ASP A 237    18195  19139  19147    234    381     18       O1-
ATOM   1525  N   VAL A 238     -27.687  81.196  -2.812  1.00 46.57           N  
ANISOU 1525  N   VAL A 238     5209   6284   6201    348    336    245       N  
ATOM   1526  CA  VAL A 238     -27.813  81.274  -4.262  1.00 37.11           C  
ANISOU 1526  CA  VAL A 238     4013   5081   5008    389    324    297       C  
ATOM   1527  C   VAL A 238     -26.574  80.678  -4.900  1.00 37.53           C  
ANISOU 1527  C   VAL A 238     4089   5122   5049    356    286    280       C  
ATOM   1528  O   VAL A 238     -25.458  80.932  -4.451  1.00 41.24           O  
ANISOU 1528  O   VAL A 238     4582   5556   5531    319    307    224       O  
ATOM   1529  CB  VAL A 238     -27.944  82.731  -4.729  1.00 32.16           C  
ANISOU 1529  CB  VAL A 238     3410   4391   4417    446    410    317       C  
ATOM   1530  CG1 VAL A 238     -28.552  82.779  -6.093  1.00 11.58           C  
ANISOU 1530  CG1 VAL A 238      799   1800   1799    516    395    386       C  
ATOM   1531  CG2 VAL A 238     -28.808  83.521  -3.766  1.00 51.76           C  
ANISOU 1531  CG2 VAL A 238     5881   6866   6918    467    467    311       C  
ATOM   1532  N   THR A 239     -26.770  79.877  -5.941  1.00 41.30           N  
ANISOU 1532  N   THR A 239     4555   5633   5503    369    228    321       N  
ATOM   1533  CA  THR A 239     -25.647  79.264  -6.637  1.00 28.43           C  
ANISOU 1533  CA  THR A 239     2948   3994   3861    342    190    311       C  
ATOM   1534  C   THR A 239     -25.014  80.293  -7.545  1.00 43.54           C  
ANISOU 1534  C   THR A 239     4900   5842   5802    378    251    322       C  
ATOM   1535  O   THR A 239     -25.534  81.394  -7.705  1.00 33.36           O  
ANISOU 1535  O   THR A 239     3622   4518   4536    429    318    346       O  
ATOM   1536  CB  THR A 239     -26.091  78.074  -7.508  1.00 38.06           C  
ANISOU 1536  CB  THR A 239     4146   5270   5047    346    112    348       C  
ATOM   1537  CG2 THR A 239     -26.698  76.984  -6.655  1.00 33.27           C  
ANISOU 1537  CG2 THR A 239     3505   4716   4419    306     67    337       C  
ATOM   1538  OG1 THR A 239     -27.062  78.513  -8.467  1.00 52.65           O  
ANISOU 1538  OG1 THR A 239     5977   7133   6893    416    117    400       O  
ATOM   1539  N   VAL A 240     -23.881  79.930  -8.127  1.00 35.11           N  
ANISOU 1539  N   VAL A 240     3855   4753   4731    353    235    306       N  
ATOM   1540  CA  VAL A 240     -23.314  80.691  -9.221  1.00 19.14           C  
ANISOU 1540  CA  VAL A 240     1873   2669   2729    390    290    329       C  
ATOM   1541  C   VAL A 240     -23.977  80.200 -10.502  1.00 35.90           C  
ANISOU 1541  C   VAL A 240     3996   4831   4814    448    243    398       C  
ATOM   1542  O   VAL A 240     -24.794  79.279 -10.461  1.00 53.35           O  
ANISOU 1542  O   VAL A 240     6167   7113   6990    446    168    414       O  
ATOM   1543  CB  VAL A 240     -21.800  80.488  -9.300  1.00 33.06           C  
ANISOU 1543  CB  VAL A 240     3657   4396   4509    337    296    277       C  
ATOM   1544  CG1 VAL A 240     -21.130  81.160  -8.126  1.00 34.63           C  
ANISOU 1544  CG1 VAL A 240     3851   4558   4749    289    349    196       C  
ATOM   1545  CG2 VAL A 240     -21.475  79.011  -9.299  1.00 39.67           C  
ANISOU 1545  CG2 VAL A 240     4475   5295   5303    296    197    268       C  
ATOM   1546  N   LYS A 241     -23.641  80.812 -11.631  1.00 35.09           N  
ANISOU 1546  N   LYS A 241     3936   4682   4715    502    290    435       N  
ATOM   1547  CA  LYS A 241     -24.188  80.376 -12.914  1.00 49.15           C  
ANISOU 1547  CA  LYS A 241     5721   6505   6449    569    242    495       C  
ATOM   1548  C   LYS A 241     -23.805  78.915 -13.214  1.00 37.07           C  
ANISOU 1548  C   LYS A 241     4170   5029   4884    520    144    481       C  
ATOM   1549  O   LYS A 241     -22.625  78.563 -13.277  1.00 53.03           O  
ANISOU 1549  O   LYS A 241     6215   7020   6915    471    143    451       O  
ATOM   1550  CB  LYS A 241     -23.734  81.317 -14.037  1.00 64.68           C  
ANISOU 1550  CB  LYS A 241     7753   8402   8422    641    323    538       C  
ATOM   1551  CG  LYS A 241     -24.379  81.047 -15.383  1.00 81.57           C  
ANISOU 1551  CG  LYS A 241     9902  10588  10502    734    281    603       C  
ATOM   1552  CD  LYS A 241     -23.870  82.000 -16.458  1.00108.62           C  
ANISOU 1552  CD  LYS A 241    13407  13937  13929    815    374    651       C  
ATOM   1553  CE  LYS A 241     -24.424  81.628 -17.829  1.00122.58           C  
ANISOU 1553  CE  LYS A 241    15188  15764  15623    915    321    711       C  
ATOM   1554  NZ  LYS A 241     -23.936  82.512 -18.925  1.00108.33           N1+
ANISOU 1554  NZ  LYS A 241    13471  13882  13806   1008    418    767       N1+
ATOM   1555  N   MET A 242     -24.817  78.072 -13.393  1.00 24.37           N  
ANISOU 1555  N   MET A 242     2517   3501   3240    533     65    498       N  
ATOM   1556  CA  MET A 242     -24.609  76.656 -13.639  1.00 29.28           C  
ANISOU 1556  CA  MET A 242     3119   4174   3833    485    -23    482       C  
ATOM   1557  C   MET A 242     -25.766  76.049 -14.418  1.00 44.99           C  
ANISOU 1557  C   MET A 242     5068   6243   5785    531    -91    509       C  
ATOM   1558  O   MET A 242     -26.854  76.628 -14.496  1.00 24.30           O  
ANISOU 1558  O   MET A 242     2419   3652   3161    592    -80    532       O  
ATOM   1559  CB  MET A 242     -24.479  75.919 -12.314  1.00 35.11           C  
ANISOU 1559  CB  MET A 242     3829   4928   4583    401    -48    435       C  
ATOM   1560  CG  MET A 242     -25.744  75.964 -11.487  1.00 41.22           C  
ANISOU 1560  CG  MET A 242     4554   5743   5365    403    -51    434       C  
ATOM   1561  SD  MET A 242     -25.550  75.173  -9.887  1.00 37.68           S  
ANISOU 1561  SD  MET A 242     4089   5304   4923    318    -64    386       S  
ATOM   1562  CE  MET A 242     -25.265  73.480 -10.387  1.00 55.17           C  
ANISOU 1562  CE  MET A 242     6298   7558   7105    273   -145    380       C  
ATOM   1563  N   SER A 243     -25.523  74.868 -14.976  1.00 41.66           N  
ANISOU 1563  N   SER A 243     4639   5857   5335    501   -161    499       N  
ATOM   1564  CA  SER A 243     -26.536  74.150 -15.739  1.00 39.40           C  
ANISOU 1564  CA  SER A 243     4305   5651   5016    533   -232    506       C  
ATOM   1565  C   SER A 243     -27.472  73.349 -14.833  1.00 46.86           C  
ANISOU 1565  C   SER A 243     5181   6646   5976    475   -269    473       C  
ATOM   1566  O   SER A 243     -27.109  72.962 -13.719  1.00 22.15           O  
ANISOU 1566  O   SER A 243     2054   3492   2870    402   -254    447       O  
ATOM   1567  CB  SER A 243     -25.863  73.218 -16.739  1.00 56.17           C  
ANISOU 1567  CB  SER A 243     6458   7782   7103    516   -279    500       C  
ATOM   1568  OG  SER A 243     -24.749  73.863 -17.329  1.00 37.53           O  
ANISOU 1568  OG  SER A 243     4161   5360   4740    552   -237    527       O  
ATOM   1569  N   THR A 244     -28.676  73.092 -15.321  1.00 38.79           N  
ANISOU 1569  N   THR A 244     4108   5693   4936    506   -306    468       N  
ATOM   1570  CA  THR A 244     -29.683  72.392 -14.532  1.00 30.30           C  
ANISOU 1570  CA  THR A 244     2967   4662   3883    452   -325    433       C  
ATOM   1571  C   THR A 244     -29.242  71.013 -14.042  1.00 21.58           C  
ANISOU 1571  C   THR A 244     1875   3542   2782    349   -344    397       C  
ATOM   1572  O   THR A 244     -29.492  70.648 -12.894  1.00 41.31           O  
ANISOU 1572  O   THR A 244     4352   6034   5311    295   -325    380       O  
ATOM   1573  CB  THR A 244     -30.982  72.241 -15.331  1.00 31.54           C  
ANISOU 1573  CB  THR A 244     3057   4905   4022    504   -371    421       C  
ATOM   1574  CG2 THR A 244     -31.737  73.560 -15.356  1.00 27.39           C  
ANISOU 1574  CG2 THR A 244     2502   4402   3502    605   -344    455       C  
ATOM   1575  OG1 THR A 244     -30.669  71.854 -16.674  1.00 76.54           O  
ANISOU 1575  OG1 THR A 244     8783  10627   9672    536   -413    420       O  
ATOM   1576  N   TYR A 245     -28.588  70.244 -14.903  1.00 22.39           N  
ANISOU 1576  N   TYR A 245     2016   3638   2854    330   -374    388       N  
ATOM   1577  CA  TYR A 245     -28.250  68.866 -14.558  1.00 44.61           C  
ANISOU 1577  CA  TYR A 245     4842   6438   5669    244   -390    356       C  
ATOM   1578  C   TYR A 245     -27.265  68.768 -13.395  1.00 32.18           C  
ANISOU 1578  C   TYR A 245     3313   4805   4108    194   -354    359       C  
ATOM   1579  O   TYR A 245     -27.081  67.695 -12.816  1.00 53.35           O  
ANISOU 1579  O   TYR A 245     6002   7475   6793    133   -357    339       O  
ATOM   1580  CB  TYR A 245     -27.729  68.097 -15.779  1.00 23.82           C  
ANISOU 1580  CB  TYR A 245     2241   3808   3000    241   -427    346       C  
ATOM   1581  CG  TYR A 245     -26.290  68.380 -16.142  1.00 35.30           C  
ANISOU 1581  CG  TYR A 245     3772   5205   4435    249   -407    367       C  
ATOM   1582  CD1 TYR A 245     -25.962  69.380 -17.048  1.00 39.04           C  
ANISOU 1582  CD1 TYR A 245     4271   5675   4889    325   -398    398       C  
ATOM   1583  CD2 TYR A 245     -25.256  67.638 -15.588  1.00 26.40           C  
ANISOU 1583  CD2 TYR A 245     2690   4029   3310    187   -394    357       C  
ATOM   1584  CE1 TYR A 245     -24.646  69.637 -17.386  1.00 29.98           C  
ANISOU 1584  CE1 TYR A 245     3185   4473   3733    329   -375    414       C  
ATOM   1585  CE2 TYR A 245     -23.942  67.887 -15.916  1.00 21.82           C  
ANISOU 1585  CE2 TYR A 245     2168   3402   2718    193   -377    368       C  
ATOM   1586  CZ  TYR A 245     -23.641  68.888 -16.816  1.00 37.41           C  
ANISOU 1586  CZ  TYR A 245     4160   5371   4682    259   -366    395       C  
ATOM   1587  OH  TYR A 245     -22.329  69.140 -17.145  1.00 40.24           O  
ANISOU 1587  OH  TYR A 245     4568   5682   5038    263   -345    403       O  
ATOM   1588  N   LEU A 246     -26.636  69.885 -13.050  1.00 18.34           N  
ANISOU 1588  N   LEU A 246     1587   3018   2363    227   -318    379       N  
ATOM   1589  CA  LEU A 246     -25.653  69.895 -11.973  1.00 30.99           C  
ANISOU 1589  CA  LEU A 246     3225   4576   3975    190   -290    370       C  
ATOM   1590  C   LEU A 246     -26.263  70.285 -10.629  1.00 37.22           C  
ANISOU 1590  C   LEU A 246     3976   5373   4793    182   -260    363       C  
ATOM   1591  O   LEU A 246     -25.606  70.187  -9.594  1.00 32.40           O  
ANISOU 1591  O   LEU A 246     3386   4740   4184    154   -241    348       O  
ATOM   1592  CB  LEU A 246     -24.484  70.814 -12.323  1.00 20.65           C  
ANISOU 1592  CB  LEU A 246     1955   3224   2667    221   -267    380       C  
ATOM   1593  CG  LEU A 246     -23.538  70.228 -13.359  1.00 29.80           C  
ANISOU 1593  CG  LEU A 246     3161   4364   3798    212   -288    380       C  
ATOM   1594  CD1 LEU A 246     -22.384  71.173 -13.636  1.00 33.42           C  
ANISOU 1594  CD1 LEU A 246     3648   4779   4271    243   -259    388       C  
ATOM   1595  CD2 LEU A 246     -23.028  68.893 -12.862  1.00 26.80           C  
ANISOU 1595  CD2 LEU A 246     2806   3976   3401    147   -305    354       C  
ATOM   1596  N   VAL A 247     -27.516  70.728 -10.655  1.00 17.73           N  
ANISOU 1596  N   VAL A 247     1451   2942   2345    212   -256    372       N  
ATOM   1597  CA  VAL A 247     -28.251  71.047  -9.435  1.00 34.23           C  
ANISOU 1597  CA  VAL A 247     3513   5034   4458    201   -215    365       C  
ATOM   1598  C   VAL A 247     -28.595  69.776  -8.657  1.00 38.04           C  
ANISOU 1598  C   VAL A 247     3983   5528   4944    139   -220    345       C  
ATOM   1599  O   VAL A 247     -28.897  68.733  -9.243  1.00 45.29           O  
ANISOU 1599  O   VAL A 247     4877   6470   5859    112   -257    336       O  
ATOM   1600  CB  VAL A 247     -29.548  71.816  -9.750  1.00 37.79           C  
ANISOU 1600  CB  VAL A 247     3907   5523   4927    254   -206    379       C  
ATOM   1601  CG1 VAL A 247     -30.321  72.104  -8.474  1.00 30.92           C  
ANISOU 1601  CG1 VAL A 247     3012   4653   4083    239   -159    371       C  
ATOM   1602  CG2 VAL A 247     -29.234  73.100 -10.487  1.00 17.88           C  
ANISOU 1602  CG2 VAL A 247     1412   2982   2400    327   -187    406       C  
ATOM   1603  N   ALA A 248     -28.554  69.861  -7.334  1.00 38.60           N  
ANISOU 1603  N   ALA A 248     4071   5578   5018    118   -176    338       N  
ATOM   1604  CA  ALA A 248     -28.716  68.667  -6.516  1.00 36.99           C  
ANISOU 1604  CA  ALA A 248     3875   5372   4809     67   -165    326       C  
ATOM   1605  C   ALA A 248     -29.146  68.983  -5.089  1.00 44.16           C  
ANISOU 1605  C   ALA A 248     4788   6269   5724     64   -108    323       C  
ATOM   1606  O   ALA A 248     -28.787  70.017  -4.529  1.00 55.77           O  
ANISOU 1606  O   ALA A 248     6278   7724   7189     92    -82    321       O  
ATOM   1607  CB  ALA A 248     -27.428  67.862  -6.515  1.00 15.13           C  
ANISOU 1607  CB  ALA A 248     1166   2578   2005     44   -187    321       C  
ATOM   1608  N   PHE A 249     -29.920  68.075  -4.509  1.00 50.86           N  
ANISOU 1608  N   PHE A 249     5618   7122   6583     28    -82    319       N  
ATOM   1609  CA  PHE A 249     -30.316  68.178  -3.114  1.00 37.02           C  
ANISOU 1609  CA  PHE A 249     3881   5357   4830     25    -21    319       C  
ATOM   1610  C   PHE A 249     -30.651  66.805  -2.554  1.00 48.96           C  
ANISOU 1610  C   PHE A 249     5407   6855   6341    -19     11    319       C  
ATOM   1611  O   PHE A 249     -31.193  65.944  -3.250  1.00 45.23           O  
ANISOU 1611  O   PHE A 249     4897   6391   5896    -55     -1    311       O  
ATOM   1612  CB  PHE A 249     -31.500  69.122  -2.944  1.00 17.81           C  
ANISOU 1612  CB  PHE A 249     1388   2944   2436     48      9    321       C  
ATOM   1613  CG  PHE A 249     -32.525  68.998  -4.024  1.00 47.28           C  
ANISOU 1613  CG  PHE A 249     5040   6716   6208     46    -19    317       C  
ATOM   1614  CD1 PHE A 249     -33.530  68.049  -3.938  1.00 31.10           C  
ANISOU 1614  CD1 PHE A 249     2941   4683   4194      3      1    301       C  
ATOM   1615  CD2 PHE A 249     -32.483  69.830  -5.134  1.00 39.99           C  
ANISOU 1615  CD2 PHE A 249     4091   5817   5287     91    -62    323       C  
ATOM   1616  CE1 PHE A 249     -34.478  67.930  -4.940  1.00 31.53           C  
ANISOU 1616  CE1 PHE A 249     2909   4785   4285      2    -32    282       C  
ATOM   1617  CE2 PHE A 249     -33.428  69.717  -6.135  1.00 52.27           C  
ANISOU 1617  CE2 PHE A 249     5571   7422   6869    103    -95    314       C  
ATOM   1618  CZ  PHE A 249     -34.432  68.765  -6.036  1.00 33.26           C  
ANISOU 1618  CZ  PHE A 249     3102   5040   4496     57    -86    288       C  
ATOM   1619  N   ILE A 250     -30.316  66.611  -1.286  1.00 50.43           N  
ANISOU 1619  N   ILE A 250     5650   7017   6493    -13     57    324       N  
ATOM   1620  CA  ILE A 250     -30.521  65.338  -0.624  1.00 31.30           C  
ANISOU 1620  CA  ILE A 250     3263   4568   4060    -43    105    332       C  
ATOM   1621  C   ILE A 250     -31.300  65.541   0.659  1.00 41.50           C  
ANISOU 1621  C   ILE A 250     4561   5850   5356    -34    183    339       C  
ATOM   1622  O   ILE A 250     -31.006  66.451   1.441  1.00 67.77           O  
ANISOU 1622  O   ILE A 250     7913   9181   8653      6    195    338       O  
ATOM   1623  CB  ILE A 250     -29.174  64.675  -0.295  1.00 32.62           C  
ANISOU 1623  CB  ILE A 250     3516   4716   4161    -29     90    338       C  
ATOM   1624  CG1 ILE A 250     -28.365  64.463  -1.578  1.00 40.28           C  
ANISOU 1624  CG1 ILE A 250     4482   5694   5130    -38     17    331       C  
ATOM   1625  CG2 ILE A 250     -29.392  63.363   0.426  1.00 36.38           C  
ANISOU 1625  CG2 ILE A 250     4042   5158   4622    -48    153    354       C  
ATOM   1626  CD1 ILE A 250     -27.054  63.729  -1.367  1.00 45.38           C  
ANISOU 1626  CD1 ILE A 250     5204   6324   5715    -23     -2    335       C  
ATOM   1627  N   ILE A 251     -32.306  64.705   0.873  1.00 31.09           N  
ANISOU 1627  N   ILE A 251     3219   4516   4077    -74    242    342       N  
ATOM   1628  CA  ILE A 251     -33.034  64.716   2.136  1.00 46.29           C  
ANISOU 1628  CA  ILE A 251     5161   6422   6004    -67    330    353       C  
ATOM   1629  C   ILE A 251     -32.883  63.352   2.801  1.00 44.96           C  
ANISOU 1629  C   ILE A 251     5065   6206   5810    -85    398    371       C  
ATOM   1630  O   ILE A 251     -33.270  62.329   2.237  1.00 56.97           O  
ANISOU 1630  O   ILE A 251     6565   7706   7373   -137    416    365       O  
ATOM   1631  CB  ILE A 251     -34.517  65.065   1.934  1.00 34.37           C  
ANISOU 1631  CB  ILE A 251     3553   4931   4574    -94    364    339       C  
ATOM   1632  CG1 ILE A 251     -34.645  66.338   1.088  1.00 27.13           C  
ANISOU 1632  CG1 ILE A 251     2569   4061   3679    -67    295    326       C  
ATOM   1633  CG2 ILE A 251     -35.202  65.250   3.279  1.00 27.02           C  
ANISOU 1633  CG2 ILE A 251     2643   3981   3644    -80    458    352       C  
ATOM   1634  CD1 ILE A 251     -36.060  66.648   0.647  1.00 31.10           C  
ANISOU 1634  CD1 ILE A 251     2964   4597   4256    -83    309    307       C  
ATOM   1635  N   SER A 252     -32.301  63.337   3.994  1.00 48.70           N  
ANISOU 1635  N   SER A 252     5628   6664   6213    -36    437    392       N  
ATOM   1636  CA  SER A 252     -32.006  62.076   4.666  1.00 59.04           C  
ANISOU 1636  CA  SER A 252     7026   7926   7480    -31    503    418       C  
ATOM   1637  C   SER A 252     -31.682  62.286   6.138  1.00 35.23           C  
ANISOU 1637  C   SER A 252     4097   4905   4385     38    557    439       C  
ATOM   1638  O   SER A 252     -32.034  63.310   6.718  1.00 62.68           O  
ANISOU 1638  O   SER A 252     7552   8403   7859     65    565    431       O  
ATOM   1639  CB  SER A 252     -30.837  61.365   3.974  1.00 50.53           C  
ANISOU 1639  CB  SER A 252     5993   6845   6363    -29    441    420       C  
ATOM   1640  OG  SER A 252     -29.615  62.060   4.178  1.00 25.08           O  
ANISOU 1640  OG  SER A 252     2807   3655   3066     31    370    413       O  
ATOM   1641  N   ASP A 253     -31.007  61.307   6.731  1.00 39.85           N  
ANISOU 1641  N   ASP A 253     4782   5459   4899     74    593    466       N  
ATOM   1642  CA  ASP A 253     -30.607  61.380   8.132  1.00 53.86           C  
ANISOU 1642  CA  ASP A 253     6651   7235   6579    156    641    486       C  
ATOM   1643  C   ASP A 253     -29.129  61.046   8.290  1.00 45.53           C  
ANISOU 1643  C   ASP A 253     5675   6201   5423    222    581    488       C  
ATOM   1644  O   ASP A 253     -28.714  60.488   9.302  1.00 53.33           O  
ANISOU 1644  O   ASP A 253     6762   7179   6322    294    630    514       O  
ATOM   1645  CB  ASP A 253     -31.454  60.437   8.987  1.00 41.31           C  
ANISOU 1645  CB  ASP A 253     5119   5582   4993    155    779    527       C  
ATOM   1646  CG  ASP A 253     -31.374  58.995   8.526  1.00 91.91           C  
ANISOU 1646  CG  ASP A 253    11570  11934  11419    120    826    551       C  
ATOM   1647  OD1 ASP A 253     -30.948  58.751   7.375  1.00 86.77           O  
ANISOU 1647  OD1 ASP A 253    10877  11292  10801     76    749    531       O  
ATOM   1648  OD2 ASP A 253     -31.744  58.102   9.319  1.00101.53           O1-
ANISOU 1648  OD2 ASP A 253    12868  13091  12618    137    946    590       O1-
ATOM   1649  N   PHE A 254     -28.338  61.406   7.284  1.00 31.00           N  
ANISOU 1649  N   PHE A 254     3790   4395   3595    204    475    458       N  
ATOM   1650  CA  PHE A 254     -26.920  61.066   7.251  1.00 46.27           C  
ANISOU 1650  CA  PHE A 254     5782   6353   5447    258    412    451       C  
ATOM   1651  C   PHE A 254     -26.087  61.761   8.316  1.00 42.74           C  
ANISOU 1651  C   PHE A 254     5379   5957   4903    347    383    426       C  
ATOM   1652  O   PHE A 254     -26.418  62.853   8.783  1.00 52.45           O  
ANISOU 1652  O   PHE A 254     6574   7213   6141    357    380    400       O  
ATOM   1653  CB  PHE A 254     -26.317  61.392   5.883  1.00 57.99           C  
ANISOU 1653  CB  PHE A 254     7200   7859   6976    213    312    421       C  
ATOM   1654  CG  PHE A 254     -26.883  60.583   4.756  1.00 57.94           C  
ANISOU 1654  CG  PHE A 254     7156   7813   7046    136    322    436       C  
ATOM   1655  CD1 PHE A 254     -27.587  59.420   5.003  1.00 81.71           C  
ANISOU 1655  CD1 PHE A 254    10205  10767  10073    112    414    470       C  
ATOM   1656  CD2 PHE A 254     -26.699  60.984   3.445  1.00 43.64           C  
ANISOU 1656  CD2 PHE A 254     5272   6019   5288     90    244    411       C  
ATOM   1657  CE1 PHE A 254     -28.104  58.678   3.965  1.00 88.64           C  
ANISOU 1657  CE1 PHE A 254    11042  11612  11026     37    423    469       C  
ATOM   1658  CE2 PHE A 254     -27.210  60.245   2.404  1.00 37.15           C  
ANISOU 1658  CE2 PHE A 254     4414   5171   4531     25    246    415       C  
ATOM   1659  CZ  PHE A 254     -27.914  59.094   2.662  1.00 59.06           C  
ANISOU 1659  CZ  PHE A 254     7219   7893   7326     -6    333    439       C  
ATOM   1660  N   GLU A 255     -24.991  61.110   8.686  1.00 49.43           N  
ANISOU 1660  N   GLU A 255     6302   6822   5657    416    360    431       N  
ATOM   1661  CA  GLU A 255     -23.950  61.741   9.478  1.00 54.91           C  
ANISOU 1661  CA  GLU A 255     7023   7582   6257    502    305    387       C  
ATOM   1662  C   GLU A 255     -22.934  62.319   8.515  1.00 49.44           C  
ANISOU 1662  C   GLU A 255     6267   6928   5588    477    197    334       C  
ATOM   1663  O   GLU A 255     -22.994  62.061   7.313  1.00 32.83           O  
ANISOU 1663  O   GLU A 255     4120   4798   3556    409    171    344       O  
ATOM   1664  CB  GLU A 255     -23.273  60.721  10.392  1.00 58.47           C  
ANISOU 1664  CB  GLU A 255     7587   8042   6587    604    334    416       C  
ATOM   1665  CG  GLU A 255     -24.136  60.273  11.548  1.00 83.88           C  
ANISOU 1665  CG  GLU A 255    10883  11226   9762    651    449    466       C  
ATOM   1666  CD  GLU A 255     -24.599  61.438  12.396  1.00112.85           C  
ANISOU 1666  CD  GLU A 255    14526  14929  13421    672    459    432       C  
ATOM   1667  OE1 GLU A 255     -23.800  62.379  12.600  1.00112.71           O  
ANISOU 1667  OE1 GLU A 255    14476  14982  13366    707    375    365       O  
ATOM   1668  OE2 GLU A 255     -25.760  61.414  12.856  1.00121.65           O1-
ANISOU 1668  OE2 GLU A 255    15651  15999  14570    652    554    468       O1-
ATOM   1669  N   SER A 256     -22.001  63.100   9.043  1.00 39.99           N  
ANISOU 1669  N   SER A 256     5065   5796   4334    534    138    273       N  
ATOM   1670  CA  SER A 256     -20.931  63.649   8.226  1.00 43.79           C  
ANISOU 1670  CA  SER A 256     5490   6312   4837    515     46    215       C  
ATOM   1671  C   SER A 256     -19.642  63.748   9.023  1.00 42.49           C  
ANISOU 1671  C   SER A 256     5356   6220   4569    606     -8    156       C  
ATOM   1672  O   SER A 256     -19.662  63.879  10.245  1.00 46.06           O  
ANISOU 1672  O   SER A 256     5852   6708   4941    681     15    142       O  
ATOM   1673  CB  SER A 256     -21.317  65.030   7.689  1.00 29.91           C  
ANISOU 1673  CB  SER A 256     3643   4552   3168    451     26    174       C  
ATOM   1674  OG  SER A 256     -21.539  65.950   8.746  1.00 37.70           O  
ANISOU 1674  OG  SER A 256     4628   5568   4127    487     46    135       O  
ATOM   1675  N   VAL A 257     -18.522  63.657   8.321  1.00 38.45           N  
ANISOU 1675  N   VAL A 257     4818   5735   4057    603    -79    120       N  
ATOM   1676  CA  VAL A 257     -17.226  64.004   8.890  1.00 37.76           C  
ANISOU 1676  CA  VAL A 257     4725   5727   3894    675   -146     38       C  
ATOM   1677  C   VAL A 257     -16.638  65.098   8.004  1.00 54.71           C  
ANISOU 1677  C   VAL A 257     6778   7884   6125    609   -202    -36       C  
ATOM   1678  O   VAL A 257     -16.752  65.038   6.778  1.00 49.13           O  
ANISOU 1678  O   VAL A 257     6037   7130   5500    535   -209     -8       O  
ATOM   1679  CB  VAL A 257     -16.277  62.784   8.997  1.00 29.43           C  
ANISOU 1679  CB  VAL A 257     3733   4702   2748    752   -173     56       C  
ATOM   1680  CG1 VAL A 257     -16.833  61.767   9.979  1.00 45.51           C  
ANISOU 1680  CG1 VAL A 257     5875   6723   4694    831   -102    128       C  
ATOM   1681  CG2 VAL A 257     -16.058  62.141   7.636  1.00 44.48           C  
ANISOU 1681  CG2 VAL A 257     5623   6560   4719    687   -190     93       C  
ATOM   1682  N   SER A 258     -16.035  66.110   8.617  1.00 60.47           N  
ANISOU 1682  N   SER A 258     7468   8671   6837    635   -235   -131       N  
ATOM   1683  CA  SER A 258     -15.624  67.293   7.868  1.00 39.34           C  
ANISOU 1683  CA  SER A 258     4706   5989   4253    566   -264   -202       C  
ATOM   1684  C   SER A 258     -14.180  67.673   8.119  1.00 42.29           C  
ANISOU 1684  C   SER A 258     5039   6437   4592    604   -330   -315       C  
ATOM   1685  O   SER A 258     -13.712  67.646   9.256  1.00 62.66           O  
ANISOU 1685  O   SER A 258     7639   9091   7080    686   -353   -372       O  
ATOM   1686  CB  SER A 258     -16.525  68.480   8.216  1.00 42.85           C  
ANISOU 1686  CB  SER A 258     5119   6410   4751    531   -218   -220       C  
ATOM   1687  OG  SER A 258     -17.871  68.226   7.853  1.00 93.14           O  
ANISOU 1687  OG  SER A 258    11507  12713  11168    488   -160   -125       O  
ATOM   1688  N   LYS A 259     -13.476  68.028   7.050  1.00 34.93           N  
ANISOU 1688  N   LYS A 259     4049   5487   3734    546   -359   -351       N  
ATOM   1689  CA  LYS A 259     -12.151  68.619   7.179  1.00 46.80           C  
ANISOU 1689  CA  LYS A 259     5493   7053   5237    560   -412   -475       C  
ATOM   1690  C   LYS A 259     -12.093  69.928   6.395  1.00 56.71           C  
ANISOU 1690  C   LYS A 259     6673   8259   6614    470   -389   -529       C  
ATOM   1691  O   LYS A 259     -12.867  70.134   5.460  1.00 55.41           O  
ANISOU 1691  O   LYS A 259     6509   8017   6528    406   -349   -456       O  
ATOM   1692  CB  LYS A 259     -11.066  67.646   6.712  1.00 33.30           C  
ANISOU 1692  CB  LYS A 259     3789   5377   3488    593   -465   -478       C  
ATOM   1693  CG  LYS A 259      -9.652  68.151   6.938  1.00 63.57           C  
ANISOU 1693  CG  LYS A 259     7554   9288   7313    616   -523   -616       C  
ATOM   1694  CD  LYS A 259      -8.612  67.151   6.464  1.00 81.33           C  
ANISOU 1694  CD  LYS A 259     9808  11572   9522    654   -575   -614       C  
ATOM   1695  CE  LYS A 259      -7.206  67.728   6.568  1.00125.19           C  
ANISOU 1695  CE  LYS A 259    15275  17202  15088    665   -629   -762       C  
ATOM   1696  NZ  LYS A 259      -6.164  66.767   6.106  1.00134.77           N1+
ANISOU 1696  NZ  LYS A 259    16489  18454  16263    706   -680   -763       N1+
ATOM   1697  N   ILE A 260     -11.190  70.819   6.793  1.00 51.74           N  
ANISOU 1697  N   ILE A 260     5982   7677   5999    471   -411   -660       N  
ATOM   1698  CA  ILE A 260     -11.019  72.098   6.107  1.00 54.06           C  
ANISOU 1698  CA  ILE A 260     6211   7919   6412    389   -376   -721       C  
ATOM   1699  C   ILE A 260      -9.707  72.125   5.334  1.00 40.86           C  
ANISOU 1699  C   ILE A 260     4483   6257   4783    363   -409   -793       C  
ATOM   1700  O   ILE A 260      -8.639  71.898   5.901  1.00 51.03           O  
ANISOU 1700  O   ILE A 260     5741   7631   6019    410   -464   -889       O  
ATOM   1701  CB  ILE A 260     -11.019  73.284   7.090  1.00 40.19           C  
ANISOU 1701  CB  ILE A 260     4415   6189   4665    390   -356   -832       C  
ATOM   1702  CG1 ILE A 260     -12.239  73.226   8.018  1.00 38.25           C  
ANISOU 1702  CG1 ILE A 260     4226   5944   4363    428   -326   -771       C  
ATOM   1703  CG2 ILE A 260     -10.993  74.596   6.328  1.00 28.31           C  
ANISOU 1703  CG2 ILE A 260     2857   4609   3291    303   -298   -879       C  
ATOM   1704  CD1 ILE A 260     -13.510  73.784   7.408  1.00 55.76           C  
ANISOU 1704  CD1 ILE A 260     6457   8067   6663    368   -254   -681       C  
ATOM   1705  N   THR A 261      -9.791  72.412   4.039  1.00 63.12           N  
ANISOU 1705  N   THR A 261     7289   8995   7698    293   -373   -747       N  
ATOM   1706  CA  THR A 261      -8.611  72.467   3.182  1.00 47.30           C  
ANISOU 1706  CA  THR A 261     5237   6988   5748    261   -389   -805       C  
ATOM   1707  C   THR A 261      -7.707  73.640   3.582  1.00 56.27           C  
ANISOU 1707  C   THR A 261     6292   8147   6941    233   -376   -965       C  
ATOM   1708  O   THR A 261      -8.081  74.457   4.427  1.00 45.67           O  
ANISOU 1708  O   THR A 261     4935   6815   5602    233   -351  -1024       O  
ATOM   1709  CB  THR A 261      -9.017  72.593   1.699  1.00 49.90           C  
ANISOU 1709  CB  THR A 261     5579   7217   6163    198   -343   -714       C  
ATOM   1710  CG2 THR A 261      -9.371  74.032   1.351  1.00 28.06           C  
ANISOU 1710  CG2 THR A 261     2783   4378   3501    138   -265   -745       C  
ATOM   1711  OG1 THR A 261      -7.944  72.149   0.864  1.00 97.82           O  
ANISOU 1711  OG1 THR A 261    11626  13290  12253    187   -368   -734       O  
ATOM   1712  N   LYS A 262      -6.522  73.717   2.984  1.00 62.63           N  
ANISOU 1712  N   LYS A 262     7043   8960   7795    207   -388  -1041       N  
ATOM   1713  CA  LYS A 262      -5.595  74.815   3.272  1.00 56.54           C  
ANISOU 1713  CA  LYS A 262     6183   8204   7093    169   -367  -1207       C  
ATOM   1714  C   LYS A 262      -6.155  76.182   2.860  1.00 55.64           C  
ANISOU 1714  C   LYS A 262     6059   7988   7096     93   -266  -1216       C  
ATOM   1715  O   LYS A 262      -5.864  77.196   3.495  1.00 42.96           O  
ANISOU 1715  O   LYS A 262     4399   6391   5534     68   -235  -1343       O  
ATOM   1716  CB  LYS A 262      -4.231  74.570   2.615  1.00 48.81           C  
ANISOU 1716  CB  LYS A 262     5145   7247   6153    152   -391  -1282       C  
ATOM   1717  CG  LYS A 262      -3.426  73.462   3.283  1.00 91.88           C  
ANISOU 1717  CG  LYS A 262    10589  12826  11494    237   -491  -1323       C  
ATOM   1718  CD  LYS A 262      -2.087  73.232   2.599  1.00 85.61           C  
ANISOU 1718  CD  LYS A 262     9731  12054  10744    220   -513  -1398       C  
ATOM   1719  CE  LYS A 262      -1.334  72.078   3.249  1.00 85.70           C  
ANISOU 1719  CE  LYS A 262     9738  12192  10633    320   -614  -1429       C  
ATOM   1720  NZ  LYS A 262      -0.075  71.745   2.525  1.00101.74           N1+
ANISOU 1720  NZ  LYS A 262    11709  14244  12703    309   -637  -1489       N1+
ATOM   1721  N   SER A 263      -6.963  76.200   1.805  1.00 58.44           N  
ANISOU 1721  N   SER A 263     6463   8245   7495     62   -214  -1084       N  
ATOM   1722  CA  SER A 263      -7.568  77.436   1.327  1.00 39.41           C  
ANISOU 1722  CA  SER A 263     4056   5732   5186      5   -114  -1071       C  
ATOM   1723  C   SER A 263      -8.918  77.732   1.980  1.00 56.10           C  
ANISOU 1723  C   SER A 263     6215   7833   7267     27    -92  -1006       C  
ATOM   1724  O   SER A 263      -9.651  78.610   1.523  1.00 58.52           O  
ANISOU 1724  O   SER A 263     6539   8053   7642     -5    -12   -963       O  
ATOM   1725  CB  SER A 263      -7.715  77.411  -0.194  1.00 42.85           C  
ANISOU 1725  CB  SER A 263     4522   6075   5686    -28    -66   -969       C  
ATOM   1726  OG  SER A 263      -8.482  76.298  -0.613  1.00 74.68           O  
ANISOU 1726  OG  SER A 263     8615  10113   9647      8   -112   -827       O  
ATOM   1727  N   GLY A 264      -9.244  76.997   3.040  1.00 52.47           N  
ANISOU 1727  N   GLY A 264     5777   7457   6701     86   -158   -997       N  
ATOM   1728  CA  GLY A 264     -10.443  77.264   3.818  1.00 52.64           C  
ANISOU 1728  CA  GLY A 264     5836   7476   6688    110   -137   -951       C  
ATOM   1729  C   GLY A 264     -11.737  76.699   3.261  1.00 45.55           C  
ANISOU 1729  C   GLY A 264     5002   6532   5772    120   -124   -787       C  
ATOM   1730  O   GLY A 264     -12.823  77.012   3.750  1.00 59.65           O  
ANISOU 1730  O   GLY A 264     6815   8303   7547    132    -93   -742       O  
ATOM   1731  N   VAL A 265     -11.630  75.870   2.232  1.00 41.03           N  
ANISOU 1731  N   VAL A 265     4451   5941   5199    116   -147   -704       N  
ATOM   1732  CA  VAL A 265     -12.795  75.201   1.676  1.00 36.98           C  
ANISOU 1732  CA  VAL A 265     3990   5396   4666    125   -145   -562       C  
ATOM   1733  C   VAL A 265     -13.163  74.026   2.564  1.00 55.45           C  
ANISOU 1733  C   VAL A 265     6367   7802   6899    180   -199   -522       C  
ATOM   1734  O   VAL A 265     -12.347  73.133   2.787  1.00 45.67           O  
ANISOU 1734  O   VAL A 265     5134   6620   5600    212   -256   -545       O  
ATOM   1735  CB  VAL A 265     -12.522  74.668   0.258  1.00 38.19           C  
ANISOU 1735  CB  VAL A 265     4152   5509   4850    103   -153   -496       C  
ATOM   1736  CG1 VAL A 265     -13.736  73.920  -0.269  1.00 28.36           C  
ANISOU 1736  CG1 VAL A 265     2952   4242   3581    113   -158   -365       C  
ATOM   1737  CG2 VAL A 265     -12.148  75.806  -0.677  1.00 60.09           C  
ANISOU 1737  CG2 VAL A 265     6898   8208   7725     57    -87   -526       C  
ATOM   1738  N   LYS A 266     -14.393  74.026   3.071  1.00 46.85           N  
ANISOU 1738  N   LYS A 266     5309   6703   5787    195   -173   -459       N  
ATOM   1739  CA  LYS A 266     -14.844  72.943   3.934  1.00 29.46           C  
ANISOU 1739  CA  LYS A 266     3153   4551   3490    247   -204   -413       C  
ATOM   1740  C   LYS A 266     -15.269  71.721   3.125  1.00 59.00           C  
ANISOU 1740  C   LYS A 266     6930   8272   7214    245   -222   -305       C  
ATOM   1741  O   LYS A 266     -16.157  71.799   2.272  1.00 70.93           O  
ANISOU 1741  O   LYS A 266     8444   9730   8776    212   -193   -230       O  
ATOM   1742  CB  LYS A 266     -15.984  73.403   4.843  1.00 38.56           C  
ANISOU 1742  CB  LYS A 266     4322   5700   4629    263   -161   -394       C  
ATOM   1743  CG  LYS A 266     -16.355  72.378   5.905  1.00 51.76           C  
ANISOU 1743  CG  LYS A 266     6047   7422   6199    323   -179   -359       C  
ATOM   1744  CD  LYS A 266     -17.493  72.848   6.792  1.00 47.14           C  
ANISOU 1744  CD  LYS A 266     5479   6829   5603    338   -129   -339       C  
ATOM   1745  CE  LYS A 266     -18.673  71.892   6.709  1.00 78.56           C  
ANISOU 1745  CE  LYS A 266     9502  10784   9564    343   -103   -224       C  
ATOM   1746  NZ  LYS A 266     -19.636  72.069   7.833  1.00 71.83           N1+
ANISOU 1746  NZ  LYS A 266     8678   9939   8676    375    -57   -208       N1+
ATOM   1747  N   VAL A 267     -14.623  70.592   3.402  1.00 41.24           N  
ANISOU 1747  N   VAL A 267     4710   6070   4891    285   -269   -303       N  
ATOM   1748  CA  VAL A 267     -14.934  69.326   2.743  1.00 24.80           C  
ANISOU 1748  CA  VAL A 267     2667   3969   2786    285   -283   -210       C  
ATOM   1749  C   VAL A 267     -15.589  68.369   3.735  1.00 38.50           C  
ANISOU 1749  C   VAL A 267     4461   5729   4440    336   -274   -160       C  
ATOM   1750  O   VAL A 267     -15.076  68.147   4.831  1.00 36.21           O  
ANISOU 1750  O   VAL A 267     4193   5496   4070    398   -292   -204       O  
ATOM   1751  CB  VAL A 267     -13.668  68.657   2.195  1.00 39.37           C  
ANISOU 1751  CB  VAL A 267     4509   5838   4613    296   -333   -236       C  
ATOM   1752  CG1 VAL A 267     -14.037  67.620   1.148  1.00 50.33           C  
ANISOU 1752  CG1 VAL A 267     5928   7187   6010    274   -337   -144       C  
ATOM   1753  CG2 VAL A 267     -12.718  69.694   1.616  1.00 20.58           C  
ANISOU 1753  CG2 VAL A 267     2069   3450   2302    260   -337   -319       C  
ATOM   1754  N   SER A 268     -16.719  67.799   3.343  1.00 44.66           N  
ANISOU 1754  N   SER A 268     5267   6465   5238    312   -241    -70       N  
ATOM   1755  CA  SER A 268     -17.461  66.916   4.224  1.00 35.96           C  
ANISOU 1755  CA  SER A 268     4222   5368   4072    351   -212    -17       C  
ATOM   1756  C   SER A 268     -17.868  65.651   3.500  1.00 42.13           C  
ANISOU 1756  C   SER A 268     5037   6114   4856    331   -204     63       C  
ATOM   1757  O   SER A 268     -18.144  65.668   2.301  1.00 34.34           O  
ANISOU 1757  O   SER A 268     4021   5091   3937    276   -209     90       O  
ATOM   1758  CB  SER A 268     -18.718  67.614   4.753  1.00 37.59           C  
ANISOU 1758  CB  SER A 268     4419   5554   4308    337   -156      2       C  
ATOM   1759  OG  SER A 268     -18.389  68.783   5.482  1.00 64.90           O  
ANISOU 1759  OG  SER A 268     7851   9042   7764    354   -157    -75       O  
ATOM   1760  N   VAL A 269     -17.907  64.547   4.235  1.00 56.48           N  
ANISOU 1760  N   VAL A 269     6921   7941   6599    381   -186     98       N  
ATOM   1761  CA  VAL A 269     -18.443  63.308   3.702  1.00 37.28           C  
ANISOU 1761  CA  VAL A 269     4527   5464   4172    359   -159    172       C  
ATOM   1762  C   VAL A 269     -19.689  62.925   4.480  1.00 53.79           C  
ANISOU 1762  C   VAL A 269     6655   7528   6254    364    -84    222       C  
ATOM   1763  O   VAL A 269     -19.654  62.789   5.705  1.00 56.73           O  
ANISOU 1763  O   VAL A 269     7078   7924   6552    430    -57    220       O  
ATOM   1764  CB  VAL A 269     -17.428  62.165   3.784  1.00 32.97           C  
ANISOU 1764  CB  VAL A 269     4038   4936   3552    412   -185    180       C  
ATOM   1765  CG1 VAL A 269     -18.034  60.895   3.224  1.00 37.62           C  
ANISOU 1765  CG1 VAL A 269     4669   5468   4156    383   -145    252       C  
ATOM   1766  CG2 VAL A 269     -16.160  62.529   3.030  1.00 47.32           C  
ANISOU 1766  CG2 VAL A 269     5814   6782   5382    407   -255    126       C  
ATOM   1767  N   TYR A 270     -20.798  62.773   3.766  1.00 34.40           N  
ANISOU 1767  N   TYR A 270     4173   5026   3874    298    -50    263       N  
ATOM   1768  CA  TYR A 270     -22.038  62.306   4.371  1.00 34.83           C  
ANISOU 1768  CA  TYR A 270     4253   5046   3935    290     30    309       C  
ATOM   1769  C   TYR A 270     -22.252  60.829   4.061  1.00 30.58           C  
ANISOU 1769  C   TYR A 270     3765   4462   3391    275     69    360       C  
ATOM   1770  O   TYR A 270     -21.995  60.376   2.947  1.00 49.51           O  
ANISOU 1770  O   TYR A 270     6143   6843   5825    234     36    365       O  
ATOM   1771  CB  TYR A 270     -23.225  63.121   3.856  1.00 49.45           C  
ANISOU 1771  CB  TYR A 270     6031   6879   5879    227     50    311       C  
ATOM   1772  CG  TYR A 270     -23.288  64.539   4.380  1.00 44.98           C  
ANISOU 1772  CG  TYR A 270     5428   6343   5321    243     42    270       C  
ATOM   1773  CD1 TYR A 270     -24.238  64.908   5.317  1.00 50.74           C  
ANISOU 1773  CD1 TYR A 270     6162   7068   6050    255    103    280       C  
ATOM   1774  CD2 TYR A 270     -22.403  65.510   3.929  1.00 30.94           C  
ANISOU 1774  CD2 TYR A 270     3611   4591   3553    245    -19    220       C  
ATOM   1775  CE1 TYR A 270     -24.308  66.199   5.792  1.00 54.71           C  
ANISOU 1775  CE1 TYR A 270     6633   7594   6561    270    100    241       C  
ATOM   1776  CE2 TYR A 270     -22.464  66.806   4.400  1.00 39.91           C  
ANISOU 1776  CE2 TYR A 270     4715   5745   4703    255    -15    178       C  
ATOM   1777  CZ  TYR A 270     -23.419  67.145   5.333  1.00 50.45           C  
ANISOU 1777  CZ  TYR A 270     6057   7077   6035    269     42    188       C  
ATOM   1778  OH  TYR A 270     -23.490  68.434   5.811  1.00 42.08           O  
ANISOU 1778  OH  TYR A 270     4969   6032   4989    280     49    144       O  
ATOM   1779  N   ALA A 271     -22.718  60.082   5.052  1.00 49.96           N  
ANISOU 1779  N   ALA A 271     6289   6893   5801    312    147    397       N  
ATOM   1780  CA  ALA A 271     -23.010  58.667   4.865  1.00 58.19           C  
ANISOU 1780  CA  ALA A 271     7388   7879   6844    296    207    446       C  
ATOM   1781  C   ALA A 271     -24.056  58.210   5.870  1.00 53.17           C  
ANISOU 1781  C   ALA A 271     6801   7200   6201    308    320    486       C  
ATOM   1782  O   ALA A 271     -24.359  58.923   6.825  1.00 50.59           O  
ANISOU 1782  O   ALA A 271     6479   6897   5846    347    343    478       O  
ATOM   1783  CB  ALA A 271     -21.748  57.840   5.010  1.00 35.15           C  
ANISOU 1783  CB  ALA A 271     4545   4973   3839    365    180    455       C  
ATOM   1784  N   VAL A 272     -24.611  57.025   5.644  1.00 60.77           N  
ANISOU 1784  N   VAL A 272     7800   8096   7193    272    397    525       N  
ATOM   1785  CA  VAL A 272     -25.525  56.418   6.602  1.00 37.57           C  
ANISOU 1785  CA  VAL A 272     4922   5104   4249    285    524    566       C  
ATOM   1786  C   VAL A 272     -24.871  56.385   7.982  1.00 51.78           C  
ANISOU 1786  C   VAL A 272     6823   6930   5922    407    549    587       C  
ATOM   1787  O   VAL A 272     -23.675  56.115   8.105  1.00 55.51           O  
ANISOU 1787  O   VAL A 272     7348   7437   6307    482    495    585       O  
ATOM   1788  CB  VAL A 272     -25.939  55.005   6.155  1.00 50.49           C  
ANISOU 1788  CB  VAL A 272     6599   6658   5928    236    608    600       C  
ATOM   1789  CG1 VAL A 272     -26.428  54.180   7.335  1.00105.84           C  
ANISOU 1789  CG1 VAL A 272    13715  13606  12895    284    751    653       C  
ATOM   1790  CG2 VAL A 272     -27.002  55.095   5.067  1.00 51.24           C  
ANISOU 1790  CG2 VAL A 272     6585   6730   6154    115    609    571       C  
ATOM   1791  N   PRO A 273     -25.655  56.676   9.029  1.00 48.53           N  
ANISOU 1791  N   PRO A 273     6437   6507   5496    434    630    604       N  
ATOM   1792  CA  PRO A 273     -25.092  56.886  10.369  1.00 50.84           C  
ANISOU 1792  CA  PRO A 273     6814   6841   5662    558    642    613       C  
ATOM   1793  C   PRO A 273     -24.224  55.730  10.867  1.00 54.13           C  
ANISOU 1793  C   PRO A 273     7356   7244   5967    658    675    656       C  
ATOM   1794  O   PRO A 273     -23.267  55.969  11.602  1.00 55.33           O  
ANISOU 1794  O   PRO A 273     7557   7463   6002    770    624    641       O  
ATOM   1795  CB  PRO A 273     -26.338  57.033  11.248  1.00 28.34           C  
ANISOU 1795  CB  PRO A 273     3981   3951   2835    552    758    639       C  
ATOM   1796  CG  PRO A 273     -27.400  57.510  10.312  1.00 51.77           C  
ANISOU 1796  CG  PRO A 273     6829   6895   5946    424    756    616       C  
ATOM   1797  CD  PRO A 273     -27.119  56.840   9.009  1.00 43.23           C  
ANISOU 1797  CD  PRO A 273     5711   5789   4925    354    713    610       C  
ATOM   1798  N   ASP A 274     -24.552  54.506  10.463  1.00 48.18           N  
ANISOU 1798  N   ASP A 274     6651   6406   5250    622    759    703       N  
ATOM   1799  CA  ASP A 274     -23.824  53.321  10.908  1.00 57.62           C  
ANISOU 1799  CA  ASP A 274     7976   7573   6344    720    810    755       C  
ATOM   1800  C   ASP A 274     -22.481  53.151  10.203  1.00 56.95           C  
ANISOU 1800  C   ASP A 274     7883   7540   6216    750    693    729       C  
ATOM   1801  O   ASP A 274     -21.611  52.416  10.674  1.00 50.03           O  
ANISOU 1801  O   ASP A 274     7107   6673   5229    861    702    760       O  
ATOM   1802  CB  ASP A 274     -24.666  52.060  10.686  1.00 75.66           C  
ANISOU 1802  CB  ASP A 274    10316   9737   8695    661    956    810       C  
ATOM   1803  CG  ASP A 274     -26.101  52.225  11.139  1.00107.99           C  
ANISOU 1803  CG  ASP A 274    14390  13773  12867    599   1075    824       C  
ATOM   1804  OD1 ASP A 274     -26.463  51.658  12.194  1.00 68.50           O  
ANISOU 1804  OD1 ASP A 274     9499   8719   7809    670   1208    879       O  
ATOM   1805  OD2 ASP A 274     -26.870  52.919  10.437  1.00119.82           O1-
ANISOU 1805  OD2 ASP A 274    15764  15280  14482    486   1038    779       O1-
ATOM   1806  N   LYS A 275     -22.316  53.827   9.071  1.00 68.98           N  
ANISOU 1806  N   LYS A 275     9289   9097   7824    658    586    675       N  
ATOM   1807  CA  LYS A 275     -21.126  53.639   8.248  1.00 57.90           C  
ANISOU 1807  CA  LYS A 275     7870   7731   6400    669    484    650       C  
ATOM   1808  C   LYS A 275     -20.239  54.876   8.195  1.00 59.07           C  
ANISOU 1808  C   LYS A 275     7942   7983   6519    697    350    580       C  
ATOM   1809  O   LYS A 275     -19.155  54.840   7.612  1.00 33.70           O  
ANISOU 1809  O   LYS A 275     4711   4811   3284    715    263    551       O  
ATOM   1810  CB  LYS A 275     -21.526  53.247   6.825  1.00 45.16           C  
ANISOU 1810  CB  LYS A 275     6191   6062   4906    543    476    645       C  
ATOM   1811  CG  LYS A 275     -22.292  51.952   6.726  1.00 47.43           C  
ANISOU 1811  CG  LYS A 275     6543   6244   5234    503    606    699       C  
ATOM   1812  CD  LYS A 275     -22.662  51.658   5.282  1.00 62.48           C  
ANISOU 1812  CD  LYS A 275     8371   8111   7257    377    582    676       C  
ATOM   1813  CE  LYS A 275     -23.296  50.286   5.144  1.00 66.49           C  
ANISOU 1813  CE  LYS A 275     8944   8511   7809    334    712    716       C  
ATOM   1814  NZ  LYS A 275     -23.709  50.019   3.743  1.00 84.82           N1+
ANISOU 1814  NZ  LYS A 275    11182  10803  10244    211    685    681       N1+
ATOM   1815  N   ILE A 276     -20.697  55.966   8.802  1.00 33.54           N  
ANISOU 1815  N   ILE A 276     4664   4787   3291    697    341    548       N  
ATOM   1816  CA  ILE A 276     -19.967  57.230   8.739  1.00 52.41           C  
ANISOU 1816  CA  ILE A 276     6976   7265   5673    707    229    472       C  
ATOM   1817  C   ILE A 276     -18.501  57.100   9.160  1.00 42.26           C  
ANISOU 1817  C   ILE A 276     5728   6056   4272    819    155    439       C  
ATOM   1818  O   ILE A 276     -17.657  57.887   8.738  1.00 53.77           O  
ANISOU 1818  O   ILE A 276     7113   7575   5740    810     56    370       O  
ATOM   1819  CB  ILE A 276     -20.639  58.320   9.593  1.00 41.72           C  
ANISOU 1819  CB  ILE A 276     5593   5938   4320    714    247    446       C  
ATOM   1820  CG1 ILE A 276     -20.131  59.702   9.182  1.00 40.38           C  
ANISOU 1820  CG1 ILE A 276     5321   5832   4190    681    146    365       C  
ATOM   1821  CG2 ILE A 276     -20.380  58.067  11.066  1.00 22.67           C  
ANISOU 1821  CG2 ILE A 276     3278   3560   1774    846    288    461       C  
ATOM   1822  CD1 ILE A 276     -20.362  60.030   7.723  1.00 43.57           C  
ANISOU 1822  CD1 ILE A 276     5634   6205   4714    566    106    353       C  
ATOM   1823  N   ASN A 277     -18.199  56.104   9.988  1.00 53.10           N  
ANISOU 1823  N   ASN A 277     7214   7424   5536    928    208    487       N  
ATOM   1824  CA  ASN A 277     -16.829  55.888  10.438  1.00 67.87           C  
ANISOU 1824  CA  ASN A 277     9124   9378   7287   1051    139    456       C  
ATOM   1825  C   ASN A 277     -15.922  55.301   9.351  1.00 64.17           C  
ANISOU 1825  C   ASN A 277     8636   8906   6839   1029     79    451       C  
ATOM   1826  O   ASN A 277     -14.728  55.096   9.569  1.00 42.94           O  
ANISOU 1826  O   ASN A 277     5967   6288   4062   1124     15    420       O  
ATOM   1827  CB  ASN A 277     -16.801  55.015  11.698  1.00 60.02           C  
ANISOU 1827  CB  ASN A 277     8265   8384   6156   1194    218    514       C  
ATOM   1828  CG  ASN A 277     -17.266  53.590  11.439  1.00 99.31           C  
ANISOU 1828  CG  ASN A 277    13338  13253  11141   1188    330    610       C  
ATOM   1829  ND2 ASN A 277     -17.921  53.374  10.303  1.00 97.84           N  
ANISOU 1829  ND2 ASN A 277    13101  12987  11088   1048    355    627       N  
ATOM   1830  OD1 ASN A 277     -17.036  52.693  12.252  1.00120.19           O  
ANISOU 1830  OD1 ASN A 277    16106  15889  13673   1312    396    665       O  
ATOM   1831  N   GLN A 278     -16.490  55.046   8.177  1.00 55.46           N  
ANISOU 1831  N   GLN A 278     7493   7727   5853    906     99    476       N  
ATOM   1832  CA  GLN A 278     -15.726  54.505   7.054  1.00 53.00           C  
ANISOU 1832  CA  GLN A 278     7162   7404   5570    874     49    472       C  
ATOM   1833  C   GLN A 278     -15.400  55.581   6.020  1.00 74.43           C  
ANISOU 1833  C   GLN A 278     9753  10151   8375    782    -46    403       C  
ATOM   1834  O   GLN A 278     -14.895  55.279   4.937  1.00 75.49           O  
ANISOU 1834  O   GLN A 278     9859  10271   8553    737    -87    398       O  
ATOM   1835  CB  GLN A 278     -16.498  53.363   6.390  1.00 41.57           C  
ANISOU 1835  CB  GLN A 278     5763   5849   4184    806    138    544       C  
ATOM   1836  CG  GLN A 278     -16.742  52.181   7.305  1.00 52.68           C  
ANISOU 1836  CG  GLN A 278     7303   7204   5507    895    250    618       C  
ATOM   1837  CD  GLN A 278     -17.738  51.189   6.739  1.00 67.15           C  
ANISOU 1837  CD  GLN A 278     9173   8920   7423    808    359    677       C  
ATOM   1838  NE2 GLN A 278     -18.258  50.321   7.601  1.00 59.29           N  
ANISOU 1838  NE2 GLN A 278     8289   7861   6378    865    486    742       N  
ATOM   1839  OE1 GLN A 278     -18.039  51.200   5.544  1.00 65.43           O  
ANISOU 1839  OE1 GLN A 278     8883   8667   7310    692    334    660       O  
ATOM   1840  N   ALA A 279     -15.688  56.833   6.356  1.00 49.37           N  
ANISOU 1840  N   ALA A 279     6512   7017   5229    759    -74    351       N  
ATOM   1841  CA  ALA A 279     -15.481  57.928   5.413  1.00 51.89           C  
ANISOU 1841  CA  ALA A 279     6722   7356   5639    674   -145    291       C  
ATOM   1842  C   ALA A 279     -14.106  58.564   5.566  1.00 49.86           C  
ANISOU 1842  C   ALA A 279     6422   7186   5336    729   -235    208       C  
ATOM   1843  O   ALA A 279     -13.668  59.309   4.694  1.00 56.95           O  
ANISOU 1843  O   ALA A 279     7240   8094   6304    668   -290    158       O  
ATOM   1844  CB  ALA A 279     -16.567  58.975   5.567  1.00 54.92           C  
ANISOU 1844  CB  ALA A 279     7052   7724   6092    611   -118    279       C  
ATOM   1845  N   ASP A 280     -13.431  58.255   6.671  1.00 57.74           N  
ANISOU 1845  N   ASP A 280     7474   8248   6217    849   -247    190       N  
ATOM   1846  CA  ASP A 280     -12.136  58.861   6.988  1.00 45.46           C  
ANISOU 1846  CA  ASP A 280     5870   6790   4611    911   -333     95       C  
ATOM   1847  C   ASP A 280     -11.160  58.885   5.814  1.00 53.50           C  
ANISOU 1847  C   ASP A 280     6829   7816   5683    866   -397     57       C  
ATOM   1848  O   ASP A 280     -10.467  59.878   5.602  1.00 52.75           O  
ANISOU 1848  O   ASP A 280     6648   7770   5625    842   -456    -33       O  
ATOM   1849  CB  ASP A 280     -11.486  58.168   8.190  1.00 43.43           C  
ANISOU 1849  CB  ASP A 280     5693   6603   4205   1063   -339     94       C  
ATOM   1850  CG  ASP A 280     -12.243  58.403   9.485  1.00104.21           C  
ANISOU 1850  CG  ASP A 280    13442  14315  11837   1124   -287    108       C  
ATOM   1851  OD1 ASP A 280     -13.260  59.131   9.467  1.00 94.01           O  
ANISOU 1851  OD1 ASP A 280    12118  12981  10621   1044   -248    114       O  
ATOM   1852  OD2 ASP A 280     -11.814  57.856  10.523  1.00134.48           O1-
ANISOU 1852  OD2 ASP A 280    17351  18207  15539   1261   -284    113       O1-
ATOM   1853  N   TYR A 281     -11.100  57.798   5.052  1.00 63.24           N  
ANISOU 1853  N   TYR A 281     8107   8997   6925    852   -379    122       N  
ATOM   1854  CA  TYR A 281     -10.186  57.738   3.916  1.00 56.03           C  
ANISOU 1854  CA  TYR A 281     7136   8070   6084    809   -413     84       C  
ATOM   1855  C   TYR A 281     -10.612  58.670   2.787  1.00 58.87           C  
ANISOU 1855  C   TYR A 281     7414   8384   6570    683   -419     66       C  
ATOM   1856  O   TYR A 281      -9.837  59.522   2.351  1.00 49.67           O  
ANISOU 1856  O   TYR A 281     6172   7244   5457    655   -455    -12       O  
ATOM   1857  CB  TYR A 281     -10.043  56.310   3.384  1.00 54.75           C  
ANISOU 1857  CB  TYR A 281     7043   7853   5905    827   -381    154       C  
ATOM   1858  CG  TYR A 281      -9.103  56.234   2.205  1.00 50.88           C  
ANISOU 1858  CG  TYR A 281     6499   7348   5483    784   -412    116       C  
ATOM   1859  CD1 TYR A 281      -7.729  56.254   2.389  1.00 28.33           C  
ANISOU 1859  CD1 TYR A 281     3614   4561   2590    856   -459     46       C  
ATOM   1860  CD2 TYR A 281      -9.588  56.166   0.906  1.00 46.29           C  
ANISOU 1860  CD2 TYR A 281     5895   6692   5000    676   -394    147       C  
ATOM   1861  CE1 TYR A 281      -6.859  56.199   1.310  1.00 33.87           C  
ANISOU 1861  CE1 TYR A 281     4270   5247   3351    817   -479     13       C  
ATOM   1862  CE2 TYR A 281      -8.727  56.107  -0.178  1.00 36.81           C  
ANISOU 1862  CE2 TYR A 281     4655   5477   3855    641   -415    116       C  
ATOM   1863  CZ  TYR A 281      -7.364  56.125   0.030  1.00 47.46           C  
ANISOU 1863  CZ  TYR A 281     5980   6886   5168    709   -454     51       C  
ATOM   1864  OH  TYR A 281      -6.503  56.064  -1.042  1.00 65.52           O  
ANISOU 1864  OH  TYR A 281     8231   9156   7506    675   -468     23       O  
ATOM   1865  N   ALA A 282     -11.840  58.497   2.309  1.00 54.30           N  
ANISOU 1865  N   ALA A 282     6856   7739   6038    612   -377    137       N  
ATOM   1866  CA  ALA A 282     -12.348  59.331   1.232  1.00 26.25           C  
ANISOU 1866  CA  ALA A 282     3233   4146   2596    507   -381    129       C  
ATOM   1867  C   ALA A 282     -12.176  60.809   1.562  1.00 36.31           C  
ANISOU 1867  C   ALA A 282     4435   5463   3898    494   -409     53       C  
ATOM   1868  O   ALA A 282     -11.744  61.590   0.719  1.00 58.53           O  
ANISOU 1868  O   ALA A 282     7186   8264   6788    441   -422      8       O  
ATOM   1869  CB  ALA A 282     -13.805  59.016   0.944  1.00 31.82           C  
ANISOU 1869  CB  ALA A 282     3960   4787   3343    447   -327    201       C  
ATOM   1870  N   LEU A 283     -12.504  61.189   2.794  1.00 41.43           N  
ANISOU 1870  N   LEU A 283     5098   6149   4494    542   -396     35       N  
ATOM   1871  CA  LEU A 283     -12.400  62.584   3.211  1.00 36.33           C  
ANISOU 1871  CA  LEU A 283     4387   5538   3878    530   -411    -43       C  
ATOM   1872  C   LEU A 283     -10.982  63.116   3.053  1.00 46.76           C  
ANISOU 1872  C   LEU A 283     5651   6917   5199    547   -472   -140       C  
ATOM   1873  O   LEU A 283     -10.775  64.203   2.515  1.00 46.75           O  
ANISOU 1873  O   LEU A 283     5580   6906   5277    488   -479   -195       O  
ATOM   1874  CB  LEU A 283     -12.866  62.763   4.654  1.00 35.00           C  
ANISOU 1874  CB  LEU A 283     4253   5406   3639    593   -385    -53       C  
ATOM   1875  CG  LEU A 283     -12.720  64.182   5.208  1.00 41.99           C  
ANISOU 1875  CG  LEU A 283     5075   6332   4548    586   -399   -144       C  
ATOM   1876  CD1 LEU A 283     -13.448  65.186   4.330  1.00 43.66           C  
ANISOU 1876  CD1 LEU A 283     5229   6482   4876    487   -372   -138       C  
ATOM   1877  CD2 LEU A 283     -13.239  64.252   6.625  1.00 37.04           C  
ANISOU 1877  CD2 LEU A 283     4490   5739   3843    654   -371   -147       C  
ATOM   1878  N   ASP A 284     -10.006  62.351   3.523  1.00 24.40           N  
ANISOU 1878  N   ASP A 284     2847   4138   2287    628   -502   -164       N  
ATOM   1879  CA  ASP A 284      -8.610  62.749   3.389  1.00 45.21           C  
ANISOU 1879  CA  ASP A 284     5420   6824   4934    647   -544   -265       C  
ATOM   1880  C   ASP A 284      -8.209  62.815   1.924  1.00 56.29           C  
ANISOU 1880  C   ASP A 284     6788   8164   6436    568   -531   -260       C  
ATOM   1881  O   ASP A 284      -7.510  63.735   1.501  1.00 54.30           O  
ANISOU 1881  O   ASP A 284     6465   7921   6244    530   -546   -339       O  
ATOM   1882  CB  ASP A 284      -7.688  61.794   4.148  1.00 41.32           C  
ANISOU 1882  CB  ASP A 284     4966   6401   4334    763   -574   -285       C  
ATOM   1883  CG  ASP A 284      -7.852  61.903   5.653  1.00109.07           C  
ANISOU 1883  CG  ASP A 284    13577  15062  12803    859   -592   -313       C  
ATOM   1884  OD1 ASP A 284      -8.435  62.904   6.116  1.00134.14           O  
ANISOU 1884  OD1 ASP A 284    16724  18251  15993    827   -593   -346       O  
ATOM   1885  OD2 ASP A 284      -7.395  60.991   6.375  1.00137.71           O1-
ANISOU 1885  OD2 ASP A 284    17261  18740  16323    971   -605   -300       O1-
ATOM   1886  N   ALA A 285      -8.655  61.836   1.148  1.00 50.76           N  
ANISOU 1886  N   ALA A 285     6140   7398   5750    544   -501   -169       N  
ATOM   1887  CA  ALA A 285      -8.363  61.814  -0.277  1.00 50.06           C  
ANISOU 1887  CA  ALA A 285     6030   7247   5742    474   -486   -156       C  
ATOM   1888  C   ALA A 285      -8.972  63.036  -0.953  1.00 57.46           C  
ANISOU 1888  C   ALA A 285     6920   8142   6770    390   -467   -163       C  
ATOM   1889  O   ALA A 285      -8.356  63.649  -1.825  1.00 53.63           O  
ANISOU 1889  O   ALA A 285     6394   7634   6347    348   -466   -201       O  
ATOM   1890  CB  ALA A 285      -8.898  60.542  -0.904  1.00 50.66           C  
ANISOU 1890  CB  ALA A 285     6171   7264   5814    462   -459    -62       C  
ATOM   1891  N   ALA A 286     -10.183  63.386  -0.539  1.00 42.03           N  
ANISOU 1891  N   ALA A 286     4975   6176   4819    373   -451   -125       N  
ATOM   1892  CA  ALA A 286     -10.877  64.529  -1.111  1.00 48.68           C  
ANISOU 1892  CA  ALA A 286     5775   6980   5741    306   -431   -124       C  
ATOM   1893  C   ALA A 286     -10.109  65.817  -0.834  1.00 53.77           C  
ANISOU 1893  C   ALA A 286     6353   7660   6418    300   -448   -225       C  
ATOM   1894  O   ALA A 286      -9.869  66.610  -1.742  1.00 40.03           O  
ANISOU 1894  O   ALA A 286     4574   5881   4753    250   -432   -246       O  
ATOM   1895  CB  ALA A 286     -12.301  64.621  -0.564  1.00 31.91           C  
ANISOU 1895  CB  ALA A 286     3667   4850   3607    300   -414    -68       C  
ATOM   1896  N   VAL A 287      -9.712  66.010   0.420  1.00 36.34           N  
ANISOU 1896  N   VAL A 287     4131   5526   4151    354   -478   -291       N  
ATOM   1897  CA  VAL A 287      -9.005  67.221   0.819  1.00 34.56           C  
ANISOU 1897  CA  VAL A 287     3833   5338   3958    345   -492   -405       C  
ATOM   1898  C   VAL A 287      -7.721  67.446   0.026  1.00 42.74           C  
ANISOU 1898  C   VAL A 287     4822   6372   5044    323   -502   -473       C  
ATOM   1899  O   VAL A 287      -7.503  68.528  -0.516  1.00 56.34           O  
ANISOU 1899  O   VAL A 287     6488   8064   6853    266   -480   -523       O  
ATOM   1900  CB  VAL A 287      -8.696  67.238   2.340  1.00 29.45           C  
ANISOU 1900  CB  VAL A 287     3187   4777   3225    420   -519   -476       C  
ATOM   1901  CG1 VAL A 287      -7.767  68.394   2.684  1.00 36.64           C  
ANISOU 1901  CG1 VAL A 287     4016   5730   4176    407   -531   -617       C  
ATOM   1902  CG2 VAL A 287      -9.984  67.335   3.150  1.00 23.72           C  
ANISOU 1902  CG2 VAL A 287     2505   4038   2469    433   -482   -423       C  
ATOM   1903  N   THR A 288      -6.875  66.426  -0.049  1.00 40.32           N  
ANISOU 1903  N   THR A 288     4541   6092   4688    369   -524   -473       N  
ATOM   1904  CA  THR A 288      -5.591  66.573  -0.724  1.00 61.98           C  
ANISOU 1904  CA  THR A 288     7237   8839   7472    354   -533   -542       C  
ATOM   1905  C   THR A 288      -5.763  66.752  -2.229  1.00 47.79           C  
ANISOU 1905  C   THR A 288     5449   6950   5758    283   -491   -484       C  
ATOM   1906  O   THR A 288      -4.990  67.464  -2.863  1.00 27.88           O  
ANISOU 1906  O   THR A 288     2873   4413   3306    244   -481   -547       O  
ATOM   1907  CB  THR A 288      -4.659  65.378  -0.454  1.00 38.39           C  
ANISOU 1907  CB  THR A 288     4274   5905   4408    430   -568   -551       C  
ATOM   1908  CG2 THR A 288      -4.628  65.053   1.020  1.00 47.43           C  
ANISOU 1908  CG2 THR A 288     5430   7142   5451    520   -608   -587       C  
ATOM   1909  OG1 THR A 288      -5.125  64.236  -1.176  1.00 80.02           O  
ANISOU 1909  OG1 THR A 288     9622  11118   9664    429   -545   -436       O  
ATOM   1910  N   LEU A 289      -6.777  66.104  -2.797  1.00 37.10           N  
ANISOU 1910  N   LEU A 289     4160   5538   4397    269   -467   -370       N  
ATOM   1911  CA  LEU A 289      -7.035  66.190  -4.231  1.00 30.31           C  
ANISOU 1911  CA  LEU A 289     3316   4600   3600    214   -434   -310       C  
ATOM   1912  C   LEU A 289      -7.626  67.545  -4.606  1.00 40.48           C  
ANISOU 1912  C   LEU A 289     4565   5849   4966    162   -403   -318       C  
ATOM   1913  O   LEU A 289      -7.347  68.080  -5.675  1.00 48.24           O  
ANISOU 1913  O   LEU A 289     5530   6785   6014    125   -379   -317       O  
ATOM   1914  CB  LEU A 289      -7.972  65.068  -4.675  1.00 19.71           C  
ANISOU 1914  CB  LEU A 289     2045   3217   2227    214   -420   -201       C  
ATOM   1915  CG  LEU A 289      -7.342  63.707  -4.997  1.00 38.93           C  
ANISOU 1915  CG  LEU A 289     4522   5652   4619    243   -431   -173       C  
ATOM   1916  CD1 LEU A 289      -8.371  62.580  -4.927  1.00 32.57           C  
ANISOU 1916  CD1 LEU A 289     3775   4822   3777    249   -419    -86       C  
ATOM   1917  CD2 LEU A 289      -6.681  63.743  -6.362  1.00 33.99           C  
ANISOU 1917  CD2 LEU A 289     3891   4981   4041    210   -420   -170       C  
ATOM   1918  N   LEU A 290      -8.448  68.095  -3.725  1.00 40.85           N  
ANISOU 1918  N   LEU A 290     4598   5917   5007    166   -401   -324       N  
ATOM   1919  CA  LEU A 290      -9.022  69.405  -3.965  1.00 26.20           C  
ANISOU 1919  CA  LEU A 290     2699   4026   3228    125   -365   -334       C  
ATOM   1920  C   LEU A 290      -7.895  70.416  -3.998  1.00 30.02           C  
ANISOU 1920  C   LEU A 290     3124   4506   3775    101   -341   -444       C  
ATOM   1921  O   LEU A 290      -7.814  71.236  -4.912  1.00 36.80           O  
ANISOU 1921  O   LEU A 290     3970   5301   4713     61   -286   -444       O  
ATOM   1922  CB  LEU A 290     -10.031  69.753  -2.871  1.00 36.50           C  
ANISOU 1922  CB  LEU A 290     4014   5347   4507    140   -352   -328       C  
ATOM   1923  CG  LEU A 290     -10.736  71.107  -2.969  1.00 67.40           C  
ANISOU 1923  CG  LEU A 290     7908   9210   8491    107   -289   -335       C  
ATOM   1924  CD1 LEU A 290     -11.559  71.180  -4.232  1.00 80.15           C  
ANISOU 1924  CD1 LEU A 290     9546  10760  10147     84   -259   -242       C  
ATOM   1925  CD2 LEU A 290     -11.611  71.324  -1.758  1.00 63.76           C  
ANISOU 1925  CD2 LEU A 290     7456   8776   7994    129   -282   -337       C  
ATOM   1926  N   GLU A 291      -7.021  70.347  -2.998  1.00 21.03           N  
ANISOU 1926  N   GLU A 291     1950   3440   2602    128   -377   -542       N  
ATOM   1927  CA  GLU A 291      -5.823  71.181  -2.950  1.00 27.95           C  
ANISOU 1927  CA  GLU A 291     2755   4326   3538    103   -360   -669       C  
ATOM   1928  C   GLU A 291      -4.965  71.020  -4.205  1.00 43.16           C  
ANISOU 1928  C   GLU A 291     4669   6213   5517     75   -345   -666       C  
ATOM   1929  O   GLU A 291      -4.393  71.990  -4.696  1.00 46.14           O  
ANISOU 1929  O   GLU A 291     5003   6543   5984     29   -287   -730       O  
ATOM   1930  CB  GLU A 291      -4.983  70.856  -1.713  1.00 42.38           C  
ANISOU 1930  CB  GLU A 291     4544   6258   5299    153   -421   -775       C  
ATOM   1931  CG  GLU A 291      -5.681  71.113  -0.393  1.00 61.79           C  
ANISOU 1931  CG  GLU A 291     7013   8762   7704    187   -431   -796       C  
ATOM   1932  CD  GLU A 291      -4.847  70.700   0.806  1.00 77.32           C  
ANISOU 1932  CD  GLU A 291     8948  10843   9586    255   -500   -896       C  
ATOM   1933  OE1 GLU A 291      -3.800  70.045   0.608  1.00 82.26           O  
ANISOU 1933  OE1 GLU A 291     9551  11518  10187    283   -546   -935       O  
ATOM   1934  OE2 GLU A 291      -5.239  71.028   1.947  1.00 70.11           O1-
ANISOU 1934  OE2 GLU A 291     8035   9976   8627    287   -508   -938       O1-
ATOM   1935  N   PHE A 292      -4.868  69.797  -4.717  1.00 35.53           N  
ANISOU 1935  N   PHE A 292     3748   5256   4495    103   -387   -592       N  
ATOM   1936  CA  PHE A 292      -4.077  69.558  -5.919  1.00 37.50           C  
ANISOU 1936  CA  PHE A 292     3998   5465   4784     83   -370   -582       C  
ATOM   1937  C   PHE A 292      -4.670  70.310  -7.097  1.00 40.69           C  
ANISOU 1937  C   PHE A 292     4414   5778   5267     36   -305   -519       C  
ATOM   1938  O   PHE A 292      -3.981  71.066  -7.772  1.00 28.32           O  
ANISOU 1938  O   PHE A 292     2817   4163   3781      0   -248   -566       O  
ATOM   1939  CB  PHE A 292      -3.987  68.067  -6.259  1.00 28.33           C  
ANISOU 1939  CB  PHE A 292     2912   4311   3541    127   -403   -504       C  
ATOM   1940  CG  PHE A 292      -3.481  67.797  -7.651  1.00 44.80           C  
ANISOU 1940  CG  PHE A 292     5013   6344   5665    104   -383   -466       C  
ATOM   1941  CD1 PHE A 292      -2.122  67.647  -7.897  1.00 59.19           C  
ANISOU 1941  CD1 PHE A 292     6793   8190   7507    107   -393   -540       C  
ATOM   1942  CD2 PHE A 292      -4.362  67.715  -8.720  1.00 50.50           C  
ANISOU 1942  CD2 PHE A 292     5787   6998   6403     82   -357   -363       C  
ATOM   1943  CE1 PHE A 292      -1.656  67.408  -9.177  1.00 26.84           C  
ANISOU 1943  CE1 PHE A 292     2710   4044   3445     87   -373   -505       C  
ATOM   1944  CE2 PHE A 292      -3.900  67.478 -10.004  1.00 45.45           C  
ANISOU 1944  CE2 PHE A 292     5161   6315   5792     68   -342   -329       C  
ATOM   1945  CZ  PHE A 292      -2.548  67.323 -10.232  1.00 33.32           C  
ANISOU 1945  CZ  PHE A 292     3586   4797   4275     69   -348   -397       C  
ATOM   1946  N   TYR A 293      -5.953  70.088  -7.343  1.00 42.65           N  
ANISOU 1946  N   TYR A 293     4717   5997   5489     42   -302   -414       N  
ATOM   1947  CA  TYR A 293      -6.621  70.706  -8.473  1.00 38.23           C  
ANISOU 1947  CA  TYR A 293     4186   5357   4984     18   -241   -344       C  
ATOM   1948  C   TYR A 293      -6.561  72.233  -8.417  1.00 46.15           C  
ANISOU 1948  C   TYR A 293     5156   6307   6072    -13   -158   -402       C  
ATOM   1949  O   TYR A 293      -6.392  72.884  -9.444  1.00 37.78           O  
ANISOU 1949  O   TYR A 293     4106   5176   5075    -33    -91   -385       O  
ATOM   1950  CB  TYR A 293      -8.073  70.237  -8.564  1.00 34.38           C  
ANISOU 1950  CB  TYR A 293     3747   4865   4451     36   -260   -238       C  
ATOM   1951  CG  TYR A 293      -8.241  68.814  -9.049  1.00 44.59           C  
ANISOU 1951  CG  TYR A 293     5100   6167   5676     55   -304   -167       C  
ATOM   1952  CD1 TYR A 293      -9.014  67.899  -8.340  1.00 46.33           C  
ANISOU 1952  CD1 TYR A 293     5365   6411   5826     76   -327   -126       C  
ATOM   1953  CD2 TYR A 293      -7.638  68.388 -10.225  1.00 48.49           C  
ANISOU 1953  CD2 TYR A 293     5614   6631   6180     51   -301   -142       C  
ATOM   1954  CE1 TYR A 293      -9.179  66.602  -8.791  1.00 53.96           C  
ANISOU 1954  CE1 TYR A 293     6389   7368   6745     85   -339    -68       C  
ATOM   1955  CE2 TYR A 293      -7.795  67.092 -10.679  1.00 53.70           C  
ANISOU 1955  CE2 TYR A 293     6337   7285   6781     64   -322    -83       C  
ATOM   1956  CZ  TYR A 293      -8.564  66.204  -9.961  1.00 54.73           C  
ANISOU 1956  CZ  TYR A 293     6506   7436   6854     77   -337    -49       C  
ATOM   1957  OH  TYR A 293      -8.714  64.917 -10.422  1.00 36.38           O  
ANISOU 1957  OH  TYR A 293     4231   5099   4491     81   -344      0       O  
ATOM   1958  N   GLU A 294      -6.702  72.804  -7.224  1.00 50.67           N  
ANISOU 1958  N   GLU A 294     5697   6911   6645    -15   -155   -471       N  
ATOM   1959  CA  GLU A 294      -6.663  74.260  -7.073  1.00 41.65           C  
ANISOU 1959  CA  GLU A 294     4525   5715   5586    -48    -69   -535       C  
ATOM   1960  C   GLU A 294      -5.330  74.814  -7.564  1.00 40.15           C  
ANISOU 1960  C   GLU A 294     4289   5490   5475    -85    -16   -627       C  
ATOM   1961  O   GLU A 294      -5.273  75.884  -8.164  1.00 37.95           O  
ANISOU 1961  O   GLU A 294     4012   5128   5281   -115     81   -638       O  
ATOM   1962  CB  GLU A 294      -6.896  74.677  -5.616  1.00 26.71           C  
ANISOU 1962  CB  GLU A 294     2600   3874   3674    -43    -84   -611       C  
ATOM   1963  CG  GLU A 294      -8.294  74.398  -5.094  1.00 94.91           C  
ANISOU 1963  CG  GLU A 294    11280  12528  12252    -13   -109   -526       C  
ATOM   1964  CD  GLU A 294      -8.452  74.757  -3.627  1.00103.73           C  
ANISOU 1964  CD  GLU A 294    12371  13701  13343     -2   -124   -603       C  
ATOM   1965  OE1 GLU A 294      -7.432  75.044  -2.968  1.00101.76           O  
ANISOU 1965  OE1 GLU A 294    12067  13491  13105    -10   -133   -726       O  
ATOM   1966  OE2 GLU A 294      -9.598  74.751  -3.129  1.00109.75           O1-
ANISOU 1966  OE2 GLU A 294    13162  14467  14070     18   -125   -545       O1-
ATOM   1967  N   ASP A 295      -4.258  74.078  -7.297  1.00 47.70           N  
ANISOU 1967  N   ASP A 295     5206   6511   6405    -79    -75   -694       N  
ATOM   1968  CA  ASP A 295      -2.928  74.462  -7.745  1.00 47.38           C  
ANISOU 1968  CA  ASP A 295     5113   6449   6441   -115    -32   -790       C  
ATOM   1969  C   ASP A 295      -2.807  74.259  -9.255  1.00 57.65           C  
ANISOU 1969  C   ASP A 295     6460   7674   7770   -121     11   -702       C  
ATOM   1970  O   ASP A 295      -2.453  75.182  -9.987  1.00 60.67           O  
ANISOU 1970  O   ASP A 295     6838   7971   8243   -156    113   -723       O  
ATOM   1971  CB  ASP A 295      -1.873  73.644  -6.993  1.00 52.87           C  
ANISOU 1971  CB  ASP A 295     5752   7249   7087    -93   -119   -884       C  
ATOM   1972  CG  ASP A 295      -0.462  73.920  -7.470  1.00 92.51           C  
ANISOU 1972  CG  ASP A 295    10707  12257  12186   -129    -81   -988       C  
ATOM   1973  OD1 ASP A 295      -0.153  73.614  -8.641  1.00 85.89           O  
ANISOU 1973  OD1 ASP A 295     9897  11365  11372   -137    -52   -928       O  
ATOM   1974  OD2 ASP A 295       0.348  74.426  -6.665  1.00122.01           O1-
ANISOU 1974  OD2 ASP A 295    14358  16040  15958   -148    -80  -1136       O1-
ATOM   1975  N   TYR A 296      -3.117  73.048  -9.711  1.00 45.57           N  
ANISOU 1975  N   TYR A 296     4977   6174   6162    -84    -59   -605       N  
ATOM   1976  CA  TYR A 296      -3.026  72.700 -11.125  1.00 21.78           C  
ANISOU 1976  CA  TYR A 296     2013   3105   3160    -81    -33   -521       C  
ATOM   1977  C   TYR A 296      -3.769  73.691 -12.027  1.00 44.38           C  
ANISOU 1977  C   TYR A 296     4920   5867   6074    -89     63   -452       C  
ATOM   1978  O   TYR A 296      -3.177  74.293 -12.927  1.00 39.53           O  
ANISOU 1978  O   TYR A 296     4312   5180   5530   -109    149   -461       O  
ATOM   1979  CB  TYR A 296      -3.553  71.281 -11.369  1.00 31.06           C  
ANISOU 1979  CB  TYR A 296     3239   4326   4238    -41   -123   -423       C  
ATOM   1980  CG  TYR A 296      -3.329  70.805 -12.787  1.00 47.43           C  
ANISOU 1980  CG  TYR A 296     5356   6352   6313    -35   -108   -351       C  
ATOM   1981  CD1 TYR A 296      -2.123  70.224 -13.159  1.00 27.81           C  
ANISOU 1981  CD1 TYR A 296     2849   3883   3834    -37   -123   -392       C  
ATOM   1982  CD2 TYR A 296      -4.312  70.957 -13.759  1.00 48.94           C  
ANISOU 1982  CD2 TYR A 296     5609   6490   6498    -21    -78   -246       C  
ATOM   1983  CE1 TYR A 296      -1.904  69.796 -14.458  1.00 56.49           C  
ANISOU 1983  CE1 TYR A 296     6526   7473   7466    -30   -106   -327       C  
ATOM   1984  CE2 TYR A 296      -4.099  70.532 -15.065  1.00 63.30           C  
ANISOU 1984  CE2 TYR A 296     7469   8270   8310     -8    -66   -184       C  
ATOM   1985  CZ  TYR A 296      -2.893  69.953 -15.405  1.00 58.49           C  
ANISOU 1985  CZ  TYR A 296     6844   7673   7709    -15    -78   -224       C  
ATOM   1986  OH  TYR A 296      -2.670  69.527 -16.695  1.00 47.35           O  
ANISOU 1986  OH  TYR A 296     5478   6224   6289      0    -63   -164       O  
ATOM   1987  N   PHE A 297      -5.068  73.844 -11.788  1.00 24.19           N  
ANISOU 1987  N   PHE A 297     2399   3309   3482    -68     53   -381       N  
ATOM   1988  CA  PHE A 297      -5.886  74.751 -12.583  1.00 40.21           C  
ANISOU 1988  CA  PHE A 297     4475   5256   5547    -58    136   -309       C  
ATOM   1989  C   PHE A 297      -5.624  76.220 -12.259  1.00 53.78           C  
ANISOU 1989  C   PHE A 297     6167   6910   7359    -91    246   -385       C  
ATOM   1990  O   PHE A 297      -6.130  77.108 -12.949  1.00 50.58           O  
ANISOU 1990  O   PHE A 297     5803   6423   6992    -79    337   -332       O  
ATOM   1991  CB  PHE A 297      -7.368  74.458 -12.371  1.00 50.80           C  
ANISOU 1991  CB  PHE A 297     5852   6625   6824    -24     89   -219       C  
ATOM   1992  CG  PHE A 297      -7.762  73.059 -12.702  1.00 28.40           C  
ANISOU 1992  CG  PHE A 297     3044   3843   3905      2     -5   -148       C  
ATOM   1993  CD1 PHE A 297      -7.464  72.521 -13.936  1.00 26.33           C  
ANISOU 1993  CD1 PHE A 297     2816   3557   3630     16     -8    -94       C  
ATOM   1994  CD2 PHE A 297      -8.451  72.285 -11.781  1.00 42.55           C  
ANISOU 1994  CD2 PHE A 297     4830   5703   5634     13    -83   -135       C  
ATOM   1995  CE1 PHE A 297      -7.835  71.230 -14.249  1.00 49.94           C  
ANISOU 1995  CE1 PHE A 297     5832   6594   6550     35    -91    -36       C  
ATOM   1996  CE2 PHE A 297      -8.822  70.995 -12.087  1.00 32.97           C  
ANISOU 1996  CE2 PHE A 297     3645   4529   4354     31   -157    -73       C  
ATOM   1997  CZ  PHE A 297      -8.514  70.468 -13.326  1.00 28.53           C  
ANISOU 1997  CZ  PHE A 297     3113   3944   3783     40   -162    -27       C  
ATOM   1998  N   SER A 298      -4.850  76.468 -11.204  1.00 28.50           N  
ANISOU 1998  N   SER A 298     2896   3744   4188   -127    240   -510       N  
ATOM   1999  CA  SER A 298      -4.544  77.835 -10.778  1.00 47.90           C  
ANISOU 1999  CA  SER A 298     5318   6142   6739   -168    344   -604       C  
ATOM   2000  C   SER A 298      -5.809  78.677 -10.648  1.00 48.27           C  
ANISOU 2000  C   SER A 298     5406   6143   6790   -148    396   -541       C  
ATOM   2001  O   SER A 298      -5.808  79.876 -10.922  1.00 49.06           O  
ANISOU 2001  O   SER A 298     5518   6151   6972   -166    517   -560       O  
ATOM   2002  CB  SER A 298      -3.556  78.496 -11.740  1.00 40.24           C  
ANISOU 2002  CB  SER A 298     4345   5080   5866   -201    458   -641       C  
ATOM   2003  OG  SER A 298      -2.313  77.812 -11.734  1.00 65.54           O  
ANISOU 2003  OG  SER A 298     7495   8332   9077   -223    414   -719       O  
ATOM   2004  N   ILE A 299      -6.889  78.021 -10.243  1.00 41.87           N  
ANISOU 2004  N   ILE A 299     4620   5393   5894   -110    310   -466       N  
ATOM   2005  CA  ILE A 299      -8.163  78.674  -9.998  1.00 37.05           C  
ANISOU 2005  CA  ILE A 299     4042   4758   5277    -86    341   -408       C  
ATOM   2006  C   ILE A 299      -8.730  78.070  -8.736  1.00 39.52           C  
ANISOU 2006  C   ILE A 299     4331   5164   5521    -76    246   -424       C  
ATOM   2007  O   ILE A 299      -8.891  76.853  -8.650  1.00 47.97           O  
ANISOU 2007  O   ILE A 299     5408   6303   6514    -55    149   -382       O  
ATOM   2008  CB  ILE A 299      -9.156  78.420 -11.141  1.00 41.84           C  
ANISOU 2008  CB  ILE A 299     4716   5337   5844    -34    342   -266       C  
ATOM   2009  CG1 ILE A 299      -8.663  79.078 -12.433  1.00 38.06           C  
ANISOU 2009  CG1 ILE A 299     4276   4760   5424    -28    447   -237       C  
ATOM   2010  CG2 ILE A 299     -10.540  78.935 -10.764  1.00 12.64           C  
ANISOU 2010  CG2 ILE A 299     1040   1637   2128     -2    354   -209       C  
ATOM   2011  CD1 ILE A 299      -9.570  78.847 -13.614  1.00 26.82           C  
ANISOU 2011  CD1 ILE A 299     2919   3319   3953     35    444   -105       C  
ATOM   2012  N   PRO A 300      -9.018  78.912  -7.742  1.00 33.87           N  
ANISOU 2012  N   PRO A 300     3591   4446   4832    -89    282   -487       N  
ATOM   2013  CA  PRO A 300      -9.558  78.460  -6.457  1.00 42.41           C  
ANISOU 2013  CA  PRO A 300     4655   5611   5848    -76    205   -508       C  
ATOM   2014  C   PRO A 300     -10.862  77.701  -6.644  1.00 42.09           C  
ANISOU 2014  C   PRO A 300     4659   5599   5735    -33    149   -383       C  
ATOM   2015  O   PRO A 300     -11.640  78.035  -7.537  1.00 38.53           O  
ANISOU 2015  O   PRO A 300     4247   5096   5298    -12    191   -294       O  
ATOM   2016  CB  PRO A 300      -9.823  79.767  -5.715  1.00 20.25           C  
ANISOU 2016  CB  PRO A 300     1830   2765   3098    -95    284   -575       C  
ATOM   2017  CG  PRO A 300      -8.897  80.742  -6.321  1.00 25.83           C  
ANISOU 2017  CG  PRO A 300     2521   3387   3907   -135    390   -643       C  
ATOM   2018  CD  PRO A 300      -8.799  80.365  -7.768  1.00 31.98           C  
ANISOU 2018  CD  PRO A 300     3343   4118   4689   -119    406   -547       C  
ATOM   2019  N   TYR A 301     -11.089  76.689  -5.815  1.00 28.20           N  
ANISOU 2019  N   TYR A 301     2894   3922   3898    -16     60   -380       N  
ATOM   2020  CA  TYR A 301     -12.344  75.957  -5.861  1.00 39.93           C  
ANISOU 2020  CA  TYR A 301     4414   5435   5324     15     15   -276       C  
ATOM   2021  C   TYR A 301     -13.494  76.961  -5.871  1.00 39.66           C  
ANISOU 2021  C   TYR A 301     4393   5355   5321     27     79   -234       C  
ATOM   2022  O   TYR A 301     -13.606  77.791  -4.973  1.00 25.64           O  
ANISOU 2022  O   TYR A 301     2599   3573   3569     19    118   -292       O  
ATOM   2023  CB  TYR A 301     -12.445  75.002  -4.673  1.00 26.93           C  
ANISOU 2023  CB  TYR A 301     2761   3870   3600     31    -60   -296       C  
ATOM   2024  CG  TYR A 301     -13.758  74.267  -4.576  1.00 41.90           C  
ANISOU 2024  CG  TYR A 301     4687   5789   5444     55    -93   -201       C  
ATOM   2025  CD1 TYR A 301     -14.649  74.540  -3.550  1.00 44.14           C  
ANISOU 2025  CD1 TYR A 301     4970   6092   5708     68    -83   -201       C  
ATOM   2026  CD2 TYR A 301     -14.107  73.307  -5.508  1.00 25.59           C  
ANISOU 2026  CD2 TYR A 301     2646   3723   3352     63   -128   -120       C  
ATOM   2027  CE1 TYR A 301     -15.853  73.873  -3.452  1.00 37.12           C  
ANISOU 2027  CE1 TYR A 301     4102   5221   4781     85   -104   -122       C  
ATOM   2028  CE2 TYR A 301     -15.314  72.633  -5.417  1.00 42.03           C  
ANISOU 2028  CE2 TYR A 301     4747   5825   5397     77   -152    -47       C  
ATOM   2029  CZ  TYR A 301     -16.182  72.924  -4.387  1.00 29.70           C  
ANISOU 2029  CZ  TYR A 301     3180   4280   3822     87   -137    -49       C  
ATOM   2030  OH  TYR A 301     -17.382  72.263  -4.289  1.00 45.64           O  
ANISOU 2030  OH  TYR A 301     5211   6317   5814     96   -152     17       O  
ATOM   2031  N   PRO A 302     -14.340  76.903  -6.907  1.00 35.64           N  
ANISOU 2031  N   PRO A 302     3914   4816   4810     51     90   -135       N  
ATOM   2032  CA  PRO A 302     -15.372  77.914  -7.169  1.00 23.01           C  
ANISOU 2032  CA  PRO A 302     2330   3170   3243     75    157    -88       C  
ATOM   2033  C   PRO A 302     -16.390  78.089  -6.053  1.00 34.34           C  
ANISOU 2033  C   PRO A 302     3755   4637   4657     86    151    -87       C  
ATOM   2034  O   PRO A 302     -16.964  79.163  -5.937  1.00 39.53           O  
ANISOU 2034  O   PRO A 302     4416   5253   5352     99    220    -82       O  
ATOM   2035  CB  PRO A 302     -16.066  77.380  -8.423  1.00 44.55           C  
ANISOU 2035  CB  PRO A 302     5086   5896   5945    110    133     14       C  
ATOM   2036  CG  PRO A 302     -15.053  76.513  -9.076  1.00 38.44           C  
ANISOU 2036  CG  PRO A 302     4318   5132   5156     94     90      7       C  
ATOM   2037  CD  PRO A 302     -14.315  75.867  -7.951  1.00 31.39           C  
ANISOU 2037  CD  PRO A 302     3398   4292   4238     63     39    -68       C  
ATOM   2038  N   LEU A 303     -16.614  77.057  -5.247  1.00 43.06           N  
ANISOU 2038  N   LEU A 303     4850   5810   5702     84     79    -89       N  
ATOM   2039  CA  LEU A 303     -17.692  77.084  -4.263  1.00 16.33           C  
ANISOU 2039  CA  LEU A 303     1459   2455   2291     98     75    -74       C  
ATOM   2040  C   LEU A 303     -17.195  77.170  -2.820  1.00 27.85           C  
ANISOU 2040  C   LEU A 303     2902   3949   3729     86     67   -162       C  
ATOM   2041  O   LEU A 303     -16.024  76.929  -2.547  1.00 38.08           O  
ANISOU 2041  O   LEU A 303     4186   5265   5017     70     43   -233       O  
ATOM   2042  CB  LEU A 303     -18.592  75.856  -4.443  1.00 31.89           C  
ANISOU 2042  CB  LEU A 303     3438   4470   4209    112     15      1       C  
ATOM   2043  CG  LEU A 303     -19.685  75.921  -5.511  1.00 25.10           C  
ANISOU 2043  CG  LEU A 303     2582   3594   3360    137     23     86       C  
ATOM   2044  CD1 LEU A 303     -19.659  77.248  -6.252  1.00 35.21           C  
ANISOU 2044  CD1 LEU A 303     3871   4813   4696    156     95     93       C  
ATOM   2045  CD2 LEU A 303     -19.543  74.771  -6.473  1.00 50.54           C  
ANISOU 2045  CD2 LEU A 303     5813   6836   6554    134    -35    128       C  
ATOM   2046  N   PRO A 304     -18.094  77.521  -1.891  1.00 38.91           N  
ANISOU 2046  N   PRO A 304     4301   5363   5119     99     87   -160       N  
ATOM   2047  CA  PRO A 304     -17.728  77.645  -0.474  1.00 44.84           C  
ANISOU 2047  CA  PRO A 304     5042   6154   5842     99     80   -243       C  
ATOM   2048  C   PRO A 304     -17.356  76.309   0.159  1.00 41.29           C  
ANISOU 2048  C   PRO A 304     4602   5774   5312    111      5   -249       C  
ATOM   2049  O   PRO A 304     -16.429  76.261   0.967  1.00 51.82           O  
ANISOU 2049  O   PRO A 304     5925   7147   6619    114    -18   -335       O  
ATOM   2050  CB  PRO A 304     -19.011  78.185   0.178  1.00  9.72           C  
ANISOU 2050  CB  PRO A 304      598   1700   1395    117    120   -212       C  
ATOM   2051  CG  PRO A 304     -19.813  78.751  -0.945  1.00 51.29           C  
ANISOU 2051  CG  PRO A 304     5867   6911   6710    126    164   -136       C  
ATOM   2052  CD  PRO A 304     -19.493  77.915  -2.135  1.00 21.81           C  
ANISOU 2052  CD  PRO A 304     2141   3178   2968    122    121    -86       C  
ATOM   2053  N   LYS A 305     -18.071  75.245  -0.197  1.00 50.12           N  
ANISOU 2053  N   LYS A 305     5741   6908   6394    122    -29   -163       N  
ATOM   2054  CA  LYS A 305     -17.815  73.930   0.386  1.00 50.96           C  
ANISOU 2054  CA  LYS A 305     5869   7069   6426    140    -86   -156       C  
ATOM   2055  C   LYS A 305     -17.903  72.810  -0.646  1.00 34.23           C  
ANISOU 2055  C   LYS A 305     3766   4946   4295    133   -122    -84       C  
ATOM   2056  O   LYS A 305     -18.362  73.016  -1.766  1.00 54.40           O  
ANISOU 2056  O   LYS A 305     6313   7464   6893    118   -109    -35       O  
ATOM   2057  CB  LYS A 305     -18.779  73.660   1.557  1.00 26.84           C  
ANISOU 2057  CB  LYS A 305     2831   4042   3323    165    -74   -135       C  
ATOM   2058  CG  LYS A 305     -20.260  73.791   1.215  1.00 34.04           C  
ANISOU 2058  CG  LYS A 305     3741   4926   4266    160    -39    -57       C  
ATOM   2059  CD  LYS A 305     -20.857  72.465   0.768  1.00 13.49           C  
ANISOU 2059  CD  LYS A 305     1156   2333   1638    157    -65     18       C  
ATOM   2060  CE  LYS A 305     -22.299  72.631   0.308  1.00 34.64           C  
ANISOU 2060  CE  LYS A 305     3815   4991   4355    149    -35     81       C  
ATOM   2061  NZ  LYS A 305     -22.887  71.351  -0.175  1.00 26.81           N1+
ANISOU 2061  NZ  LYS A 305     2831   4008   3349    137    -57    139       N1+
ATOM   2062  N   GLN A 306     -17.459  71.625  -0.250  1.00 36.83           N  
ANISOU 2062  N   GLN A 306     4119   5314   4561    149   -167    -82       N  
ATOM   2063  CA  GLN A 306     -17.562  70.436  -1.086  1.00 34.36           C  
ANISOU 2063  CA  GLN A 306     3827   4998   4232    141   -198    -19       C  
ATOM   2064  C   GLN A 306     -18.074  69.279  -0.237  1.00 32.42           C  
ANISOU 2064  C   GLN A 306     3618   4780   3921    164   -206     16       C  
ATOM   2065  O   GLN A 306     -17.438  68.898   0.743  1.00 51.41           O  
ANISOU 2065  O   GLN A 306     6045   7223   6265    199   -223    -21       O  
ATOM   2066  CB  GLN A 306     -16.198  70.096  -1.699  1.00 13.33           C  
ANISOU 2066  CB  GLN A 306     1162   2340   1563    138   -236    -53       C  
ATOM   2067  CG  GLN A 306     -16.153  68.809  -2.512  1.00 14.07           C  
ANISOU 2067  CG  GLN A 306     1281   2431   1634    133   -270      4       C  
ATOM   2068  CD  GLN A 306     -17.372  68.616  -3.399  1.00 56.29           C  
ANISOU 2068  CD  GLN A 306     6627   7747   7013    111   -256     77       C  
ATOM   2069  NE2 GLN A 306     -17.555  69.510  -4.356  1.00 20.56           N  
ANISOU 2069  NE2 GLN A 306     2078   3191   2544     97   -238     86       N  
ATOM   2070  OE1 GLN A 306     -18.138  67.669  -3.222  1.00 94.83           O  
ANISOU 2070  OE1 GLN A 306    11528  12635  11869    111   -258    122       O  
ATOM   2071  N   ASP A 307     -19.231  68.735  -0.605  1.00 34.48           N  
ANISOU 2071  N   ASP A 307     3884   5022   4194    149   -191     84       N  
ATOM   2072  CA  ASP A 307     -19.851  67.638   0.139  1.00 20.26           C  
ANISOU 2072  CA  ASP A 307     2120   3231   2345    163   -178    122       C  
ATOM   2073  C   ASP A 307     -19.869  66.363  -0.681  1.00 27.40           C  
ANISOU 2073  C   ASP A 307     3046   4123   3243    145   -198    168       C  
ATOM   2074  O   ASP A 307     -20.517  66.310  -1.723  1.00 52.23           O  
ANISOU 2074  O   ASP A 307     6165   7246   6436    111   -200    200       O  
ATOM   2075  CB  ASP A 307     -21.295  67.985   0.514  1.00 29.58           C  
ANISOU 2075  CB  ASP A 307     3286   4400   3554    153   -130    154       C  
ATOM   2076  CG  ASP A 307     -21.392  68.878   1.744  1.00 79.23           C  
ANISOU 2076  CG  ASP A 307     9574  10704   9824    181   -100    115       C  
ATOM   2077  OD1 ASP A 307     -20.418  68.940   2.527  1.00105.24           O  
ANISOU 2077  OD1 ASP A 307    12890  14028  13067    215   -117     64       O  
ATOM   2078  OD2 ASP A 307     -22.454  69.509   1.936  1.00 48.11           O1-
ANISOU 2078  OD2 ASP A 307     5610   6751   5919    174    -60    131       O1-
ATOM   2079  N   LEU A 308     -19.174  65.331  -0.211  1.00 29.12           N  
ANISOU 2079  N   LEU A 308     3310   4355   3398    172   -213    168       N  
ATOM   2080  CA  LEU A 308     -19.270  64.010  -0.833  1.00 38.17           C  
ANISOU 2080  CA  LEU A 308     4487   5482   4536    156   -219    213       C  
ATOM   2081  C   LEU A 308     -20.252  63.143  -0.049  1.00 42.30           C  
ANISOU 2081  C   LEU A 308     5048   5990   5036    161   -166    254       C  
ATOM   2082  O   LEU A 308     -20.081  62.923   1.153  1.00 44.10           O  
ANISOU 2082  O   LEU A 308     5320   6234   5204    209   -142    250       O  
ATOM   2083  CB  LEU A 308     -17.906  63.317  -0.918  1.00 17.28           C  
ANISOU 2083  CB  LEU A 308     1875   2852   1838    187   -259    195       C  
ATOM   2084  CG  LEU A 308     -16.735  64.017  -1.613  1.00 35.78           C  
ANISOU 2084  CG  LEU A 308     4185   5209   4200    185   -304    147       C  
ATOM   2085  CD1 LEU A 308     -16.330  65.291  -0.880  1.00 19.70           C  
ANISOU 2085  CD1 LEU A 308     2118   3201   2168    204   -304     84       C  
ATOM   2086  CD2 LEU A 308     -15.552  63.073  -1.718  1.00 19.20           C  
ANISOU 2086  CD2 LEU A 308     2120   3126   2049    215   -339    139       C  
ATOM   2087  N   ALA A 309     -21.281  62.654  -0.733  1.00 25.88           N  
ANISOU 2087  N   ALA A 309     2949   3880   3004    114   -143    290       N  
ATOM   2088  CA  ALA A 309     -22.316  61.851  -0.091  1.00 34.55           C  
ANISOU 2088  CA  ALA A 309     4074   4953   4101    104    -79    324       C  
ATOM   2089  C   ALA A 309     -22.360  60.422  -0.629  1.00 49.87           C  
ANISOU 2089  C   ALA A 309     6048   6859   6040     79    -65    353       C  
ATOM   2090  O   ALA A 309     -22.490  60.202  -1.833  1.00 39.72           O  
ANISOU 2090  O   ALA A 309     4728   5564   4799     35    -95    353       O  
ATOM   2091  CB  ALA A 309     -23.670  62.515  -0.257  1.00 18.06           C  
ANISOU 2091  CB  ALA A 309     1924   2859   2079     67    -49    329       C  
ATOM   2092  N   ALA A 310     -22.254  59.457   0.278  1.00 47.70           N  
ANISOU 2092  N   ALA A 310     5847   6566   5712    111    -14    378       N  
ATOM   2093  CA  ALA A 310     -22.389  58.048  -0.069  1.00 38.31           C  
ANISOU 2093  CA  ALA A 310     4701   5331   4524     88     22    407       C  
ATOM   2094  C   ALA A 310     -23.863  57.641  -0.088  1.00 28.56           C  
ANISOU 2094  C   ALA A 310     3440   4057   3356     28     95    422       C  
ATOM   2095  O   ALA A 310     -24.526  57.628   0.947  1.00 56.30           O  
ANISOU 2095  O   ALA A 310     6976   7555   6860     44    166    438       O  
ATOM   2096  CB  ALA A 310     -21.615  57.197   0.912  1.00 18.75           C  
ANISOU 2096  CB  ALA A 310     2321   2845   1957    160     55    431       C  
ATOM   2097  N   ILE A 311     -24.367  57.298  -1.267  1.00 33.64           N  
ANISOU 2097  N   ILE A 311     4032   4685   4065    -38     79    411       N  
ATOM   2098  CA  ILE A 311     -25.792  57.037  -1.452  1.00 36.15           C  
ANISOU 2098  CA  ILE A 311     4297   4979   4459   -102    135    406       C  
ATOM   2099  C   ILE A 311     -26.129  55.557  -1.592  1.00 51.22           C  
ANISOU 2099  C   ILE A 311     6246   6826   6390   -145    204    417       C  
ATOM   2100  O   ILE A 311     -25.585  54.864  -2.456  1.00 70.50           O  
ANISOU 2100  O   ILE A 311     8702   9255   8831   -163    172    411       O  
ATOM   2101  CB  ILE A 311     -26.321  57.747  -2.708  1.00 55.63           C  
ANISOU 2101  CB  ILE A 311     6663   7482   6992   -147     69    373       C  
ATOM   2102  CG1 ILE A 311     -25.896  59.221  -2.725  1.00 32.65           C  
ANISOU 2102  CG1 ILE A 311     3720   4620   4065   -106      7    364       C  
ATOM   2103  CG2 ILE A 311     -27.831  57.594  -2.800  1.00 23.33           C  
ANISOU 2103  CG2 ILE A 311     2504   3381   2979   -206    121    356       C  
ATOM   2104  CD1 ILE A 311     -26.755  60.122  -1.872  1.00 36.01           C  
ANISOU 2104  CD1 ILE A 311     4114   5061   4509    -94     46    363       C  
ATOM   2105  N   PRO A 312     -27.039  55.071  -0.740  1.00 59.96           N  
ANISOU 2105  N   PRO A 312     7373   7890   7519   -162    308    431       N  
ATOM   2106  CA  PRO A 312     -27.591  53.717  -0.838  1.00 45.85           C  
ANISOU 2106  CA  PRO A 312     5614   6032   5774   -216    399    434       C  
ATOM   2107  C   PRO A 312     -28.268  53.510  -2.186  1.00 49.45           C  
ANISOU 2107  C   PRO A 312     5973   6496   6318   -302    363    383       C  
ATOM   2108  O   PRO A 312     -28.980  54.401  -2.647  1.00 68.69           O  
ANISOU 2108  O   PRO A 312     8312   8984   8804   -327    316    350       O  
ATOM   2109  CB  PRO A 312     -28.644  53.693   0.272  1.00 42.77           C  
ANISOU 2109  CB  PRO A 312     5232   5609   5410   -223    512    448       C  
ATOM   2110  CG  PRO A 312     -28.184  54.713   1.253  1.00 38.87           C  
ANISOU 2110  CG  PRO A 312     4768   5158   4843   -140    487    471       C  
ATOM   2111  CD  PRO A 312     -27.543  55.793   0.440  1.00 60.77           C  
ANISOU 2111  CD  PRO A 312     7480   8004   7607   -126    356    445       C  
ATOM   2112  N   ASP A 313     -28.036  52.360  -2.811  1.00 59.53           N  
ANISOU 2112  N   ASP A 313     7281   7728   7610   -340    383    374       N  
ATOM   2113  CA  ASP A 313     -28.702  52.009  -4.067  1.00 62.30           C  
ANISOU 2113  CA  ASP A 313     7543   8087   8042   -422    354    316       C  
ATOM   2114  C   ASP A 313     -28.421  52.992  -5.200  1.00 42.13           C  
ANISOU 2114  C   ASP A 313     4911   5613   5485   -412    220    288       C  
ATOM   2115  O   ASP A 313     -29.196  53.091  -6.150  1.00 57.91           O  
ANISOU 2115  O   ASP A 313     6813   7644   7546   -465    184    235       O  
ATOM   2116  CB  ASP A 313     -30.214  51.891  -3.856  1.00 69.66           C  
ANISOU 2116  CB  ASP A 313     8396   9002   9067   -493    434    277       C  
ATOM   2117  CG  ASP A 313     -30.584  50.794  -2.882  1.00 95.95           C  
ANISOU 2117  CG  ASP A 313    11803  12237  12415   -515    586    299       C  
ATOM   2118  OD1 ASP A 313     -29.855  49.781  -2.826  1.00 96.50           O  
ANISOU 2118  OD1 ASP A 313    11970  12246  12451   -504    629    326       O  
ATOM   2119  OD2 ASP A 313     -31.606  50.942  -2.178  1.00 93.35           O1-
ANISOU 2119  OD2 ASP A 313    11441  11892  12137   -540    669    292       O1-
ATOM   2120  N   PHE A 314     -27.319  53.724  -5.099  1.00 39.30           N  
ANISOU 2120  N   PHE A 314     4592   5288   5054   -342    151    320       N  
ATOM   2121  CA  PHE A 314     -26.926  54.629  -6.168  1.00 49.07           C  
ANISOU 2121  CA  PHE A 314     5772   6588   6284   -326     39    301       C  
ATOM   2122  C   PHE A 314     -26.549  53.814  -7.405  1.00 43.10           C  
ANISOU 2122  C   PHE A 314     5014   5823   5537   -359     -2    276       C  
ATOM   2123  O   PHE A 314     -25.935  52.752  -7.293  1.00 56.93           O  
ANISOU 2123  O   PHE A 314     6842   7524   7265   -363     35    292       O  
ATOM   2124  CB  PHE A 314     -25.770  55.520  -5.715  1.00 49.92           C  
ANISOU 2124  CB  PHE A 314     5926   6722   6319   -250     -8    334       C  
ATOM   2125  CG  PHE A 314     -25.540  56.710  -6.595  1.00 57.89           C  
ANISOU 2125  CG  PHE A 314     6875   7789   7331   -230    -99    318       C  
ATOM   2126  CD1 PHE A 314     -26.446  57.759  -6.624  1.00 52.14           C  
ANISOU 2126  CD1 PHE A 314     6071   7100   6641   -231   -109    304       C  
ATOM   2127  CD2 PHE A 314     -24.413  56.786  -7.385  1.00 24.67           C  
ANISOU 2127  CD2 PHE A 314     2692   3594   3089   -205   -164    320       C  
ATOM   2128  CE1 PHE A 314     -26.230  58.858  -7.431  1.00 47.95           C  
ANISOU 2128  CE1 PHE A 314     5496   6613   6108   -203   -180    297       C  
ATOM   2129  CE2 PHE A 314     -24.195  57.894  -8.192  1.00 27.71           C  
ANISOU 2129  CE2 PHE A 314     3030   4021   3476   -183   -232    311       C  
ATOM   2130  CZ  PHE A 314     -25.099  58.923  -8.215  1.00 39.34           C  
ANISOU 2130  CZ  PHE A 314     4436   5527   4984   -180   -237    301       C  
ATOM   2131  N   GLN A 315     -26.916  54.314  -8.582  1.00 60.16           N  
ANISOU 2131  N   GLN A 315     7093   8036   7728   -377    -76    239       N  
ATOM   2132  CA  GLN A 315     -26.822  53.527  -9.807  1.00 38.83           C  
ANISOU 2132  CA  GLN A 315     4377   5333   5044   -415   -112    203       C  
ATOM   2133  C   GLN A 315     -26.044  54.217 -10.935  1.00 71.42           C  
ANISOU 2133  C   GLN A 315     8492   9510   9135   -375   -214    203       C  
ATOM   2134  O   GLN A 315     -26.203  53.860 -12.103  1.00 73.53           O  
ANISOU 2134  O   GLN A 315     8723   9797   9418   -400   -259    164       O  
ATOM   2135  CB  GLN A 315     -28.232  53.193 -10.306  1.00 28.73           C  
ANISOU 2135  CB  GLN A 315     3002   4072   3844   -484    -95    138       C  
ATOM   2136  CG  GLN A 315     -29.146  52.582  -9.251  1.00 46.31           C  
ANISOU 2136  CG  GLN A 315     5227   6246   6122   -532     19    131       C  
ATOM   2137  CD  GLN A 315     -28.923  51.091  -9.073  1.00 58.55           C  
ANISOU 2137  CD  GLN A 315     6848   7712   7686   -579    102    127       C  
ATOM   2138  NE2 GLN A 315     -28.917  50.638  -7.828  1.00 70.28           N  
ANISOU 2138  NE2 GLN A 315     8407   9132   9164   -574    207    169       N  
ATOM   2139  OE1 GLN A 315     -28.766  50.355 -10.046  1.00 53.83           O  
ANISOU 2139  OE1 GLN A 315     6243   7107   7102   -616     76     88       O  
ATOM   2140  N   SER A 316     -25.203  55.190 -10.596  1.00 60.94           N  
ANISOU 2140  N   SER A 316     7196   8200   7760   -313   -245    241       N  
ATOM   2141  CA  SER A 316     -24.523  55.980 -11.621  1.00 55.06           C  
ANISOU 2141  CA  SER A 316     6438   7494   6988   -273   -326    243       C  
ATOM   2142  C   SER A 316     -23.161  55.457 -12.086  1.00 93.28           C  
ANISOU 2142  C   SER A 316    11347  12311  11782   -254   -353    259       C  
ATOM   2143  O   SER A 316     -22.969  55.258 -13.288  1.00144.34           O  
ANISOU 2143  O   SER A 316    17802  18793  18247   -259   -401    241       O  
ATOM   2144  CB  SER A 316     -24.413  57.448 -11.217  1.00100.03           C  
ANISOU 2144  CB  SER A 316    12114  13221  12671   -222   -344    264       C  
ATOM   2145  OG  SER A 316     -25.668  58.100 -11.349  1.00116.64           O  
ANISOU 2145  OG  SER A 316    14137  15364  14817   -229   -346    244       O  
ATOM   2146  N   GLY A 317     -22.217  55.223 -11.173  1.00 68.20           N  
ANISOU 2146  N   GLY A 317     8243   9103   8566   -226   -324    290       N  
ATOM   2147  CA  GLY A 317     -22.422  55.337  -9.745  1.00 33.82           C  
ANISOU 2147  CA  GLY A 317     3914   4733   4204   -213   -265    310       C  
ATOM   2148  C   GLY A 317     -21.737  56.529  -9.098  1.00 56.23           C  
ANISOU 2148  C   GLY A 317     6759   7597   7008   -156   -285    326       C  
ATOM   2149  O   GLY A 317     -21.647  56.598  -7.873  1.00 63.85           O  
ANISOU 2149  O   GLY A 317     7757   8552   7950   -132   -243    341       O  
ATOM   2150  N   ALA A 318     -21.260  57.474  -9.904  1.00 46.01           N  
ANISOU 2150  N   ALA A 318     5437   6333   5713   -134   -342    319       N  
ATOM   2151  CA  ALA A 318     -20.771  58.746  -9.364  1.00 45.68           C  
ANISOU 2151  CA  ALA A 318     5387   6312   5657    -92   -352    322       C  
ATOM   2152  C   ALA A 318     -21.270  59.941 -10.181  1.00 26.09           C  
ANISOU 2152  C   ALA A 318     2853   3852   3208    -87   -371    313       C  
ATOM   2153  O   ALA A 318     -21.473  59.832 -11.382  1.00 53.89           O  
ANISOU 2153  O   ALA A 318     6366   7370   6740    -99   -386    306       O  
ATOM   2154  CB  ALA A 318     -19.260  58.748  -9.276  1.00 14.96           C  
ANISOU 2154  CB  ALA A 318     1547   2413   1724    -57   -367    321       C  
ATOM   2155  N   MET A 319     -21.475  61.076  -9.523  1.00 28.69           N  
ANISOU 2155  N   MET A 319     3163   4193   3544    -64   -354    312       N  
ATOM   2156  CA  MET A 319     -22.000  62.257 -10.199  1.00 17.36           C  
ANISOU 2156  CA  MET A 319     1697   2766   2134    -51   -351    309       C  
ATOM   2157  C   MET A 319     -21.288  63.537  -9.779  1.00 20.19           C  
ANISOU 2157  C   MET A 319     2069   3115   2487    -19   -332    303       C  
ATOM   2158  O   MET A 319     -20.887  63.691  -8.630  1.00 42.17           O  
ANISOU 2158  O   MET A 319     4862   5903   5257     -8   -321    296       O  
ATOM   2159  CB  MET A 319     -23.503  62.384  -9.973  1.00 39.13           C  
ANISOU 2159  CB  MET A 319     4384   5555   4928    -64   -349    309       C  
ATOM   2160  CG  MET A 319     -24.124  63.554 -10.682  1.00 53.89           C  
ANISOU 2160  CG  MET A 319     6221   7440   6814    -37   -350    310       C  
ATOM   2161  SD  MET A 319     -23.766  63.544 -12.440  1.00 43.00           S  
ANISOU 2161  SD  MET A 319     4864   6055   5419    -22   -378    308       S  
ATOM   2162  CE  MET A 319     -24.645  65.020 -12.933  1.00 63.75           C  
ANISOU 2162  CE  MET A 319     7446   8713   8062     28   -376    317       C  
ATOM   2163  N   GLU A 320     -21.156  64.461 -10.724  1.00 67.63           N  
ANISOU 2163  N   GLU A 320     8075   9114   8506      0   -331    304       N  
ATOM   2164  CA  GLU A 320     -20.285  65.624 -10.575  1.00 51.75           C  
ANISOU 2164  CA  GLU A 320     6076   7088   6499     25   -314    293       C  
ATOM   2165  C   GLU A 320     -21.000  66.838  -9.997  1.00 28.55           C  
ANISOU 2165  C   GLU A 320     3097   4164   3586     47   -297    295       C  
ATOM   2166  O   GLU A 320     -20.501  67.956 -10.099  1.00 55.71           O  
ANISOU 2166  O   GLU A 320     6534   7591   7042     71   -282    288       O  
ATOM   2167  CB  GLU A 320     -19.711  65.984 -11.948  1.00 40.29           C  
ANISOU 2167  CB  GLU A 320     4641   5616   5050     39   -318    298       C  
ATOM   2168  CG  GLU A 320     -20.759  66.579 -12.886  1.00104.55           C  
ANISOU 2168  CG  GLU A 320    12749  13773  13203     64   -325    319       C  
ATOM   2169  CD  GLU A 320     -21.656  65.535 -13.519  1.00159.66           C  
ANISOU 2169  CD  GLU A 320    19714  20777  20173     47   -352    323       C  
ATOM   2170  OE1 GLU A 320     -21.525  64.346 -13.152  1.00158.76           O  
ANISOU 2170  OE1 GLU A 320    19613  20658  20049     11   -361    314       O  
ATOM   2171  OE2 GLU A 320     -22.493  65.898 -14.377  1.00212.34           O1-
ANISOU 2171  OE2 GLU A 320    26357  27476  26848     74   -367    332       O1-
ATOM   2172  N   ASN A 321     -22.166  66.621  -9.396  1.00 36.46           N  
ANISOU 2172  N   ASN A 321     4063   5192   4599     40   -295    304       N  
ATOM   2173  CA  ASN A 321     -22.974  67.715  -8.863  1.00 44.20           C  
ANISOU 2173  CA  ASN A 321     4999   6188   5608     63   -275    308       C  
ATOM   2174  C   ASN A 321     -22.129  68.789  -8.193  1.00 39.05           C  
ANISOU 2174  C   ASN A 321     4352   5521   4964     83   -253    287       C  
ATOM   2175  O   ASN A 321     -21.333  68.501  -7.299  1.00 47.65           O  
ANISOU 2175  O   ASN A 321     5461   6609   6033     74   -253    262       O  
ATOM   2176  CB  ASN A 321     -24.015  67.188  -7.878  1.00 42.63           C  
ANISOU 2176  CB  ASN A 321     4762   6016   5419     46   -266    310       C  
ATOM   2177  CG  ASN A 321     -24.813  66.033  -8.439  1.00 39.03           C  
ANISOU 2177  CG  ASN A 321     4284   5576   4968     17   -287    317       C  
ATOM   2178  ND2 ASN A 321     -24.663  64.866  -7.823  1.00 44.88           N  
ANISOU 2178  ND2 ASN A 321     5052   6307   5692    -15   -279    314       N  
ATOM   2179  OD1 ASN A 321     -25.558  66.183  -9.410  1.00 44.74           O  
ANISOU 2179  OD1 ASN A 321     4978   6317   5706     24   -301    321       O  
ATOM   2180  N   TRP A 322     -22.310  70.029  -8.628  1.00 39.81           N  
ANISOU 2180  N   TRP A 322     4429   5607   5089    114   -231    294       N  
ATOM   2181  CA  TRP A 322     -21.482  71.134  -8.160  1.00 21.62           C  
ANISOU 2181  CA  TRP A 322     2141   3273   2802    125   -192    264       C  
ATOM   2182  C   TRP A 322     -21.620  71.353  -6.650  1.00 42.58           C  
ANISOU 2182  C   TRP A 322     4793   5935   5452    116   -165    234       C  
ATOM   2183  O   TRP A 322     -22.696  71.686  -6.155  1.00 41.24           O  
ANISOU 2183  O   TRP A 322     4601   5775   5293    124   -142    247       O  
ATOM   2184  CB  TRP A 322     -21.827  72.408  -8.935  1.00 31.81           C  
ANISOU 2184  CB  TRP A 322     3423   4539   4125    163   -154    284       C  
ATOM   2185  CG  TRP A 322     -20.624  73.228  -9.312  1.00 43.08           C  
ANISOU 2185  CG  TRP A 322     4875   5919   5573    169   -120    261       C  
ATOM   2186  CD1 TRP A 322     -19.321  72.958  -9.011  1.00 30.48           C  
ANISOU 2186  CD1 TRP A 322     3296   4312   3974    142   -127    217       C  
ATOM   2187  CD2 TRP A 322     -20.618  74.453 -10.057  1.00 38.69           C  
ANISOU 2187  CD2 TRP A 322     4330   5320   5049    207    -66    278       C  
ATOM   2188  CE2 TRP A 322     -19.278  74.870 -10.162  1.00 49.72           C  
ANISOU 2188  CE2 TRP A 322     5749   6673   6469    190    -34    239       C  
ATOM   2189  CE3 TRP A 322     -21.616  75.237 -10.638  1.00 47.62           C  
ANISOU 2189  CE3 TRP A 322     5456   6446   6192    258    -36    322       C  
ATOM   2190  NE1 TRP A 322     -18.507  73.941  -9.515  1.00 41.23           N  
ANISOU 2190  NE1 TRP A 322     4671   5624   5372    150    -78    198       N  
ATOM   2191  CZ2 TRP A 322     -18.911  76.036 -10.831  1.00 38.77           C  
ANISOU 2191  CZ2 TRP A 322     4384   5226   5121    217     37    244       C  
ATOM   2192  CZ3 TRP A 322     -21.249  76.390 -11.301  1.00 51.60           C  
ANISOU 2192  CZ3 TRP A 322     5988   6893   6724    296     31    334       C  
ATOM   2193  CH2 TRP A 322     -19.910  76.779 -11.393  1.00 36.22           C  
ANISOU 2193  CH2 TRP A 322     4067   4892   4804    272     72    296       C  
ATOM   2194  N   GLY A 323     -20.524  71.146  -5.924  1.00 32.98           N  
ANISOU 2194  N   GLY A 323     3597   4719   4215    104   -171    191       N  
ATOM   2195  CA  GLY A 323     -20.499  71.340  -4.484  1.00 33.56           C  
ANISOU 2195  CA  GLY A 323     3674   4806   4272    105   -151    155       C  
ATOM   2196  C   GLY A 323     -21.109  70.205  -3.677  1.00 54.93           C  
ANISOU 2196  C   GLY A 323     6393   7541   6938    100   -164    174       C  
ATOM   2197  O   GLY A 323     -21.043  70.204  -2.445  1.00 33.18           O  
ANISOU 2197  O   GLY A 323     3651   4802   4155    110   -149    148       O  
ATOM   2198  N   LEU A 324     -21.702  69.238  -4.369  1.00 50.46           N  
ANISOU 2198  N   LEU A 324     5825   6980   6369     86   -186    216       N  
ATOM   2199  CA  LEU A 324     -22.339  68.100  -3.717  1.00 31.13           C  
ANISOU 2199  CA  LEU A 324     3390   4546   3893     76   -183    236       C  
ATOM   2200  C   LEU A 324     -22.299  66.865  -4.611  1.00 35.95           C  
ANISOU 2200  C   LEU A 324     4010   5155   4495     54   -216    261       C  
ATOM   2201  O   LEU A 324     -23.321  66.455  -5.170  1.00 36.51           O  
ANISOU 2201  O   LEU A 324     4054   5229   4590     35   -215    285       O  
ATOM   2202  CB  LEU A 324     -23.784  68.441  -3.348  1.00 44.38           C  
ANISOU 2202  CB  LEU A 324     5035   6228   5598     74   -145    256       C  
ATOM   2203  CG  LEU A 324     -24.675  67.312  -2.827  1.00 19.34           C  
ANISOU 2203  CG  LEU A 324     1869   3062   2417     54   -125    279       C  
ATOM   2204  CD1 LEU A 324     -24.095  66.713  -1.555  1.00 40.65           C  
ANISOU 2204  CD1 LEU A 324     4623   5761   5061     69   -107    269       C  
ATOM   2205  CD2 LEU A 324     -26.093  67.817  -2.601  1.00 23.23           C  
ANISOU 2205  CD2 LEU A 324     2316   3561   2950     52    -87    292       C  
ATOM   2206  N   THR A 325     -21.115  66.273  -4.746  1.00 37.65           N  
ANISOU 2206  N   THR A 325     4260   5368   4678     57   -244    248       N  
ATOM   2207  CA  THR A 325     -20.948  65.070  -5.554  1.00 25.49           C  
ANISOU 2207  CA  THR A 325     2736   3822   3126     38   -272    268       C  
ATOM   2208  C   THR A 325     -21.550  63.841  -4.868  1.00 47.71           C  
ANISOU 2208  C   THR A 325     5576   6632   5918     24   -248    287       C  
ATOM   2209  O   THR A 325     -21.552  63.738  -3.640  1.00 34.25           O  
ANISOU 2209  O   THR A 325     3900   4932   4183     43   -218    284       O  
ATOM   2210  CB  THR A 325     -19.466  64.800  -5.916  1.00 26.15           C  
ANISOU 2210  CB  THR A 325     2852   3901   3182     48   -303    248       C  
ATOM   2211  CG2 THR A 325     -18.904  65.941  -6.729  1.00 42.67           C  
ANISOU 2211  CG2 THR A 325     4936   5973   5303     51   -296    228       C  
ATOM   2212  OG1 THR A 325     -18.687  64.644  -4.727  1.00 52.94           O  
ANISOU 2212  OG1 THR A 325     6274   7311   6530     75   -301    223       O  
ATOM   2213  N   THR A 326     -22.067  62.913  -5.667  1.00 27.79           N  
ANISOU 2213  N   THR A 326     3047   4099   3411     -7   -256    306       N  
ATOM   2214  CA  THR A 326     -22.686  61.712  -5.134  1.00 32.77           C  
ANISOU 2214  CA  THR A 326     3703   4714   4035    -29   -219    322       C  
ATOM   2215  C   THR A 326     -22.006  60.445  -5.647  1.00 50.35           C  
ANISOU 2215  C   THR A 326     5973   6921   6237    -41   -235    329       C  
ATOM   2216  O   THR A 326     -21.465  60.421  -6.749  1.00 62.52           O  
ANISOU 2216  O   THR A 326     7506   8466   7783    -46   -280    324       O  
ATOM   2217  CB  THR A 326     -24.191  61.667  -5.443  1.00 21.43           C  
ANISOU 2217  CB  THR A 326     2210   3280   2653    -66   -195    325       C  
ATOM   2218  CG2 THR A 326     -24.929  62.667  -4.584  1.00 15.19           C  
ANISOU 2218  CG2 THR A 326     1391   2502   1878    -50   -160    324       C  
ATOM   2219  OG1 THR A 326     -24.412  61.981  -6.824  1.00 34.31           O  
ANISOU 2219  OG1 THR A 326     3792   4928   4315    -78   -242    318       O  
ATOM   2220  N   TYR A 327     -22.037  59.395  -4.835  1.00 36.99           N  
ANISOU 2220  N   TYR A 327     4334   5206   4516    -39   -190    345       N  
ATOM   2221  CA  TYR A 327     -21.344  58.158  -5.149  1.00 27.60           C  
ANISOU 2221  CA  TYR A 327     3198   3991   3297    -41   -193    355       C  
ATOM   2222  C   TYR A 327     -22.143  56.940  -4.700  1.00 49.70           C  
ANISOU 2222  C   TYR A 327     6030   6748   6105    -70   -122    374       C  
ATOM   2223  O   TYR A 327     -23.017  57.042  -3.841  1.00 33.70           O  
ANISOU 2223  O   TYR A 327     3999   4713   4092    -74    -65    382       O  
ATOM   2224  CB  TYR A 327     -19.992  58.119  -4.445  1.00 33.19           C  
ANISOU 2224  CB  TYR A 327     3964   4711   3935     20   -208    355       C  
ATOM   2225  CG  TYR A 327     -19.019  59.197  -4.852  1.00 36.35           C  
ANISOU 2225  CG  TYR A 327     4335   5145   4330     43   -268    327       C  
ATOM   2226  CD1 TYR A 327     -18.126  58.995  -5.892  1.00 60.62           C  
ANISOU 2226  CD1 TYR A 327     7410   8219   7404     40   -314    319       C  
ATOM   2227  CD2 TYR A 327     -18.975  60.409  -4.177  1.00 57.17           C  
ANISOU 2227  CD2 TYR A 327     6946   7810   6967     67   -269    304       C  
ATOM   2228  CE1 TYR A 327     -17.223  59.978  -6.256  1.00 69.12           C  
ANISOU 2228  CE1 TYR A 327     8465   9309   8489     54   -339    286       C  
ATOM   2229  CE2 TYR A 327     -18.081  61.396  -4.533  1.00 53.81           C  
ANISOU 2229  CE2 TYR A 327     6493   7405   6547     82   -309    271       C  
ATOM   2230  CZ  TYR A 327     -17.210  61.183  -5.562  1.00 53.78           C  
ANISOU 2230  CZ  TYR A 327     6494   7388   6551     73   -334    261       C  
ATOM   2231  OH  TYR A 327     -16.331  62.189  -5.884  1.00 53.92           O  
ANISOU 2231  OH  TYR A 327     6497   7404   6588     78   -334    220       O  
ATOM   2232  N   ARG A 328     -21.835  55.791  -5.297  1.00 33.53           N  
ANISOU 2232  N   ARG A 328     4017   4668   4053    -90   -118    380       N  
ATOM   2233  CA  ARG A 328     -22.282  54.501  -4.793  1.00 47.72           C  
ANISOU 2233  CA  ARG A 328     5869   6411   5850   -109    -37    400       C  
ATOM   2234  C   ARG A 328     -21.455  54.224  -3.543  1.00 62.08           C  
ANISOU 2234  C   ARG A 328     7776   8224   7589    -33     -4    430       C  
ATOM   2235  O   ARG A 328     -20.270  54.550  -3.510  1.00 32.41           O  
ANISOU 2235  O   ARG A 328     4040   4498   3777     21    -59    427       O  
ATOM   2236  CB  ARG A 328     -22.030  53.412  -5.837  1.00 23.67           C  
ANISOU 2236  CB  ARG A 328     2840   3333   2820   -146    -45    394       C  
ATOM   2237  CG  ARG A 328     -20.558  53.183  -6.131  1.00 44.60           C  
ANISOU 2237  CG  ARG A 328     5543   5992   5410    -97    -95    404       C  
ATOM   2238  CD  ARG A 328     -20.338  52.117  -7.192  1.00 67.17           C  
ANISOU 2238  CD  ARG A 328     8421   8817   8285   -134   -101    397       C  
ATOM   2239  NE  ARG A 328     -18.938  51.701  -7.243  1.00 81.20           N  
ANISOU 2239  NE  ARG A 328    10262  10592   9998    -79   -129    414       N  
ATOM   2240  CZ  ARG A 328     -17.998  52.312  -7.958  1.00 68.06           C  
ANISOU 2240  CZ  ARG A 328     8575   8967   8317    -56   -207    400       C  
ATOM   2241  NH1 ARG A 328     -18.303  53.372  -8.697  1.00 84.09           N1+
ANISOU 2241  NH1 ARG A 328    10529  11035  10386    -80   -261    375       N1+
ATOM   2242  NH2 ARG A 328     -16.749  51.862  -7.936  1.00 57.52           N  
ANISOU 2242  NH2 ARG A 328     7296   7633   6928     -5   -226    411       N  
ATOM   2243  N   GLU A 329     -22.067  53.628  -2.520  1.00 38.23           N  
ANISOU 2243  N   GLU A 329     4804   5163   4558    -25     88    455       N  
ATOM   2244  CA  GLU A 329     -21.399  53.498  -1.221  1.00 33.49           C  
ANISOU 2244  CA  GLU A 329     4288   4567   3869     63    121    485       C  
ATOM   2245  C   GLU A 329     -20.026  52.824  -1.287  1.00 50.44           C  
ANISOU 2245  C   GLU A 329     6506   6717   5942    126     91    498       C  
ATOM   2246  O   GLU A 329     -19.138  53.134  -0.491  1.00 37.25           O  
ANISOU 2246  O   GLU A 329     4874   5088   4192    211     66    501       O  
ATOM   2247  CB  GLU A 329     -22.290  52.786  -0.206  1.00 35.89           C  
ANISOU 2247  CB  GLU A 329     4649   4815   4173     66    241    518       C  
ATOM   2248  CG  GLU A 329     -23.566  53.536   0.131  1.00 83.88           C  
ANISOU 2248  CG  GLU A 329    10660  10898  10312     22    276    505       C  
ATOM   2249  CD  GLU A 329     -24.207  53.054   1.420  1.00 95.80           C  
ANISOU 2249  CD  GLU A 329    12239  12362  11799     51    395    541       C  
ATOM   2250  OE1 GLU A 329     -23.937  51.904   1.828  1.00 65.52           O  
ANISOU 2250  OE1 GLU A 329     8500   8471   7924     82    471    578       O  
ATOM   2251  OE2 GLU A 329     -24.977  53.828   2.024  1.00112.78           O1-
ANISOU 2251  OE2 GLU A 329    14352  14530  13970     47    419    535       O1-
ATOM   2252  N   SER A 330     -19.856  51.908  -2.234  1.00 51.61           N  
ANISOU 2252  N   SER A 330     6668   6826   6115     87     92    501       N  
ATOM   2253  CA  SER A 330     -18.593  51.193  -2.385  1.00 53.10           C  
ANISOU 2253  CA  SER A 330     6923   7013   6238    145     68    516       C  
ATOM   2254  C   SER A 330     -17.485  52.058  -2.993  1.00 60.63           C  
ANISOU 2254  C   SER A 330     7828   8034   7174    168    -43    482       C  
ATOM   2255  O   SER A 330     -16.309  51.702  -2.936  1.00 67.37           O  
ANISOU 2255  O   SER A 330     8726   8905   7965    232    -74    486       O  
ATOM   2256  CB  SER A 330     -18.788  49.920  -3.215  1.00 40.74           C  
ANISOU 2256  CB  SER A 330     5391   5379   4710     92    112    527       C  
ATOM   2257  OG  SER A 330     -19.247  50.205  -4.526  1.00 59.65           O  
ANISOU 2257  OG  SER A 330     7700   7779   7184      5     61    490       O  
ATOM   2258  N   ALA A 331     -17.865  53.195  -3.569  1.00 45.95           N  
ANISOU 2258  N   ALA A 331     5879   6209   5371    121    -97    448       N  
ATOM   2259  CA  ALA A 331     -16.905  54.092  -4.208  1.00 45.39           C  
ANISOU 2259  CA  ALA A 331     5760   6190   5297    134   -186    415       C  
ATOM   2260  C   ALA A 331     -16.430  55.198  -3.270  1.00 60.78           C  
ANISOU 2260  C   ALA A 331     7690   8195   7208    190   -213    390       C  
ATOM   2261  O   ALA A 331     -15.715  56.108  -3.687  1.00 63.11           O  
ANISOU 2261  O   ALA A 331     7937   8530   7512    195   -274    354       O  
ATOM   2262  CB  ALA A 331     -17.511  54.702  -5.464  1.00 29.13           C  
ANISOU 2262  CB  ALA A 331     3621   4132   3316     60   -223    394       C  
ATOM   2263  N   LEU A 332     -16.822  55.118  -2.005  1.00 43.07           N  
ANISOU 2263  N   LEU A 332     5486   5953   4924    232   -162    407       N  
ATOM   2264  CA  LEU A 332     -16.551  56.201  -1.071  1.00 33.04           C  
ANISOU 2264  CA  LEU A 332     4194   4738   3622    279   -183    376       C  
ATOM   2265  C   LEU A 332     -16.218  55.661   0.316  1.00 52.79           C  
ANISOU 2265  C   LEU A 332     6775   7255   6029    371   -145    394       C  
ATOM   2266  O   LEU A 332     -15.288  56.130   0.971  1.00 51.97           O  
ANISOU 2266  O   LEU A 332     6673   7211   5862    442   -187    359       O  
ATOM   2267  CB  LEU A 332     -17.760  57.133  -1.000  1.00 48.12           C  
ANISOU 2267  CB  LEU A 332     6045   6643   5595    227   -162    369       C  
ATOM   2268  CG  LEU A 332     -17.539  58.551  -0.473  1.00 36.56           C  
ANISOU 2268  CG  LEU A 332     4531   5229   4129    249   -194    325       C  
ATOM   2269  CD1 LEU A 332     -16.482  59.257  -1.302  1.00 37.16           C  
ANISOU 2269  CD1 LEU A 332     4561   5336   4223    243   -266    280       C  
ATOM   2270  CD2 LEU A 332     -18.846  59.328  -0.487  1.00 38.44           C  
ANISOU 2270  CD2 LEU A 332     4718   5454   4433    198   -163    328       C  
ATOM   2271  N   LEU A 333     -16.981  54.665   0.755  1.00 45.61           N  
ANISOU 2271  N   LEU A 333     5932   6291   5108    373    -61    445       N  
ATOM   2272  CA  LEU A 333     -16.784  54.080   2.073  1.00 40.71           C  
ANISOU 2272  CA  LEU A 333     5402   5674   4391    470     -8    475       C  
ATOM   2273  C   LEU A 333     -15.783  52.931   2.035  1.00 54.63           C  
ANISOU 2273  C   LEU A 333     7245   7430   6083    539     -7    501       C  
ATOM   2274  O   LEU A 333     -15.726  52.175   1.062  1.00 51.19           O  
ANISOU 2274  O   LEU A 333     6817   6947   5687    491     -1    518       O  
ATOM   2275  CB  LEU A 333     -18.115  53.605   2.647  1.00 41.40           C  
ANISOU 2275  CB  LEU A 333     5530   5699   4503    444    101    521       C  
ATOM   2276  CG  LEU A 333     -19.220  54.661   2.627  1.00 40.81           C  
ANISOU 2276  CG  LEU A 333     5373   5627   4506    373    107    499       C  
ATOM   2277  CD1 LEU A 333     -20.417  54.172   3.414  1.00 44.44           C  
ANISOU 2277  CD1 LEU A 333     5878   6030   4976    364    222    540       C  
ATOM   2278  CD2 LEU A 333     -18.705  55.988   3.186  1.00 24.68           C  
ANISOU 2278  CD2 LEU A 333     3286   3663   2430    418     40    450       C  
ATOM   2279  N   PHE A 334     -15.000  52.807   3.105  1.00 58.90           N  
ANISOU 2279  N   PHE A 334     7845   8021   6514    658    -13    501       N  
ATOM   2280  CA  PHE A 334     -13.938  51.805   3.186  1.00 39.81           C  
ANISOU 2280  CA  PHE A 334     5502   5612   4012    748    -20    522       C  
ATOM   2281  C   PHE A 334     -13.908  51.124   4.546  1.00 68.60           C  
ANISOU 2281  C   PHE A 334     9263   9260   7544    874     51    568       C  
ATOM   2282  O   PHE A 334     -13.852  51.789   5.582  1.00 60.65           O  
ANISOU 2282  O   PHE A 334     8255   8315   6474    943     38    545       O  
ATOM   2283  CB  PHE A 334     -12.584  52.454   2.915  1.00 39.69           C  
ANISOU 2283  CB  PHE A 334     5427   5687   3967    789   -133    455       C  
ATOM   2284  CG  PHE A 334     -11.416  51.555   3.180  1.00 36.33           C  
ANISOU 2284  CG  PHE A 334     5067   5289   3449    902   -147    463       C  
ATOM   2285  CD1 PHE A 334     -11.047  50.590   2.261  1.00 59.85           C  
ANISOU 2285  CD1 PHE A 334     8072   8214   6456    880   -134    488       C  
ATOM   2286  CD2 PHE A 334     -10.675  51.683   4.343  1.00 43.46           C  
ANISOU 2286  CD2 PHE A 334     5996   6271   4245   1035   -169    434       C  
ATOM   2287  CE1 PHE A 334      -9.967  49.764   2.496  1.00 48.35           C  
ANISOU 2287  CE1 PHE A 334     6669   6778   4925    989   -139    490       C  
ATOM   2288  CE2 PHE A 334      -9.593  50.857   4.585  1.00 68.64           C  
ANISOU 2288  CE2 PHE A 334     9237   9489   7356   1151   -179    434       C  
ATOM   2289  CZ  PHE A 334      -9.240  49.896   3.659  1.00 61.88           C  
ANISOU 2289  CZ  PHE A 334     8407   8573   6530   1128   -162    465       C  
ATOM   2290  N   ASP A 335     -13.935  49.794   4.536  1.00103.59           N  
ANISOU 2290  N   ASP A 335    13795  13621  11944    908    132    634       N  
ATOM   2291  CA  ASP A 335     -13.894  49.006   5.764  1.00101.88           C  
ANISOU 2291  CA  ASP A 335    13705  13392  11611   1039    217    692       C  
ATOM   2292  C   ASP A 335     -12.556  48.278   5.876  1.00109.45           C  
ANISOU 2292  C   ASP A 335    14729  14395  12462   1167    179    701       C  
ATOM   2293  O   ASP A 335     -11.942  47.942   4.865  1.00122.53           O  
ANISOU 2293  O   ASP A 335    16358  16043  14155   1129    133    689       O  
ATOM   2294  CB  ASP A 335     -15.046  47.995   5.776  1.00 98.96           C  
ANISOU 2294  CB  ASP A 335    13416  12894  11289    987    365    765       C  
ATOM   2295  CG  ASP A 335     -15.372  47.491   7.172  1.00125.52           C  
ANISOU 2295  CG  ASP A 335    16904  16235  14552   1106    476    826       C  
ATOM   2296  OD1 ASP A 335     -14.743  47.962   8.143  1.00136.21           O  
ANISOU 2296  OD1 ASP A 335    18280  17683  15793   1233    428    809       O  
ATOM   2297  OD2 ASP A 335     -16.265  46.628   7.295  1.00124.38           O1-
ANISOU 2297  OD2 ASP A 335    16836  15979  14442   1074    615    887       O1-
ATOM   2298  N   ALA A 336     -12.099  48.043   7.105  1.00118.46           N  
ANISOU 2298  N   ALA A 336    15956  15588  13466   1326    198    722       N  
ATOM   2299  CA  ALA A 336     -10.883  47.266   7.328  1.00120.09           C  
ANISOU 2299  CA  ALA A 336    16235  15840  13555   1469    172    737       C  
ATOM   2300  C   ALA A 336     -11.127  45.831   6.878  1.00125.10           C  
ANISOU 2300  C   ALA A 336    16977  16352  14203   1462    286    823       C  
ATOM   2301  O   ALA A 336     -10.235  44.984   6.923  1.00124.03           O  
ANISOU 2301  O   ALA A 336    16912  16223  13990   1572    289    847       O  
ATOM   2302  CB  ALA A 336     -10.478  47.308   8.789  1.00113.89           C  
ANISOU 2302  CB  ALA A 336    15522  15136  12615   1651    176    742       C  
ATOM   2303  N   GLU A 337     -12.361  45.579   6.459  1.00112.77           N  
ANISOU 2303  N   GLU A 337    15420  14674  12753   1331    383    857       N  
ATOM   2304  CA  GLU A 337     -12.746  44.336   5.818  1.00 91.74           C  
ANISOU 2304  CA  GLU A 337    12832  11884  10142   1278    492    918       C  
ATOM   2305  C   GLU A 337     -13.091  44.676   4.374  1.00127.35           C  
ANISOU 2305  C   GLU A 337    17223  16363  14801   1100    438    869       C  
ATOM   2306  O   GLU A 337     -14.174  44.354   3.883  1.00105.76           O  
ANISOU 2306  O   GLU A 337    14481  13530  12172    977    520    884       O  
ATOM   2307  CB  GLU A 337     -13.960  43.746   6.526  1.00 94.78           C  
ANISOU 2307  CB  GLU A 337    13313  12158  10541   1268    660    985       C  
ATOM   2308  CG  GLU A 337     -14.375  42.378   6.029  1.00152.45           C  
ANISOU 2308  CG  GLU A 337    20709  19319  17895   1223    797   1046       C  
ATOM   2309  CD  GLU A 337     -15.604  41.861   6.747  1.00193.69           C  
ANISOU 2309  CD  GLU A 337    26019  24429  23146   1203    975   1104       C  
ATOM   2310  OE1 GLU A 337     -16.281  42.667   7.418  1.00214.10           O  
ANISOU 2310  OE1 GLU A 337    28566  27045  25736   1191    980   1090       O  
ATOM   2311  OE2 GLU A 337     -15.892  40.650   6.640  1.00191.96           O1-
ANISOU 2311  OE2 GLU A 337    25905  24085  22945   1199   1116   1162       O1-
ATOM   2312  N   LYS A 338     -12.154  45.344   3.709  1.00157.46           N  
ANISOU 2312  N   LYS A 338    20943  20265  18620   1090    299    806       N  
ATOM   2313  CA  LYS A 338     -12.372  45.918   2.384  1.00145.76           C  
ANISOU 2313  CA  LYS A 338    19340  18778  17264    939    229    753       C  
ATOM   2314  C   LYS A 338     -12.824  44.899   1.347  1.00162.69           C  
ANISOU 2314  C   LYS A 338    21513  20812  19491    844    297    782       C  
ATOM   2315  O   LYS A 338     -12.465  43.725   1.420  1.00173.99           O  
ANISOU 2315  O   LYS A 338    23050  22186  20874    906    368    833       O  
ATOM   2316  CB  LYS A 338     -11.098  46.616   1.903  1.00133.73           C  
ANISOU 2316  CB  LYS A 338    17735  17358  15718    969     88    689       C  
ATOM   2317  CG  LYS A 338      -9.860  45.725   1.903  1.00134.71           C  
ANISOU 2317  CG  LYS A 338    17916  17495  15773   1083     78    693       C  
ATOM   2318  CD  LYS A 338      -8.586  46.549   1.784  1.00147.53           C  
ANISOU 2318  CD  LYS A 338    19437  19228  17389   1130    -43    600       C  
ATOM   2319  CE  LYS A 338      -7.346  45.670   1.814  1.00138.18           C  
ANISOU 2319  CE  LYS A 338    18306  18067  16131   1251    -53    603       C  
ATOM   2320  NZ  LYS A 338      -6.099  46.483   1.868  1.00136.36           N1+
ANISOU 2320  NZ  LYS A 338    17975  17951  15884   1306   -161    508       N1+
ATOM   2321  N   SER A 339     -13.611  45.362   0.383  1.00189.48           N  
ANISOU 2321  N   SER A 339    24811  24178  23005    697    277    746       N  
ATOM   2322  CA  SER A 339     -14.034  44.521  -0.728  1.00209.98           C  
ANISOU 2322  CA  SER A 339    27411  26685  25686    596    322    752       C  
ATOM   2323  C   SER A 339     -12.804  43.971  -1.435  1.00204.10           C  
ANISOU 2323  C   SER A 339    26691  25955  24904    640    268    750       C  
ATOM   2324  O   SER A 339     -12.843  42.894  -2.028  1.00243.25           O  
ANISOU 2324  O   SER A 339    31705  30831  29887    611    330    774       O  
ATOM   2325  CB  SER A 339     -14.887  45.320  -1.714  1.00213.09           C  
ANISOU 2325  CB  SER A 339    27682  27083  26201    451    273    698       C  
ATOM   2326  OG  SER A 339     -14.131  46.354  -2.323  1.00204.04           O  
ANISOU 2326  OG  SER A 339    26443  26026  25058    447    141    648       O  
ATOM   2327  N   SER A 340     -11.712  44.725  -1.355  1.00117.24           N  
ANISOU 2327  N   SER A 340    15643  15057  13845    710    155    717       N  
ATOM   2328  CA  SER A 340     -10.454  44.348  -1.983  1.00100.83           C  
ANISOU 2328  CA  SER A 340    13571  13007  11734    758     94    705       C  
ATOM   2329  C   SER A 340      -9.431  45.447  -1.766  1.00112.33           C  
ANISOU 2329  C   SER A 340    14930  14574  13174    814    -17    626       C  
ATOM   2330  O   SER A 340      -9.751  46.500  -1.220  1.00133.68           O  
ANISOU 2330  O   SER A 340    17576  17333  15885    807    -50    596       O  
ATOM   2331  CB  SER A 340     -10.656  44.121  -3.479  1.00116.88           C  
ANISOU 2331  CB  SER A 340    15557  14990  13860    637     75    686       C  
ATOM   2332  OG  SER A 340     -11.523  45.101  -4.021  1.00123.88           O  
ANISOU 2332  OG  SER A 340    16340  15889  14841    522     37    644       O  
ATOM   2333  N   ALA A 341      -8.197  45.200  -2.188  1.00116.02           N  
ANISOU 2333  N   ALA A 341    15383  15074  13626    868    -65    592       N  
ATOM   2334  CA  ALA A 341      -7.183  46.243  -2.168  1.00129.46           C  
ANISOU 2334  CA  ALA A 341    16982  16874  15333    898   -160    508       C  
ATOM   2335  C   ALA A 341      -7.570  47.285  -3.205  1.00114.30           C  
ANISOU 2335  C   ALA A 341    14949  14954  13527    763   -209    458       C  
ATOM   2336  O   ALA A 341      -7.247  48.469  -3.076  1.00 97.31           O  
ANISOU 2336  O   ALA A 341    12708  12866  11401    752   -265    394       O  
ATOM   2337  CB  ALA A 341      -5.816  45.664  -2.478  1.00127.60           C  
ANISOU 2337  CB  ALA A 341    16757  16665  15059    978   -188    487       C  
ATOM   2338  N   SER A 342      -8.283  46.823  -4.227  1.00 80.11           N  
ANISOU 2338  N   SER A 342    10630  10550   9260    663   -183    488       N  
ATOM   2339  CA  SER A 342      -8.692  47.671  -5.338  1.00 97.05           C  
ANISOU 2339  CA  SER A 342    12680  12690  11504    545   -226    449       C  
ATOM   2340  C   SER A 342      -9.659  48.772  -4.918  1.00 93.49           C  
ANISOU 2340  C   SER A 342    12175  12263  11085    496   -234    438       C  
ATOM   2341  O   SER A 342      -9.760  49.793  -5.588  1.00114.79           O  
ANISOU 2341  O   SER A 342    14784  14978  13852    429   -275    394       O  
ATOM   2342  CB  SER A 342      -9.326  46.827  -6.445  1.00 87.80           C  
ANISOU 2342  CB  SER A 342    11541  11442  10376    462   -197    485       C  
ATOM   2343  OG  SER A 342     -10.571  46.297  -6.033  1.00 82.02           O  
ANISOU 2343  OG  SER A 342    10873  10657   9633    430   -128    546       O  
ATOM   2344  N   SER A 343     -10.371  48.565  -3.813  1.00 60.44           N  
ANISOU 2344  N   SER A 343     8048   8071   6846    535   -185    483       N  
ATOM   2345  CA  SER A 343     -11.368  49.530  -3.359  1.00 58.24           C  
ANISOU 2345  CA  SER A 343     7726   7810   6591    492   -185    480       C  
ATOM   2346  C   SER A 343     -10.726  50.864  -2.993  1.00 62.14           C  
ANISOU 2346  C   SER A 343     8135   8382   7095    517   -247    408       C  
ATOM   2347  O   SER A 343     -11.158  51.916  -3.461  1.00 65.18           O  
ANISOU 2347  O   SER A 343     8441   8779   7548    446   -276    376       O  
ATOM   2348  CB  SER A 343     -12.151  48.992  -2.165  1.00 42.66           C  
ANISOU 2348  CB  SER A 343     5844   5813   4554    538   -105    543       C  
ATOM   2349  OG  SER A 343     -11.453  49.228  -0.958  1.00 53.60           O  
ANISOU 2349  OG  SER A 343     7254   7259   5853    654   -116    529       O  
ATOM   2350  N   LYS A 344      -9.698  50.819  -2.152  1.00 40.65           N  
ANISOU 2350  N   LYS A 344     5431   5713   4301    622   -263    383       N  
ATOM   2351  CA  LYS A 344      -8.959  52.026  -1.807  1.00 39.61           C  
ANISOU 2351  CA  LYS A 344     5219   5657   4174    646   -318    306       C  
ATOM   2352  C   LYS A 344      -8.574  52.755  -3.091  1.00 48.69           C  
ANISOU 2352  C   LYS A 344     6283   6798   5420    559   -353    256       C  
ATOM   2353  O   LYS A 344      -8.864  53.935  -3.256  1.00 54.31           O  
ANISOU 2353  O   LYS A 344     6926   7524   6186    505   -370    219       O  
ATOM   2354  CB  LYS A 344      -7.720  51.678  -0.984  1.00 36.77           C  
ANISOU 2354  CB  LYS A 344     4886   5361   3723    774   -340    277       C  
ATOM   2355  CG  LYS A 344      -7.343  52.730   0.047  1.00 53.47           C  
ANISOU 2355  CG  LYS A 344     6953   7564   5798    831   -379    213       C  
ATOM   2356  CD  LYS A 344      -6.548  52.120   1.188  1.00 95.71           C  
ANISOU 2356  CD  LYS A 344    12361  12979  11024    982   -387    210       C  
ATOM   2357  CE  LYS A 344      -6.617  52.993   2.428  1.00 96.25           C  
ANISOU 2357  CE  LYS A 344    12408  13127  11034   1044   -411    166       C  
ATOM   2358  NZ  LYS A 344      -5.962  52.367   3.609  1.00 71.05           N1+
ANISOU 2358  NZ  LYS A 344     9284  10007   7706   1207   -418    167       N1+
ATOM   2359  N   LEU A 345      -7.936  52.031  -4.005  1.00 58.15           N  
ANISOU 2359  N   LEU A 345     7493   7966   6634    550   -356    260       N  
ATOM   2360  CA  LEU A 345      -7.603  52.559  -5.322  1.00 42.60           C  
ANISOU 2360  CA  LEU A 345     5462   5976   4748    472   -375    227       C  
ATOM   2361  C   LEU A 345      -8.850  52.998  -6.078  1.00 42.80           C  
ANISOU 2361  C   LEU A 345     5461   5956   4846    371   -363    250       C  
ATOM   2362  O   LEU A 345      -8.859  54.033  -6.741  1.00 76.96           O  
ANISOU 2362  O   LEU A 345     9725  10282   9233    317   -375    217       O  
ATOM   2363  CB  LEU A 345      -6.866  51.504  -6.142  1.00 50.77           C  
ANISOU 2363  CB  LEU A 345     6533   6980   5778    483   -373    240       C  
ATOM   2364  CG  LEU A 345      -6.668  51.828  -7.623  1.00 59.08           C  
ANISOU 2364  CG  LEU A 345     7541   7997   6909    402   -383    221       C  
ATOM   2365  CD1 LEU A 345      -5.503  52.791  -7.819  1.00 57.62           C  
ANISOU 2365  CD1 LEU A 345     7294   7854   6744    415   -410    156       C  
ATOM   2366  CD2 LEU A 345      -6.446  50.554  -8.417  1.00 28.34           C  
ANISOU 2366  CD2 LEU A 345     3702   4058   3009    400   -371    255       C  
ATOM   2367  N   ASP A 346      -9.903  52.195  -5.982  1.00 35.33           N  
ANISOU 2367  N   ASP A 346     4567   4971   3886    352   -334    309       N  
ATOM   2368  CA  ASP A 346     -11.153  52.470  -6.679  1.00 47.49           C  
ANISOU 2368  CA  ASP A 346     6081   6479   5486    264   -328    330       C  
ATOM   2369  C   ASP A 346     -11.708  53.825  -6.275  1.00 62.96           C  
ANISOU 2369  C   ASP A 346     7980   8470   7474    243   -337    306       C  
ATOM   2370  O   ASP A 346     -12.059  54.642  -7.124  1.00 85.81           O  
ANISOU 2370  O   ASP A 346    10817  11355  10431    183   -349    288       O  
ATOM   2371  CB  ASP A 346     -12.183  51.377  -6.371  1.00 75.65           C  
ANISOU 2371  CB  ASP A 346     9719  10005   9018    256   -287    397       C  
ATOM   2372  CG  ASP A 346     -13.486  51.569  -7.125  1.00 98.01           C  
ANISOU 2372  CG  ASP A 346    12520  12814  11904    168   -288    416       C  
ATOM   2373  OD1 ASP A 346     -13.575  52.503  -7.948  1.00 99.61           O  
ANISOU 2373  OD1 ASP A 346    12647  13031  12168    123   -322    379       O  
ATOM   2374  OD2 ASP A 346     -14.424  50.777  -6.895  1.00129.33           O1-
ANISOU 2374  OD2 ASP A 346    16524  16733  15881    140   -225    445       O1-
ATOM   2375  N   ILE A 347     -11.777  54.063  -4.971  1.00 38.21           N  
ANISOU 2375  N   ILE A 347     4862   5370   4286    299   -329    307       N  
ATOM   2376  CA  ILE A 347     -12.441  55.254  -4.459  1.00 57.76           C  
ANISOU 2376  CA  ILE A 347     7290   7873   6782    282   -334    290       C  
ATOM   2377  C   ILE A 347     -11.543  56.483  -4.540  1.00 50.85           C  
ANISOU 2377  C   ILE A 347     6354   7033   5935    287   -360    222       C  
ATOM   2378  O   ILE A 347     -12.032  57.608  -4.564  1.00 51.82           O  
ANISOU 2378  O   ILE A 347     6428   7165   6098    254   -363    203       O  
ATOM   2379  CB  ILE A 347     -12.956  55.057  -3.009  1.00 60.86           C  
ANISOU 2379  CB  ILE A 347     7733   8288   7101    340   -309    321       C  
ATOM   2380  CG1 ILE A 347     -11.821  55.193  -1.997  1.00 57.03           C  
ANISOU 2380  CG1 ILE A 347     7262   7859   6547    434   -326    280       C  
ATOM   2381  CG2 ILE A 347     -13.648  53.709  -2.858  1.00 83.61           C  
ANISOU 2381  CG2 ILE A 347    10702  11124   9944    343   -259    395       C  
ATOM   2382  CD1 ILE A 347     -12.228  54.798  -0.598  1.00 74.55           C  
ANISOU 2382  CD1 ILE A 347     9550  10098   8675    509   -294    317       C  
ATOM   2383  N   THR A 348     -10.235  56.268  -4.591  1.00 41.08           N  
ANISOU 2383  N   THR A 348     5119   5815   4675    331   -376    186       N  
ATOM   2384  CA  THR A 348      -9.298  57.375  -4.716  1.00 39.06           C  
ANISOU 2384  CA  THR A 348     4806   5590   4444    333   -398    118       C  
ATOM   2385  C   THR A 348      -9.335  57.967  -6.121  1.00 35.01           C  
ANISOU 2385  C   THR A 348     4258   5034   4009    259   -392    113       C  
ATOM   2386  O   THR A 348      -8.948  59.116  -6.341  1.00 51.93           O  
ANISOU 2386  O   THR A 348     6357   7187   6187    243   -397     69       O  
ATOM   2387  CB  THR A 348      -7.859  56.941  -4.404  1.00 34.29           C  
ANISOU 2387  CB  THR A 348     4209   5027   3791    404   -421     76       C  
ATOM   2388  CG2 THR A 348      -6.941  58.146  -4.369  1.00 36.34           C  
ANISOU 2388  CG2 THR A 348     4403   5328   4074    407   -445     -4       C  
ATOM   2389  OG1 THR A 348      -7.819  56.290  -3.132  1.00 61.58           O  
ANISOU 2389  OG1 THR A 348     7712   8526   7161    490   -425     88       O  
ATOM   2390  N   MET A 349      -9.809  57.180  -7.074  1.00 44.09           N  
ANISOU 2390  N   MET A 349     5434   6137   5183    220   -380    158       N  
ATOM   2391  CA  MET A 349      -9.878  57.643  -8.450  1.00 43.74           C  
ANISOU 2391  CA  MET A 349     5366   6054   5199    163   -375    159       C  
ATOM   2392  C   MET A 349     -11.275  58.110  -8.831  1.00 42.25           C  
ANISOU 2392  C   MET A 349     5160   5844   5047    112   -364    189       C  
ATOM   2393  O   MET A 349     -11.422  59.046  -9.611  1.00 45.79           O  
ANISOU 2393  O   MET A 349     5581   6278   5538     83   -359    182       O  
ATOM   2394  CB  MET A 349      -9.372  56.565  -9.405  1.00 43.94           C  
ANISOU 2394  CB  MET A 349     5423   6048   5225    156   -376    176       C  
ATOM   2395  CG  MET A 349      -7.859  56.432  -9.397  1.00 25.98           C  
ANISOU 2395  CG  MET A 349     3149   3794   2930    200   -388    137       C  
ATOM   2396  SD  MET A 349      -7.235  55.807 -10.957  1.00110.89           S  
ANISOU 2396  SD  MET A 349    13919  14503  13711    174   -387    147       S  
ATOM   2397  CE  MET A 349      -7.987  54.178 -10.991  1.00 49.55           C  
ANISOU 2397  CE  MET A 349     6207   6706   5914    170   -383    200       C  
ATOM   2398  N   THR A 350     -12.298  57.470  -8.275  1.00 57.00           N  
ANISOU 2398  N   THR A 350     7046   7714   6896    109   -360    225       N  
ATOM   2399  CA  THR A 350     -13.666  57.919  -8.502  1.00 45.20           C  
ANISOU 2399  CA  THR A 350     5526   6213   5434     68   -355    249       C  
ATOM   2400  C   THR A 350     -13.845  59.326  -7.942  1.00 47.77           C  
ANISOU 2400  C   THR A 350     5813   6562   5775     75   -351    225       C  
ATOM   2401  O   THR A 350     -14.447  60.192  -8.581  1.00 35.66           O  
ANISOU 2401  O   THR A 350     4249   5019   4282     47   -346    227       O  
ATOM   2402  CB  THR A 350     -14.700  56.973  -7.882  1.00 39.12           C  
ANISOU 2402  CB  THR A 350     4781   5446   4637     65   -352    291       C  
ATOM   2403  CG2 THR A 350     -16.097  57.499  -8.122  1.00 28.26           C  
ANISOU 2403  CG2 THR A 350     3363   4074   3299     25   -353    307       C  
ATOM   2404  OG1 THR A 350     -14.583  55.677  -8.483  1.00 78.43           O  
ANISOU 2404  OG1 THR A 350     9799  10397   9603     54   -355    314       O  
ATOM   2405  N   VAL A 351     -13.307  59.553  -6.749  1.00 29.36           N  
ANISOU 2405  N   VAL A 351     3486   4265   3405    119   -354    200       N  
ATOM   2406  CA  VAL A 351     -13.273  60.897  -6.185  1.00 42.75           C  
ANISOU 2406  CA  VAL A 351     5145   5985   5112    129   -354    164       C  
ATOM   2407  C   VAL A 351     -12.545  61.857  -7.126  1.00 53.17           C  
ANISOU 2407  C   VAL A 351     6439   7289   6476    110   -353    131       C  
ATOM   2408  O   VAL A 351     -13.150  62.790  -7.650  1.00 44.43           O  
ANISOU 2408  O   VAL A 351     5306   6166   5410     85   -343    138       O  
ATOM   2409  CB  VAL A 351     -12.620  60.931  -4.781  1.00 37.49           C  
ANISOU 2409  CB  VAL A 351     4486   5369   4389    188   -366    128       C  
ATOM   2410  CG1 VAL A 351     -12.345  62.362  -4.360  1.00 33.64           C  
ANISOU 2410  CG1 VAL A 351     3953   4908   3921    192   -372     73       C  
ATOM   2411  CG2 VAL A 351     -13.510  60.243  -3.752  1.00 15.74           C  
ANISOU 2411  CG2 VAL A 351     1766   2631   1585    214   -360    170       C  
ATOM   2412  N   ALA A 352     -11.255  61.618  -7.347  1.00 32.75           N  
ANISOU 2412  N   ALA A 352     3860   4705   3878    130   -362     98       N  
ATOM   2413  CA  ALA A 352     -10.455  62.479  -8.222  1.00 35.61           C  
ANISOU 2413  CA  ALA A 352     4199   5051   4280    115   -360     67       C  
ATOM   2414  C   ALA A 352     -11.174  62.818  -9.525  1.00 46.68           C  
ANISOU 2414  C   ALA A 352     5601   6409   5724     77   -345    107       C  
ATOM   2415  O   ALA A 352     -11.054  63.934 -10.037  1.00 21.73           O  
ANISOU 2415  O   ALA A 352     2418   3238   2601     68   -338     94       O  
ATOM   2416  CB  ALA A 352      -9.107  61.839  -8.521  1.00 33.51           C  
ANISOU 2416  CB  ALA A 352     3945   4791   3998    137   -373     40       C  
ATOM   2417  N   HIS A 353     -11.914  61.853 -10.064  1.00 26.75           N  
ANISOU 2417  N   HIS A 353     3103   3866   3196     59   -344    153       N  
ATOM   2418  CA  HIS A 353     -12.662  62.079 -11.289  1.00 15.07           C  
ANISOU 2418  CA  HIS A 353     1621   2358   1746     33   -337    186       C  
ATOM   2419  C   HIS A 353     -13.752  63.121 -11.070  1.00 42.40           C  
ANISOU 2419  C   HIS A 353     5052   5828   5229     28   -330    197       C  
ATOM   2420  O   HIS A 353     -13.881  64.065 -11.847  1.00 50.60           O  
ANISOU 2420  O   HIS A 353     6077   6855   6296     28   -323    202       O  
ATOM   2421  CB  HIS A 353     -13.289  60.784 -11.793  1.00 10.06           C  
ANISOU 2421  CB  HIS A 353     1009   1712   1102     14   -344    219       C  
ATOM   2422  CG  HIS A 353     -14.064  60.949 -13.067  1.00 31.99           C  
ANISOU 2422  CG  HIS A 353     3779   4474   3902     -6   -347    242       C  
ATOM   2423  CD2 HIS A 353     -15.182  61.663 -13.346  1.00 28.42           C  
ANISOU 2423  CD2 HIS A 353     3300   4030   3467    -10   -346    258       C  
ATOM   2424  ND1 HIS A 353     -13.692  60.349 -14.250  1.00 57.62           N  
ANISOU 2424  ND1 HIS A 353     7044   7699   7149    -13   -354    249       N  
ATOM   2425  CE1 HIS A 353     -14.554  60.673 -15.198  1.00 46.35           C  
ANISOU 2425  CE1 HIS A 353     5604   6273   5736    -19   -361    265       C  
ATOM   2426  NE2 HIS A 353     -15.468  61.469 -14.674  1.00 20.93           N  
ANISOU 2426  NE2 HIS A 353     2355   3072   2526    -16   -356    271       N  
ATOM   2427  N   GLU A 354     -14.536  62.945 -10.011  1.00 37.84           N  
ANISOU 2427  N   GLU A 354     4466   5274   4637     30   -330    203       N  
ATOM   2428  CA  GLU A 354     -15.663  63.828  -9.751  1.00 32.26           C  
ANISOU 2428  CA  GLU A 354     3728   4578   3952     27   -323    215       C  
ATOM   2429  C   GLU A 354     -15.222  65.216  -9.305  1.00 43.73           C  
ANISOU 2429  C   GLU A 354     5155   6038   5423     44   -314    183       C  
ATOM   2430  O   GLU A 354     -15.868  66.212  -9.628  1.00 41.89           O  
ANISOU 2430  O   GLU A 354     4895   5800   5221     46   -304    193       O  
ATOM   2431  CB  GLU A 354     -16.596  63.218  -8.714  1.00  6.38           C  
ANISOU 2431  CB  GLU A 354      445   1324    656     25   -325    232       C  
ATOM   2432  CG  GLU A 354     -17.131  61.862  -9.101  1.00 25.46           C  
ANISOU 2432  CG  GLU A 354     2878   3734   3062      4   -335    260       C  
ATOM   2433  CD  GLU A 354     -17.641  61.818 -10.523  1.00 54.85           C  
ANISOU 2433  CD  GLU A 354     6591   7440   6810    -17   -342    275       C  
ATOM   2434  OE1 GLU A 354     -18.156  62.841 -11.019  1.00 82.01           O  
ANISOU 2434  OE1 GLU A 354    10004  10883  10274    -12   -337    278       O  
ATOM   2435  OE2 GLU A 354     -17.524  60.744 -11.140  1.00 64.92           O1-
ANISOU 2435  OE2 GLU A 354     7886   8704   8078    -33   -353    284       O1-
ATOM   2436  N   LEU A 355     -14.127  65.276  -8.557  1.00 18.02           N  
ANISOU 2436  N   LEU A 355     1900   2797   2150     59   -320    138       N  
ATOM   2437  CA  LEU A 355     -13.580  66.552  -8.119  1.00 29.01           C  
ANISOU 2437  CA  LEU A 355     3257   4199   3568     69   -315     90       C  
ATOM   2438  C   LEU A 355     -12.996  67.373  -9.275  1.00 44.91           C  
ANISOU 2438  C   LEU A 355     5256   6181   5627     62   -303     83       C  
ATOM   2439  O   LEU A 355     -13.033  68.604  -9.255  1.00 38.52           O  
ANISOU 2439  O   LEU A 355     4406   5366   4864     64   -286     62       O  
ATOM   2440  CB  LEU A 355     -12.524  66.340  -7.036  1.00  7.29           C  
ANISOU 2440  CB  LEU A 355      500   1484    784     91   -331     30       C  
ATOM   2441  CG  LEU A 355     -13.023  65.935  -5.650  1.00 27.70           C  
ANISOU 2441  CG  LEU A 355     3090   4111   3323    114   -341     27       C  
ATOM   2442  CD1 LEU A 355     -11.880  65.993  -4.643  1.00 41.46           C  
ANISOU 2442  CD1 LEU A 355     4820   5902   5031    149   -364    -45       C  
ATOM   2443  CD2 LEU A 355     -14.168  66.830  -5.203  1.00 15.06           C  
ANISOU 2443  CD2 LEU A 355     1458   2515   1748    108   -327     40       C  
ATOM   2444  N   ALA A 356     -12.456  66.698 -10.281  1.00 28.62           N  
ANISOU 2444  N   ALA A 356     3221   4097   3557     57   -309    100       N  
ATOM   2445  CA  ALA A 356     -11.913  67.396 -11.438  1.00 35.46           C  
ANISOU 2445  CA  ALA A 356     4077   4934   4463     57   -298    102       C  
ATOM   2446  C   ALA A 356     -13.015  68.120 -12.204  1.00 43.81           C  
ANISOU 2446  C   ALA A 356     5124   5976   5547     65   -283    151       C  
ATOM   2447  O   ALA A 356     -12.773  69.151 -12.830  1.00 49.29           O  
ANISOU 2447  O   ALA A 356     5790   6650   6289     80   -262    152       O  
ATOM   2448  CB  ALA A 356     -11.171  66.433 -12.352  1.00 25.21           C  
ANISOU 2448  CB  ALA A 356     2814   3620   3146     54   -308    114       C  
ATOM   2449  N   HIS A 357     -14.230  67.582 -12.149  1.00 28.92           N  
ANISOU 2449  N   HIS A 357     3252   4099   3636     62   -290    190       N  
ATOM   2450  CA  HIS A 357     -15.366  68.194 -12.833  1.00 33.39           C  
ANISOU 2450  CA  HIS A 357     3805   4664   4219     80   -282    232       C  
ATOM   2451  C   HIS A 357     -15.797  69.502 -12.188  1.00 47.56           C  
ANISOU 2451  C   HIS A 357     5555   6463   6053     98   -259    224       C  
ATOM   2452  O   HIS A 357     -16.487  70.307 -12.810  1.00 32.72           O  
ANISOU 2452  O   HIS A 357     3657   4577   4198    131   -243    257       O  
ATOM   2453  CB  HIS A 357     -16.561  67.238 -12.883  1.00 29.10           C  
ANISOU 2453  CB  HIS A 357     3271   4138   3648     67   -297    261       C  
ATOM   2454  CG  HIS A 357     -16.480  66.229 -13.981  1.00 26.05           C  
ANISOU 2454  CG  HIS A 357     2912   3744   3241     57   -313    277       C  
ATOM   2455  CD2 HIS A 357     -16.671  64.889 -13.977  1.00 31.90           C  
ANISOU 2455  CD2 HIS A 357     3671   4489   3960     32   -328    278       C  
ATOM   2456  ND1 HIS A 357     -16.173  66.569 -15.279  1.00 18.92           N  
ANISOU 2456  ND1 HIS A 357     2020   2827   2343     79   -312    293       N  
ATOM   2457  CE1 HIS A 357     -16.174  65.483 -16.028  1.00 46.51           C  
ANISOU 2457  CE1 HIS A 357     5536   6320   5816     65   -329    298       C  
ATOM   2458  NE2 HIS A 357     -16.473  64.450 -15.261  1.00 34.49           N  
ANISOU 2458  NE2 HIS A 357     4016   4806   4281     35   -338    289       N  
ATOM   2459  N   GLN A 358     -15.407  69.707 -10.936  1.00 25.68           N  
ANISOU 2459  N   GLN A 358     2764   3705   3288     86   -254    178       N  
ATOM   2460  CA  GLN A 358     -15.757  70.935 -10.249  1.00 25.05           C  
ANISOU 2460  CA  GLN A 358     2656   3616   3246     94   -211    157       C  
ATOM   2461  C   GLN A 358     -15.250  72.126 -11.063  1.00 45.69           C  
ANISOU 2461  C   GLN A 358     5277   6175   5909    106   -150    151       C  
ATOM   2462  O   GLN A 358     -15.920  73.151 -11.166  1.00 49.95           O  
ANISOU 2462  O   GLN A 358     5813   6687   6476    126   -100    168       O  
ATOM   2463  CB  GLN A 358     -15.194  70.941  -8.829  1.00 46.61           C  
ANISOU 2463  CB  GLN A 358     5373   6370   5967     79   -213     93       C  
ATOM   2464  CG  GLN A 358     -15.685  69.778  -7.968  1.00 20.33           C  
ANISOU 2464  CG  GLN A 358     2052   3087   2586     77   -257    105       C  
ATOM   2465  CD  GLN A 358     -17.193  69.629  -7.992  1.00 39.27           C  
ANISOU 2465  CD  GLN A 358     4448   5492   4979     82   -254    159       C  
ATOM   2466  NE2 GLN A 358     -17.673  68.637  -8.724  1.00 33.88           N  
ANISOU 2466  NE2 GLN A 358     3795   4805   4271     72   -270    200       N  
ATOM   2467  OE1 GLN A 358     -17.918  70.393  -7.359  1.00 47.69           O  
ANISOU 2467  OE1 GLN A 358     5496   6560   6064     89   -223    156       O  
ATOM   2468  N   TRP A 359     -14.072  71.968 -11.658  1.00 29.60           N  
ANISOU 2468  N   TRP A 359     3249   4116   3881     96   -147    128       N  
ATOM   2469  CA  TRP A 359     -13.536  72.954 -12.591  1.00 28.85           C  
ANISOU 2469  CA  TRP A 359     3170   3959   3832    108    -79    130       C  
ATOM   2470  C   TRP A 359     -13.936  72.630 -14.034  1.00 29.53           C  
ANISOU 2470  C   TRP A 359     3289   4035   3896    143    -90    202       C  
ATOM   2471  O   TRP A 359     -14.751  73.325 -14.635  1.00 40.40           O  
ANISOU 2471  O   TRP A 359     4680   5390   5278    183    -55    250       O  
ATOM   2472  CB  TRP A 359     -12.011  73.032 -12.477  1.00 25.88           C  
ANISOU 2472  CB  TRP A 359     2782   3563   3487     78    -59     59       C  
ATOM   2473  CG  TRP A 359     -11.522  73.633 -11.187  1.00 32.44           C  
ANISOU 2473  CG  TRP A 359     3576   4402   4348     51    -36    -28       C  
ATOM   2474  CD1 TRP A 359     -11.162  74.929 -10.977  1.00 39.65           C  
ANISOU 2474  CD1 TRP A 359     4475   5263   5328     37     48    -80       C  
ATOM   2475  CD2 TRP A 359     -11.338  72.961  -9.931  1.00 36.30           C  
ANISOU 2475  CD2 TRP A 359     4038   4954   4798     38    -95    -77       C  
ATOM   2476  CE2 TRP A 359     -10.866  73.918  -9.010  1.00 37.22           C  
ANISOU 2476  CE2 TRP A 359     4121   5063   4957     19    -51   -164       C  
ATOM   2477  CE3 TRP A 359     -11.528  71.646  -9.498  1.00 48.25           C  
ANISOU 2477  CE3 TRP A 359     5560   6528   6245     46   -173    -57       C  
ATOM   2478  NE1 TRP A 359     -10.767  75.110  -9.674  1.00 45.32           N  
ANISOU 2478  NE1 TRP A 359     5152   6015   6052     13     38   -167       N  
ATOM   2479  CZ2 TRP A 359     -10.580  73.604  -7.683  1.00 29.32           C  
ANISOU 2479  CZ2 TRP A 359     3092   4124   3925     15    -93   -231       C  
ATOM   2480  CZ3 TRP A 359     -11.244  71.334  -8.175  1.00 37.91           C  
ANISOU 2480  CZ3 TRP A 359     4229   5270   4903     45   -206   -114       C  
ATOM   2481  CH2 TRP A 359     -10.774  72.311  -7.285  1.00 38.16           C  
ANISOU 2481  CH2 TRP A 359     4226   5303   4969     34   -170   -201       C  
ATOM   2482  N   PHE A 360     -13.363  71.560 -14.579  1.00 50.58           N  
ANISOU 2482  N   PHE A 360     5967   6719   6531    134   -140    209       N  
ATOM   2483  CA  PHE A 360     -13.598  71.175 -15.971  1.00 41.18           C  
ANISOU 2483  CA  PHE A 360     4809   5523   5314    168   -155    267       C  
ATOM   2484  C   PHE A 360     -14.926  70.442 -16.163  1.00 42.21           C  
ANISOU 2484  C   PHE A 360     4934   5705   5399    185   -216    312       C  
ATOM   2485  O   PHE A 360     -15.003  69.231 -15.978  1.00 27.23           O  
ANISOU 2485  O   PHE A 360     3043   3838   3465    154   -264    305       O  
ATOM   2486  CB  PHE A 360     -12.455  70.294 -16.475  1.00 28.30           C  
ANISOU 2486  CB  PHE A 360     3193   3890   3669    150   -182    251       C  
ATOM   2487  CG  PHE A 360     -12.386  70.179 -17.973  1.00 42.75           C  
ANISOU 2487  CG  PHE A 360     5063   5698   5481    187   -175    300       C  
ATOM   2488  CD1 PHE A 360     -11.477  70.933 -18.697  1.00 35.72           C  
ANISOU 2488  CD1 PHE A 360     4199   4747   4626    201   -102    297       C  
ATOM   2489  CD2 PHE A 360     -13.222  69.312 -18.659  1.00 65.12           C  
ANISOU 2489  CD2 PHE A 360     7908   8572   8262    209   -237    344       C  
ATOM   2490  CE1 PHE A 360     -11.405  70.828 -20.075  1.00 40.61           C  
ANISOU 2490  CE1 PHE A 360     4863   5346   5221    244    -91    345       C  
ATOM   2491  CE2 PHE A 360     -13.157  69.204 -20.037  1.00 42.33           C  
ANISOU 2491  CE2 PHE A 360     5060   5673   5350    251   -235    384       C  
ATOM   2492  CZ  PHE A 360     -12.248  69.963 -20.745  1.00 52.16           C  
ANISOU 2492  CZ  PHE A 360     6338   6857   6622    273   -162    389       C  
ATOM   2493  N   GLY A 361     -15.963  71.180 -16.548  1.00 33.01           N  
ANISOU 2493  N   GLY A 361     3768   4538   4234    229   -194    351       N  
ATOM   2494  CA  GLY A 361     -17.261  70.586 -16.792  1.00 25.51           C  
ANISOU 2494  CA  GLY A 361     2802   3642   3248    246   -247    382       C  
ATOM   2495  C   GLY A 361     -18.377  71.304 -16.064  1.00 43.08           C  
ANISOU 2495  C   GLY A 361     4995   5883   5489    262   -229    389       C  
ATOM   2496  O   GLY A 361     -19.514  71.326 -16.521  1.00 70.64           O  
ANISOU 2496  O   GLY A 361     8472   9408   8960    298   -248    418       O  
ATOM   2497  N   ASN A 362     -18.050  71.887 -14.918  1.00 52.62           N  
ANISOU 2497  N   ASN A 362     6192   7068   6731    233   -189    353       N  
ATOM   2498  CA  ASN A 362     -19.026  72.626 -14.136  1.00 46.27           C  
ANISOU 2498  CA  ASN A 362     5363   6273   5946    245   -162    356       C  
ATOM   2499  C   ASN A 362     -18.790  74.120 -14.267  1.00 49.46           C  
ANISOU 2499  C   ASN A 362     5786   6617   6389    279    -75    359       C  
ATOM   2500  O   ASN A 362     -19.710  74.885 -14.567  1.00 75.06           O  
ANISOU 2500  O   ASN A 362     9028   9857   9634    331    -46    395       O  
ATOM   2501  CB  ASN A 362     -18.965  72.200 -12.672  1.00 32.08           C  
ANISOU 2501  CB  ASN A 362     3542   4495   4151    195   -177    312       C  
ATOM   2502  CG  ASN A 362     -19.286  70.734 -12.483  1.00 46.34           C  
ANISOU 2502  CG  ASN A 362     5341   6347   5919    164   -242    314       C  
ATOM   2503  ND2 ASN A 362     -19.497  70.327 -11.240  1.00 25.38           N  
ANISOU 2503  ND2 ASN A 362     2677   3708   3256    133   -245    289       N  
ATOM   2504  OD1 ASN A 362     -19.342  69.973 -13.447  1.00 59.66           O  
ANISOU 2504  OD1 ASN A 362     7053   8037   7577    160   -265    331       O  
ATOM   2505  N   LEU A 363     -17.547  74.528 -14.041  1.00 37.41           N  
ANISOU 2505  N   LEU A 363     4276   5042   4896    250    -30    317       N  
ATOM   2506  CA  LEU A 363     -17.149  75.916 -14.211  1.00 23.01           C  
ANISOU 2506  CA  LEU A 363     2475   3147   3122    271     69    311       C  
ATOM   2507  C   LEU A 363     -17.161  76.276 -15.690  1.00 40.54           C  
ANISOU 2507  C   LEU A 363     4740   5333   5331    334    103    370       C  
ATOM   2508  O   LEU A 363     -17.578  77.367 -16.075  1.00 54.60           O  
ANISOU 2508  O   LEU A 363     6546   7070   7129    388    177    403       O  
ATOM   2509  CB  LEU A 363     -15.756  76.131 -13.625  1.00 18.31           C  
ANISOU 2509  CB  LEU A 363     1875   2514   2570    216    105    235       C  
ATOM   2510  CG  LEU A 363     -15.192  77.549 -13.632  1.00 26.34           C  
ANISOU 2510  CG  LEU A 363     2907   3446   3654    218    220    206       C  
ATOM   2511  CD1 LEU A 363     -16.097  78.488 -12.855  1.00 25.63           C  
ANISOU 2511  CD1 LEU A 363     2807   3346   3586    233    265    205       C  
ATOM   2512  CD2 LEU A 363     -13.802  77.512 -13.029  1.00 24.28           C  
ANISOU 2512  CD2 LEU A 363     2623   3169   3433    155    234    114       C  
ATOM   2513  N   VAL A 364     -16.696  75.348 -16.518  1.00 18.61           N  
ANISOU 2513  N   VAL A 364     1978   2574   2520    333     53    384       N  
ATOM   2514  CA  VAL A 364     -16.836  75.477 -17.961  1.00 44.65           C  
ANISOU 2514  CA  VAL A 364     5320   5858   5788    402     67    444       C  
ATOM   2515  C   VAL A 364     -17.465  74.192 -18.495  1.00 29.38           C  
ANISOU 2515  C   VAL A 364     3370   4001   3790    412    -39    468       C  
ATOM   2516  O   VAL A 364     -16.787  73.181 -18.673  1.00 69.20           O  
ANISOU 2516  O   VAL A 364     8414   9060   8817    373    -88    449       O  
ATOM   2517  CB  VAL A 364     -15.483  75.752 -18.650  1.00 36.45           C  
ANISOU 2517  CB  VAL A 364     4324   4749   4778    396    132    434       C  
ATOM   2518  CG1 VAL A 364     -15.683  75.997 -20.130  1.00  9.63           C  
ANISOU 2518  CG1 VAL A 364      984   1332   1343    482    159    503       C  
ATOM   2519  CG2 VAL A 364     -14.802  76.943 -18.013  1.00 30.41           C  
ANISOU 2519  CG2 VAL A 364     3562   3905   4088    368    240    389       C  
ATOM   2520  N   THR A 365     -18.773  74.239 -18.722  1.00 30.51           N  
ANISOU 2520  N   THR A 365     3496   4195   3902    463    -71    503       N  
ATOM   2521  CA  THR A 365     -19.511  73.073 -19.179  1.00 57.65           C  
ANISOU 2521  CA  THR A 365     6907   7711   7288    468   -168    512       C  
ATOM   2522  C   THR A 365     -19.758  73.121 -20.688  1.00 33.11           C  
ANISOU 2522  C   THR A 365     3834   4618   4130    554   -179    559       C  
ATOM   2523  O   THR A 365     -19.752  74.188 -21.293  1.00 26.75           O  
ANISOU 2523  O   THR A 365     3070   3771   3321    629   -110    599       O  
ATOM   2524  CB  THR A 365     -20.855  72.932 -18.434  1.00 32.67           C  
ANISOU 2524  CB  THR A 365     3684   4606   4121    464   -207    506       C  
ATOM   2525  CG2 THR A 365     -21.796  74.002 -18.855  1.00 32.93           C  
ANISOU 2525  CG2 THR A 365     3720   4646   4147    552   -171    547       C  
ATOM   2526  OG1 THR A 365     -21.442  71.663 -18.746  1.00112.73           O  
ANISOU 2526  OG1 THR A 365    13803  14807  14221    430   -276    486       O  
ATOM   2527  N   MET A 366     -19.971  71.957 -21.286  1.00 24.61           N  
ANISOU 2527  N   MET A 366     2749   3594   3007    534   -248    543       N  
ATOM   2528  CA  MET A 366     -20.187  71.868 -22.724  1.00 31.89           C  
ANISOU 2528  CA  MET A 366     3704   4541   3870    607   -260    569       C  
ATOM   2529  C   MET A 366     -21.396  72.693 -23.149  1.00 25.60           C  
ANISOU 2529  C   MET A 366     2896   3786   3044    709   -257    607       C  
ATOM   2530  O   MET A 366     -22.195  73.117 -22.318  1.00 49.46           O  
ANISOU 2530  O   MET A 366     5873   6827   6091    708   -256    604       O  
ATOM   2531  CB  MET A 366     -20.388  70.410 -23.135  1.00 33.32           C  
ANISOU 2531  CB  MET A 366     3869   4774   4017    552   -326    523       C  
ATOM   2532  CG  MET A 366     -21.710  69.815 -22.672  1.00 57.13           C  
ANISOU 2532  CG  MET A 366     6821   7858   7027    523   -377    490       C  
ATOM   2533  SD  MET A 366     -21.506  68.274 -21.765  1.00 57.05           S  
ANISOU 2533  SD  MET A 366     6788   7845   7045    394   -408    431       S  
ATOM   2534  CE  MET A 366     -20.702  68.872 -20.276  1.00 91.57           C  
ANISOU 2534  CE  MET A 366    11165  12156  11471    343   -359    433       C  
ATOM   2535  N   GLU A 367     -21.517  72.920 -24.451  1.00 37.71           N  
ANISOU 2535  N   GLU A 367     4472   5338   4520    805   -255    641       N  
ATOM   2536  CA  GLU A 367     -22.672  73.602 -25.001  1.00 44.06           C  
ANISOU 2536  CA  GLU A 367     5266   6196   5277    920   -261    674       C  
ATOM   2537  C   GLU A 367     -23.764  72.581 -25.241  1.00 37.56           C  
ANISOU 2537  C   GLU A 367     4376   5480   4414    902   -353    621       C  
ATOM   2538  O   GLU A 367     -24.953  72.889 -25.183  1.00 76.83           O  
ANISOU 2538  O   GLU A 367     9302  10520   9369    957   -381    621       O  
ATOM   2539  CB  GLU A 367     -22.306  74.281 -26.315  1.00 57.06           C  
ANISOU 2539  CB  GLU A 367     6994   7817   6868   1046   -214    736       C  
ATOM   2540  CG  GLU A 367     -23.438  75.060 -26.958  1.00 93.63           C  
ANISOU 2540  CG  GLU A 367    11629  12507  11439   1190   -215    778       C  
ATOM   2541  CD  GLU A 367     -22.994  75.756 -28.225  1.00114.21           C  
ANISOU 2541  CD  GLU A 367    14334  15076  13984   1324   -153    847       C  
ATOM   2542  OE1 GLU A 367     -21.811  75.609 -28.579  1.00 91.24           O  
ANISOU 2542  OE1 GLU A 367    11485  12093  11088   1294   -108    858       O  
ATOM   2543  OE2 GLU A 367     -23.816  76.449 -28.860  1.00139.91           O1-
ANISOU 2543  OE2 GLU A 367    17607  18375  17177   1465   -144    890       O1-
ATOM   2544  N   TRP A 368     -23.345  71.353 -25.511  1.00 35.39           N  
ANISOU 2544  N   TRP A 368     4098   5218   4131    826   -398    574       N  
ATOM   2545  CA  TRP A 368     -24.277  70.284 -25.828  1.00 44.15           C  
ANISOU 2545  CA  TRP A 368     5148   6417   5211    805   -480    518       C  
ATOM   2546  C   TRP A 368     -23.661  68.907 -25.608  1.00 44.94           C  
ANISOU 2546  C   TRP A 368     5245   6496   5335    686   -507    466       C  
ATOM   2547  O   TRP A 368     -22.453  68.774 -25.441  1.00 60.80           O  
ANISOU 2547  O   TRP A 368     7301   8432   7367    638   -469    475       O  
ATOM   2548  CB  TRP A 368     -24.769  70.415 -27.265  1.00 40.64           C  
ANISOU 2548  CB  TRP A 368     4718   6041   4682    929   -517    529       C  
ATOM   2549  CG  TRP A 368     -25.874  69.485 -27.574  1.00 31.66           C  
ANISOU 2549  CG  TRP A 368     3505   5006   3518    921   -605    464       C  
ATOM   2550  CD1 TRP A 368     -25.867  68.481 -28.490  1.00 49.77           C  
ANISOU 2550  CD1 TRP A 368     5794   7347   5770    920   -664    419       C  
ATOM   2551  CD2 TRP A 368     -27.152  69.445 -26.941  1.00 46.57           C  
ANISOU 2551  CD2 TRP A 368     5303   6963   5428    910   -644    429       C  
ATOM   2552  CE2 TRP A 368     -27.879  68.400 -27.537  1.00 57.50           C  
ANISOU 2552  CE2 TRP A 368     6628   8437   6785    901   -726    358       C  
ATOM   2553  CE3 TRP A 368     -27.758  70.196 -25.930  1.00 52.75           C  
ANISOU 2553  CE3 TRP A 368     6048   7742   6253    908   -615    447       C  
ATOM   2554  NE1 TRP A 368     -27.071  67.825 -28.482  1.00 37.13           N  
ANISOU 2554  NE1 TRP A 368     4102   5840   4164    908   -738    353       N  
ATOM   2555  CZ2 TRP A 368     -29.182  68.088 -27.159  1.00 49.31           C  
ANISOU 2555  CZ2 TRP A 368     5488   7484   5764    886   -780    302       C  
ATOM   2556  CZ3 TRP A 368     -29.049  69.886 -25.555  1.00 39.53           C  
ANISOU 2556  CZ3 TRP A 368     4277   6150   4592    896   -667    398       C  
ATOM   2557  CH2 TRP A 368     -29.747  68.841 -26.167  1.00 42.15           C  
ANISOU 2557  CH2 TRP A 368     4545   6570   4899    884   -747    325       C  
ATOM   2558  N   TRP A 369     -24.503  67.884 -25.628  1.00 38.35           N  
ANISOU 2558  N   TRP A 369     4351   5724   4495    646   -570    410       N  
ATOM   2559  CA  TRP A 369     -24.096  66.540 -25.248  1.00 53.33           C  
ANISOU 2559  CA  TRP A 369     6242   7597   6422    534   -588    364       C  
ATOM   2560  C   TRP A 369     -23.117  65.874 -26.209  1.00 54.09           C  
ANISOU 2560  C   TRP A 369     6393   7668   6489    532   -595    359       C  
ATOM   2561  O   TRP A 369     -22.503  64.864 -25.876  1.00 57.35           O  
ANISOU 2561  O   TRP A 369     6819   8043   6930    447   -594    334       O  
ATOM   2562  CB  TRP A 369     -25.339  65.683 -25.026  1.00 43.41           C  
ANISOU 2562  CB  TRP A 369     4906   6413   5176    497   -646    306       C  
ATOM   2563  CG  TRP A 369     -26.198  66.302 -23.991  1.00 43.19           C  
ANISOU 2563  CG  TRP A 369     4825   6401   5183    491   -632    312       C  
ATOM   2564  CD1 TRP A 369     -27.331  67.027 -24.189  1.00 41.28           C  
ANISOU 2564  CD1 TRP A 369     4530   6232   4924    569   -656    313       C  
ATOM   2565  CD2 TRP A 369     -25.959  66.303 -22.581  1.00 39.84           C  
ANISOU 2565  CD2 TRP A 369     4400   5920   4816    411   -589    319       C  
ATOM   2566  CE2 TRP A 369     -27.003  67.027 -21.982  1.00 26.68           C  
ANISOU 2566  CE2 TRP A 369     2677   4292   3167    439   -587    324       C  
ATOM   2567  CE3 TRP A 369     -24.968  65.748 -21.767  1.00 24.99           C  
ANISOU 2567  CE3 TRP A 369     2560   3965   2968    326   -554    320       C  
ATOM   2568  NE1 TRP A 369     -27.830  67.459 -22.984  1.00 54.93           N  
ANISOU 2568  NE1 TRP A 369     6221   7950   6701    536   -628    320       N  
ATOM   2569  CZ2 TRP A 369     -27.085  67.212 -20.606  1.00 34.96           C  
ANISOU 2569  CZ2 TRP A 369     3711   5305   4266    383   -550    330       C  
ATOM   2570  CZ3 TRP A 369     -25.049  65.937 -20.406  1.00 43.27           C  
ANISOU 2570  CZ3 TRP A 369     4862   6251   5326    277   -522    326       C  
ATOM   2571  CH2 TRP A 369     -26.101  66.664 -19.838  1.00 39.44           C  
ANISOU 2571  CH2 TRP A 369     4324   5804   4859    304   -519    331       C  
ATOM   2572  N   ASN A 370     -22.956  66.451 -27.392  1.00 56.22           N  
ANISOU 2572  N   ASN A 370     6702   7959   6702    635   -596    387       N  
ATOM   2573  CA  ASN A 370     -22.000  65.929 -28.357  1.00 22.42           C  
ANISOU 2573  CA  ASN A 370     2477   3651   2389    645   -597    388       C  
ATOM   2574  C   ASN A 370     -20.551  66.054 -27.880  1.00 49.00           C  
ANISOU 2574  C   ASN A 370     5899   6920   5797    590   -533    415       C  
ATOM   2575  O   ASN A 370     -19.658  65.376 -28.393  1.00 56.52           O  
ANISOU 2575  O   ASN A 370     6890   7842   6743    566   -531    406       O  
ATOM   2576  CB  ASN A 370     -22.179  66.607 -29.718  1.00 35.62           C  
ANISOU 2576  CB  ASN A 370     4185   5368   3982    784   -607    420       C  
ATOM   2577  CG  ASN A 370     -21.951  68.102 -29.662  1.00 51.87           C  
ANISOU 2577  CG  ASN A 370     6286   7388   6033    869   -539    492       C  
ATOM   2578  ND2 ASN A 370     -21.247  68.629 -30.658  1.00 58.55           N  
ANISOU 2578  ND2 ASN A 370     7208   8205   6832    958   -500    540       N  
ATOM   2579  OD1 ASN A 370     -22.406  68.779 -28.740  1.00 74.37           O  
ANISOU 2579  OD1 ASN A 370     9105  10230   8922    858   -515    507       O  
ATOM   2580  N   ASP A 371     -20.323  66.919 -26.897  1.00 35.53           N  
ANISOU 2580  N   ASP A 371     4193   5171   4137    572   -483    443       N  
ATOM   2581  CA  ASP A 371     -18.979  67.144 -26.373  1.00 13.25           C  
ANISOU 2581  CA  ASP A 371     1411   2267   1356    526   -427    459       C  
ATOM   2582  C   ASP A 371     -18.787  66.455 -25.030  1.00 37.57           C  
ANISOU 2582  C   ASP A 371     4460   5324   4491    416   -429    423       C  
ATOM   2583  O   ASP A 371     -17.745  66.605 -24.392  1.00 46.76           O  
ANISOU 2583  O   ASP A 371     5643   6432   5690    374   -392    426       O  
ATOM   2584  CB  ASP A 371     -18.691  68.639 -26.249  1.00 62.11           C  
ANISOU 2584  CB  ASP A 371     7626   8416   7557    592   -365    514       C  
ATOM   2585  CG  ASP A 371     -18.575  69.322 -27.597  1.00 77.74           C  
ANISOU 2585  CG  ASP A 371     9663  10395   9480    710   -340    563       C  
ATOM   2586  OD1 ASP A 371     -18.190  68.642 -28.569  1.00 45.26           O  
ANISOU 2586  OD1 ASP A 371     5579   6291   5326    724   -361    554       O  
ATOM   2587  OD2 ASP A 371     -18.863  70.533 -27.683  1.00101.92           O1-
ANISOU 2587  OD2 ASP A 371    12747  13443  12537    794   -294    615       O1-
ATOM   2588  N   LEU A 372     -19.794  65.691 -24.612  1.00 35.06           N  
ANISOU 2588  N   LEU A 372     4095   5050   4176    376   -471    390       N  
ATOM   2589  CA  LEU A 372     -19.737  64.988 -23.333  1.00 49.52           C  
ANISOU 2589  CA  LEU A 372     5905   6859   6049    285   -467    364       C  
ATOM   2590  C   LEU A 372     -18.495  64.108 -23.224  1.00 49.62           C  
ANISOU 2590  C   LEU A 372     5956   6822   6074    229   -454    350       C  
ATOM   2591  O   LEU A 372     -17.958  63.912 -22.132  1.00 57.55           O  
ANISOU 2591  O   LEU A 372     6964   7793   7110    177   -432    342       O  
ATOM   2592  CB  LEU A 372     -21.001  64.156 -23.100  1.00 18.31           C  
ANISOU 2592  CB  LEU A 372     1901   2960   2097    256   -512    331       C  
ATOM   2593  CG  LEU A 372     -20.990  63.256 -21.860  1.00 39.02           C  
ANISOU 2593  CG  LEU A 372     4511   5558   4755    171   -505    310       C  
ATOM   2594  CD1 LEU A 372     -20.738  64.057 -20.581  1.00 32.42           C  
ANISOU 2594  CD1 LEU A 372     3675   4692   3950    155   -463    327       C  
ATOM   2595  CD2 LEU A 372     -22.283  62.457 -21.759  1.00 20.57           C  
ANISOU 2595  CD2 LEU A 372     2119   3275   2423    146   -547    277       C  
ATOM   2596  N   TRP A 373     -18.042  63.583 -24.357  1.00 23.10           N  
ANISOU 2596  N   TRP A 373     2627   3463   2687    249   -471    346       N  
ATOM   2597  CA  TRP A 373     -16.861  62.728 -24.381  1.00 30.27           C  
ANISOU 2597  CA  TRP A 373     3570   4326   3604    206   -460    334       C  
ATOM   2598  C   TRP A 373     -15.618  63.477 -23.917  1.00 40.85           C  
ANISOU 2598  C   TRP A 373     4935   5617   4969    203   -414    349       C  
ATOM   2599  O   TRP A 373     -14.708  62.888 -23.350  1.00 23.05           O  
ANISOU 2599  O   TRP A 373     2694   3330   2733    158   -402    334       O  
ATOM   2600  CB  TRP A 373     -16.629  62.176 -25.789  1.00 33.05           C  
ANISOU 2600  CB  TRP A 373     3951   4690   3917    239   -485    329       C  
ATOM   2601  CG  TRP A 373     -16.301  63.236 -26.783  1.00 37.52           C  
ANISOU 2601  CG  TRP A 373     4546   5256   4453    321   -467    362       C  
ATOM   2602  CD1 TRP A 373     -17.175  63.897 -27.598  1.00 63.74           C  
ANISOU 2602  CD1 TRP A 373     7860   8625   7731    403   -484    380       C  
ATOM   2603  CD2 TRP A 373     -15.004  63.769 -27.063  1.00 40.75           C  
ANISOU 2603  CD2 TRP A 373     4998   5615   4869    340   -423    386       C  
ATOM   2604  CE2 TRP A 373     -15.163  64.751 -28.066  1.00 51.86           C  
ANISOU 2604  CE2 TRP A 373     6433   7035   6238    435   -407    425       C  
ATOM   2605  CE3 TRP A 373     -13.722  63.514 -26.567  1.00 26.27           C  
ANISOU 2605  CE3 TRP A 373     3181   3730   3068    292   -395    379       C  
ATOM   2606  NE1 TRP A 373     -16.499  64.810 -28.375  1.00 48.67           N  
ANISOU 2606  NE1 TRP A 373     5999   6693   5799    476   -446    421       N  
ATOM   2607  CZ2 TRP A 373     -14.090  65.472 -28.579  1.00 25.98           C  
ANISOU 2607  CZ2 TRP A 373     3204   3708   2959    478   -355    462       C  
ATOM   2608  CZ3 TRP A 373     -12.662  64.232 -27.073  1.00 23.13           C  
ANISOU 2608  CZ3 TRP A 373     2820   3295   2672    331   -354    406       C  
ATOM   2609  CH2 TRP A 373     -12.851  65.199 -28.070  1.00 40.03           C  
ANISOU 2609  CH2 TRP A 373     4993   5437   4780    420   -330    449       C  
ATOM   2610  N   LEU A 374     -15.578  64.781 -24.165  1.00 24.38           N  
ANISOU 2610  N   LEU A 374     2853   3528   2882    260   -388    380       N  
ATOM   2611  CA  LEU A 374     -14.430  65.581 -23.768  1.00 36.87           C  
ANISOU 2611  CA  LEU A 374     4451   5064   4493    262   -346    392       C  
ATOM   2612  C   LEU A 374     -14.494  65.862 -22.280  1.00 43.78           C  
ANISOU 2612  C   LEU A 374     5295   5934   5406    218   -335    377       C  
ATOM   2613  O   LEU A 374     -13.475  65.852 -21.586  1.00 27.46           O  
ANISOU 2613  O   LEU A 374     3229   3839   3364    187   -320    359       O  
ATOM   2614  CB  LEU A 374     -14.378  66.892 -24.554  1.00 37.18           C  
ANISOU 2614  CB  LEU A 374     4515   5091   4523    346   -311    440       C  
ATOM   2615  CG  LEU A 374     -13.266  67.878 -24.185  1.00 46.55           C  
ANISOU 2615  CG  LEU A 374     5715   6220   5752    358   -259    459       C  
ATOM   2616  CD1 LEU A 374     -11.918  67.184 -24.084  1.00 47.99           C  
ANISOU 2616  CD1 LEU A 374     5908   6374   5951    311   -259    432       C  
ATOM   2617  CD2 LEU A 374     -13.202  69.012 -25.194  1.00 55.67           C  
ANISOU 2617  CD2 LEU A 374     6917   7340   6896    453   -206    519       C  
ATOM   2618  N   ASN A 375     -15.707  66.119 -21.799  1.00 41.99           N  
ANISOU 2618  N   ASN A 375     5037   5739   5179    222   -346    380       N  
ATOM   2619  CA  ASN A 375     -15.938  66.336 -20.382  1.00 34.07           C  
ANISOU 2619  CA  ASN A 375     4005   4736   4204    185   -338    365       C  
ATOM   2620  C   ASN A 375     -15.436  65.121 -19.620  1.00 56.32           C  
ANISOU 2620  C   ASN A 375     6831   7545   7025    123   -348    333       C  
ATOM   2621  O   ASN A 375     -14.616  65.238 -18.705  1.00 32.18           O  
ANISOU 2621  O   ASN A 375     3774   4469   3985    101   -333    315       O  
ATOM   2622  CB  ASN A 375     -17.432  66.539 -20.124  1.00 55.72           C  
ANISOU 2622  CB  ASN A 375     6711   7518   6940    198   -354    373       C  
ATOM   2623  CG  ASN A 375     -17.712  67.193 -18.787  1.00 62.65           C  
ANISOU 2623  CG  ASN A 375     7562   8395   7847    183   -336    368       C  
ATOM   2624  ND2 ASN A 375     -18.328  66.447 -17.873  1.00 71.15           N  
ANISOU 2624  ND2 ASN A 375     8619   9489   8925    139   -350    349       N  
ATOM   2625  OD1 ASN A 375     -17.392  68.359 -18.583  1.00 77.80           O  
ANISOU 2625  OD1 ASN A 375     9477  10295   9790    216   -308    383       O  
ATOM   2626  N   GLU A 376     -15.923  63.953 -20.033  1.00 44.00           N  
ANISOU 2626  N   GLU A 376     5275   5999   5445    102   -375    325       N  
ATOM   2627  CA  GLU A 376     -15.590  62.684 -19.396  1.00 60.06           C  
ANISOU 2627  CA  GLU A 376     7322   8022   7478     55   -382    305       C  
ATOM   2628  C   GLU A 376     -14.167  62.219 -19.702  1.00 63.25           C  
ANISOU 2628  C   GLU A 376     7759   8393   7880     48   -373    295       C  
ATOM   2629  O   GLU A 376     -13.491  61.657 -18.839  1.00 47.10           O  
ANISOU 2629  O   GLU A 376     5723   6335   5837     25   -366    280       O  
ATOM   2630  CB  GLU A 376     -16.607  61.611 -19.795  1.00 47.76           C  
ANISOU 2630  CB  GLU A 376     5753   6488   5906     38   -414    301       C  
ATOM   2631  CG  GLU A 376     -17.975  61.837 -19.179  1.00 44.28           C  
ANISOU 2631  CG  GLU A 376     5270   6082   5472     34   -424    303       C  
ATOM   2632  CD  GLU A 376     -17.881  62.110 -17.687  1.00 57.02           C  
ANISOU 2632  CD  GLU A 376     6877   7686   7102     14   -401    302       C  
ATOM   2633  OE1 GLU A 376     -17.167  61.352 -16.993  1.00 40.89           O  
ANISOU 2633  OE1 GLU A 376     4856   5622   5056    -11   -392    294       O  
ATOM   2634  OE2 GLU A 376     -18.512  63.083 -17.214  1.00 46.30           O1-
ANISOU 2634  OE2 GLU A 376     5491   6345   5756     31   -392    310       O1-
ATOM   2635  N   GLY A 377     -13.715  62.455 -20.928  1.00 48.79           N  
ANISOU 2635  N   GLY A 377     5944   6554   6039     77   -374    304       N  
ATOM   2636  CA  GLY A 377     -12.353  62.126 -21.305  1.00 10.31           C  
ANISOU 2636  CA  GLY A 377     1099   1652   1166     75   -365    296       C  
ATOM   2637  C   GLY A 377     -11.360  62.831 -20.408  1.00 40.17           C  
ANISOU 2637  C   GLY A 377     4873   5420   4971     73   -342    282       C  
ATOM   2638  O   GLY A 377     -10.422  62.228 -19.889  1.00 22.79           O  
ANISOU 2638  O   GLY A 377     2681   3209   2771     55   -341    260       O  
ATOM   2639  N   PHE A 378     -11.579  64.123 -20.215  1.00 28.83           N  
ANISOU 2639  N   PHE A 378     3416   3987   3552     96   -328    293       N  
ATOM   2640  CA  PHE A 378     -10.653  64.932 -19.441  1.00 24.69           C  
ANISOU 2640  CA  PHE A 378     2873   3453   3056     97   -311    273       C  
ATOM   2641  C   PHE A 378     -10.634  64.508 -17.969  1.00 40.91           C  
ANISOU 2641  C   PHE A 378     4913   5522   5109     67   -317    240       C  
ATOM   2642  O   PHE A 378      -9.572  64.447 -17.348  1.00 37.59           O  
ANISOU 2642  O   PHE A 378     4486   5102   4696     61   -316    205       O  
ATOM   2643  CB  PHE A 378     -10.990  66.419 -19.591  1.00 28.01           C  
ANISOU 2643  CB  PHE A 378     3271   3868   3504    136   -291    297       C  
ATOM   2644  CG  PHE A 378     -10.057  67.325 -18.850  1.00 42.14           C  
ANISOU 2644  CG  PHE A 378     5021   5647   5344    139   -274    266       C  
ATOM   2645  CD1 PHE A 378      -8.873  67.738 -19.424  1.00 36.45           C  
ANISOU 2645  CD1 PHE A 378     4309   4884   4655    143   -227    249       C  
ATOM   2646  CD2 PHE A 378     -10.360  67.761 -17.572  1.00 40.09           C  
ANISOU 2646  CD2 PHE A 378     4724   5404   5104    121   -271    234       C  
ATOM   2647  CE1 PHE A 378      -8.011  68.565 -18.737  1.00 27.84           C  
ANISOU 2647  CE1 PHE A 378     3189   3767   3622    119   -172    189       C  
ATOM   2648  CE2 PHE A 378      -9.501  68.592 -16.883  1.00 42.13           C  
ANISOU 2648  CE2 PHE A 378     4955   5641   5412    103   -224    177       C  
ATOM   2649  CZ  PHE A 378      -8.330  68.997 -17.468  1.00 41.01           C  
ANISOU 2649  CZ  PHE A 378     4819   5456   5309     99   -173    150       C  
ATOM   2650  N   ALA A 379     -11.808  64.209 -17.419  1.00 52.28           N  
ANISOU 2650  N   ALA A 379     6347   6978   6537     55   -324    250       N  
ATOM   2651  CA  ALA A 379     -11.906  63.799 -16.023  1.00 29.03           C  
ANISOU 2651  CA  ALA A 379     3395   4049   3585     38   -326    228       C  
ATOM   2652  C   ALA A 379     -11.185  62.479 -15.796  1.00 39.01           C  
ANISOU 2652  C   ALA A 379     4684   5309   4827     26   -335    214       C  
ATOM   2653  O   ALA A 379     -10.525  62.292 -14.775  1.00 47.47           O  
ANISOU 2653  O   ALA A 379     5754   6394   5889     31   -335    186       O  
ATOM   2654  CB  ALA A 379     -13.352  63.688 -15.604  1.00 39.50           C  
ANISOU 2654  CB  ALA A 379     4708   5393   4905     29   -330    247       C  
ATOM   2655  N   LYS A 380     -11.316  61.567 -16.753  1.00 43.11           N  
ANISOU 2655  N   LYS A 380     5227   5816   5337     18   -343    232       N  
ATOM   2656  CA  LYS A 380     -10.590  60.305 -16.706  1.00 30.18           C  
ANISOU 2656  CA  LYS A 380     3615   4171   3682     12   -351    223       C  
ATOM   2657  C   LYS A 380      -9.090  60.568 -16.718  1.00 47.73           C  
ANISOU 2657  C   LYS A 380     5839   6388   5908     29   -346    196       C  
ATOM   2658  O   LYS A 380      -8.362  60.103 -15.843  1.00 35.86           O  
ANISOU 2658  O   LYS A 380     4338   4899   4390     40   -349    172       O  
ATOM   2659  CB  LYS A 380     -10.976  59.419 -17.892  1.00 29.85           C  
ANISOU 2659  CB  LYS A 380     3593   4116   3634      1   -363    242       C  
ATOM   2660  CG  LYS A 380     -12.390  58.876 -17.825  1.00 52.61           C  
ANISOU 2660  CG  LYS A 380     6467   7010   6511    -18   -377    258       C  
ATOM   2661  CD  LYS A 380     -12.710  58.012 -19.030  1.00 50.90           C  
ANISOU 2661  CD  LYS A 380     6266   6788   6286    -27   -397    266       C  
ATOM   2662  CE  LYS A 380     -13.906  57.116 -18.749  1.00 52.98           C  
ANISOU 2662  CE  LYS A 380     6521   7067   6544    -52   -417    272       C  
ATOM   2663  NZ  LYS A 380     -13.668  56.219 -17.583  1.00 60.73           N1+
ANISOU 2663  NZ  LYS A 380     7517   8043   7515    -65   -413    272       N1+
ATOM   2664  N   PHE A 381      -8.639  61.318 -17.721  1.00 23.62           N  
ANISOU 2664  N   PHE A 381     2782   3321   2871     38   -340    199       N  
ATOM   2665  CA  PHE A 381      -7.228  61.664 -17.863  1.00 37.02           C  
ANISOU 2665  CA  PHE A 381     4472   5015   4579     52   -337    172       C  
ATOM   2666  C   PHE A 381      -6.720  62.336 -16.595  1.00 46.73           C  
ANISOU 2666  C   PHE A 381     5667   6271   5819     59   -337    128       C  
ATOM   2667  O   PHE A 381      -5.594  62.101 -16.153  1.00 43.08           O  
ANISOU 2667  O   PHE A 381     5192   5823   5351     71   -345     88       O  
ATOM   2668  CB  PHE A 381      -7.041  62.586 -19.074  1.00 56.82           C  
ANISOU 2668  CB  PHE A 381     6975   7505   7109     65   -328    190       C  
ATOM   2669  CG  PHE A 381      -5.681  63.226 -19.158  1.00 52.57           C  
ANISOU 2669  CG  PHE A 381     6410   6965   6599     78   -322    159       C  
ATOM   2670  CD1 PHE A 381      -4.556  62.469 -19.442  1.00 50.17           C  
ANISOU 2670  CD1 PHE A 381     6116   6659   6287     81   -330    140       C  
ATOM   2671  CD2 PHE A 381      -5.534  64.592 -18.984  1.00 30.76           C  
ANISOU 2671  CD2 PHE A 381     3599   4203   3885     86   -308    144       C  
ATOM   2672  CE1 PHE A 381      -3.309  63.063 -19.533  1.00 45.61           C  
ANISOU 2672  CE1 PHE A 381     5496   6087   5748     89   -325    101       C  
ATOM   2673  CE2 PHE A 381      -4.289  65.190 -19.073  1.00 49.83           C  
ANISOU 2673  CE2 PHE A 381     5970   6610   6353     86   -285     98       C  
ATOM   2674  CZ  PHE A 381      -3.176  64.427 -19.348  1.00 54.05           C  
ANISOU 2674  CZ  PHE A 381     6504   7152   6879     87   -301     75       C  
ATOM   2675  N   MET A 382      -7.571  63.164 -16.003  1.00 55.33           N  
ANISOU 2675  N   MET A 382     6735   7369   6919     55   -331    130       N  
ATOM   2676  CA  MET A 382      -7.200  63.915 -14.819  1.00 45.96           C  
ANISOU 2676  CA  MET A 382     5509   6208   5744     61   -332     81       C  
ATOM   2677  C   MET A 382      -7.160  63.023 -13.581  1.00 48.30           C  
ANISOU 2677  C   MET A 382     5815   6536   6001     71   -345     61       C  
ATOM   2678  O   MET A 382      -6.504  63.362 -12.598  1.00 23.97           O  
ANISOU 2678  O   MET A 382     2702   3488   2916     86   -354      6       O  
ATOM   2679  CB  MET A 382      -8.163  65.087 -14.621  1.00 35.00           C  
ANISOU 2679  CB  MET A 382     4096   4819   4385     57   -320     93       C  
ATOM   2680  CG  MET A 382      -7.584  66.257 -13.843  1.00 54.67           C  
ANISOU 2680  CG  MET A 382     6528   7327   6918     57   -311     30       C  
ATOM   2681  SD  MET A 382      -6.006  66.872 -14.477  1.00 56.96           S  
ANISOU 2681  SD  MET A 382     6767   7605   7270     51   -295    -27       S  
ATOM   2682  CE  MET A 382      -6.311  66.882 -16.236  1.00 31.79           C  
ANISOU 2682  CE  MET A 382     3610   4373   4095     63   -280     51       C  
ATOM   2683  N   GLU A 383      -7.857  61.886 -13.636  1.00 42.26           N  
ANISOU 2683  N   GLU A 383     5087   5764   5208     66   -348    101       N  
ATOM   2684  CA  GLU A 383      -7.810  60.902 -12.556  1.00 29.44           C  
ANISOU 2684  CA  GLU A 383     3475   4165   3545     84   -358     94       C  
ATOM   2685  C   GLU A 383      -6.361  60.545 -12.288  1.00 47.43           C  
ANISOU 2685  C   GLU A 383     5748   6467   5805    114   -372     49       C  
ATOM   2686  O   GLU A 383      -5.962  60.314 -11.149  1.00 39.56           O  
ANISOU 2686  O   GLU A 383     4742   5511   4776    148   -386     17       O  
ATOM   2687  CB  GLU A 383      -8.546  59.611 -12.933  1.00 32.67           C  
ANISOU 2687  CB  GLU A 383     3922   4555   3938     70   -359    139       C  
ATOM   2688  CG  GLU A 383     -10.048  59.706 -13.109  1.00 62.46           C  
ANISOU 2688  CG  GLU A 383     7693   8317   7723     42   -353    176       C  
ATOM   2689  CD  GLU A 383     -10.670  58.347 -13.410  1.00 79.17           C  
ANISOU 2689  CD  GLU A 383     9837  10420   9826     26   -360    207       C  
ATOM   2690  OE1 GLU A 383     -11.854  58.293 -13.802  1.00 63.04           O  
ANISOU 2690  OE1 GLU A 383     7787   8372   7795      1   -362    232       O  
ATOM   2691  OE2 GLU A 383      -9.964  57.329 -13.254  1.00 82.69           O1-
ANISOU 2691  OE2 GLU A 383    10308  10863  10247     42   -366    204       O1-
ATOM   2692  N   PHE A 384      -5.575  60.493 -13.357  1.00 40.30           N  
ANISOU 2692  N   PHE A 384     4850   5543   4921    109   -371     47       N  
ATOM   2693  CA  PHE A 384      -4.206  60.009 -13.274  1.00 43.99           C  
ANISOU 2693  CA  PHE A 384     5309   6032   5372    139   -385      8       C  
ATOM   2694  C   PHE A 384      -3.237  61.119 -12.936  1.00 54.38           C  
ANISOU 2694  C   PHE A 384     6568   7380   6714    147   -392    -64       C  
ATOM   2695  O   PHE A 384      -2.495  61.027 -11.957  1.00 82.75           O  
ANISOU 2695  O   PHE A 384    10133  11025  10284    182   -412   -121       O  
ATOM   2696  CB  PHE A 384      -3.814  59.326 -14.579  1.00 45.35           C  
ANISOU 2696  CB  PHE A 384     5511   6169   5552    129   -381     37       C  
ATOM   2697  CG  PHE A 384      -4.735  58.213 -14.954  1.00 96.50           C  
ANISOU 2697  CG  PHE A 384    12035  12618  12013    114   -376     91       C  
ATOM   2698  CD1 PHE A 384      -4.538  56.938 -14.455  1.00 95.32           C  
ANISOU 2698  CD1 PHE A 384    11912  12478  11826    138   -386     97       C  
ATOM   2699  CD2 PHE A 384      -5.826  58.448 -15.773  1.00114.06           C  
ANISOU 2699  CD2 PHE A 384    14269  14810  14258     80   -365    130       C  
ATOM   2700  CE1 PHE A 384      -5.398  55.910 -14.782  1.00 70.97           C  
ANISOU 2700  CE1 PHE A 384     8865   9367   8734    120   -383    139       C  
ATOM   2701  CE2 PHE A 384      -6.691  57.424 -16.106  1.00103.10           C  
ANISOU 2701  CE2 PHE A 384    12910  13403  12859     63   -367    165       C  
ATOM   2702  CZ  PHE A 384      -6.476  56.153 -15.610  1.00 74.79           C  
ANISOU 2702  CZ  PHE A 384     9351   9822   9244     78   -376    168       C  
ATOM   2703  N   VAL A 385      -3.251  62.174 -13.740  1.00 24.09           N  
ANISOU 2703  N   VAL A 385     2708   3516   2929    119   -377    -66       N  
ATOM   2704  CA  VAL A 385      -2.392  63.314 -13.481  1.00 40.30           C  
ANISOU 2704  CA  VAL A 385     4691   5591   5029    113   -376   -144       C  
ATOM   2705  C   VAL A 385      -2.435  63.692 -12.000  1.00 38.18           C  
ANISOU 2705  C   VAL A 385     4386   5375   4744    130   -390   -204       C  
ATOM   2706  O   VAL A 385      -1.395  63.907 -11.378  1.00 57.62           O  
ANISOU 2706  O   VAL A 385     6794   7885   7213    146   -406   -290       O  
ATOM   2707  CB  VAL A 385      -2.799  64.514 -14.341  1.00 46.67           C  
ANISOU 2707  CB  VAL A 385     5474   6356   5901     80   -347   -127       C  
ATOM   2708  CG1 VAL A 385      -1.821  65.663 -14.137  1.00 44.18           C  
ANISOU 2708  CG1 VAL A 385     5071   6053   5663     61   -326   -220       C  
ATOM   2709  CG2 VAL A 385      -2.864  64.104 -15.808  1.00 24.96           C  
ANISOU 2709  CG2 VAL A 385     2766   3564   3155     77   -338    -61       C  
ATOM   2710  N   SER A 386      -3.639  63.744 -11.437  1.00 36.41           N  
ANISOU 2710  N   SER A 386     4188   5148   4499    127   -386   -164       N  
ATOM   2711  CA  SER A 386      -3.822  64.077 -10.024  1.00 45.87           C  
ANISOU 2711  CA  SER A 386     5358   6397   5675    147   -400   -212       C  
ATOM   2712  C   SER A 386      -3.274  63.013  -9.077  1.00 41.67           C  
ANISOU 2712  C   SER A 386     4837   5920   5074    201   -430   -235       C  
ATOM   2713  O   SER A 386      -2.389  63.292  -8.271  1.00 38.40           O  
ANISOU 2713  O   SER A 386     4373   5567   4651    231   -454   -321       O  
ATOM   2714  CB  SER A 386      -5.303  64.334  -9.711  1.00 24.20           C  
ANISOU 2714  CB  SER A 386     2638   3632   2924    133   -386   -156       C  
ATOM   2715  OG  SER A 386      -6.087  63.170  -9.910  1.00 47.94           O  
ANISOU 2715  OG  SER A 386     5705   6619   5892    137   -384    -80       O  
ATOM   2716  N   VAL A 387      -3.805  61.797  -9.179  1.00 34.58           N  
ANISOU 2716  N   VAL A 387     4001   5005   4132    217   -429   -164       N  
ATOM   2717  CA  VAL A 387      -3.459  60.727  -8.247  1.00 47.15           C  
ANISOU 2717  CA  VAL A 387     5613   6644   5656    277   -453   -170       C  
ATOM   2718  C   VAL A 387      -1.978  60.354  -8.287  1.00 52.70           C  
ANISOU 2718  C   VAL A 387     6291   7391   6343    319   -478   -229       C  
ATOM   2719  O   VAL A 387      -1.355  60.185  -7.241  1.00 63.27           O  
ANISOU 2719  O   VAL A 387     7605   8801   7633    380   -510   -286       O  
ATOM   2720  CB  VAL A 387      -4.329  59.468  -8.461  1.00 28.04           C  
ANISOU 2720  CB  VAL A 387     3261   4186   3206    277   -439    -84       C  
ATOM   2721  CG1 VAL A 387      -3.896  58.366  -7.521  1.00 17.05           C  
ANISOU 2721  CG1 VAL A 387     1896   2840   1741    350   -460    -87       C  
ATOM   2722  CG2 VAL A 387      -5.794  59.789  -8.231  1.00 41.39           C  
ANISOU 2722  CG2 VAL A 387     4966   5852   4909    243   -420    -37       C  
ATOM   2723  N   SER A 388      -1.416  60.230  -9.486  1.00 36.36           N  
ANISOU 2723  N   SER A 388     4224   5283   4309    292   -468   -219       N  
ATOM   2724  CA  SER A 388       0.003  59.911  -9.637  1.00 37.71           C  
ANISOU 2724  CA  SER A 388     4363   5493   4472    327   -491   -277       C  
ATOM   2725  C   SER A 388       0.853  60.751  -8.692  1.00 46.62           C  
ANISOU 2725  C   SER A 388     5409   6701   5603    354   -521   -391       C  
ATOM   2726  O   SER A 388       1.893  60.309  -8.203  1.00 63.20           O  
ANISOU 2726  O   SER A 388     7478   8869   7665    413   -555   -452       O  
ATOM   2727  CB  SER A 388       0.458  60.163 -11.073  1.00 35.45           C  
ANISOU 2727  CB  SER A 388     4071   5155   4244    281   -472   -265       C  
ATOM   2728  OG  SER A 388      -0.385  59.495 -11.992  1.00 67.63           O  
ANISOU 2728  OG  SER A 388     8214   9162   8318    253   -448   -171       O  
ATOM   2729  N   VAL A 389       0.396  61.972  -8.451  1.00 40.13           N  
ANISOU 2729  N   VAL A 389     4547   5872   4827    313   -508   -425       N  
ATOM   2730  CA  VAL A 389       1.070  62.901  -7.562  1.00 53.34           C  
ANISOU 2730  CA  VAL A 389     6133   7616   6518    324   -530   -546       C  
ATOM   2731  C   VAL A 389       0.582  62.675  -6.135  1.00 58.77           C  
ANISOU 2731  C   VAL A 389     6832   8367   7132    382   -558   -556       C  
ATOM   2732  O   VAL A 389       1.376  62.482  -5.214  1.00 49.83           O  
ANISOU 2732  O   VAL A 389     5658   7324   5951    447   -600   -637       O  
ATOM   2733  CB  VAL A 389       0.768  64.364  -7.979  1.00 42.25           C  
ANISOU 2733  CB  VAL A 389     4679   6167   5208    248   -494   -580       C  
ATOM   2734  CG1 VAL A 389       1.326  65.345  -6.963  1.00 37.76           C  
ANISOU 2734  CG1 VAL A 389     4016   5667   4665    249   -510   -715       C  
ATOM   2735  CG2 VAL A 389       1.317  64.651  -9.371  1.00 33.39           C  
ANISOU 2735  CG2 VAL A 389     3541   4985   4161    198   -462   -573       C  
ATOM   2736  N   THR A 390      -0.740  62.672  -5.980  1.00 51.76           N  
ANISOU 2736  N   THR A 390     5999   7435   6233    362   -535   -475       N  
ATOM   2737  CA  THR A 390      -1.396  62.654  -4.678  1.00 45.54           C  
ANISOU 2737  CA  THR A 390     5222   6695   5386    406   -552   -478       C  
ATOM   2738  C   THR A 390      -1.223  61.350  -3.901  1.00 71.18           C  
ANISOU 2738  C   THR A 390     8517   9993   8535    496   -580   -450       C  
ATOM   2739  O   THR A 390      -0.875  61.368  -2.719  1.00 45.55           O  
ANISOU 2739  O   THR A 390     5247   6833   5228    567   -618   -512       O  
ATOM   2740  CB  THR A 390      -2.895  62.931  -4.831  1.00 49.53           C  
ANISOU 2740  CB  THR A 390     5772   7135   5912    357   -516   -392       C  
ATOM   2741  CG2 THR A 390      -3.573  62.888  -3.485  1.00 70.76           C  
ANISOU 2741  CG2 THR A 390     8473   9872   8539    403   -532   -392       C  
ATOM   2742  OG1 THR A 390      -3.080  64.229  -5.402  1.00 81.61           O  
ANISOU 2742  OG1 THR A 390     9791  11160  10059    289   -491   -420       O  
ATOM   2743  N   HIS A 391      -1.488  60.227  -4.562  1.00 70.35           N  
ANISOU 2743  N   HIS A 391     8481   9836   8414    498   -561   -359       N  
ATOM   2744  CA  HIS A 391      -1.332  58.910  -3.949  1.00 62.72           C  
ANISOU 2744  CA  HIS A 391     7570   8903   7359    584   -578   -323       C  
ATOM   2745  C   HIS A 391      -0.452  58.010  -4.813  1.00 61.12           C  
ANISOU 2745  C   HIS A 391     7384   8684   7155    599   -580   -308       C  
ATOM   2746  O   HIS A 391      -0.957  57.127  -5.507  1.00 64.61           O  
ANISOU 2746  O   HIS A 391     7889   9059   7601    577   -552   -224       O  
ATOM   2747  CB  HIS A 391      -2.696  58.242  -3.758  1.00 73.90           C  
ANISOU 2747  CB  HIS A 391     9061  10265   8751    574   -546   -221       C  
ATOM   2748  CG  HIS A 391      -3.668  59.052  -2.959  1.00 54.13           C  
ANISOU 2748  CG  HIS A 391     6548   7772   6249    559   -539   -223       C  
ATOM   2749  CD2 HIS A 391      -4.572  59.987  -3.338  1.00 58.47           C  
ANISOU 2749  CD2 HIS A 391     7078   8274   6863    479   -514   -208       C  
ATOM   2750  ND1 HIS A 391      -3.797  58.927  -1.593  1.00 58.80           N  
ANISOU 2750  ND1 HIS A 391     7152   8429   6759    638   -561   -240       N  
ATOM   2751  CE1 HIS A 391      -4.733  59.755  -1.162  1.00 61.24           C  
ANISOU 2751  CE1 HIS A 391     7449   8732   7088    602   -549   -238       C  
ATOM   2752  NE2 HIS A 391      -5.220  60.410  -2.202  1.00 52.44           N  
ANISOU 2752  NE2 HIS A 391     6313   7548   6063    506   -521   -219       N  
ATOM   2753  N   PRO A 392       0.873  58.224  -4.769  1.00 61.37           N  
ANISOU 2753  N   PRO A 392     7355   8782   7182    637   -616   -398       N  
ATOM   2754  CA  PRO A 392       1.790  57.486  -5.647  1.00 66.15           C  
ANISOU 2754  CA  PRO A 392     7967   9375   7791    648   -620   -391       C  
ATOM   2755  C   PRO A 392       1.813  56.001  -5.306  1.00 72.83           C  
ANISOU 2755  C   PRO A 392     8889  10230   8552    733   -624   -328       C  
ATOM   2756  O   PRO A 392       1.989  55.160  -6.189  1.00 61.02           O  
ANISOU 2756  O   PRO A 392     7436   8684   7066    721   -607   -276       O  
ATOM   2757  CB  PRO A 392       3.158  58.115  -5.341  1.00 43.63           C  
ANISOU 2757  CB  PRO A 392     5018   6615   4944    684   -664   -520       C  
ATOM   2758  CG  PRO A 392       2.863  59.379  -4.579  1.00 57.63           C  
ANISOU 2758  CG  PRO A 392     6728   8425   6742    659   -674   -595       C  
ATOM   2759  CD  PRO A 392       1.588  59.123  -3.849  1.00 42.37           C  
ANISOU 2759  CD  PRO A 392     4863   6472   4763    674   -658   -518       C  
ATOM   2760  N   GLU A 393       1.630  55.692  -4.026  1.00 55.34           N  
ANISOU 2760  N   GLU A 393     6695   8078   6253    821   -645   -333       N  
ATOM   2761  CA  GLU A 393       1.657  54.320  -3.540  1.00 38.23           C  
ANISOU 2761  CA  GLU A 393     4608   5923   3993    919   -646   -274       C  
ATOM   2762  C   GLU A 393       0.666  53.422  -4.276  1.00 53.63           C  
ANISOU 2762  C   GLU A 393     6646   7764   5966    864   -592   -160       C  
ATOM   2763  O   GLU A 393       0.880  52.212  -4.380  1.00 54.66           O  
ANISOU 2763  O   GLU A 393     6842   7879   6048    921   -582   -109       O  
ATOM   2764  CB  GLU A 393       1.369  54.280  -2.037  1.00 69.21           C  
ANISOU 2764  CB  GLU A 393     8553   9922   7823   1017   -667   -285       C  
ATOM   2765  CG  GLU A 393      -0.032  54.750  -1.647  1.00 82.67           C  
ANISOU 2765  CG  GLU A 393    10284  11578   9548    961   -634   -237       C  
ATOM   2766  CD  GLU A 393      -0.106  56.245  -1.377  1.00 95.50           C  
ANISOU 2766  CD  GLU A 393    11823  13238  11226    906   -653   -320       C  
ATOM   2767  OE1 GLU A 393      -1.187  56.721  -0.970  1.00108.72           O  
ANISOU 2767  OE1 GLU A 393    13512  14886  12912    869   -632   -290       O  
ATOM   2768  OE2 GLU A 393       0.912  56.943  -1.561  1.00 79.82           O1-
ANISOU 2768  OE2 GLU A 393     9753  11306   9270    901   -688   -418       O1-
ATOM   2769  N   LEU A 394      -0.415  54.009  -4.782  1.00 55.96           N  
ANISOU 2769  N   LEU A 394     6939   7988   6335    759   -559   -125       N  
ATOM   2770  CA  LEU A 394      -1.458  53.229  -5.446  1.00 36.85           C  
ANISOU 2770  CA  LEU A 394     4588   5474   3939    702   -515    -32       C  
ATOM   2771  C   LEU A 394      -1.018  52.688  -6.810  1.00 48.12           C  
ANISOU 2771  C   LEU A 394     6026   6846   5413    657   -503    -12       C  
ATOM   2772  O   LEU A 394      -1.555  51.683  -7.282  1.00 86.89           O  
ANISOU 2772  O   LEU A 394    10999  11695  10320    640   -476     54       O  
ATOM   2773  CB  LEU A 394      -2.740  54.052  -5.599  1.00 39.88           C  
ANISOU 2773  CB  LEU A 394     4958   5811   4384    610   -490     -9       C  
ATOM   2774  CG  LEU A 394      -3.358  54.630  -4.326  1.00 46.76           C  
ANISOU 2774  CG  LEU A 394     5822   6726   5217    642   -496    -22       C  
ATOM   2775  CD1 LEU A 394      -4.740  55.186  -4.627  1.00 63.31           C  
ANISOU 2775  CD1 LEU A 394     7916   8765   7373    552   -467     19       C  
ATOM   2776  CD2 LEU A 394      -3.431  53.578  -3.242  1.00 37.78           C  
ANISOU 2776  CD2 LEU A 394     4757   5619   3979    747   -494     16       C  
ATOM   2777  N   LYS A 395      -0.050  53.351  -7.437  1.00 30.98           N  
ANISOU 2777  N   LYS A 395     3793   4695   3281    637   -523    -72       N  
ATOM   2778  CA  LYS A 395       0.444  52.944  -8.750  1.00 58.78           C  
ANISOU 2778  CA  LYS A 395     7321   8168   6843    598   -512    -57       C  
ATOM   2779  C   LYS A 395      -0.636  52.987  -9.823  1.00 64.79           C  
ANISOU 2779  C   LYS A 395     8107   8840   7669    498   -477      1       C  
ATOM   2780  O   LYS A 395      -0.813  52.024 -10.571  1.00 83.78           O  
ANISOU 2780  O   LYS A 395    10560  11194  10077    482   -461     48       O  
ATOM   2781  CB  LYS A 395       1.042  51.534  -8.697  1.00 76.98           C  
ANISOU 2781  CB  LYS A 395     9684  10480   9084    675   -516    -27       C  
ATOM   2782  CG  LYS A 395       2.530  51.486  -8.411  1.00 59.72           C  
ANISOU 2782  CG  LYS A 395     7458   8377   6857    760   -556    -94       C  
ATOM   2783  CD  LYS A 395       2.859  52.117  -7.073  1.00 54.65           C  
ANISOU 2783  CD  LYS A 395     6769   7832   6164    832   -593   -160       C  
ATOM   2784  CE  LYS A 395       3.902  51.297  -6.335  1.00 65.19           C  
ANISOU 2784  CE  LYS A 395     8115   9251   7401    968   -628   -186       C  
ATOM   2785  NZ  LYS A 395       5.004  50.874  -7.241  1.00 82.71           N1+
ANISOU 2785  NZ  LYS A 395    10318  11474   9635    978   -640   -206       N1+
ATOM   2786  N   VAL A 396      -1.350  54.104  -9.904  1.00 64.05           N  
ANISOU 2786  N   VAL A 396     7978   8732   7625    436   -468     -8       N  
ATOM   2787  CA  VAL A 396      -2.430  54.259 -10.878  1.00 68.99           C  
ANISOU 2787  CA  VAL A 396     8620   9286   8306    352   -440     40       C  
ATOM   2788  C   VAL A 396      -1.946  54.105 -12.320  1.00 73.79           C  
ANISOU 2788  C   VAL A 396     9231   9852   8954    315   -433     48       C  
ATOM   2789  O   VAL A 396      -2.693  53.647 -13.186  1.00 71.41           O  
ANISOU 2789  O   VAL A 396     8961   9497   8675    269   -418     92       O  
ATOM   2790  CB  VAL A 396      -3.134  55.623 -10.721  1.00 56.85           C  
ANISOU 2790  CB  VAL A 396     7041   7750   6810    306   -433     24       C  
ATOM   2791  CG1 VAL A 396      -4.115  55.583  -9.560  1.00 63.55           C  
ANISOU 2791  CG1 VAL A 396     7903   8616   7628    322   -431     42       C  
ATOM   2792  CG2 VAL A 396      -2.109  56.730 -10.526  1.00 47.26           C  
ANISOU 2792  CG2 VAL A 396     5766   6581   5612    321   -450    -48       C  
ATOM   2793  N   GLY A 397      -0.693  54.484 -12.560  1.00 60.71           N  
ANISOU 2793  N   GLY A 397     7540   8226   7302    339   -448      0       N  
ATOM   2794  CA  GLY A 397      -0.113  54.460 -13.892  1.00 63.90           C  
ANISOU 2794  CA  GLY A 397     7944   8595   7740    310   -441      4       C  
ATOM   2795  C   GLY A 397      -0.444  53.233 -14.720  1.00 67.57           C  
ANISOU 2795  C   GLY A 397     8467   9009   8197    297   -430     57       C  
ATOM   2796  O   GLY A 397      -0.866  53.354 -15.872  1.00 33.83           O  
ANISOU 2796  O   GLY A 397     4205   4689   3961    247   -417     82       O  
ATOM   2797  N   ASP A 398      -0.251  52.054 -14.130  1.00 67.45           N  
ANISOU 2797  N   ASP A 398     8491   9008   8131    349   -437     71       N  
ATOM   2798  CA  ASP A 398      -0.482  50.780 -14.815  1.00 64.84           C  
ANISOU 2798  CA  ASP A 398     8218   8630   7788    343   -428    115       C  
ATOM   2799  C   ASP A 398      -1.871  50.674 -15.444  1.00 65.15           C  
ANISOU 2799  C   ASP A 398     8279   8615   7860    273   -412    155       C  
ATOM   2800  O   ASP A 398      -2.014  50.269 -16.599  1.00 66.79           O  
ANISOU 2800  O   ASP A 398     8508   8782   8089    237   -408    172       O  
ATOM   2801  CB  ASP A 398      -0.279  49.612 -13.843  1.00 63.62           C  
ANISOU 2801  CB  ASP A 398     8111   8496   7565    417   -431    131       C  
ATOM   2802  CG  ASP A 398       1.178  49.396 -13.478  1.00103.68           C  
ANISOU 2802  CG  ASP A 398    13171  13626  12596    500   -452     94       C  
ATOM   2803  OD1 ASP A 398       1.942  48.908 -14.339  1.00 94.04           O  
ANISOU 2803  OD1 ASP A 398    11961  12390  11379    506   -454     94       O  
ATOM   2804  OD2 ASP A 398       1.556  49.703 -12.324  1.00 98.79           O1-
ANISOU 2804  OD2 ASP A 398    12528  13072  11936    563   -471     62       O1-
ATOM   2805  N   TYR A 399      -2.889  51.043 -14.675  1.00 54.02           N  
ANISOU 2805  N   TYR A 399     6862   7213   6451    257   -408    165       N  
ATOM   2806  CA  TYR A 399      -4.272  50.857 -15.092  1.00 42.91           C  
ANISOU 2806  CA  TYR A 399     5470   5767   5067    198   -399    199       C  
ATOM   2807  C   TYR A 399      -4.671  51.787 -16.230  1.00 59.45           C  
ANISOU 2807  C   TYR A 399     7534   7842   7214    142   -397    195       C  
ATOM   2808  O   TYR A 399      -5.615  51.500 -16.968  1.00 65.22           O  
ANISOU 2808  O   TYR A 399     8276   8544   7961     99   -398    217       O  
ATOM   2809  CB  TYR A 399      -5.199  51.021 -13.888  1.00 34.81           C  
ANISOU 2809  CB  TYR A 399     4443   4760   4023    203   -395    211       C  
ATOM   2810  CG  TYR A 399      -4.708  50.215 -12.711  1.00 93.13           C  
ANISOU 2810  CG  TYR A 399    11867  12173  11346    278   -394    217       C  
ATOM   2811  CD1 TYR A 399      -5.021  48.864 -12.592  1.00 96.55           C  
ANISOU 2811  CD1 TYR A 399    12368  12576  11740    296   -382    258       C  
ATOM   2812  CD2 TYR A 399      -3.895  50.788 -11.741  1.00103.95           C  
ANISOU 2812  CD2 TYR A 399    13210  13598  12687    338   -405    182       C  
ATOM   2813  CE1 TYR A 399      -4.557  48.115 -11.528  1.00102.71           C  
ANISOU 2813  CE1 TYR A 399    13197  13378  12452    380   -373    272       C  
ATOM   2814  CE2 TYR A 399      -3.427  50.047 -10.673  1.00120.16           C  
ANISOU 2814  CE2 TYR A 399    15302  15684  14669    424   -407    188       C  
ATOM   2815  CZ  TYR A 399      -3.761  48.711 -10.570  1.00125.08           C  
ANISOU 2815  CZ  TYR A 399    16001  16272  15251    449   -388    238       C  
ATOM   2816  OH  TYR A 399      -3.297  47.973  -9.509  1.00141.85           O  
ANISOU 2816  OH  TYR A 399    18176  18425  17295    548   -381    252       O  
ATOM   2817  N   PHE A 400      -3.944  52.894 -16.377  1.00 40.91           N  
ANISOU 2817  N   PHE A 400     5147   5510   4885    149   -396    166       N  
ATOM   2818  CA  PHE A 400      -4.210  53.836 -17.455  1.00 32.27           C  
ANISOU 2818  CA  PHE A 400     4033   4397   3831    112   -389    168       C  
ATOM   2819  C   PHE A 400      -4.008  53.189 -18.812  1.00 61.18           C  
ANISOU 2819  C   PHE A 400     7722   8026   7497     98   -391    182       C  
ATOM   2820  O   PHE A 400      -4.945  53.051 -19.601  1.00 41.22           O  
ANISOU 2820  O   PHE A 400     5205   5476   4981     66   -393    202       O  
ATOM   2821  CB  PHE A 400      -3.294  55.056 -17.347  1.00 43.34           C  
ANISOU 2821  CB  PHE A 400     5396   5822   5248    127   -386    134       C  
ATOM   2822  CG  PHE A 400      -3.506  56.067 -18.439  1.00 40.45           C  
ANISOU 2822  CG  PHE A 400     5017   5435   4917    101   -377    142       C  
ATOM   2823  CD1 PHE A 400      -4.677  56.803 -18.498  1.00 30.66           C  
ANISOU 2823  CD1 PHE A 400     3766   4188   3694     75   -370    160       C  
ATOM   2824  CD2 PHE A 400      -2.538  56.283 -19.406  1.00 54.96           C  
ANISOU 2824  CD2 PHE A 400     6853   7263   6765    108   -375    134       C  
ATOM   2825  CE1 PHE A 400      -4.885  57.736 -19.498  1.00 46.99           C  
ANISOU 2825  CE1 PHE A 400     5827   6243   5785     65   -362    171       C  
ATOM   2826  CE2 PHE A 400      -2.738  57.216 -20.413  1.00 68.44           C  
ANISOU 2826  CE2 PHE A 400     8554   8952   8497     95   -365    147       C  
ATOM   2827  CZ  PHE A 400      -3.913  57.944 -20.457  1.00 61.85           C  
ANISOU 2827  CZ  PHE A 400     7712   8113   7674     77   -359    167       C  
ATOM   2828  N   PHE A 401      -2.768  52.794 -19.079  1.00 51.47           N  
ANISOU 2828  N   PHE A 401     6501   6798   6256    128   -394    167       N  
ATOM   2829  CA  PHE A 401      -2.410  52.278 -20.389  1.00 49.19           C  
ANISOU 2829  CA  PHE A 401     6239   6481   5970    121   -395    177       C  
ATOM   2830  C   PHE A 401      -3.184  51.012 -20.709  1.00 50.02           C  
ANISOU 2830  C   PHE A 401     6386   6560   6059    103   -403    200       C  
ATOM   2831  O   PHE A 401      -3.461  50.723 -21.870  1.00 61.35           O  
ANISOU 2831  O   PHE A 401     7840   7972   7499     84   -408    209       O  
ATOM   2832  CB  PHE A 401      -0.906  52.063 -20.480  1.00 36.54           C  
ANISOU 2832  CB  PHE A 401     4635   4892   4355    161   -397    156       C  
ATOM   2833  CG  PHE A 401      -0.116  53.336 -20.408  1.00 53.41           C  
ANISOU 2833  CG  PHE A 401     6726   7054   6513    171   -394    127       C  
ATOM   2834  CD1 PHE A 401       0.020  54.146 -21.525  1.00 35.99           C  
ANISOU 2834  CD1 PHE A 401     4511   4829   4333    154   -385    133       C  
ATOM   2835  CD2 PHE A 401       0.483  53.730 -19.222  1.00 46.46           C  
ANISOU 2835  CD2 PHE A 401     5809   6219   5623    201   -402     92       C  
ATOM   2836  CE1 PHE A 401       0.741  55.321 -21.464  1.00 50.51           C  
ANISOU 2836  CE1 PHE A 401     6307   6689   6196    161   -382    107       C  
ATOM   2837  CE2 PHE A 401       1.206  54.906 -19.154  1.00 47.85           C  
ANISOU 2837  CE2 PHE A 401     5935   6421   5824    206   -404     55       C  
ATOM   2838  CZ  PHE A 401       1.336  55.702 -20.276  1.00 59.98           C  
ANISOU 2838  CZ  PHE A 401     7462   7932   7394    182   -393     63       C  
ATOM   2839  N   GLY A 402      -3.547  50.266 -19.675  1.00 26.41           N  
ANISOU 2839  N   GLY A 402     3413   3578   3045    114   -405    208       N  
ATOM   2840  CA  GLY A 402      -4.414  49.123 -19.858  1.00 49.57           C  
ANISOU 2840  CA  GLY A 402     6387   6486   5963     93   -412    231       C  
ATOM   2841  C   GLY A 402      -5.674  49.524 -20.601  1.00 51.64           C  
ANISOU 2841  C   GLY A 402     6633   6739   6248     43   -421    240       C  
ATOM   2842  O   GLY A 402      -6.070  48.867 -21.560  1.00 35.71           O  
ANISOU 2842  O   GLY A 402     4640   4701   4226     21   -434    246       O  
ATOM   2843  N   LYS A 403      -6.298  50.615 -20.165  1.00 33.52           N  
ANISOU 2843  N   LYS A 403     4298   4463   3974     30   -417    237       N  
ATOM   2844  CA  LYS A 403      -7.528  51.093 -20.795  1.00 56.33           C  
ANISOU 2844  CA  LYS A 403     7167   7354   6881     -5   -427    244       C  
ATOM   2845  C   LYS A 403      -7.262  51.648 -22.182  1.00 50.55           C  
ANISOU 2845  C   LYS A 403     6432   6614   6160     -3   -430    239       C  
ATOM   2846  O   LYS A 403      -8.140  51.616 -23.044  1.00 44.59           O  
ANISOU 2846  O   LYS A 403     5676   5862   5404    -20   -447    242       O  
ATOM   2847  CB  LYS A 403      -8.214  52.167 -19.947  1.00 49.78           C  
ANISOU 2847  CB  LYS A 403     6298   6547   6066    -11   -418    245       C  
ATOM   2848  CG  LYS A 403      -8.745  51.696 -18.606  1.00 40.26           C  
ANISOU 2848  CG  LYS A 403     5097   5354   4846    -12   -416    254       C  
ATOM   2849  CD  LYS A 403      -9.654  52.760 -18.010  1.00 97.82           C  
ANISOU 2849  CD  LYS A 403    12348  12667  12153    -24   -411    256       C  
ATOM   2850  CE  LYS A 403      -9.590  52.792 -16.492  1.00 92.01           C  
ANISOU 2850  CE  LYS A 403    11610  11949  11400     -3   -401    257       C  
ATOM   2851  NZ  LYS A 403     -10.391  53.926 -15.955  1.00 93.75           N1+
ANISOU 2851  NZ  LYS A 403    11791  12191  11637    -12   -395    256       N1+
ATOM   2852  N   CYS A 404      -6.056  52.171 -22.389  1.00 26.95           N  
ANISOU 2852  N   CYS A 404     3440   3623   3176     23   -416    228       N  
ATOM   2853  CA  CYS A 404      -5.648  52.652 -23.708  1.00 55.99           C  
ANISOU 2853  CA  CYS A 404     7123   7293   6859     33   -415    227       C  
ATOM   2854  C   CYS A 404      -5.542  51.502 -24.704  1.00 43.85           C  
ANISOU 2854  C   CYS A 404     5625   5736   5301     31   -431    229       C  
ATOM   2855  O   CYS A 404      -6.053  51.587 -25.820  1.00 39.05           O  
ANISOU 2855  O   CYS A 404     5025   5127   4684     30   -445    232       O  
ATOM   2856  CB  CYS A 404      -4.322  53.411 -23.634  1.00 54.39           C  
ANISOU 2856  CB  CYS A 404     6907   7092   6665     59   -397    215       C  
ATOM   2857  SG  CYS A 404      -4.482  55.114 -23.042  1.00128.61           S  
ANISOU 2857  SG  CYS A 404    16264  16514  16090     62   -381    211       S  
ATOM   2858  N   PHE A 405      -4.876  50.430 -24.286  1.00 25.20           N  
ANISOU 2858  N   PHE A 405     3290   3362   2925     38   -431    227       N  
ATOM   2859  CA  PHE A 405      -4.828  49.197 -25.057  1.00 29.00           C  
ANISOU 2859  CA  PHE A 405     3815   3821   3383     34   -447    229       C  
ATOM   2860  C   PHE A 405      -6.225  48.663 -25.317  1.00 40.03           C  
ANISOU 2860  C   PHE A 405     5219   5220   4770      0   -472    234       C  
ATOM   2861  O   PHE A 405      -6.515  48.154 -26.400  1.00 26.54           O  
ANISOU 2861  O   PHE A 405     3534   3506   3046     -6   -492    230       O  
ATOM   2862  CB  PHE A 405      -4.034  48.134 -24.302  1.00 25.30           C  
ANISOU 2862  CB  PHE A 405     3377   3341   2894     54   -440    231       C  
ATOM   2863  CG  PHE A 405      -2.558  48.359 -24.316  1.00 48.50           C  
ANISOU 2863  CG  PHE A 405     6313   6283   5832     93   -425    220       C  
ATOM   2864  CD1 PHE A 405      -1.930  48.837 -25.454  1.00 42.55           C  
ANISOU 2864  CD1 PHE A 405     5559   5523   5085    102   -421    215       C  
ATOM   2865  CD2 PHE A 405      -1.792  48.078 -23.200  1.00 53.51           C  
ANISOU 2865  CD2 PHE A 405     6946   6932   6452    127   -417    215       C  
ATOM   2866  CE1 PHE A 405      -0.569  49.042 -25.468  1.00 40.16           C  
ANISOU 2866  CE1 PHE A 405     5249   5227   4781    137   -409    205       C  
ATOM   2867  CE2 PHE A 405      -0.430  48.280 -23.212  1.00 60.94           C  
ANISOU 2867  CE2 PHE A 405     7877   7887   7389    166   -410    201       C  
ATOM   2868  CZ  PHE A 405       0.183  48.759 -24.347  1.00 49.35           C  
ANISOU 2868  CZ  PHE A 405     6405   6411   5934    167   -406    195       C  
ATOM   2869  N   ASP A 406      -7.078  48.763 -24.302  1.00 37.00           N  
ANISOU 2869  N   ASP A 406     4814   4850   4393    -19   -472    241       N  
ATOM   2870  CA  ASP A 406      -8.452  48.285 -24.383  1.00 25.63           C  
ANISOU 2870  CA  ASP A 406     3371   3421   2945    -55   -498    242       C  
ATOM   2871  C   ASP A 406      -9.218  49.081 -25.421  1.00 49.12           C  
ANISOU 2871  C   ASP A 406     6316   6421   5926    -57   -518    232       C  
ATOM   2872  O   ASP A 406      -9.899  48.517 -26.276  1.00 46.18           O  
ANISOU 2872  O   ASP A 406     5951   6059   5535    -72   -550    218       O  
ATOM   2873  CB  ASP A 406      -9.143  48.404 -23.022  1.00 74.34           C  
ANISOU 2873  CB  ASP A 406     9520   9604   9120    -70   -490    252       C  
ATOM   2874  CG  ASP A 406      -8.630  47.390 -22.010  1.00 92.00           C  
ANISOU 2874  CG  ASP A 406    11799  11822  11333    -58   -475    266       C  
ATOM   2875  OD1 ASP A 406      -7.776  46.549 -22.373  1.00 70.98           O  
ANISOU 2875  OD1 ASP A 406     9183   9137   8651    -40   -471    268       O  
ATOM   2876  OD2 ASP A 406      -9.090  47.437 -20.848  1.00 88.77           O1-
ANISOU 2876  OD2 ASP A 406    11383  11424  10920    -60   -465    278       O1-
ATOM   2877  N   ALA A 407      -9.107  50.401 -25.336  1.00 55.21           N  
ANISOU 2877  N   ALA A 407     7055   7204   6717    -38   -500    235       N  
ATOM   2878  CA  ALA A 407      -9.731  51.275 -26.309  1.00 27.58           C  
ANISOU 2878  CA  ALA A 407     3535   3730   3215    -22   -514    231       C  
ATOM   2879  C   ALA A 407      -9.273  50.891 -27.713  1.00 52.69           C  
ANISOU 2879  C   ALA A 407     6747   6904   6370     -1   -529    223       C  
ATOM   2880  O   ALA A 407     -10.090  50.556 -28.570  1.00 45.22           O  
ANISOU 2880  O   ALA A 407     5800   5982   5401     -1   -565    209       O  
ATOM   2881  CB  ALA A 407      -9.384  52.717 -26.008  1.00 47.99           C  
ANISOU 2881  CB  ALA A 407     6095   6321   5820      1   -485    240       C  
ATOM   2882  N   MET A 408      -7.964  50.923 -27.938  1.00 33.89           N  
ANISOU 2882  N   MET A 408     4391   4495   3990     21   -506    228       N  
ATOM   2883  CA  MET A 408      -7.402  50.612 -29.250  1.00 41.64           C  
ANISOU 2883  CA  MET A 408     5408   5468   4946     47   -515    223       C  
ATOM   2884  C   MET A 408      -7.951  49.321 -29.846  1.00 44.59           C  
ANISOU 2884  C   MET A 408     5808   5844   5291     28   -552    209       C  
ATOM   2885  O   MET A 408      -8.306  49.272 -31.023  1.00 42.53           O  
ANISOU 2885  O   MET A 408     5559   5602   4999     49   -580    197       O  
ATOM   2886  CB  MET A 408      -5.872  50.553 -29.186  1.00 41.67           C  
ANISOU 2886  CB  MET A 408     5433   5442   4956     64   -485    227       C  
ATOM   2887  CG  MET A 408      -5.223  51.899 -28.959  1.00 56.91           C  
ANISOU 2887  CG  MET A 408     7339   7376   6907     87   -453    235       C  
ATOM   2888  SD  MET A 408      -3.438  51.806 -28.798  1.00 59.87           S  
ANISOU 2888  SD  MET A 408     7727   7731   7291    106   -425    232       S  
ATOM   2889  CE  MET A 408      -2.970  51.427 -30.468  1.00 81.36           C  
ANISOU 2889  CE  MET A 408    10496  10438   9979    138   -430    236       C  
ATOM   2890  N   GLU A 409      -8.015  48.272 -29.037  1.00 50.79           N  
ANISOU 2890  N   GLU A 409     6606   6613   6079     -6   -555    207       N  
ATOM   2891  CA  GLU A 409      -8.476  46.976 -29.522  1.00 54.83           C  
ANISOU 2891  CA  GLU A 409     7148   7124   6560    -31   -589    190       C  
ATOM   2892  C   GLU A 409      -9.886  47.077 -30.098  1.00 34.10           C  
ANISOU 2892  C   GLU A 409     4489   4548   3921    -46   -634    162       C  
ATOM   2893  O   GLU A 409     -10.250  46.341 -31.014  1.00 59.53           O  
ANISOU 2893  O   GLU A 409     7725   7785   7110    -54   -671    131       O  
ATOM   2894  CB  GLU A 409      -8.424  45.932 -28.400  1.00 50.02           C  
ANISOU 2894  CB  GLU A 409     6562   6491   5951    -64   -580    198       C  
ATOM   2895  CG  GLU A 409      -8.799  44.520 -28.837  1.00 87.37           C  
ANISOU 2895  CG  GLU A 409    11336  11217  10645    -97   -609    177       C  
ATOM   2896  CD  GLU A 409      -7.852  43.948 -29.880  1.00134.10           C  
ANISOU 2896  CD  GLU A 409    17307  17110  16536    -71   -609    174       C  
ATOM   2897  OE1 GLU A 409      -6.756  44.515 -30.074  1.00145.72           O  
ANISOU 2897  OE1 GLU A 409    18783  18563  18020    -29   -581    192       O  
ATOM   2898  OE2 GLU A 409      -8.205  42.926 -30.505  1.00152.62           O1-
ANISOU 2898  OE2 GLU A 409    19686  19457  18844    -98   -638    145       O1-
ATOM   2899  N   VAL A 410     -10.669  48.004 -29.567  1.00 39.78           N  
ANISOU 2899  N   VAL A 410     5157   5295   4661    -48   -632    165       N  
ATOM   2900  CA  VAL A 410     -12.058  48.161 -29.970  1.00 42.17           C  
ANISOU 2900  CA  VAL A 410     5414   5653   4954    -58   -676    132       C  
ATOM   2901  C   VAL A 410     -12.189  49.101 -31.161  1.00 49.34           C  
ANISOU 2901  C   VAL A 410     6313   6597   5837      1   -692    127       C  
ATOM   2902  O   VAL A 410     -13.099  48.972 -31.980  1.00 51.32           O  
ANISOU 2902  O   VAL A 410     6539   6901   6060     10   -741     88       O  
ATOM   2903  CB  VAL A 410     -12.894  48.730 -28.810  1.00 43.12           C  
ANISOU 2903  CB  VAL A 410     5485   5792   5106    -81   -665    139       C  
ATOM   2904  CG1 VAL A 410     -14.294  49.069 -29.275  1.00 37.12           C  
ANISOU 2904  CG1 VAL A 410     4667   5097   4339    -82   -709    100       C  
ATOM   2905  CG2 VAL A 410     -12.935  47.734 -27.672  1.00 31.68           C  
ANISOU 2905  CG2 VAL A 410     4050   4318   3670   -134   -655    141       C  
ATOM   2906  N   ASP A 411     -11.272  50.055 -31.245  1.00 58.74           N  
ANISOU 2906  N   ASP A 411     7521   7763   7035     42   -652    162       N  
ATOM   2907  CA  ASP A 411     -11.259  50.994 -32.347  1.00 48.16           C  
ANISOU 2907  CA  ASP A 411     6185   6449   5663    107   -659    166       C  
ATOM   2908  C   ASP A 411     -10.794  50.259 -33.596  1.00 51.41           C  
ANISOU 2908  C   ASP A 411     6642   6860   6031    133   -683    150       C  
ATOM   2909  O   ASP A 411     -11.159  50.614 -34.719  1.00 93.15           O  
ANISOU 2909  O   ASP A 411    11933  12189  11271    188   -712    138       O  
ATOM   2910  CB  ASP A 411     -10.319  52.149 -32.023  1.00 53.26           C  
ANISOU 2910  CB  ASP A 411     6840   7064   6331    135   -605    203       C  
ATOM   2911  CG  ASP A 411     -10.719  53.424 -32.703  1.00 68.99           C  
ANISOU 2911  CG  ASP A 411     8823   9092   8299    198   -605    216       C  
ATOM   2912  OD1 ASP A 411     -11.753  53.416 -33.403  1.00 88.24           O  
ANISOU 2912  OD1 ASP A 411    11245  11585  10698    228   -651    196       O  
ATOM   2913  OD2 ASP A 411     -10.006  54.437 -32.544  1.00 81.35           O1-
ANISOU 2913  OD2 ASP A 411    10396  10636   9878    223   -561    243       O1-
ATOM   2914  N   ALA A 412      -9.992  49.220 -33.382  1.00 57.97           N  
ANISOU 2914  N   ALA A 412     7509   7646   6871     99   -671    150       N  
ATOM   2915  CA  ALA A 412      -9.410  48.441 -34.467  1.00 57.08           C  
ANISOU 2915  CA  ALA A 412     7446   7523   6719    118   -687    137       C  
ATOM   2916  C   ALA A 412     -10.444  47.578 -35.179  1.00 66.86           C  
ANISOU 2916  C   ALA A 412     8675   8812   7918    104   -751     85       C  
ATOM   2917  O   ALA A 412     -10.103  46.793 -36.060  1.00 94.99           O  
ANISOU 2917  O   ALA A 412    12278  12371  11442    113   -772     63       O  
ATOM   2918  CB  ALA A 412      -8.286  47.579 -33.933  1.00 58.94           C  
ANISOU 2918  CB  ALA A 412     7722   7699   6975     88   -655    152       C  
ATOM   2919  N   LEU A 413     -11.704  47.725 -34.795  1.00 65.86           N  
ANISOU 2919  N   LEU A 413     8489   8733   7799     80   -783     56       N  
ATOM   2920  CA  LEU A 413     -12.776  46.948 -35.399  1.00 49.32           C  
ANISOU 2920  CA  LEU A 413     6366   6699   5675     58   -849    -16       C  
ATOM   2921  C   LEU A 413     -13.498  47.745 -36.475  1.00 88.37           C  
ANISOU 2921  C   LEU A 413    11283  11722  10572    131   -894    -41       C  
ATOM   2922  O   LEU A 413     -13.330  48.959 -36.577  1.00103.20           O  
ANISOU 2922  O   LEU A 413    13163  13606  12444    193   -869      3       O  
ATOM   2923  CB  LEU A 413     -13.770  46.501 -34.332  1.00 50.96           C  
ANISOU 2923  CB  LEU A 413     6518   6922   5925    -19   -860    -49       C  
ATOM   2924  CG  LEU A 413     -13.178  45.610 -33.237  1.00 79.15           C  
ANISOU 2924  CG  LEU A 413    10122  10424   9528    -84   -821    -28       C  
ATOM   2925  CD1 LEU A 413     -14.210  45.343 -32.158  1.00 99.49           C  
ANISOU 2925  CD1 LEU A 413    12642  13015  12143   -153   -825    -58       C  
ATOM   2926  CD2 LEU A 413     -12.668  44.313 -33.824  1.00 69.70           C  
ANISOU 2926  CD2 LEU A 413     8979   9202   8302   -112   -834    -62       C  
ATOM   2927  N   ASN A 414     -14.298  47.058 -37.284  1.00107.02           N  
ANISOU 2927  N   ASN A 414    13619  14149  12896    126   -960   -119       N  
ATOM   2928  CA  ASN A 414     -15.106  47.721 -38.300  1.00127.63           C  
ANISOU 2928  CA  ASN A 414    16195  16851  15449    204  -1015   -156       C  
ATOM   2929  C   ASN A 414     -16.057  48.730 -37.670  1.00132.86           C  
ANISOU 2929  C   ASN A 414    16789  17557  16134    219  -1018   -148       C  
ATOM   2930  O   ASN A 414     -16.406  49.740 -38.281  1.00 91.29           O  
ANISOU 2930  O   ASN A 414    11514  12347  10824    310  -1036   -136       O  
ATOM   2931  CB  ASN A 414     -15.910  46.696 -39.100  1.00131.13           C  
ANISOU 2931  CB  ASN A 414    16603  17365  15856    180  -1091   -265       C  
ATOM   2932  CG  ASN A 414     -15.033  45.790 -39.937  1.00149.19           C  
ANISOU 2932  CG  ASN A 414    18961  19620  18103    182  -1095   -279       C  
ATOM   2933  ND2 ASN A 414     -15.606  44.690 -40.413  1.00153.26           N  
ANISOU 2933  ND2 ASN A 414    19450  20177  18603    131  -1150   -383       N  
ATOM   2934  OD1 ASN A 414     -13.856  46.076 -40.159  1.00154.47           O  
ANISOU 2934  OD1 ASN A 414    19706  20227  18758    225  -1048   -204       O  
ATOM   2935  N   SER A 415     -16.463  48.443 -36.436  1.00154.50           N  
ANISOU 2935  N   SER A 415    19489  20273  18942    135   -997   -152       N  
ATOM   2936  CA  SER A 415     -17.474  49.235 -35.742  1.00142.56           C  
ANISOU 2936  CA  SER A 415    17906  18804  17457    135  -1002   -155       C  
ATOM   2937  C   SER A 415     -16.875  50.245 -34.766  1.00148.48           C  
ANISOU 2937  C   SER A 415    18680  19491  18245    145   -931    -66       C  
ATOM   2938  O   SER A 415     -16.332  49.872 -33.726  1.00170.13           O  
ANISOU 2938  O   SER A 415    21441  22163  21036     82   -884    -35       O  
ATOM   2939  CB  SER A 415     -18.447  48.312 -35.005  1.00111.40           C  
ANISOU 2939  CB  SER A 415    13890  14878  13561     35  -1025   -228       C  
ATOM   2940  OG  SER A 415     -17.752  47.358 -34.222  1.00 88.28           O  
ANISOU 2940  OG  SER A 415    11004  11866  10674    -46   -982   -211       O  
ATOM   2941  N   SER A 416     -16.993  51.524 -35.111  1.00114.80           N  
ANISOU 2941  N   SER A 416    14413  15254  13951    228   -924    -31       N  
ATOM   2942  CA  SER A 416     -16.527  52.616 -34.261  1.00 89.51           C  
ANISOU 2942  CA  SER A 416    11224  12002  10783    239   -860     38       C  
ATOM   2943  C   SER A 416     -16.699  53.957 -34.967  1.00 90.85           C  
ANISOU 2943  C   SER A 416    11401  12214  10905    343   -860     67       C  
ATOM   2944  O   SER A 416     -16.823  55.000 -34.325  1.00 94.45           O  
ANISOU 2944  O   SER A 416    11844  12661  11383    358   -824    105       O  
ATOM   2945  CB  SER A 416     -15.063  52.412 -33.859  1.00 85.63           C  
ANISOU 2945  CB  SER A 416    10797  11416  10320    210   -797     87       C  
ATOM   2946  OG  SER A 416     -14.237  52.233 -34.997  1.00105.18           O  
ANISOU 2946  OG  SER A 416    13330  13881  12751    258   -799     93       O  
TER    2947      SER A 416 
ATOM   2948  N   ASP A 434     -19.400  53.399 -24.653  1.00 66.67           N  
ANISOU 2948  N   ASP A 434     8116   8998   8217   -110   -672    120       N  
ATOM   2949  CA  ASP A 434     -19.037  54.805 -24.495  1.00 76.62           C  
ANISOU 2949  CA  ASP A 434     9389  10250   9474    -59   -641    162       C  
ATOM   2950  C   ASP A 434     -17.887  55.020 -23.513  1.00 75.42           C  
ANISOU 2950  C   ASP A 434     9284  10037   9336    -67   -588    203       C  
ATOM   2951  O   ASP A 434     -16.945  55.748 -23.813  1.00 76.54           O  
ANISOU 2951  O   ASP A 434     9457  10153   9471    -32   -563    225       O  
ATOM   2952  CB  ASP A 434     -20.252  55.648 -24.095  1.00117.87           C  
ANISOU 2952  CB  ASP A 434    14549  15524  14711    -46   -650    154       C  
ATOM   2953  CG  ASP A 434     -20.866  55.211 -22.778  1.00149.25           C  
ANISOU 2953  CG  ASP A 434    18491  19494  18721   -103   -637    147       C  
ATOM   2954  OD1 ASP A 434     -20.435  54.181 -22.218  1.00134.81           O  
ANISOU 2954  OD1 ASP A 434    16689  17630  16903   -150   -626    147       O  
ATOM   2955  OD2 ASP A 434     -21.791  55.901 -22.304  1.00166.92           O1-
ANISOU 2955  OD2 ASP A 434    20679  21768  20976    -96   -638    143       O1-
ATOM   2956  N   ASP A 435     -17.963  54.392 -22.343  1.00 63.51           N  
ANISOU 2956  N   ASP A 435     7775   8511   7847   -110   -574    206       N  
ATOM   2957  CA  ASP A 435     -16.888  54.479 -21.360  1.00 65.54           C  
ANISOU 2957  CA  ASP A 435     8071   8721   8109   -111   -532    235       C  
ATOM   2958  C   ASP A 435     -15.520  54.279 -22.033  1.00 84.39           C  
ANISOU 2958  C   ASP A 435    10509  11072  10484    -91   -520    242       C  
ATOM   2959  O   ASP A 435     -14.523  54.871 -21.621  1.00103.00           O  
ANISOU 2959  O   ASP A 435    12886  13404  12847    -73   -488    256       O  
ATOM   2960  CB  ASP A 435     -17.108  53.464 -20.232  1.00 47.92           C  
ANISOU 2960  CB  ASP A 435     5844   6481   5883   -153   -530    236       C  
ATOM   2961  CG  ASP A 435     -16.045  53.549 -19.144  1.00100.55           C  
ANISOU 2961  CG  ASP A 435    12547  13113  12545   -140   -493    261       C  
ATOM   2962  OD1 ASP A 435     -15.184  54.450 -19.215  1.00136.95           O  
ANISOU 2962  OD1 ASP A 435    17168  17709  17157   -109   -470    268       O  
ATOM   2963  OD2 ASP A 435     -16.070  52.715 -18.216  1.00 96.94           O1-
ANISOU 2963  OD2 ASP A 435    12105  12649  12079   -158   -490    268       O1-
ATOM   2964  N   VAL A 436     -15.489  53.455 -23.078  1.00 60.77           N  
ANISOU 2964  N   VAL A 436     7532   8082   7475    -96   -548    226       N  
ATOM   2965  CA  VAL A 436     -14.268  53.218 -23.837  1.00 67.32           C  
ANISOU 2965  CA  VAL A 436     8406   8880   8292    -76   -540    230       C  
ATOM   2966  C   VAL A 436     -13.947  54.396 -24.753  1.00 68.85           C  
ANISOU 2966  C   VAL A 436     8599   9083   8480    -29   -533    236       C  
ATOM   2967  O   VAL A 436     -12.781  54.752 -24.947  1.00 43.31           O  
ANISOU 2967  O   VAL A 436     5391   5819   5247     -9   -507    246       O  
ATOM   2968  CB  VAL A 436     -14.368  51.932 -24.668  1.00 64.06           C  
ANISOU 2968  CB  VAL A 436     8012   8468   7858    -95   -574    209       C  
ATOM   2969  CG1 VAL A 436     -13.160  51.786 -25.588  1.00 56.12           C  
ANISOU 2969  CG1 VAL A 436     7052   7433   6838    -67   -566    214       C  
ATOM   2970  CG2 VAL A 436     -14.496  50.728 -23.748  1.00 54.37           C  
ANISOU 2970  CG2 VAL A 436     6799   7226   6634   -140   -576    207       C  
ATOM   2971  N   SER A 437     -14.989  54.999 -25.317  1.00 63.01           N  
ANISOU 2971  N   SER A 437     7825   8386   7729     -7   -558    228       N  
ATOM   2972  CA  SER A 437     -14.812  56.212 -26.101  1.00 53.40           C  
ANISOU 2972  CA  SER A 437     6609   7182   6498     48   -550    240       C  
ATOM   2973  C   SER A 437     -14.305  57.335 -25.197  1.00 36.15           C  
ANISOU 2973  C   SER A 437     4421   4976   4339     54   -506    262       C  
ATOM   2974  O   SER A 437     -13.570  58.213 -25.637  1.00 43.79           O  
ANISOU 2974  O   SER A 437     5405   5931   5303     90   -484    276       O  
ATOM   2975  CB  SER A 437     -16.114  56.618 -26.792  1.00 35.79           C  
ANISOU 2975  CB  SER A 437     4340   5014   4244     81   -590    226       C  
ATOM   2976  OG  SER A 437     -16.934  57.394 -25.939  1.00 83.37           O  
ANISOU 2976  OG  SER A 437    10326  11062  10289     79   -581    234       O  
ATOM   2977  N   TYR A 438     -14.692  57.300 -23.925  1.00 43.64           N  
ANISOU 2977  N   TYR A 438     5347   5923   5310     20   -495    263       N  
ATOM   2978  CA  TYR A 438     -14.187  58.274 -22.967  1.00 42.89           C  
ANISOU 2978  CA  TYR A 438     5248   5812   5237     23   -458    275       C  
ATOM   2979  C   TYR A 438     -12.758  57.917 -22.588  1.00 24.05           C  
ANISOU 2979  C   TYR A 438     2891   3386   2859     13   -434    272       C  
ATOM   2980  O   TYR A 438     -11.987  58.770 -22.161  1.00 62.95           O  
ANISOU 2980  O   TYR A 438     7817   8301   7799     25   -408    274       O  
ATOM   2981  CB  TYR A 438     -15.061  58.337 -21.714  1.00 44.02           C  
ANISOU 2981  CB  TYR A 438     5360   5970   5395     -2   -455    275       C  
ATOM   2982  CG  TYR A 438     -16.511  58.684 -21.969  1.00 51.01           C  
ANISOU 2982  CG  TYR A 438     6205   6901   6276      9   -481    273       C  
ATOM   2983  CD1 TYR A 438     -17.496  58.351 -21.043  1.00 31.87           C  
ANISOU 2983  CD1 TYR A 438     3749   4497   3864    -21   -489    268       C  
ATOM   2984  CD2 TYR A 438     -16.898  59.337 -23.134  1.00 46.58           C  
ANISOU 2984  CD2 TYR A 438     5636   6369   5695     55   -498    276       C  
ATOM   2985  CE1 TYR A 438     -18.820  58.661 -21.268  1.00 32.31           C  
ANISOU 2985  CE1 TYR A 438     3756   4600   3918    -11   -515    258       C  
ATOM   2986  CE2 TYR A 438     -18.221  59.650 -23.369  1.00 35.77           C  
ANISOU 2986  CE2 TYR A 438     4223   5052   4317     75   -527    268       C  
ATOM   2987  CZ  TYR A 438     -19.178  59.311 -22.433  1.00 65.31           C  
ANISOU 2987  CZ  TYR A 438     7925   8813   8078     38   -536    257       C  
ATOM   2988  OH  TYR A 438     -20.498  59.621 -22.662  1.00 54.99           O  
ANISOU 2988  OH  TYR A 438     6563   7565   6766     58   -567    242       O  
ATOM   2989  N   ASP A 439     -12.410  56.647 -22.747  1.00 42.10           N  
ANISOU 2989  N   ASP A 439     5202   5658   5137     -7   -446    264       N  
ATOM   2990  CA  ASP A 439     -11.041  56.210 -22.524  1.00 48.88           C  
ANISOU 2990  CA  ASP A 439     6088   6487   5998     -8   -429    259       C  
ATOM   2991  C   ASP A 439     -10.132  56.698 -23.652  1.00 52.03           C  
ANISOU 2991  C   ASP A 439     6504   6873   6391     22   -422    260       C  
ATOM   2992  O   ASP A 439      -8.987  57.087 -23.416  1.00 42.38           O  
ANISOU 2992  O   ASP A 439     5287   5636   5179     33   -401    255       O  
ATOM   2993  CB  ASP A 439     -10.971  54.689 -22.396  1.00 55.63           C  
ANISOU 2993  CB  ASP A 439     6967   7329   6840    -31   -445    255       C  
ATOM   2994  CG  ASP A 439     -11.457  54.190 -21.046  1.00 74.39           C  
ANISOU 2994  CG  ASP A 439     9336   9711   9218    -53   -442    258       C  
ATOM   2995  OD1 ASP A 439     -11.212  54.880 -20.032  1.00 64.18           O  
ANISOU 2995  OD1 ASP A 439     8028   8423   7934    -44   -422    258       O  
ATOM   2996  OD2 ASP A 439     -12.074  53.102 -20.997  1.00 71.44           O1-
ANISOU 2996  OD2 ASP A 439     8972   9339   8834    -76   -462    259       O1-
ATOM   2997  N   LYS A 440     -10.645  56.682 -24.877  1.00 22.74           N  
ANISOU 2997  N   LYS A 440     2801   3175   2662     41   -442    264       N  
ATOM   2998  CA  LYS A 440      -9.882  57.185 -26.008  1.00 33.13           C  
ANISOU 2998  CA  LYS A 440     4140   4483   3966     78   -433    270       C  
ATOM   2999  C   LYS A 440      -9.596  58.662 -25.801  1.00 42.14           C  
ANISOU 2999  C   LYS A 440     5266   5625   5121    105   -405    284       C  
ATOM   3000  O   LYS A 440      -8.482  59.124 -26.039  1.00 52.67           O  
ANISOU 3000  O   LYS A 440     6613   6939   6462    122   -383    288       O  
ATOM   3001  CB  LYS A 440     -10.634  56.973 -27.325  1.00 22.68           C  
ANISOU 3001  CB  LYS A 440     2827   3183   2607    107   -464    272       C  
ATOM   3002  CG  LYS A 440      -9.808  57.299 -28.564  1.00 31.56           C  
ANISOU 3002  CG  LYS A 440     3986   4296   3708    154   -454    283       C  
ATOM   3003  CD  LYS A 440     -10.593  57.052 -29.849  1.00 42.91           C  
ANISOU 3003  CD  LYS A 440     5437   5766   5099    194   -490    281       C  
ATOM   3004  CE  LYS A 440      -9.814  57.521 -31.071  1.00 35.00           C  
ANISOU 3004  CE  LYS A 440     4479   4754   4065    255   -473    299       C  
ATOM   3005  NZ  LYS A 440     -10.592  57.381 -32.333  1.00 66.22           N1+
ANISOU 3005  NZ  LYS A 440     8449   8750   7961    311   -511    297       N1+
ATOM   3006  N   GLY A 441     -10.605  59.397 -25.345  1.00 47.06           N  
ANISOU 3006  N   GLY A 441     5860   6270   5750    108   -407    292       N  
ATOM   3007  CA  GLY A 441     -10.461  60.817 -25.073  1.00 23.80           C  
ANISOU 3007  CA  GLY A 441     2900   3323   2818    134   -380    308       C  
ATOM   3008  C   GLY A 441      -9.280  61.096 -24.166  1.00 36.44           C  
ANISOU 3008  C   GLY A 441     4496   4902   4448    116   -356    296       C  
ATOM   3009  O   GLY A 441      -8.454  61.962 -24.449  1.00 41.08           O  
ANISOU 3009  O   GLY A 441     5087   5474   5046    142   -334    307       O  
ATOM   3010  N   ALA A 442      -9.200  60.352 -23.072  1.00 27.12           N  
ANISOU 3010  N   ALA A 442     3305   3722   3277     78   -362    275       N  
ATOM   3011  CA  ALA A 442      -8.093  60.474 -22.141  1.00 30.38           C  
ANISOU 3011  CA  ALA A 442     3709   4126   3707     68   -349    254       C  
ATOM   3012  C   ALA A 442      -6.766  60.127 -22.813  1.00 34.23           C  
ANISOU 3012  C   ALA A 442     4217   4597   4193     80   -345    247       C  
ATOM   3013  O   ALA A 442      -5.768  60.819 -22.619  1.00 55.71           O  
ANISOU 3013  O   ALA A 442     6923   7314   6931     92   -333    236       O  
ATOM   3014  CB  ALA A 442      -8.330  59.587 -20.924  1.00 42.23           C  
ANISOU 3014  CB  ALA A 442     5205   5635   5203     41   -357    238       C  
ATOM   3015  N   CYS A 443      -6.759  59.056 -23.603  1.00 32.81           N  
ANISOU 3015  N   CYS A 443     4065   4407   3992     77   -358    251       N  
ATOM   3016  CA  CYS A 443      -5.547  58.625 -24.299  1.00 44.55           C  
ANISOU 3016  CA  CYS A 443     5574   5878   5474     90   -354    246       C  
ATOM   3017  C   CYS A 443      -5.062  59.700 -25.264  1.00 51.38           C  
ANISOU 3017  C   CYS A 443     6446   6734   6344    125   -335    266       C  
ATOM   3018  O   CYS A 443      -3.882  60.058 -25.277  1.00 37.56           O  
ANISOU 3018  O   CYS A 443     4690   4974   4608    138   -322    260       O  
ATOM   3019  CB  CYS A 443      -5.790  57.314 -25.048  1.00 37.60           C  
ANISOU 3019  CB  CYS A 443     4726   4989   4570     83   -372    248       C  
ATOM   3020  SG  CYS A 443      -6.114  55.902 -23.962  1.00 80.76           S  
ANISOU 3020  SG  CYS A 443    10196  10457  10031     51   -388    234       S  
ATOM   3021  N   ILE A 444      -5.988  60.210 -26.067  1.00 52.07           N  
ANISOU 3021  N   ILE A 444     6544   6824   6415    149   -334    292       N  
ATOM   3022  CA  ILE A 444      -5.720  61.330 -26.957  1.00 53.19           C  
ANISOU 3022  CA  ILE A 444     6703   6951   6554    199   -305    326       C  
ATOM   3023  C   ILE A 444      -5.101  62.507 -26.203  1.00 42.34           C  
ANISOU 3023  C   ILE A 444     5301   5563   5222    206   -278    331       C  
ATOM   3024  O   ILE A 444      -4.041  63.006 -26.581  1.00 46.06           O  
ANISOU 3024  O   ILE A 444     5782   6003   5716    233   -249    347       O  
ATOM   3025  CB  ILE A 444      -7.005  61.801 -27.651  1.00 27.81           C  
ANISOU 3025  CB  ILE A 444     3501   3753   3313    235   -308    352       C  
ATOM   3026  CG1 ILE A 444      -7.607  60.668 -28.478  1.00 72.15           C  
ANISOU 3026  CG1 ILE A 444     9138   9387   8889    235   -342    342       C  
ATOM   3027  CG2 ILE A 444      -6.713  62.952 -28.550  1.00 58.44           C  
ANISOU 3027  CG2 ILE A 444     7413   7606   7184    302   -263    399       C  
ATOM   3028  CD1 ILE A 444      -6.678  60.145 -29.549  1.00 97.88           C  
ANISOU 3028  CD1 ILE A 444    12439  12625  12125    259   -335    347       C  
ATOM   3029  N   LEU A 445      -5.769  62.942 -25.139  1.00 29.21           N  
ANISOU 3029  N   LEU A 445     3601   3919   3577    185   -286    318       N  
ATOM   3030  CA  LEU A 445      -5.274  64.033 -24.303  1.00 25.11           C  
ANISOU 3030  CA  LEU A 445     3042   3391   3107    192   -270    312       C  
ATOM   3031  C   LEU A 445      -3.862  63.769 -23.801  1.00 50.71           C  
ANISOU 3031  C   LEU A 445     6256   6629   6383    167   -261    260       C  
ATOM   3032  O   LEU A 445      -3.010  64.659 -23.832  1.00 45.27           O  
ANISOU 3032  O   LEU A 445     5549   5898   5752    160   -188    228       O  
ATOM   3033  CB  LEU A 445      -6.212  64.282 -23.121  1.00 33.70           C  
ANISOU 3033  CB  LEU A 445     4095   4506   4202    164   -284    292       C  
ATOM   3034  CG  LEU A 445      -7.565  64.914 -23.454  1.00 32.13           C  
ANISOU 3034  CG  LEU A 445     3906   4312   3989    190   -275    329       C  
ATOM   3035  CD1 LEU A 445      -8.476  64.895 -22.241  1.00 30.36           C  
ANISOU 3035  CD1 LEU A 445     3650   4117   3770    157   -291    307       C  
ATOM   3036  CD2 LEU A 445      -7.374  66.331 -23.968  1.00 24.09           C  
ANISOU 3036  CD2 LEU A 445     2899   3248   3006    238   -210    361       C  
ATOM   3037  N   ASN A 446      -3.611  62.549 -23.334  1.00 28.27           N  
ANISOU 3037  N   ASN A 446     3415   3816   3511    141   -303    234       N  
ATOM   3038  CA  ASN A 446      -2.276  62.195 -22.871  1.00 23.07           C  
ANISOU 3038  CA  ASN A 446     2725   3170   2872    134   -312    188       C  
ATOM   3039  C   ASN A 446      -1.258  62.388 -23.987  1.00 43.96           C  
ANISOU 3039  C   ASN A 446     5389   5774   5542    151   -266    192       C  
ATOM   3040  O   ASN A 446      -0.201  62.989 -23.788  1.00 31.60           O  
ANISOU 3040  O   ASN A 446     3786   4188   4035    137   -212    139       O  
ATOM   3041  CB  ASN A 446      -2.235  60.757 -22.375  1.00 33.33           C  
ANISOU 3041  CB  ASN A 446     4052   4482   4130    113   -332    168       C  
ATOM   3042  CG  ASN A 446      -0.867  60.359 -21.876  1.00 42.39           C  
ANISOU 3042  CG  ASN A 446     5171   5650   5286    119   -342    120       C  
ATOM   3043  ND2 ASN A 446      -0.253  61.233 -21.083  1.00 24.78           N  
ANISOU 3043  ND2 ASN A 446     2872   3443   3098    117   -341     67       N  
ATOM   3044  OD1 ASN A 446      -0.357  59.283 -22.209  1.00 37.22           O  
ANISOU 3044  OD1 ASN A 446     4546   4991   4606    126   -349    122       O  
ATOM   3045  N   MET A 447      -1.590  61.871 -25.164  1.00 36.66           N  
ANISOU 3045  N   MET A 447     4523   4834   4574    177   -275    247       N  
ATOM   3046  CA  MET A 447      -0.752  62.027 -26.343  1.00 35.52           C  
ANISOU 3046  CA  MET A 447     4412   4641   4442    197   -218    259       C  
ATOM   3047  C   MET A 447      -0.387  63.492 -26.556  1.00 33.74           C  
ANISOU 3047  C   MET A 447     4175   4358   4286    197   -115    247       C  
ATOM   3048  O   MET A 447       0.786  63.844 -26.676  1.00 40.72           O  
ANISOU 3048  O   MET A 447     5038   5207   5225    184    -51    206       O  
ATOM   3049  CB  MET A 447      -1.483  61.483 -27.570  1.00 23.84           C  
ANISOU 3049  CB  MET A 447     3002   3160   2898    234   -243    323       C  
ATOM   3050  CG  MET A 447      -0.648  61.426 -28.839  1.00 26.80           C  
ANISOU 3050  CG  MET A 447     3425   3490   3270    263   -191    343       C  
ATOM   3051  SD  MET A 447      -1.543  60.647 -30.189  1.00 47.56           S  
ANISOU 3051  SD  MET A 447     6120   6131   5821    294   -217    377       S  
ATOM   3052  CE  MET A 447      -2.876  61.809 -30.438  1.00 24.69           C  
ANISOU 3052  CE  MET A 447     3233   3235   2912    331   -195    413       C  
ATOM   3053  N   LEU A 448      -1.411  64.337 -26.595  1.00 35.79           N  
ANISOU 3053  N   LEU A 448     4449   4606   4545    213    -94    279       N  
ATOM   3054  CA  LEU A 448      -1.250  65.776 -26.795  1.00 49.99           C  
ANISOU 3054  CA  LEU A 448     6248   6341   6406    220     14    277       C  
ATOM   3055  C   LEU A 448      -0.419  66.424 -25.697  1.00 42.80           C  
ANISOU 3055  C   LEU A 448     5263   5420   5579    169     56    192       C  
ATOM   3056  O   LEU A 448       0.426  67.280 -25.954  1.00 39.32           O  
ANISOU 3056  O   LEU A 448     4812   4918   5210    156    159    160       O  
ATOM   3057  CB  LEU A 448      -2.623  66.442 -26.831  1.00 31.67           C  
ANISOU 3057  CB  LEU A 448     3950   4023   4060    251     12    325       C  
ATOM   3058  CG  LEU A 448      -2.661  67.959 -26.954  1.00 41.39           C  
ANISOU 3058  CG  LEU A 448     5190   5185   5350    265    127    331       C  
ATOM   3059  CD1 LEU A 448      -1.950  68.408 -28.220  1.00 28.71           C  
ANISOU 3059  CD1 LEU A 448     3645   3504   3760    303    229    363       C  
ATOM   3060  CD2 LEU A 448      -4.099  68.430 -26.944  1.00 32.13           C  
ANISOU 3060  CD2 LEU A 448     4038   4032   4139    306    106    382       C  
ATOM   3061  N   ARG A 449      -0.679  66.015 -24.465  1.00 39.39           N  
ANISOU 3061  N   ARG A 449     4779   5050   5136    140    -18    152       N  
ATOM   3062  CA  ARG A 449       0.022  66.564 -23.321  1.00 31.36           C  
ANISOU 3062  CA  ARG A 449     3686   4043   4186     98      5     63       C  
ATOM   3063  C   ARG A 449       1.514  66.244 -23.368  1.00 30.14           C  
ANISOU 3063  C   ARG A 449     3493   3887   4072     78     26     -3       C  
ATOM   3064  O   ARG A 449       2.333  67.017 -22.873  1.00 71.14           O  
ANISOU 3064  O   ARG A 449     8625   9061   9343     45     86    -85       O  
ATOM   3065  CB  ARG A 449      -0.588  66.033 -22.029  1.00 32.39           C  
ANISOU 3065  CB  ARG A 449     3780   4248   4278     86    -88     42       C  
ATOM   3066  CG  ARG A 449      -0.014  66.650 -20.776  1.00 32.91           C  
ANISOU 3066  CG  ARG A 449     3768   4336   4400     51    -73    -54       C  
ATOM   3067  CD  ARG A 449      -0.069  65.663 -19.634  1.00 62.19           C  
ANISOU 3067  CD  ARG A 449     7446   8128   8054     53   -173    -82       C  
ATOM   3068  NE  ARG A 449       0.264  66.296 -18.363  1.00 75.76           N  
ANISOU 3068  NE  ARG A 449     9094   9880   9812     31   -169   -171       N  
ATOM   3069  CZ  ARG A 449       0.741  65.639 -17.315  1.00 55.34           C  
ANISOU 3069  CZ  ARG A 449     6466   7368   7194     38   -235   -228       C  
ATOM   3070  NH1 ARG A 449       0.950  64.330 -17.398  1.00 35.77           N1+
ANISOU 3070  NH1 ARG A 449     4013   4928   4649     67   -302   -198       N1+
ATOM   3071  NH2 ARG A 449       1.017  66.291 -16.192  1.00 53.45           N  
ANISOU 3071  NH2 ARG A 449     6160   7162   6986     23   -232   -316       N  
ATOM   3072  N   GLU A 450       1.866  65.101 -23.948  1.00 45.66           N  
ANISOU 3072  N   GLU A 450     5490   5873   5987     98    -23     25       N  
ATOM   3073  CA  GLU A 450       3.262  64.675 -23.998  1.00 46.85           C  
ANISOU 3073  CA  GLU A 450     5603   6031   6169     86    -11    -35       C  
ATOM   3074  C   GLU A 450       3.984  65.273 -25.192  1.00 30.47           C  
ANISOU 3074  C   GLU A 450     3555   3875   4148     89     98    -26       C  
ATOM   3075  O   GLU A 450       5.205  65.428 -25.178  1.00 66.48           O  
ANISOU 3075  O   GLU A 450     8066   8422   8772     67    147    -96       O  
ATOM   3076  CB  GLU A 450       3.369  63.148 -24.010  1.00 76.32           C  
ANISOU 3076  CB  GLU A 450     9356   9818   9823    109   -107    -11       C  
ATOM   3077  CG  GLU A 450       2.894  62.486 -22.724  1.00 88.05           C  
ANISOU 3077  CG  GLU A 450    10813  11380  11260    110   -200    -29       C  
ATOM   3078  CD  GLU A 450       3.659  62.965 -21.502  1.00 94.04           C  
ANISOU 3078  CD  GLU A 450    11483  12181  12068     90   -199   -131       C  
ATOM   3079  OE1 GLU A 450       4.870  63.249 -21.626  1.00 88.09           O  
ANISOU 3079  OE1 GLU A 450    10679  11418  11372     77   -155   -200       O  
ATOM   3080  OE2 GLU A 450       3.048  63.053 -20.416  1.00106.06           O1-
ANISOU 3080  OE2 GLU A 450    12981  13747  13569     87   -243   -148       O1-
ATOM   3081  N   TYR A 451       3.226  65.612 -26.228  1.00 46.07           N  
ANISOU 3081  N   TYR A 451     5610   5798   6098    121    139     59       N  
ATOM   3082  CA  TYR A 451       3.788  66.312 -27.377  1.00 52.13           C  
ANISOU 3082  CA  TYR A 451     6419   6478   6911    134    260     79       C  
ATOM   3083  C   TYR A 451       4.183  67.725 -26.960  1.00 49.04           C  
ANISOU 3083  C   TYR A 451     5980   6027   6626     97    375     17       C  
ATOM   3084  O   TYR A 451       5.370  68.044 -26.885  1.00 66.03           O  
ANISOU 3084  O   TYR A 451     8078   8150   8860     61    446    -60       O  
ATOM   3085  CB  TYR A 451       2.794  66.342 -28.539  1.00 49.05           C  
ANISOU 3085  CB  TYR A 451     6129   6057   6452    194    270    186       C  
ATOM   3086  CG  TYR A 451       3.289  67.124 -29.728  1.00 54.72           C  
ANISOU 3086  CG  TYR A 451     6905   6681   7207    222    405    219       C  
ATOM   3087  CD1 TYR A 451       4.219  66.578 -30.607  1.00 66.33           C  
ANISOU 3087  CD1 TYR A 451     8402   8125   8675    235    436    224       C  
ATOM   3088  CD2 TYR A 451       2.831  68.409 -29.972  1.00 55.84           C  
ANISOU 3088  CD2 TYR A 451     7079   6753   7385    241    508    247       C  
ATOM   3089  CE1 TYR A 451       4.676  67.298 -31.697  1.00 70.68           C  
ANISOU 3089  CE1 TYR A 451     9014   8584   9259    266    571    258       C  
ATOM   3090  CE2 TYR A 451       3.279  69.137 -31.054  1.00101.50           C  
ANISOU 3090  CE2 TYR A 451    12925  12441  13199    275    646    283       C  
ATOM   3091  CZ  TYR A 451       4.200  68.580 -31.912  1.00111.38           C  
ANISOU 3091  CZ  TYR A 451    14205  13668  14448    287    678    288       C  
ATOM   3092  OH  TYR A 451       4.645  69.312 -32.993  1.00110.27           O  
ANISOU 3092  OH  TYR A 451    14134  13426  14337    325    827    328       O  
ATOM   3093  N   LEU A 452       3.188  68.568 -26.687  1.00 42.16           N  
ANISOU 3093  N   LEU A 452     5127   5138   5757    104    397     46       N  
ATOM   3094  CA  LEU A 452       3.440  69.825 -25.997  1.00 22.24           C  
ANISOU 3094  CA  LEU A 452     2550   2570   3332     61    489    -25       C  
ATOM   3095  C   LEU A 452       3.961  69.462 -24.618  1.00 64.57           C  
ANISOU 3095  C   LEU A 452     7806   8010   8716     11    412   -132       C  
ATOM   3096  O   LEU A 452       3.633  68.396 -24.103  1.00 60.02           O  
ANISOU 3096  O   LEU A 452     7220   7520   8064     23    285   -121       O  
ATOM   3097  CB  LEU A 452       2.145  70.619 -25.850  1.00 23.83           C  
ANISOU 3097  CB  LEU A 452     2789   2752   3512     86    504     30       C  
ATOM   3098  CG  LEU A 452       1.454  71.112 -27.123  1.00 71.34           C  
ANISOU 3098  CG  LEU A 452     8912   8700   9493    154    577    138       C  
ATOM   3099  CD1 LEU A 452       0.097  71.694 -26.779  1.00 40.24           C  
ANISOU 3099  CD1 LEU A 452     4997   4772   5522    184    559    187       C  
ATOM   3100  CD2 LEU A 452       2.324  72.137 -27.844  1.00122.86           C  
ANISOU 3100  CD2 LEU A 452    15463  15110  16109    150    751    125       C  
ATOM   3101  N   SER A 453       4.768  70.320 -24.007  1.00 29.83           N  
ANISOU 3101  N   SER A 453     3329   3585   4419    -41    488   -239       N  
ATOM   3102  CA  SER A 453       5.257  70.001 -22.664  1.00 50.81           C  
ANISOU 3102  CA  SER A 453     5884   6331   7090    -78    408   -348       C  
ATOM   3103  C   SER A 453       4.079  69.818 -21.708  1.00 55.14           C  
ANISOU 3103  C   SER A 453     6435   6945   7570    -64    309   -321       C  
ATOM   3104  O   SER A 453       2.947  70.172 -22.033  1.00 69.22           O  
ANISOU 3104  O   SER A 453     8285   8697   9320    -38    321   -235       O  
ATOM   3105  CB  SER A 453       6.226  71.075 -22.149  1.00 57.74           C  
ANISOU 3105  CB  SER A 453     6671   7173   8096   -139    510   -481       C  
ATOM   3106  OG  SER A 453       5.652  72.371 -22.193  1.00 58.08           O  
ANISOU 3106  OG  SER A 453     6738   7132   8198   -156    618   -471       O  
ATOM   3107  N   ALA A 454       4.336  69.251 -20.536  1.00 49.73           N  
ANISOU 3107  N   ALA A 454     5681   6354   6860    -73    213   -392       N  
ATOM   3108  CA  ALA A 454       3.290  69.127 -19.530  1.00 51.78           C  
ANISOU 3108  CA  ALA A 454     5941   6673   7062    -62    131   -376       C  
ATOM   3109  C   ALA A 454       2.818  70.513 -19.104  1.00 50.46           C  
ANISOU 3109  C   ALA A 454     5756   6455   6962    -91    212   -408       C  
ATOM   3110  O   ALA A 454       1.649  70.710 -18.767  1.00 69.73           O  
ANISOU 3110  O   ALA A 454     8230   8903   9362    -76    186   -353       O  
ATOM   3111  CB  ALA A 454       3.798  68.352 -18.327  1.00 35.31           C  
ANISOU 3111  CB  ALA A 454     3785   4693   4938    -59     29   -455       C  
ATOM   3112  N   ASP A 455       3.739  71.470 -19.127  1.00 32.40           N  
ANISOU 3112  N   ASP A 455     3414   4115   4781   -136    317   -502       N  
ATOM   3113  CA  ASP A 455       3.441  72.838 -18.712  1.00 69.32           C  
ANISOU 3113  CA  ASP A 455     8069   8733   9535   -170    411   -548       C  
ATOM   3114  C   ASP A 455       2.661  73.606 -19.774  1.00 71.28           C  
ANISOU 3114  C   ASP A 455     8412   8874   9798   -148    516   -442       C  
ATOM   3115  O   ASP A 455       1.679  74.283 -19.460  1.00 87.23           O  
ANISOU 3115  O   ASP A 455    10458  10872  11813   -139    536   -408       O  
ATOM   3116  CB  ASP A 455       4.724  73.584 -18.331  1.00 67.14           C  
ANISOU 3116  CB  ASP A 455     7696   8437   9378   -232    494   -701       C  
ATOM   3117  CG  ASP A 455       5.218  73.225 -16.941  1.00104.62           C  
ANISOU 3117  CG  ASP A 455    12339  13299  14112   -248    395   -826       C  
ATOM   3118  OD1 ASP A 455       4.619  72.328 -16.306  1.00107.08           O  
ANISOU 3118  OD1 ASP A 455    12665  13702  14319   -206    267   -784       O  
ATOM   3119  OD2 ASP A 455       6.202  73.843 -16.478  1.00111.51           O1-
ANISOU 3119  OD2 ASP A 455    13116  14174  15079   -298    448   -970       O1-
ATOM   3120  N   ALA A 456       3.102  73.505 -21.025  1.00 49.16           N  
ANISOU 3120  N   ALA A 456     5663   6007   7009   -131    583   -389       N  
ATOM   3121  CA  ALA A 456       2.351  74.069 -22.143  1.00 45.58           C  
ANISOU 3121  CA  ALA A 456     5312   5463   6544    -87    671   -273       C  
ATOM   3122  C   ALA A 456       0.901  73.611 -22.062  1.00 47.88           C  
ANISOU 3122  C   ALA A 456     5659   5806   6728    -33    570   -170       C  
ATOM   3123  O   ALA A 456      -0.020  74.388 -22.295  1.00 48.36           O  
ANISOU 3123  O   ALA A 456     5772   5819   6785     -3    624   -108       O  
ATOM   3124  CB  ALA A 456       2.968  73.645 -23.468  1.00 55.79           C  
ANISOU 3124  CB  ALA A 456     6661   6709   7830    -59    718   -219       C  
ATOM   3125  N   PHE A 457       0.713  72.338 -21.718  1.00 53.97           N  
ANISOU 3125  N   PHE A 457     6417   6675   7415    -20    429   -155       N  
ATOM   3126  CA  PHE A 457      -0.613  71.746 -21.578  1.00 54.81           C  
ANISOU 3126  CA  PHE A 457     6563   6837   7424     20    328    -72       C  
ATOM   3127  C   PHE A 457      -1.352  72.363 -20.392  1.00 42.09           C  
ANISOU 3127  C   PHE A 457     4915   5252   5826      3    313   -105       C  
ATOM   3128  O   PHE A 457      -2.491  72.807 -20.519  1.00 57.38           O  
ANISOU 3128  O   PHE A 457     6893   7173   7736     34    322    -38       O  
ATOM   3129  CB  PHE A 457      -0.485  70.225 -21.401  1.00 51.84           C  
ANISOU 3129  CB  PHE A 457     6178   6548   6969     28    198    -63       C  
ATOM   3130  CG  PHE A 457      -1.801  69.491 -21.396  1.00 45.83           C  
ANISOU 3130  CG  PHE A 457     5459   5839   6116     65    103     20       C  
ATOM   3131  CD1 PHE A 457      -2.337  69.000 -22.573  1.00 28.49           C  
ANISOU 3131  CD1 PHE A 457     3333   3630   3862    109     88    109       C  
ATOM   3132  CD2 PHE A 457      -2.490  69.277 -20.215  1.00 29.93           C  
ANISOU 3132  CD2 PHE A 457     3411   3887   4074     54     32      1       C  
ATOM   3133  CE1 PHE A 457      -3.544  68.327 -22.576  1.00 27.69           C  
ANISOU 3133  CE1 PHE A 457     3258   3578   3684    136      4    170       C  
ATOM   3134  CE2 PHE A 457      -3.687  68.598 -20.215  1.00 24.39           C  
ANISOU 3134  CE2 PHE A 457     2742   3228   3298     80    -44     69       C  
ATOM   3135  CZ  PHE A 457      -4.218  68.125 -21.398  1.00 44.21           C  
ANISOU 3135  CZ  PHE A 457     5313   5726   5759    118    -59    150       C  
ATOM   3136  N   LYS A 458      -0.685  72.380 -19.242  1.00 49.81           N  
ANISOU 3136  N   LYS A 458     5812   6274   6840    -43    287   -213       N  
ATOM   3137  CA  LYS A 458      -1.219  72.975 -18.020  1.00 52.68           C  
ANISOU 3137  CA  LYS A 458     6132   6665   7218    -63    275   -263       C  
ATOM   3138  C   LYS A 458      -1.763  74.375 -18.288  1.00 62.82           C  
ANISOU 3138  C   LYS A 458     7446   7859   8563    -62    395   -243       C  
ATOM   3139  O   LYS A 458      -2.947  74.644 -18.068  1.00 62.50           O  
ANISOU 3139  O   LYS A 458     7436   7824   8487    -35    378   -184       O  
ATOM   3140  CB  LYS A 458      -0.110  73.039 -16.963  1.00 44.57           C  
ANISOU 3140  CB  LYS A 458     5011   5684   6242   -110    263   -403       C  
ATOM   3141  CG  LYS A 458      -0.549  73.371 -15.541  1.00 19.31           C  
ANISOU 3141  CG  LYS A 458     1761   2539   3036   -124    221   -467       C  
ATOM   3142  CD  LYS A 458       0.684  73.484 -14.634  1.00 32.95           C  
ANISOU 3142  CD  LYS A 458     3390   4315   4814   -164    213   -618       C  
ATOM   3143  CE  LYS A 458       0.327  73.607 -13.161  1.00 72.90           C  
ANISOU 3143  CE  LYS A 458     8400   9451   9847   -166    151   -687       C  
ATOM   3144  NZ  LYS A 458      -0.122  74.975 -12.779  1.00 55.55           N1+
ANISOU 3144  NZ  LYS A 458     6192   7194   7720   -197    242   -726       N1+
ATOM   3145  N   SER A 459      -0.892  75.256 -18.776  1.00 54.08           N  
ANISOU 3145  N   SER A 459     6332   6666   7551    -90    522   -291       N  
ATOM   3146  CA  SER A 459      -1.251  76.657 -18.995  1.00 64.66           C  
ANISOU 3146  CA  SER A 459     7703   7906   8961    -92    659   -282       C  
ATOM   3147  C   SER A 459      -2.386  76.817 -20.001  1.00 45.28           C  
ANISOU 3147  C   SER A 459     5348   5409   6447    -18    682   -140       C  
ATOM   3148  O   SER A 459      -3.306  77.604 -19.790  1.00 65.71           O  
ANISOU 3148  O   SER A 459     7962   7967   9037      5    722   -105       O  
ATOM   3149  CB  SER A 459      -0.033  77.471 -19.440  1.00 23.07           C  
ANISOU 3149  CB  SER A 459     2414   2542   3809   -137    805   -358       C  
ATOM   3150  OG  SER A 459       0.310  77.183 -20.780  1.00 57.25           O  
ANISOU 3150  OG  SER A 459     6809   6818   8126   -102    853   -284       O  
ATOM   3151  N   GLY A 460      -2.316  76.075 -21.099  1.00 30.11           N  
ANISOU 3151  N   GLY A 460     3481   3489   4471     25    657    -63       N  
ATOM   3152  CA  GLY A 460      -3.381  76.087 -22.085  1.00 37.49           C  
ANISOU 3152  CA  GLY A 460     4506   4406   5335    105    659     64       C  
ATOM   3153  C   GLY A 460      -4.735  75.785 -21.466  1.00 53.03           C  
ANISOU 3153  C   GLY A 460     6470   6450   7230    132    555    108       C  
ATOM   3154  O   GLY A 460      -5.750  76.346 -21.871  1.00 67.04           O  
ANISOU 3154  O   GLY A 460     8296   8200   8976    190    586    183       O  
ATOM   3155  N   ILE A 461      -4.753  74.896 -20.479  1.00 23.43           N  
ANISOU 3155  N   ILE A 461     2661   2793   3450     95    435     60       N  
ATOM   3156  CA  ILE A 461      -5.993  74.533 -19.807  1.00 43.24           C  
ANISOU 3156  CA  ILE A 461     5162   5373   5896    113    341     94       C  
ATOM   3157  C   ILE A 461      -6.447  75.634 -18.859  1.00 38.34           C  
ANISOU 3157  C   ILE A 461     4513   4728   5324     95    396     55       C  
ATOM   3158  O   ILE A 461      -7.612  76.030 -18.869  1.00 30.70           O  
ANISOU 3158  O   ILE A 461     3573   3763   4329    136    396    114       O  
ATOM   3159  CB  ILE A 461      -5.860  73.206 -19.044  1.00 47.99           C  
ANISOU 3159  CB  ILE A 461     5718   6070   6444     85    211     61       C  
ATOM   3160  CG1 ILE A 461      -5.953  72.034 -20.019  1.00 46.22           C  
ANISOU 3160  CG1 ILE A 461     5536   5877   6150    117    142    127       C  
ATOM   3161  CG2 ILE A 461      -6.951  73.076 -18.000  1.00 29.67           C  
ANISOU 3161  CG2 ILE A 461     3375   3810   4089     85    143     66       C  
ATOM   3162  CD1 ILE A 461      -5.782  70.714 -19.352  1.00 81.43           C  
ANISOU 3162  CD1 ILE A 461     9964  10417  10561     95     30    101       C  
ATOM   3163  N   VAL A 462      -5.521  76.124 -18.042  1.00 27.75           N  
ANISOU 3163  N   VAL A 462     3116   3371   4058     35    440    -51       N  
ATOM   3164  CA  VAL A 462      -5.787  77.284 -17.199  1.00 25.12           C  
ANISOU 3164  CA  VAL A 462     2757   3002   3786     13    511   -103       C  
ATOM   3165  C   VAL A 462      -6.469  78.388 -18.005  1.00 40.11           C  
ANISOU 3165  C   VAL A 462     4724   4809   5707     62    626    -27       C  
ATOM   3166  O   VAL A 462      -7.516  78.899 -17.614  1.00 54.86           O  
ANISOU 3166  O   VAL A 462     6605   6680   7560     89    630      7       O  
ATOM   3167  CB  VAL A 462      -4.488  77.833 -16.579  1.00 14.58           C  
ANISOU 3167  CB  VAL A 462     1356   1638   2546    -57    576   -237       C  
ATOM   3168  CG1 VAL A 462      -4.674  79.263 -16.132  1.00 35.84           C  
ANISOU 3168  CG1 VAL A 462     4043   4255   5320    -78    695   -283       C  
ATOM   3169  CG2 VAL A 462      -4.035  76.954 -15.415  1.00 36.73           C  
ANISOU 3169  CG2 VAL A 462     4086   4550   5321    -93    458   -323       C  
ATOM   3170  N   GLN A 463      -5.875  78.736 -19.141  1.00 33.28           N  
ANISOU 3170  N   GLN A 463     3908   3862   4874     82    723      3       N  
ATOM   3171  CA  GLN A 463      -6.414  79.777 -20.006  1.00 40.11           C  
ANISOU 3171  CA  GLN A 463     4852   4633   5755    144    847     82       C  
ATOM   3172  C   GLN A 463      -7.833  79.461 -20.463  1.00 37.98           C  
ANISOU 3172  C   GLN A 463     4632   4413   5385    230    775    197       C  
ATOM   3173  O   GLN A 463      -8.678  80.349 -20.553  1.00 46.71           O  
ANISOU 3173  O   GLN A 463     5777   5478   6491    281    839    246       O  
ATOM   3174  CB  GLN A 463      -5.509  79.983 -21.223  1.00 30.60           C  
ANISOU 3174  CB  GLN A 463     3700   3341   4585    159    954    104       C  
ATOM   3175  CG  GLN A 463      -5.797  81.259 -21.995  1.00 78.21           C  
ANISOU 3175  CG  GLN A 463     9814   9250  10652    219   1121    167       C  
ATOM   3176  CD  GLN A 463      -4.810  81.501 -23.117  1.00124.24           C  
ANISOU 3176  CD  GLN A 463    15698  14983  16525    230   1245    182       C  
ATOM   3177  NE2 GLN A 463      -4.556  82.770 -23.419  1.00137.16           N  
ANISOU 3177  NE2 GLN A 463    17383  16488  18245    238   1431    181       N  
ATOM   3178  OE1 GLN A 463      -4.285  80.561 -23.710  1.00146.87           O  
ANISOU 3178  OE1 GLN A 463    18566  17886  19352    232   1183    195       O  
ATOM   3179  N   TYR A 464      -8.084  78.191 -20.760  1.00 42.27           N  
ANISOU 3179  N   TYR A 464     5171   5044   5844    247    644    234       N  
ATOM   3180  CA  TYR A 464      -9.403  77.729 -21.185  1.00 20.59           C  
ANISOU 3180  CA  TYR A 464     2456   2361   3005    320    560    325       C  
ATOM   3181  C   TYR A 464     -10.434  77.951 -20.082  1.00 52.08           C  
ANISOU 3181  C   TYR A 464     6404   6398   6986    311    513    313       C  
ATOM   3182  O   TYR A 464     -11.527  78.460 -20.332  1.00 51.37           O  
ANISOU 3182  O   TYR A 464     6344   6308   6866    378    528    376       O  
ATOM   3183  CB  TYR A 464      -9.334  76.249 -21.557  1.00 27.29           C  
ANISOU 3183  CB  TYR A 464     3296   3292   3781    317    431    341       C  
ATOM   3184  CG  TYR A 464     -10.664  75.571 -21.809  1.00 28.81           C  
ANISOU 3184  CG  TYR A 464     3496   3566   3885    371    326    407       C  
ATOM   3185  CD1 TYR A 464     -11.324  75.716 -23.019  1.00 22.46           C  
ANISOU 3185  CD1 TYR A 464     2753   2757   3024    463    339    491       C  
ATOM   3186  CD2 TYR A 464     -11.239  74.757 -20.844  1.00 26.21           C  
ANISOU 3186  CD2 TYR A 464     3112   3321   3528    332    217    380       C  
ATOM   3187  CE1 TYR A 464     -12.526  75.078 -23.256  1.00 29.46           C  
ANISOU 3187  CE1 TYR A 464     3632   3727   3833    509    238    535       C  
ATOM   3188  CE2 TYR A 464     -12.445  74.120 -21.067  1.00 16.31           C  
ANISOU 3188  CE2 TYR A 464     1855   2138   2203    372    129    429       C  
ATOM   3189  CZ  TYR A 464     -13.080  74.281 -22.276  1.00 33.54           C  
ANISOU 3189  CZ  TYR A 464     4087   4322   4336    457    136    501       C  
ATOM   3190  OH  TYR A 464     -14.282  73.642 -22.498  1.00 36.44           O  
ANISOU 3190  OH  TYR A 464     4439   4768   4637    493     45    534       O  
ATOM   3191  N   LEU A 465     -10.075  77.573 -18.860  1.00 29.58           N  
ANISOU 3191  N   LEU A 465     3487   3593   4161    236    459    230       N  
ATOM   3192  CA  LEU A 465     -10.976  77.717 -17.729  1.00 38.78           C  
ANISOU 3192  CA  LEU A 465     4613   4805   5317    225    415    213       C  
ATOM   3193  C   LEU A 465     -11.236  79.186 -17.420  1.00 37.65           C  
ANISOU 3193  C   LEU A 465     4483   4585   5237    236    536    202       C  
ATOM   3194  O   LEU A 465     -12.381  79.598 -17.262  1.00 61.09           O  
ANISOU 3194  O   LEU A 465     7464   7567   8183    281    535    249       O  
ATOM   3195  CB  LEU A 465     -10.426  76.992 -16.495  1.00 27.71           C  
ANISOU 3195  CB  LEU A 465     3144   3465   3920    153    337    125       C  
ATOM   3196  CG  LEU A 465     -10.384  75.465 -16.612  1.00 48.35           C  
ANISOU 3196  CG  LEU A 465     5748   6160   6464    147    215    141       C  
ATOM   3197  CD1 LEU A 465      -9.883  74.829 -15.323  1.00 17.84           C  
ANISOU 3197  CD1 LEU A 465     1827   2356   2597     93    148     61       C  
ATOM   3198  CD2 LEU A 465     -11.753  74.901 -16.997  1.00 15.42           C  
ANISOU 3198  CD2 LEU A 465     1597   2040   2222    196    145    225       C  
ATOM   3199  N   GLN A 466     -10.172  79.975 -17.350  1.00 42.00           N  
ANISOU 3199  N   GLN A 466     5031   5054   5872    194    644    136       N  
ATOM   3200  CA  GLN A 466     -10.303  81.384 -17.017  1.00 34.28           C  
ANISOU 3200  CA  GLN A 466     4066   3992   4967    194    773    113       C  
ATOM   3201  C   GLN A 466     -11.128  82.161 -18.046  1.00 28.84           C  
ANISOU 3201  C   GLN A 466     3460   3240   4259    290    859    221       C  
ATOM   3202  O   GLN A 466     -11.947  83.007 -17.689  1.00 43.10           O  
ANISOU 3202  O   GLN A 466     5279   5020   6075    322    910    242       O  
ATOM   3203  CB  GLN A 466      -8.924  82.019 -16.831  1.00 28.61           C  
ANISOU 3203  CB  GLN A 466     3324   3194   4352    123    881     10       C  
ATOM   3204  CG  GLN A 466      -8.124  81.424 -15.682  1.00 49.01           C  
ANISOU 3204  CG  GLN A 466     5819   5847   6955     39    801   -111       C  
ATOM   3205  CD  GLN A 466      -6.777  82.102 -15.487  1.00 81.37           C  
ANISOU 3205  CD  GLN A 466     9879   9875  11162    -33    907   -230       C  
ATOM   3206  NE2 GLN A 466      -6.101  81.775 -14.388  1.00 67.45           N  
ANISOU 3206  NE2 GLN A 466     8033   8176   9420    -98    845   -350       N  
ATOM   3207  OE1 GLN A 466      -6.350  82.909 -16.314  1.00 77.26           O  
ANISOU 3207  OE1 GLN A 466     9404   9245  10708    -26   1046   -216       O  
ATOM   3208  N   LYS A 467     -10.916  81.868 -19.323  1.00 38.58           N  
ANISOU 3208  N   LYS A 467     4750   4451   5457    343    875    290       N  
ATOM   3209  CA  LYS A 467     -11.598  82.585 -20.397  1.00 18.75           C  
ANISOU 3209  CA  LYS A 467     2326   1883   2916    451    959    394       C  
ATOM   3210  C   LYS A 467     -13.077  82.230 -20.509  1.00 39.02           C  
ANISOU 3210  C   LYS A 467     4897   4539   5389    531    859    473       C  
ATOM   3211  O   LYS A 467     -13.881  83.056 -20.941  1.00 44.44           O  
ANISOU 3211  O   LYS A 467     5636   5190   6057    621    926    543       O  
ATOM   3212  CB  LYS A 467     -10.913  82.325 -21.743  1.00 34.76           C  
ANISOU 3212  CB  LYS A 467     4416   3868   4924    493   1002    443       C  
ATOM   3213  CG  LYS A 467     -11.646  82.942 -22.932  1.00 46.75           C  
ANISOU 3213  CG  LYS A 467     6032   5343   6388    625   1075    559       C  
ATOM   3214  CD  LYS A 467     -10.892  82.734 -24.240  1.00 52.30           C  
ANISOU 3214  CD  LYS A 467     6804   5997   7071    669   1131    604       C  
ATOM   3215  CE  LYS A 467     -11.605  83.417 -25.396  1.00 65.08           C  
ANISOU 3215  CE  LYS A 467     8528   7572   8627    817   1212    721       C  
ATOM   3216  NZ  LYS A 467     -10.647  84.128 -26.283  1.00 59.76           N1+
ANISOU 3216  NZ  LYS A 467     7940   6764   8002    844   1388    745       N1+
ATOM   3217  N   HIS A 468     -13.434  81.005 -20.126  1.00 34.98           N  
ANISOU 3217  N   HIS A 468     4330   4140   4821    502    704    460       N  
ATOM   3218  CA  HIS A 468     -14.800  80.526 -20.313  1.00 37.19           C  
ANISOU 3218  CA  HIS A 468     4604   4511   5016    569    604    525       C  
ATOM   3219  C   HIS A 468     -15.557  80.252 -19.014  1.00 36.85           C  
ANISOU 3219  C   HIS A 468     4491   4539   4973    523    524    485       C  
ATOM   3220  O   HIS A 468     -16.658  79.706 -19.043  1.00 37.51           O  
ANISOU 3220  O   HIS A 468     4552   4704   4995    561    433    522       O  
ATOM   3221  CB  HIS A 468     -14.818  79.280 -21.195  1.00 20.41           C  
ANISOU 3221  CB  HIS A 468     2483   2456   2814    592    496    559       C  
ATOM   3222  CG  HIS A 468     -14.253  79.495 -22.564  1.00 51.89           C  
ANISOU 3222  CG  HIS A 468     6548   6386   6784    657    566    611       C  
ATOM   3223  CD2 HIS A 468     -13.009  79.294 -23.058  1.00 45.02           C  
ANISOU 3223  CD2 HIS A 468     5702   5462   5943    622    612    589       C  
ATOM   3224  ND1 HIS A 468     -15.008  79.972 -23.614  1.00 64.67           N  
ANISOU 3224  ND1 HIS A 468     8230   7999   8343    781    599    698       N  
ATOM   3225  CE1 HIS A 468     -14.253  80.057 -24.696  1.00 27.26           C  
ANISOU 3225  CE1 HIS A 468     3560   3204   3595    821    665    731       C  
ATOM   3226  NE2 HIS A 468     -13.036  79.652 -24.385  1.00 43.17           N  
ANISOU 3226  NE2 HIS A 468     5550   5185   5667    722    676    666       N  
ATOM   3227  N   SER A 469     -14.969  80.640 -17.883  1.00 34.33           N  
ANISOU 3227  N   SER A 469     4134   4188   4723    442    562    403       N  
ATOM   3228  CA  SER A 469     -15.599  80.450 -16.572  1.00 48.38           C  
ANISOU 3228  CA  SER A 469     5853   6027   6501    399    500    362       C  
ATOM   3229  C   SER A 469     -17.066  80.854 -16.559  1.00 31.38           C  
ANISOU 3229  C   SER A 469     3704   3905   4313    472    491    424       C  
ATOM   3230  O   SER A 469     -17.418  81.953 -16.983  1.00 32.02           O  
ANISOU 3230  O   SER A 469     3830   3923   4412    537    590    466       O  
ATOM   3231  CB  SER A 469     -14.852  81.238 -15.491  1.00 25.56           C  
ANISOU 3231  CB  SER A 469     2936   3081   3693    328    576    270       C  
ATOM   3232  OG  SER A 469     -13.557  80.711 -15.266  1.00 76.74           O  
ANISOU 3232  OG  SER A 469     9392   9562  10204    256    559    194       O  
ATOM   3233  N   TYR A 470     -17.906  79.953 -16.061  1.00 32.85           N  
ANISOU 3233  N   TYR A 470     3843   4186   4452    461    379    427       N  
ATOM   3234  CA  TYR A 470     -19.345  80.177 -15.943  1.00 30.93           C  
ANISOU 3234  CA  TYR A 470     3586   3990   4177    521    355    474       C  
ATOM   3235  C   TYR A 470     -20.058  80.271 -17.294  1.00 27.82           C  
ANISOU 3235  C   TYR A 470     3230   3613   3728    628    351    558       C  
ATOM   3236  O   TYR A 470     -21.180  80.768 -17.383  1.00 14.00           O  
ANISOU 3236  O   TYR A 470     1476   1887   1956    700    357    601       O  
ATOM   3237  CB  TYR A 470     -19.639  81.395 -15.062  1.00 10.71           C  
ANISOU 3237  CB  TYR A 470     1024   1377   1668    521    445    453       C  
ATOM   3238  CG  TYR A 470     -18.922  81.355 -13.731  1.00 34.67           C  
ANISOU 3238  CG  TYR A 470     4021   4402   4751    424    448    362       C  
ATOM   3239  CD1 TYR A 470     -17.746  82.066 -13.536  1.00 17.57           C  
ANISOU 3239  CD1 TYR A 470     1872   2154   2651    380    539    302       C  
ATOM   3240  CD2 TYR A 470     -19.411  80.596 -12.675  1.00 27.59           C  
ANISOU 3240  CD2 TYR A 470     3071   3580   3831    381    363    331       C  
ATOM   3241  CE1 TYR A 470     -17.080  82.033 -12.332  1.00 17.09           C  
ANISOU 3241  CE1 TYR A 470     1770   2097   2628    299    534    207       C  
ATOM   3242  CE2 TYR A 470     -18.748  80.555 -11.458  1.00 33.26           C  
ANISOU 3242  CE2 TYR A 470     3760   4299   4580    307    362    247       C  
ATOM   3243  CZ  TYR A 470     -17.578  81.279 -11.295  1.00 37.51           C  
ANISOU 3243  CZ  TYR A 470     4309   4765   5178    268    442    182       C  
ATOM   3244  OH  TYR A 470     -16.905  81.261 -10.097  1.00 44.69           O  
ANISOU 3244  OH  TYR A 470     5181   5685   6112    202    436     88       O  
ATOM   3245  N   LYS A 471     -19.406  79.767 -18.336  1.00 22.81           N  
ANISOU 3245  N   LYS A 471     2629   2971   3066    644    335    578       N  
ATOM   3246  CA  LYS A 471     -20.006  79.710 -19.668  1.00 34.87           C  
ANISOU 3246  CA  LYS A 471     4194   4529   4528    751    316    651       C  
ATOM   3247  C   LYS A 471     -19.926  78.303 -20.276  1.00 58.80           C  
ANISOU 3247  C   LYS A 471     7203   7635   7502    733    200    648       C  
ATOM   3248  O   LYS A 471     -19.532  77.345 -19.607  1.00 46.23           O  
ANISOU 3248  O   LYS A 471     5569   6074   5922    641    134    596       O  
ATOM   3249  CB  LYS A 471     -19.345  80.727 -20.591  1.00 20.69           C  
ANISOU 3249  CB  LYS A 471     2482   2633   2746    817    442    693       C  
ATOM   3250  CG  LYS A 471     -19.554  82.172 -20.172  1.00 50.19           C  
ANISOU 3250  CG  LYS A 471     6249   6286   6533    852    571    706       C  
ATOM   3251  CD  LYS A 471     -18.882  83.140 -21.135  1.00 46.06           C  
ANISOU 3251  CD  LYS A 471     5820   5653   6028    920    711    751       C  
ATOM   3252  CE  LYS A 471     -19.224  84.581 -20.802  1.00 90.44           C  
ANISOU 3252  CE  LYS A 471    11480  11188  11695    968    847    772       C  
ATOM   3253  NZ  LYS A 471     -18.559  85.542 -21.722  1.00104.38           N1+
ANISOU 3253  NZ  LYS A 471    13345  12830  13482   1035   1005    819       N1+
ATOM   3254  N   ASN A 472     -20.306  78.188 -21.545  1.00 54.02           N  
ANISOU 3254  N   ASN A 472     6632   7059   6832    828    179    703       N  
ATOM   3255  CA  ASN A 472     -20.307  76.904 -22.239  1.00 17.06           C  
ANISOU 3255  CA  ASN A 472     1936   2451   2096    821     73    699       C  
ATOM   3256  C   ASN A 472     -19.308  76.879 -23.389  1.00 30.62           C  
ANISOU 3256  C   ASN A 472     3725   4118   3791    855    113    726       C  
ATOM   3257  O   ASN A 472     -18.743  77.912 -23.747  1.00 54.01           O  
ANISOU 3257  O   ASN A 472     6752   6990   6779    899    229    756       O  
ATOM   3258  CB  ASN A 472     -21.708  76.570 -22.744  1.00 49.98           C  
ANISOU 3258  CB  ASN A 472     6069   6724   6199    899    -12    723       C  
ATOM   3259  CG  ASN A 472     -22.748  76.621 -21.646  1.00 32.68           C  
ANISOU 3259  CG  ASN A 472     3805   4580   4032    868    -43    698       C  
ATOM   3260  ND2 ASN A 472     -23.174  77.829 -21.285  1.00 69.81           N  
ANISOU 3260  ND2 ASN A 472     8522   9245   8759    919     37    724       N  
ATOM   3261  OD1 ASN A 472     -23.166  75.590 -21.128  1.00 58.25           O  
ANISOU 3261  OD1 ASN A 472     6979   7883   7269    801   -129    657       O  
ATOM   3262  N   THR A 473     -19.103  75.705 -23.978  1.00 57.70           N  
ANISOU 3262  N   THR A 473     7145   7600   7177    837     26    715       N  
ATOM   3263  CA  THR A 473     -17.952  75.498 -24.854  1.00 30.62           C  
ANISOU 3263  CA  THR A 473     3777   4120   3739    841     60    726       C  
ATOM   3264  C   THR A 473     -18.162  74.420 -25.921  1.00 49.80           C  
ANISOU 3264  C   THR A 473     6211   6622   6089    879    -35    737       C  
ATOM   3265  O   THR A 473     -19.052  73.578 -25.797  1.00 47.08           O  
ANISOU 3265  O   THR A 473     5808   6370   5710    861   -135    709       O  
ATOM   3266  CB  THR A 473     -16.712  75.150 -24.004  1.00 36.25           C  
ANISOU 3266  CB  THR A 473     4473   4780   4522    720     81    667       C  
ATOM   3267  CG2 THR A 473     -15.616  74.551 -24.848  1.00 61.88           C  
ANISOU 3267  CG2 THR A 473     7760   7999   7753    709     84    667       C  
ATOM   3268  OG1 THR A 473     -16.215  76.343 -23.382  1.00 52.67           O  
ANISOU 3268  OG1 THR A 473     6568   6770   6673    702    198    656       O  
ATOM   3269  N   LYS A 474     -17.346  74.475 -26.972  1.00 40.38           N  
ANISOU 3269  N   LYS A 474     5089   5384   4871    924     10    767       N  
ATOM   3270  CA  LYS A 474     -17.263  73.416 -27.975  1.00 40.39           C  
ANISOU 3270  CA  LYS A 474     5101   5441   4802    940    -64    762       C  
ATOM   3271  C   LYS A 474     -15.836  72.867 -28.020  1.00 34.48           C  
ANISOU 3271  C   LYS A 474     4378   4632   4089    867    -44    742       C  
ATOM   3272  O   LYS A 474     -14.911  73.532 -27.564  1.00 28.62           O  
ANISOU 3272  O   LYS A 474     3657   3802   3417    826     52    735       O  
ATOM   3273  CB  LYS A 474     -17.649  73.954 -29.353  1.00 42.99           C  
ANISOU 3273  CB  LYS A 474     5500   5784   5051   1084    -33    821       C  
ATOM   3274  CG  LYS A 474     -19.080  74.449 -29.456  1.00 49.36           C  
ANISOU 3274  CG  LYS A 474     6281   6666   5809   1177    -62    840       C  
ATOM   3275  CD  LYS A 474     -19.384  74.981 -30.854  1.00 59.61           C  
ANISOU 3275  CD  LYS A 474     7655   7981   7013   1338    -30    902       C  
ATOM   3276  CE  LYS A 474     -20.865  75.291 -31.010  1.00 99.42           C  
ANISOU 3276  CE  LYS A 474    12658  13124  11994   1437    -83    909       C  
ATOM   3277  NZ  LYS A 474     -21.220  75.837 -32.342  1.00113.30           N1+
ANISOU 3277  NZ  LYS A 474    14491  14911  13647   1614    -57    970       N1+
ATOM   3278  N   ASN A 475     -15.657  71.666 -28.575  1.00 66.14           N  
ANISOU 3278  N   ASN A 475     8379   8694   8058    830   -110    703       N  
ATOM   3279  CA  ASN A 475     -14.327  71.057 -28.704  1.00 46.40           C  
ANISOU 3279  CA  ASN A 475     5902   6145   5583    769    -96    683       C  
ATOM   3280  C   ASN A 475     -13.264  72.070 -29.102  1.00 61.20           C  
ANISOU 3280  C   ASN A 475     7849   7910   7493    813     23    733       C  
ATOM   3281  O   ASN A 475     -12.233  72.190 -28.441  1.00 48.57           O  
ANISOU 3281  O   ASN A 475     6238   6249   5969    732     77    696       O  
ATOM   3282  CB  ASN A 475     -14.322  69.940 -29.752  1.00 38.74           C  
ANISOU 3282  CB  ASN A 475     4945   5228   4546    777   -153    659       C  
ATOM   3283  CG  ASN A 475     -15.531  69.045 -29.664  1.00 84.72           C  
ANISOU 3283  CG  ASN A 475    10708  11148  10333    753   -248    611       C  
ATOM   3284  ND2 ASN A 475     -15.655  68.330 -28.555  1.00 98.96           N  
ANISOU 3284  ND2 ASN A 475    12451  12966  12182    647   -288    559       N  
ATOM   3285  OD1 ASN A 475     -16.346  68.990 -30.585  1.00104.90           O  
ANISOU 3285  OD1 ASN A 475    13274  13762  12821    834   -280    620       O  
ATOM   3286  N   GLU A 476     -13.525  72.783 -30.197  1.00 49.13           N  
ANISOU 3286  N   GLU A 476     6393   6362   5914    932     81    796       N  
ATOM   3287  CA  GLU A 476     -12.573  73.730 -30.774  1.00 55.11           C  
ANISOU 3287  CA  GLU A 476     7229   7009   6701    972    225    833       C  
ATOM   3288  C   GLU A 476     -12.051  74.738 -29.765  1.00 56.41           C  
ANISOU 3288  C   GLU A 476     7378   7085   6972    909    335    807       C  
ATOM   3289  O   GLU A 476     -10.924  75.211 -29.884  1.00 43.92           O  
ANISOU 3289  O   GLU A 476     5830   5406   5451    881    446    799       O  
ATOM   3290  CB  GLU A 476     -13.210  74.477 -31.945  1.00 86.00           C  
ANISOU 3290  CB  GLU A 476    11224  10919  10534   1129    275    913       C  
ATOM   3291  CG  GLU A 476     -13.638  73.590 -33.094  1.00123.44           C  
ANISOU 3291  CG  GLU A 476    15986  15751  15165   1201    183    924       C  
ATOM   3292  CD  GLU A 476     -14.199  74.388 -34.252  1.00150.12           C  
ANISOU 3292  CD  GLU A 476    19450  19132  18455   1368    240    999       C  
ATOM   3293  OE1 GLU A 476     -14.247  75.632 -34.147  1.00139.58           O  
ANISOU 3293  OE1 GLU A 476    18168  17716  17149   1435    353   1059       O  
ATOM   3294  OE2 GLU A 476     -14.590  73.773 -35.266  1.00161.23           O1-
ANISOU 3294  OE2 GLU A 476    20875  20621  19764   1439    177    994       O1-
ATOM   3295  N   ASP A 477     -12.881  75.067 -28.779  1.00 35.34           N  
ANISOU 3295  N   ASP A 477     4653   4448   4327    885    306    788       N  
ATOM   3296  CA  ASP A 477     -12.523  76.053 -27.764  1.00 39.45           C  
ANISOU 3296  CA  ASP A 477     5154   4893   4944    827    403    756       C  
ATOM   3297  C   ASP A 477     -11.355  75.590 -26.901  1.00 29.71           C  
ANISOU 3297  C   ASP A 477     3867   3632   3787    699    402    676       C  
ATOM   3298  O   ASP A 477     -10.495  76.386 -26.525  1.00 52.23           O  
ANISOU 3298  O   ASP A 477     6725   6396   6725    656    514    643       O  
ATOM   3299  CB  ASP A 477     -13.733  76.388 -26.885  1.00 51.54           C  
ANISOU 3299  CB  ASP A 477     6633   6477   6474    832    359    752       C  
ATOM   3300  CG  ASP A 477     -14.817  77.132 -27.641  1.00 64.02           C  
ANISOU 3300  CG  ASP A 477     8264   8072   7990    969    386    828       C  
ATOM   3301  OD1 ASP A 477     -14.499  77.795 -28.650  1.00 52.33           O  
ANISOU 3301  OD1 ASP A 477     6870   6526   6488   1059    485    886       O  
ATOM   3302  OD2 ASP A 477     -15.990  77.062 -27.224  1.00 82.70           O1-
ANISOU 3302  OD2 ASP A 477    10583  10514  10325    992    312    831       O1-
ATOM   3303  N   LEU A 478     -11.327  74.304 -26.581  1.00 39.02           N  
ANISOU 3303  N   LEU A 478     4995   4890   4939    640    277    639       N  
ATOM   3304  CA  LEU A 478     -10.206  73.756 -25.836  1.00 39.82           C  
ANISOU 3304  CA  LEU A 478     5051   4979   5099    536    266    566       C  
ATOM   3305  C   LEU A 478      -8.946  73.817 -26.698  1.00 49.42           C  
ANISOU 3305  C   LEU A 478     6315   6123   6338    539    347    568       C  
ATOM   3306  O   LEU A 478      -7.893  74.270 -26.250  1.00 41.87           O  
ANISOU 3306  O   LEU A 478     5342   5104   5465    479    427    515       O  
ATOM   3307  CB  LEU A 478     -10.499  72.323 -25.400  1.00 14.05           C  
ANISOU 3307  CB  LEU A 478     1737   1810   1791    488    124    538       C  
ATOM   3308  CG  LEU A 478      -9.354  71.612 -24.675  1.00 40.62           C  
ANISOU 3308  CG  LEU A 478     5060   5175   5199    397    100    469       C  
ATOM   3309  CD1 LEU A 478      -8.977  72.352 -23.400  1.00 10.57           C  
ANISOU 3309  CD1 LEU A 478     1205   1341   1471    337    149    406       C  
ATOM   3310  CD2 LEU A 478      -9.709  70.161 -24.378  1.00 37.02           C  
ANISOU 3310  CD2 LEU A 478     4572   4803   4690    366    -28    456       C  
ATOM   3311  N   TRP A 479      -9.063  73.369 -27.944  1.00 31.43           N  
ANISOU 3311  N   TRP A 479     4096   3859   3988    610    327    625       N  
ATOM   3312  CA  TRP A 479      -7.936  73.384 -28.867  1.00 48.79           C  
ANISOU 3312  CA  TRP A 479     6348   5989   6200    623    406    635       C  
ATOM   3313  C   TRP A 479      -7.423  74.804 -29.109  1.00 53.03           C  
ANISOU 3313  C   TRP A 479     6935   6409   6806    649    580    651       C  
ATOM   3314  O   TRP A 479      -6.218  75.064 -29.033  1.00 42.71           O  
ANISOU 3314  O   TRP A 479     5623   5029   5577    594    669    607       O  
ATOM   3315  CB  TRP A 479      -8.319  72.718 -30.192  1.00 47.92           C  
ANISOU 3315  CB  TRP A 479     6300   5921   5988    710    354    698       C  
ATOM   3316  CG  TRP A 479      -9.016  71.391 -30.034  1.00 32.88           C  
ANISOU 3316  CG  TRP A 479     4351   4128   4016    690    194    682       C  
ATOM   3317  CD1 TRP A 479     -10.022  70.895 -30.816  1.00 26.51           C  
ANISOU 3317  CD1 TRP A 479     3565   3393   3113    766    112    723       C  
ATOM   3318  CD2 TRP A 479      -8.759  70.395 -29.035  1.00 31.89           C  
ANISOU 3318  CD2 TRP A 479     4151   4049   3915    590    104    618       C  
ATOM   3319  CE2 TRP A 479      -9.644  69.322 -29.277  1.00 39.88           C  
ANISOU 3319  CE2 TRP A 479     5149   5152   4851    605    -19    625       C  
ATOM   3320  CE3 TRP A 479      -7.867  70.308 -27.957  1.00 28.11           C  
ANISOU 3320  CE3 TRP A 479     3618   3549   3513    496    119    551       C  
ATOM   3321  NE1 TRP A 479     -10.403  69.652 -30.371  1.00 28.33           N  
ANISOU 3321  NE1 TRP A 479     3736   3710   3320    704    -11    676       N  
ATOM   3322  CZ2 TRP A 479      -9.667  68.175 -28.478  1.00 12.85           C  
ANISOU 3322  CZ2 TRP A 479     1666   1786   1432    521   -110    569       C  
ATOM   3323  CZ3 TRP A 479      -7.890  69.172 -27.167  1.00 36.95           C  
ANISOU 3323  CZ3 TRP A 479     4683   4733   4623    431     14    507       C  
ATOM   3324  CH2 TRP A 479      -8.784  68.118 -27.434  1.00 41.93           C  
ANISOU 3324  CH2 TRP A 479     5310   5441   5180    446    -96    525       C  
ATOM   3325  N   ASP A 480      -8.340  75.723 -29.399  1.00 36.08           N  
ANISOU 3325  N   ASP A 480     4834   4243   4633    735    632    711       N  
ATOM   3326  CA  ASP A 480      -7.994  77.133 -29.586  1.00 42.68           C  
ANISOU 3326  CA  ASP A 480     5725   4957   5533    767    809    732       C  
ATOM   3327  C   ASP A 480      -7.209  77.690 -28.402  1.00 44.41           C  
ANISOU 3327  C   ASP A 480     5878   5118   5877    652    879    641       C  
ATOM   3328  O   ASP A 480      -6.192  78.362 -28.573  1.00 48.94           O  
ANISOU 3328  O   ASP A 480     6474   5587   6534    623   1020    615       O  
ATOM   3329  CB  ASP A 480      -9.259  77.964 -29.813  1.00 44.00           C  
ANISOU 3329  CB  ASP A 480     5938   5131   5650    875    835    804       C  
ATOM   3330  CG  ASP A 480      -9.855  77.754 -31.192  1.00 73.56           C  
ANISOU 3330  CG  ASP A 480     9766   8909   9275   1014    812    896       C  
ATOM   3331  OD1 ASP A 480      -9.109  77.316 -32.088  1.00 72.09           O  
ANISOU 3331  OD1 ASP A 480     9627   8699   9064   1033    834    913       O  
ATOM   3332  OD2 ASP A 480     -11.059  78.032 -31.383  1.00 85.53           O1-
ANISOU 3332  OD2 ASP A 480    11298  10479  10721   1109    772    947       O1-
ATOM   3333  N   SER A 481      -7.694  77.398 -27.199  1.00 50.03           N  
ANISOU 3333  N   SER A 481     6506   5900   6601    588    782    588       N  
ATOM   3334  CA  SER A 481      -7.077  77.882 -25.970  1.00 53.33           C  
ANISOU 3334  CA  SER A 481     6854   6285   7124    486    826    492       C  
ATOM   3335  C   SER A 481      -5.651  77.358 -25.793  1.00 45.46           C  
ANISOU 3335  C   SER A 481     5813   5272   6188    398    834    411       C  
ATOM   3336  O   SER A 481      -4.775  78.080 -25.321  1.00 64.98           O  
ANISOU 3336  O   SER A 481     8255   7672   8763    335    939    337       O  
ATOM   3337  CB  SER A 481      -7.939  77.498 -24.766  1.00 44.42           C  
ANISOU 3337  CB  SER A 481     5652   5249   5975    448    704    459       C  
ATOM   3338  OG  SER A 481      -7.336  77.905 -23.554  1.00 63.01           O  
ANISOU 3338  OG  SER A 481     7938   7584   8420    355    736    361       O  
ATOM   3339  N   MET A 482      -5.426  76.103 -26.173  1.00 52.26           N  
ANISOU 3339  N   MET A 482     6666   6202   6987    396    724    419       N  
ATOM   3340  CA  MET A 482      -4.114  75.481 -26.012  1.00 74.85           C  
ANISOU 3340  CA  MET A 482     9482   9063   9895    322    716    345       C  
ATOM   3341  C   MET A 482      -3.169  75.831 -27.153  1.00 79.80           C  
ANISOU 3341  C   MET A 482    10170   9595  10555    347    843    367       C  
ATOM   3342  O   MET A 482      -1.962  75.973 -26.947  1.00 71.04           O  
ANISOU 3342  O   MET A 482     9021   8440   9532    281    911    290       O  
ATOM   3343  CB  MET A 482      -4.245  73.961 -25.881  1.00 47.29           C  
ANISOU 3343  CB  MET A 482     5960   5681   6327    309    552    343       C  
ATOM   3344  CG  MET A 482      -4.909  73.532 -24.594  1.00 69.12           C  
ANISOU 3344  CG  MET A 482     8656   8531   9075    268    440    304       C  
ATOM   3345  SD  MET A 482      -5.049  71.752 -24.442  1.00 89.40           S  
ANISOU 3345  SD  MET A 482    11199  11210  11560    253    272    304       S  
ATOM   3346  CE  MET A 482      -3.333  71.304 -24.266  1.00277.04           C  
ANISOU 3346  CE  MET A 482    34921  34957  35382    191    293    221       C  
ATOM   3347  N   ALA A 483      -3.726  75.974 -28.352  1.00 59.85           N  
ANISOU 3347  N   ALA A 483     7738   7043   7959    446    877    468       N  
ATOM   3348  CA  ALA A 483      -2.932  76.315 -29.523  1.00 46.92           C  
ANISOU 3348  CA  ALA A 483     6176   5312   6340    487   1006    504       C  
ATOM   3349  C   ALA A 483      -2.362  77.730 -29.430  1.00 64.21           C  
ANISOU 3349  C   ALA A 483     8383   7369   8644    466   1202    477       C  
ATOM   3350  O   ALA A 483      -1.546  78.128 -30.261  1.00 86.35           O  
ANISOU 3350  O   ALA A 483    11243  10077  11489    482   1338    491       O  
ATOM   3351  CB  ALA A 483      -3.757  76.151 -30.788  1.00 31.49           C  
ANISOU 3351  CB  ALA A 483     4323   3372   4269    613    990    620       C  
ATOM   3352  N   SER A 484      -2.783  78.479 -28.413  1.00 45.44           N  
ANISOU 3352  N   SER A 484     5961   4983   6321    428   1222    433       N  
ATOM   3353  CA  SER A 484      -2.355  79.862 -28.246  1.00 38.42           C  
ANISOU 3353  CA  SER A 484     5087   3965   5545    404   1412    401       C  
ATOM   3354  C   SER A 484      -1.362  80.042 -27.093  1.00 77.14           C  
ANISOU 3354  C   SER A 484     9878   8858  10573    272   1434    255       C  
ATOM   3355  O   SER A 484      -1.314  81.106 -26.470  1.00 72.03           O  
ANISOU 3355  O   SER A 484     9210   8141  10016    233   1542    201       O  
ATOM   3356  CB  SER A 484      -3.566  80.761 -28.025  1.00 67.71           C  
ANISOU 3356  CB  SER A 484     8839   7658   9231    469   1445    459       C  
ATOM   3357  OG  SER A 484      -4.212  80.435 -26.807  1.00 78.83           O  
ANISOU 3357  OG  SER A 484    10162   9165  10626    419   1311    408       O  
ATOM   3358  N   ILE A 485      -0.577  79.006 -26.813  1.00 72.72           N  
ANISOU 3358  N   ILE A 485     9245   8370  10014    210   1333    187       N  
ATOM   3359  CA  ILE A 485       0.460  79.085 -25.787  1.00 80.81           C  
ANISOU 3359  CA  ILE A 485    10156   9400  11146     97   1343     41       C  
ATOM   3360  C   ILE A 485       1.861  79.092 -26.396  1.00102.03           C  
ANISOU 3360  C   ILE A 485    12833  12017  13915     56   1451    -12       C  
ATOM   3361  O   ILE A 485       2.608  80.061 -26.250  1.00122.37           O  
ANISOU 3361  O   ILE A 485    15385  14494  16618     -1   1608    -91       O  
ATOM   3362  CB  ILE A 485       0.356  77.934 -24.767  1.00 60.98           C  
ANISOU 3362  CB  ILE A 485     7554   7036   8581     55   1145    -15       C  
ATOM   3363  CG1 ILE A 485      -0.616  78.304 -23.645  1.00 60.87           C  
ANISOU 3363  CG1 ILE A 485     7505   7069   8553     45   1085    -33       C  
ATOM   3364  CG2 ILE A 485       1.719  77.630 -24.167  1.00 72.26           C  
ANISOU 3364  CG2 ILE A 485     8880   8485  10092    -35   1140   -151       C  
ATOM   3365  CD1 ILE A 485      -1.980  78.715 -24.130  1.00 70.20           C  
ANISOU 3365  CD1 ILE A 485     8774   8234   9663    134   1094     89       C  
TER    3366      ILE A 485 
ATOM   3367  N   VAL A 515       1.884  75.159 -33.672  1.00 51.95           N  
ANISOU 3367  N   VAL A 515     6989   5693   7058    510   1355    526       N  
ATOM   3368  CA  VAL A 515       1.286  73.841 -33.859  1.00 69.93           C  
ANISOU 3368  CA  VAL A 515     9265   8093   9211    542   1166    560       C  
ATOM   3369  C   VAL A 515      -0.230  73.966 -33.997  1.00 66.28           C  
ANISOU 3369  C   VAL A 515     8852   7687   8645    630   1090    640       C  
ATOM   3370  O   VAL A 515      -0.896  74.455 -33.089  1.00 62.81           O  
ANISOU 3370  O   VAL A 515     8367   7267   8229    605   1064    618       O  
ATOM   3371  CB  VAL A 515       1.598  72.920 -32.658  1.00 69.79           C  
ANISOU 3371  CB  VAL A 515     9125   8171   9220    441   1023    463       C  
ATOM   3372  CG1 VAL A 515       1.222  71.471 -32.972  1.00 46.77           C  
ANISOU 3372  CG1 VAL A 515     6216   5361   6192    467    856    493       C  
ATOM   3373  CG2 VAL A 515       3.069  73.028 -32.269  1.00 60.70           C  
ANISOU 3373  CG2 VAL A 515     7901   6971   8190    350   1104    362       C  
ATOM   3374  N   ASP A 516      -0.777  73.526 -35.128  1.00 48.61           N  
ANISOU 3374  N   ASP A 516     6702   5477   6290    734   1051    726       N  
ATOM   3375  CA  ASP A 516      -2.214  73.658 -35.362  1.00 55.41           C  
ANISOU 3375  CA  ASP A 516     7605   6399   7048    829    979    797       C  
ATOM   3376  C   ASP A 516      -3.008  72.576 -34.642  1.00 75.32           C  
ANISOU 3376  C   ASP A 516    10050   9055   9515    789    780    764       C  
ATOM   3377  O   ASP A 516      -3.553  71.666 -35.271  1.00 61.79           O  
ANISOU 3377  O   ASP A 516     8360   7420   7697    841    669    797       O  
ATOM   3378  CB  ASP A 516      -2.546  73.640 -36.855  1.00 43.95           C  
ANISOU 3378  CB  ASP A 516     6275   4938   5486    967   1011    894       C  
ATOM   3379  CG  ASP A 516      -4.014  73.929 -37.128  1.00 78.01           C  
ANISOU 3379  CG  ASP A 516    10629   9316   9696   1078    950    961       C  
ATOM   3380  OD1 ASP A 516      -4.751  74.247 -36.169  1.00 90.84           O  
ANISOU 3380  OD1 ASP A 516    12192  10977  11346   1044    901    937       O  
ATOM   3381  OD2 ASP A 516      -4.433  73.842 -38.301  1.00 64.86           O1-
ANISOU 3381  OD2 ASP A 516     9055   7669   7921   1204    949   1035       O1-
ATOM   3382  N   VAL A 517      -3.075  72.695 -33.321  1.00 48.90           N  
ANISOU 3382  N   VAL A 517     6610   5730   6238    697    742    696       N  
ATOM   3383  CA  VAL A 517      -3.771  71.722 -32.489  1.00 42.20           C  
ANISOU 3383  CA  VAL A 517     5687   4996   5350    651    573    662       C  
ATOM   3384  C   VAL A 517      -5.162  71.375 -33.027  1.00 44.45           C  
ANISOU 3384  C   VAL A 517     6007   5362   5520    740    473    724       C  
ATOM   3385  O   VAL A 517      -5.520  70.204 -33.123  1.00 45.71           O  
ANISOU 3385  O   VAL A 517     6146   5607   5615    731    344    716       O  
ATOM   3386  CB  VAL A 517      -3.873  72.213 -31.029  1.00 41.25           C  
ANISOU 3386  CB  VAL A 517     5481   4880   5312    568    569    596       C  
ATOM   3387  CG1 VAL A 517      -4.621  71.212 -30.174  1.00 36.09           C  
ANISOU 3387  CG1 VAL A 517     4759   4337   4615    528    407    567       C  
ATOM   3388  CG2 VAL A 517      -2.488  72.464 -30.457  1.00 27.47           C  
ANISOU 3388  CG2 VAL A 517     3684   3073   3678    479    651    514       C  
ATOM   3389  N   LYS A 518      -5.936  72.390 -33.395  1.00 43.72           N  
ANISOU 3389  N   LYS A 518     5966   5243   5402    827    538    782       N  
ATOM   3390  CA  LYS A 518      -7.313  72.163 -33.827  1.00 39.35           C  
ANISOU 3390  CA  LYS A 518     5431   4777   4743    916    442    831       C  
ATOM   3391  C   LYS A 518      -7.419  71.174 -34.988  1.00 53.30           C  
ANISOU 3391  C   LYS A 518     7245   6601   6406    979    365    860       C  
ATOM   3392  O   LYS A 518      -8.138  70.183 -34.899  1.00 38.92           O  
ANISOU 3392  O   LYS A 518     5378   4884   4528    964    229    831       O  
ATOM   3393  CB  LYS A 518      -7.996  73.480 -34.198  1.00 55.43           C  
ANISOU 3393  CB  LYS A 518     7530   6768   6763   1021    542    896       C  
ATOM   3394  CG  LYS A 518      -9.506  73.351 -34.341  1.00 49.15           C  
ANISOU 3394  CG  LYS A 518     6726   6076   5873   1103    434    928       C  
ATOM   3395  CD  LYS A 518     -10.117  74.583 -34.987  1.00 59.85           C  
ANISOU 3395  CD  LYS A 518     8162   7390   7186   1241    536   1007       C  
ATOM   3396  CE  LYS A 518      -9.562  75.849 -34.373  1.00 48.08           C  
ANISOU 3396  CE  LYS A 518     6687   5776   5806   1206    698   1006       C  
ATOM   3397  NZ  LYS A 518     -10.495  77.003 -34.514  1.00 89.37           N1+
ANISOU 3397  NZ  LYS A 518    11964  10985  11006   1319    768   1069       N1+
ATOM   3398  N   THR A 519      -6.711  71.448 -36.079  1.00 37.19           N  
ANISOU 3398  N   THR A 519     5293   4494   4345   1045    463    904       N  
ATOM   3399  CA  THR A 519      -6.807  70.590 -37.256  1.00 61.85           C  
ANISOU 3399  CA  THR A 519     8466   7673   7363   1114    401    926       C  
ATOM   3400  C   THR A 519      -6.292  69.195 -36.933  1.00 57.99           C  
ANISOU 3400  C   THR A 519     7911   7236   6885   1010    298    853       C  
ATOM   3401  O   THR A 519      -6.850  68.197 -37.392  1.00 60.78           O  
ANISOU 3401  O   THR A 519     8247   7683   7164   1020    192    819       O  
ATOM   3402  CB  THR A 519      -6.045  71.167 -38.468  1.00 61.30           C  
ANISOU 3402  CB  THR A 519     8513   7509   7270   1208    539    994       C  
ATOM   3403  CG2 THR A 519      -6.124  70.215 -39.650  1.00 55.41           C  
ANISOU 3403  CG2 THR A 519     7806   6835   6414   1271    473    990       C  
ATOM   3404  OG1 THR A 519      -6.624  72.421 -38.845  1.00 56.62           O  
ANISOU 3404  OG1 THR A 519     7989   6872   6652   1322    640   1063       O  
ATOM   3405  N   MET A 520      -5.232  69.133 -36.132  1.00 48.55           N  
ANISOU 3405  N   MET A 520     6677   5980   5790    909    335    819       N  
ATOM   3406  CA  MET A 520      -4.677  67.857 -35.699  1.00 43.33           C  
ANISOU 3406  CA  MET A 520     5960   5361   5144    817    243    760       C  
ATOM   3407  C   MET A 520      -5.695  67.048 -34.906  1.00 56.57           C  
ANISOU 3407  C   MET A 520     7554   7145   6796    763    107    703       C  
ATOM   3408  O   MET A 520      -6.046  65.932 -35.282  1.00 46.65           O  
ANISOU 3408  O   MET A 520     6282   5959   5485    752     19    665       O  
ATOM   3409  CB  MET A 520      -3.428  68.067 -34.843  1.00 41.85           C  
ANISOU 3409  CB  MET A 520     5722   5107   5071    717    314    703       C  
ATOM   3410  CG  MET A 520      -2.900  66.768 -34.237  1.00 42.95           C  
ANISOU 3410  CG  MET A 520     5800   5298   5223    631    215    643       C  
ATOM   3411  SD  MET A 520      -1.377  66.930 -33.284  1.00 56.59           S  
ANISOU 3411  SD  MET A 520     7459   6969   7075    529    285    566       S  
ATOM   3412  CE  MET A 520      -1.983  67.750 -31.824  1.00 44.54           C  
ANISOU 3412  CE  MET A 520     5857   5454   5610    477    281    527       C  
ATOM   3413  N   MET A 521      -6.165  67.626 -33.807  1.00 49.98           N  
ANISOU 3413  N   MET A 521     6668   6311   6011    727    101    695       N  
ATOM   3414  CA  MET A 521      -7.082  66.943 -32.900  1.00 41.70           C  
ANISOU 3414  CA  MET A 521     5538   5348   4956    666     -7    640       C  
ATOM   3415  C   MET A 521      -8.358  66.444 -33.576  1.00 40.04           C  
ANISOU 3415  C   MET A 521     5327   5223   4662    714    -80    630       C  
ATOM   3416  O   MET A 521      -8.932  65.445 -33.159  1.00 45.05           O  
ANISOU 3416  O   MET A 521     5908   5920   5289    655   -166    576       O  
ATOM   3417  CB  MET A 521      -7.425  67.843 -31.714  1.00 30.39           C  
ANISOU 3417  CB  MET A 521     4064   3896   3585    639     13    644       C  
ATOM   3418  CG  MET A 521      -6.226  68.184 -30.844  1.00 46.14           C  
ANISOU 3418  CG  MET A 521     6026   5827   5677    561     81    600       C  
ATOM   3419  SD  MET A 521      -5.378  66.694 -30.294  1.00 58.91           S  
ANISOU 3419  SD  MET A 521     7596   7482   7304    475     -5    540       S  
ATOM   3420  CE  MET A 521      -6.742  65.865 -29.513  1.00 30.61           C  
ANISOU 3420  CE  MET A 521     3956   3996   3677    442   -128    515       C  
ATOM   3421  N   ASN A 522      -8.803  67.136 -34.617  1.00 38.54           N  
ANISOU 3421  N   ASN A 522     5201   5031   4413    824    -39    683       N  
ATOM   3422  CA  ASN A 522     -10.026  66.740 -35.311  1.00 49.36           C  
ANISOU 3422  CA  ASN A 522     6568   6488   5700    886   -111    673       C  
ATOM   3423  C   ASN A 522      -9.863  65.453 -36.102  1.00 44.55           C  
ANISOU 3423  C   ASN A 522     5967   5917   5043    876   -174    633       C  
ATOM   3424  O   ASN A 522     -10.830  64.724 -36.309  1.00 69.18           O  
ANISOU 3424  O   ASN A 522     9053   9113   8120    878   -259    594       O  
ATOM   3425  CB  ASN A 522     -10.526  67.857 -36.225  1.00 49.62           C  
ANISOU 3425  CB  ASN A 522     6671   6513   5669   1027    -51    743       C  
ATOM   3426  CG  ASN A 522     -10.908  69.103 -35.461  1.00 46.24           C  
ANISOU 3426  CG  ASN A 522     6235   6049   5286   1044      8    782       C  
ATOM   3427  ND2 ASN A 522     -10.665  70.258 -36.065  1.00 53.48           N  
ANISOU 3427  ND2 ASN A 522     7235   6896   6189   1146    119    858       N  
ATOM   3428  OD1 ASN A 522     -11.416  69.034 -34.339  1.00 96.97           O  
ANISOU 3428  OD1 ASN A 522    12584  12501  11758    970    -37    746       O  
ATOM   3429  N   THR A 523      -8.642  65.178 -36.553  1.00 51.92           N  
ANISOU 3429  N   THR A 523     6946   6795   5987    866   -129    643       N  
ATOM   3430  CA  THR A 523      -8.355  63.915 -37.228  1.00 59.32           C  
ANISOU 3430  CA  THR A 523     7893   7758   6887    849   -183    605       C  
ATOM   3431  C   THR A 523      -8.599  62.757 -36.264  1.00 39.17           C  
ANISOU 3431  C   THR A 523     5262   5240   4380    732   -263    534       C  
ATOM   3432  O   THR A 523      -8.996  61.669 -36.672  1.00 58.67           O  
ANISOU 3432  O   THR A 523     7722   7752   6817    718   -330    493       O  
ATOM   3433  CB  THR A 523      -6.904  63.849 -37.743  1.00 41.27           C  
ANISOU 3433  CB  THR A 523     5665   5400   4616    851   -112    629       C  
ATOM   3434  CG2 THR A 523      -6.628  64.983 -38.719  1.00 31.82           C  
ANISOU 3434  CG2 THR A 523     4559   4151   3379    968    -11    707       C  
ATOM   3435  OG1 THR A 523      -5.993  63.944 -36.641  1.00 49.30           O  
ANISOU 3435  OG1 THR A 523     6642   6365   5724    759    -80    616       O  
ATOM   3436  N   TRP A 524      -8.370  63.012 -34.978  1.00 29.30           N  
ANISOU 3436  N   TRP A 524     3961   3967   3204    654   -250    521       N  
ATOM   3437  CA  TRP A 524      -8.539  62.003 -33.940  1.00 31.13           C  
ANISOU 3437  CA  TRP A 524     4129   4219   3480    551   -307    464       C  
ATOM   3438  C   TRP A 524      -9.951  61.991 -33.367  1.00 50.83           C  
ANISOU 3438  C   TRP A 524     6572   6769   5973    536   -358    443       C  
ATOM   3439  O   TRP A 524     -10.391  60.997 -32.789  1.00 53.61           O  
ANISOU 3439  O   TRP A 524     6884   7144   6343    468   -407    399       O  
ATOM   3440  CB  TRP A 524      -7.545  62.250 -32.807  1.00 23.78           C  
ANISOU 3440  CB  TRP A 524     3172   3242   2621    484   -271    459       C  
ATOM   3441  CG  TRP A 524      -6.107  62.132 -33.200  1.00 29.46           C  
ANISOU 3441  CG  TRP A 524     3929   3911   3354    485   -227    470       C  
ATOM   3442  CD1 TRP A 524      -5.259  63.149 -33.525  1.00 51.96           C  
ANISOU 3442  CD1 TRP A 524     6818   6702   6221    529   -146    518       C  
ATOM   3443  CD2 TRP A 524      -5.342  60.926 -33.297  1.00 37.62           C  
ANISOU 3443  CD2 TRP A 524     4965   4940   4391    442   -252    437       C  
ATOM   3444  CE2 TRP A 524      -4.039  61.289 -33.688  1.00 50.16           C  
ANISOU 3444  CE2 TRP A 524     6589   6475   5994    463   -191    464       C  
ATOM   3445  CE3 TRP A 524      -5.634  59.572 -33.095  1.00 33.82           C  
ANISOU 3445  CE3 TRP A 524     4463   4485   3904    390   -311    392       C  
ATOM   3446  NE1 TRP A 524      -4.014  62.652 -33.821  1.00 57.62           N  
ANISOU 3446  NE1 TRP A 524     7558   7383   6952    513   -123    514       N  
ATOM   3447  CZ2 TRP A 524      -3.031  60.350 -33.877  1.00 47.43           C  
ANISOU 3447  CZ2 TRP A 524     6255   6115   5653    437   -197    444       C  
ATOM   3448  CZ3 TRP A 524      -4.631  58.643 -33.282  1.00 35.35           C  
ANISOU 3448  CZ3 TRP A 524     4673   4657   4101    366   -312    375       C  
ATOM   3449  CH2 TRP A 524      -3.346  59.035 -33.669  1.00 47.65           C  
ANISOU 3449  CH2 TRP A 524     6262   6175   5669    391   -261    399       C  
ATOM   3450  N   THR A 525     -10.657  63.103 -33.524  1.00 67.97           N  
ANISOU 3450  N   THR A 525     8748   8957   8121    604   -338    479       N  
ATOM   3451  CA  THR A 525     -11.983  63.260 -32.939  1.00 24.63           C  
ANISOU 3451  CA  THR A 525     3206   3521   2633    597   -379    463       C  
ATOM   3452  C   THR A 525     -13.090  62.964 -33.946  1.00 50.64           C  
ANISOU 3452  C   THR A 525     6503   6886   5852    669   -436    454       C  
ATOM   3453  O   THR A 525     -14.114  62.376 -33.596  1.00 48.66           O  
ANISOU 3453  O   THR A 525     6199   6688   5602    635   -495    414       O  
ATOM   3454  CB  THR A 525     -12.172  64.676 -32.402  1.00 38.75           C  
ANISOU 3454  CB  THR A 525     4991   5288   4443    633   -327    507       C  
ATOM   3455  CG2 THR A 525     -13.508  64.801 -31.695  1.00102.05           C  
ANISOU 3455  CG2 THR A 525    12948  13359  12465    620   -369    489       C  
ATOM   3456  OG1 THR A 525     -11.119  64.978 -31.481  1.00 59.54           O  
ANISOU 3456  OG1 THR A 525     7618   7861   7144    572   -280    509       O  
ATOM   3457  N   LEU A 526     -12.881  63.371 -35.196  1.00 44.68           N  
ANISOU 3457  N   LEU A 526     5811   6135   5031    772   -416    490       N  
ATOM   3458  CA  LEU A 526     -13.898  63.197 -36.233  1.00 47.80           C  
ANISOU 3458  CA  LEU A 526     6212   6610   5341    863   -474    480       C  
ATOM   3459  C   LEU A 526     -13.698  61.904 -37.013  1.00 50.83           C  
ANISOU 3459  C   LEU A 526     6608   7015   5691    847   -528    436       C  
ATOM   3460  O   LEU A 526     -14.485  61.576 -37.897  1.00 43.58           O  
ANISOU 3460  O   LEU A 526     5688   6170   4699    916   -589    414       O  
ATOM   3461  CB  LEU A 526     -13.908  64.394 -37.191  1.00 39.29           C  
ANISOU 3461  CB  LEU A 526     5204   5531   4194   1007   -422    549       C  
ATOM   3462  CG  LEU A 526     -14.622  65.690 -36.780  1.00 40.76           C  
ANISOU 3462  CG  LEU A 526     5382   5727   4379   1070   -388    593       C  
ATOM   3463  CD1 LEU A 526     -14.774  65.825 -35.264  1.00 49.30           C  
ANISOU 3463  CD1 LEU A 526     6394   6785   5554    959   -383    573       C  
ATOM   3464  CD2 LEU A 526     -13.887  66.895 -37.363  1.00 30.60           C  
ANISOU 3464  CD2 LEU A 526     4188   4369   3070   1170   -281    678       C  
ATOM   3465  N   GLN A 527     -12.645  61.168 -36.677  1.00 47.75           N  
ANISOU 3465  N   GLN A 527     6227   6565   5351    761   -508    421       N  
ATOM   3466  CA  GLN A 527     -12.350  59.903 -37.342  1.00 45.60           C  
ANISOU 3466  CA  GLN A 527     5971   6302   5054    739   -551    383       C  
ATOM   3467  C   GLN A 527     -12.281  58.733 -36.363  1.00 38.84           C  
ANISOU 3467  C   GLN A 527     5065   5427   4265    613   -579    334       C  
ATOM   3468  O   GLN A 527     -11.577  58.793 -35.349  1.00 51.52           O  
ANISOU 3468  O   GLN A 527     6658   6977   5939    541   -538    341       O  
ATOM   3469  CB  GLN A 527     -11.026  59.998 -38.105  1.00 63.33           C  
ANISOU 3469  CB  GLN A 527     8292   8489   7282    776   -494    418       C  
ATOM   3470  CG  GLN A 527     -11.142  60.436 -39.551  1.00 53.87           C  
ANISOU 3470  CG  GLN A 527     7163   7321   5986    911   -490    451       C  
ATOM   3471  CD  GLN A 527      -9.788  60.695 -40.184  1.00 77.57           C  
ANISOU 3471  CD  GLN A 527    10244  10250   8978    946   -412    496       C  
ATOM   3472  NE2 GLN A 527      -9.694  60.488 -41.494  1.00 90.95           N  
ANISOU 3472  NE2 GLN A 527    12004  11967  10586   1040   -420    508       N  
ATOM   3473  OE1 GLN A 527      -8.838  61.081 -39.504  1.00 72.99           O  
ANISOU 3473  OE1 GLN A 527     9666   9600   8466    892   -346    519       O  
ATOM   3474  N   ARG A 528     -13.000  57.662 -36.683  1.00 33.97           N  
ANISOU 3474  N   ARG A 528     4423   4858   3625    594   -648    284       N  
ATOM   3475  CA  ARG A 528     -12.898  56.430 -35.914  1.00 59.08           C  
ANISOU 3475  CA  ARG A 528     7574   8014   6859    487   -668    245       C  
ATOM   3476  C   ARG A 528     -11.552  55.771 -36.197  1.00 37.57           C  
ANISOU 3476  C   ARG A 528     4902   5228   4144    462   -638    252       C  
ATOM   3477  O   ARG A 528     -10.933  56.015 -37.227  1.00 71.68           O  
ANISOU 3477  O   ARG A 528     9277   9541   8418    530   -622    273       O  
ATOM   3478  CB  ARG A 528     -14.030  55.468 -36.273  1.00 59.75           C  
ANISOU 3478  CB  ARG A 528     7620   8168   6914    475   -747    187       C  
ATOM   3479  CG  ARG A 528     -13.830  54.755 -37.601  1.00 96.10           C  
ANISOU 3479  CG  ARG A 528    12265  12798  11452    522   -787    162       C  
ATOM   3480  CD  ARG A 528     -14.921  53.727 -37.855  1.00109.67           C  
ANISOU 3480  CD  ARG A 528    13933  14587  13150    496   -868     89       C  
ATOM   3481  NE  ARG A 528     -14.590  52.838 -38.967  1.00112.73           N  
ANISOU 3481  NE  ARG A 528    14359  14990  13483    519   -906     56       N  
ATOM   3482  CZ  ARG A 528     -13.865  51.731 -38.845  1.00110.88           C  
ANISOU 3482  CZ  ARG A 528    14152  14700  13275    450   -897     43       C  
ATOM   3483  NH1 ARG A 528     -13.389  51.379 -37.659  1.00 95.22           N1+
ANISOU 3483  NH1 ARG A 528    12163  12648  11367    362   -852     63       N1+
ATOM   3484  NH2 ARG A 528     -13.610  50.978 -39.908  1.00 99.25           N  
ANISOU 3484  NH2 ARG A 528    12717  13246  11747    478   -932     12       N  
ATOM   3485  N   GLY A 529     -11.091  54.940 -35.278  1.00 44.71           N  
ANISOU 3485  N   GLY A 529     5793   6088   5105    374   -627    238       N  
ATOM   3486  CA  GLY A 529      -9.849  54.222 -35.491  1.00 56.88           C  
ANISOU 3486  CA  GLY A 529     7379   7578   6656    353   -604    241       C  
ATOM   3487  C   GLY A 529      -8.601  55.026 -35.195  1.00 50.68           C  
ANISOU 3487  C   GLY A 529     6616   6741   5901    361   -537    276       C  
ATOM   3488  O   GLY A 529      -8.659  56.199 -34.823  1.00 50.38           O  
ANISOU 3488  O   GLY A 529     6563   6703   5877    383   -505    302       O  
ATOM   3489  N   PHE A 530      -7.463  54.365 -35.360  1.00 41.84           N  
ANISOU 3489  N   PHE A 530     5529   5579   4789    344   -518    275       N  
ATOM   3490  CA  PHE A 530      -6.156  54.974 -35.196  1.00 40.67           C  
ANISOU 3490  CA  PHE A 530     5399   5387   4665    352   -460    300       C  
ATOM   3491  C   PHE A 530      -5.230  54.372 -36.254  1.00 45.48           C  
ANISOU 3491  C   PHE A 530     6065   5974   5241    383   -451    304       C  
ATOM   3492  O   PHE A 530      -5.557  53.354 -36.859  1.00 40.34           O  
ANISOU 3492  O   PHE A 530     5435   5337   4557    382   -492    282       O  
ATOM   3493  CB  PHE A 530      -5.621  54.682 -33.799  1.00 37.37           C  
ANISOU 3493  CB  PHE A 530     4945   4944   4310    282   -445    288       C  
ATOM   3494  CG  PHE A 530      -5.478  53.217 -33.509  1.00 49.17           C  
ANISOU 3494  CG  PHE A 530     6445   6425   5811    235   -471    262       C  
ATOM   3495  CD1 PHE A 530      -4.278  52.570 -33.736  1.00 44.26           C  
ANISOU 3495  CD1 PHE A 530     5855   5772   5190    234   -454    261       C  
ATOM   3496  CD2 PHE A 530      -6.550  52.483 -33.032  1.00 34.04           C  
ANISOU 3496  CD2 PHE A 530     4508   4529   3899    196   -509    243       C  
ATOM   3497  CE1 PHE A 530      -4.144  51.221 -33.484  1.00 59.82           C  
ANISOU 3497  CE1 PHE A 530     7839   7728   7162    199   -474    243       C  
ATOM   3498  CE2 PHE A 530      -6.423  51.138 -32.778  1.00 47.00           C  
ANISOU 3498  CE2 PHE A 530     6163   6152   5542    157   -527    227       C  
ATOM   3499  CZ  PHE A 530      -5.220  50.505 -33.004  1.00 49.78           C  
ANISOU 3499  CZ  PHE A 530     6551   6471   5892    161   -509    228       C  
ATOM   3500  N   PRO A 531      -4.075  55.006 -36.496  1.00 48.88           N  
ANISOU 3500  N   PRO A 531     6522   6371   5679    411   -396    331       N  
ATOM   3501  CA  PRO A 531      -3.175  54.533 -37.552  1.00 35.71           C  
ANISOU 3501  CA  PRO A 531     4912   4680   3976    448   -379    340       C  
ATOM   3502  C   PRO A 531      -2.109  53.536 -37.108  1.00 44.38           C  
ANISOU 3502  C   PRO A 531     6010   5747   5105    400   -375    321       C  
ATOM   3503  O   PRO A 531      -1.566  53.646 -36.011  1.00 35.97           O  
ANISOU 3503  O   PRO A 531     4906   4669   4092    356   -359    315       O  
ATOM   3504  CB  PRO A 531      -2.483  55.815 -37.992  1.00 29.62           C  
ANISOU 3504  CB  PRO A 531     4171   3883   3199    507   -310    387       C  
ATOM   3505  CG  PRO A 531      -2.415  56.626 -36.753  1.00 19.19           C  
ANISOU 3505  CG  PRO A 531     2796   2556   1941    466   -288    391       C  
ATOM   3506  CD  PRO A 531      -3.678  56.331 -35.990  1.00 38.43           C  
ANISOU 3506  CD  PRO A 531     5183   5032   4387    424   -344    361       C  
ATOM   3507  N   LEU A 532      -1.811  52.573 -37.975  1.00 40.50           N  
ANISOU 3507  N   LEU A 532     5565   5248   4577    416   -390    312       N  
ATOM   3508  CA  LEU A 532      -0.584  51.796 -37.858  1.00 29.52           C  
ANISOU 3508  CA  LEU A 532     4191   3824   3203    396   -371    306       C  
ATOM   3509  C   LEU A 532       0.536  52.616 -38.485  1.00 50.85           C  
ANISOU 3509  C   LEU A 532     6924   6498   5898    446   -308    342       C  
ATOM   3510  O   LEU A 532       0.373  53.184 -39.567  1.00 40.63           O  
ANISOU 3510  O   LEU A 532     5678   5203   4557    510   -285    369       O  
ATOM   3511  CB  LEU A 532      -0.711  50.459 -38.583  1.00 46.62           C  
ANISOU 3511  CB  LEU A 532     6398   5987   5328    396   -409    286       C  
ATOM   3512  CG  LEU A 532       0.604  49.764 -38.958  1.00 34.69           C  
ANISOU 3512  CG  LEU A 532     4927   4442   3812    406   -381    290       C  
ATOM   3513  CD1 LEU A 532       1.446  49.483 -37.724  1.00 18.02           C  
ANISOU 3513  CD1 LEU A 532     2776   2316   1756    361   -366    281       C  
ATOM   3514  CD2 LEU A 532       0.342  48.479 -39.741  1.00 32.17           C  
ANISOU 3514  CD2 LEU A 532     4656   4121   3446    409   -420    270       C  
ATOM   3515  N   ILE A 533       1.673  52.685 -37.802  1.00 38.32           N  
ANISOU 3515  N   ILE A 533     5315   4889   4355    423   -275    344       N  
ATOM   3516  CA  ILE A 533       2.786  53.494 -38.273  1.00 29.95           C  
ANISOU 3516  CA  ILE A 533     4280   3796   3302    463   -206    381       C  
ATOM   3517  C   ILE A 533       4.016  52.642 -38.545  1.00 53.42           C  
ANISOU 3517  C   ILE A 533     7277   6746   6275    465   -189    377       C  
ATOM   3518  O   ILE A 533       4.598  52.055 -37.633  1.00 49.17           O  
ANISOU 3518  O   ILE A 533     6700   6213   5770    427   -207    354       O  
ATOM   3519  CB  ILE A 533       3.095  54.648 -37.292  1.00 48.05           C  
ANISOU 3519  CB  ILE A 533     6522   6083   5653    446   -172    395       C  
ATOM   3520  CG1 ILE A 533       2.141  55.812 -37.561  1.00 44.32           C  
ANISOU 3520  CG1 ILE A 533     6057   5613   5168    477   -152    423       C  
ATOM   3521  CG2 ILE A 533       4.542  55.108 -37.413  1.00  7.68           C  
ANISOU 3521  CG2 ILE A 533     1419    925    574    464   -103    424       C  
ATOM   3522  CD1 ILE A 533       2.273  56.933 -36.599  1.00 35.38           C  
ANISOU 3522  CD1 ILE A 533     4880   4471   4093    459   -121    437       C  
ATOM   3523  N   THR A 534       4.395  52.569 -39.815  1.00 61.83           N  
ANISOU 3523  N   THR A 534     8410   7786   7297    518   -155    402       N  
ATOM   3524  CA  THR A 534       5.505  51.726 -40.233  1.00 42.19           C  
ANISOU 3524  CA  THR A 534     5953   5275   4802    527   -136    402       C  
ATOM   3525  C   THR A 534       6.787  52.535 -40.395  1.00 38.10           C  
ANISOU 3525  C   THR A 534     5444   4712   4320    552    -51    442       C  
ATOM   3526  O   THR A 534       6.795  53.581 -41.029  1.00 30.58           O  
ANISOU 3526  O   THR A 534     4526   3727   3366    593     15    484       O  
ATOM   3527  CB  THR A 534       5.179  50.998 -41.542  1.00 42.96           C  
ANISOU 3527  CB  THR A 534     6126   5369   4829    569   -150    402       C  
ATOM   3528  CG2 THR A 534       6.317  50.076 -41.927  1.00 47.85           C  
ANISOU 3528  CG2 THR A 534     6779   5962   5441    577   -131    402       C  
ATOM   3529  OG1 THR A 534       3.986  50.222 -41.374  1.00 64.87           O  
ANISOU 3529  OG1 THR A 534     8889   8177   7580    541   -227    366       O  
ATOM   3530  N   ILE A 535       7.872  52.039 -39.811  1.00 37.22           N  
ANISOU 3530  N   ILE A 535     5303   4593   4247    531    -46    432       N  
ATOM   3531  CA  ILE A 535       9.151  52.737 -39.852  1.00 37.52           C  
ANISOU 3531  CA  ILE A 535     5328   4582   4345    544     40    452       C  
ATOM   3532  C   ILE A 535      10.182  52.035 -40.726  1.00 41.50           C  
ANISOU 3532  C   ILE A 535     5877   5054   4835    573     82    456       C  
ATOM   3533  O   ILE A 535      10.646  50.941 -40.405  1.00 54.91           O  
ANISOU 3533  O   ILE A 535     7565   6774   6523    563     38    434       O  
ATOM   3534  CB  ILE A 535       9.747  52.905 -38.450  1.00 36.27           C  
ANISOU 3534  CB  ILE A 535     5067   4448   4267    495     31    398       C  
ATOM   3535  CG1 ILE A 535       8.838  53.785 -37.590  1.00 42.42           C  
ANISOU 3535  CG1 ILE A 535     5799   5249   5070    467      8    392       C  
ATOM   3536  CG2 ILE A 535      11.169  53.463 -38.542  1.00 19.73           C  
ANISOU 3536  CG2 ILE A 535     2928   2313   2256    492    132    366       C  
ATOM   3537  CD1 ILE A 535       8.334  55.026 -38.303  1.00 21.70           C  
ANISOU 3537  CD1 ILE A 535     3211   2584   2450    492     78    429       C  
ATOM   3538  N   THR A 536      10.551  52.684 -41.825  1.00 57.89           N  
ANISOU 3538  N   THR A 536     8008   7077   6910    614    176    488       N  
ATOM   3539  CA  THR A 536      11.565  52.153 -42.721  1.00 52.84           C  
ANISOU 3539  CA  THR A 536     7414   6400   6263    645    233    494       C  
ATOM   3540  C   THR A 536      12.813  53.011 -42.657  1.00 27.66           C  
ANISOU 3540  C   THR A 536     4174   3160   3176    633    355    470       C  
ATOM   3541  O   THR A 536      12.749  54.214 -42.877  1.00 58.19           O  
ANISOU 3541  O   THR A 536     8043   6983   7083    639    441    485       O  
ATOM   3542  CB  THR A 536      11.073  52.144 -44.167  1.00 36.05           C  
ANISOU 3542  CB  THR A 536     5401   4248   4047    711    257    549       C  
ATOM   3543  CG2 THR A 536      12.093  51.483 -45.057  1.00 29.01           C  
ANISOU 3543  CG2 THR A 536     4561   3322   3141    743    310    554       C  
ATOM   3544  OG1 THR A 536       9.833  51.433 -44.253  1.00 57.71           O  
ANISOU 3544  OG1 THR A 536     8168   7051   6710    713    151    535       O  
ATOM   3545  N   VAL A 537      13.947  52.393 -42.364  1.00 31.01           N  
ANISOU 3545  N   VAL A 537     4551   3587   3644    617    366    429       N  
ATOM   3546  CA  VAL A 537      15.213  53.113 -42.319  1.00 38.39           C  
ANISOU 3546  CA  VAL A 537     5424   4478   4684    601    482    391       C  
ATOM   3547  C   VAL A 537      16.148  52.748 -43.478  1.00 29.25           C  
ANISOU 3547  C   VAL A 537     4327   3269   3519    641    567    410       C  
ATOM   3548  O   VAL A 537      16.321  51.575 -43.809  1.00 36.42           O  
ANISOU 3548  O   VAL A 537     5274   4196   4366    665    514    418       O  
ATOM   3549  CB  VAL A 537      15.931  52.874 -40.989  1.00 10.31           C  
ANISOU 3549  CB  VAL A 537     1743    972   1201    555    441    314       C  
ATOM   3550  CG1 VAL A 537      17.361  53.399 -41.059  1.00 29.79           C  
ANISOU 3550  CG1 VAL A 537     4140   3402   3775    540    556    260       C  
ATOM   3551  CG2 VAL A 537      15.167  53.527 -39.873  1.00 33.09           C  
ANISOU 3551  CG2 VAL A 537     4566   3896   4112    515    390    291       C  
ATOM   3552  N   ARG A 538      16.751  53.766 -44.081  1.00 42.17           N  
ANISOU 3552  N   ARG A 538     5970   4832   5219    649    708    415       N  
ATOM   3553  CA  ARG A 538      17.684  53.588 -45.190  1.00 42.74           C  
ANISOU 3553  CA  ARG A 538     6098   4845   5296    687    811    434       C  
ATOM   3554  C   ARG A 538      18.867  54.523 -45.008  1.00 35.49           C  
ANISOU 3554  C   ARG A 538     5097   3872   4516    652    953    380       C  
ATOM   3555  O   ARG A 538      18.885  55.615 -45.568  1.00 39.76           O  
ANISOU 3555  O   ARG A 538     5674   4337   5097    662   1081    405       O  
ATOM   3556  CB  ARG A 538      17.001  53.904 -46.522  1.00 15.11           C  
ANISOU 3556  CB  ARG A 538     2738   1295   1707    756    863    517       C  
ATOM   3557  CG  ARG A 538      15.818  53.020 -46.857  1.00 37.08           C  
ANISOU 3557  CG  ARG A 538     5602   4132   4354    794    731    560       C  
ATOM   3558  CD  ARG A 538      16.282  51.593 -47.101  1.00 80.47           C  
ANISOU 3558  CD  ARG A 538    11119   9655   9801    805    669    548       C  
ATOM   3559  NE  ARG A 538      15.176  50.682 -47.361  1.00 48.93           N  
ANISOU 3559  NE  ARG A 538     7192   5711   5688    829    546    572       N  
ATOM   3560  CZ  ARG A 538      15.295  49.361 -47.353  1.00106.05           C  
ANISOU 3560  CZ  ARG A 538    14441  12978  12876    828    469    557       C  
ATOM   3561  NH1 ARG A 538      16.472  48.803 -47.093  1.00154.83           N1+
ANISOU 3561  NH1 ARG A 538    20573  19146  19108    813    498    524       N1+
ATOM   3562  NH2 ARG A 538      14.241  48.597 -47.601  1.00129.41           N  
ANISOU 3562  NH2 ARG A 538    17457  15976  15736    842    367    570       N  
ATOM   3563  N   GLY A 539      19.848  54.101 -44.216  1.00 44.44           N  
ANISOU 3563  N   GLY A 539     6118   5044   5723    613    933    302       N  
ATOM   3564  CA  GLY A 539      20.958  54.967 -43.856  1.00 34.74           C  
ANISOU 3564  CA  GLY A 539     4782   3781   4638    567   1052    226       C  
ATOM   3565  C   GLY A 539      20.554  55.947 -42.769  1.00 36.10           C  
ANISOU 3565  C   GLY A 539     4863   3972   4881    510   1041    176       C  
ATOM   3566  O   GLY A 539      20.052  55.545 -41.721  1.00 53.98           O  
ANISOU 3566  O   GLY A 539     7072   6319   7118    490    910    148       O  
ATOM   3567  N   ARG A 540      20.767  57.236 -43.021  1.00 49.66           N  
ANISOU 3567  N   ARG A 540     6571   5608   6689    486   1188    165       N  
ATOM   3568  CA  ARG A 540      20.314  58.278 -42.107  1.00 30.80           C  
ANISOU 3568  CA  ARG A 540     4112   3224   4367    434   1195    123       C  
ATOM   3569  C   ARG A 540      18.863  58.632 -42.419  1.00 41.03           C  
ANISOU 3569  C   ARG A 540     5517   4505   5566    470   1157    216       C  
ATOM   3570  O   ARG A 540      18.218  59.398 -41.696  1.00 38.96           O  
ANISOU 3570  O   ARG A 540     5219   4252   5332    439   1142    200       O  
ATOM   3571  CB  ARG A 540      21.203  59.517 -42.223  1.00 46.80           C  
ANISOU 3571  CB  ARG A 540     6077   5161   6543    388   1382     62       C  
ATOM   3572  CG  ARG A 540      22.680  59.239 -41.977  1.00 25.37           C  
ANISOU 3572  CG  ARG A 540     3242   2461   3935    352   1430    -42       C  
ATOM   3573  CD  ARG A 540      23.417  60.496 -41.536  1.00 44.85           C  
ANISOU 3573  CD  ARG A 540     5595   4873   6571    278   1575   -145       C  
ATOM   3574  NE  ARG A 540      24.137  61.150 -42.627  1.00 49.31           N  
ANISOU 3574  NE  ARG A 540     6208   5312   7215    280   1783   -130       N  
ATOM   3575  CZ  ARG A 540      24.098  62.455 -42.882  1.00 45.79           C  
ANISOU 3575  CZ  ARG A 540     5780   4757   6860    249   1952   -132       C  
ATOM   3576  NH1 ARG A 540      23.366  63.272 -42.134  1.00 34.98           N1+
ANISOU 3576  NH1 ARG A 540     4383   3391   5516    214   1935   -150       N1+
ATOM   3577  NH2 ARG A 540      24.791  62.943 -43.894  1.00 70.04           N  
ANISOU 3577  NH2 ARG A 540     8903   7710   9998    258   2148   -113       N  
ATOM   3578  N   ASN A 541      18.353  58.052 -43.497  1.00 31.29           N  
ANISOU 3578  N   ASN A 541     4416   3256   4217    540   1139    308       N  
ATOM   3579  CA  ASN A 541      16.996  58.320 -43.938  1.00 33.45           C  
ANISOU 3579  CA  ASN A 541     4796   3525   4389    588   1101    394       C  
ATOM   3580  C   ASN A 541      15.975  57.459 -43.219  1.00 46.05           C  
ANISOU 3580  C   ASN A 541     6381   5221   5894    584    913    400       C  
ATOM   3581  O   ASN A 541      15.894  56.255 -43.447  1.00 27.04           O  
ANISOU 3581  O   ASN A 541     4007   2861   3406    608    818    415       O  
ATOM   3582  CB  ASN A 541      16.895  58.115 -45.442  1.00 27.66           C  
ANISOU 3582  CB  ASN A 541     4206   2736   3566    671   1165    481       C  
ATOM   3583  CG  ASN A 541      17.948  58.881 -46.191  1.00 35.30           C  
ANISOU 3583  CG  ASN A 541     5194   3598   4622    678   1362    480       C  
ATOM   3584  ND2 ASN A 541      19.075  58.234 -46.463  1.00 39.71           N  
ANISOU 3584  ND2 ASN A 541     5724   4147   5216    670   1397    445       N  
ATOM   3585  OD1 ASN A 541      17.763  60.049 -46.508  1.00 48.01           O  
ANISOU 3585  OD1 ASN A 541     6843   5129   6269    692   1490    510       O  
ATOM   3586  N   VAL A 542      15.203  58.087 -42.342  1.00 43.67           N  
ANISOU 3586  N   VAL A 542     6034   4947   5612    552    870    385       N  
ATOM   3587  CA  VAL A 542      14.147  57.399 -41.624  1.00 33.46           C  
ANISOU 3587  CA  VAL A 542     4731   3740   4241    546    708    392       C  
ATOM   3588  C   VAL A 542      12.820  57.696 -42.292  1.00 44.17           C  
ANISOU 3588  C   VAL A 542     6190   5092   5502    600    684    472       C  
ATOM   3589  O   VAL A 542      12.450  58.853 -42.471  1.00 30.92           O  
ANISOU 3589  O   VAL A 542     4535   3364   3850    613    768    497       O  
ATOM   3590  CB  VAL A 542      14.083  57.845 -40.163  1.00 35.17           C  
ANISOU 3590  CB  VAL A 542     4828   4001   4533    480    664    322       C  
ATOM   3591  CG1 VAL A 542      12.960  57.123 -39.451  1.00 21.91           C  
ANISOU 3591  CG1 VAL A 542     3148   2405   2773    477    508    335       C  
ATOM   3592  CG2 VAL A 542      15.413  57.587 -39.475  1.00 30.81           C  
ANISOU 3592  CG2 VAL A 542     4164   3469   4072    436    681    231       C  
ATOM   3593  N   HIS A 543      12.110  56.645 -42.676  1.00 30.36           N  
ANISOU 3593  N   HIS A 543     4501   3392   3641    634    574    507       N  
ATOM   3594  CA  HIS A 543      10.840  56.807 -43.367  1.00 32.61           C  
ANISOU 3594  CA  HIS A 543     4877   3689   3825    692    537    572       C  
ATOM   3595  C   HIS A 543       9.694  56.458 -42.441  1.00 60.26           C  
ANISOU 3595  C   HIS A 543     8338   7269   7291    662    401    558       C  
ATOM   3596  O   HIS A 543       9.705  55.412 -41.791  1.00 53.08           O  
ANISOU 3596  O   HIS A 543     7386   6412   6369    626    302    524       O  
ATOM   3597  CB  HIS A 543      10.785  55.931 -44.616  1.00 32.24           C  
ANISOU 3597  CB  HIS A 543     4932   3642   3674    757    518    614       C  
ATOM   3598  CG  HIS A 543      11.880  56.208 -45.598  1.00 68.46           C  
ANISOU 3598  CG  HIS A 543     9572   8152   8288    794    655    634       C  
ATOM   3599  CD2 HIS A 543      13.148  55.743 -45.673  1.00 65.00           C  
ANISOU 3599  CD2 HIS A 543     9106   7686   7905    772    708    601       C  
ATOM   3600  ND1 HIS A 543      11.724  57.066 -46.666  1.00 68.65           N  
ANISOU 3600  ND1 HIS A 543     9691   8115   8279    868    764    695       N  
ATOM   3601  CE1 HIS A 543      12.849  57.116 -47.356  1.00 69.84           C  
ANISOU 3601  CE1 HIS A 543     9872   8197   8466    886    883    700       C  
ATOM   3602  NE2 HIS A 543      13.729  56.323 -46.775  1.00 71.69           N  
ANISOU 3602  NE2 HIS A 543    10029   8452   8758    826    850    641       N  
ATOM   3603  N   MET A 544       8.712  57.347 -42.375  1.00 25.47           N  
ANISOU 3603  N   MET A 544     3945   2863   2869    681    404    587       N  
ATOM   3604  CA  MET A 544       7.490  57.057 -41.651  1.00 47.02           C  
ANISOU 3604  CA  MET A 544     6646   5664   5556    661    281    580       C  
ATOM   3605  C   MET A 544       6.345  56.927 -42.641  1.00 37.85           C  
ANISOU 3605  C   MET A 544     5564   4534   4285    730    239    619       C  
ATOM   3606  O   MET A 544       6.362  57.538 -43.704  1.00 40.86           O  
ANISOU 3606  O   MET A 544     6024   4872   4629    803    319    667       O  
ATOM   3607  CB  MET A 544       7.199  58.128 -40.592  1.00 24.85           C  
ANISOU 3607  CB  MET A 544     3765   2853   2825    619    304    559       C  
ATOM   3608  CG  MET A 544       7.628  59.531 -40.971  1.00 84.34           C  
ANISOU 3608  CG  MET A 544    11318  10306  10422    641    453    579       C  
ATOM   3609  SD  MET A 544       9.135  60.041 -40.128  1.00 84.42           S  
ANISOU 3609  SD  MET A 544    11226  10267  10581    564    552    502       S  
ATOM   3610  CE  MET A 544       8.708  59.670 -38.440  1.00 38.49           C  
ANISOU 3610  CE  MET A 544     5296   4535   4792    490    424    438       C  
ATOM   3611  N   LYS A 545       5.367  56.099 -42.292  1.00 36.48           N  
ANISOU 3611  N   LYS A 545     5356   4437   4067    704    123    571       N  
ATOM   3612  CA  LYS A 545       4.169  55.912 -43.095  1.00 35.17           C  
ANISOU 3612  CA  LYS A 545     5233   4316   3816    756     72    568       C  
ATOM   3613  C   LYS A 545       3.010  55.571 -42.165  1.00 61.36           C  
ANISOU 3613  C   LYS A 545     8478   7697   7139    702    -28    521       C  
ATOM   3614  O   LYS A 545       3.196  54.920 -41.136  1.00 64.12           O  
ANISOU 3614  O   LYS A 545     8765   8063   7535    629    -75    480       O  
ATOM   3615  CB  LYS A 545       4.369  54.788 -44.116  1.00 29.29           C  
ANISOU 3615  CB  LYS A 545     4545   3579   3003    787     44    556       C  
ATOM   3616  CG  LYS A 545       3.114  54.446 -44.911  1.00 40.35           C  
ANISOU 3616  CG  LYS A 545     5983   5033   4317    838    -25    542       C  
ATOM   3617  CD  LYS A 545       3.109  52.993 -45.363  1.00 44.11           C  
ANISOU 3617  CD  LYS A 545     6478   5531   4752    825    -93    501       C  
ATOM   3618  CE  LYS A 545       1.805  52.650 -46.072  1.00 70.77           C  
ANISOU 3618  CE  LYS A 545     9878   8964   8046    870   -170    480       C  
ATOM   3619  NZ  LYS A 545       1.652  51.183 -46.297  1.00 77.37           N1+
ANISOU 3619  NZ  LYS A 545    10720   9821   8856    837   -243    431       N1+
ATOM   3620  N   GLN A 546       1.813  56.015 -42.522  1.00 26.97           N  
ANISOU 3620  N   GLN A 546     4136   3376   2736    745    -56    528       N  
ATOM   3621  CA  GLN A 546       0.641  55.697 -41.719  1.00 53.47           C  
ANISOU 3621  CA  GLN A 546     7427   6787   6099    697   -143    485       C  
ATOM   3622  C   GLN A 546      -0.453  55.040 -42.549  1.00 45.82           C  
ANISOU 3622  C   GLN A 546     6487   5870   5054    736   -215    463       C  
ATOM   3623  O   GLN A 546      -0.502  55.189 -43.768  1.00 38.54           O  
ANISOU 3623  O   GLN A 546     5635   4948   4058    822   -196    490       O  
ATOM   3624  CB  GLN A 546       0.100  56.950 -41.031  1.00 54.83           C  
ANISOU 3624  CB  GLN A 546     7565   6963   6306    698   -118    507       C  
ATOM   3625  CG  GLN A 546      -0.228  58.086 -41.979  1.00 41.22           C  
ANISOU 3625  CG  GLN A 546     5907   5224   4531    799    -55    565       C  
ATOM   3626  CD  GLN A 546      -1.420  58.896 -41.514  1.00 56.80           C  
ANISOU 3626  CD  GLN A 546     7846   7233   6501    813    -78    571       C  
ATOM   3627  NE2 GLN A 546      -1.193  60.177 -41.234  1.00 18.79           N  
ANISOU 3627  NE2 GLN A 546     3042   2375   1724    836      6    619       N  
ATOM   3628  OE1 GLN A 546      -2.535  58.378 -41.410  1.00 61.87           O  
ANISOU 3628  OE1 GLN A 546     8455   7938   7113    803   -164    534       O  
ATOM   3629  N   GLU A 547      -1.330  54.308 -41.878  1.00 36.94           N  
ANISOU 3629  N   GLU A 547     5306   4786   3945    676   -294    415       N  
ATOM   3630  CA  GLU A 547      -2.459  53.677 -42.543  1.00 43.26           C  
ANISOU 3630  CA  GLU A 547     6117   5638   4680    703   -368    387       C  
ATOM   3631  C   GLU A 547      -3.470  53.247 -41.495  1.00 52.54           C  
ANISOU 3631  C   GLU A 547     7218   6849   5896    628   -431    345       C  
ATOM   3632  O   GLU A 547      -3.094  52.760 -40.432  1.00 48.65           O  
ANISOU 3632  O   GLU A 547     6683   6333   5469    547   -431    327       O  
ATOM   3633  CB  GLU A 547      -1.990  52.478 -43.368  1.00 27.95           C  
ANISOU 3633  CB  GLU A 547     4227   3691   2700    710   -391    367       C  
ATOM   3634  CG  GLU A 547      -1.359  51.367 -42.542  1.00 85.55           C  
ANISOU 3634  CG  GLU A 547    11493  10957  10055    620   -404    336       C  
ATOM   3635  CD  GLU A 547      -0.449  50.465 -43.360  1.00111.85           C  
ANISOU 3635  CD  GLU A 547    14886  14259  13353    638   -392    334       C  
ATOM   3636  OE1 GLU A 547       0.781  50.516 -43.144  1.00123.19           O  
ANISOU 3636  OE1 GLU A 547    16331  15651  14825    627   -335    353       O  
ATOM   3637  OE2 GLU A 547      -0.958  49.711 -44.215  1.00 88.66           O1-
ANISOU 3637  OE2 GLU A 547    11986  11349  10354    664   -441    312       O1-
ATOM   3638  N   HIS A 548      -4.751  53.442 -41.783  1.00 48.80           N  
ANISOU 3638  N   HIS A 548     6729   6432   5380    661   -482    332       N  
ATOM   3639  CA  HIS A 548      -5.800  53.046 -40.850  1.00 55.06           C  
ANISOU 3639  CA  HIS A 548     7452   7260   6209    594   -538    294       C  
ATOM   3640  C   HIS A 548      -5.672  51.573 -40.476  1.00 58.90           C  
ANISOU 3640  C   HIS A 548     7927   7731   6721    516   -574    254       C  
ATOM   3641  O   HIS A 548      -5.835  50.686 -41.316  1.00 46.75           O  
ANISOU 3641  O   HIS A 548     6420   6211   5132    532   -615    228       O  
ATOM   3642  CB  HIS A 548      -7.191  53.327 -41.426  1.00 54.07           C  
ANISOU 3642  CB  HIS A 548     7312   7210   6021    651   -596    278       C  
ATOM   3643  CG  HIS A 548      -8.311  52.975 -40.494  1.00 60.36           C  
ANISOU 3643  CG  HIS A 548     8034   8043   6855    584   -647    240       C  
ATOM   3644  CD2 HIS A 548      -8.307  52.363 -39.285  1.00 73.46           C  
ANISOU 3644  CD2 HIS A 548     9649   9674   8587    484   -648    221       C  
ATOM   3645  ND1 HIS A 548      -9.629  53.257 -40.774  1.00 58.97           N  
ANISOU 3645  ND1 HIS A 548     7824   7943   6637    624   -703    217       N  
ATOM   3646  CE1 HIS A 548     -10.390  52.834 -39.780  1.00 41.68           C  
ANISOU 3646  CE1 HIS A 548     5569   5768   4498    545   -733    184       C  
ATOM   3647  NE2 HIS A 548      -9.612  52.287 -38.864  1.00 68.78           N  
ANISOU 3647  NE2 HIS A 548     8999   9135   7998    462   -698    190       N  
ATOM   3648  N   TYR A 549      -5.382  51.328 -39.202  1.00 28.16           N  
ANISOU 3648  N   TYR A 549     3993   3806   2900    437   -557    249       N  
ATOM   3649  CA  TYR A 549      -5.215  49.976 -38.685  1.00 35.53           C  
ANISOU 3649  CA  TYR A 549     4923   4718   3860    368   -579    221       C  
ATOM   3650  C   TYR A 549      -6.563  49.370 -38.349  1.00 43.12           C  
ANISOU 3650  C   TYR A 549     5845   5721   4818    328   -639    185       C  
ATOM   3651  O   TYR A 549      -7.311  49.903 -37.527  1.00 67.33           O  
ANISOU 3651  O   TYR A 549     8861   8807   7916    304   -642    185       O  
ATOM   3652  CB  TYR A 549      -4.339  50.011 -37.438  1.00 30.68           C  
ANISOU 3652  CB  TYR A 549     4284   4059   3314    316   -535    233       C  
ATOM   3653  CG  TYR A 549      -4.123  48.675 -36.763  1.00 33.22           C  
ANISOU 3653  CG  TYR A 549     4608   4356   3658    257   -548    214       C  
ATOM   3654  CD1 TYR A 549      -2.990  47.923 -37.025  1.00 59.69           C  
ANISOU 3654  CD1 TYR A 549     8003   7672   7005    261   -529    216       C  
ATOM   3655  CD2 TYR A 549      -5.033  48.185 -35.840  1.00 41.70           C  
ANISOU 3655  CD2 TYR A 549     5647   5442   4755    204   -575    197       C  
ATOM   3656  CE1 TYR A 549      -2.777  46.712 -36.400  1.00 35.93           C  
ANISOU 3656  CE1 TYR A 549     5005   4639   4009    218   -537    205       C  
ATOM   3657  CE2 TYR A 549      -4.826  46.975 -35.213  1.00 56.27           C  
ANISOU 3657  CE2 TYR A 549     7506   7262   6613    158   -580    188       C  
ATOM   3658  CZ  TYR A 549      -3.695  46.246 -35.496  1.00 42.63           C  
ANISOU 3658  CZ  TYR A 549     5824   5497   4875    168   -561    192       C  
ATOM   3659  OH  TYR A 549      -3.476  45.040 -34.875  1.00 45.29           O  
ANISOU 3659  OH  TYR A 549     6184   5808   5216    134   -562    188       O  
ATOM   3660  N   MET A 550      -6.864  48.250 -38.988  1.00 33.22           N  
ANISOU 3660  N   MET A 550     4615   4483   3525    319   -684    151       N  
ATOM   3661  CA  MET A 550      -8.119  47.553 -38.750  1.00 66.41           C  
ANISOU 3661  CA  MET A 550     8780   8731   7723    275   -743    105       C  
ATOM   3662  C   MET A 550      -7.959  46.070 -39.063  1.00 84.25           C  
ANISOU 3662  C   MET A 550    11074  10976   9960    235   -771     69       C  
ATOM   3663  O   MET A 550      -7.205  45.693 -39.961  1.00 64.80           O  
ANISOU 3663  O   MET A 550     8667   8495   7457    270   -766     72       O  
ATOM   3664  CB  MET A 550      -9.230  48.165 -39.597  1.00 66.23           C  
ANISOU 3664  CB  MET A 550     8732   8788   7646    333   -794     79       C  
ATOM   3665  CG  MET A 550      -8.856  48.294 -41.060  1.00103.55           C  
ANISOU 3665  CG  MET A 550    13514  13535  12295    419   -806     80       C  
ATOM   3666  SD  MET A 550      -9.710  49.633 -41.904  1.00138.80           S  
ANISOU 3666  SD  MET A 550    17965  18079  16693    529   -831     87       S  
ATOM   3667  CE  MET A 550      -8.752  49.715 -43.412  1.00 64.55           C  
ANISOU 3667  CE  MET A 550     8655   8664   7206    629   -813    111       C  
ATOM   3668  N   LYS A 551      -8.668  45.235 -38.309  1.00108.41           N  
ANISOU 3668  N   LYS A 551    14104  14043  13044    163   -796     35       N  
ATOM   3669  CA  LYS A 551      -8.576  43.787 -38.451  1.00119.29           C  
ANISOU 3669  CA  LYS A 551    15517  15404  14402    113   -816     -4       C  
ATOM   3670  C   LYS A 551      -8.576  43.351 -39.912  1.00124.91           C  
ANISOU 3670  C   LYS A 551    16267  16149  15043    153   -858    -47       C  
ATOM   3671  O   LYS A 551      -9.137  42.311 -40.256  1.00121.96           O  
ANISOU 3671  O   LYS A 551    15896  15801  14643    109   -901   -118       O  
ATOM   3672  CB  LYS A 551      -9.726  43.116 -37.705  1.00117.05           C  
ANISOU 3672  CB  LYS A 551    15186  15147  14140     33   -849    -58       C  
ATOM   3673  CG  LYS A 551      -9.827  43.545 -36.255  1.00134.62           C  
ANISOU 3673  CG  LYS A 551    17377  17347  16426     -1   -811    -17       C  
ATOM   3674  CD  LYS A 551      -8.583  43.140 -35.489  1.00127.13           C  
ANISOU 3674  CD  LYS A 551    16480  16323  15500     -9   -755     37       C  
ATOM   3675  CE  LYS A 551      -8.464  41.629 -35.431  1.00143.10           C  
ANISOU 3675  CE  LYS A 551    18555  18319  17498    -62   -762      2       C  
ATOM   3676  NZ  LYS A 551      -7.125  41.197 -34.951  1.00136.67           N1+
ANISOU 3676  NZ  LYS A 551    17802  17439  16687    -45   -711     56       N1+
TER    3677      LYS A 551 
ATOM   3678  N   ALA A 556     -10.632  43.262 -48.774  1.00143.97           N  
ANISOU 3678  N   ALA A 556    18807  19016  16879    632  -1211   -363       N  
ATOM   3679  CA  ALA A 556     -11.523  43.898 -47.809  1.00144.79           C  
ANISOU 3679  CA  ALA A 556    18820  19147  17045    598  -1220   -361       C  
ATOM   3680  C   ALA A 556     -10.936  45.182 -47.209  1.00170.90           C  
ANISOU 3680  C   ALA A 556    22145  22395  20394    642  -1142   -240       C  
ATOM   3681  O   ALA A 556     -11.612  46.210 -47.162  1.00135.14           O  
ANISOU 3681  O   ALA A 556    17575  17921  15851    702  -1155   -224       O  
ATOM   3682  CB  ALA A 556     -11.918  42.911 -46.707  1.00 98.83           C  
ANISOU 3682  CB  ALA A 556    12944  13293  11315    450  -1220   -416       C  
ATOM   3683  N   PRO A 557      -9.671  45.131 -46.752  1.00214.30           N  
ANISOU 3683  N   PRO A 557    27700  27783  25940    612  -1059   -161       N  
ATOM   3684  CA  PRO A 557      -9.053  46.307 -46.127  1.00225.14           C  
ANISOU 3684  CA  PRO A 557    29082  29098  27363    638   -981    -65       C  
ATOM   3685  C   PRO A 557      -8.844  47.445 -47.122  1.00216.30           C  
ANISOU 3685  C   PRO A 557    28011  28006  26167    774   -963    -17       C  
ATOM   3686  O   PRO A 557      -7.982  47.331 -47.991  1.00221.54           O  
ANISOU 3686  O   PRO A 557    28753  28642  26778    831   -936      8       O  
ATOM   3687  CB  PRO A 557      -7.692  45.777 -45.654  1.00229.32           C  
ANISOU 3687  CB  PRO A 557    29662  29521  27948    583   -910    -18       C  
ATOM   3688  CG  PRO A 557      -7.826  44.287 -45.641  1.00227.02           C  
ANISOU 3688  CG  PRO A 557    29375  29227  27655    505   -950    -85       C  
ATOM   3689  CD  PRO A 557      -8.762  43.972 -46.757  1.00224.62           C  
ANISOU 3689  CD  PRO A 557    29063  29021  27262    551  -1034   -168       C  
ATOM   3690  N   ASP A 558      -9.610  48.527 -46.986  1.00195.37           N  
ANISOU 3690  N   ASP A 558    25321  25407  23506    828   -972     -2       N  
ATOM   3691  CA  ASP A 558      -9.525  49.651 -47.918  1.00177.88           C  
ANISOU 3691  CA  ASP A 558    23157  23222  21206    968   -951     47       C  
ATOM   3692  C   ASP A 558     -10.131  50.942 -47.364  1.00132.58           C  
ANISOU 3692  C   ASP A 558    17379  17507  15489   1005   -931     86       C  
ATOM   3693  O   ASP A 558     -11.292  51.248 -47.633  1.00131.11           O  
ANISOU 3693  O   ASP A 558    17147  17417  15250   1061   -997     47       O  
ATOM   3694  CB  ASP A 558     -10.216  49.300 -49.236  1.00205.16           C  
ANISOU 3694  CB  ASP A 558    26632  26782  24538   1065  -1037    -15       C  
ATOM   3695  CG  ASP A 558      -9.408  48.340 -50.084  1.00226.42           C  
ANISOU 3695  CG  ASP A 558    29397  29447  27184   1070  -1038    -33       C  
ATOM   3696  OD1 ASP A 558      -8.195  48.581 -50.262  1.00236.66           O  
ANISOU 3696  OD1 ASP A 558    30771  30659  28490   1091   -955     39       O  
ATOM   3697  OD2 ASP A 558      -9.986  47.349 -50.577  1.00231.20           O1-
ANISOU 3697  OD2 ASP A 558    29981  30119  27744   1051  -1121   -125       O1-
ATOM   3698  N   THR A 559      -9.344  51.703 -46.608  1.00 98.09           N  
ANISOU 3698  N   THR A 559    13023  13054  11192    978   -840    157       N  
ATOM   3699  CA  THR A 559      -9.802  52.988 -46.071  1.00106.32           C  
ANISOU 3699  CA  THR A 559    14036  14107  12254   1012   -809    199       C  
ATOM   3700  C   THR A 559      -8.822  54.116 -46.389  1.00108.12           C  
ANISOU 3700  C   THR A 559    14340  14272  12470   1089   -709    286       C  
ATOM   3701  O   THR A 559      -7.614  53.891 -46.473  1.00120.00           O  
ANISOU 3701  O   THR A 559    15894  15700  14001   1065   -647    315       O  
ATOM   3702  CB  THR A 559     -10.048  52.921 -44.543  1.00 88.80           C  
ANISOU 3702  CB  THR A 559    11736  11855  10149    887   -799    188       C  
ATOM   3703  CG2 THR A 559      -9.836  54.277 -43.900  1.00 49.94           C  
ANISOU 3703  CG2 THR A 559     6811   6896   5267    906   -726    253       C  
ATOM   3704  OG1 THR A 559     -11.396  52.506 -44.291  1.00104.87           O  
ANISOU 3704  OG1 THR A 559    13693  13973  12179    859   -883    122       O  
ATOM   3705  N   GLY A 560      -9.349  55.326 -46.570  1.00 47.22           N  
ANISOU 3705  N   GLY A 560     6635   6591   4714   1184   -688    327       N  
ATOM   3706  CA  GLY A 560      -8.520  56.478 -46.882  1.00 55.72           C  
ANISOU 3706  CA  GLY A 560     7787   7606   5776   1263   -583    412       C  
ATOM   3707  C   GLY A 560      -8.227  57.370 -45.688  1.00 71.19           C  
ANISOU 3707  C   GLY A 560     9710   9504   7834   1199   -512    451       C  
ATOM   3708  O   GLY A 560      -7.827  58.521 -45.855  1.00 63.85           O  
ANISOU 3708  O   GLY A 560     8832   8533   6894   1270   -425    521       O  
ATOM   3709  N   TYR A 561      -8.418  56.837 -44.483  1.00 57.31           N  
ANISOU 3709  N   TYR A 561     7869   7737   6170   1069   -543    408       N  
ATOM   3710  CA  TYR A 561      -8.247  57.615 -43.258  1.00 58.65           C  
ANISOU 3710  CA  TYR A 561     7994   7862   6429   1004   -490    433       C  
ATOM   3711  C   TYR A 561      -6.840  58.179 -43.116  1.00 50.29           C  
ANISOU 3711  C   TYR A 561     6981   6710   5415    994   -385    486       C  
ATOM   3712  O   TYR A 561      -5.859  57.526 -43.464  1.00 65.94           O  
ANISOU 3712  O   TYR A 561     9000   8651   7404    972   -364    483       O  
ATOM   3713  CB  TYR A 561      -8.601  56.781 -42.028  1.00 69.92           C  
ANISOU 3713  CB  TYR A 561     9334   9292   7940    870   -539    377       C  
ATOM   3714  CG  TYR A 561     -10.075  56.758 -41.690  1.00 80.92           C  
ANISOU 3714  CG  TYR A 561    10660  10764   9321    866   -612    339       C  
ATOM   3715  CD1 TYR A 561     -10.537  56.074 -40.574  1.00 90.53           C  
ANISOU 3715  CD1 TYR A 561    11803  11984  10609    754   -648    295       C  
ATOM   3716  CD2 TYR A 561     -11.003  57.423 -42.478  1.00 87.42           C  
ANISOU 3716  CD2 TYR A 561    11494  11660  10059    982   -642    349       C  
ATOM   3717  CE1 TYR A 561     -11.878  56.046 -40.255  1.00 97.68           C  
ANISOU 3717  CE1 TYR A 561    12645  12961  11509    748   -709    259       C  
ATOM   3718  CE2 TYR A 561     -12.351  57.402 -42.164  1.00 95.56           C  
ANISOU 3718  CE2 TYR A 561    12456  12772  11081    980   -712    308       C  
ATOM   3719  CZ  TYR A 561     -12.782  56.711 -41.051  1.00101.55           C  
ANISOU 3719  CZ  TYR A 561    13138  13529  11919    858   -744    262       C  
ATOM   3720  OH  TYR A 561     -14.118  56.679 -40.724  1.00101.34           O  
ANISOU 3720  OH  TYR A 561    13038  13580  11888    853   -808    219       O  
ATOM   3721  N   LEU A 562      -6.754  59.389 -42.575  1.00 51.79           N  
ANISOU 3721  N   LEU A 562     7168   6868   5641   1008   -318    532       N  
ATOM   3722  CA  LEU A 562      -5.496  60.120 -42.524  1.00 48.31           C  
ANISOU 3722  CA  LEU A 562     6774   6341   5242   1013   -209    586       C  
ATOM   3723  C   LEU A 562      -5.446  61.014 -41.287  1.00 43.99           C  
ANISOU 3723  C   LEU A 562     6174   5761   4778    956   -166    601       C  
ATOM   3724  O   LEU A 562      -6.377  61.773 -41.026  1.00 68.58           O  
ANISOU 3724  O   LEU A 562     9269   8905   7881    991   -173    616       O  
ATOM   3725  CB  LEU A 562      -5.346  60.941 -43.805  1.00 53.17           C  
ANISOU 3725  CB  LEU A 562     7491   6938   5772   1155   -138    654       C  
ATOM   3726  CG  LEU A 562      -4.068  61.732 -44.066  1.00 66.06           C  
ANISOU 3726  CG  LEU A 562     9192   8471   7435   1183     -4    719       C  
ATOM   3727  CD1 LEU A 562      -3.851  61.858 -45.562  1.00 85.41           C  
ANISOU 3727  CD1 LEU A 562    11755  10912   9785   1315     43    767       C  
ATOM   3728  CD2 LEU A 562      -4.128  63.107 -43.406  1.00 95.22           C  
ANISOU 3728  CD2 LEU A 562    12881  12116  11181   1193     81    768       C  
ATOM   3729  N   TRP A 563      -4.357  60.920 -40.528  1.00 29.42           N  
ANISOU 3729  N   TRP A 563     4306   3857   3014    873   -124    595       N  
ATOM   3730  CA  TRP A 563      -4.239  61.645 -39.261  1.00 33.94           C  
ANISOU 3730  CA  TRP A 563     4823   4403   3669    810    -94    598       C  
ATOM   3731  C   TRP A 563      -3.071  62.623 -39.222  1.00 36.74           C  
ANISOU 3731  C   TRP A 563     5216   4667   4076    823     25    650       C  
ATOM   3732  O   TRP A 563      -2.109  62.490 -39.972  1.00 57.41           O  
ANISOU 3732  O   TRP A 563     7891   7237   6685    850     82    673       O  
ATOM   3733  CB  TRP A 563      -4.068  60.661 -38.102  1.00 41.00           C  
ANISOU 3733  CB  TRP A 563     5639   5315   4625    692   -158    535       C  
ATOM   3734  CG  TRP A 563      -5.263  59.828 -37.805  1.00 39.35           C  
ANISOU 3734  CG  TRP A 563     5381   5174   4397    658   -254    485       C  
ATOM   3735  CD1 TRP A 563      -6.299  60.154 -36.989  1.00 51.53           C  
ANISOU 3735  CD1 TRP A 563     6869   6752   5959    633   -287    472       C  
ATOM   3736  CD2 TRP A 563      -5.539  58.514 -38.300  1.00 46.05           C  
ANISOU 3736  CD2 TRP A 563     6232   6054   5210    642   -320    444       C  
ATOM   3737  CE2 TRP A 563      -6.768  58.110 -37.748  1.00 52.14           C  
ANISOU 3737  CE2 TRP A 563     6949   6877   5985    605   -388    407       C  
ATOM   3738  CE3 TRP A 563      -4.869  57.642 -39.161  1.00 47.78           C  
ANISOU 3738  CE3 TRP A 563     6498   6259   5396    655   -325    436       C  
ATOM   3739  NE1 TRP A 563      -7.214  59.130 -36.950  1.00 58.48           N  
ANISOU 3739  NE1 TRP A 563     7716   7682   6820    601   -366    425       N  
ATOM   3740  CZ2 TRP A 563      -7.340  56.874 -38.029  1.00 43.85           C  
ANISOU 3740  CZ2 TRP A 563     5888   5861   4910    580   -457    363       C  
ATOM   3741  CZ3 TRP A 563      -5.439  56.415 -39.437  1.00 53.14           C  
ANISOU 3741  CZ3 TRP A 563     7168   6975   6049    632   -398    391       C  
ATOM   3742  CH2 TRP A 563      -6.660  56.042 -38.871  1.00 38.26           C  
ANISOU 3742  CH2 TRP A 563     5227   5137   4171    593   -462    355       C  
ATOM   3743  N   HIS A 564      -3.175  63.608 -38.333  1.00 39.54           N  
ANISOU 3743  N   HIS A 564     5540   4993   4490    801     66    667       N  
ATOM   3744  CA  HIS A 564      -2.033  64.419 -37.921  1.00 48.12           C  
ANISOU 3744  CA  HIS A 564     6637   5985   5661    777    173    697       C  
ATOM   3745  C   HIS A 564      -1.487  63.753 -36.669  1.00 51.88           C  
ANISOU 3745  C   HIS A 564     7031   6475   6208    668    117    640       C  
ATOM   3746  O   HIS A 564      -2.001  63.978 -35.574  1.00 43.22           O  
ANISOU 3746  O   HIS A 564     5871   5404   5147    621     79    617       O  
ATOM   3747  CB  HIS A 564      -2.464  65.846 -37.567  1.00 29.14           C  
ANISOU 3747  CB  HIS A 564     4245   3534   3294    812    251    742       C  
ATOM   3748  CG  HIS A 564      -2.619  66.758 -38.747  1.00 56.31           C  
ANISOU 3748  CG  HIS A 564     7785   6925   6684    930    353    814       C  
ATOM   3749  CD2 HIS A 564      -2.244  68.046 -38.929  1.00 40.94           C  
ANISOU 3749  CD2 HIS A 564     5890   4878   4786    971    502    861       C  
ATOM   3750  ND1 HIS A 564      -3.258  66.379 -39.909  1.00 55.46           N  
ANISOU 3750  ND1 HIS A 564     7733   6875   6465   1023    315    831       N  
ATOM   3751  CE1 HIS A 564      -3.250  67.388 -40.764  1.00 55.38           C  
ANISOU 3751  CE1 HIS A 564     7816   6804   6423   1131    429    904       C  
ATOM   3752  NE2 HIS A 564      -2.642  68.412 -40.193  1.00 69.56           N  
ANISOU 3752  NE2 HIS A 564     9617   8495   8318   1102    548    932       N  
ATOM   3753  N   VAL A 565      -0.464  62.920 -36.815  1.00 32.18           N  
ANISOU 3753  N   VAL A 565     4536   3966   3725    635    112    619       N  
ATOM   3754  CA  VAL A 565       0.033  62.167 -35.670  1.00 41.62           C  
ANISOU 3754  CA  VAL A 565     5658   5185   4970    548     51    566       C  
ATOM   3755  C   VAL A 565       1.348  62.711 -35.109  1.00 43.22           C  
ANISOU 3755  C   VAL A 565     5819   5328   5275    498    143    527       C  
ATOM   3756  O   VAL A 565       2.339  62.835 -35.831  1.00 39.42           O  
ANISOU 3756  O   VAL A 565     5372   4790   4816    514    227    532       O  
ATOM   3757  CB  VAL A 565       0.140  60.653 -35.979  1.00 23.02           C  
ANISOU 3757  CB  VAL A 565     3298   2882   2567    524    -27    523       C  
ATOM   3758  CG1 VAL A 565       1.107  60.403 -37.088  1.00 45.45           C  
ANISOU 3758  CG1 VAL A 565     6204   5678   5389    564     28    548       C  
ATOM   3759  CG2 VAL A 565       0.557  59.887 -34.730  1.00 71.77           C  
ANISOU 3759  CG2 VAL A 565     9402   9084   8784    446    -86    471       C  
ATOM   3760  N   PRO A 566       1.347  63.039 -33.806  1.00 35.02           N  
ANISOU 3760  N   PRO A 566     4701   4304   4300    437    129    478       N  
ATOM   3761  CA  PRO A 566       2.476  63.575 -33.038  1.00 43.59           C  
ANISOU 3761  CA  PRO A 566     5721   5353   5488    381    200    415       C  
ATOM   3762  C   PRO A 566       3.504  62.501 -32.711  1.00 35.05           C  
ANISOU 3762  C   PRO A 566     4600   4299   4419    343    156    365       C  
ATOM   3763  O   PRO A 566       3.540  62.024 -31.576  1.00 52.84           O  
ANISOU 3763  O   PRO A 566     6787   6604   6685    299     85    317       O  
ATOM   3764  CB  PRO A 566       1.827  64.042 -31.731  1.00 19.92           C  
ANISOU 3764  CB  PRO A 566     2657   2390   2523    340    162    381       C  
ATOM   3765  CG  PRO A 566       0.350  63.965 -31.953  1.00 53.13           C  
ANISOU 3765  CG  PRO A 566     6900   6635   6651    381     96    436       C  
ATOM   3766  CD  PRO A 566       0.145  62.913 -32.972  1.00 31.78           C  
ANISOU 3766  CD  PRO A 566     4256   3957   3863    422     38    475       C  
ATOM   3767  N   LEU A 567       4.322  62.123 -33.685  1.00 35.68           N  
ANISOU 3767  N   LEU A 567     4722   4343   4490    367    200    379       N  
ATOM   3768  CA  LEU A 567       5.307  61.070 -33.474  1.00 46.22           C  
ANISOU 3768  CA  LEU A 567     6026   5705   5831    342    162    337       C  
ATOM   3769  C   LEU A 567       6.381  61.498 -32.490  1.00 46.35           C  
ANISOU 3769  C   LEU A 567     5947   5717   5946    288    203    253       C  
ATOM   3770  O   LEU A 567       6.746  62.671 -32.415  1.00 47.61           O  
ANISOU 3770  O   LEU A 567     6081   5823   6185    271    305    227       O  
ATOM   3771  CB  LEU A 567       5.944  60.647 -34.799  1.00 38.43           C  
ANISOU 3771  CB  LEU A 567     5109   4677   4815    383    210    372       C  
ATOM   3772  CG  LEU A 567       4.994  59.898 -35.732  1.00 37.66           C  
ANISOU 3772  CG  LEU A 567     5097   4604   4607    436    143    437       C  
ATOM   3773  CD1 LEU A 567       5.638  59.604 -37.071  1.00 35.71           C  
ANISOU 3773  CD1 LEU A 567     4925   4313   4329    483    200    471       C  
ATOM   3774  CD2 LEU A 567       4.548  58.623 -35.065  1.00 42.26           C  
ANISOU 3774  CD2 LEU A 567     5656   5260   5142    411     15    419       C  
ATOM   3775  N   THR A 568       6.878  60.535 -31.725  1.00 41.15           N  
ANISOU 3775  N   THR A 568     5237   5117   5281    265    126    206       N  
ATOM   3776  CA  THR A 568       8.014  60.768 -30.848  1.00 51.80           C  
ANISOU 3776  CA  THR A 568     6489   6480   6711    226    151    115       C  
ATOM   3777  C   THR A 568       8.958  59.599 -31.027  1.00 46.28           C  
ANISOU 3777  C   THR A 568     5785   5809   5991    238    115     97       C  
ATOM   3778  O   THR A 568       8.531  58.511 -31.391  1.00 39.09           O  
ANISOU 3778  O   THR A 568     4932   4922   4997    266     44    146       O  
ATOM   3779  CB  THR A 568       7.589  60.867 -29.378  1.00 32.07           C  
ANISOU 3779  CB  THR A 568     3919   4045   4221    196     80     66       C  
ATOM   3780  CG2 THR A 568       6.800  62.138 -29.150  1.00 38.61           C  
ANISOU 3780  CG2 THR A 568     4744   4840   5085    181    130     74       C  
ATOM   3781  OG1 THR A 568       6.768  59.742 -29.041  1.00 43.62           O  
ANISOU 3781  OG1 THR A 568     5414   5566   5594    214    -33    105       O  
ATOM   3782  N   PHE A 569      10.244  59.821 -30.796  1.00 25.52           N  
ANISOU 3782  N   PHE A 569     3083   3176   3438    218    168     21       N  
ATOM   3783  CA  PHE A 569      11.195  58.731 -30.940  1.00 41.44           C  
ANISOU 3783  CA  PHE A 569     5089   5222   5436    237    136      0       C  
ATOM   3784  C   PHE A 569      12.514  58.966 -30.225  1.00 46.26           C  
ANISOU 3784  C   PHE A 569     5584   5862   6130    212    164   -109       C  
ATOM   3785  O   PHE A 569      12.947  60.103 -30.046  1.00 30.53           O  
ANISOU 3785  O   PHE A 569     3531   3837   4233    175    250   -170       O  
ATOM   3786  CB  PHE A 569      11.424  58.376 -32.419  1.00 26.15           C  
ANISOU 3786  CB  PHE A 569     3242   3226   3470    269    190     64       C  
ATOM   3787  CG  PHE A 569      12.205  59.404 -33.196  1.00 59.94           C  
ANISOU 3787  CG  PHE A 569     7515   7423   7836    258    333     46       C  
ATOM   3788  CD1 PHE A 569      13.584  59.294 -33.330  1.00 34.19           C  
ANISOU 3788  CD1 PHE A 569     4197   4153   4641    248    391    -17       C  
ATOM   3789  CD2 PHE A 569      11.554  60.462 -33.823  1.00 71.81           C  
ANISOU 3789  CD2 PHE A 569     9075   8857   9354    263    416     95       C  
ATOM   3790  CE1 PHE A 569      14.306  60.233 -34.062  1.00 38.81           C  
ANISOU 3790  CE1 PHE A 569     4779   4653   5314    233    537    -35       C  
ATOM   3791  CE2 PHE A 569      12.266  61.404 -34.556  1.00 48.20           C  
ANISOU 3791  CE2 PHE A 569     6092   5779   6444    256    565     85       C  
ATOM   3792  CZ  PHE A 569      13.644  61.289 -34.677  1.00 36.88           C  
ANISOU 3792  CZ  PHE A 569     4600   4330   5084    237    629     19       C  
ATOM   3793  N   ILE A 570      13.125  57.870 -29.791  1.00 40.54           N  
ANISOU 3793  N   ILE A 570     4831   5203   5371    237     91   -137       N  
ATOM   3794  CA  ILE A 570      14.451  57.917 -29.201  1.00 45.95           C  
ANISOU 3794  CA  ILE A 570     5405   5931   6123    228    105   -244       C  
ATOM   3795  C   ILE A 570      15.383  57.067 -30.039  1.00 46.50           C  
ANISOU 3795  C   ILE A 570     5498   5989   6182    260    125   -233       C  
ATOM   3796  O   ILE A 570      14.942  56.313 -30.905  1.00 40.27           O  
ANISOU 3796  O   ILE A 570     4812   5169   5320    290    109   -144       O  
ATOM   3797  CB  ILE A 570      14.461  57.443 -27.734  1.00 47.40           C  
ANISOU 3797  CB  ILE A 570     5517   6220   6274    243     -2   -302       C  
ATOM   3798  CG1 ILE A 570      13.811  56.065 -27.603  1.00 41.88           C  
ANISOU 3798  CG1 ILE A 570     4897   5558   5456    292   -104   -225       C  
ATOM   3799  CG2 ILE A 570      13.750  58.453 -26.845  1.00 37.04           C  
ANISOU 3799  CG2 ILE A 570     4162   4919   4993    206     -6   -335       C  
ATOM   3800  CD1 ILE A 570      13.874  55.501 -26.207  1.00 35.85           C  
ANISOU 3800  CD1 ILE A 570     4080   4894   4649    323   -200   -272       C  
ATOM   3801  N   THR A 571      16.676  57.192 -29.777  1.00 64.28           N  
ANISOU 3801  N   THR A 571     7648   8268   8506    254    159   -330       N  
ATOM   3802  CA  THR A 571      17.688  56.613 -30.643  1.00 48.43           C  
ANISOU 3802  CA  THR A 571     5651   6239   6512    278    204   -330       C  
ATOM   3803  C   THR A 571      18.842  56.068 -29.814  1.00 49.38           C  
ANISOU 3803  C   THR A 571     5659   6453   6652    303    154   -431       C  
ATOM   3804  O   THR A 571      19.114  56.557 -28.720  1.00 54.98           O  
ANISOU 3804  O   THR A 571     6259   7228   7404    286    126   -528       O  
ATOM   3805  CB  THR A 571      18.201  57.678 -31.635  1.00 41.02           C  
ANISOU 3805  CB  THR A 571     4709   5201   5674    239    356   -344       C  
ATOM   3806  CG2 THR A 571      19.631  57.420 -32.017  1.00 37.52           C  
ANISOU 3806  CG2 THR A 571     4203   4760   5295    245    414   -411       C  
ATOM   3807  OG1 THR A 571      17.390  57.664 -32.814  1.00 52.90           O  
ANISOU 3807  OG1 THR A 571     6350   6623   7125    254    396   -227       O  
ATOM   3808  N   SER A 572      19.512  55.044 -30.329  1.00 46.24           N  
ANISOU 3808  N   SER A 572     5287   6066   6217    349    141   -411       N  
ATOM   3809  CA  SER A 572      20.672  54.486 -29.648  1.00 29.34           C  
ANISOU 3809  CA  SER A 572     3040   4016   4089    386     98   -504       C  
ATOM   3810  C   SER A 572      21.713  55.570 -29.385  1.00 47.80           C  
ANISOU 3810  C   SER A 572     5234   6365   6564    339    178   -639       C  
ATOM   3811  O   SER A 572      22.546  55.441 -28.488  1.00 61.44           O  
ANISOU 3811  O   SER A 572     6839   8190   8314    360    130   -749       O  
ATOM   3812  CB  SER A 572      21.288  53.361 -30.477  1.00 36.37           C  
ANISOU 3812  CB  SER A 572     3988   4895   4935    439    101   -458       C  
ATOM   3813  OG  SER A 572      22.215  53.868 -31.425  1.00 56.91           O  
ANISOU 3813  OG  SER A 572     6559   7434   7630    412    219   -492       O  
ATOM   3814  N   LYS A 573      21.661  56.639 -30.173  1.00 54.80           N  
ANISOU 3814  N   LYS A 573     6134   7150   7537    277    303   -635       N  
ATOM   3815  CA  LYS A 573      22.599  57.747 -30.030  1.00 73.26           C  
ANISOU 3815  CA  LYS A 573     8341   9474  10020    218    404   -765       C  
ATOM   3816  C   LYS A 573      22.002  58.865 -29.181  1.00 66.53           C  
ANISOU 3816  C   LYS A 573     7436   8627   9217    163    409   -820       C  
ATOM   3817  O   LYS A 573      22.574  59.256 -28.167  1.00 66.66           O  
ANISOU 3817  O   LYS A 573     7314   8723   9292    145    382   -953       O  
ATOM   3818  CB  LYS A 573      23.018  58.269 -31.405  1.00 44.68           C  
ANISOU 3818  CB  LYS A 573     4769   5730   6477    186    562   -733       C  
ATOM   3819  CG  LYS A 573      23.370  57.154 -32.381  1.00 83.63           C  
ANISOU 3819  CG  LYS A 573     9788  10644  11344    243    558   -653       C  
ATOM   3820  CD  LYS A 573      24.723  57.377 -33.033  1.00 86.16           C  
ANISOU 3820  CD  LYS A 573    10036  10928  11774    225    678   -728       C  
ATOM   3821  CE  LYS A 573      25.562  56.107 -33.032  1.00 91.02           C  
ANISOU 3821  CE  LYS A 573    10625  11619  12338    291    607   -742       C  
ATOM   3822  NZ  LYS A 573      25.049  55.088 -33.986  1.00114.73           N1+
ANISOU 3822  NZ  LYS A 573    13788  14578  15225    346    582   -600       N1+
ATOM   3823  N   SER A 574      20.843  59.367 -29.591  1.00 85.63           N  
ANISOU 3823  N   SER A 574     9962  10965  11608    142    441   -721       N  
ATOM   3824  CA  SER A 574      20.169  60.410 -28.829  1.00102.39           C  
ANISOU 3824  CA  SER A 574    12050  13085  13770     95    448   -759       C  
ATOM   3825  C   SER A 574      20.087  60.024 -27.358  1.00 88.26           C  
ANISOU 3825  C   SER A 574    10176  11427  11932    119    310   -831       C  
ATOM   3826  O   SER A 574      20.202  58.852 -27.001  1.00 93.54           O  
ANISOU 3826  O   SER A 574    10856  12179  12507    183    200   -809       O  
ATOM   3827  CB  SER A 574      18.761  60.651 -29.375  1.00101.49           C  
ANISOU 3827  CB  SER A 574    12077  12893  13590     97    457   -622       C  
ATOM   3828  OG  SER A 574      17.893  59.583 -29.040  1.00 99.03           O  
ANISOU 3828  OG  SER A 574    11840  12643  13145    149    322   -537       O  
ATOM   3829  N   ASP A 575      19.898  61.022 -26.507  1.00 81.08           N  
ANISOU 3829  N   ASP A 575     9187  10534  11084     71    322   -916       N  
ATOM   3830  CA  ASP A 575      19.627  60.785 -25.097  1.00112.17           C  
ANISOU 3830  CA  ASP A 575    13062  14591  14967     97    196   -973       C  
ATOM   3831  C   ASP A 575      18.304  61.456 -24.767  1.00108.16           C  
ANISOU 3831  C   ASP A 575    12618  14045  14435     69    191   -913       C  
ATOM   3832  O   ASP A 575      17.726  61.247 -23.699  1.00 98.58           O  
ANISOU 3832  O   ASP A 575    11391  12910  13155     93     90   -922       O  
ATOM   3833  CB  ASP A 575      20.755  61.341 -24.226  1.00156.08           C  
ANISOU 3833  CB  ASP A 575    18444  20232  20625     71    203  -1161       C  
ATOM   3834  CG  ASP A 575      21.263  62.684 -24.713  1.00191.24           C  
ANISOU 3834  CG  ASP A 575    22833  24590  25238    -20    363  -1246       C  
ATOM   3835  OD1 ASP A 575      21.889  62.728 -25.793  1.00202.64           O  
ANISOU 3835  OD1 ASP A 575    24295  25954  26745    -38    469  -1230       O  
ATOM   3836  OD2 ASP A 575      21.042  63.697 -24.015  1.00201.82           O1-
ANISOU 3836  OD2 ASP A 575    24107  25931  26644    -73    390  -1330       O1-
ATOM   3837  N   MET A 576      17.827  62.259 -25.715  1.00 87.38           N  
ANISOU 3837  N   MET A 576    10058  11288  11853     25    307   -848       N  
ATOM   3838  CA  MET A 576      16.594  63.014 -25.553  1.00 75.30           C  
ANISOU 3838  CA  MET A 576     8590   9709  10311      0    322   -789       C  
ATOM   3839  C   MET A 576      15.527  62.553 -26.537  1.00 54.03           C  
ANISOU 3839  C   MET A 576     6053   6949   7527     33    317   -623       C  
ATOM   3840  O   MET A 576      15.834  61.993 -27.587  1.00 87.13           O  
ANISOU 3840  O   MET A 576    10309  11098  11697     58    349   -560       O  
ATOM   3841  CB  MET A 576      16.864  64.504 -25.751  1.00102.45           C  
ANISOU 3841  CB  MET A 576    11979  13059  13889    -73    471   -861       C  
ATOM   3842  CG  MET A 576      17.568  64.823 -27.060  1.00115.20           C  
ANISOU 3842  CG  MET A 576    13624  14564  15581    -93    617   -843       C  
ATOM   3843  SD  MET A 576      17.869  66.586 -27.300  1.00122.19           S  
ANISOU 3843  SD  MET A 576    14463  15326  16636   -180    816   -923       S  
ATOM   3844  CE  MET A 576      16.244  67.150 -27.809  1.00 62.50           C  
ANISOU 3844  CE  MET A 576     7061   7675   9010   -160    848   -764       C  
ATOM   3845  N   VAL A 577      14.271  62.804 -26.188  1.00 31.49           N  
ANISOU 3845  N   VAL A 577     3255   4089   4619     35    277   -559       N  
ATOM   3846  CA  VAL A 577      13.138  62.382 -26.996  1.00 49.43           C  
ANISOU 3846  CA  VAL A 577     5664   6317   6802     68    257   -415       C  
ATOM   3847  C   VAL A 577      12.850  63.350 -28.151  1.00 33.82           C  
ANISOU 3847  C   VAL A 577     3757   4218   4874     51    392   -356       C  
ATOM   3848  O   VAL A 577      12.724  64.556 -27.940  1.00 66.33           O  
ANISOU 3848  O   VAL A 577     7845   8287   9070     11    476   -395       O  
ATOM   3849  CB  VAL A 577      11.887  62.214 -26.111  1.00 18.17           C  
ANISOU 3849  CB  VAL A 577     1730   2409   2766     79    157   -375       C  
ATOM   3850  CG1 VAL A 577      11.793  63.351 -25.105  1.00 75.86           C  
ANISOU 3850  CG1 VAL A 577     8952   9726  10143     35    184   -462       C  
ATOM   3851  CG2 VAL A 577      10.626  62.128 -26.964  1.00 24.59           C  
ANISOU 3851  CG2 VAL A 577     2666   3167   3510    101    158   -245       C  
ATOM   3852  N   HIS A 578      12.745  62.816 -29.368  1.00 31.08           N  
ANISOU 3852  N   HIS A 578     3509   3823   4476     88    414   -263       N  
ATOM   3853  CA  HIS A 578      12.510  63.635 -30.561  1.00 35.44           C  
ANISOU 3853  CA  HIS A 578     4143   4264   5057     93    543   -197       C  
ATOM   3854  C   HIS A 578      11.042  63.694 -30.984  1.00 50.57           C  
ANISOU 3854  C   HIS A 578     6168   6162   6885    130    510    -83       C  
ATOM   3855  O   HIS A 578      10.281  62.752 -30.766  1.00 55.20           O  
ANISOU 3855  O   HIS A 578     6789   6811   7373    158    387    -34       O  
ATOM   3856  CB  HIS A 578      13.342  63.120 -31.737  1.00 13.70           C  
ANISOU 3856  CB  HIS A 578     1435   1466   2303    119    603   -168       C  
ATOM   3857  CG  HIS A 578      14.812  63.079 -31.469  1.00 53.27           C  
ANISOU 3857  CG  HIS A 578     6340   6493   7408     86    647   -280       C  
ATOM   3858  CD2 HIS A 578      15.581  62.146 -30.860  1.00 50.17           C  
ANISOU 3858  CD2 HIS A 578     5872   6189   7003     92    560   -346       C  
ATOM   3859  ND1 HIS A 578      15.667  64.089 -31.850  1.00 53.66           N  
ANISOU 3859  ND1 HIS A 578     6348   6460   7581     46    804   -341       N  
ATOM   3860  CE1 HIS A 578      16.898  63.781 -31.484  1.00 58.47           C  
ANISOU 3860  CE1 HIS A 578     6850   7112   8255     23    805   -447       C  
ATOM   3861  NE2 HIS A 578      16.874  62.607 -30.882  1.00 55.05           N  
ANISOU 3861  NE2 HIS A 578     6395   6786   7737     55    655   -450       N  
ATOM   3862  N   ARG A 579      10.654  64.802 -31.608  1.00 44.30           N  
ANISOU 3862  N   ARG A 579     5427   5279   6128    133    624    -43       N  
ATOM   3863  CA  ARG A 579       9.297  64.949 -32.125  1.00 44.06           C  
ANISOU 3863  CA  ARG A 579     5496   5231   6012    180    602     63       C  
ATOM   3864  C   ARG A 579       9.269  65.059 -33.645  1.00 37.89           C  
ANISOU 3864  C   ARG A 579     4827   4372   5196    236    691    151       C  
ATOM   3865  O   ARG A 579      10.253  65.451 -34.270  1.00 36.57           O  
ANISOU 3865  O   ARG A 579     4663   4133   5098    230    813    131       O  
ATOM   3866  CB  ARG A 579       8.611  66.173 -31.517  1.00 34.99           C  
ANISOU 3866  CB  ARG A 579     4329   4055   4912    157    650     51       C  
ATOM   3867  CG  ARG A 579       7.987  65.927 -30.170  1.00 32.40           C  
ANISOU 3867  CG  ARG A 579     3934   3815   4560    131    529     11       C  
ATOM   3868  CD  ARG A 579       8.285  67.069 -29.216  1.00 46.11           C  
ANISOU 3868  CD  ARG A 579     5585   5532   6404     74    596    -81       C  
ATOM   3869  NE  ARG A 579       7.953  66.706 -27.844  1.00 83.32           N  
ANISOU 3869  NE  ARG A 579    10224  10340  11095     49    477   -136       N  
ATOM   3870  CZ  ARG A 579       8.364  67.378 -26.775  1.00108.53           C  
ANISOU 3870  CZ  ARG A 579    13319  13550  14367     -2    496   -241       C  
ATOM   3871  NH1 ARG A 579       9.129  68.453 -26.919  1.00123.35           N1+
ANISOU 3871  NH1 ARG A 579    15155  15352  16360    -43    633   -310       N1+
ATOM   3872  NH2 ARG A 579       8.013  66.973 -25.560  1.00102.38           N  
ANISOU 3872  NH2 ARG A 579    12485  12864  13552    -10    383   -282       N  
ATOM   3873  N   PHE A 580       8.127  64.704 -34.224  1.00 13.50           N  
ANISOU 3873  N   PHE A 580     1828   1300   2000    294    628    244       N  
ATOM   3874  CA  PHE A 580       7.884  64.856 -35.651  1.00 28.66           C  
ANISOU 3874  CA  PHE A 580     3864   3160   3866    365    699    333       C  
ATOM   3875  C   PHE A 580       6.385  64.781 -35.921  1.00 52.01           C  
ANISOU 3875  C   PHE A 580     6891   6154   6717    422    620    413       C  
ATOM   3876  O   PHE A 580       5.721  63.808 -35.543  1.00 23.41           O  
ANISOU 3876  O   PHE A 580     3257   2615   3023    421    480    418       O  
ATOM   3877  CB  PHE A 580       8.622  63.786 -36.465  1.00 20.82           C  
ANISOU 3877  CB  PHE A 580     2906   2173   2831    388    681    347       C  
ATOM   3878  CG  PHE A 580       8.470  63.953 -37.951  1.00 32.25           C  
ANISOU 3878  CG  PHE A 580     4475   3559   4220    467    760    433       C  
ATOM   3879  CD1 PHE A 580       9.465  64.558 -38.701  1.00 26.05           C  
ANISOU 3879  CD1 PHE A 580     3719   2679   3501    476    918    433       C  
ATOM   3880  CD2 PHE A 580       7.317  63.529 -38.592  1.00 50.32           C  
ANISOU 3880  CD2 PHE A 580     6848   5886   6386    536    680    510       C  
ATOM   3881  CE1 PHE A 580       9.315  64.731 -40.060  1.00 24.72           C  
ANISOU 3881  CE1 PHE A 580     3671   2452   3269    560    997    518       C  
ATOM   3882  CE2 PHE A 580       7.165  63.697 -39.954  1.00 55.08           C  
ANISOU 3882  CE2 PHE A 580     7564   6441   6923    621    748    586       C  
ATOM   3883  CZ  PHE A 580       8.165  64.298 -40.690  1.00 31.85           C  
ANISOU 3883  CZ  PHE A 580     4659   3402   4039    638    908    595       C  
ATOM   3884  N   LEU A 581       5.848  65.804 -36.575  1.00 17.89           N  
ANISOU 3884  N   LEU A 581     2640   1770   2388    475    714    472       N  
ATOM   3885  CA  LEU A 581       4.421  65.819 -36.848  1.00 29.52           C  
ANISOU 3885  CA  LEU A 581     4171   3285   3761    538    642    541       C  
ATOM   3886  C   LEU A 581       4.114  65.243 -38.230  1.00 49.15           C  
ANISOU 3886  C   LEU A 581     6762   5776   6137    627    626    616       C  
ATOM   3887  O   LEU A 581       4.440  65.841 -39.255  1.00 54.72           O  
ANISOU 3887  O   LEU A 581     7548   6405   6836    689    747    665       O  
ATOM   3888  CB  LEU A 581       3.848  67.228 -36.683  1.00 41.52           C  
ANISOU 3888  CB  LEU A 581     5707   4749   5319    559    737    565       C  
ATOM   3889  CG  LEU A 581       2.324  67.336 -36.543  1.00 50.27           C  
ANISOU 3889  CG  LEU A 581     6838   5917   6345    607    648    613       C  
ATOM   3890  CD1 LEU A 581       1.645  67.240 -37.895  1.00 73.21           C  
ANISOU 3890  CD1 LEU A 581     9854   8825   9135    721    647    701       C  
ATOM   3891  CD2 LEU A 581       1.773  66.284 -35.588  1.00 39.14           C  
ANISOU 3891  CD2 LEU A 581     5355   4614   4903    555    479    572       C  
ATOM   3892  N   LEU A 582       3.484  64.075 -38.240  1.00 32.50           N  
ANISOU 3892  N   LEU A 582     4654   3755   3941    634    480    621       N  
ATOM   3893  CA  LEU A 582       3.166  63.377 -39.472  1.00 29.51           C  
ANISOU 3893  CA  LEU A 582     4363   3397   3453    712    442    674       C  
ATOM   3894  C   LEU A 582       1.810  63.830 -40.008  1.00 56.11           C  
ANISOU 3894  C   LEU A 582     7791   6796   6732    798    413    735       C  
ATOM   3895  O   LEU A 582       0.767  63.389 -39.528  1.00 70.08           O  
ANISOU 3895  O   LEU A 582     9521   8648   8457    786    295    717       O  
ATOM   3896  CB  LEU A 582       3.167  61.870 -39.216  1.00 45.73           C  
ANISOU 3896  CB  LEU A 582     6385   5528   5465    672    307    639       C  
ATOM   3897  CG  LEU A 582       3.360  60.914 -40.387  1.00 30.81           C  
ANISOU 3897  CG  LEU A 582     4568   3648   3489    724    279    666       C  
ATOM   3898  CD1 LEU A 582       2.207  61.013 -41.342  1.00 80.88           C  
ANISOU 3898  CD1 LEU A 582    10968  10035   9730    807    252    689       C  
ATOM   3899  CD2 LEU A 582       4.666  61.206 -41.091  1.00 47.89           C  
ANISOU 3899  CD2 LEU A 582     6771   5729   5697    739    409    675       C  
ATOM   3900  N   LYS A 583       1.829  64.708 -41.006  1.00 53.09           N  
ANISOU 3900  N   LYS A 583     7498   6351   6323    887    527    797       N  
ATOM   3901  CA  LYS A 583       0.599  65.258 -41.574  1.00 34.24           C  
ANISOU 3901  CA  LYS A 583     5169   3994   3846    988    513    853       C  
ATOM   3902  C   LYS A 583       0.153  64.553 -42.847  1.00 41.87           C  
ANISOU 3902  C   LYS A 583     6201   5022   4687   1078    462    863       C  
ATOM   3903  O   LYS A 583      -0.962  64.764 -43.318  1.00 50.20           O  
ANISOU 3903  O   LYS A 583     7282   6135   5655   1160    420    880       O  
ATOM   3904  CB  LYS A 583       0.773  66.748 -41.878  1.00 41.99           C  
ANISOU 3904  CB  LYS A 583     6212   4875   4869   1046    681    907       C  
ATOM   3905  CG  LYS A 583       0.477  67.669 -40.718  1.00 47.52           C  
ANISOU 3905  CG  LYS A 583     6843   5553   5659    988    713    881       C  
ATOM   3906  CD  LYS A 583       0.517  69.135 -41.133  1.00 65.96           C  
ANISOU 3906  CD  LYS A 583     9251   7786   8025   1059    888    937       C  
ATOM   3907  CE  LYS A 583       1.916  69.560 -41.537  1.00 85.55           C  
ANISOU 3907  CE  LYS A 583    11763  10147  10593   1036   1058    932       C  
ATOM   3908  NZ  LYS A 583       1.961  71.000 -41.910  1.00114.68           N1+
ANISOU 3908  NZ  LYS A 583    15530  13722  14322   1100   1247    986       N1+
ATOM   3909  N   THR A 584       1.025  63.726 -43.411  1.00 48.89           N  
ANISOU 3909  N   THR A 584     7115   5897   5564   1067    466    851       N  
ATOM   3910  CA  THR A 584       0.766  63.128 -44.717  1.00 43.45           C  
ANISOU 3910  CA  THR A 584     6501   5247   4760   1159    437    864       C  
ATOM   3911  C   THR A 584       0.801  61.606 -44.673  1.00 44.07           C  
ANISOU 3911  C   THR A 584     6534   5397   4813   1099    311    795       C  
ATOM   3912  O   THR A 584       0.982  61.021 -43.614  1.00 46.01           O  
ANISOU 3912  O   THR A 584     6692   5664   5126    992    247    741       O  
ATOM   3913  CB  THR A 584       1.780  63.632 -45.751  1.00 41.67           C  
ANISOU 3913  CB  THR A 584     6382   4922   4529   1231    588    930       C  
ATOM   3914  CG2 THR A 584       1.520  65.093 -46.081  1.00 30.76           C  
ANISOU 3914  CG2 THR A 584     5073   3469   3145   1322    721   1006       C  
ATOM   3915  OG1 THR A 584       3.098  63.510 -45.210  1.00 72.87           O  
ANISOU 3915  OG1 THR A 584    10298   8796   8592   1137    654    914       O  
ATOM   3916  N   LYS A 585       0.622  60.964 -45.823  1.00 56.53           N  
ANISOU 3916  N   LYS A 585     8176   7008   6294   1173    279    797       N  
ATOM   3917  CA  LYS A 585       0.640  59.500 -45.883  1.00 37.90           C  
ANISOU 3917  CA  LYS A 585     5785   4705   3912   1121    170    732       C  
ATOM   3918  C   LYS A 585       2.038  58.954 -45.599  1.00 52.44           C  
ANISOU 3918  C   LYS A 585     7613   6488   5823   1048    213    721       C  
ATOM   3919  O   LYS A 585       2.196  57.961 -44.886  1.00 37.09           O  
ANISOU 3919  O   LYS A 585     5602   4574   3917    958    136    663       O  
ATOM   3920  CB  LYS A 585       0.134  59.011 -47.235  1.00 37.34           C  
ANISOU 3920  CB  LYS A 585     5790   4678   3718   1226    132    738       C  
ATOM   3921  CG  LYS A 585       0.188  57.505 -47.429  1.00 25.95           C  
ANISOU 3921  CG  LYS A 585     4329   3278   2253   1178     34    674       C  
ATOM   3922  CD  LYS A 585      -0.924  56.783 -46.687  1.00 49.06           C  
ANISOU 3922  CD  LYS A 585     7168   6283   5190   1108    -95    605       C  
ATOM   3923  CE  LYS A 585      -0.799  55.272 -46.858  1.00 66.98           C  
ANISOU 3923  CE  LYS A 585     9426   8575   7447   1056   -173    546       C  
ATOM   3924  NZ  LYS A 585      -1.869  54.524 -46.142  1.00 77.81           N1+
ANISOU 3924  NZ  LYS A 585    10718  10009   8837    985   -282    481       N1+
ATOM   3925  N   THR A 586       3.048  59.614 -46.161  1.00 63.11           N  
ANISOU 3925  N   THR A 586     9032   7752   7194   1091    345    778       N  
ATOM   3926  CA  THR A 586       4.446  59.269 -45.911  1.00 62.27           C  
ANISOU 3926  CA  THR A 586     8913   7584   7164   1028    404    773       C  
ATOM   3927  C   THR A 586       5.236  60.536 -45.623  1.00 48.06           C  
ANISOU 3927  C   THR A 586     7123   5679   5458   1022    553    822       C  
ATOM   3928  O   THR A 586       4.800  61.618 -45.993  1.00 54.00           O  
ANISOU 3928  O   THR A 586     7928   6395   6193   1091    632    873       O  
ATOM   3929  CB  THR A 586       5.084  58.594 -47.131  1.00 59.47           C  
ANISOU 3929  CB  THR A 586     8641   7209   6746   1086    434    789       C  
ATOM   3930  CG2 THR A 586       4.374  57.301 -47.461  1.00 80.63           C  
ANISOU 3930  CG2 THR A 586    11314   9977   9344   1087    297    735       C  
ATOM   3931  OG1 THR A 586       5.007  59.477 -48.257  1.00101.58           O  
ANISOU 3931  OG1 THR A 586    14082  12496  12018   1203    540    859       O  
ATOM   3932  N   ASP A 587       6.388  60.389 -44.971  1.00 15.37           N  
ANISOU 3932  N   ASP A 587     2925   1491   1423    939    598    789       N  
ATOM   3933  CA  ASP A 587       7.335  61.485 -44.775  1.00 42.22           C  
ANISOU 3933  CA  ASP A 587     6308   4795   4940    914    760    785       C  
ATOM   3934  C   ASP A 587       8.729  60.931 -44.482  1.00 46.75           C  
ANISOU 3934  C   ASP A 587     6823   5340   5600    842    797    728       C  
ATOM   3935  O   ASP A 587       8.871  59.789 -44.040  1.00 22.20           O  
ANISOU 3935  O   ASP A 587     3664   2293   2477    796    683    686       O  
ATOM   3936  CB  ASP A 587       6.898  62.411 -43.637  1.00 64.17           C  
ANISOU 3936  CB  ASP A 587     9012   7573   7798    860    768    759       C  
ATOM   3937  CG  ASP A 587       5.789  63.364 -44.043  1.00108.89           C  
ANISOU 3937  CG  ASP A 587    14742  13229  13402    944    796    824       C  
ATOM   3938  OD1 ASP A 587       5.638  63.634 -45.252  1.00 96.98           O  
ANISOU 3938  OD1 ASP A 587    13345  11688  11813   1050    862    892       O  
ATOM   3939  OD2 ASP A 587       5.066  63.863 -43.149  1.00141.39           O1-
ANISOU 3939  OD2 ASP A 587    18802  17373  17546    912    756    808       O1-
ATOM   3940  N   VAL A 588       9.756  61.737 -44.730  1.00 50.58           N  
ANISOU 3940  N   VAL A 588     7313   5729   6177    834    961    724       N  
ATOM   3941  CA  VAL A 588      11.118  61.338 -44.399  1.00 39.80           C  
ANISOU 3941  CA  VAL A 588     5875   4339   4908    765   1005    660       C  
ATOM   3942  C   VAL A 588      11.678  62.180 -43.256  1.00 42.83           C  
ANISOU 3942  C   VAL A 588     6144   4693   5437    676   1070    586       C  
ATOM   3943  O   VAL A 588      11.095  63.184 -42.861  1.00 41.96           O  
ANISOU 3943  O   VAL A 588     6026   4560   5357    672   1109    594       O  
ATOM   3944  CB  VAL A 588      12.068  61.422 -45.617  1.00 36.55           C  
ANISOU 3944  CB  VAL A 588     5546   3843   4500    816   1148    694       C  
ATOM   3945  CG1 VAL A 588      13.487  61.041 -45.224  1.00 57.09           C  
ANISOU 3945  CG1 VAL A 588     8057   6423   7210    742   1194    618       C  
ATOM   3946  CG2 VAL A 588      11.586  60.518 -46.720  1.00 43.17           C  
ANISOU 3946  CG2 VAL A 588     6493   4718   5193    903   1077    754       C  
ATOM   3947  N   LEU A 589      12.824  61.755 -42.747  1.00 42.74           N  
ANISOU 3947  N   LEU A 589     6043   4686   5511    610   1079    510       N  
ATOM   3948  CA  LEU A 589      13.458  62.367 -41.610  1.00 13.03           C  
ANISOU 3948  CA  LEU A 589     2153    915   1882    523   1119    419       C  
ATOM   3949  C   LEU A 589      14.902  61.936 -41.675  1.00 32.48           C  
ANISOU 3949  C   LEU A 589     4556   3361   4424    487   1176    354       C  
ATOM   3950  O   LEU A 589      15.193  60.758 -41.861  1.00 63.85           O  
ANISOU 3950  O   LEU A 589     8534   7386   8340    501   1089    354       O  
ATOM   3951  CB  LEU A 589      12.821  61.823 -40.344  1.00 46.12           C  
ANISOU 3951  CB  LEU A 589     6261   5212   6052    478    952    375       C  
ATOM   3952  CG  LEU A 589      13.311  62.326 -38.997  1.00 28.69           C  
ANISOU 3952  CG  LEU A 589     3916   3025   3960    394    954    273       C  
ATOM   3953  CD1 LEU A 589      12.930  63.789 -38.847  1.00110.10           C  
ANISOU 3953  CD1 LEU A 589    14229  13266  14338    381   1067    276       C  
ATOM   3954  CD2 LEU A 589      12.679  61.489 -37.899  1.00 55.80           C  
ANISOU 3954  CD2 LEU A 589     7291   6569   7340    371    776    247       C  
ATOM   3955  N   ILE A 590      15.818  62.879 -41.533  1.00 37.28           N  
ANISOU 3955  N   ILE A 590     5106   3894   5167    440   1327    295       N  
ATOM   3956  CA  ILE A 590      17.227  62.572 -41.721  1.00 31.39           C  
ANISOU 3956  CA  ILE A 590     4301   3124   4504    410   1402    231       C  
ATOM   3957  C   ILE A 590      18.004  62.673 -40.421  1.00 20.30           C  
ANISOU 3957  C   ILE A 590     2728   1770   3217    321   1375     99       C  
ATOM   3958  O   ILE A 590      18.054  63.725 -39.787  1.00 49.57           O  
ANISOU 3958  O   ILE A 590     6367   5444   7024    268   1447     40       O  
ATOM   3959  CB  ILE A 590      17.866  63.492 -42.776  1.00 32.12           C  
ANISOU 3959  CB  ILE A 590     4458   3081   4665    429   1622    259       C  
ATOM   3960  CG1 ILE A 590      17.033  63.476 -44.062  1.00 32.39           C  
ANISOU 3960  CG1 ILE A 590     4668   3071   4568    534   1649    393       C  
ATOM   3961  CG2 ILE A 590      19.298  63.080 -43.046  1.00 27.43           C  
ANISOU 3961  CG2 ILE A 590     3805   2465   4152    402   1697    195       C  
ATOM   3962  CD1 ILE A 590      16.913  62.122 -44.691  1.00 34.52           C  
ANISOU 3962  CD1 ILE A 590     5002   3404   4711    591   1530    441       C  
ATOM   3963  N   LEU A 591      18.611  61.566 -40.025  1.00 43.63           N  
ANISOU 3963  N   LEU A 591     5616   4807   6156    312   1270     50       N  
ATOM   3964  CA  LEU A 591      19.419  61.543 -38.822  1.00 45.32           C  
ANISOU 3964  CA  LEU A 591     5667   5086   6466    245   1232    -80       C  
ATOM   3965  C   LEU A 591      20.813  62.051 -39.153  1.00 60.86           C  
ANISOU 3965  C   LEU A 591     7565   6988   8573    207   1393   -161       C  
ATOM   3966  O   LEU A 591      21.243  61.987 -40.305  1.00 27.47           O  
ANISOU 3966  O   LEU A 591     3416   2682   4341    241   1500   -109       O  
ATOM   3967  CB  LEU A 591      19.467  60.126 -38.247  1.00 57.32           C  
ANISOU 3967  CB  LEU A 591     7152   6723   7903    265   1055    -95       C  
ATOM   3968  CG  LEU A 591      18.087  59.523 -37.969  1.00 43.88           C  
ANISOU 3968  CG  LEU A 591     5523   5082   6069    300    904    -16       C  
ATOM   3969  CD1 LEU A 591      18.221  58.159 -37.347  1.00 12.10           C  
ANISOU 3969  CD1 LEU A 591     1463   1160   1975    317    752    -36       C  
ATOM   3970  CD2 LEU A 591      17.258  60.440 -37.071  1.00 35.64           C  
ANISOU 3970  CD2 LEU A 591     4441   4050   5052    263    884    -37       C  
ATOM   3971  N   PRO A 592      21.512  62.586 -38.145  1.00 56.75           N  
ANISOU 3971  N   PRO A 592     6890   6496   8175    136   1414   -295       N  
ATOM   3972  CA  PRO A 592      22.864  63.130 -38.300  1.00 29.58           C  
ANISOU 3972  CA  PRO A 592     3352   3001   4887     84   1567   -400       C  
ATOM   3973  C   PRO A 592      23.859  62.017 -38.558  1.00 36.75           C  
ANISOU 3973  C   PRO A 592     4221   3963   5781    109   1525   -430       C  
ATOM   3974  O   PRO A 592      24.949  62.258 -39.072  1.00 56.44           O  
ANISOU 3974  O   PRO A 592     6670   6398   8377     87   1660   -485       O  
ATOM   3975  CB  PRO A 592      23.149  63.755 -36.932  1.00 34.05           C  
ANISOU 3975  CB  PRO A 592     3754   3627   5558      8   1540   -545       C  
ATOM   3976  CG  PRO A 592      21.818  63.890 -36.265  1.00 27.40           C  
ANISOU 3976  CG  PRO A 592     2955   2828   4629     20   1424   -491       C  
ATOM   3977  CD  PRO A 592      21.000  62.757 -36.776  1.00 30.01           C  
ANISOU 3977  CD  PRO A 592     3413   3198   4791     99   1296   -359       C  
ATOM   3978  N   GLU A 593      23.479  60.798 -38.191  1.00 59.76           N  
ANISOU 3978  N   GLU A 593     7152   6983   8572    157   1343   -394       N  
ATOM   3979  CA  GLU A 593      24.353  59.644 -38.334  1.00 63.68           C  
ANISOU 3979  CA  GLU A 593     7614   7540   9042    190   1287   -418       C  
ATOM   3980  C   GLU A 593      23.542  58.368 -38.198  1.00 52.96           C  
ANISOU 3980  C   GLU A 593     6337   6262   7522    253   1108   -332       C  
ATOM   3981  O   GLU A 593      22.438  58.387 -37.655  1.00 55.40           O  
ANISOU 3981  O   GLU A 593     6682   6606   7760    257   1011   -290       O  
ATOM   3982  CB  GLU A 593      25.461  59.679 -37.284  1.00 82.98           C  
ANISOU 3982  CB  GLU A 593     9866  10068  11593    146   1264   -580       C  
ATOM   3983  CG  GLU A 593      24.960  59.951 -35.878  1.00109.92           C  
ANISOU 3983  CG  GLU A 593    13187  13573  15006    116   1149   -650       C  
ATOM   3984  CD  GLU A 593      26.087  60.106 -34.886  1.00124.05           C  
ANISOU 3984  CD  GLU A 593    14781  15450  16904     77   1136   -824       C  
ATOM   3985  OE1 GLU A 593      27.256  59.918 -35.283  1.00119.49           O  
ANISOU 3985  OE1 GLU A 593    14134  14866  16399     74   1208   -890       O  
ATOM   3986  OE2 GLU A 593      25.807  60.416 -33.710  1.00140.34           O1-
ANISOU 3986  OE2 GLU A 593    16756  17590  18977     53   1053   -899       O1-
ATOM   3987  N   GLU A 594      24.090  57.265 -38.696  1.00 54.08           N  
ANISOU 3987  N   GLU A 594     6507   6428   7611    301   1074   -308       N  
ATOM   3988  CA  GLU A 594      23.397  55.983 -38.642  1.00 55.86           C  
ANISOU 3988  CA  GLU A 594     6815   6719   7691    359    921   -230       C  
ATOM   3989  C   GLU A 594      23.273  55.483 -37.203  1.00 50.38           C  
ANISOU 3989  C   GLU A 594     6023   6146   6971    356    771   -294       C  
ATOM   3990  O   GLU A 594      24.191  55.628 -36.392  1.00 48.15           O  
ANISOU 3990  O   GLU A 594     5600   5926   6771    335    766   -410       O  
ATOM   3991  CB  GLU A 594      24.102  54.946 -39.517  1.00 55.45           C  
ANISOU 3991  CB  GLU A 594     6816   6657   7597    409    934   -196       C  
ATOM   3992  CG  GLU A 594      23.384  53.610 -39.582  1.00100.72           C  
ANISOU 3992  CG  GLU A 594    12646  12440  13184    466    795   -115       C  
ATOM   3993  CD  GLU A 594      24.090  52.604 -40.470  1.00115.35           C  
ANISOU 3993  CD  GLU A 594    14554  14276  14997    516    815    -84       C  
ATOM   3994  OE1 GLU A 594      25.139  52.950 -41.055  1.00 88.35           O  
ANISOU 3994  OE1 GLU A 594    11099  10809  11663    509    937   -122       O  
ATOM   3995  OE2 GLU A 594      23.592  51.463 -40.582  1.00126.31           O1-
ANISOU 3995  OE2 GLU A 594    16022  15697  16273    560    715    -25       O1-
ATOM   3996  N   VAL A 595      22.129  54.890 -36.890  1.00 46.16           N  
ANISOU 3996  N   VAL A 595     5567   5650   6323    382    650   -221       N  
ATOM   3997  CA  VAL A 595      21.852  54.451 -35.531  1.00 40.73           C  
ANISOU 3997  CA  VAL A 595     4808   5068   5600    386    515   -266       C  
ATOM   3998  C   VAL A 595      21.775  52.928 -35.434  1.00 41.97           C  
ANISOU 3998  C   VAL A 595     5018   5284   5646    448    402   -221       C  
ATOM   3999  O   VAL A 595      21.514  52.249 -36.424  1.00 53.45           O  
ANISOU 3999  O   VAL A 595     6586   6692   7031    480    410   -137       O  
ATOM   4000  CB  VAL A 595      20.555  55.087 -35.024  1.00 30.02           C  
ANISOU 4000  CB  VAL A 595     3483   3709   4215    359    474   -231       C  
ATOM   4001  CG1 VAL A 595      20.242  54.612 -33.624  1.00 84.03           C  
ANISOU 4001  CG1 VAL A 595    10260  10655  11013    368    341   -272       C  
ATOM   4002  CG2 VAL A 595      20.682  56.595 -35.061  1.00 34.35           C  
ANISOU 4002  CG2 VAL A 595     3978   4195   4878    300    594   -280       C  
ATOM   4003  N   GLU A 596      22.014  52.396 -34.239  1.00 59.70           N  
ANISOU 4003  N   GLU A 596     7182   7629   7871    469    302   -279       N  
ATOM   4004  CA  GLU A 596      21.948  50.955 -34.017  1.00 49.44           C  
ANISOU 4004  CA  GLU A 596     5934   6383   6469    533    203   -237       C  
ATOM   4005  C   GLU A 596      20.511  50.481 -33.783  1.00 41.79           C  
ANISOU 4005  C   GLU A 596     5067   5414   5397    539    117   -151       C  
ATOM   4006  O   GLU A 596      20.175  49.336 -34.077  1.00 53.13           O  
ANISOU 4006  O   GLU A 596     6595   6849   6745    580     68    -86       O  
ATOM   4007  CB  GLU A 596      22.860  50.547 -32.862  1.00 64.41           C  
ANISOU 4007  CB  GLU A 596     7707   8387   8378    570    139   -332       C  
ATOM   4008  CG  GLU A 596      24.332  50.839 -33.121  1.00 94.69           C  
ANISOU 4008  CG  GLU A 596    11433  12233  12312    570    216   -426       C  
ATOM   4009  CD  GLU A 596      25.211  50.545 -31.922  1.00138.43           C  
ANISOU 4009  CD  GLU A 596    16835  17896  17864    613    145   -535       C  
ATOM   4010  OE1 GLU A 596      24.671  50.133 -30.872  1.00161.64           O  
ANISOU 4010  OE1 GLU A 596    19774  20911  20732    648     39   -531       O  
ATOM   4011  OE2 GLU A 596      26.441  50.727 -32.028  1.00142.76           O1-
ANISOU 4011  OE2 GLU A 596    17276  18471  18494    617    196   -627       O1-
ATOM   4012  N   TRP A 597      19.669  51.368 -33.259  1.00 37.87           N  
ANISOU 4012  N   TRP A 597     4553   4916   4918    496    107   -155       N  
ATOM   4013  CA  TRP A 597      18.241  51.091 -33.131  1.00 27.19           C  
ANISOU 4013  CA  TRP A 597     3292   3555   3483    492     41    -77       C  
ATOM   4014  C   TRP A 597      17.454  52.379 -32.955  1.00 36.31           C  
ANISOU 4014  C   TRP A 597     4431   4683   4683    439     73    -80       C  
ATOM   4015  O   TRP A 597      17.947  53.328 -32.349  1.00 61.29           O  
ANISOU 4015  O   TRP A 597     7491   7865   7931    408    108   -160       O  
ATOM   4016  CB  TRP A 597      17.963  50.137 -31.959  1.00 36.57           C  
ANISOU 4016  CB  TRP A 597     4469   4825   4600    529    -70    -82       C  
ATOM   4017  CG  TRP A 597      18.476  50.610 -30.618  1.00 41.24           C  
ANISOU 4017  CG  TRP A 597     4934   5500   5236    530   -104   -177       C  
ATOM   4018  CD1 TRP A 597      19.632  50.230 -30.004  1.00 26.37           C  
ANISOU 4018  CD1 TRP A 597     2960   3689   3370    574   -125   -253       C  
ATOM   4019  CD2 TRP A 597      17.840  51.538 -29.726  1.00 47.05           C  
ANISOU 4019  CD2 TRP A 597     5616   6261   5999    492   -124   -210       C  
ATOM   4020  CE2 TRP A 597      18.675  51.673 -28.597  1.00 28.91           C  
ANISOU 4020  CE2 TRP A 597     3197   4054   3733    513   -159   -311       C  
ATOM   4021  CE3 TRP A 597      16.648  52.270 -29.775  1.00 53.89           C  
ANISOU 4021  CE3 TRP A 597     6524   7086   6864    446   -117   -168       C  
ATOM   4022  NE1 TRP A 597      19.759  50.861 -28.792  1.00 35.29           N  
ANISOU 4022  NE1 TRP A 597     3982   4893   4532    566   -161   -336       N  
ATOM   4023  CZ2 TRP A 597      18.359  52.511 -27.529  1.00 25.86           C  
ANISOU 4023  CZ2 TRP A 597     2734   3715   3378    487   -185   -372       C  
ATOM   4024  CZ3 TRP A 597      16.337  53.104 -28.711  1.00 43.61           C  
ANISOU 4024  CZ3 TRP A 597     5148   5826   5597    418   -139   -223       C  
ATOM   4025  CH2 TRP A 597      17.190  53.215 -27.606  1.00 47.32           C  
ANISOU 4025  CH2 TRP A 597     5500   6382   6097    437   -171   -325       C  
ATOM   4026  N   ILE A 598      16.235  52.415 -33.489  1.00 38.18           N  
ANISOU 4026  N   ILE A 598     4766   4877   4863    431     61      1       N  
ATOM   4027  CA  ILE A 598      15.332  53.544 -33.256  1.00 39.46           C  
ANISOU 4027  CA  ILE A 598     4922   5019   5053    391     79      8       C  
ATOM   4028  C   ILE A 598      13.953  53.064 -32.811  1.00 31.97           C  
ANISOU 4028  C   ILE A 598     4030   4096   4020    394    -14     63       C  
ATOM   4029  O   ILE A 598      13.430  52.092 -33.348  1.00 29.80           O  
ANISOU 4029  O   ILE A 598     3842   3813   3667    419    -55    123       O  
ATOM   4030  CB  ILE A 598      15.192  54.464 -34.500  1.00 32.99           C  
ANISOU 4030  CB  ILE A 598     4159   4108   4266    380    188     49       C  
ATOM   4031  CG1 ILE A 598      14.414  55.726 -34.137  1.00 42.56           C  
ANISOU 4031  CG1 ILE A 598     5352   5300   5518    344    218     46       C  
ATOM   4032  CG2 ILE A 598      14.497  53.744 -35.645  1.00 11.28           C  
ANISOU 4032  CG2 ILE A 598     1537   1323   1425    414    173    140       C  
ATOM   4033  CD1 ILE A 598      14.096  56.614 -35.324  1.00 31.96           C  
ANISOU 4033  CD1 ILE A 598     4082   3869   4190    348    323    101       C  
ATOM   4034  N   LYS A 599      13.378  53.749 -31.824  1.00 23.78           N  
ANISOU 4034  N   LYS A 599     2942   3090   3005    367    -41     36       N  
ATOM   4035  CA  LYS A 599      12.077  53.377 -31.271  1.00 39.37           C  
ANISOU 4035  CA  LYS A 599     4957   5092   4912    365   -122     79       C  
ATOM   4036  C   LYS A 599      11.112  54.551 -31.240  1.00 39.93           C  
ANISOU 4036  C   LYS A 599     5029   5136   5007    332    -96     95       C  
ATOM   4037  O   LYS A 599      11.411  55.595 -30.662  1.00 42.43           O  
ANISOU 4037  O   LYS A 599     5270   5456   5396    305    -57     39       O  
ATOM   4038  CB  LYS A 599      12.233  52.824 -29.855  1.00 38.97           C  
ANISOU 4038  CB  LYS A 599     4846   5119   4842    377   -199     34       C  
ATOM   4039  CG  LYS A 599      10.992  52.982 -28.975  1.00 29.93           C  
ANISOU 4039  CG  LYS A 599     3706   4001   3664    360   -257     52       C  
ATOM   4040  CD  LYS A 599      10.329  51.644 -28.696  1.00 54.34           C  
ANISOU 4040  CD  LYS A 599     6864   7115   6669    386   -330    100       C  
ATOM   4041  CE  LYS A 599       9.369  51.722 -27.516  1.00 47.49           C  
ANISOU 4041  CE  LYS A 599     5980   6287   5777    375   -384    100       C  
ATOM   4042  NZ  LYS A 599       8.075  52.376 -27.850  1.00 47.67           N1+
ANISOU 4042  NZ  LYS A 599     6037   6273   5803    333   -367    134       N1+
ATOM   4043  N   PHE A 600       9.945  54.369 -31.847  1.00 33.02           N  
ANISOU 4043  N   PHE A 600     4236   4238   4072    337   -119    165       N  
ATOM   4044  CA  PHE A 600       8.925  55.412 -31.870  1.00 44.36           C  
ANISOU 4044  CA  PHE A 600     5681   5654   5520    319   -100    188       C  
ATOM   4045  C   PHE A 600       7.881  55.219 -30.776  1.00 57.47           C  
ANISOU 4045  C   PHE A 600     7324   7365   7148    304   -181    189       C  
ATOM   4046  O   PHE A 600       7.856  54.188 -30.109  1.00 44.01           O  
ANISOU 4046  O   PHE A 600     5617   5704   5402    311   -250    183       O  
ATOM   4047  CB  PHE A 600       8.247  55.470 -33.242  1.00 21.77           C  
ANISOU 4047  CB  PHE A 600     2915   2745   2612    343    -73    258       C  
ATOM   4048  CG  PHE A 600       9.042  56.196 -34.282  1.00 33.34           C  
ANISOU 4048  CG  PHE A 600     4400   4145   4122    358     36    264       C  
ATOM   4049  CD1 PHE A 600      10.168  55.613 -34.845  1.00 43.87           C  
ANISOU 4049  CD1 PHE A 600     5743   5462   5465    374     70    251       C  
ATOM   4050  CD2 PHE A 600       8.665  57.461 -34.701  1.00 33.43           C  
ANISOU 4050  CD2 PHE A 600     4427   4108   4166    360    113    285       C  
ATOM   4051  CE1 PHE A 600      10.903  56.285 -35.805  1.00 45.32           C  
ANISOU 4051  CE1 PHE A 600     5947   5579   5692    387    182    258       C  
ATOM   4052  CE2 PHE A 600       9.395  58.131 -35.661  1.00 31.52           C  
ANISOU 4052  CE2 PHE A 600     4214   3797   3966    377    229    295       C  
ATOM   4053  CZ  PHE A 600      10.516  57.546 -36.213  1.00 22.38           C  
ANISOU 4053  CZ  PHE A 600     3063   2621   2821    388    265    281       C  
ATOM   4054  N   ASN A 601       7.026  56.224 -30.604  1.00 49.98           N  
ANISOU 4054  N   ASN A 601     6368   6405   6218    286   -165    201       N  
ATOM   4055  CA  ASN A 601       5.977  56.184 -29.596  1.00 27.35           C  
ANISOU 4055  CA  ASN A 601     3484   3581   3327    270   -231    203       C  
ATOM   4056  C   ASN A 601       6.552  56.028 -28.193  1.00 41.65           C  
ANISOU 4056  C   ASN A 601     5218   5446   5163    259   -265    139       C  
ATOM   4057  O   ASN A 601       6.129  55.160 -27.431  1.00 21.74           O  
ANISOU 4057  O   ASN A 601     2701   2967   2592    265   -334    144       O  
ATOM   4058  CB  ASN A 601       4.996  55.050 -29.899  1.00 53.08           C  
ANISOU 4058  CB  ASN A 601     6807   6853   6507    277   -293    246       C  
ATOM   4059  CG  ASN A 601       3.716  55.152 -29.093  1.00 41.64           C  
ANISOU 4059  CG  ASN A 601     5343   5421   5056    242   -312    232       C  
ATOM   4060  ND2 ASN A 601       2.775  54.252 -29.358  1.00 64.26           N  
ANISOU 4060  ND2 ASN A 601     8246   8278   7892    224   -325    234       N  
ATOM   4061  OD1 ASN A 601       3.574  56.028 -28.247  1.00 19.37           O  
ANISOU 4061  OD1 ASN A 601     2474   2619   2265    233   -316    219       O  
ATOM   4062  N   VAL A 602       7.517  56.881 -27.860  1.00 48.44           N  
ANISOU 4062  N   VAL A 602     6005   6303   6097    245   -211     75       N  
ATOM   4063  CA  VAL A 602       8.210  56.810 -26.576  1.00 52.26           C  
ANISOU 4063  CA  VAL A 602     6405   6847   6603    243   -243     -1       C  
ATOM   4064  C   VAL A 602       7.255  56.988 -25.399  1.00 40.88           C  
ANISOU 4064  C   VAL A 602     4943   5449   5139    233   -297     -5       C  
ATOM   4065  O   VAL A 602       6.363  57.833 -25.430  1.00 49.63           O  
ANISOU 4065  O   VAL A 602     6061   6533   6265    210   -276     16       O  
ATOM   4066  CB  VAL A 602       9.367  57.841 -26.493  1.00 31.83           C  
ANISOU 4066  CB  VAL A 602     3733   4248   4113    221   -168    -84       C  
ATOM   4067  CG1 VAL A 602       9.959  57.880 -25.099  1.00 24.77           C  
ANISOU 4067  CG1 VAL A 602     2742   3431   3238    222   -210   -175       C  
ATOM   4068  CG2 VAL A 602      10.442  57.498 -27.520  1.00 84.62           C  
ANISOU 4068  CG2 VAL A 602    10431  10899  10820    235   -116    -87       C  
ATOM   4069  N   GLY A 603       7.444  56.174 -24.365  1.00 52.26           N  
ANISOU 4069  N   GLY A 603     6362   6955   6539    257   -364    -30       N  
ATOM   4070  CA  GLY A 603       6.593  56.212 -23.188  1.00 47.24           C  
ANISOU 4070  CA  GLY A 603     5719   6356   5875    252   -404    -35       C  
ATOM   4071  C   GLY A 603       5.264  55.524 -23.426  1.00 37.42           C  
ANISOU 4071  C   GLY A 603     4570   5068   4579    238   -395     33       C  
ATOM   4072  O   GLY A 603       4.493  55.301 -22.490  1.00 40.40           O  
ANISOU 4072  O   GLY A 603     4960   5455   4935    231   -400     33       O  
ATOM   4073  N   MET A 604       5.004  55.184 -24.686  1.00 43.68           N  
ANISOU 4073  N   MET A 604     5420   5816   5360    234   -380     85       N  
ATOM   4074  CA  MET A 604       3.738  54.575 -25.077  1.00 42.46           C  
ANISOU 4074  CA  MET A 604     5332   5624   5177    212   -371    128       C  
ATOM   4075  C   MET A 604       2.602  55.593 -24.943  1.00 58.40           C  
ANISOU 4075  C   MET A 604     7341   7635   7214    185   -362    143       C  
ATOM   4076  O   MET A 604       1.431  55.234 -24.846  1.00 48.20           O  
ANISOU 4076  O   MET A 604     6076   6329   5909    165   -362    161       O  
ATOM   4077  CB  MET A 604       3.465  53.332 -24.230  1.00 45.03           C  
ANISOU 4077  CB  MET A 604     5681   5959   5471    217   -384    122       C  
ATOM   4078  CG  MET A 604       2.242  52.539 -24.637  1.00 64.82           C  
ANISOU 4078  CG  MET A 604     8239   8430   7962    193   -381    153       C  
ATOM   4079  SD  MET A 604       2.079  51.029 -23.673  1.00 81.67           S  
ANISOU 4079  SD  MET A 604    10401  10569  10062    208   -394    152       S  
ATOM   4080  CE  MET A 604       2.312  51.654 -22.016  1.00 45.30           C  
ANISOU 4080  CE  MET A 604     5744   6013   5454    229   -402    121       C  
ATOM   4081  N   ASN A 605       2.963  56.871 -24.960  1.00 38.31           N  
ANISOU 4081  N   ASN A 605     4750   5099   4707    189   -355    133       N  
ATOM   4082  CA  ASN A 605       2.005  57.949 -24.745  1.00 44.89           C  
ANISOU 4082  CA  ASN A 605     5568   5927   5561    173   -345    145       C  
ATOM   4083  C   ASN A 605       1.097  58.249 -25.942  1.00 47.52           C  
ANISOU 4083  C   ASN A 605     5952   6224   5880    177   -326    200       C  
ATOM   4084  O   ASN A 605       0.086  58.933 -25.803  1.00 67.30           O  
ANISOU 4084  O   ASN A 605     8455   8726   8390    168   -319    216       O  
ATOM   4085  CB  ASN A 605       2.736  59.223 -24.319  1.00 40.20           C  
ANISOU 4085  CB  ASN A 605     4898   5343   5034    172   -322    100       C  
ATOM   4086  CG  ASN A 605       3.499  59.050 -23.022  1.00 41.74           C  
ANISOU 4086  CG  ASN A 605     5026   5594   5241    171   -352     28       C  
ATOM   4087  ND2 ASN A 605       4.780  59.400 -23.038  1.00 50.42           N  
ANISOU 4087  ND2 ASN A 605     6072   6692   6392    168   -313    -37       N  
ATOM   4088  OD1 ASN A 605       2.941  58.613 -22.014  1.00 54.33           O  
ANISOU 4088  OD1 ASN A 605     6634   7211   6798    168   -372     20       O  
ATOM   4089  N   GLY A 606       1.457  57.738 -27.112  1.00 28.76           N  
ANISOU 4089  N   GLY A 606     3621   3823   3483    195   -315    225       N  
ATOM   4090  CA  GLY A 606       0.697  58.006 -28.318  1.00 42.57           C  
ANISOU 4090  CA  GLY A 606     5419   5544   5210    211   -294    268       C  
ATOM   4091  C   GLY A 606      -0.317  56.932 -28.666  1.00 50.20           C  
ANISOU 4091  C   GLY A 606     6418   6513   6142    193   -316    264       C  
ATOM   4092  O   GLY A 606      -0.079  55.739 -28.455  1.00 29.57           O  
ANISOU 4092  O   GLY A 606     3815   3902   3517    179   -334    245       O  
ATOM   4093  N   TYR A 607      -1.447  57.364 -29.223  1.00 38.67           N  
ANISOU 4093  N   TYR A 607     4973   5053   4667    202   -315    284       N  
ATOM   4094  CA  TYR A 607      -2.563  56.468 -29.516  1.00 31.73           C  
ANISOU 4094  CA  TYR A 607     4111   4183   3762    187   -344    278       C  
ATOM   4095  C   TYR A 607      -2.413  55.804 -30.874  1.00 28.61           C  
ANISOU 4095  C   TYR A 607     3765   3776   3330    215   -349    286       C  
ATOM   4096  O   TYR A 607      -3.262  55.947 -31.753  1.00 50.75           O  
ANISOU 4096  O   TYR A 607     6591   6589   6104    240   -359    299       O  
ATOM   4097  CB  TYR A 607      -3.888  57.229 -29.439  1.00 20.46           C  
ANISOU 4097  CB  TYR A 607     2668   2774   2333    191   -350    290       C  
ATOM   4098  CG  TYR A 607      -5.111  56.340 -29.425  1.00 23.14           C  
ANISOU 4098  CG  TYR A 607     3007   3129   2656    168   -386    278       C  
ATOM   4099  CD1 TYR A 607      -5.381  55.515 -28.345  1.00 24.16           C  
ANISOU 4099  CD1 TYR A 607     3119   3261   2802    125   -401    260       C  
ATOM   4100  CD2 TYR A 607      -6.002  56.336 -30.487  1.00 34.40           C  
ANISOU 4100  CD2 TYR A 607     4454   4572   4046    198   -406    288       C  
ATOM   4101  CE1 TYR A 607      -6.503  54.705 -28.329  1.00 40.98           C  
ANISOU 4101  CE1 TYR A 607     5249   5402   4919    104   -431    254       C  
ATOM   4102  CE2 TYR A 607      -7.120  55.533 -30.479  1.00 21.57           C  
ANISOU 4102  CE2 TYR A 607     2821   2967   2407    177   -444    274       C  
ATOM   4103  CZ  TYR A 607      -7.368  54.717 -29.401  1.00 38.48           C  
ANISOU 4103  CZ  TYR A 607     4943   5104   4572    126   -455    258       C  
ATOM   4104  OH  TYR A 607      -8.484  53.916 -29.400  1.00 34.92           O  
ANISOU 4104  OH  TYR A 607     4487   4674   4110    104   -491    247       O  
ATOM   4105  N   TYR A 608      -1.315  55.077 -31.040  1.00 47.25           N  
ANISOU 4105  N   TYR A 608     6143   6120   5689    216   -343    278       N  
ATOM   4106  CA  TYR A 608      -1.034  54.380 -32.285  1.00 45.65           C  
ANISOU 4106  CA  TYR A 608     5990   5903   5451    242   -346    284       C  
ATOM   4107  C   TYR A 608      -0.066  53.228 -32.045  1.00 29.57           C  
ANISOU 4107  C   TYR A 608     3964   3854   3416    229   -351    267       C  
ATOM   4108  O   TYR A 608       0.688  53.232 -31.074  1.00 35.36           O  
ANISOU 4108  O   TYR A 608     4667   4591   4176    216   -345    255       O  
ATOM   4109  CB  TYR A 608      -0.446  55.345 -33.314  1.00 22.93           C  
ANISOU 4109  CB  TYR A 608     3145   3010   2559    295   -304    318       C  
ATOM   4110  CG  TYR A 608       0.762  56.102 -32.820  1.00 27.71           C  
ANISOU 4110  CG  TYR A 608     3729   3598   3201    299   -265    329       C  
ATOM   4111  CD1 TYR A 608       2.038  55.575 -32.948  1.00 44.08           C  
ANISOU 4111  CD1 TYR A 608     5812   5656   5280    305   -252    326       C  
ATOM   4112  CD2 TYR A 608       0.628  57.352 -32.237  1.00 39.17           C  
ANISOU 4112  CD2 TYR A 608     5150   5049   4685    302   -242    345       C  
ATOM   4113  CE1 TYR A 608       3.148  56.274 -32.500  1.00 34.45           C  
ANISOU 4113  CE1 TYR A 608     4567   4423   4101    314   -221    336       C  
ATOM   4114  CE2 TYR A 608       1.729  58.055 -31.789  1.00 39.78           C  
ANISOU 4114  CE2 TYR A 608     5205   5104   4805    309   -208    356       C  
ATOM   4115  CZ  TYR A 608       2.985  57.515 -31.922  1.00 33.86           C  
ANISOU 4115  CZ  TYR A 608     4460   4341   4066    315   -200    351       C  
ATOM   4116  OH  TYR A 608       4.079  58.220 -31.472  1.00 35.91           O  
ANISOU 4116  OH  TYR A 608     4666   4577   4402    297   -135    307       O  
ATOM   4117  N   ILE A 609      -0.101  52.234 -32.927  1.00 33.54           N  
ANISOU 4117  N   ILE A 609     4511   4346   3887    238   -366    264       N  
ATOM   4118  CA  ILE A 609       0.902  51.178 -32.895  1.00 53.70           C  
ANISOU 4118  CA  ILE A 609     7085   6883   6436    238   -366    254       C  
ATOM   4119  C   ILE A 609       1.909  51.370 -34.027  1.00 28.86           C  
ANISOU 4119  C   ILE A 609     3977   3719   3269    281   -336    272       C  
ATOM   4120  O   ILE A 609       1.552  51.761 -35.136  1.00 43.84           O  
ANISOU 4120  O   ILE A 609     5909   5612   5137    312   -328    289       O  
ATOM   4121  CB  ILE A 609       0.280  49.762 -32.947  1.00 35.53           C  
ANISOU 4121  CB  ILE A 609     4812   4575   4114    216   -399    241       C  
ATOM   4122  CG1 ILE A 609      -0.528  49.561 -34.216  1.00 65.19           C  
ANISOU 4122  CG1 ILE A 609     8607   8332   7831    232   -420    244       C  
ATOM   4123  CG2 ILE A 609      -0.620  49.525 -31.751  1.00 56.89           C  
ANISOU 4123  CG2 ILE A 609     7484   7291   6840    177   -418    231       C  
ATOM   4124  CD1 ILE A 609      -1.040  48.160 -34.342  1.00 80.65           C  
ANISOU 4124  CD1 ILE A 609    10595  10281   9767    210   -454    230       C  
ATOM   4125  N   VAL A 610       3.174  51.110 -33.731  1.00 33.47           N  
ANISOU 4125  N   VAL A 610     4555   4296   3865    289   -319    269       N  
ATOM   4126  CA  VAL A 610       4.234  51.264 -34.717  1.00 55.98           C  
ANISOU 4126  CA  VAL A 610     7441   7126   6701    329   -284    290       C  
ATOM   4127  C   VAL A 610       4.815  49.908 -35.142  1.00 36.77           C  
ANISOU 4127  C   VAL A 610     5049   4680   4243    338   -294    280       C  
ATOM   4128  O   VAL A 610       4.954  48.994 -34.329  1.00 45.66           O  
ANISOU 4128  O   VAL A 610     6162   5813   5375    320   -316    260       O  
ATOM   4129  CB  VAL A 610       5.343  52.216 -34.202  1.00 29.86           C  
ANISOU 4129  CB  VAL A 610     4094   3818   3431    342   -251    302       C  
ATOM   4130  CG1 VAL A 610       5.648  51.945 -32.740  1.00 77.81           C  
ANISOU 4130  CG1 VAL A 610    10109   9923   9533    317   -280    272       C  
ATOM   4131  CG2 VAL A 610       6.597  52.095 -35.046  1.00 36.90           C  
ANISOU 4131  CG2 VAL A 610     5021   4683   4318    380   -211    325       C  
ATOM   4132  N   HIS A 611       5.131  49.782 -36.427  1.00 41.32           N  
ANISOU 4132  N   HIS A 611     5680   5233   4785    373   -272    298       N  
ATOM   4133  CA  HIS A 611       5.736  48.570 -36.964  1.00 44.62           C  
ANISOU 4133  CA  HIS A 611     6144   5634   5175    388   -275    293       C  
ATOM   4134  C   HIS A 611       7.059  48.908 -37.630  1.00 48.53           C  
ANISOU 4134  C   HIS A 611     6661   6107   5669    429   -224    319       C  
ATOM   4135  O   HIS A 611       7.145  49.888 -38.362  1.00 29.63           O  
ANISOU 4135  O   HIS A 611     4288   3698   3274    457   -182    349       O  
ATOM   4136  CB  HIS A 611       4.802  47.910 -37.977  1.00 25.38           C  
ANISOU 4136  CB  HIS A 611     3764   3189   2692    393   -301    289       C  
ATOM   4137  CG  HIS A 611       5.405  46.727 -38.669  1.00 40.97           C  
ANISOU 4137  CG  HIS A 611     5795   5140   4632    412   -300    286       C  
ATOM   4138  CD2 HIS A 611       5.327  46.311 -39.953  1.00 23.99           C  
ANISOU 4138  CD2 HIS A 611     3710   2974   2431    444   -299    292       C  
ATOM   4139  ND1 HIS A 611       6.192  45.805 -38.014  1.00 46.01           N  
ANISOU 4139  ND1 HIS A 611     6429   5771   5282    404   -301    276       N  
ATOM   4140  CE1 HIS A 611       6.579  44.877 -38.869  1.00 41.52           C  
ANISOU 4140  CE1 HIS A 611     5922   5179   4676    427   -297    279       C  
ATOM   4141  NE2 HIS A 611       6.066  45.161 -40.052  1.00 45.55           N  
ANISOU 4141  NE2 HIS A 611     6475   5683   5147    448   -297    287       N  
ATOM   4142  N   TYR A 612       8.089  48.105 -37.371  1.00 38.48           N  
ANISOU 4142  N   TYR A 612     5389   4831   4400    438   -221    313       N  
ATOM   4143  CA  TYR A 612       9.403  48.367 -37.952  1.00 40.81           C  
ANISOU 4143  CA  TYR A 612     5701   5104   4702    478   -170    340       C  
ATOM   4144  C   TYR A 612       9.686  47.520 -39.193  1.00 49.48           C  
ANISOU 4144  C   TYR A 612     6877   6172   5753    508   -152    350       C  
ATOM   4145  O   TYR A 612       9.719  46.289 -39.141  1.00 31.23           O  
ANISOU 4145  O   TYR A 612     4588   3860   3417    505   -181    331       O  
ATOM   4146  CB  TYR A 612      10.513  48.211 -36.907  1.00 31.22           C  
ANISOU 4146  CB  TYR A 612     4430   3909   3523    484   -176    331       C  
ATOM   4147  CG  TYR A 612      10.311  49.091 -35.699  1.00 35.24           C  
ANISOU 4147  CG  TYR A 612     4862   4451   4075    462   -197    318       C  
ATOM   4148  CD1 TYR A 612       9.675  48.603 -34.566  1.00 30.03           C  
ANISOU 4148  CD1 TYR A 612     4169   3829   3414    432   -246    284       C  
ATOM   4149  CD2 TYR A 612      10.728  50.418 -35.698  1.00 30.96           C  
ANISOU 4149  CD2 TYR A 612     4270   3894   3600    453   -135    303       C  
ATOM   4150  CE1 TYR A 612       9.469  49.403 -33.460  1.00 48.02           C  
ANISOU 4150  CE1 TYR A 612     6380   6140   5727    414   -264    268       C  
ATOM   4151  CE2 TYR A 612      10.525  51.227 -34.596  1.00 49.31           C  
ANISOU 4151  CE2 TYR A 612     6517   6248   5972    425   -145    271       C  
ATOM   4152  CZ  TYR A 612       9.894  50.713 -33.477  1.00 50.03           C  
ANISOU 4152  CZ  TYR A 612     6587   6387   6037    412   -222    262       C  
ATOM   4153  OH  TYR A 612       9.686  51.504 -32.371  1.00 49.39           O  
ANISOU 4153  OH  TYR A 612     6432   6337   5997    388   -233    229       O  
ATOM   4154  N   GLU A 613       9.881  48.212 -40.310  1.00 60.48           N  
ANISOU 4154  N   GLU A 613     8314   7534   7132    543    -99    384       N  
ATOM   4155  CA  GLU A 613      10.228  47.591 -41.579  1.00 41.95           C  
ANISOU 4155  CA  GLU A 613     6046   5158   4737    581    -72    398       C  
ATOM   4156  C   GLU A 613      11.590  46.910 -41.470  1.00 37.11           C  
ANISOU 4156  C   GLU A 613     5433   4528   4139    599    -48    404       C  
ATOM   4157  O   GLU A 613      12.277  47.044 -40.456  1.00 62.55           O  
ANISOU 4157  O   GLU A 613     8592   7764   7408    589    -52    400       O  
ATOM   4158  CB  GLU A 613      10.250  48.660 -42.673  1.00125.46           C  
ANISOU 4158  CB  GLU A 613    16670  15701  15299    624     -4    440       C  
ATOM   4159  CG  GLU A 613      10.416  48.134 -44.085  1.00161.05           C  
ANISOU 4159  CG  GLU A 613    21268  20182  19743    674     23    455       C  
ATOM   4160  CD  GLU A 613       9.280  47.229 -44.502  1.00140.43           C  
ANISOU 4160  CD  GLU A 613    18692  17596  17068    670    -52    423       C  
ATOM   4161  OE1 GLU A 613       8.263  47.178 -43.774  1.00 60.58           O  
ANISOU 4161  OE1 GLU A 613     8535   7517   6966    629   -113    394       O  
ATOM   4162  OE2 GLU A 613       9.404  46.573 -45.556  1.00164.52           O1-
ANISOU 4162  OE2 GLU A 613    21815  20631  20063    707    -46    427       O1-
ATOM   4163  N   ASP A 614      11.982  46.188 -42.517  1.00 91.54           N  
ANISOU 4163  N   ASP A 614    12397  11394  10988    632    -25    414       N  
ATOM   4164  CA  ASP A 614      13.265  45.497 -42.529  1.00 95.44           C  
ANISOU 4164  CA  ASP A 614    12899  11870  11494    656      1    423       C  
ATOM   4165  C   ASP A 614      13.381  44.670 -41.264  1.00 92.96           C  
ANISOU 4165  C   ASP A 614    12533  11593  11196    633    -56    392       C  
ATOM   4166  O   ASP A 614      12.555  43.793 -41.009  1.00 94.39           O  
ANISOU 4166  O   ASP A 614    12730  11787  11346    609   -107    363       O  
ATOM   4167  CB  ASP A 614      14.420  46.495 -42.598  1.00111.39           C  
ANISOU 4167  CB  ASP A 614    14869  13863  13589    667     92    421       C  
ATOM   4168  CG  ASP A 614      14.170  47.614 -43.591  1.00150.64           C  
ANISOU 4168  CG  ASP A 614    19882  18795  18559    687    164    453       C  
ATOM   4169  OD1 ASP A 614      13.404  48.542 -43.260  1.00165.70           O  
ANISOU 4169  OD1 ASP A 614    21766  20712  20480    669    156    459       O  
ATOM   4170  OD2 ASP A 614      14.748  47.572 -44.697  1.00164.85           O1-
ANISOU 4170  OD2 ASP A 614    21742  20551  20341    726    233    473       O1-
ATOM   4171  N   ASP A 615      14.399  44.953 -40.460  1.00 32.48           N  
ANISOU 4171  N   ASP A 615     4798   3947   3595    638    -35    376       N  
ATOM   4172  CA  ASP A 615      14.517  44.285 -39.173  1.00100.45           C  
ANISOU 4172  CA  ASP A 615    13357  12599  12209    633    -91    352       C  
ATOM   4173  C   ASP A 615      14.945  45.237 -38.068  1.00 86.29           C  
ANISOU 4173  C   ASP A 615    11452  10844  10489    617    -85    312       C  
ATOM   4174  O   ASP A 615      16.023  45.103 -37.487  1.00 48.30           O  
ANISOU 4174  O   ASP A 615     6576   6060   5717    637    -73    275       O  
ATOM   4175  CB  ASP A 615      15.445  43.071 -39.252  1.00167.71           C  
ANISOU 4175  CB  ASP A 615    21902  21113  20708    673    -86    347       C  
ATOM   4176  CG  ASP A 615      16.863  43.442 -39.625  1.00180.82           C  
ANISOU 4176  CG  ASP A 615    23517  22763  22424    700    -13    324       C  
ATOM   4177  OD1 ASP A 615      17.166  44.653 -39.701  1.00104.71           O  
ANISOU 4177  OD1 ASP A 615    13820  13119  12848    683     37    306       O  
ATOM   4178  OD2 ASP A 615      17.676  42.515 -39.839  1.00213.50           O1-
ANISOU 4178  OD2 ASP A 615    27678  26895  26546    739      0    322       O1-
ATOM   4179  N   GLY A 616      14.084  46.208 -37.788  1.00 65.09           N  
ANISOU 4179  N   GLY A 616     8744   8167   7822    582    -96    314       N  
ATOM   4180  CA  GLY A 616      14.266  47.068 -36.639  1.00 41.06           C  
ANISOU 4180  CA  GLY A 616     5599   5162   4840    560   -101    273       C  
ATOM   4181  C   GLY A 616      13.912  46.303 -35.380  1.00 54.17           C  
ANISOU 4181  C   GLY A 616     7238   6874   6471    563   -179    261       C  
ATOM   4182  O   GLY A 616      14.478  46.535 -34.311  1.00 61.53           O  
ANISOU 4182  O   GLY A 616     8085   7853   7439    569   -193    217       O  
ATOM   4183  N   TRP A 617      12.966  45.381 -35.516  1.00 46.62           N  
ANISOU 4183  N   TRP A 617     6358   5908   5448    559   -224    296       N  
ATOM   4184  CA  TRP A 617      12.597  44.496 -34.423  1.00 40.48           C  
ANISOU 4184  CA  TRP A 617     5570   5159   4652    554   -263    270       C  
ATOM   4185  C   TRP A 617      13.811  43.722 -33.935  1.00 49.70           C  
ANISOU 4185  C   TRP A 617     6722   6354   5807    614   -271    264       C  
ATOM   4186  O   TRP A 617      14.043  43.603 -32.732  1.00 54.83           O  
ANISOU 4186  O   TRP A 617     7321   7053   6459    636   -302    241       O  
ATOM   4187  CB  TRP A 617      11.527  43.509 -34.874  1.00 33.09           C  
ANISOU 4187  CB  TRP A 617     4708   4185   3681    526   -268    270       C  
ATOM   4188  CG  TRP A 617      10.181  44.121 -35.086  1.00 40.35           C  
ANISOU 4188  CG  TRP A 617     5629   5094   4610    474   -277    266       C  
ATOM   4189  CD1 TRP A 617       9.532  44.287 -36.277  1.00 56.53           C  
ANISOU 4189  CD1 TRP A 617     7724   7112   6642    461   -267    275       C  
ATOM   4190  CD2 TRP A 617       9.313  44.643 -34.079  1.00 24.60           C  
ANISOU 4190  CD2 TRP A 617     3586   3122   2638    439   -301    251       C  
ATOM   4191  CE2 TRP A 617       8.152  45.109 -34.729  1.00 28.64           C  
ANISOU 4191  CE2 TRP A 617     4115   3617   3150    404   -305    254       C  
ATOM   4192  CE3 TRP A 617       9.405  44.767 -32.689  1.00 21.71           C  
ANISOU 4192  CE3 TRP A 617     3165   2793   2289    440   -319    235       C  
ATOM   4193  NE1 TRP A 617       8.310  44.881 -36.070  1.00 18.20           N  
ANISOU 4193  NE1 TRP A 617     2850   2265   1800    422   -287    267       N  
ATOM   4194  CZ2 TRP A 617       7.093  45.688 -34.039  1.00 46.00           C  
ANISOU 4194  CZ2 TRP A 617     6277   5831   5371    367   -324    244       C  
ATOM   4195  CZ3 TRP A 617       8.348  45.339 -32.004  1.00 21.67           C  
ANISOU 4195  CZ3 TRP A 617     3130   2800   2305    401   -335    226       C  
ATOM   4196  CH2 TRP A 617       7.209  45.795 -32.680  1.00 41.53           C  
ANISOU 4196  CH2 TRP A 617     5661   5294   4825    362   -336    232       C  
ATOM   4197  N   ASP A 618      14.577  43.188 -34.879  1.00 48.41           N  
ANISOU 4197  N   ASP A 618     6604   6160   5628    649   -243    285       N  
ATOM   4198  CA  ASP A 618      15.786  42.448 -34.549  1.00 44.99           C  
ANISOU 4198  CA  ASP A 618     6150   5751   5194    707   -235    265       C  
ATOM   4199  C   ASP A 618      16.686  43.225 -33.603  1.00 38.98           C  
ANISOU 4199  C   ASP A 618     5268   5053   4491    723   -235    205       C  
ATOM   4200  O   ASP A 618      17.140  42.690 -32.600  1.00 35.82           O  
ANISOU 4200  O   ASP A 618     4833   4705   4071    772   -269    185       O  
ATOM   4201  CB  ASP A 618      16.552  42.082 -35.819  1.00 84.92           C  
ANISOU 4201  CB  ASP A 618    11253  10762  10249    728   -181    276       C  
ATOM   4202  CG  ASP A 618      15.884  40.972 -36.600  1.00101.41           C  
ANISOU 4202  CG  ASP A 618    13461  12800  12270    729   -189    322       C  
ATOM   4203  OD1 ASP A 618      14.776  40.553 -36.205  1.00 98.07           O  
ANISOU 4203  OD1 ASP A 618    13064  12371  11827    690   -211    310       O  
ATOM   4204  OD2 ASP A 618      16.467  40.516 -37.606  1.00 99.61           O1-
ANISOU 4204  OD2 ASP A 618    13282  12534  12030    751   -149    333       O1-
ATOM   4205  N   SER A 619      16.943  44.488 -33.930  1.00 40.23           N  
ANISOU 4205  N   SER A 619     5363   5206   4718    687   -193    174       N  
ATOM   4206  CA  SER A 619      17.783  45.335 -33.091  1.00 44.43           C  
ANISOU 4206  CA  SER A 619     5769   5795   5317    691   -186    102       C  
ATOM   4207  C   SER A 619      17.111  45.668 -31.760  1.00 56.68           C  
ANISOU 4207  C   SER A 619     7273   7401   6860    680   -247     82       C  
ATOM   4208  O   SER A 619      17.775  45.745 -30.728  1.00 52.43           O  
ANISOU 4208  O   SER A 619     6648   6934   6338    713   -274     24       O  
ATOM   4209  CB  SER A 619      18.159  46.617 -33.835  1.00 39.50           C  
ANISOU 4209  CB  SER A 619     5098   5134   4776    647   -109     74       C  
ATOM   4210  OG  SER A 619      17.026  47.176 -34.476  1.00 78.78           O  
ANISOU 4210  OG  SER A 619    10139  10056   9740    602    -94    124       O  
ATOM   4211  N   LEU A 620      15.796  45.863 -31.785  1.00 18.57           N  
ANISOU 4211  N   LEU A 620     2502   2548   2008    638   -268    126       N  
ATOM   4212  CA  LEU A 620      15.066  46.154 -30.558  1.00 41.44           C  
ANISOU 4212  CA  LEU A 620     5363   5490   4893    626   -321    114       C  
ATOM   4213  C   LEU A 620      15.077  44.960 -29.610  1.00 51.24           C  
ANISOU 4213  C   LEU A 620     6630   6772   6065    685   -374    126       C  
ATOM   4214  O   LEU A 620      15.349  45.110 -28.420  1.00 47.80           O  
ANISOU 4214  O   LEU A 620     6128   6405   5629    715   -410     84       O  
ATOM   4215  CB  LEU A 620      13.629  46.596 -30.855  1.00 22.58           C  
ANISOU 4215  CB  LEU A 620     3027   3061   2492    571   -328    159       C  
ATOM   4216  CG  LEU A 620      13.465  48.029 -31.376  1.00 44.38           C  
ANISOU 4216  CG  LEU A 620     5750   5795   5319    522   -280    144       C  
ATOM   4217  CD1 LEU A 620      11.996  48.333 -31.618  1.00 33.89           C  
ANISOU 4217  CD1 LEU A 620     4476   4438   3964    483   -297    191       C  
ATOM   4218  CD2 LEU A 620      14.085  49.054 -30.414  1.00 16.13           C  
ANISOU 4218  CD2 LEU A 620     2053   2266   1810    512   -271     69       C  
ATOM   4219  N   THR A 621      14.789  43.775 -30.139  1.00 35.26           N  
ANISOU 4219  N   THR A 621     4706   4705   3985    702   -371    176       N  
ATOM   4220  CA  THR A 621      14.803  42.569 -29.316  1.00 80.15           C  
ANISOU 4220  CA  THR A 621    10429  10406   9617    749   -381    177       C  
ATOM   4221  C   THR A 621      16.237  42.245 -28.915  1.00 63.74           C  
ANISOU 4221  C   THR A 621     8297   8392   7527    842   -404    154       C  
ATOM   4222  O   THR A 621      16.484  41.570 -27.916  1.00 50.60           O  
ANISOU 4222  O   THR A 621     6633   6773   5819    905   -423    142       O  
ATOM   4223  CB  THR A 621      14.166  41.363 -30.034  1.00 43.48           C  
ANISOU 4223  CB  THR A 621     5899   5687   4937    734   -350    216       C  
ATOM   4224  CG2 THR A 621      12.764  41.701 -30.477  1.00 66.67           C  
ANISOU 4224  CG2 THR A 621     8867   8572   7893    650   -339    225       C  
ATOM   4225  OG1 THR A 621      14.935  41.029 -31.188  1.00 71.96           O  
ANISOU 4225  OG1 THR A 621     9538   9264   8538    756   -328    234       O  
ATOM   4226  N   GLY A 622      17.181  42.739 -29.704  1.00 44.42           N  
ANISOU 4226  N   GLY A 622     5801   5942   5133    839   -370    123       N  
ATOM   4227  CA  GLY A 622      18.583  42.632 -29.357  1.00 33.49           C  
ANISOU 4227  CA  GLY A 622     4336   4621   3766    906   -369     65       C  
ATOM   4228  C   GLY A 622      18.889  43.609 -28.244  1.00 60.52           C  
ANISOU 4228  C   GLY A 622     7635   8130   7231    909   -399    -13       C  
ATOM   4229  O   GLY A 622      19.692  43.329 -27.357  1.00 60.24           O  
ANISOU 4229  O   GLY A 622     7535   8177   7176    985   -433    -61       O  
ATOM   4230  N   LEU A 623      18.235  44.763 -28.296  1.00 57.90           N  
ANISOU 4230  N   LEU A 623     7269   7778   6951    830   -388    -28       N  
ATOM   4231  CA  LEU A 623      18.413  45.794 -27.286  1.00 39.89           C  
ANISOU 4231  CA  LEU A 623     4872   5569   4716    818   -411   -106       C  
ATOM   4232  C   LEU A 623      17.844  45.332 -25.946  1.00 61.97           C  
ANISOU 4232  C   LEU A 623     7681   8425   7440    866   -479    -96       C  
ATOM   4233  O   LEU A 623      18.488  45.466 -24.907  1.00 48.75           O  
ANISOU 4233  O   LEU A 623     5919   6843   5759    922   -518   -165       O  
ATOM   4234  CB  LEU A 623      17.743  47.091 -27.739  1.00 32.29           C  
ANISOU 4234  CB  LEU A 623     3889   4555   3823    723   -371   -112       C  
ATOM   4235  CG  LEU A 623      17.473  48.151 -26.669  1.00 45.69           C  
ANISOU 4235  CG  LEU A 623     5496   6307   5558    695   -396   -175       C  
ATOM   4236  CD1 LEU A 623      18.767  48.796 -26.192  1.00 27.43           C  
ANISOU 4236  CD1 LEU A 623     3041   4066   3315    711   -386   -292       C  
ATOM   4237  CD2 LEU A 623      16.511  49.200 -27.193  1.00 10.09           C  
ANISOU 4237  CD2 LEU A 623     1009   1731   1095    610   -356   -148       C  
ATOM   4238  N   LEU A 624      16.636  44.778 -25.982  1.00 64.23           N  
ANISOU 4238  N   LEU A 624     8076   8660   7671    848   -491    -14       N  
ATOM   4239  CA  LEU A 624      15.951  44.341 -24.768  1.00 53.69           C  
ANISOU 4239  CA  LEU A 624     6773   7352   6274    874   -514     -7       C  
ATOM   4240  C   LEU A 624      16.634  43.161 -24.082  1.00 52.28           C  
ANISOU 4240  C   LEU A 624     6621   7221   6021    983   -532     -7       C  
ATOM   4241  O   LEU A 624      16.604  43.042 -22.857  1.00 54.86           O  
ANISOU 4241  O   LEU A 624     6929   7610   6304   1037   -557    -33       O  
ATOM   4242  CB  LEU A 624      14.496  43.988 -25.076  1.00 43.35           C  
ANISOU 4242  CB  LEU A 624     5571   5952   4950    805   -478     55       C  
ATOM   4243  CG  LEU A 624      13.594  45.194 -25.314  1.00 46.51           C  
ANISOU 4243  CG  LEU A 624     5944   6322   5406    713   -468     51       C  
ATOM   4244  CD1 LEU A 624      12.166  44.749 -25.524  1.00 45.70           C  
ANISOU 4244  CD1 LEU A 624     5929   6144   5291    657   -440     99       C  
ATOM   4245  CD2 LEU A 624      13.690  46.139 -24.133  1.00 54.02           C  
ANISOU 4245  CD2 LEU A 624     6803   7348   6376    720   -499     -9       C  
ATOM   4246  N   LYS A 625      17.244  42.287 -24.873  1.00 46.81           N  
ANISOU 4246  N   LYS A 625     5976   6500   5309   1024   -516     26       N  
ATOM   4247  CA  LYS A 625      17.915  41.118 -24.321  1.00 59.65           C  
ANISOU 4247  CA  LYS A 625     7637   8166   6861   1137   -526     36       C  
ATOM   4248  C   LYS A 625      19.284  41.477 -23.751  1.00 32.68           C  
ANISOU 4248  C   LYS A 625     4093   4871   3455   1226   -576    -43       C  
ATOM   4249  O   LYS A 625      19.785  40.808 -22.852  1.00 49.30           O  
ANISOU 4249  O   LYS A 625     6197   7044   5489   1335   -602    -57       O  
ATOM   4250  CB  LYS A 625      18.008  39.995 -25.362  1.00 28.54           C  
ANISOU 4250  CB  LYS A 625     3803   4147   2896   1149   -485    100       C  
ATOM   4251  CG  LYS A 625      16.639  39.502 -25.796  1.00 59.49           C  
ANISOU 4251  CG  LYS A 625     7837   7959   6807   1070   -439    157       C  
ATOM   4252  CD  LYS A 625      16.643  38.041 -26.196  1.00 64.66           C  
ANISOU 4252  CD  LYS A 625     8606   8552   7409   1115   -402    211       C  
ATOM   4253  CE  LYS A 625      17.053  37.862 -27.642  1.00 74.70           C  
ANISOU 4253  CE  LYS A 625     9909   9769   8706   1086   -377    230       C  
ATOM   4254  NZ  LYS A 625      16.323  36.724 -28.259  1.00 72.54           N1+
ANISOU 4254  NZ  LYS A 625     9759   9399   8405   1060   -330    278       N1+
ATOM   4255  N   GLY A 626      19.877  42.544 -24.265  1.00 58.58           N  
ANISOU 4255  N   GLY A 626     7263   8168   6827   1172   -568   -111       N  
ATOM   4256  CA  GLY A 626      21.143  43.022 -23.749  1.00 59.14           C  
ANISOU 4256  CA  GLY A 626     7194   8347   6932   1226   -592   -220       C  
ATOM   4257  C   GLY A 626      20.954  43.924 -22.544  1.00 61.27           C  
ANISOU 4257  C   GLY A 626     7366   8702   7210   1224   -641   -293       C  
ATOM   4258  O   GLY A 626      21.393  43.602 -21.443  1.00 76.63           O  
ANISOU 4258  O   GLY A 626     9270  10752   9093   1328   -697   -334       O  
ATOM   4259  N   THR A 627      20.294  45.057 -22.757  1.00 82.84           N  
ANISOU 4259  N   THR A 627    10067  11392  10014   1113   -619   -311       N  
ATOM   4260  CA  THR A 627      20.067  46.033 -21.699  1.00 81.32           C  
ANISOU 4260  CA  THR A 627     9783  11271   9843   1096   -657   -385       C  
ATOM   4261  C   THR A 627      18.636  46.555 -21.759  1.00 67.33           C  
ANISOU 4261  C   THR A 627     8079   9424   8080   1005   -643   -323       C  
ATOM   4262  O   THR A 627      18.363  47.575 -22.389  1.00 81.34           O  
ANISOU 4262  O   THR A 627     9822  11142   9940    906   -598   -341       O  
ATOM   4263  CB  THR A 627      21.037  47.218 -21.821  1.00 80.84           C  
ANISOU 4263  CB  THR A 627     9565  11256   9894   1050   -635   -515       C  
ATOM   4264  CG2 THR A 627      22.467  46.754 -21.607  1.00 75.58           C  
ANISOU 4264  CG2 THR A 627     8810  10687   9221   1146   -658   -596       C  
ATOM   4265  OG1 THR A 627      20.924  47.798 -23.128  1.00 79.22           O  
ANISOU 4265  OG1 THR A 627     9379  10944   9779    946   -554   -492       O  
ATOM   4266  N   HIS A 628      17.726  45.856 -21.090  1.00 71.52           N  
ANISOU 4266  N   HIS A 628     8716   9935   8522   1031   -649   -261       N  
ATOM   4267  CA  HIS A 628      16.307  46.164 -21.206  1.00 64.47           C  
ANISOU 4267  CA  HIS A 628     7903   8958   7637    943   -616   -201       C  
ATOM   4268  C   HIS A 628      15.914  47.475 -20.531  1.00 59.95           C  
ANISOU 4268  C   HIS A 628     7248   8418   7113    888   -627   -264       C  
ATOM   4269  O   HIS A 628      14.854  48.029 -20.820  1.00 63.41           O  
ANISOU 4269  O   HIS A 628     7724   8787   7582    805   -599   -225       O  
ATOM   4270  CB  HIS A 628      15.456  45.007 -20.673  1.00 46.62           C  
ANISOU 4270  CB  HIS A 628     5766   6658   5288    982   -599   -128       C  
ATOM   4271  CG  HIS A 628      15.449  44.897 -19.181  1.00 64.06           C  
ANISOU 4271  CG  HIS A 628     7955   8949   7435   1060   -632   -163       C  
ATOM   4272  CD2 HIS A 628      14.534  45.290 -18.264  1.00 63.00           C  
ANISOU 4272  CD2 HIS A 628     7830   8818   7288   1041   -631   -163       C  
ATOM   4273  ND1 HIS A 628      16.475  44.311 -18.472  1.00 71.19           N  
ANISOU 4273  ND1 HIS A 628     8827   9947   8273   1184   -670   -201       N  
ATOM   4274  CE1 HIS A 628      16.195  44.352 -17.182  1.00 66.91           C  
ANISOU 4274  CE1 HIS A 628     8280   9467   7676   1242   -694   -224       C  
ATOM   4275  NE2 HIS A 628      15.021  44.941 -17.029  1.00 65.04           N  
ANISOU 4275  NE2 HIS A 628     8067   9172   7471   1155   -669   -201       N  
ATOM   4276  N   THR A 629      16.762  47.977 -19.639  1.00 46.90           N  
ANISOU 4276  N   THR A 629     5481   6872   5468    937   -669   -365       N  
ATOM   4277  CA  THR A 629      16.457  49.225 -18.942  1.00 56.43           C  
ANISOU 4277  CA  THR A 629     6605   8113   6723    887   -678   -437       C  
ATOM   4278  C   THR A 629      16.767  50.446 -19.808  1.00 66.20           C  
ANISOU 4278  C   THR A 629     7745   9321   8086    796   -649   -486       C  
ATOM   4279  O   THR A 629      16.450  51.575 -19.434  1.00 58.65           O  
ANISOU 4279  O   THR A 629     6725   8372   7188    737   -640   -541       O  
ATOM   4280  CB  THR A 629      17.191  49.343 -17.581  1.00 47.23           C  
ANISOU 4280  CB  THR A 629     5349   7080   5518    973   -733   -542       C  
ATOM   4281  CG2 THR A 629      16.833  48.172 -16.677  1.00 58.55           C  
ANISOU 4281  CG2 THR A 629     6881   8540   6826   1076   -753   -486       C  
ATOM   4282  OG1 THR A 629      18.607  49.369 -17.788  1.00 51.01           O  
ANISOU 4282  OG1 THR A 629     5711   7635   6033   1018   -757   -632       O  
ATOM   4283  N   ALA A 630      17.379  50.200 -20.966  1.00 53.48           N  
ANISOU 4283  N   ALA A 630     6138   7664   6518    783   -610   -468       N  
ATOM   4284  CA  ALA A 630      17.732  51.259 -21.910  1.00 48.57           C  
ANISOU 4284  CA  ALA A 630     5460   6982   6013    693   -534   -511       C  
ATOM   4285  C   ALA A 630      16.511  52.073 -22.321  1.00 48.68           C  
ANISOU 4285  C   ALA A 630     5529   6908   6060    604   -494   -455       C  
ATOM   4286  O   ALA A 630      16.627  53.214 -22.777  1.00 50.52           O  
ANISOU 4286  O   ALA A 630     5709   7097   6389    532   -430   -499       O  
ATOM   4287  CB  ALA A 630      18.405  50.664 -23.137  1.00 49.18           C  
ANISOU 4287  CB  ALA A 630     5576   7004   6106    700   -487   -476       C  
ATOM   4288  N   VAL A 631      15.340  51.469 -22.166  1.00 35.67           N  
ANISOU 4288  N   VAL A 631     3987   5232   4335    613   -526   -357       N  
ATOM   4289  CA  VAL A 631      14.077  52.139 -22.430  1.00 54.26           C  
ANISOU 4289  CA  VAL A 631     6391   7518   6706    542   -502   -302       C  
ATOM   4290  C   VAL A 631      13.194  51.940 -21.207  1.00 53.36           C  
ANISOU 4290  C   VAL A 631     6310   7440   6525    562   -546   -289       C  
ATOM   4291  O   VAL A 631      13.469  51.074 -20.379  1.00 53.43           O  
ANISOU 4291  O   VAL A 631     6339   7500   6461    632   -575   -299       O  
ATOM   4292  CB  VAL A 631      13.384  51.562 -23.676  1.00 57.88           C  
ANISOU 4292  CB  VAL A 631     6968   7884   7139    519   -472   -195       C  
ATOM   4293  CG1 VAL A 631      14.303  51.658 -24.888  1.00 19.66           C  
ANISOU 4293  CG1 VAL A 631     2120   2997   2353    506   -409   -206       C  
ATOM   4294  CG2 VAL A 631      12.971  50.120 -23.434  1.00 49.87           C  
ANISOU 4294  CG2 VAL A 631     6051   6870   6025    571   -508   -129       C  
ATOM   4295  N   SER A 632      12.140  52.741 -21.088  1.00 53.79           N  
ANISOU 4295  N   SER A 632     6381   7456   6602    503   -527   -269       N  
ATOM   4296  CA  SER A 632      11.266  52.669 -19.922  1.00 42.37           C  
ANISOU 4296  CA  SER A 632     4969   6026   5104    512   -538   -264       C  
ATOM   4297  C   SER A 632      10.541  51.329 -19.831  1.00 53.05           C  
ANISOU 4297  C   SER A 632     6437   7342   6378    543   -533   -181       C  
ATOM   4298  O   SER A 632      10.568  50.528 -20.765  1.00 51.85           O  
ANISOU 4298  O   SER A 632     6347   7141   6212    544   -517   -127       O  
ATOM   4299  CB  SER A 632      10.238  53.801 -19.951  1.00 43.64           C  
ANISOU 4299  CB  SER A 632     5125   6144   5311    441   -514   -252       C  
ATOM   4300  OG  SER A 632       9.097  53.427 -20.704  1.00 63.51           O  
ANISOU 4300  OG  SER A 632     7741   8581   7809    406   -487   -157       O  
ATOM   4301  N   SER A 633       9.895  51.094 -18.694  1.00 52.69           N  
ANISOU 4301  N   SER A 633     6414   7319   6288    568   -542   -178       N  
ATOM   4302  CA  SER A 633       9.080  49.902 -18.516  1.00 37.85           C  
ANISOU 4302  CA  SER A 633     4631   5398   4353    588   -527   -107       C  
ATOM   4303  C   SER A 633       7.965  49.877 -19.550  1.00 51.67           C  
ANISOU 4303  C   SER A 633     6443   7055   6136    511   -491    -40       C  
ATOM   4304  O   SER A 633       7.744  48.870 -20.220  1.00 53.44           O  
ANISOU 4304  O   SER A 633     6734   7229   6340    510   -475      9       O  
ATOM   4305  CB  SER A 633       8.483  49.875 -17.108  1.00 36.87           C  
ANISOU 4305  CB  SER A 633     4509   5312   4187    622   -539   -116       C  
ATOM   4306  OG  SER A 633       7.617  48.769 -16.944  1.00 85.82           O  
ANISOU 4306  OG  SER A 633    10798  11465  10346    634   -520    -48       O  
ATOM   4307  N   ASN A 634       7.264  50.998 -19.681  1.00 54.60           N  
ANISOU 4307  N   ASN A 634     6787   7405   6552    449   -479    -43       N  
ATOM   4308  CA  ASN A 634       6.146  51.093 -20.610  1.00 36.12           C  
ANISOU 4308  CA  ASN A 634     4496   4990   4239    384   -450     12       C  
ATOM   4309  C   ASN A 634       6.592  51.018 -22.068  1.00 56.16           C  
ANISOU 4309  C   ASN A 634     7052   7490   6797    366   -438     33       C  
ATOM   4310  O   ASN A 634       5.854  50.538 -22.932  1.00 40.62           O  
ANISOU 4310  O   ASN A 634     5141   5466   4828    336   -421     77       O  
ATOM   4311  CB  ASN A 634       5.338  52.363 -20.346  1.00 46.05           C  
ANISOU 4311  CB  ASN A 634     5720   6244   5534    337   -442      4       C  
ATOM   4312  CG  ASN A 634       4.624  52.329 -19.008  1.00 62.76           C  
ANISOU 4312  CG  ASN A 634     7835   8386   7627    349   -449     -2       C  
ATOM   4313  ND2 ASN A 634       4.371  51.124 -18.498  1.00 61.70           N  
ANISOU 4313  ND2 ASN A 634     7748   8249   7445    383   -452     23       N  
ATOM   4314  OD1 ASN A 634       4.307  53.370 -18.435  1.00 47.83           O  
ANISOU 4314  OD1 ASN A 634     5901   6514   5757    331   -450    -28       O  
ATOM   4315  N   ASP A 635       7.802  51.491 -22.343  1.00 42.00           N  
ANISOU 4315  N   ASP A 635     5205   5731   5024    388   -449     -6       N  
ATOM   4316  CA  ASP A 635       8.382  51.321 -23.667  1.00 40.26           C  
ANISOU 4316  CA  ASP A 635     5003   5480   4816    385   -438     15       C  
ATOM   4317  C   ASP A 635       8.476  49.831 -23.992  1.00 46.81           C  
ANISOU 4317  C   ASP A 635     5904   6285   5597    415   -435     48       C  
ATOM   4318  O   ASP A 635       8.089  49.390 -25.074  1.00 35.26           O  
ANISOU 4318  O   ASP A 635     4499   4767   4131    393   -416     89       O  
ATOM   4319  CB  ASP A 635       9.759  51.988 -23.746  1.00 64.43           C  
ANISOU 4319  CB  ASP A 635     7974   8590   7918    409   -453    -43       C  
ATOM   4320  CG  ASP A 635       9.675  53.480 -24.034  1.00 79.25           C  
ANISOU 4320  CG  ASP A 635     9781  10461   9869    367   -439    -66       C  
ATOM   4321  OD1 ASP A 635       8.823  53.879 -24.853  1.00 76.56           O  
ANISOU 4321  OD1 ASP A 635     9490  10061   9536    332   -410    -13       O  
ATOM   4322  OD2 ASP A 635      10.468  54.252 -23.451  1.00 72.65           O1-
ANISOU 4322  OD2 ASP A 635     8851   9663   9088    363   -425   -150       O1-
ATOM   4323  N   ARG A 636       8.980  49.054 -23.042  1.00 43.23           N  
ANISOU 4323  N   ARG A 636     5447   5875   5104    471   -454     28       N  
ATOM   4324  CA  ARG A 636       9.065  47.608 -23.211  1.00 40.20           C  
ANISOU 4324  CA  ARG A 636     5134   5468   4673    508   -449     61       C  
ATOM   4325  C   ARG A 636       7.687  46.981 -23.393  1.00 49.54           C  
ANISOU 4325  C   ARG A 636     6387   6588   5848    466   -430    106       C  
ATOM   4326  O   ARG A 636       7.515  46.068 -24.198  1.00 32.98           O  
ANISOU 4326  O   ARG A 636     4351   4444   3737    460   -417    136       O  
ATOM   4327  CB  ARG A 636       9.798  46.970 -22.029  1.00 22.87           C  
ANISOU 4327  CB  ARG A 636     2923   3338   2427    591   -474     34       C  
ATOM   4328  CG  ARG A 636      11.211  47.501 -21.848  1.00 41.18           C  
ANISOU 4328  CG  ARG A 636     5157   5734   4757    638   -503    -28       C  
ATOM   4329  CD  ARG A 636      11.996  46.670 -20.860  1.00 41.41           C  
ANISOU 4329  CD  ARG A 636     5179   5832   4722    738   -531    -52       C  
ATOM   4330  NE  ARG A 636      11.428  46.756 -19.520  1.00 53.14           N  
ANISOU 4330  NE  ARG A 636     6661   7356   6174    764   -543    -65       N  
ATOM   4331  CZ  ARG A 636      11.934  47.494 -18.539  1.00 44.59           C  
ANISOU 4331  CZ  ARG A 636     5494   6359   5089    799   -578   -137       C  
ATOM   4332  NH1 ARG A 636      13.031  48.208 -18.744  1.00 41.96           N1+
ANISOU 4332  NH1 ARG A 636     5063   6084   4795    806   -604   -210       N1+
ATOM   4333  NH2 ARG A 636      11.346  47.509 -17.349  1.00 39.73           N  
ANISOU 4333  NH2 ARG A 636     4886   5774   4434    828   -587   -141       N  
ATOM   4334  N   ALA A 637       6.704  47.478 -22.650  1.00 36.17           N  
ANISOU 4334  N   ALA A 637     4680   4896   4166    436   -430    106       N  
ATOM   4335  CA  ALA A 637       5.347  46.959 -22.758  1.00 49.41           C  
ANISOU 4335  CA  ALA A 637     6408   6523   5842    392   -418    140       C  
ATOM   4336  C   ALA A 637       4.734  47.238 -24.129  1.00 53.09           C  
ANISOU 4336  C   ALA A 637     6893   6940   6340    334   -406    158       C  
ATOM   4337  O   ALA A 637       4.033  46.388 -24.682  1.00 54.35           O  
ANISOU 4337  O   ALA A 637     7105   7058   6489    312   -402    181       O  
ATOM   4338  CB  ALA A 637       4.465  47.523 -21.656  1.00 45.02           C  
ANISOU 4338  CB  ALA A 637     5827   5986   5293    376   -421    135       C  
ATOM   4339  N   SER A 638       4.995  48.425 -24.673  1.00 28.84           N  
ANISOU 4339  N   SER A 638     3781   3876   3302    314   -402    147       N  
ATOM   4340  CA  SER A 638       4.416  48.809 -25.956  1.00 40.55           C  
ANISOU 4340  CA  SER A 638     5282   5320   4804    274   -391    165       C  
ATOM   4341  C   SER A 638       4.995  47.944 -27.063  1.00 54.95           C  
ANISOU 4341  C   SER A 638     7154   7117   6608    291   -386    177       C  
ATOM   4342  O   SER A 638       4.290  47.566 -27.997  1.00 38.76           O  
ANISOU 4342  O   SER A 638     5145   5031   4552    267   -384    193       O  
ATOM   4343  CB  SER A 638       4.657  50.289 -26.258  1.00 24.31           C  
ANISOU 4343  CB  SER A 638     3180   3278   2780    263   -383    157       C  
ATOM   4344  OG  SER A 638       5.964  50.512 -26.757  1.00 53.30           O  
ANISOU 4344  OG  SER A 638     6835   6962   6455    294   -380    148       O  
ATOM   4345  N   LEU A 639       6.283  47.633 -26.947  1.00 22.49           N  
ANISOU 4345  N   LEU A 639     3034   3027   2483    337   -388    166       N  
ATOM   4346  CA  LEU A 639       6.946  46.721 -27.871  1.00 37.96           C  
ANISOU 4346  CA  LEU A 639     5042   4963   4419    362   -381    178       C  
ATOM   4347  C   LEU A 639       6.288  45.340 -27.892  1.00 41.11           C  
ANISOU 4347  C   LEU A 639     5505   5327   4786    359   -383    194       C  
ATOM   4348  O   LEU A 639       5.854  44.870 -28.944  1.00 48.69           O  
ANISOU 4348  O   LEU A 639     6512   6248   5738    338   -379    207       O  
ATOM   4349  CB  LEU A 639       8.433  46.604 -27.528  1.00 31.89           C  
ANISOU 4349  CB  LEU A 639     4243   4235   3639    420   -387    161       C  
ATOM   4350  CG  LEU A 639       9.262  47.845 -27.870  1.00 35.04           C  
ANISOU 4350  CG  LEU A 639     4582   4661   4072    424   -385    146       C  
ATOM   4351  CD1 LEU A 639      10.697  47.728 -27.360  1.00 26.95           C  
ANISOU 4351  CD1 LEU A 639     3505   3693   3043    484   -405    114       C  
ATOM   4352  CD2 LEU A 639       9.231  48.094 -29.372  1.00 21.02           C  
ANISOU 4352  CD2 LEU A 639     2844   2838   2303    408   -361    175       C  
ATOM   4353  N   ILE A 640       6.214  44.696 -26.731  1.00 23.62           N  
ANISOU 4353  N   ILE A 640     3296   3129   2551    383   -389    193       N  
ATOM   4354  CA  ILE A 640       5.578  43.385 -26.611  1.00 55.47           C  
ANISOU 4354  CA  ILE A 640     7396   7127   6554    383   -387    213       C  
ATOM   4355  C   ILE A 640       4.162  43.417 -27.162  1.00 57.13           C  
ANISOU 4355  C   ILE A 640     7626   7302   6779    318   -392    222       C  
ATOM   4356  O   ILE A 640       3.725  42.494 -27.851  1.00 40.42           O  
ANISOU 4356  O   ILE A 640     5568   5147   4644    303   -392    234       O  
ATOM   4357  CB  ILE A 640       5.497  42.914 -25.140  1.00 37.48           C  
ANISOU 4357  CB  ILE A 640     5121   4873   4248    422   -389    217       C  
ATOM   4358  CG1 ILE A 640       6.879  42.555 -24.607  1.00 35.70           C  
ANISOU 4358  CG1 ILE A 640     4889   4688   3988    505   -390    209       C  
ATOM   4359  CG2 ILE A 640       4.599  41.704 -25.015  1.00 42.27           C  
ANISOU 4359  CG2 ILE A 640     5801   5434   4826    410   -380    245       C  
ATOM   4360  CD1 ILE A 640       6.837  42.016 -23.206  1.00 86.50           C  
ANISOU 4360  CD1 ILE A 640    11338  11150  10380    562   -391    217       C  
ATOM   4361  N   ASN A 641       3.442  44.487 -26.846  1.00 41.70           N  
ANISOU 4361  N   ASN A 641     5623   5365   4857    282   -398    214       N  
ATOM   4362  CA  ASN A 641       2.055  44.615 -27.264  1.00 23.03           C  
ANISOU 4362  CA  ASN A 641     3266   2980   2505    228   -409    220       C  
ATOM   4363  C   ASN A 641       1.901  44.777 -28.771  1.00 40.02           C  
ANISOU 4363  C   ASN A 641     5437   5112   4658    210   -413    220       C  
ATOM   4364  O   ASN A 641       1.073  44.115 -29.392  1.00 40.32           O  
ANISOU 4364  O   ASN A 641     5513   5127   4680    185   -427    225       O  
ATOM   4365  CB  ASN A 641       1.389  45.775 -26.541  1.00 27.45           C  
ANISOU 4365  CB  ASN A 641     3768   3566   3094    204   -411    214       C  
ATOM   4366  CG  ASN A 641       0.019  46.087 -27.091  1.00 44.16           C  
ANISOU 4366  CG  ASN A 641     5883   5671   5224    155   -424    219       C  
ATOM   4367  ND2 ASN A 641      -0.025  46.917 -28.129  1.00 56.07           N  
ANISOU 4367  ND2 ASN A 641     7378   7181   6744    149   -424    216       N  
ATOM   4368  OD1 ASN A 641      -0.993  45.587 -26.593  1.00 42.38           O  
ANISOU 4368  OD1 ASN A 641     5670   5441   4993    130   -434    226       O  
ATOM   4369  N   ASN A 642       2.701  45.664 -29.355  1.00 51.36           N  
ANISOU 4369  N   ASN A 642     6847   6559   6107    228   -402    215       N  
ATOM   4370  CA  ASN A 642       2.652  45.922 -30.788  1.00 34.61           C  
ANISOU 4370  CA  ASN A 642     4749   4423   3979    227   -401    218       C  
ATOM   4371  C   ASN A 642       3.123  44.727 -31.611  1.00 39.86           C  
ANISOU 4371  C   ASN A 642     5476   5059   4610    245   -401    223       C  
ATOM   4372  O   ASN A 642       2.511  44.373 -32.621  1.00 38.86           O  
ANISOU 4372  O   ASN A 642     5388   4916   4463    233   -414    224       O  
ATOM   4373  CB  ASN A 642       3.479  47.161 -31.139  1.00 40.14           C  
ANISOU 4373  CB  ASN A 642     5415   5140   4698    248   -381    219       C  
ATOM   4374  CG  ASN A 642       2.862  48.441 -30.610  1.00 39.23           C  
ANISOU 4374  CG  ASN A 642     5248   5045   4611    228   -379    218       C  
ATOM   4375  ND2 ASN A 642       3.569  49.551 -30.778  1.00 43.73           N  
ANISOU 4375  ND2 ASN A 642     5790   5627   5198    245   -360    222       N  
ATOM   4376  OD1 ASN A 642       1.763  48.432 -30.057  1.00 46.37           O  
ANISOU 4376  OD1 ASN A 642     6141   5954   5522    199   -394    216       O  
ATOM   4377  N   ALA A 643       4.216  44.108 -31.178  1.00 36.17           N  
ANISOU 4377  N   ALA A 643     5020   4592   4131    280   -388    223       N  
ATOM   4378  CA  ALA A 643       4.752  42.941 -31.869  1.00 39.50           C  
ANISOU 4378  CA  ALA A 643     5506   4985   4519    303   -383    230       C  
ATOM   4379  C   ALA A 643       3.688  41.862 -32.050  1.00 39.94           C  
ANISOU 4379  C   ALA A 643     5616   5010   4549    273   -400    234       C  
ATOM   4380  O   ALA A 643       3.442  41.402 -33.160  1.00 26.83           O  
ANISOU 4380  O   ALA A 643     4003   3328   2865    266   -408    234       O  
ATOM   4381  CB  ALA A 643       5.954  42.385 -31.118  1.00 18.18           C  
ANISOU 4381  CB  ALA A 643     2805   2295   1806    352   -369    232       C  
ATOM   4382  N   PHE A 644       3.043  41.467 -30.960  1.00 29.92           N  
ANISOU 4382  N   PHE A 644     4345   3743   3283    256   -406    238       N  
ATOM   4383  CA  PHE A 644       2.067  40.385 -31.023  1.00 44.80           C  
ANISOU 4383  CA  PHE A 644     6286   5597   5139    225   -417    246       C  
ATOM   4384  C   PHE A 644       0.776  40.753 -31.744  1.00 48.29           C  
ANISOU 4384  C   PHE A 644     6719   6046   5585    175   -448    235       C  
ATOM   4385  O   PHE A 644       0.013  39.867 -32.140  1.00 50.67           O  
ANISOU 4385  O   PHE A 644     7070   6327   5854    146   -464    235       O  
ATOM   4386  CB  PHE A 644       1.767  39.839 -29.628  1.00 14.86           C  
ANISOU 4386  CB  PHE A 644     2503   1802   1341    228   -406    260       C  
ATOM   4387  CG  PHE A 644       2.827  38.934 -29.102  1.00 53.93           C  
ANISOU 4387  CG  PHE A 644     7495   6736   6260    286   -377    276       C  
ATOM   4388  CD1 PHE A 644       2.894  37.621 -29.521  1.00 42.78           C  
ANISOU 4388  CD1 PHE A 644     6170   5277   4808    295   -359    293       C  
ATOM   4389  CD2 PHE A 644       3.768  39.395 -28.197  1.00 65.86           C  
ANISOU 4389  CD2 PHE A 644     8963   8283   7778    338   -368    274       C  
ATOM   4390  CE1 PHE A 644       3.873  36.781 -29.045  1.00 54.73           C  
ANISOU 4390  CE1 PHE A 644     7729   6775   6290    360   -327    313       C  
ATOM   4391  CE2 PHE A 644       4.752  38.557 -27.714  1.00 46.92           C  
ANISOU 4391  CE2 PHE A 644     6603   5880   5344    406   -345    289       C  
ATOM   4392  CZ  PHE A 644       4.805  37.250 -28.139  1.00 70.09           C  
ANISOU 4392  CZ  PHE A 644     9627   8764   8240    420   -323    311       C  
ATOM   4393  N   GLN A 645       0.530  42.051 -31.904  1.00 12.53           N  
ANISOU 4393  N   GLN A 645     2129   1546   1086    168   -455    227       N  
ATOM   4394  CA  GLN A 645      -0.610  42.514 -32.691  1.00 27.27           C  
ANISOU 4394  CA  GLN A 645     3983   3428   2949    139   -485    216       C  
ATOM   4395  C   GLN A 645      -0.259  42.487 -34.166  1.00 58.34           C  
ANISOU 4395  C   GLN A 645     7954   7358   6856    163   -492    210       C  
ATOM   4396  O   GLN A 645      -1.051  42.057 -35.004  1.00 47.35           O  
ANISOU 4396  O   GLN A 645     6590   5971   5430    148   -523    198       O  
ATOM   4397  CB  GLN A 645      -1.023  43.925 -32.289  1.00 40.72           C  
ANISOU 4397  CB  GLN A 645     5618   5163   4690    134   -484    215       C  
ATOM   4398  CG  GLN A 645      -1.617  44.032 -30.899  1.00 64.79           C  
ANISOU 4398  CG  GLN A 645     8632   8223   7763    108   -483    219       C  
ATOM   4399  CD  GLN A 645      -2.516  45.241 -30.756  1.00 96.49           C  
ANISOU 4399  CD  GLN A 645    12591  12268  11803     92   -491    216       C  
ATOM   4400  NE2 GLN A 645      -3.346  45.482 -31.766  1.00 81.00           N  
ANISOU 4400  NE2 GLN A 645    10630  10321   9825     86   -517    209       N  
ATOM   4401  OE1 GLN A 645      -2.464  45.955 -29.756  1.00119.60           O  
ANISOU 4401  OE1 GLN A 645    15477  15209  14759     90   -476    220       O  
ATOM   4402  N   LEU A 646       0.941  42.957 -34.475  1.00 35.24           N  
ANISOU 4402  N   LEU A 646     5025   4428   3938    203   -463    217       N  
ATOM   4403  CA  LEU A 646       1.436  42.916 -35.833  1.00 36.89           C  
ANISOU 4403  CA  LEU A 646     5275   4627   4115    235   -459    217       C  
ATOM   4404  C   LEU A 646       1.534  41.480 -36.307  1.00 31.07           C  
ANISOU 4404  C   LEU A 646     4610   3861   3336    233   -469    214       C  
ATOM   4405  O   LEU A 646       1.339  41.192 -37.483  1.00 38.66           O  
ANISOU 4405  O   LEU A 646     5613   4819   4256    244   -485    206       O  
ATOM   4406  CB  LEU A 646       2.794  43.612 -35.915  1.00 48.76           C  
ANISOU 4406  CB  LEU A 646     6763   6130   5635    275   -420    228       C  
ATOM   4407  CG  LEU A 646       2.671  45.113 -35.653  1.00 23.71           C  
ANISOU 4407  CG  LEU A 646     3531   2984   2494    277   -408    233       C  
ATOM   4408  CD1 LEU A 646       4.011  45.739 -35.309  1.00 32.74           C  
ANISOU 4408  CD1 LEU A 646     4648   4132   3661    304   -371    241       C  
ATOM   4409  CD2 LEU A 646       2.026  45.793 -36.852  1.00 28.36           C  
ANISOU 4409  CD2 LEU A 646     4137   3583   3057    295   -417    237       C  
ATOM   4410  N   VAL A 647       1.825  40.577 -35.379  1.00 34.60           N  
ANISOU 4410  N   VAL A 647     5075   4287   3786    224   -456    220       N  
ATOM   4411  CA  VAL A 647       1.876  39.155 -35.695  1.00 47.99           C  
ANISOU 4411  CA  VAL A 647     6847   5948   5438    220   -457    222       C  
ATOM   4412  C   VAL A 647       0.509  38.651 -36.132  1.00 37.92           C  
ANISOU 4412  C   VAL A 647     5599   4682   4129    173   -498    203       C  
ATOM   4413  O   VAL A 647       0.404  37.843 -37.052  1.00 55.13           O  
ANISOU 4413  O   VAL A 647     7840   6849   6258    169   -511    190       O  
ATOM   4414  CB  VAL A 647       2.325  38.311 -34.488  1.00 48.14           C  
ANISOU 4414  CB  VAL A 647     6888   5944   5461    228   -429    239       C  
ATOM   4415  CG1 VAL A 647       2.136  36.833 -34.790  1.00 28.39           C  
ANISOU 4415  CG1 VAL A 647     4479   3399   2908    217   -422    247       C  
ATOM   4416  CG2 VAL A 647       3.772  38.607 -34.133  1.00 33.30           C  
ANISOU 4416  CG2 VAL A 647     4985   4068   3598    283   -397    248       C  
ATOM   4417  N   SER A 648      -0.535  39.139 -35.469  1.00 40.33           N  
ANISOU 4417  N   SER A 648     5853   5014   4456    136   -520    196       N  
ATOM   4418  CA  SER A 648      -1.892  38.660 -35.711  1.00 73.30           C  
ANISOU 4418  CA  SER A 648    10040   9212   8599     84   -562    167       C  
ATOM   4419  C   SER A 648      -2.535  39.261 -36.962  1.00 61.38           C  
ANISOU 4419  C   SER A 648     8508   7746   7067     90   -606    133       C  
ATOM   4420  O   SER A 648      -3.633  38.864 -37.350  1.00 66.24           O  
ANISOU 4420  O   SER A 648     9123   8396   7650     50   -651     85       O  
ATOM   4421  CB  SER A 648      -2.775  38.944 -34.500  1.00 55.46           C  
ANISOU 4421  CB  SER A 648     7732   6970   6369     45   -567    170       C  
ATOM   4422  OG  SER A 648      -3.067  40.325 -34.410  1.00 48.03           O  
ANISOU 4422  OG  SER A 648     6714   6064   5473     57   -577    171       O  
ATOM   4423  N   ILE A 649      -1.862  40.222 -37.584  1.00 45.41           N  
ANISOU 4423  N   ILE A 649     6467   5728   5058    142   -592    149       N  
ATOM   4424  CA  ILE A 649      -2.371  40.811 -38.818  1.00 56.03           C  
ANISOU 4424  CA  ILE A 649     7805   7113   6370    169   -626    126       C  
ATOM   4425  C   ILE A 649      -1.438  40.506 -39.983  1.00 54.58           C  
ANISOU 4425  C   ILE A 649     7684   6910   6144    217   -612    130       C  
ATOM   4426  O   ILE A 649      -1.616  41.018 -41.086  1.00 47.83           O  
ANISOU 4426  O   ILE A 649     6838   6084   5252    259   -630    120       O  
ATOM   4427  CB  ILE A 649      -2.579  42.334 -38.694  1.00 46.40           C  
ANISOU 4427  CB  ILE A 649     6522   5921   5185    196   -617    143       C  
ATOM   4428  CG1 ILE A 649      -1.236  43.064 -38.692  1.00 26.01           C  
ANISOU 4428  CG1 ILE A 649     3942   3310   2629    240   -562    177       C  
ATOM   4429  CG2 ILE A 649      -3.386  42.660 -37.450  1.00 44.41           C  
ANISOU 4429  CG2 ILE A 649     6211   5684   4979    152   -623    144       C  
ATOM   4430  CD1 ILE A 649      -1.363  44.565 -38.796  1.00 36.24           C  
ANISOU 4430  CD1 ILE A 649     5195   4632   3942    272   -548    192       C  
ATOM   4431  N   GLY A 650      -0.435  39.675 -39.720  1.00 35.02           N  
ANISOU 4431  N   GLY A 650     5254   4384   3667    218   -577    148       N  
ATOM   4432  CA  GLY A 650       0.459  39.193 -40.756  1.00 41.45           C  
ANISOU 4432  CA  GLY A 650     6134   5175   4439    259   -560    151       C  
ATOM   4433  C   GLY A 650       1.565  40.129 -41.210  1.00 36.62           C  
ANISOU 4433  C   GLY A 650     5516   4553   3844    319   -518    180       C  
ATOM   4434  O   GLY A 650       2.111  39.950 -42.295  1.00 49.21           O  
ANISOU 4434  O   GLY A 650     7163   6138   5394    360   -508    182       O  
ATOM   4435  N   LYS A 651       1.908  41.118 -40.390  1.00 34.80           N  
ANISOU 4435  N   LYS A 651     5224   4326   3670    322   -490    200       N  
ATOM   4436  CA  LYS A 651       2.990  42.037 -40.734  1.00 42.69           C  
ANISOU 4436  CA  LYS A 651     6215   5320   4683    370   -444    223       C  
ATOM   4437  C   LYS A 651       4.280  41.691 -40.003  1.00 31.22           C  
ANISOU 4437  C   LYS A 651     4759   3842   3264    377   -402    236       C  
ATOM   4438  O   LYS A 651       5.355  42.152 -40.373  1.00 56.67           O  
ANISOU 4438  O   LYS A 651     7985   7056   6490    415   -362    252       O  
ATOM   4439  CB  LYS A 651       2.585  43.490 -40.469  1.00 38.51           C  
ANISOU 4439  CB  LYS A 651     5626   4821   4185    375   -438    231       C  
ATOM   4440  CG  LYS A 651       1.393  43.944 -41.301  1.00 39.36           C  
ANISOU 4440  CG  LYS A 651     5739   4964   4252    390   -477    221       C  
ATOM   4441  CD  LYS A 651       1.415  45.444 -41.555  1.00 34.86           C  
ANISOU 4441  CD  LYS A 651     5144   4412   3689    430   -449    244       C  
ATOM   4442  CE  LYS A 651       2.371  45.813 -42.677  1.00 68.67           C  
ANISOU 4442  CE  LYS A 651     9481   8676   7934    496   -405    269       C  
ATOM   4443  NZ  LYS A 651       2.393  47.286 -42.923  1.00 67.76           N1+
ANISOU 4443  NZ  LYS A 651     9353   8572   7821    539   -366    299       N1+
ATOM   4444  N   LEU A 652       4.161  40.870 -38.967  1.00 31.12           N  
ANISOU 4444  N   LEU A 652     4739   3818   3268    344   -411    231       N  
ATOM   4445  CA  LEU A 652       5.323  40.375 -38.242  1.00 37.37           C  
ANISOU 4445  CA  LEU A 652     5530   4592   4076    363   -378    241       C  
ATOM   4446  C   LEU A 652       5.213  38.860 -38.123  1.00 54.48           C  
ANISOU 4446  C   LEU A 652     7763   6726   6211    353   -384    241       C  
ATOM   4447  O   LEU A 652       4.116  38.315 -38.021  1.00 49.63           O  
ANISOU 4447  O   LEU A 652     7170   6108   5579    313   -413    231       O  
ATOM   4448  CB  LEU A 652       5.408  41.019 -36.850  1.00 21.99           C  
ANISOU 4448  CB  LEU A 652     3509   2668   2177    351   -373    242       C  
ATOM   4449  CG  LEU A 652       6.665  40.717 -36.030  1.00 35.46           C  
ANISOU 4449  CG  LEU A 652     5201   4376   3896    385   -346    250       C  
ATOM   4450  CD1 LEU A 652       7.916  41.035 -36.833  1.00 17.08           C  
ANISOU 4450  CD1 LEU A 652     2881   2046   1561    429   -315    260       C  
ATOM   4451  CD2 LEU A 652       6.658  41.488 -34.713  1.00 43.98           C  
ANISOU 4451  CD2 LEU A 652     6206   5491   5015    376   -349    246       C  
ATOM   4452  N   SER A 653       6.355  38.186 -38.148  1.00 50.54           N  
ANISOU 4452  N   SER A 653     7300   6204   5700    391   -352    253       N  
ATOM   4453  CA  SER A 653       6.379  36.730 -38.088  1.00 35.23           C  
ANISOU 4453  CA  SER A 653     5436   4225   3724    391   -344    259       C  
ATOM   4454  C   SER A 653       6.395  36.259 -36.642  1.00 43.47           C  
ANISOU 4454  C   SER A 653     6467   5266   4785    390   -333    270       C  
ATOM   4455  O   SER A 653       7.156  36.769 -35.822  1.00 54.76           O  
ANISOU 4455  O   SER A 653     7841   6721   6243    422   -319    275       O  
ATOM   4456  CB  SER A 653       7.600  36.198 -38.833  1.00 50.66           C  
ANISOU 4456  CB  SER A 653     7441   6154   5652    443   -310    271       C  
ATOM   4457  OG  SER A 653       7.427  34.835 -39.174  1.00 79.59           O  
ANISOU 4457  OG  SER A 653    11197   9773   9270    438   -302    276       O  
ATOM   4458  N   ILE A 654       5.556  35.279 -36.338  1.00 42.92           N  
ANISOU 4458  N   ILE A 654     6452   5167   4691    358   -337    275       N  
ATOM   4459  CA  ILE A 654       5.383  34.806 -34.966  1.00 43.94           C  
ANISOU 4459  CA  ILE A 654     6582   5287   4828    359   -320    292       C  
ATOM   4460  C   ILE A 654       6.688  34.618 -34.182  1.00 45.59           C  
ANISOU 4460  C   ILE A 654     6780   5502   5040    431   -287    309       C  
ATOM   4461  O   ILE A 654       6.724  34.851 -32.978  1.00 53.29           O  
ANISOU 4461  O   ILE A 654     7717   6501   6031    448   -283    316       O  
ATOM   4462  CB  ILE A 654       4.554  33.502 -34.922  1.00 60.61           C  
ANISOU 4462  CB  ILE A 654     8786   7344   6898    324   -305    307       C  
ATOM   4463  CG1 ILE A 654       4.163  33.164 -33.482  1.00 48.48           C  
ANISOU 4463  CG1 ILE A 654     7253   5797   5372    323   -280    331       C  
ATOM   4464  CG2 ILE A 654       5.317  32.352 -35.553  1.00 57.84           C  
ANISOU 4464  CG2 ILE A 654     8529   6939   6508    359   -265    324       C  
ATOM   4465  CD1 ILE A 654       3.274  34.192 -32.848  1.00 29.28           C  
ANISOU 4465  CD1 ILE A 654     4739   3411   2975    283   -316    316       C  
ATOM   4466  N   GLU A 655       7.754  34.204 -34.858  1.00 50.09           N  
ANISOU 4466  N   GLU A 655     7386   6057   5591    478   -264    316       N  
ATOM   4467  CA  GLU A 655       9.021  33.946 -34.181  1.00 49.63           C  
ANISOU 4467  CA  GLU A 655     7319   6012   5526    555   -237    332       C  
ATOM   4468  C   GLU A 655       9.743  35.233 -33.799  1.00 57.45           C  
ANISOU 4468  C   GLU A 655     8208   7069   6553    578   -254    317       C  
ATOM   4469  O   GLU A 655      10.499  35.260 -32.832  1.00 52.69           O  
ANISOU 4469  O   GLU A 655     7572   6500   5947    634   -248    324       O  
ATOM   4470  CB  GLU A 655       9.942  33.062 -35.031  1.00 41.20           C  
ANISOU 4470  CB  GLU A 655     6323   4908   4425    601   -205    346       C  
ATOM   4471  CG  GLU A 655      10.575  33.759 -36.222  1.00 64.45           C  
ANISOU 4471  CG  GLU A 655     9243   7867   7378    605   -211    332       C  
ATOM   4472  CD  GLU A 655       9.633  33.878 -37.398  1.00 71.76           C  
ANISOU 4472  CD  GLU A 655    10202   8770   8294    546   -231    317       C  
ATOM   4473  OE1 GLU A 655       8.469  33.451 -37.268  1.00 97.21           O  
ANISOU 4473  OE1 GLU A 655    13458  11971  11506    495   -246    313       O  
ATOM   4474  OE2 GLU A 655      10.059  34.393 -38.454  1.00 57.15           O1-
ANISOU 4474  OE2 GLU A 655     8347   6926   6442    555   -230    310       O1-
ATOM   4475  N   LYS A 656       9.516  36.295 -34.563  1.00 33.32           N  
ANISOU 4475  N   LYS A 656     5105   4031   3524    540   -272    299       N  
ATOM   4476  CA  LYS A 656      10.145  37.575 -34.274  1.00 42.02           C  
ANISOU 4476  CA  LYS A 656     6117   5186   4662    554   -279    288       C  
ATOM   4477  C   LYS A 656       9.615  38.109 -32.952  1.00 48.84           C  
ANISOU 4477  C   LYS A 656     6922   6086   5549    538   -298    280       C  
ATOM   4478  O   LYS A 656      10.363  38.655 -32.145  1.00 47.83           O  
ANISOU 4478  O   LYS A 656     6734   6006   5434    575   -301    275       O  
ATOM   4479  CB  LYS A 656       9.877  38.575 -35.397  1.00 55.21           C  
ANISOU 4479  CB  LYS A 656     7768   6858   6351    519   -284    279       C  
ATOM   4480  CG  LYS A 656      10.402  38.139 -36.763  1.00 85.07           C  
ANISOU 4480  CG  LYS A 656    11612  10606  10104    540   -263    287       C  
ATOM   4481  CD  LYS A 656      11.918  38.032 -36.767  1.00 84.48           C  
ANISOU 4481  CD  LYS A 656    11528  10544  10026    604   -235    301       C  
ATOM   4482  CE  LYS A 656      12.444  37.673 -38.146  1.00121.86           C  
ANISOU 4482  CE  LYS A 656    16326  15243  14733    625   -208    312       C  
ATOM   4483  NZ  LYS A 656      13.929  37.573 -38.164  1.00128.96           N1+
ANISOU 4483  NZ  LYS A 656    17214  16154  15633    689   -179    328       N1+
ATOM   4484  N   ALA A 657       8.316  37.925 -32.733  1.00 47.89           N  
ANISOU 4484  N   ALA A 657     6819   5945   5431    486   -312    278       N  
ATOM   4485  CA  ALA A 657       7.657  38.377 -31.514  1.00 40.81           C  
ANISOU 4485  CA  ALA A 657     5876   5076   4554    468   -326    274       C  
ATOM   4486  C   ALA A 657       7.920  37.444 -30.330  1.00 42.96           C  
ANISOU 4486  C   ALA A 657     6180   5348   4796    518   -312    291       C  
ATOM   4487  O   ALA A 657       7.863  37.864 -29.171  1.00 43.21           O  
ANISOU 4487  O   ALA A 657     6166   5417   4835    533   -319    288       O  
ATOM   4488  CB  ALA A 657       6.170  38.537 -31.753  1.00 10.45           C  
ANISOU 4488  CB  ALA A 657     2038   1212    721    397   -345    268       C  
ATOM   4489  N   LEU A 658       8.199  36.178 -30.622  1.00 47.32           N  
ANISOU 4489  N   LEU A 658     6816   5856   5308    549   -287    312       N  
ATOM   4490  CA  LEU A 658       8.557  35.215 -29.585  1.00 27.00           C  
ANISOU 4490  CA  LEU A 658     4288   3275   2694    615   -262    338       C  
ATOM   4491  C   LEU A 658      10.003  35.409 -29.148  1.00 43.44           C  
ANISOU 4491  C   LEU A 658     6330   5412   4762    703   -262    336       C  
ATOM   4492  O   LEU A 658      10.311  35.332 -27.964  1.00 30.13           O  
ANISOU 4492  O   LEU A 658     4629   3765   3054    763   -262    344       O  
ATOM   4493  CB  LEU A 658       8.329  33.782 -30.069  1.00 22.63           C  
ANISOU 4493  CB  LEU A 658     3849   2647   2101    618   -225    367       C  
ATOM   4494  CG  LEU A 658       6.867  33.328 -30.179  1.00 56.63           C  
ANISOU 4494  CG  LEU A 658     8208   6900   6408    541   -219    375       C  
ATOM   4495  CD1 LEU A 658       6.742  32.079 -31.037  1.00 37.57           C  
ANISOU 4495  CD1 LEU A 658     5902   4410   3961    530   -183    394       C  
ATOM   4496  CD2 LEU A 658       6.256  33.094 -28.808  1.00 12.63           C  
ANISOU 4496  CD2 LEU A 658     2647   1326    826    552   -201    397       C  
ATOM   4497  N   ASP A 659      10.889  35.663 -30.107  1.00 43.13           N  
ANISOU 4497  N   ASP A 659     6275   5381   4732    715   -263    327       N  
ATOM   4498  CA  ASP A 659      12.275  35.989 -29.791  1.00 42.91           C  
ANISOU 4498  CA  ASP A 659     6194   5413   4696    793   -270    320       C  
ATOM   4499  C   ASP A 659      12.302  37.227 -28.911  1.00 55.78           C  
ANISOU 4499  C   ASP A 659     7724   7115   6356    786   -303    292       C  
ATOM   4500  O   ASP A 659      13.184  37.378 -28.061  1.00 54.26           O  
ANISOU 4500  O   ASP A 659     7485   6987   6145    860   -318    282       O  
ATOM   4501  CB  ASP A 659      13.087  36.250 -31.059  1.00 42.43           C  
ANISOU 4501  CB  ASP A 659     6127   5347   4649    792   -264    315       C  
ATOM   4502  CG  ASP A 659      13.597  34.979 -31.700  1.00 97.47           C  
ANISOU 4502  CG  ASP A 659    13187  12268  11579    837   -231    341       C  
ATOM   4503  OD1 ASP A 659      14.167  34.133 -30.976  1.00101.41           O  
ANISOU 4503  OD1 ASP A 659    13719  12777  12036    918   -218    360       O  
ATOM   4504  OD2 ASP A 659      13.438  34.834 -32.933  1.00107.79           O1-
ANISOU 4504  OD2 ASP A 659    14537  13528  12891    798   -217    343       O1-
ATOM   4505  N   LEU A 660      11.329  38.108 -29.128  1.00 56.61           N  
ANISOU 4505  N   LEU A 660     7796   7210   6504    703   -314    277       N  
ATOM   4506  CA  LEU A 660      11.211  39.345 -28.365  1.00 60.37           C  
ANISOU 4506  CA  LEU A 660     8182   7742   7012    685   -339    252       C  
ATOM   4507  C   LEU A 660      10.918  39.033 -26.907  1.00 48.21           C  
ANISOU 4507  C   LEU A 660     6641   6232   5445    725   -347    254       C  
ATOM   4508  O   LEU A 660      11.623  39.489 -26.009  1.00 36.98           O  
ANISOU 4508  O   LEU A 660     5159   4879   4013    779   -368    234       O  
ATOM   4509  CB  LEU A 660      10.083  40.214 -28.930  1.00 50.24           C  
ANISOU 4509  CB  LEU A 660     6882   6434   5775    594   -344    244       C  
ATOM   4510  CG  LEU A 660      10.181  41.736 -28.766  1.00 35.76           C  
ANISOU 4510  CG  LEU A 660     4960   4643   3985    567   -359    219       C  
ATOM   4511  CD1 LEU A 660       8.804  42.350 -28.697  1.00 33.32           C  
ANISOU 4511  CD1 LEU A 660     4640   4316   3705    495   -364    217       C  
ATOM   4512  CD2 LEU A 660      10.997  42.127 -27.549  1.00 36.82           C  
ANISOU 4512  CD2 LEU A 660     5028   4849   4113    623   -378    197       C  
ATOM   4513  N   SER A 661       9.870  38.246 -26.684  1.00 41.66           N  
ANISOU 4513  N   SER A 661     5879   5351   4598    700   -331    279       N  
ATOM   4514  CA  SER A 661       9.464  37.867 -25.341  1.00 34.70           C  
ANISOU 4514  CA  SER A 661     5014   4485   3684    739   -328    292       C  
ATOM   4515  C   SER A 661      10.595  37.219 -24.542  1.00 39.20           C  
ANISOU 4515  C   SER A 661     5599   5101   4195    859   -325    301       C  
ATOM   4516  O   SER A 661      10.583  37.250 -23.315  1.00 40.74           O  
ANISOU 4516  O   SER A 661     5782   5340   4358    915   -333    302       O  
ATOM   4517  CB  SER A 661       8.262  36.926 -25.402  1.00 36.27           C  
ANISOU 4517  CB  SER A 661     5301   4611   3870    698   -301    324       C  
ATOM   4518  OG  SER A 661       8.601  35.722 -26.063  1.00 52.33           O  
ANISOU 4518  OG  SER A 661     7422   6591   5871    726   -270    351       O  
ATOM   4519  N   LEU A 662      11.566  36.631 -25.233  1.00 39.40           N  
ANISOU 4519  N   LEU A 662     5652   5119   4200    906   -315    309       N  
ATOM   4520  CA  LEU A 662      12.679  35.969 -24.557  1.00 57.84           C  
ANISOU 4520  CA  LEU A 662     8003   7503   6473   1032   -314    320       C  
ATOM   4521  C   LEU A 662      13.351  36.896 -23.550  1.00 53.74           C  
ANISOU 4521  C   LEU A 662     7382   7090   5947   1087   -359    278       C  
ATOM   4522  O   LEU A 662      13.970  36.442 -22.588  1.00 40.21           O  
ANISOU 4522  O   LEU A 662     5675   5433   4171   1199   -368    282       O  
ATOM   4523  CB  LEU A 662      13.716  35.470 -25.570  1.00 71.40           C  
ANISOU 4523  CB  LEU A 662     9741   9207   8181   1067   -304    326       C  
ATOM   4524  CG  LEU A 662      13.371  34.195 -26.345  1.00 73.17           C  
ANISOU 4524  CG  LEU A 662    10082   9334   8383   1058   -255    369       C  
ATOM   4525  CD1 LEU A 662      14.435  33.889 -27.391  1.00 49.56           C  
ANISOU 4525  CD1 LEU A 662     7102   6338   5390   1089   -247    370       C  
ATOM   4526  CD2 LEU A 662      13.208  33.032 -25.389  1.00 17.98           C  
ANISOU 4526  CD2 LEU A 662     3183   2322   1326   1142   -219    412       C  
ATOM   4527  N   TYR A 663      13.226  38.197 -23.781  1.00 30.39           N  
ANISOU 4527  N   TYR A 663     4335   4161   3051   1013   -387    237       N  
ATOM   4528  CA  TYR A 663      13.825  39.181 -22.895  1.00 54.19           C  
ANISOU 4528  CA  TYR A 663     7246   7275   6068   1051   -431    186       C  
ATOM   4529  C   TYR A 663      13.133  39.153 -21.533  1.00 32.93           C  
ANISOU 4529  C   TYR A 663     4564   4609   3339   1082   -436    190       C  
ATOM   4530  O   TYR A 663      13.737  39.481 -20.514  1.00 54.64           O  
ANISOU 4530  O   TYR A 663     7257   7450   6054   1160   -471    153       O  
ATOM   4531  CB  TYR A 663      13.732  40.584 -23.506  1.00 60.49           C  
ANISOU 4531  CB  TYR A 663     7959   8081   6944    957   -447    148       C  
ATOM   4532  CG  TYR A 663      12.476  41.334 -23.120  1.00 44.13           C  
ANISOU 4532  CG  TYR A 663     5875   5986   4907    875   -444    145       C  
ATOM   4533  CD1 TYR A 663      12.448  42.140 -21.989  1.00 15.26           C  
ANISOU 4533  CD1 TYR A 663     2150   2399   1250    892   -472    106       C  
ATOM   4534  CD2 TYR A 663      11.321  41.234 -23.883  1.00 63.93           C  
ANISOU 4534  CD2 TYR A 663     8437   8409   7447    786   -416    177       C  
ATOM   4535  CE1 TYR A 663      11.304  42.819 -21.626  1.00 32.16           C  
ANISOU 4535  CE1 TYR A 663     4280   4517   3422    821   -467    107       C  
ATOM   4536  CE2 TYR A 663      10.174  41.910 -23.532  1.00 80.72           C  
ANISOU 4536  CE2 TYR A 663    10546  10519   9604    718   -415    175       C  
ATOM   4537  CZ  TYR A 663      10.173  42.704 -22.397  1.00 68.80           C  
ANISOU 4537  CZ  TYR A 663     8973   9074   8095    735   -438    143       C  
ATOM   4538  OH  TYR A 663       9.046  43.390 -22.024  1.00 84.90           O  
ANISOU 4538  OH  TYR A 663    10997  11097  10165    672   -435    143       O  
ATOM   4539  N   LEU A 664      11.868  38.748 -21.527  1.00 39.35           N  
ANISOU 4539  N   LEU A 664     5448   5345   4158   1023   -403    230       N  
ATOM   4540  CA  LEU A 664      11.052  38.764 -20.315  1.00 51.99           C  
ANISOU 4540  CA  LEU A 664     7064   6958   5732   1040   -401    240       C  
ATOM   4541  C   LEU A 664      11.640  37.977 -19.151  1.00 57.45           C  
ANISOU 4541  C   LEU A 664     7793   7703   6331   1182   -402    256       C  
ATOM   4542  O   LEU A 664      11.258  38.195 -18.007  1.00 45.58           O  
ANISOU 4542  O   LEU A 664     6283   6239   4796   1221   -411    253       O  
ATOM   4543  CB  LEU A 664       9.633  38.269 -20.606  1.00 30.86           C  
ANISOU 4543  CB  LEU A 664     4465   4185   3077    958   -362    284       C  
ATOM   4544  CG  LEU A 664       8.706  39.299 -21.246  1.00 35.45           C  
ANISOU 4544  CG  LEU A 664     4995   4737   3736    831   -371    263       C  
ATOM   4545  CD1 LEU A 664       7.361  38.687 -21.565  1.00 47.36           C  
ANISOU 4545  CD1 LEU A 664     6576   6162   5257    760   -341    300       C  
ATOM   4546  CD2 LEU A 664       8.548  40.481 -20.319  1.00 37.15           C  
ANISOU 4546  CD2 LEU A 664     5129   5018   3970    824   -399    227       C  
ATOM   4547  N   LYS A 665      12.558  37.060 -19.433  1.00 51.69           N  
ANISOU 4547  N   LYS A 665     7108   6977   5554   1269   -392    275       N  
ATOM   4548  CA  LYS A 665      13.210  36.309 -18.368  1.00 49.25           C  
ANISOU 4548  CA  LYS A 665     6838   6728   5148   1424   -394    293       C  
ATOM   4549  C   LYS A 665      13.878  37.242 -17.361  1.00 54.76           C  
ANISOU 4549  C   LYS A 665     7429   7557   5822   1492   -456    227       C  
ATOM   4550  O   LYS A 665      14.161  36.853 -16.230  1.00 59.92           O  
ANISOU 4550  O   LYS A 665     8104   8274   6389   1620   -467    233       O  
ATOM   4551  CB  LYS A 665      14.244  35.342 -18.942  1.00 70.36           C  
ANISOU 4551  CB  LYS A 665     9558   9396   7780   1509   -380    315       C  
ATOM   4552  CG  LYS A 665      14.904  34.467 -17.883  1.00125.38           C  
ANISOU 4552  CG  LYS A 665    16579  16423  14636   1687   -376    342       C  
ATOM   4553  CD  LYS A 665      15.885  33.485 -18.493  1.00148.29           C  
ANISOU 4553  CD  LYS A 665    19532  19313  17498   1773   -357    369       C  
ATOM   4554  CE  LYS A 665      16.513  32.610 -17.423  1.00164.29           C  
ANISOU 4554  CE  LYS A 665    21618  21399  19405   1965   -350    402       C  
ATOM   4555  NZ  LYS A 665      17.476  31.634 -17.999  1.00181.78           N1+
ANISOU 4555  NZ  LYS A 665    23887  23603  21579   2058   -328    432       N1+
ATOM   4556  N   HIS A 666      14.121  38.480 -17.776  1.00 47.32           N  
ANISOU 4556  N   HIS A 666     6373   6653   4953   1410   -496    162       N  
ATOM   4557  CA  HIS A 666      14.826  39.444 -16.941  1.00 61.40           C  
ANISOU 4557  CA  HIS A 666     8041   8562   6726   1460   -558     83       C  
ATOM   4558  C   HIS A 666      13.937  40.579 -16.449  1.00 60.51           C  
ANISOU 4558  C   HIS A 666     7874   8454   6662   1372   -569     51       C  
ATOM   4559  O   HIS A 666      14.343  41.366 -15.596  1.00 60.44           O  
ANISOU 4559  O   HIS A 666     7778   8545   6640   1413   -616    -17       O  
ATOM   4560  CB  HIS A 666      16.018  40.022 -17.701  1.00 66.31           C  
ANISOU 4560  CB  HIS A 666     8562   9240   7395   1451   -596     20       C  
ATOM   4561  CG  HIS A 666      17.059  39.006 -18.042  1.00 77.47           C  
ANISOU 4561  CG  HIS A 666    10007  10672   8755   1557   -596     38       C  
ATOM   4562  CD2 HIS A 666      17.585  38.632 -19.232  1.00 98.92           C  
ANISOU 4562  CD2 HIS A 666    12739  13342  11504   1533   -578     57       C  
ATOM   4563  ND1 HIS A 666      17.694  38.244 -17.085  1.00 81.06           N  
ANISOU 4563  ND1 HIS A 666    10484  11206   9107   1718   -616     41       N  
ATOM   4564  CE1 HIS A 666      18.562  37.441 -17.673  1.00118.84           C  
ANISOU 4564  CE1 HIS A 666    15296  15991  13866   1788   -609     61       C  
ATOM   4565  NE2 HIS A 666      18.515  37.656 -18.975  1.00130.42           N  
ANISOU 4565  NE2 HIS A 666    16758  17379  15415   1674   -586     71       N  
ATOM   4566  N   GLU A 667      12.729  40.665 -16.991  1.00 47.10           N  
ANISOU 4566  N   GLU A 667     6226   6652   5019   1255   -527     95       N  
ATOM   4567  CA  GLU A 667      11.792  41.707 -16.600  1.00 41.92           C  
ANISOU 4567  CA  GLU A 667     5527   5991   4411   1170   -531     75       C  
ATOM   4568  C   GLU A 667      11.419  41.627 -15.119  1.00 51.47           C  
ANISOU 4568  C   GLU A 667     6752   7254   5553   1250   -542     76       C  
ATOM   4569  O   GLU A 667      11.380  40.543 -14.535  1.00 76.30           O  
ANISOU 4569  O   GLU A 667     9982  10392   8617   1348   -521    125       O  
ATOM   4570  CB  GLU A 667      10.526  41.629 -17.453  1.00 47.63           C  
ANISOU 4570  CB  GLU A 667     6306   6597   5195   1046   -487    126       C  
ATOM   4571  CG  GLU A 667       9.580  42.789 -17.237  1.00 52.31           C  
ANISOU 4571  CG  GLU A 667     6849   7182   5846    953   -490    105       C  
ATOM   4572  CD  GLU A 667      10.206  44.100 -17.643  1.00 67.69           C  
ANISOU 4572  CD  GLU A 667     8691   9175   7853    907   -519     40       C  
ATOM   4573  OE1 GLU A 667      10.517  44.914 -16.747  1.00 59.68           O  
ANISOU 4573  OE1 GLU A 667     7604   8239   6831    936   -552    -15       O  
ATOM   4574  OE2 GLU A 667      10.403  44.305 -18.860  1.00 66.76           O1-
ANISOU 4574  OE2 GLU A 667     8566   9014   7786    846   -509     44       O1-
ATOM   4575  N   THR A 668      11.141  42.780 -14.521  1.00 60.41           N  
ANISOU 4575  N   THR A 668     7806   8433   6713   1214   -568     24       N  
ATOM   4576  CA  THR A 668      10.723  42.847 -13.124  1.00 62.67           C  
ANISOU 4576  CA  THR A 668     8103   8772   6938   1284   -580     21       C  
ATOM   4577  C   THR A 668       9.438  43.657 -12.955  1.00 55.48           C  
ANISOU 4577  C   THR A 668     7183   7813   6085   1176   -562     30       C  
ATOM   4578  O   THR A 668       8.807  43.623 -11.896  1.00 54.33           O  
ANISOU 4578  O   THR A 668     7066   7685   5894   1217   -558     46       O  
ATOM   4579  CB  THR A 668      11.817  43.464 -12.240  1.00 64.62           C  
ANISOU 4579  CB  THR A 668     8252   9159   7141   1380   -644    -69       C  
ATOM   4580  CG2 THR A 668      12.877  42.433 -11.903  1.00 60.28           C  
ANISOU 4580  CG2 THR A 668     7732   8676   6494   1535   -664    -66       C  
ATOM   4581  OG1 THR A 668      12.432  44.553 -12.939  1.00 89.87           O  
ANISOU 4581  OG1 THR A 668    11340  12384  10422   1302   -672   -145       O  
ATOM   4582  N   GLU A 669       9.055  44.373 -14.008  1.00 54.04           N  
ANISOU 4582  N   GLU A 669     6966   7571   5997   1048   -549     23       N  
ATOM   4583  CA  GLU A 669       7.924  45.298 -13.955  1.00 56.27           C  
ANISOU 4583  CA  GLU A 669     7226   7816   6339    946   -536     24       C  
ATOM   4584  C   GLU A 669       6.618  44.647 -14.398  1.00 38.79           C  
ANISOU 4584  C   GLU A 669     5096   5498   4145    878   -490     99       C  
ATOM   4585  O   GLU A 669       6.586  43.901 -15.372  1.00 66.58           O  
ANISOU 4585  O   GLU A 669     8666   8954   7679    850   -467    135       O  
ATOM   4586  CB  GLU A 669       8.204  46.525 -14.823  1.00 46.65           C  
ANISOU 4586  CB  GLU A 669     5923   6595   5205    855   -547    -25       C  
ATOM   4587  CG  GLU A 669       9.574  47.148 -14.601  1.00 88.55           C  
ANISOU 4587  CG  GLU A 669    11137  11999  10508    908   -591   -109       C  
ATOM   4588  CD  GLU A 669       9.685  47.854 -13.267  1.00114.82           C  
ANISOU 4588  CD  GLU A 669    14404  15418  13805    958   -627   -173       C  
ATOM   4589  OE1 GLU A 669       9.267  49.028 -13.182  1.00129.80           O  
ANISOU 4589  OE1 GLU A 669    16245  17314  15758    887   -627   -209       O  
ATOM   4590  OE2 GLU A 669      10.193  47.240 -12.303  1.00109.18           O1-
ANISOU 4590  OE2 GLU A 669    13699  14779  13006   1075   -655   -188       O1-
ATOM   4591  N   ILE A 670       5.543  44.952 -13.681  1.00 42.45           N  
ANISOU 4591  N   ILE A 670     5571   5950   4610    852   -479    115       N  
ATOM   4592  CA  ILE A 670       4.240  44.343 -13.924  1.00 40.52           C  
ANISOU 4592  CA  ILE A 670     5397   5619   4380    792   -440    177       C  
ATOM   4593  C   ILE A 670       3.752  44.498 -15.363  1.00 52.43           C  
ANISOU 4593  C   ILE A 670     6902   7056   5965    680   -427    187       C  
ATOM   4594  O   ILE A 670       3.417  43.516 -16.022  1.00 47.11           O  
ANISOU 4594  O   ILE A 670     6293   6318   5287    662   -403    227       O  
ATOM   4595  CB  ILE A 670       3.161  44.960 -13.015  1.00 49.95           C  
ANISOU 4595  CB  ILE A 670     6579   6819   5579    766   -436    182       C  
ATOM   4596  CG1 ILE A 670       3.701  45.195 -11.603  1.00 60.96           C  
ANISOU 4596  CG1 ILE A 670     7955   8304   6904    873   -460    153       C  
ATOM   4597  CG2 ILE A 670       1.927  44.079 -12.997  1.00 52.25           C  
ANISOU 4597  CG2 ILE A 670     6954   7036   5864    734   -396    247       C  
ATOM   4598  CD1 ILE A 670       3.646  43.980 -10.709  1.00 64.57           C  
ANISOU 4598  CD1 ILE A 670     8507   8762   7267    982   -437    205       C  
ATOM   4599  N   MET A 671       3.700  45.740 -15.835  1.00 50.58           N  
ANISOU 4599  N   MET A 671     6594   6832   5794    612   -440    151       N  
ATOM   4600  CA  MET A 671       3.062  46.066 -17.112  1.00 45.78           C  
ANISOU 4600  CA  MET A 671     5981   6162   5251    513   -429    162       C  
ATOM   4601  C   MET A 671       3.465  45.144 -18.268  1.00 47.77           C  
ANISOU 4601  C   MET A 671     6279   6368   5501    508   -419    182       C  
ATOM   4602  O   MET A 671       2.600  44.561 -18.924  1.00 39.33           O  
ANISOU 4602  O   MET A 671     5257   5241   4447    458   -404    213       O  
ATOM   4603  CB  MET A 671       3.300  47.541 -17.467  1.00 73.93           C  
ANISOU 4603  CB  MET A 671     9468   9750   8870    468   -440    121       C  
ATOM   4604  CG  MET A 671       2.564  48.042 -18.710  1.00 91.44           C  
ANISOU 4604  CG  MET A 671    11683  11913  11146    381   -427    136       C  
ATOM   4605  SD  MET A 671       0.827  48.464 -18.459  1.00 95.09           S  
ANISOU 4605  SD  MET A 671    12148  12347  11636    314   -416    160       S  
ATOM   4606  CE  MET A 671       0.042  46.859 -18.608  1.00 40.04           C  
ANISOU 4606  CE  MET A 671     5255   5325   4632    309   -407    205       C  
ATOM   4607  N   PRO A 672       4.777  45.008 -18.523  1.00 47.47           N  
ANISOU 4607  N   PRO A 672     6228   6363   5447    562   -430    161       N  
ATOM   4608  CA  PRO A 672       5.254  44.161 -19.621  1.00 10.94           C  
ANISOU 4608  CA  PRO A 672     1646   1696    817    563   -420    178       C  
ATOM   4609  C   PRO A 672       4.862  42.700 -19.431  1.00 49.66           C  
ANISOU 4609  C   PRO A 672     6641   6557   5671    596   -399    224       C  
ATOM   4610  O   PRO A 672       4.333  42.070 -20.350  1.00 49.72           O  
ANISOU 4610  O   PRO A 672     6697   6502   5692    549   -383    248       O  
ATOM   4611  CB  PRO A 672       6.773  44.297 -19.524  1.00 18.70           C  
ANISOU 4611  CB  PRO A 672     2589   2739   1777    636   -440    144       C  
ATOM   4612  CG  PRO A 672       7.004  45.560 -18.793  1.00 19.43           C  
ANISOU 4612  CG  PRO A 672     2599   2895   1887    637   -462     97       C  
ATOM   4613  CD  PRO A 672       5.890  45.662 -17.819  1.00 33.99           C  
ANISOU 4613  CD  PRO A 672     4457   4735   3721    624   -456    112       C  
ATOM   4614  N   VAL A 673       5.128  42.165 -18.243  1.00 32.05           N  
ANISOU 4614  N   VAL A 673     4438   4360   3379    683   -396    235       N  
ATOM   4615  CA  VAL A 673       4.818  40.770 -17.939  1.00 42.93           C  
ANISOU 4615  CA  VAL A 673     5916   5694   4702    729   -364    285       C  
ATOM   4616  C   VAL A 673       3.361  40.437 -18.241  1.00 35.77           C  
ANISOU 4616  C   VAL A 673     5055   4715   3822    644   -339    318       C  
ATOM   4617  O   VAL A 673       3.058  39.376 -18.775  1.00 42.65           O  
ANISOU 4617  O   VAL A 673     6004   5523   4679    632   -310    352       O  
ATOM   4618  CB  VAL A 673       5.132  40.418 -16.474  1.00 26.59           C  
ANISOU 4618  CB  VAL A 673     3873   3675   2557    842   -360    298       C  
ATOM   4619  CG1 VAL A 673       4.815  38.964 -16.210  1.00 26.45           C  
ANISOU 4619  CG1 VAL A 673     3974   3598   2479    895   -310    361       C  
ATOM   4620  CG2 VAL A 673       6.592  40.699 -16.158  1.00 29.12           C  
ANISOU 4620  CG2 VAL A 673     4141   4081   2841    936   -394    258       C  
ATOM   4621  N   PHE A 674       2.455  41.345 -17.902  1.00 30.33           N  
ANISOU 4621  N   PHE A 674     4318   4037   3170    584   -350    306       N  
ATOM   4622  CA  PHE A 674       1.046  41.125 -18.194  1.00 58.99           C  
ANISOU 4622  CA  PHE A 674     7977   7610   6825    503   -335    331       C  
ATOM   4623  C   PHE A 674       0.778  41.150 -19.694  1.00 39.75           C  
ANISOU 4623  C   PHE A 674     5534   5134   4435    423   -345    320       C  
ATOM   4624  O   PHE A 674      -0.084  40.425 -20.191  1.00 49.80           O  
ANISOU 4624  O   PHE A 674     6861   6354   5708    375   -330    344       O  
ATOM   4625  CB  PHE A 674       0.154  42.128 -17.454  1.00 52.56           C  
ANISOU 4625  CB  PHE A 674     7110   6823   6037    465   -345    320       C  
ATOM   4626  CG  PHE A 674      -0.411  41.593 -16.172  1.00 59.62           C  
ANISOU 4626  CG  PHE A 674     8058   7713   6880    512   -317    357       C  
ATOM   4627  CD1 PHE A 674      -1.235  40.477 -16.179  1.00 89.48           C  
ANISOU 4627  CD1 PHE A 674    11930  11429  10639    495   -274    406       C  
ATOM   4628  CD2 PHE A 674      -0.116  42.192 -14.962  1.00 76.07           C  
ANISOU 4628  CD2 PHE A 674    10110   9858   8936    574   -326    345       C  
ATOM   4629  CE1 PHE A 674      -1.755  39.972 -15.007  1.00 86.45           C  
ANISOU 4629  CE1 PHE A 674    11608  11031  10206    541   -231    449       C  
ATOM   4630  CE2 PHE A 674      -0.636  41.692 -13.783  1.00 95.68           C  
ANISOU 4630  CE2 PHE A 674    12653  12337  11365    627   -294    384       C  
ATOM   4631  CZ  PHE A 674      -1.456  40.580 -13.807  1.00 86.44           C  
ANISOU 4631  CZ  PHE A 674    11578  11092  10174    611   -242    440       C  
ATOM   4632  N   GLN A 675       1.519  41.985 -20.411  1.00 52.07           N  
ANISOU 4632  N   GLN A 675     7033   6721   6030    412   -368    285       N  
ATOM   4633  CA  GLN A 675       1.430  41.989 -21.861  1.00 56.67           C  
ANISOU 4633  CA  GLN A 675     7616   7271   6644    356   -376    277       C  
ATOM   4634  C   GLN A 675       1.876  40.636 -22.387  1.00 59.58           C  
ANISOU 4634  C   GLN A 675     8066   7597   6975    386   -358    300       C  
ATOM   4635  O   GLN A 675       1.181  40.010 -23.186  1.00 46.26           O  
ANISOU 4635  O   GLN A 675     6425   5863   5289    338   -353    313       O  
ATOM   4636  CB  GLN A 675       2.284  43.106 -22.457  1.00 49.28           C  
ANISOU 4636  CB  GLN A 675     6612   6367   5743    354   -391    244       C  
ATOM   4637  CG  GLN A 675       1.695  44.476 -22.230  1.00 65.26           C  
ANISOU 4637  CG  GLN A 675     8569   8417   7811    311   -401    226       C  
ATOM   4638  CD  GLN A 675       0.227  44.518 -22.584  1.00 71.88           C  
ANISOU 4638  CD  GLN A 675     9415   9226   8670    243   -405    239       C  
ATOM   4639  NE2 GLN A 675      -0.614  44.765 -21.588  1.00 54.05           N  
ANISOU 4639  NE2 GLN A 675     7143   6980   6412    231   -404    246       N  
ATOM   4640  OE1 GLN A 675      -0.149  44.319 -23.742  1.00 47.43           O  
ANISOU 4640  OE1 GLN A 675     6337   6100   5585    205   -411    242       O  
ATOM   4641  N   GLY A 676       3.034  40.183 -21.920  1.00 41.77           N  
ANISOU 4641  N   GLY A 676     5828   5362   4680    470   -348    303       N  
ATOM   4642  CA  GLY A 676       3.535  38.877 -22.297  1.00 36.02           C  
ANISOU 4642  CA  GLY A 676     5183   4593   3909    513   -323    330       C  
ATOM   4643  C   GLY A 676       2.488  37.810 -22.066  1.00 49.85           C  
ANISOU 4643  C   GLY A 676     7024   6283   5635    491   -288    370       C  
ATOM   4644  O   GLY A 676       2.111  37.083 -22.988  1.00 44.34           O  
ANISOU 4644  O   GLY A 676     6381   5528   4937    448   -274    382       O  
ATOM   4645  N   LEU A 677       2.005  37.729 -20.831  1.00 19.17           N  
ANISOU 4645  N   LEU A 677     3154   2405   1725    519   -269    392       N  
ATOM   4646  CA  LEU A 677       1.022  36.717 -20.455  1.00 48.93           C  
ANISOU 4646  CA  LEU A 677     7015   6107   5467    503   -218    439       C  
ATOM   4647  C   LEU A 677      -0.269  36.838 -21.252  1.00 45.64           C  
ANISOU 4647  C   LEU A 677     6595   5655   5093    389   -228    434       C  
ATOM   4648  O   LEU A 677      -0.867  35.837 -21.632  1.00 35.03           O  
ANISOU 4648  O   LEU A 677     5333   4240   3735    354   -186    464       O  
ATOM   4649  CB  LEU A 677       0.714  36.805 -18.962  1.00 31.09           C  
ANISOU 4649  CB  LEU A 677     4768   3870   3176    556   -195    463       C  
ATOM   4650  CG  LEU A 677       1.864  36.500 -17.997  1.00 47.53           C  
ANISOU 4650  CG  LEU A 677     6873   5991   5194    688   -182    477       C  
ATOM   4651  CD1 LEU A 677       1.398  36.679 -16.569  1.00 35.61           C  
ANISOU 4651  CD1 LEU A 677     5375   4505   3649    737   -162    499       C  
ATOM   4652  CD2 LEU A 677       2.401  35.099 -18.221  1.00 26.85           C  
ANISOU 4652  CD2 LEU A 677     4364   3312   2524    751   -126    519       C  
ATOM   4653  N   ASN A 678      -0.700  38.065 -21.511  1.00 35.49           N  
ANISOU 4653  N   ASN A 678     5215   4415   3855    334   -277    397       N  
ATOM   4654  CA  ASN A 678      -1.965  38.269 -22.208  1.00 52.25           C  
ANISOU 4654  CA  ASN A 678     7325   6519   6007    239   -295    391       C  
ATOM   4655  C   ASN A 678      -1.943  37.801 -23.666  1.00 41.16           C  
ANISOU 4655  C   ASN A 678     5949   5085   4606    197   -308    380       C  
ATOM   4656  O   ASN A 678      -2.984  37.488 -24.237  1.00 31.53           O  
ANISOU 4656  O   ASN A 678     4754   3839   3386    129   -312    385       O  
ATOM   4657  CB  ASN A 678      -2.402  39.732 -22.121  1.00 54.48           C  
ANISOU 4657  CB  ASN A 678     7504   6859   6337    203   -340    358       C  
ATOM   4658  CG  ASN A 678      -3.840  39.934 -22.562  1.00 99.58           C  
ANISOU 4658  CG  ASN A 678    13202  12565  12068    119   -358    357       C  
ATOM   4659  ND2 ASN A 678      -4.121  41.088 -23.157  1.00122.43           N  
ANISOU 4659  ND2 ASN A 678    16017  15498  15005     85   -399    324       N  
ATOM   4660  OD1 ASN A 678      -4.686  39.062 -22.369  1.00 85.84           O  
ANISOU 4660  OD1 ASN A 678    11528  10784  10304     88   -327    389       O  
ATOM   4661  N   GLU A 679      -0.755  37.748 -24.261  1.00 27.83           N  
ANISOU 4661  N   GLU A 679     4258   3403   2914    241   -316    365       N  
ATOM   4662  CA  GLU A 679      -0.624  37.375 -25.665  1.00 49.74           C  
ANISOU 4662  CA  GLU A 679     7059   6153   5687    212   -329    352       C  
ATOM   4663  C   GLU A 679      -0.085  35.959 -25.837  1.00 55.83           C  
ANISOU 4663  C   GLU A 679     7934   6863   6414    247   -282    382       C  
ATOM   4664  O   GLU A 679      -0.224  35.362 -26.907  1.00 34.64           O  
ANISOU 4664  O   GLU A 679     5298   4144   3719    214   -281    380       O  
ATOM   4665  CB  GLU A 679       0.270  38.372 -26.408  1.00 43.62           C  
ANISOU 4665  CB  GLU A 679     6213   5420   4943    229   -362    317       C  
ATOM   4666  CG  GLU A 679      -0.301  39.783 -26.474  1.00 68.51           C  
ANISOU 4666  CG  GLU A 679     9274   8615   8141    189   -395    292       C  
ATOM   4667  CD  GLU A 679      -1.666  39.827 -27.141  1.00110.63           C  
ANISOU 4667  CD  GLU A 679    14610  13945  13481    119   -421    286       C  
ATOM   4668  OE1 GLU A 679      -1.860  39.113 -28.150  1.00 97.96           O  
ANISOU 4668  OE1 GLU A 679    13055  12315  11851     98   -430    284       O  
ATOM   4669  OE2 GLU A 679      -2.541  40.577 -26.660  1.00141.57           O1-
ANISOU 4669  OE2 GLU A 679    18478  17890  17423     88   -436    281       O1-
ATOM   4670  N   LEU A 680       0.528  35.427 -24.782  1.00 50.75           N  
ANISOU 4670  N   LEU A 680     7331   6210   5743    320   -239    411       N  
ATOM   4671  CA  LEU A 680       1.140  34.100 -24.837  1.00 49.47           C  
ANISOU 4671  CA  LEU A 680     7272   5987   5539    371   -182    445       C  
ATOM   4672  C   LEU A 680       0.197  32.999 -24.365  1.00 52.91           C  
ANISOU 4672  C   LEU A 680     7810   6337   5956    343   -107    492       C  
ATOM   4673  O   LEU A 680       0.068  31.968 -25.021  1.00 63.95           O  
ANISOU 4673  O   LEU A 680     9283   7659   7355    314    -57    492       O  
ATOM   4674  CB  LEU A 680       2.444  34.068 -24.040  1.00 42.18           C  
ANISOU 4674  CB  LEU A 680     6342   5100   4585    483   -172    452       C  
ATOM   4675  CG  LEU A 680       3.637  34.722 -24.738  1.00 57.00           C  
ANISOU 4675  CG  LEU A 680     8152   7030   6477    514   -215    416       C  
ATOM   4676  CD1 LEU A 680       4.905  34.615 -23.905  1.00 10.24           C  
ANISOU 4676  CD1 LEU A 680     2223   1150    516    629   -206    424       C  
ATOM   4677  CD2 LEU A 680       3.838  34.093 -26.105  1.00 29.94           C  
ANISOU 4677  CD2 LEU A 680     4773   3556   3047    486   -209    413       C  
ATOM   4678  N   ILE A 681      -0.460  33.217 -23.231  1.00 43.37           N  
ANISOU 4678  N   ILE A 681     6595   5134   4748    344    -85    512       N  
ATOM   4679  CA  ILE A 681      -1.384  32.223 -22.691  1.00 33.52           C  
ANISOU 4679  CA  ILE A 681     5428   3796   3513    309     11    531       C  
ATOM   4680  C   ILE A 681      -2.391  31.721 -23.722  1.00 43.46           C  
ANISOU 4680  C   ILE A 681     6688   4994   4832    190     36    473       C  
ATOM   4681  O   ILE A 681      -2.445  30.524 -24.012  1.00 52.98           O  
ANISOU 4681  O   ILE A 681     7977   6108   6045    174    117    470       O  
ATOM   4682  CB  ILE A 681      -2.174  32.760 -21.492  1.00 39.72           C  
ANISOU 4682  CB  ILE A 681     6183   4603   4305    304     23    545       C  
ATOM   4683  CG1 ILE A 681      -1.235  33.339 -20.430  1.00 46.73           C  
ANISOU 4683  CG1 ILE A 681     7048   5565   5141    420     -9    573       C  
ATOM   4684  CG2 ILE A 681      -3.070  31.670 -20.946  1.00 13.26           C  
ANISOU 4684  CG2 ILE A 681     2916   1147    977    269    142    557       C  
ATOM   4685  CD1 ILE A 681      -0.910  32.415 -19.306  1.00 24.15           C  
ANISOU 4685  CD1 ILE A 681     4288   2660   2226    518     78    629       C  
ATOM   4686  N   PRO A 682      -3.193  32.640 -24.283  1.00 52.46           N  
ANISOU 4686  N   PRO A 682     7734   6185   6014    109    -32    422       N  
ATOM   4687  CA  PRO A 682      -4.249  32.261 -25.227  1.00 54.70           C  
ANISOU 4687  CA  PRO A 682     8001   6430   6352     -1    -21    354       C  
ATOM   4688  C   PRO A 682      -3.753  31.270 -26.272  1.00 48.13           C  
ANISOU 4688  C   PRO A 682     7233   5540   5513     -8      7    332       C  
ATOM   4689  O   PRO A 682      -4.529  30.460 -26.769  1.00 53.44           O  
ANISOU 4689  O   PRO A 682     7929   6147   6227    -88     58    279       O  
ATOM   4690  CB  PRO A 682      -4.604  33.592 -25.895  1.00 22.95           C  
ANISOU 4690  CB  PRO A 682     3870   2503   2345    -36   -128    316       C  
ATOM   4691  CG  PRO A 682      -4.271  34.614 -24.874  1.00 59.27           C  
ANISOU 4691  CG  PRO A 682     8428   7169   6923     24   -163    362       C  
ATOM   4692  CD  PRO A 682      -3.060  34.102 -24.166  1.00 51.65           C  
ANISOU 4692  CD  PRO A 682     7534   6186   5906    125   -127    422       C  
ATOM   4693  N   MET A 683      -2.467  31.345 -26.598  1.00 57.46           N  
ANISOU 4693  N   MET A 683     8437   6747   6646     73    -25    366       N  
ATOM   4694  CA  MET A 683      -1.879  30.462 -27.593  1.00 68.31           C  
ANISOU 4694  CA  MET A 683     9874   8072   8009     78     -1    350       C  
ATOM   4695  C   MET A 683      -1.995  28.998 -27.192  1.00 60.02           C  
ANISOU 4695  C   MET A 683     8933   6906   6966     76    121    363       C  
ATOM   4696  O   MET A 683      -2.490  28.176 -27.963  1.00 73.22           O  
ANISOU 4696  O   MET A 683    10638   8510   8670      5    164    309       O  
ATOM   4697  CB  MET A 683      -0.415  30.828 -27.848  1.00 68.86           C  
ANISOU 4697  CB  MET A 683     9947   8191   8027    175    -49    391       C  
ATOM   4698  CG  MET A 683      -0.219  32.180 -28.520  1.00 63.28           C  
ANISOU 4698  CG  MET A 683     9144   7581   7319    171   -152    372       C  
ATOM   4699  SD  MET A 683       1.510  32.539 -28.890  1.00 56.90           S  
ANISOU 4699  SD  MET A 683     8335   6818   6464    274   -190    408       S  
ATOM   4700  CE  MET A 683       1.393  34.225 -29.469  1.00 62.11           C  
ANISOU 4700  CE  MET A 683     8869   7572   7159    246   -280    363       C  
ATOM   4701  N   TYR A 684      -1.549  28.665 -25.984  1.00 59.77           N  
ANISOU 4701  N   TYR A 684     8960   6848   6901    158    181    432       N  
ATOM   4702  CA  TYR A 684      -1.586  27.271 -25.546  1.00 73.86           C  
ANISOU 4702  CA  TYR A 684    10864   8514   8686    174    312    457       C  
ATOM   4703  C   TYR A 684      -2.984  26.822 -25.141  1.00 59.36           C  
ANISOU 4703  C   TYR A 684     9036   6602   6914     74    396    421       C  
ATOM   4704  O   TYR A 684      -3.241  25.631 -24.997  1.00 70.85           O  
ANISOU 4704  O   TYR A 684    10587   7942   8392     55    518    421       O  
ATOM   4705  CB  TYR A 684      -0.555  26.985 -24.446  1.00 64.50           C  
ANISOU 4705  CB  TYR A 684     9750   7326   7430    316    353    547       C  
ATOM   4706  CG  TYR A 684      -0.766  27.697 -23.127  1.00 70.32           C  
ANISOU 4706  CG  TYR A 684    10456   8117   8146    365    340    589       C  
ATOM   4707  CD1 TYR A 684      -1.583  27.151 -22.141  1.00 64.94           C  
ANISOU 4707  CD1 TYR A 684     9833   7361   7479    353    445    612       C  
ATOM   4708  CD2 TYR A 684      -0.115  28.890 -22.847  1.00 90.79           C  
ANISOU 4708  CD2 TYR A 684    12964  10830  10703    426    232    603       C  
ATOM   4709  CE1 TYR A 684      -1.764  27.783 -20.924  1.00 37.76           C  
ANISOU 4709  CE1 TYR A 684     6367   3968   4010    405    436    652       C  
ATOM   4710  CE2 TYR A 684      -0.287  29.530 -21.633  1.00105.39           C  
ANISOU 4710  CE2 TYR A 684    14785  12731  12528    473    219    635       C  
ATOM   4711  CZ  TYR A 684      -1.116  28.970 -20.677  1.00 88.28           C  
ANISOU 4711  CZ  TYR A 684    12680  10493  10370    465    319    661       C  
ATOM   4712  OH  TYR A 684      -1.301  29.591 -19.467  1.00 79.04           O  
ANISOU 4712  OH  TYR A 684    11487   9373   9171    516    309    693       O  
ATOM   4713  N   LYS A 685      -3.890  27.777 -24.971  1.00 51.04           N  
ANISOU 4713  N   LYS A 685     7884   5612   5896     10    337    387       N  
ATOM   4714  CA  LYS A 685      -5.281  27.442 -24.706  1.00 65.29           C  
ANISOU 4714  CA  LYS A 685     9677   7357   7773    -97    408    337       C  
ATOM   4715  C   LYS A 685      -5.990  26.988 -25.981  1.00 56.07           C  
ANISOU 4715  C   LYS A 685     8481   6157   6666   -215    406    235       C  
ATOM   4716  O   LYS A 685      -7.098  26.462 -25.934  1.00 76.92           O  
ANISOU 4716  O   LYS A 685    11117   8734   9377   -313    480    174       O  
ATOM   4717  CB  LYS A 685      -6.015  28.612 -24.048  1.00 39.96           C  
ANISOU 4717  CB  LYS A 685     6371   4230   4581   -119    348    335       C  
ATOM   4718  CG  LYS A 685      -5.795  28.687 -22.545  1.00 47.68           C  
ANISOU 4718  CG  LYS A 685     7396   5199   5520    -32    402    419       C  
ATOM   4719  CD  LYS A 685      -6.875  29.509 -21.863  1.00102.23           C  
ANISOU 4719  CD  LYS A 685    14226  12149  12468    -84    386    403       C  
ATOM   4720  CE  LYS A 685      -6.799  29.366 -20.350  1.00114.44           C  
ANISOU 4720  CE  LYS A 685    15838  13667  13978     -3    465    481       C  
ATOM   4721  NZ  LYS A 685      -7.865  30.139 -19.657  1.00117.25           N1+
ANISOU 4721  NZ  LYS A 685    16120  14057  14371    -54    457    466       N1+
ATOM   4722  N   LEU A 686      -5.335  27.194 -27.118  1.00 41.73           N  
ANISOU 4722  N   LEU A 686     6644   4388   4822   -201    323    210       N  
ATOM   4723  CA  LEU A 686      -5.833  26.713 -28.404  1.00 52.03           C  
ANISOU 4723  CA  LEU A 686     7932   5671   6167   -294    314    113       C  
ATOM   4724  C   LEU A 686      -5.198  25.365 -28.717  1.00 63.53           C  
ANISOU 4724  C   LEU A 686     9507   7017   7615   -274    413    120       C  
ATOM   4725  O   LEU A 686      -5.766  24.545 -29.440  1.00 59.98           O  
ANISOU 4725  O   LEU A 686     9075   6502   7214   -362    464     36       O  
ATOM   4726  CB  LEU A 686      -5.528  27.713 -29.523  1.00 31.00           C  
ANISOU 4726  CB  LEU A 686     5185   3120   3472   -285    173     82       C  
ATOM   4727  CG  LEU A 686      -6.570  28.794 -29.813  1.00 55.37           C  
ANISOU 4727  CG  LEU A 686     8149   6301   6589   -349     81     22       C  
ATOM   4728  CD1 LEU A 686      -6.735  29.732 -28.626  1.00 83.58           C  
ANISOU 4728  CD1 LEU A 686    11677   9923  10157   -313     62     83       C  
ATOM   4729  CD2 LEU A 686      -6.205  29.581 -31.062  1.00 40.36           C  
ANISOU 4729  CD2 LEU A 686     6192   4491   4650   -331    -37     -6       C  
ATOM   4730  N   MET A 687      -4.008  25.152 -28.170  1.00 51.62           N  
ANISOU 4730  N   MET A 687     8076   5492   6043   -156    440    215       N  
ATOM   4731  CA  MET A 687      -3.312  23.884 -28.302  1.00 67.38           C  
ANISOU 4731  CA  MET A 687    10196   7382   8023   -115    542    240       C  
ATOM   4732  C   MET A 687      -3.944  22.851 -27.376  1.00 63.63           C  
ANISOU 4732  C   MET A 687     9808   6777   7590   -142    702    254       C  
ATOM   4733  O   MET A 687      -4.094  21.687 -27.741  1.00 63.95           O  
ANISOU 4733  O   MET A 687     9931   6703   7665   -186    811    219       O  
ATOM   4734  CB  MET A 687      -1.833  24.060 -27.961  1.00 67.68           C  
ANISOU 4734  CB  MET A 687    10280   7460   7977     32    513    337       C  
ATOM   4735  CG  MET A 687      -1.122  25.113 -28.800  1.00 54.03           C  
ANISOU 4735  CG  MET A 687     8468   5851   6212     63    371    329       C  
ATOM   4736  SD  MET A 687       0.571  25.407 -28.253  1.00 70.50           S  
ANISOU 4736  SD  MET A 687    10584   7991   8211    231    339    430       S  
ATOM   4737  CE  MET A 687       1.129  26.592 -29.469  1.00 47.17           C  
ANISOU 4737  CE  MET A 687     7526   5154   5241    226    195    395       C  
ATOM   4738  N   GLU A 688      -4.312  23.292 -26.175  1.00 69.58           N  
ANISOU 4738  N   GLU A 688    10550   7547   8342   -115    724    305       N  
ATOM   4739  CA  GLU A 688      -4.976  22.435 -25.195  1.00 46.91           C  
ANISOU 4739  CA  GLU A 688     7760   4554   5509   -135    882    326       C  
ATOM   4740  C   GLU A 688      -6.167  21.708 -25.800  1.00 56.14           C  
ANISOU 4740  C   GLU A 688     8918   5633   6780   -290    964    214       C  
ATOM   4741  O   GLU A 688      -6.433  20.550 -25.469  1.00 66.87           O  
ANISOU 4741  O   GLU A 688    10380   6850   8179   -314   1125    214       O  
ATOM   4742  CB  GLU A 688      -5.449  23.256 -23.995  1.00 58.35           C  
ANISOU 4742  CB  GLU A 688     9163   6056   6951   -109    868    372       C  
ATOM   4743  CG  GLU A 688      -4.384  23.531 -22.954  1.00 66.91           C  
ANISOU 4743  CG  GLU A 688    10302   7182   7939     54    858    488       C  
ATOM   4744  CD  GLU A 688      -4.948  24.214 -21.727  1.00 90.10           C  
ANISOU 4744  CD  GLU A 688    13206  10157  10872     74    862    527       C  
ATOM   4745  OE1 GLU A 688      -5.928  24.977 -21.864  1.00112.26           O  
ANISOU 4745  OE1 GLU A 688    15904  13014  13734    -26    805    466       O  
ATOM   4746  OE2 GLU A 688      -4.410  23.988 -20.624  1.00 66.81           O1-
ANISOU 4746  OE2 GLU A 688    10338   7189   7857    196    921    617       O1-
ATOM   4747  N   LYS A 689      -6.888  22.394 -26.681  1.00 45.60           N  
ANISOU 4747  N   LYS A 689     7457   4380   5488   -391    855    114       N  
ATOM   4748  CA  LYS A 689      -8.081  21.826 -27.298  1.00 56.07           C  
ANISOU 4748  CA  LYS A 689     8745   5645   6914   -543    911    -13       C  
ATOM   4749  C   LYS A 689      -7.751  21.210 -28.650  1.00 71.22           C  
ANISOU 4749  C   LYS A 689    10681   7543   8836   -581    892    -89       C  
ATOM   4750  O   LYS A 689      -8.557  21.239 -29.579  1.00 74.12           O  
ANISOU 4750  O   LYS A 689    10966   7938   9259   -692    847   -214       O  
ATOM   4751  CB  LYS A 689      -9.169  22.893 -27.412  1.00 53.04           C  
ANISOU 4751  CB  LYS A 689     8212   5368   6573   -625    809    -85       C  
ATOM   4752  CG  LYS A 689      -9.353  23.643 -26.103  1.00 51.54           C  
ANISOU 4752  CG  LYS A 689     8003   5214   6366   -572    810     -1       C  
ATOM   4753  CD  LYS A 689     -10.684  24.349 -25.987  1.00 50.75           C  
ANISOU 4753  CD  LYS A 689     7777   5171   6334   -673    771    -77       C  
ATOM   4754  CE  LYS A 689     -10.898  24.786 -24.546  1.00 79.38           C  
ANISOU 4754  CE  LYS A 689    11415   8794   9950   -623    819      9       C  
ATOM   4755  NZ  LYS A 689      -9.624  25.257 -23.928  1.00 77.18           N1+
ANISOU 4755  NZ  LYS A 689    11194   8563   9567   -471    771    136       N1+
ATOM   4756  N   ARG A 690      -6.552  20.645 -28.738  1.00 84.14           N  
ANISOU 4756  N   ARG A 690    12425   9134  10410   -482    925    -16       N  
ATOM   4757  CA  ARG A 690      -6.089  19.993 -29.953  1.00 86.37           C  
ANISOU 4757  CA  ARG A 690    12743   9387  10687   -501    919    -74       C  
ATOM   4758  C   ARG A 690      -5.338  18.707 -29.635  1.00 96.51           C  
ANISOU 4758  C   ARG A 690    14187  10527  11955   -439   1071    -12       C  
ATOM   4759  O   ARG A 690      -4.902  18.492 -28.504  1.00 96.91           O  
ANISOU 4759  O   ARG A 690    14321  10529  11972   -344   1153     97       O  
ATOM   4760  CB  ARG A 690      -5.186  20.929 -30.749  1.00 61.14           C  
ANISOU 4760  CB  ARG A 690     9492   6325   7413   -428    754    -50       C  
ATOM   4761  CG  ARG A 690      -5.889  21.661 -31.861  1.00 71.57           C  
ANISOU 4761  CG  ARG A 690    10687   7750   8755   -514    625   -162       C  
ATOM   4762  CD  ARG A 690      -4.878  22.125 -32.892  1.00104.47           C  
ANISOU 4762  CD  ARG A 690    14845  11999  12849   -445    512   -147       C  
ATOM   4763  NE  ARG A 690      -5.510  22.513 -34.148  1.00 99.57           N  
ANISOU 4763  NE  ARG A 690    14134  11455  12242   -521    412   -263       N  
ATOM   4764  CZ  ARG A 690      -4.862  22.626 -35.303  1.00 96.78           C  
ANISOU 4764  CZ  ARG A 690    13785  11148  11839   -488    338   -284       C  
ATOM   4765  NH1 ARG A 690      -3.563  22.372 -35.363  1.00 89.98           N1+
ANISOU 4765  NH1 ARG A 690    13007  10262  10920   -389    355   -200       N1+
ATOM   4766  NH2 ARG A 690      -5.514  22.986 -36.399  1.00 98.76           N  
ANISOU 4766  NH2 ARG A 690    13956  11474  12095   -549    249   -391       N  
ATOM   4767  N   ASP A 691      -5.185  17.860 -30.645  1.00106.88           N  
ANISOU 4767  N   ASP A 691    15545  11776  13289   -485   1109    -83       N  
ATOM   4768  CA  ASP A 691      -4.527  16.576 -30.467  1.00145.03           C  
ANISOU 4768  CA  ASP A 691    20531  16461  18111   -433   1262    -36       C  
ATOM   4769  C   ASP A 691      -3.093  16.761 -29.987  1.00148.00           C  
ANISOU 4769  C   ASP A 691    20979  16872  18381   -256   1234    107       C  
ATOM   4770  O   ASP A 691      -2.703  16.242 -28.941  1.00149.16           O  
ANISOU 4770  O   ASP A 691    21232  16942  18501   -165   1348    206       O  
ATOM   4771  CB  ASP A 691      -4.551  15.781 -31.774  1.00142.56           C  
ANISOU 4771  CB  ASP A 691    20239  16094  17832   -512   1282   -145       C  
ATOM   4772  CG  ASP A 691      -4.046  14.359 -31.608  1.00141.29           C  
ANISOU 4772  CG  ASP A 691    20242  15761  17680   -478   1464   -111       C  
ATOM   4773  OD1 ASP A 691      -3.431  14.054 -30.564  1.00144.19           O  
ANISOU 4773  OD1 ASP A 691    20713  16070  18003   -362   1554     16       O  
ATOM   4774  OD2 ASP A 691      -4.264  13.543 -32.528  1.00145.99           O1-
ANISOU 4774  OD2 ASP A 691    20865  16281  18322   -563   1518   -214       O1-
ATOM   4775  N   MET A 692      -2.314  17.518 -30.752  1.00132.44           N  
ANISOU 4775  N   MET A 692    18948  15023  16349   -204   1084    114       N  
ATOM   4776  CA  MET A 692      -0.885  17.644 -30.496  1.00133.62           C  
ANISOU 4776  CA  MET A 692    19154  15211  16405    -45   1053    227       C  
ATOM   4777  C   MET A 692      -0.551  18.106 -29.082  1.00 99.14           C  
ANISOU 4777  C   MET A 692    14801  10878  11989     67   1061    341       C  
ATOM   4778  O   MET A 692      -0.805  19.247 -28.702  1.00 75.50           O  
ANISOU 4778  O   MET A 692    11705   7997   8986     67    956    350       O  
ATOM   4779  CB  MET A 692      -0.231  18.533 -31.551  1.00159.12           C  
ANISOU 4779  CB  MET A 692    22298  18572  19590    -23    889    205       C  
ATOM   4780  CG  MET A 692      -0.283  17.903 -32.929  1.00163.98           C  
ANISOU 4780  CG  MET A 692    22931  19146  20229    -96    894    110       C  
ATOM   4781  SD  MET A 692       0.389  18.918 -34.247  1.00397.16           S  
ANISOU 4781  SD  MET A 692    52373  48822  49709    -73    717     81       S  
ATOM   4782  CE  MET A 692       0.228  17.787 -35.624  1.00 67.27           C  
ANISOU 4782  CE  MET A 692    10651   6951   7956   -154    772    -28       C  
ATOM   4783  N   ASN A 693       0.023  17.189 -28.313  1.00102.63           N  
ANISOU 4783  N   ASN A 693    15377  11222  12398    168   1191    426       N  
ATOM   4784  CA  ASN A 693       0.343  17.428 -26.918  1.00 92.86           C  
ANISOU 4784  CA  ASN A 693    14175  10004  11105    289   1220    533       C  
ATOM   4785  C   ASN A 693       1.800  17.831 -26.746  1.00 61.03           C  
ANISOU 4785  C   ASN A 693    10149   6068   6973    455   1136    618       C  
ATOM   4786  O   ASN A 693       2.170  18.463 -25.759  1.00 64.56           O  
ANISOU 4786  O   ASN A 693    10573   6593   7363    556   1093    688       O  
ATOM   4787  CB  ASN A 693       0.053  16.166 -26.100  1.00 71.82           C  
ANISOU 4787  CB  ASN A 693    11660   7171   8456    316   1426    580       C  
ATOM   4788  CG  ASN A 693       0.095  16.415 -24.607  1.00100.30           C  
ANISOU 4788  CG  ASN A 693    15305  10793  12012    426   1467    680       C  
ATOM   4789  ND2 ASN A 693       0.510  15.406 -23.852  1.00 89.79           N  
ANISOU 4789  ND2 ASN A 693    14128   9350  10640    539   1620    766       N  
ATOM   4790  OD1 ASN A 693      -0.248  17.497 -24.135  1.00129.58           O  
ANISOU 4790  OD1 ASN A 693    18909  14611  15714    416   1365    680       O  
ATOM   4791  N   GLU A 694       2.628  17.463 -27.716  1.00 52.42           N  
ANISOU 4791  N   GLU A 694     9083   4973   5860    481   1114    605       N  
ATOM   4792  CA  GLU A 694       4.064  17.693 -27.624  1.00 68.21           C  
ANISOU 4792  CA  GLU A 694    11093   7052   7772    637   1051    677       C  
ATOM   4793  C   GLU A 694       4.394  19.176 -27.712  1.00 79.49           C  
ANISOU 4793  C   GLU A 694    12375   8650   9177    650    876    668       C  
ATOM   4794  O   GLU A 694       5.192  19.687 -26.930  1.00 77.13           O  
ANISOU 4794  O   GLU A 694    12056   8437   8814    776    827    734       O  
ATOM   4795  CB  GLU A 694       4.817  16.903 -28.699  1.00 87.54           C  
ANISOU 4795  CB  GLU A 694    13605   9445  10210    654   1079    660       C  
ATOM   4796  CG  GLU A 694       4.586  17.379 -30.126  1.00152.67           C  
ANISOU 4796  CG  GLU A 694    21764  17743  18501    536    979    562       C  
ATOM   4797  CD  GLU A 694       3.237  16.964 -30.685  1.00186.89           C  
ANISOU 4797  CD  GLU A 694    26093  21993  22924    366   1033    461       C  
ATOM   4798  OE1 GLU A 694       2.460  16.308 -29.963  1.00196.35           O  
ANISOU 4798  OE1 GLU A 694    27355  23087  24162    328   1157    465       O  
ATOM   4799  OE2 GLU A 694       2.956  17.291 -31.856  1.00189.21           O1-
ANISOU 4799  OE2 GLU A 694    26318  22326  23246    273    954    374       O1-
ATOM   4800  N   VAL A 695       3.780  19.867 -28.666  1.00 55.56           N  
ANISOU 4800  N   VAL A 695     9242   5669   6198    524    786    583       N  
ATOM   4801  CA  VAL A 695       3.962  21.308 -28.788  1.00 63.76           C  
ANISOU 4801  CA  VAL A 695    10145   6856   7224    523    634    571       C  
ATOM   4802  C   VAL A 695       3.362  22.015 -27.576  1.00 63.02           C  
ANISOU 4802  C   VAL A 695    10002   6810   7133    529    617    599       C  
ATOM   4803  O   VAL A 695       3.997  22.886 -26.984  1.00 58.49           O  
ANISOU 4803  O   VAL A 695     9369   6341   6514    614    539    640       O  
ATOM   4804  CB  VAL A 695       3.347  21.853 -30.096  1.00 65.23           C  
ANISOU 4804  CB  VAL A 695    10245   7079   7460    394    551    476       C  
ATOM   4805  CG1 VAL A 695       3.033  23.336 -29.974  1.00 38.42           C  
ANISOU 4805  CG1 VAL A 695     6716   3811   4070    367    425    461       C  
ATOM   4806  CG2 VAL A 695       4.282  21.595 -31.266  1.00 42.57           C  
ANISOU 4806  CG2 VAL A 695     7395   4214   4565    423    523    461       C  
ATOM   4807  N   GLU A 696       2.146  21.624 -27.206  1.00 43.82           N  
ANISOU 4807  N   GLU A 696     7594   4301   4756    438    697    572       N  
ATOM   4808  CA  GLU A 696       1.486  22.173 -26.029  1.00 34.19           C  
ANISOU 4808  CA  GLU A 696     6340   3109   3540    440    700    599       C  
ATOM   4809  C   GLU A 696       2.390  22.118 -24.806  1.00 49.96           C  
ANISOU 4809  C   GLU A 696     8393   5133   5457    604    725    698       C  
ATOM   4810  O   GLU A 696       2.532  23.107 -24.087  1.00 60.73           O  
ANISOU 4810  O   GLU A 696     9683   6600   6790    653    645    722       O  
ATOM   4811  CB  GLU A 696       0.192  21.421 -25.730  1.00 60.61           C  
ANISOU 4811  CB  GLU A 696     9737   6335   6955    336    825    566       C  
ATOM   4812  CG  GLU A 696      -0.477  21.865 -24.441  1.00 77.64           C  
ANISOU 4812  CG  GLU A 696    11877   8508   9115    348    850    603       C  
ATOM   4813  CD  GLU A 696      -1.504  20.873 -23.935  1.00 96.35           C  
ANISOU 4813  CD  GLU A 696    14332  10733  11543    280   1015    594       C  
ATOM   4814  OE1 GLU A 696      -1.988  20.045 -24.736  1.00113.92           O  
ANISOU 4814  OE1 GLU A 696    16592  12860  13831    181   1088    527       O  
ATOM   4815  OE2 GLU A 696      -1.829  20.919 -22.729  1.00 77.58           O1-
ANISOU 4815  OE2 GLU A 696    11987   8338   9150    327   1076    649       O1-
ATOM   4816  N   THR A 697       2.999  20.964 -24.573  1.00 28.42           N  
ANISOU 4816  N   THR A 697     5795   2313   2690    695    835    751       N  
ATOM   4817  CA  THR A 697       3.838  20.782 -23.393  1.00 82.97           C  
ANISOU 4817  CA  THR A 697    12769   9246   9511    868    867    845       C  
ATOM   4818  C   THR A 697       5.134  21.584 -23.479  1.00 71.17           C  
ANISOU 4818  C   THR A 697    11198   7891   7951    979    737    863       C  
ATOM   4819  O   THR A 697       5.542  22.212 -22.505  1.00 49.69           O  
ANISOU 4819  O   THR A 697     8442   5264   5175   1079    686    903       O  
ATOM   4820  CB  THR A 697       4.142  19.285 -23.104  1.00 59.38           C  
ANISOU 4820  CB  THR A 697     9952   6116   6493    951   1032    904       C  
ATOM   4821  CG2 THR A 697       2.954  18.613 -22.428  1.00 65.29           C  
ANISOU 4821  CG2 THR A 697    10783   6735   7289    888   1181    912       C  
ATOM   4822  OG1 THR A 697       4.430  18.605 -24.329  1.00 76.78           O  
ANISOU 4822  OG1 THR A 697    12191   8255   8728    900   1056    862       O  
ATOM   4823  N   GLN A 698       5.778  21.571 -24.641  1.00 54.01           N  
ANISOU 4823  N   GLN A 698     8998   5736   5787    959    685    828       N  
ATOM   4824  CA  GLN A 698       7.010  22.335 -24.823  1.00 64.45           C  
ANISOU 4824  CA  GLN A 698    10241   7186   7062   1050    570    834       C  
ATOM   4825  C   GLN A 698       6.738  23.829 -24.713  1.00 71.56           C  
ANISOU 4825  C   GLN A 698    10987   8214   7988    996    444    786       C  
ATOM   4826  O   GLN A 698       7.582  24.590 -24.246  1.00 36.24           O  
ANISOU 4826  O   GLN A 698     6426   3860   3483   1082    369    771       O  
ATOM   4827  CB  GLN A 698       7.669  22.021 -26.165  1.00 48.07           C  
ANISOU 4827  CB  GLN A 698     8170   5094   5000   1028    551    802       C  
ATOM   4828  CG  GLN A 698       8.139  20.581 -26.304  1.00 93.64           C  
ANISOU 4828  CG  GLN A 698    14086  10750  10744   1098    673    841       C  
ATOM   4829  CD  GLN A 698       8.928  20.336 -27.581  1.00 91.80           C  
ANISOU 4829  CD  GLN A 698    13852  10513  10514   1093    648    812       C  
ATOM   4830  NE2 GLN A 698       9.578  21.376 -28.082  1.00 77.69           N  
ANISOU 4830  NE2 GLN A 698    11951   8845   8725   1098    526    785       N  
ATOM   4831  OE1 GLN A 698       8.950  19.224 -28.108  1.00105.02           O  
ANISOU 4831  OE1 GLN A 698    15632  12075  12196   1084    744    813       O  
ATOM   4832  N   PHE A 699       5.554  24.250 -25.142  1.00 72.15           N  
ANISOU 4832  N   PHE A 699    11019   8266   8129    850    426    742       N  
ATOM   4833  CA  PHE A 699       5.195  25.654 -25.053  1.00 38.92           C  
ANISOU 4833  CA  PHE A 699     6677   4165   3944    797    316    706       C  
ATOM   4834  C   PHE A 699       5.045  26.063 -23.601  1.00 48.97           C  
ANISOU 4834  C   PHE A 699     7927   5489   5190    864    319    730       C  
ATOM   4835  O   PHE A 699       5.647  27.039 -23.155  1.00 76.06           O  
ANISOU 4835  O   PHE A 699    11256   9037   8607    919    238    704       O  
ATOM   4836  CB  PHE A 699       3.909  25.948 -25.817  1.00 56.70           C  
ANISOU 4836  CB  PHE A 699     8884   6387   6272    635    302    641       C  
ATOM   4837  CG  PHE A 699       3.595  27.415 -25.922  1.00 65.44           C  
ANISOU 4837  CG  PHE A 699     9859   7602   7404    584    188    606       C  
ATOM   4838  CD1 PHE A 699       4.131  28.180 -26.944  1.00 37.86           C  
ANISOU 4838  CD1 PHE A 699     6291   4176   3917    566     99    572       C  
ATOM   4839  CD2 PHE A 699       2.778  28.032 -24.991  1.00 70.37           C  
ANISOU 4839  CD2 PHE A 699    10440   8257   8043    558    178    610       C  
ATOM   4840  CE1 PHE A 699       3.854  29.524 -27.039  1.00 34.72           C  
ANISOU 4840  CE1 PHE A 699     5773   3870   3548    523     10    532       C  
ATOM   4841  CE2 PHE A 699       2.496  29.378 -25.085  1.00 62.91           C  
ANISOU 4841  CE2 PHE A 699     9378   7405   7120    515     80    580       C  
ATOM   4842  CZ  PHE A 699       3.037  30.124 -26.114  1.00 43.02           C  
ANISOU 4842  CZ  PHE A 699     6780   4949   4616    497      0    534       C  
ATOM   4843  N   LYS A 700       4.234  25.317 -22.864  1.00 42.77           N  
ANISOU 4843  N   LYS A 700     7240   4609   4401    857    421    778       N  
ATOM   4844  CA  LYS A 700       4.072  25.562 -21.439  1.00 38.04           C  
ANISOU 4844  CA  LYS A 700     6643   4047   3765    934    441    810       C  
ATOM   4845  C   LYS A 700       5.414  25.482 -20.715  1.00 51.41           C  
ANISOU 4845  C   LYS A 700     8341   5815   5377   1111    427    834       C  
ATOM   4846  O   LYS A 700       5.708  26.294 -19.838  1.00 52.30           O  
ANISOU 4846  O   LYS A 700     8379   6033   5461   1177    367    824       O  
ATOM   4847  CB  LYS A 700       3.074  24.573 -20.842  1.00 32.94           C  
ANISOU 4847  CB  LYS A 700     6118   3266   3131    906    583    854       C  
ATOM   4848  CG  LYS A 700       1.670  24.729 -21.396  1.00 62.91           C  
ANISOU 4848  CG  LYS A 700     9871   7008   7024    728    599    789       C  
ATOM   4849  CD  LYS A 700       0.697  23.730 -20.786  1.00 74.45           C  
ANISOU 4849  CD  LYS A 700    11438   8333   8515    693    755    810       C  
ATOM   4850  CE  LYS A 700      -0.715  23.990 -21.282  1.00 64.18           C  
ANISOU 4850  CE  LYS A 700    10072   6998   7315    515    760    732       C  
ATOM   4851  NZ  LYS A 700      -1.706  23.018 -20.761  1.00 68.71           N1+
ANISOU 4851  NZ  LYS A 700    10739   7432   7936    462    922    738       N1+
ATOM   4852  N   ALA A 701       6.228  24.507 -21.098  1.00 48.29           N  
ANISOU 4852  N   ALA A 701     8033   5370   4945   1187    480    864       N  
ATOM   4853  CA  ALA A 701       7.557  24.358 -20.523  1.00 56.54           C  
ANISOU 4853  CA  ALA A 701     9084   6490   5910   1361    465    887       C  
ATOM   4854  C   ALA A 701       8.359  25.637 -20.741  1.00 55.15           C  
ANISOU 4854  C   ALA A 701     8746   6465   5745   1369    328    820       C  
ATOM   4855  O   ALA A 701       9.060  26.102 -19.843  1.00 52.06           O  
ANISOU 4855  O   ALA A 701     8304   6175   5301   1484    284    818       O  
ATOM   4856  CB  ALA A 701       8.274  23.163 -21.142  1.00 26.55           C  
ANISOU 4856  CB  ALA A 701     5396   2610   2082   1423    538    922       C  
ATOM   4857  N   PHE A 702       8.233  26.198 -21.941  1.00 63.20           N  
ANISOU 4857  N   PHE A 702     9689   7493   6833   1247    267    764       N  
ATOM   4858  CA  PHE A 702       8.924  27.426 -22.322  1.00 60.86           C  
ANISOU 4858  CA  PHE A 702     9243   7316   6563   1233    155    699       C  
ATOM   4859  C   PHE A 702       8.456  28.616 -21.503  1.00 59.92           C  
ANISOU 4859  C   PHE A 702     9022   7281   6464   1207     94    668       C  
ATOM   4860  O   PHE A 702       9.253  29.465 -21.102  1.00 62.74           O  
ANISOU 4860  O   PHE A 702     9280   7747   6810   1265     26    634       O  
ATOM   4861  CB  PHE A 702       8.686  27.727 -23.798  1.00 50.74           C  
ANISOU 4861  CB  PHE A 702     7923   6008   5349   1105    120    656       C  
ATOM   4862  CG  PHE A 702       9.265  29.031 -24.244  1.00 69.08           C  
ANISOU 4862  CG  PHE A 702    10103   8435   7710   1077     23    594       C  
ATOM   4863  CD1 PHE A 702      10.610  29.125 -24.563  1.00145.23           C  
ANISOU 4863  CD1 PHE A 702    19710  18137  17335   1157     -4    580       C  
ATOM   4864  CD2 PHE A 702       8.469  30.165 -24.344  1.00 37.27           C  
ANISOU 4864  CD2 PHE A 702     5981   4443   3739    974    -32    552       C  
ATOM   4865  CE1 PHE A 702      11.153  30.320 -24.970  1.00173.42           C  
ANISOU 4865  CE1 PHE A 702    23155  21791  20945   1128    -77    526       C  
ATOM   4866  CE2 PHE A 702       9.005  31.369 -24.753  1.00 36.02           C  
ANISOU 4866  CE2 PHE A 702     5701   4365   3619    950   -103    499       C  
ATOM   4867  CZ  PHE A 702      10.349  31.449 -25.069  1.00134.00           C  
ANISOU 4867  CZ  PHE A 702    18077  16824  16011   1024   -122    487       C  
ATOM   4868  N   LEU A 703       7.153  28.681 -21.273  1.00 54.75           N  
ANISOU 4868  N   LEU A 703     8389   6573   5842   1115    120    677       N  
ATOM   4869  CA  LEU A 703       6.571  29.784 -20.541  1.00 39.95           C  
ANISOU 4869  CA  LEU A 703     6424   4766   3991   1080     69    650       C  
ATOM   4870  C   LEU A 703       7.042  29.788 -19.088  1.00 57.24           C  
ANISOU 4870  C   LEU A 703     8625   7017   6108   1219     78    677       C  
ATOM   4871  O   LEU A 703       7.369  30.837 -18.538  1.00 62.30           O  
ANISOU 4871  O   LEU A 703     9162   7761   6750   1243      9    638       O  
ATOM   4872  CB  LEU A 703       5.051  29.730 -20.639  1.00 41.51           C  
ANISOU 4872  CB  LEU A 703     6651   4887   4234    956    104    660       C  
ATOM   4873  CG  LEU A 703       4.295  30.922 -20.052  1.00 72.75           C  
ANISOU 4873  CG  LEU A 703    10511   8906   8226    899     51    630       C  
ATOM   4874  CD1 LEU A 703       2.974  31.105 -20.769  1.00 70.50           C  
ANISOU 4874  CD1 LEU A 703    10217   8566   8005    750     51    616       C  
ATOM   4875  CD2 LEU A 703       4.086  30.737 -18.557  1.00103.53           C  
ANISOU 4875  CD2 LEU A 703    14455  12812  12069    988     95    673       C  
ATOM   4876  N   ILE A 704       7.089  28.610 -18.474  1.00 51.04           N  
ANISOU 4876  N   ILE A 704     7972   6166   5256   1316    169    745       N  
ATOM   4877  CA  ILE A 704       7.531  28.500 -17.087  1.00 53.12           C  
ANISOU 4877  CA  ILE A 704     8264   6485   5433   1470    184    779       C  
ATOM   4878  C   ILE A 704       9.038  28.742 -16.931  1.00 48.40           C  
ANISOU 4878  C   ILE A 704     7607   6002   4780   1603    120    754       C  
ATOM   4879  O   ILE A 704       9.491  29.201 -15.886  1.00 71.56           O  
ANISOU 4879  O   ILE A 704    10499   9034   7656   1710     82    745       O  
ATOM   4880  CB  ILE A 704       7.141  27.139 -16.481  1.00 50.89           C  
ANISOU 4880  CB  ILE A 704     8155   6091   5090   1547    315    867       C  
ATOM   4881  CG1 ILE A 704       5.637  26.909 -16.624  1.00 60.31           C  
ANISOU 4881  CG1 ILE A 704     9401   7168   6345   1407    385    887       C  
ATOM   4882  CG2 ILE A 704       7.525  27.073 -15.015  1.00 44.34           C  
ANISOU 4882  CG2 ILE A 704     7362   5325   4160   1718    330    907       C  
ATOM   4883  CD1 ILE A 704       4.804  27.787 -15.724  1.00 50.09           C  
ANISOU 4883  CD1 ILE A 704     8049   5920   5063   1373    359    876       C  
ATOM   4884  N   ARG A 705       9.812  28.444 -17.968  1.00 55.99           N  
ANISOU 4884  N   ARG A 705     8561   6954   5757   1597    107    738       N  
ATOM   4885  CA  ARG A 705      11.245  28.732 -17.949  1.00 68.40           C  
ANISOU 4885  CA  ARG A 705    10062   8637   7288   1707     44    707       C  
ATOM   4886  C   ARG A 705      11.505  30.230 -18.101  1.00 73.74           C  
ANISOU 4886  C   ARG A 705    10572   9423   8024   1638    -60    624       C  
ATOM   4887  O   ARG A 705      12.531  30.747 -17.656  1.00 72.58           O  
ANISOU 4887  O   ARG A 705    10345   9392   7841   1731   -121    587       O  
ATOM   4888  CB  ARG A 705      11.967  27.967 -19.057  1.00 62.70           C  
ANISOU 4888  CB  ARG A 705     9386   7866   6571   1716     68    718       C  
ATOM   4889  CG  ARG A 705      11.965  26.462 -18.887  1.00 96.49           C  
ANISOU 4889  CG  ARG A 705    13834  12043  10786   1809    177    800       C  
ATOM   4890  CD  ARG A 705      12.695  25.796 -20.041  1.00111.63           C  
ANISOU 4890  CD  ARG A 705    15787  13915  12713   1810    197    804       C  
ATOM   4891  NE  ARG A 705      12.662  24.341 -19.948  1.00142.70           N  
ANISOU 4891  NE  ARG A 705    19890  17737  16594   1890    312    883       N  
ATOM   4892  CZ  ARG A 705      13.153  23.524 -20.874  1.00163.13           C  
ANISOU 4892  CZ  ARG A 705    22543  20255  19183   1897    356    901       C  
ATOM   4893  NH1 ARG A 705      13.714  24.020 -21.968  1.00157.49           N1+
ANISOU 4893  NH1 ARG A 705    21741  19579  18520   1831    290    847       N1+
ATOM   4894  NH2 ARG A 705      13.081  22.211 -20.707  1.00165.09           N  
ANISOU 4894  NH2 ARG A 705    22951  20391  19383   1972    473    975       N  
ATOM   4895  N   LEU A 706      10.566  30.920 -18.736  1.00 45.09           N  
ANISOU 4895  N   LEU A 706     6892   5755   4484   1477    -77    593       N  
ATOM   4896  CA  LEU A 706      10.653  32.362 -18.918  1.00 47.77           C  
ANISOU 4896  CA  LEU A 706     7087   6176   4887   1400   -158    521       C  
ATOM   4897  C   LEU A 706      10.387  33.089 -17.602  1.00 68.19           C  
ANISOU 4897  C   LEU A 706     9623   8838   7446   1442   -188    506       C  
ATOM   4898  O   LEU A 706      11.125  33.998 -17.218  1.00 74.02           O  
ANISOU 4898  O   LEU A 706    10257   9685   8182   1481   -252    452       O  
ATOM   4899  CB  LEU A 706       9.626  32.802 -19.964  1.00 29.95           C  
ANISOU 4899  CB  LEU A 706     4807   3849   2722   1229   -159    502       C  
ATOM   4900  CG  LEU A 706       9.782  34.153 -20.649  1.00 44.50           C  
ANISOU 4900  CG  LEU A 706     6522   5745   4641   1137   -224    437       C  
ATOM   4901  CD1 LEU A 706      11.027  34.162 -21.510  1.00 53.37           C  
ANISOU 4901  CD1 LEU A 706     7611   6898   5768   1169   -245    415       C  
ATOM   4902  CD2 LEU A 706       8.554  34.443 -21.489  1.00 41.17           C  
ANISOU 4902  CD2 LEU A 706     6100   5252   4289    991   -218    431       C  
ATOM   4903  N   LEU A 707       9.330  32.673 -16.911  1.00 49.38           N  
ANISOU 4903  N   LEU A 707     7319   6399   5045   1436   -137    552       N  
ATOM   4904  CA  LEU A 707       8.872  33.343 -15.698  1.00 45.14           C  
ANISOU 4904  CA  LEU A 707     6745   5919   4485   1463   -156    542       C  
ATOM   4905  C   LEU A 707       9.500  32.761 -14.438  1.00 48.49           C  
ANISOU 4905  C   LEU A 707     7230   6401   4793   1648   -140    577       C  
ATOM   4906  O   LEU A 707       9.413  33.347 -13.365  1.00 39.80           O  
ANISOU 4906  O   LEU A 707     6092   5375   3656   1703   -169    561       O  
ATOM   4907  CB  LEU A 707       7.348  33.263 -15.610  1.00 42.57           C  
ANISOU 4907  CB  LEU A 707     6470   5504   4200   1357   -109    574       C  
ATOM   4908  CG  LEU A 707       6.633  33.894 -16.807  1.00 54.70           C  
ANISOU 4908  CG  LEU A 707     7944   6998   5842   1185   -133    538       C  
ATOM   4909  CD1 LEU A 707       5.136  33.640 -16.756  1.00 45.37           C  
ANISOU 4909  CD1 LEU A 707     6819   5729   4691   1089    -84    571       C  
ATOM   4910  CD2 LEU A 707       6.930  35.383 -16.882  1.00 40.75           C  
ANISOU 4910  CD2 LEU A 707     6034   5322   4127   1136   -213    466       C  
ATOM   4911  N   ARG A 708      10.133  31.604 -14.586  1.00 55.51           N  
ANISOU 4911  N   ARG A 708     8216   7256   5621   1750    -92    625       N  
ATOM   4912  CA  ARG A 708      10.803  30.912 -13.490  1.00 60.45           C  
ANISOU 4912  CA  ARG A 708     8913   7931   6122   1948    -69    667       C  
ATOM   4913  C   ARG A 708      11.332  31.873 -12.430  1.00 69.22           C  
ANISOU 4913  C   ARG A 708     9923   9193   7186   2037   -151    612       C  
ATOM   4914  O   ARG A 708      10.862  31.879 -11.296  1.00 54.04           O  
ANISOU 4914  O   ARG A 708     8041   7290   5202   2108   -132    638       O  
ATOM   4915  CB  ARG A 708      11.956  30.081 -14.052  1.00 68.17           C  
ANISOU 4915  CB  ARG A 708     9931   8914   7057   2045    -59    684       C  
ATOM   4916  CG  ARG A 708      12.417  28.931 -13.181  1.00 89.61           C  
ANISOU 4916  CG  ARG A 708    12777  11627   9644   2245      4    758       C  
ATOM   4917  CD  ARG A 708      13.576  28.213 -13.859  1.00127.63           C  
ANISOU 4917  CD  ARG A 708    17616  16450  14427   2330      6    767       C  
ATOM   4918  NE  ARG A 708      14.038  27.045 -13.117  1.00148.70           N  
ANISOU 4918  NE  ARG A 708    20421  19108  16969   2531     75    846       N  
ATOM   4919  CZ  ARG A 708      14.456  27.076 -11.857  1.00152.70           C  
ANISOU 4919  CZ  ARG A 708    20937  19719  17363   2709     53    856       C  
ATOM   4920  NH1 ARG A 708      14.453  28.217 -11.181  1.00178.68           N1+
ANISOU 4920  NH1 ARG A 708    24105  23132  20655   2703    -37    787       N1+
ATOM   4921  NH2 ARG A 708      14.866  25.962 -11.267  1.00110.58           N  
ANISOU 4921  NH2 ARG A 708    15740  14367  11910   2900    125    936       N  
ATOM   4922  N   ASP A 709      12.308  32.689 -12.810  1.00 77.26           N  
ANISOU 4922  N   ASP A 709    10810  10314   8231   2031   -238    532       N  
ATOM   4923  CA  ASP A 709      12.930  33.628 -11.885  1.00 61.20           C  
ANISOU 4923  CA  ASP A 709     8667   8431   6156   2111   -321    462       C  
ATOM   4924  C   ASP A 709      11.909  34.510 -11.186  1.00 57.16           C  
ANISOU 4924  C   ASP A 709     8118   7926   5675   2037   -332    443       C  
ATOM   4925  O   ASP A 709      11.934  34.649  -9.963  1.00 64.42           O  
ANISOU 4925  O   ASP A 709     9043   8923   6512   2151   -349    441       O  
ATOM   4926  CB  ASP A 709      13.961  34.495 -12.611  1.00 86.32           C  
ANISOU 4926  CB  ASP A 709    11703  11698   9395   2068   -402    371       C  
ATOM   4927  CG  ASP A 709      15.204  33.719 -12.999  1.00127.76           C  
ANISOU 4927  CG  ASP A 709    16969  16983  14589   2186   -409    378       C  
ATOM   4928  OD1 ASP A 709      15.400  32.603 -12.469  1.00126.84           O  
ANISOU 4928  OD1 ASP A 709    16969  16855  14371   2334   -363    445       O  
ATOM   4929  OD2 ASP A 709      15.988  34.228 -13.829  1.00137.37           O1-
ANISOU 4929  OD2 ASP A 709    18089  18241  15866   2136   -455    318       O1-
ATOM   4930  N   LEU A 710      11.013  35.105 -11.965  1.00 68.78           N  
ANISOU 4930  N   LEU A 710     9552   9320   7261   1853   -323    431       N  
ATOM   4931  CA  LEU A 710       9.995  36.000 -11.424  1.00 65.92           C  
ANISOU 4931  CA  LEU A 710     9148   8958   6940   1769   -333    412       C  
ATOM   4932  C   LEU A 710       9.093  35.289 -10.411  1.00 65.76           C  
ANISOU 4932  C   LEU A 710     9250   8886   6849   1835   -266    489       C  
ATOM   4933  O   LEU A 710       8.819  35.811  -9.329  1.00 46.48           O  
ANISOU 4933  O   LEU A 710     6788   6507   4366   1885   -285    476       O  
ATOM   4934  CB  LEU A 710       9.157  36.593 -12.562  1.00 49.23           C  
ANISOU 4934  CB  LEU A 710     6990   6761   4954   1570   -327    397       C  
ATOM   4935  CG  LEU A 710       8.020  37.544 -12.177  1.00 67.49           C  
ANISOU 4935  CG  LEU A 710     9258   9063   7321   1468   -335    380       C  
ATOM   4936  CD1 LEU A 710       8.565  38.789 -11.495  1.00 46.31           C  
ANISOU 4936  CD1 LEU A 710     6455   6503   4637   1495   -407    301       C  
ATOM   4937  CD2 LEU A 710       7.194  37.916 -13.401  1.00 88.01           C  
ANISOU 4937  CD2 LEU A 710    11832  11576  10033   1292   -323    376       C  
ATOM   4938  N   ILE A 711       8.640  34.094 -10.771  1.00 44.63           N  
ANISOU 4938  N   ILE A 711     6705   6094   4160   1836   -180    569       N  
ATOM   4939  CA  ILE A 711       7.767  33.310  -9.910  1.00 54.94           C  
ANISOU 4939  CA  ILE A 711     8143   7328   5404   1893    -94    652       C  
ATOM   4940  C   ILE A 711       8.413  33.054  -8.552  1.00 60.22           C  
ANISOU 4940  C   ILE A 711     8854   8091   5935   2102    -99    671       C  
ATOM   4941  O   ILE A 711       7.760  33.148  -7.512  1.00 49.64           O  
ANISOU 4941  O   ILE A 711     7558   6756   4547   2149    -71    701       O  
ATOM   4942  CB  ILE A 711       7.410  31.969 -10.577  1.00 48.51           C  
ANISOU 4942  CB  ILE A 711     7466   6371   4593   1874      8    730       C  
ATOM   4943  CG1 ILE A 711       6.656  32.216 -11.887  1.00 44.34           C  
ANISOU 4943  CG1 ILE A 711     6899   5757   4192   1672      9    707       C  
ATOM   4944  CG2 ILE A 711       6.590  31.103  -9.636  1.00 49.45           C  
ANISOU 4944  CG2 ILE A 711     7735   6408   4645   1945    116    820       C  
ATOM   4945  CD1 ILE A 711       6.473  30.974 -12.733  1.00 43.86           C  
ANISOU 4945  CD1 ILE A 711     6954   5568   4143   1642     94    762       C  
ATOM   4946  N   ASP A 712       9.704  32.740  -8.567  1.00 62.76           N  
ANISOU 4946  N   ASP A 712     9162   8494   6190   2234   -137    653       N  
ATOM   4947  CA  ASP A 712      10.435  32.458  -7.339  1.00 67.93           C  
ANISOU 4947  CA  ASP A 712     9854   9256   6701   2453   -152    665       C  
ATOM   4948  C   ASP A 712      10.455  33.675  -6.415  1.00 70.97           C  
ANISOU 4948  C   ASP A 712    10125   9771   7068   2473   -238    590       C  
ATOM   4949  O   ASP A 712      10.284  33.542  -5.203  1.00 55.51           O  
ANISOU 4949  O   ASP A 712     8226   7859   5006   2607   -223    619       O  
ATOM   4950  CB  ASP A 712      11.859  31.986  -7.655  1.00 75.74           C  
ANISOU 4950  CB  ASP A 712    10827  10321   7631   2581   -191    646       C  
ATOM   4951  CG  ASP A 712      11.883  30.683  -8.447  1.00 93.25           C  
ANISOU 4951  CG  ASP A 712    13174  12409   9848   2587    -97    728       C  
ATOM   4952  OD1 ASP A 712      10.881  29.938  -8.399  1.00 95.89           O  
ANISOU 4952  OD1 ASP A 712    13641  12605  10188   2550     11    812       O  
ATOM   4953  OD2 ASP A 712      12.904  30.403  -9.115  1.00 76.23           O1-
ANISOU 4953  OD2 ASP A 712    10989  10287   7688   2628   -127    707       O1-
ATOM   4954  N   LYS A 713      10.646  34.858  -6.993  1.00 63.29           N  
ANISOU 4954  N   LYS A 713     8997   8853   6196   2341   -320    494       N  
ATOM   4955  CA  LYS A 713      10.703  36.094  -6.211  1.00 56.23           C  
ANISOU 4955  CA  LYS A 713     7985   8079   5300   2343   -400    410       C  
ATOM   4956  C   LYS A 713       9.378  36.415  -5.522  1.00 50.77           C  
ANISOU 4956  C   LYS A 713     7336   7333   4621   2285   -359    446       C  
ATOM   4957  O   LYS A 713       9.337  37.220  -4.594  1.00 62.12           O  
ANISOU 4957  O   LYS A 713     8714   8865   6023   2327   -408    396       O  
ATOM   4958  CB  LYS A 713      11.131  37.275  -7.086  1.00 43.87           C  
ANISOU 4958  CB  LYS A 713     6257   6558   3852   2200   -476    306       C  
ATOM   4959  CG  LYS A 713      12.511  37.136  -7.698  1.00 87.82           C  
ANISOU 4959  CG  LYS A 713    11760  12197   9410   2257   -526    256       C  
ATOM   4960  CD  LYS A 713      12.749  38.205  -8.755  1.00105.89           C  
ANISOU 4960  CD  LYS A 713    13914  14487  11831   2091   -572    175       C  
ATOM   4961  CE  LYS A 713      14.009  37.926  -9.564  1.00118.14           C  
ANISOU 4961  CE  LYS A 713    15420  16080  13388   2127   -603    140       C  
ATOM   4962  NZ  LYS A 713      14.109  38.801 -10.769  1.00115.60           N1+
ANISOU 4962  NZ  LYS A 713    14999  15725  13199   1957   -621     87       N1+
ATOM   4963  N   GLN A 714       8.296  35.787  -5.972  1.00 69.61           N  
ANISOU 4963  N   GLN A 714     9823   9569   7056   2188   -267    527       N  
ATOM   4964  CA  GLN A 714       6.981  36.043  -5.390  1.00 65.31           C  
ANISOU 4964  CA  GLN A 714     9320   8965   6531   2124   -221    565       C  
ATOM   4965  C   GLN A 714       6.906  35.692  -3.910  1.00 79.61           C  
ANISOU 4965  C   GLN A 714    11220  10825   8203   2304   -192    610       C  
ATOM   4966  O   GLN A 714       7.149  34.551  -3.516  1.00 83.35           O  
ANISOU 4966  O   GLN A 714    11826  11267   8575   2449   -125    688       O  
ATOM   4967  CB  GLN A 714       5.881  35.289  -6.144  1.00 61.15           C  
ANISOU 4967  CB  GLN A 714     8890   8269   6074   1999   -123    642       C  
ATOM   4968  CG  GLN A 714       5.605  35.821  -7.530  1.00 64.24           C  
ANISOU 4968  CG  GLN A 714     9192   8609   6605   1803   -151    596       C  
ATOM   4969  CD  GLN A 714       5.597  37.331  -7.569  1.00 56.48           C  
ANISOU 4969  CD  GLN A 714     8056   7710   5694   1712   -239    505       C  
ATOM   4970  NE2 GLN A 714       6.621  37.907  -8.180  1.00 52.22           N  
ANISOU 4970  NE2 GLN A 714     7410   7243   5187   1699   -310    432       N  
ATOM   4971  OE1 GLN A 714       4.685  37.975  -7.055  1.00 72.43           O  
ANISOU 4971  OE1 GLN A 714    10054   9726   7739   1655   -237    502       O  
ATOM   4972  N   THR A 715       6.572  36.687  -3.095  1.00 99.02           N  
ANISOU 4972  N   THR A 715    13609  13360  10654   2300   -240    563       N  
ATOM   4973  CA  THR A 715       6.222  36.447  -1.707  1.00 73.89           C  
ANISOU 4973  CA  THR A 715    10517  10208   7349   2447   -204    612       C  
ATOM   4974  C   THR A 715       4.863  35.771  -1.702  1.00 76.76           C  
ANISOU 4974  C   THR A 715    11012  10412   7742   2374    -80    716       C  
ATOM   4975  O   THR A 715       4.060  35.985  -2.605  1.00 93.75           O  
ANISOU 4975  O   THR A 715    13133  12467  10020   2185    -58    715       O  
ATOM   4976  CB  THR A 715       6.114  37.760  -0.921  1.00 61.86           C  
ANISOU 4976  CB  THR A 715     8880   8799   5825   2439   -286    529       C  
ATOM   4977  CG2 THR A 715       7.424  38.521  -0.976  1.00 83.39           C  
ANISOU 4977  CG2 THR A 715    11462  11682   8540   2489   -406    410       C  
ATOM   4978  OG1 THR A 715       5.078  38.570  -1.487  1.00 88.79           O  
ANISOU 4978  OG1 THR A 715    12225  12137   9373   2230   -281    510       O  
ATOM   4979  N   TRP A 716       4.604  34.943  -0.700  1.00 72.99           N  
ANISOU 4979  N   TRP A 716    10682   9905   7144   2526      6    804       N  
ATOM   4980  CA  TRP A 716       3.311  34.281  -0.603  1.00 70.69           C  
ANISOU 4980  CA  TRP A 716    10523   9458   6878   2461    140    902       C  
ATOM   4981  C   TRP A 716       2.427  34.997   0.408  1.00 81.94           C  
ANISOU 4981  C   TRP A 716    11942  10906   8284   2455    146    904       C  
ATOM   4982  O   TRP A 716       1.849  34.380   1.303  1.00 85.90           O  
ANISOU 4982  O   TRP A 716    12584  11351   8703   2551    251    992       O  
ATOM   4983  CB  TRP A 716       3.488  32.806  -0.249  1.00 75.66           C  
ANISOU 4983  CB  TRP A 716    11341  10005   7400   2618    264   1013       C  
ATOM   4984  CG  TRP A 716       3.842  31.971  -1.437  1.00 74.54           C  
ANISOU 4984  CG  TRP A 716    11232   9774   7316   2559    300   1033       C  
ATOM   4985  CD1 TRP A 716       4.947  32.094  -2.229  1.00 78.65           C  
ANISOU 4985  CD1 TRP A 716    11660  10366   7857   2563    209    969       C  
ATOM   4986  CD2 TRP A 716       3.082  30.883  -1.973  1.00 87.59           C  
ANISOU 4986  CD2 TRP A 716    13018  11247   9016   2486    443   1120       C  
ATOM   4987  CE2 TRP A 716       3.787  30.393  -3.090  1.00 79.61           C  
ANISOU 4987  CE2 TRP A 716    11990  10210   8048   2451    425   1103       C  
ATOM   4988  CE3 TRP A 716       1.875  30.275  -1.616  1.00 98.50           C  
ANISOU 4988  CE3 TRP A 716    14531  12484  10410   2443    590   1206       C  
ATOM   4989  NE1 TRP A 716       4.920  31.151  -3.227  1.00 63.53           N  
ANISOU 4989  NE1 TRP A 716     9816   8329   5994   2500    282   1013       N  
ATOM   4990  CZ2 TRP A 716       3.324  29.323  -3.853  1.00 78.86           C  
ANISOU 4990  CZ2 TRP A 716    12005   9952   8005   2375    544   1166       C  
ATOM   4991  CZ3 TRP A 716       1.418  29.213  -2.374  1.00 91.63           C  
ANISOU 4991  CZ3 TRP A 716    13767  11450   9599   2362    714   1266       C  
ATOM   4992  CH2 TRP A 716       2.141  28.748  -3.480  1.00 73.20           C  
ANISOU 4992  CH2 TRP A 716    11413   9096   7304   2330    688   1244       C  
ATOM   4993  N   THR A 717       2.327  36.311   0.240  1.00 77.07           N  
ANISOU 4993  N   THR A 717    11168  10368   7747   2341     42    809       N  
ATOM   4994  CA  THR A 717       1.599  37.165   1.163  1.00 69.52           C  
ANISOU 4994  CA  THR A 717    10184   9454   6778   2332     29    794       C  
ATOM   4995  C   THR A 717       0.535  37.968   0.428  1.00 69.12           C  
ANISOU 4995  C   THR A 717    10046   9337   6881   2103     22    764       C  
ATOM   4996  O   THR A 717       0.342  37.805  -0.773  1.00 73.56           O  
ANISOU 4996  O   THR A 717    10577   9822   7551   1961     29    759       O  
ATOM   4997  CB  THR A 717       2.549  38.162   1.834  1.00 86.62           C  
ANISOU 4997  CB  THR A 717    12232  11800   8880   2432    -99    693       C  
ATOM   4998  CG2 THR A 717       3.774  37.445   2.385  1.00 85.09           C  
ANISOU 4998  CG2 THR A 717    12095  11698   8537   2660   -118    701       C  
ATOM   4999  OG1 THR A 717       2.968  39.134   0.869  1.00 75.28           O  
ANISOU 4999  OG1 THR A 717    10629  10411   7565   2289   -197    589       O  
ATOM   5000  N   ASP A 718      -0.147  38.846   1.155  1.00 71.07           N  
ANISOU 5000  N   ASP A 718    10252   9620   7130   2076      4    743       N  
ATOM   5001  CA  ASP A 718      -1.138  39.734   0.558  1.00 64.51           C  
ANISOU 5001  CA  ASP A 718     9330   8746   6434   1876    -12    711       C  
ATOM   5002  C   ASP A 718      -0.611  41.159   0.472  1.00 62.72           C  
ANISOU 5002  C   ASP A 718     8936   8640   6254   1830   -137    595       C  
ATOM   5003  O   ASP A 718      -1.378  42.097   0.281  1.00 58.17           O  
ANISOU 5003  O   ASP A 718     8283   8055   5766   1699   -158    563       O  
ATOM   5004  CB  ASP A 718      -2.438  39.713   1.362  1.00 78.75           C  
ANISOU 5004  CB  ASP A 718    11213  10486   8223   1858     76    776       C  
ATOM   5005  CG  ASP A 718      -3.395  38.633   0.900  1.00104.19           C  
ANISOU 5005  CG  ASP A 718    14553  13547  11487   1782    208    869       C  
ATOM   5006  OD1 ASP A 718      -3.140  38.020  -0.157  1.00 96.44           O  
ANISOU 5006  OD1 ASP A 718    13578  12504  10562   1720    220    875       O  
ATOM   5007  OD2 ASP A 718      -4.409  38.400   1.594  1.00 97.43           O1-
ANISOU 5007  OD2 ASP A 718    13784  12625  10610   1782    305    934       O1-
ATOM   5008  N   GLU A 719       0.701  41.318   0.614  1.00 76.68           N  
ANISOU 5008  N   GLU A 719    10650  10521   7965   1938   -215    532       N  
ATOM   5009  CA  GLU A 719       1.310  42.645   0.633  1.00 73.55           C  
ANISOU 5009  CA  GLU A 719    10099  10241   7605   1907   -324    415       C  
ATOM   5010  C   GLU A 719       1.483  43.210  -0.773  1.00 86.56           C  
ANISOU 5010  C   GLU A 719    11637  11857   9395   1739   -362    360       C  
ATOM   5011  O   GLU A 719       1.461  42.472  -1.755  1.00 97.32           O  
ANISOU 5011  O   GLU A 719    13038  13134  10805   1680   -325    401       O  
ATOM   5012  CB  GLU A 719       2.653  42.608   1.367  1.00 85.83           C  
ANISOU 5012  CB  GLU A 719    11633  11940   9040   2092   -392    359       C  
ATOM   5013  CG  GLU A 719       3.750  41.851   0.638  1.00124.36           C  
ANISOU 5013  CG  GLU A 719    16517  16829  13906   2145   -406    355       C  
ATOM   5014  CD  GLU A 719       4.908  41.479   1.547  1.00151.37           C  
ANISOU 5014  CD  GLU A 719    19957  20382  17174   2366   -453    328       C  
ATOM   5015  OE1 GLU A 719       6.058  41.431   1.059  1.00166.16           O  
ANISOU 5015  OE1 GLU A 719    21764  22323  19045   2404   -511    268       O  
ATOM   5016  OE2 GLU A 719       4.669  41.236   2.750  1.00138.54           O1-
ANISOU 5016  OE2 GLU A 719    18413  18798  15427   2509   -431    365       O1-
ATOM   5017  N   GLY A 720       1.645  44.527  -0.863  1.00 96.11           N  
ANISOU 5017  N   GLY A 720    12716  13133  10669   1664   -431    268       N  
ATOM   5018  CA  GLY A 720       1.851  45.185  -2.143  1.00 78.49           C  
ANISOU 5018  CA  GLY A 720    10383  10874   8565   1516   -462    215       C  
ATOM   5019  C   GLY A 720       0.623  45.907  -2.670  1.00 73.26           C  
ANISOU 5019  C   GLY A 720     9687  10134   8014   1350   -438    226       C  
ATOM   5020  O   GLY A 720      -0.458  45.840  -2.080  1.00 70.74           O  
ANISOU 5020  O   GLY A 720     9423   9775   7680   1339   -395    278       O  
ATOM   5021  N   SER A 721       0.796  46.600  -3.792  1.00 56.03           N  
ANISOU 5021  N   SER A 721     7418   7932   5939   1228   -462    180       N  
ATOM   5022  CA  SER A 721      -0.289  47.352  -4.413  1.00 56.79           C  
ANISOU 5022  CA  SER A 721     7475   7963   6140   1078   -446    185       C  
ATOM   5023  C   SER A 721      -1.188  46.441  -5.236  1.00 67.94           C  
ANISOU 5023  C   SER A 721     8960   9262   7592   1002   -389    263       C  
ATOM   5024  O   SER A 721      -0.859  45.279  -5.478  1.00 75.18           O  
ANISOU 5024  O   SER A 721     9953  10144   8469   1052   -361    307       O  
ATOM   5025  CB  SER A 721       0.264  48.459  -5.305  1.00 65.86           C  
ANISOU 5025  CB  SER A 721     8513   9131   7379    989   -486    110       C  
ATOM   5026  OG  SER A 721       0.784  47.920  -6.506  1.00 53.08           O  
ANISOU 5026  OG  SER A 721     6901   7468   5801    952   -479    119       O  
ATOM   5027  N   VAL A 722      -2.314  46.983  -5.683  1.00 45.03           N  
ANISOU 5027  N   VAL A 722     6034   6308   4768    883   -373    276       N  
ATOM   5028  CA  VAL A 722      -3.320  46.201  -6.395  1.00 55.88           C  
ANISOU 5028  CA  VAL A 722     7468   7585   6179    805   -325    340       C  
ATOM   5029  C   VAL A 722      -2.745  45.373  -7.550  1.00 65.03           C  
ANISOU 5029  C   VAL A 722     8650   8699   7360    786   -320    349       C  
ATOM   5030  O   VAL A 722      -3.057  44.192  -7.687  1.00 74.27           O  
ANISOU 5030  O   VAL A 722     9911   9806   8501    800   -272    408       O  
ATOM   5031  CB  VAL A 722      -4.449  47.109  -6.916  1.00 59.58           C  
ANISOU 5031  CB  VAL A 722     7877   8024   6736    678   -328    331       C  
ATOM   5032  CG1 VAL A 722      -5.578  46.272  -7.502  1.00 33.72           C  
ANISOU 5032  CG1 VAL A 722     4662   4662   3487    606   -282    392       C  
ATOM   5033  CG2 VAL A 722      -4.961  47.995  -5.795  1.00 77.27           C  
ANISOU 5033  CG2 VAL A 722    10091  10312   8958    698   -334    318       C  
ATOM   5034  N   SER A 723      -1.904  45.994  -8.369  1.00 61.57           N  
ANISOU 5034  N   SER A 723     8137   8289   6971    754   -361    293       N  
ATOM   5035  CA  SER A 723      -1.315  45.325  -9.524  1.00 39.23           C  
ANISOU 5035  CA  SER A 723     5322   5419   4163    733   -360    297       C  
ATOM   5036  C   SER A 723      -0.219  44.353  -9.111  1.00 54.07           C  
ANISOU 5036  C   SER A 723     7259   7327   5959    857   -356    309       C  
ATOM   5037  O   SER A 723      -0.043  43.304  -9.728  1.00 46.35           O  
ANISOU 5037  O   SER A 723     6344   6296   4969    865   -329    345       O  
ATOM   5038  CB  SER A 723      -0.763  46.349 -10.517  1.00 56.65           C  
ANISOU 5038  CB  SER A 723     7437   7644   6445    664   -396    239       C  
ATOM   5039  OG  SER A 723       0.110  47.262  -9.876  1.00 86.01           O  
ANISOU 5039  OG  SER A 723    11088  11445  10147    715   -431    179       O  
ATOM   5040  N   GLU A 724       0.521  44.708  -8.067  1.00 56.52           N  
ANISOU 5040  N   GLU A 724     7546   7723   6205    960   -384    276       N  
ATOM   5041  CA  GLU A 724       1.516  43.808  -7.497  1.00 67.08           C  
ANISOU 5041  CA  GLU A 724     8941   9103   7446   1102   -384    288       C  
ATOM   5042  C   GLU A 724       0.855  42.540  -6.963  1.00 58.65           C  
ANISOU 5042  C   GLU A 724     8004   7971   6310   1161   -316    376       C  
ATOM   5043  O   GLU A 724       1.404  41.443  -7.092  1.00 60.58           O  
ANISOU 5043  O   GLU A 724     8326   8193   6501   1238   -288    414       O  
ATOM   5044  CB  GLU A 724       2.316  44.511  -6.395  1.00 79.08           C  
ANISOU 5044  CB  GLU A 724    10404  10741   8902   1206   -434    228       C  
ATOM   5045  CG  GLU A 724       3.437  45.392  -6.926  1.00113.88           C  
ANISOU 5045  CG  GLU A 724    14700  15216  13352   1187   -493    139       C  
ATOM   5046  CD  GLU A 724       3.742  46.577  -6.028  1.00119.74           C  
ANISOU 5046  CD  GLU A 724    15356  16059  14081   1218   -543     61       C  
ATOM   5047  OE1 GLU A 724       4.487  47.477  -6.472  1.00129.46           O  
ANISOU 5047  OE1 GLU A 724    16490  17336  15363   1178   -582    -17       O  
ATOM   5048  OE2 GLU A 724       3.237  46.615  -4.886  1.00 97.36           O1-
ANISOU 5048  OE2 GLU A 724    12551  13256  11183   1280   -539     75       O1-
ATOM   5049  N   ARG A 725      -0.328  42.695  -6.374  1.00 54.20           N  
ANISOU 5049  N   ARG A 725     7471   7374   5750   1127   -282    411       N  
ATOM   5050  CA  ARG A 725      -1.064  41.559  -5.826  1.00 69.07           C  
ANISOU 5050  CA  ARG A 725     9484   9184   7573   1173   -200    499       C  
ATOM   5051  C   ARG A 725      -1.713  40.722  -6.928  1.00 69.00           C  
ANISOU 5051  C   ARG A 725     9531   9064   7624   1073   -148    544       C  
ATOM   5052  O   ARG A 725      -1.805  39.498  -6.813  1.00 63.25           O  
ANISOU 5052  O   ARG A 725     8919   8267   6845   1125    -74    610       O  
ATOM   5053  CB  ARG A 725      -2.123  42.018  -4.822  1.00 73.25           C  
ANISOU 5053  CB  ARG A 725    10029   9715   8087   1167   -174    522       C  
ATOM   5054  CG  ARG A 725      -1.600  42.939  -3.726  1.00 78.68           C  
ANISOU 5054  CG  ARG A 725    10659  10517   8718   1257   -230    470       C  
ATOM   5055  CD  ARG A 725      -2.282  42.672  -2.391  1.00 78.83           C  
ANISOU 5055  CD  ARG A 725    10765  10534   8651   1343   -176    525       C  
ATOM   5056  NE  ARG A 725      -3.728  42.490  -2.512  1.00 90.75           N  
ANISOU 5056  NE  ARG A 725    12322  11947  10212   1239   -105    583       N  
ATOM   5057  CZ  ARG A 725      -4.497  41.991  -1.548  1.00 80.43           C  
ANISOU 5057  CZ  ARG A 725    11118  10600   8843   1294    -25    653       C  
ATOM   5058  NH1 ARG A 725      -3.956  41.622  -0.398  1.00 77.87           N1+
ANISOU 5058  NH1 ARG A 725    10866  10325   8396   1460     -7    677       N1+
ATOM   5059  NH2 ARG A 725      -5.803  41.853  -1.733  1.00 75.08           N  
ANISOU 5059  NH2 ARG A 725    10473   9834   8221   1187     43    699       N  
ATOM   5060  N   MET A 726      -2.162  41.384  -7.992  1.00 53.14           N  
ANISOU 5060  N   MET A 726     7440   7034   5715    934   -181    507       N  
ATOM   5061  CA  MET A 726      -2.754  40.690  -9.136  1.00 44.10           C  
ANISOU 5061  CA  MET A 726     6332   5797   4626    835   -146    535       C  
ATOM   5062  C   MET A 726      -1.730  39.828  -9.863  1.00 62.42           C  
ANISOU 5062  C   MET A 726     8691   8099   6927    878   -144    538       C  
ATOM   5063  O   MET A 726      -2.055  38.749 -10.362  1.00 61.32           O  
ANISOU 5063  O   MET A 726     8639   7875   6786    857    -85    585       O  
ATOM   5064  CB  MET A 726      -3.383  41.685 -10.111  1.00 35.78           C  
ANISOU 5064  CB  MET A 726     5179   4744   3673    696   -193    490       C  
ATOM   5065  CG  MET A 726      -4.867  41.887  -9.903  1.00 41.80           C  
ANISOU 5065  CG  MET A 726     5949   5466   4466    614   -162    518       C  
ATOM   5066  SD  MET A 726      -5.496  43.400 -10.654  1.00 98.64           S  
ANISOU 5066  SD  MET A 726    13017  12701  11762    494   -228    460       S  
ATOM   5067  CE  MET A 726      -5.167  43.098 -12.385  1.00 35.15           C  
ANISOU 5067  CE  MET A 726     4955   4623   3775    421   -253    438       C  
ATOM   5068  N   LEU A 727      -0.494  40.312  -9.926  1.00 57.44           N  
ANISOU 5068  N   LEU A 727     7996   7547   6284    937   -202    486       N  
ATOM   5069  CA  LEU A 727       0.581  39.566 -10.565  1.00 41.77           C  
ANISOU 5069  CA  LEU A 727     6039   5555   4275    989   -204    486       C  
ATOM   5070  C   LEU A 727       0.975  38.367  -9.711  1.00 52.15           C  
ANISOU 5070  C   LEU A 727     7474   6855   5485   1131   -146    547       C  
ATOM   5071  O   LEU A 727       1.186  37.274 -10.231  1.00 49.09           O  
ANISOU 5071  O   LEU A 727     7170   6401   5080   1149    -99    587       O  
ATOM   5072  CB  LEU A 727       1.796  40.466 -10.810  1.00 59.53           C  
ANISOU 5072  CB  LEU A 727     8183   7897   6540   1013   -277    413       C  
ATOM   5073  CG  LEU A 727       2.952  39.848 -11.602  1.00 56.45           C  
ANISOU 5073  CG  LEU A 727     7804   7508   6137   1055   -286    404       C  
ATOM   5074  CD1 LEU A 727       2.600  39.746 -13.073  1.00 16.79           C  
ANISOU 5074  CD1 LEU A 727     2772   2413   1195    932   -281    402       C  
ATOM   5075  CD2 LEU A 727       4.219  40.653 -11.421  1.00 44.92           C  
ANISOU 5075  CD2 LEU A 727     6250   6153   4664   1115   -349    336       C  
ATOM   5076  N   ARG A 728       1.075  38.575  -8.402  1.00 61.16           N  
ANISOU 5076  N   ARG A 728     8630   8056   6552   1236   -146    555       N  
ATOM   5077  CA  ARG A 728       1.380  37.482  -7.491  1.00 55.19           C  
ANISOU 5077  CA  ARG A 728     7999   7287   5683   1389    -83    620       C  
ATOM   5078  C   ARG A 728       0.342  36.384  -7.646  1.00 56.43           C  
ANISOU 5078  C   ARG A 728     8284   7309   5847   1345     26    703       C  
ATOM   5079  O   ARG A 728       0.674  35.209  -7.804  1.00 52.34           O  
ANISOU 5079  O   ARG A 728     7873   6729   5284   1409     92    756       O  
ATOM   5080  CB  ARG A 728       1.403  37.963  -6.042  1.00 47.35           C  
ANISOU 5080  CB  ARG A 728     7005   6376   4609   1500    -97    618       C  
ATOM   5081  CG  ARG A 728       1.649  36.838  -5.041  1.00 43.66           C  
ANISOU 5081  CG  ARG A 728     6681   5894   4014   1674    -23    695       C  
ATOM   5082  CD  ARG A 728       1.663  37.331  -3.607  1.00 60.22           C  
ANISOU 5082  CD  ARG A 728     8780   8081   6020   1795    -40    691       C  
ATOM   5083  NE  ARG A 728       2.749  38.275  -3.357  1.00 71.00           N  
ANISOU 5083  NE  ARG A 728    10022   9592   7362   1855   -152    598       N  
ATOM   5084  CZ  ARG A 728       2.574  39.580  -3.194  1.00 73.90           C  
ANISOU 5084  CZ  ARG A 728    10268  10029   7782   1783   -222    524       C  
ATOM   5085  NH1 ARG A 728       1.353  40.095  -3.251  1.00 62.60           N1+
ANISOU 5085  NH1 ARG A 728     8822   8538   6424   1655   -197    536       N1+
ATOM   5086  NH2 ARG A 728       3.618  40.370  -2.970  1.00 78.95           N  
ANISOU 5086  NH2 ARG A 728    10801  10797   8400   1839   -314    435       N  
ATOM   5087  N   SER A 729      -0.924  36.784  -7.598  1.00 59.87           N  
ANISOU 5087  N   SER A 729     8708   7699   6340   1233     51    713       N  
ATOM   5088  CA  SER A 729      -2.037  35.858  -7.743  1.00 56.28           C  
ANISOU 5088  CA  SER A 729     8362   7116   5906   1169    160    782       C  
ATOM   5089  C   SER A 729      -1.945  35.037  -9.031  1.00 54.59           C  
ANISOU 5089  C   SER A 729     8181   6819   5741   1095    188    789       C  
ATOM   5090  O   SER A 729      -2.033  33.809  -9.002  1.00 74.03           O  
ANISOU 5090  O   SER A 729    10772   9186   8171   1133    290    852       O  
ATOM   5091  CB  SER A 729      -3.360  36.627  -7.700  1.00 46.55           C  
ANISOU 5091  CB  SER A 729     7076   5866   4744   1040    160    771       C  
ATOM   5092  OG  SER A 729      -4.431  35.834  -8.178  1.00 77.85           O  
ANISOU 5092  OG  SER A 729    11116   9708   8756    940    255    818       O  
ATOM   5093  N   GLU A 730      -1.759  35.720 -10.156  1.00 33.04           N  
ANISOU 5093  N   GLU A 730     5343   4123   3088    994    102    724       N  
ATOM   5094  CA  GLU A 730      -1.743  35.066 -11.460  1.00 67.74           C  
ANISOU 5094  CA  GLU A 730     9759   8448   7531    915    117    723       C  
ATOM   5095  C   GLU A 730      -0.489  34.238 -11.721  1.00 62.41           C  
ANISOU 5095  C   GLU A 730     9139   7772   6803   1019    127    735       C  
ATOM   5096  O   GLU A 730      -0.563  33.160 -12.310  1.00 56.81           O  
ANISOU 5096  O   GLU A 730     8520   6968   6095   1002    196    771       O  
ATOM   5097  CB  GLU A 730      -1.952  36.088 -12.579  1.00 68.13           C  
ANISOU 5097  CB  GLU A 730     9681   8535   7671    787     27    654       C  
ATOM   5098  CG  GLU A 730      -3.361  36.649 -12.607  1.00111.35           C  
ANISOU 5098  CG  GLU A 730    15119  13986  13203    668     32    652       C  
ATOM   5099  CD  GLU A 730      -4.410  35.554 -12.569  1.00141.85           C  
ANISOU 5099  CD  GLU A 730    19095  17731  17071    618    145    714       C  
ATOM   5100  OE1 GLU A 730      -4.291  34.592 -13.357  1.00155.06           O  
ANISOU 5100  OE1 GLU A 730    20833  19328  18752    592    190    730       O  
ATOM   5101  OE2 GLU A 730      -5.351  35.650 -11.751  1.00136.93           O1-
ANISOU 5101  OE2 GLU A 730    18496  17083  16447    600    198    744       O1-
ATOM   5102  N   LEU A 731       0.664  34.736 -11.292  1.00 52.88           N  
ANISOU 5102  N   LEU A 731     7875   6668   5547   1125     60    701       N  
ATOM   5103  CA  LEU A 731       1.898  33.976 -11.449  1.00 51.65           C  
ANISOU 5103  CA  LEU A 731     7768   6525   5332   1239     66    713       C  
ATOM   5104  C   LEU A 731       1.829  32.628 -10.742  1.00 62.53           C  
ANISOU 5104  C   LEU A 731     9309   7824   6627   1350    181    801       C  
ATOM   5105  O   LEU A 731       2.074  31.591 -11.352  1.00 65.49           O  
ANISOU 5105  O   LEU A 731     9770   8120   6995   1360    241    835       O  
ATOM   5106  CB  LEU A 731       3.097  34.770 -10.937  1.00 60.74           C  
ANISOU 5106  CB  LEU A 731     8828   7811   6440   1343    -21    660       C  
ATOM   5107  CG  LEU A 731       3.609  35.881 -11.848  1.00 55.72           C  
ANISOU 5107  CG  LEU A 731     8048   7241   5882   1256   -115    576       C  
ATOM   5108  CD1 LEU A 731       4.876  36.478 -11.264  1.00 44.82           C  
ANISOU 5108  CD1 LEU A 731     6593   5987   4450   1370   -183    526       C  
ATOM   5109  CD2 LEU A 731       3.861  35.339 -13.244  1.00 47.72           C  
ANISOU 5109  CD2 LEU A 731     7050   6166   4917   1187   -107    574       C  
ATOM   5110  N   LEU A 732       1.493  32.649  -9.457  1.00 51.05           N  
ANISOU 5110  N   LEU A 732     7904   6386   5108   1437    220    839       N  
ATOM   5111  CA  LEU A 732       1.446  31.427  -8.663  1.00 42.01           C  
ANISOU 5111  CA  LEU A 732     6923   5165   3874   1562    342    929       C  
ATOM   5112  C   LEU A 732       0.425  30.433  -9.216  1.00 59.81           C  
ANISOU 5112  C   LEU A 732     9287   7256   6183   1457    467    984       C  
ATOM   5113  O   LEU A 732       0.738  29.260  -9.420  1.00 64.05           O  
ANISOU 5113  O   LEU A 732     9943   7707   6687   1514    557   1037       O  
ATOM   5114  CB  LEU A 732       1.156  31.747  -7.198  1.00 23.90           C  
ANISOU 5114  CB  LEU A 732     4659   2919   1502   1667    361    958       C  
ATOM   5115  CG  LEU A 732       2.104  32.738  -6.518  1.00 39.96           C  
ANISOU 5115  CG  LEU A 732     6587   5119   3478   1774    243    897       C  
ATOM   5116  CD1 LEU A 732       1.645  33.037  -5.102  1.00 47.56           C  
ANISOU 5116  CD1 LEU A 732     7586   6119   4365   1866    268    927       C  
ATOM   5117  CD2 LEU A 732       3.525  32.222  -6.513  1.00 38.08           C  
ANISOU 5117  CD2 LEU A 732     6369   4944   3154   1930    215    896       C  
ATOM   5118  N   LEU A 733      -0.794  30.901  -9.464  1.00 54.90           N  
ANISOU 5118  N   LEU A 733     8623   6591   5646   1303    476    968       N  
ATOM   5119  CA  LEU A 733      -1.818  30.038 -10.041  1.00 59.68           C  
ANISOU 5119  CA  LEU A 733     9313   7045   6316   1183    592   1005       C  
ATOM   5120  C   LEU A 733      -1.291  29.349 -11.291  1.00 55.92           C  
ANISOU 5120  C   LEU A 733     8856   6518   5872   1142    593    992       C  
ATOM   5121  O   LEU A 733      -1.460  28.150 -11.473  1.00 55.34           O  
ANISOU 5121  O   LEU A 733     8910   6318   5797   1144    716   1044       O  
ATOM   5122  CB  LEU A 733      -3.068  30.838 -10.400  1.00 50.02           C  
ANISOU 5122  CB  LEU A 733     8002   5814   5191   1010    564    967       C  
ATOM   5123  CG  LEU A 733      -4.052  30.022 -11.243  1.00 48.47           C  
ANISOU 5123  CG  LEU A 733     7853   5477   5087    865    665    965       C  
ATOM   5124  CD1 LEU A 733      -4.606  28.867 -10.427  1.00 35.28           C  
ANISOU 5124  CD1 LEU A 733     6332   3674   3400    907    848   1030       C  
ATOM   5125  CD2 LEU A 733      -5.178  30.878 -11.793  1.00 22.92           C  
ANISOU 5125  CD2 LEU A 733     4495   2257   1957    696    615    894       C  
ATOM   5126  N   LEU A 734      -0.654  30.129 -12.151  1.00 61.04           N  
ANISOU 5126  N   LEU A 734     9380   7259   6553   1102    461    920       N  
ATOM   5127  CA  LEU A 734      -0.102  29.626 -13.398  1.00 51.83           C  
ANISOU 5127  CA  LEU A 734     8217   6059   5417   1062    447    900       C  
ATOM   5128  C   LEU A 734       0.927  28.535 -13.134  1.00 60.86           C  
ANISOU 5128  C   LEU A 734     9476   7172   6478   1214    512    951       C  
ATOM   5129  O   LEU A 734       0.832  27.432 -13.671  1.00 69.12           O  
ANISOU 5129  O   LEU A 734    10627   8102   7535   1193    607    987       O  
ATOM   5130  CB  LEU A 734       0.556  30.772 -14.161  1.00 47.33           C  
ANISOU 5130  CB  LEU A 734     7494   5608   4883   1023    299    818       C  
ATOM   5131  CG  LEU A 734       0.992  30.472 -15.592  1.00 59.26           C  
ANISOU 5131  CG  LEU A 734     8989   7092   6436    959    271    787       C  
ATOM   5132  CD1 LEU A 734      -0.222  30.444 -16.496  1.00 51.51           C  
ANISOU 5132  CD1 LEU A 734     8000   6034   5537    791    290    773       C  
ATOM   5133  CD2 LEU A 734       1.980  31.521 -16.050  1.00 61.30           C  
ANISOU 5133  CD2 LEU A 734     9113   7470   6706    974    147    719       C  
ATOM   5134  N   ALA A 735       1.910  28.860 -12.302  1.00 45.54           N  
ANISOU 5134  N   ALA A 735     7513   5337   4453   1368    461    952       N  
ATOM   5135  CA  ALA A 735       3.000  27.948 -11.988  1.00 44.52           C  
ANISOU 5135  CA  ALA A 735     7480   5206   4231   1536    506    998       C  
ATOM   5136  C   ALA A 735       2.501  26.600 -11.474  1.00 56.65           C  
ANISOU 5136  C   ALA A 735     9202   6597   5726   1592    676   1093       C  
ATOM   5137  O   ALA A 735       2.975  25.551 -11.905  1.00 66.46           O  
ANISOU 5137  O   ALA A 735    10544   7762   6947   1641    750   1131       O  
ATOM   5138  CB  ALA A 735       3.943  28.588 -10.981  1.00 33.35           C  
ANISOU 5138  CB  ALA A 735     6008   3938   2727   1695    426    982       C  
ATOM   5139  N   CYS A 736       1.546  26.631 -10.553  1.00 47.43           N  
ANISOU 5139  N   CYS A 736     8084   5386   4550   1586    750   1132       N  
ATOM   5140  CA  CYS A 736       1.003  25.408  -9.970  1.00 57.12           C  
ANISOU 5140  CA  CYS A 736     9493   6465   5745   1637    932   1225       C  
ATOM   5141  C   CYS A 736       0.105  24.649 -10.947  1.00 47.96           C  
ANISOU 5141  C   CYS A 736     8391   5141   4690   1468   1037   1230       C  
ATOM   5142  O   CYS A 736       0.067  23.420 -10.942  1.00 72.29           O  
ANISOU 5142  O   CYS A 736    11623   8086   7758   1505   1187   1292       O  
ATOM   5143  CB  CYS A 736       0.249  25.718  -8.672  1.00 38.18           C  
ANISOU 5143  CB  CYS A 736     7129   4070   3308   1681    986   1265       C  
ATOM   5144  SG  CYS A 736       1.312  26.266  -7.317  1.00 86.89           S  
ANISOU 5144  SG  CYS A 736    13280  10407   9326   1921    903   1277       S  
ATOM   5145  N   VAL A 737      -0.617  25.386 -11.782  1.00 34.99           N  
ANISOU 5145  N   VAL A 737     6630   3513   3153   1283    962   1161       N  
ATOM   5146  CA  VAL A 737      -1.454  24.785 -12.811  1.00 57.84           C  
ANISOU 5146  CA  VAL A 737     9536   6278   6161   1112   1039   1120       C  
ATOM   5147  C   VAL A 737      -0.601  24.026 -13.825  1.00 62.71           C  
ANISOU 5147  C   VAL A 737    10194   6856   6775   1129   1041   1115       C  
ATOM   5148  O   VAL A 737      -1.067  23.093 -14.478  1.00 69.51           O  
ANISOU 5148  O   VAL A 737    11121   7584   7704   1040   1150   1099       O  
ATOM   5149  CB  VAL A 737      -2.291  25.855 -13.537  1.00 51.59           C  
ANISOU 5149  CB  VAL A 737     8586   5544   5474    933    932   1029       C  
ATOM   5150  CG1 VAL A 737      -2.639  25.406 -14.942  1.00 47.84           C  
ANISOU 5150  CG1 VAL A 737     8086   4995   5095    785    942    963       C  
ATOM   5151  CG2 VAL A 737      -3.542  26.187 -12.738  1.00 34.86           C  
ANISOU 5151  CG2 VAL A 737     6454   3394   3396    866    992   1028       C  
ATOM   5152  N   HIS A 738       0.657  24.430 -13.946  1.00 45.04           N  
ANISOU 5152  N   HIS A 738     7912   4736   4464   1241    924   1119       N  
ATOM   5153  CA  HIS A 738       1.576  23.800 -14.880  1.00 49.90           C  
ANISOU 5153  CA  HIS A 738     8557   5332   5071   1271    916   1111       C  
ATOM   5154  C   HIS A 738       2.610  22.943 -14.160  1.00 45.80           C  
ANISOU 5154  C   HIS A 738     8158   4805   4440   1477    986   1182       C  
ATOM   5155  O   HIS A 738       3.711  22.711 -14.656  1.00 59.95           O  
ANISOU 5155  O   HIS A 738     9945   6640   6194   1556    940   1173       O  
ATOM   5156  CB  HIS A 738       2.248  24.854 -15.761  1.00 49.56           C  
ANISOU 5156  CB  HIS A 738     8352   5426   5051   1228    741   1029       C  
ATOM   5157  CG  HIS A 738       1.304  25.527 -16.703  1.00 71.90           C  
ANISOU 5157  CG  HIS A 738    11085   8250   7985   1035    683    967       C  
ATOM   5158  CD2 HIS A 738       0.976  25.247 -17.986  1.00 72.70           C  
ANISOU 5158  CD2 HIS A 738    11167   8292   8163    905    684    914       C  
ATOM   5159  ND1 HIS A 738       0.552  26.623 -16.347  1.00118.26           N  
ANISOU 5159  ND1 HIS A 738    16853  14190  13891    963    615    933       N  
ATOM   5160  CE1 HIS A 738      -0.192  26.998 -17.373  1.00110.15           C  
ANISOU 5160  CE1 HIS A 738    15749  13149  12956    803    576    866       C  
ATOM   5161  NE2 HIS A 738       0.047  26.178 -18.380  1.00 91.84           N  
ANISOU 5161  NE2 HIS A 738    13476  10756  10663    766    614    849       N  
ATOM   5162  N   ASN A 739       2.241  22.474 -12.979  1.00 63.25           N  
ANISOU 5162  N   ASN A 739    10479   6959   6593   1571   1101   1254       N  
ATOM   5163  CA  ASN A 739       3.054  21.515 -12.251  1.00 87.85           C  
ANISOU 5163  CA  ASN A 739    13737  10043   9597   1775   1196   1335       C  
ATOM   5164  C   ASN A 739       4.520  21.924 -12.112  1.00 63.34           C  
ANISOU 5164  C   ASN A 739    10565   7102   6399   1940   1068   1317       C  
ATOM   5165  O   ASN A 739       5.407  21.073 -12.076  1.00 82.73           O  
ANISOU 5165  O   ASN A 739    13117   9536   8781   2083   1120   1364       O  
ATOM   5166  CB  ASN A 739       2.945  20.134 -12.898  1.00 84.40           C  
ANISOU 5166  CB  ASN A 739    13450   9426   9192   1746   1353   1379       C  
ATOM   5167  CG  ASN A 739       3.345  19.023 -11.961  1.00 90.76           C  
ANISOU 5167  CG  ASN A 739    14442  10149   9893   1942   1509   1485       C  
ATOM   5168  ND2 ASN A 739       3.323  17.794 -12.457  1.00113.29           N  
ANISOU 5168  ND2 ASN A 739    17435  12838  12771   1931   1658   1526       N  
ATOM   5169  OD1 ASN A 739       3.670  19.264 -10.799  1.00 96.94           O  
ANISOU 5169  OD1 ASN A 739    15247  11013  10571   2106   1499   1528       O  
ATOM   5170  N   TYR A 740       4.771  23.226 -12.044  1.00 46.32           N  
ANISOU 5170  N   TYR A 740     8242   5106   4252   1917    905   1244       N  
ATOM   5171  CA  TYR A 740       6.072  23.715 -11.611  1.00 56.56           C  
ANISOU 5171  CA  TYR A 740     9466   6565   5457   2081    793   1222       C  
ATOM   5172  C   TYR A 740       6.249  23.272 -10.164  1.00 62.61           C  
ANISOU 5172  C   TYR A 740    10347   7345   6096   2285    868   1300       C  
ATOM   5173  O   TYR A 740       5.634  23.829  -9.257  1.00 46.85           O  
ANISOU 5173  O   TYR A 740     8334   5383   4082   2292    864   1305       O  
ATOM   5174  CB  TYR A 740       6.143  25.240 -11.722  1.00 61.91           C  
ANISOU 5174  CB  TYR A 740     9947   7392   6183   1999    626   1126       C  
ATOM   5175  CG  TYR A 740       7.454  25.841 -11.258  1.00 52.86           C  
ANISOU 5175  CG  TYR A 740     8710   6418   4957   2151    511   1087       C  
ATOM   5176  CD1 TYR A 740       8.646  25.528 -11.894  1.00 53.13           C  
ANISOU 5176  CD1 TYR A 740     8726   6494   4965   2222    471   1071       C  
ATOM   5177  CD2 TYR A 740       7.496  26.731 -10.196  1.00 69.98           C  
ANISOU 5177  CD2 TYR A 740    10806   8706   7076   2221    442   1062       C  
ATOM   5178  CE1 TYR A 740       9.843  26.076 -11.478  1.00 55.57           C  
ANISOU 5178  CE1 TYR A 740     8944   6963   5205   2356    367   1029       C  
ATOM   5179  CE2 TYR A 740       8.689  27.285  -9.774  1.00 70.37           C  
ANISOU 5179  CE2 TYR A 740    10766   8917   7056   2355    336   1016       C  
ATOM   5180  CZ  TYR A 740       9.859  26.954 -10.418  1.00 66.28           C  
ANISOU 5180  CZ  TYR A 740    10227   8439   6516   2421    299    998       C  
ATOM   5181  OH  TYR A 740      11.051  27.503 -10.006  1.00 64.39           O  
ANISOU 5181  OH  TYR A 740     9890   8365   6210   2550    194    945       O  
ATOM   5182  N   GLN A 741       7.082  22.260  -9.952  1.00 71.70           N  
ANISOU 5182  N   GLN A 741    11621   8470   7153   2458    940   1365       N  
ATOM   5183  CA  GLN A 741       7.147  21.582  -8.659  1.00 75.70           C  
ANISOU 5183  CA  GLN A 741    12277   8953   7531   2662   1049   1460       C  
ATOM   5184  C   GLN A 741       7.284  22.500  -7.439  1.00 65.27           C  
ANISOU 5184  C   GLN A 741    10887   7787   6126   2776    960   1442       C  
ATOM   5185  O   GLN A 741       6.509  22.375  -6.494  1.00 53.07           O  
ANISOU 5185  O   GLN A 741     9430   6191   4545   2814   1050   1499       O  
ATOM   5186  CB  GLN A 741       8.239  20.504  -8.656  1.00 67.80           C  
ANISOU 5186  CB  GLN A 741    11397   7936   6429   2857   1110   1523       C  
ATOM   5187  CG  GLN A 741       7.989  19.392  -7.647  1.00111.70           C  
ANISOU 5187  CG  GLN A 741    17173  13382  11884   3027   1294   1646       C  
ATOM   5188  CD  GLN A 741       6.667  18.681  -7.884  1.00130.12           C  
ANISOU 5188  CD  GLN A 741    19631  15496  14313   2873   1474   1696       C  
ATOM   5189  NE2 GLN A 741       6.118  18.080  -6.832  1.00110.29           N  
ANISOU 5189  NE2 GLN A 741    17281  12892  11734   2979   1631   1791       N  
ATOM   5190  OE1 GLN A 741       6.145  18.672  -9.000  1.00131.26           O  
ANISOU 5190  OE1 GLN A 741    19727  15555  14590   2662   1476   1647       O  
ATOM   5191  N   PRO A 742       8.267  23.417  -7.451  1.00 56.07           N  
ANISOU 5191  N   PRO A 742     9566   6807   4933   2830    791   1362       N  
ATOM   5192  CA  PRO A 742       8.478  24.265  -6.269  1.00 47.72           C  
ANISOU 5192  CA  PRO A 742     8442   5902   3789   2949    706   1336       C  
ATOM   5193  C   PRO A 742       7.183  24.884  -5.743  1.00 62.76           C  
ANISOU 5193  C   PRO A 742    10331   7767   5746   2830    731   1335       C  
ATOM   5194  O   PRO A 742       6.857  24.705  -4.569  1.00 55.56           O  
ANISOU 5194  O   PRO A 742     9514   6856   4741   2957    796   1395       O  
ATOM   5195  CB  PRO A 742       9.428  25.345  -6.783  1.00 49.76           C  
ANISOU 5195  CB  PRO A 742     8497   6330   4079   2915    523   1220       C  
ATOM   5196  CG  PRO A 742      10.196  24.671  -7.858  1.00 60.05           C  
ANISOU 5196  CG  PRO A 742     9816   7593   5406   2910    531   1221       C  
ATOM   5197  CD  PRO A 742       9.236  23.717  -8.520  1.00 56.95           C  
ANISOU 5197  CD  PRO A 742     9556   6993   5089   2786    679   1287       C  
ATOM   5198  N   CYS A 743       6.455  25.593  -6.600  1.00 68.37           N  
ANISOU 5198  N   CYS A 743    10930   8447   6601   2597    682   1269       N  
ATOM   5199  CA  CYS A 743       5.194  26.214  -6.201  1.00 83.05           C  
ANISOU 5199  CA  CYS A 743    12764  10270   8521   2472    701   1263       C  
ATOM   5200  C   CYS A 743       4.105  25.181  -5.882  1.00 70.49           C  
ANISOU 5200  C   CYS A 743    11354   8494   6936   2450    893   1364       C  
ATOM   5201  O   CYS A 743       3.294  25.388  -4.983  1.00 60.67           O  
ANISOU 5201  O   CYS A 743    10151   7230   5672   2459    947   1396       O  
ATOM   5202  CB  CYS A 743       4.710  27.212  -7.267  1.00 28.74           C  
ANISOU 5202  CB  CYS A 743     5722   3406   1790   2238    601   1170       C  
ATOM   5203  SG  CYS A 743       2.924  27.501  -7.256  1.00311.82           S  
ANISOU 5203  SG  CYS A 743    41584  39143  37750   2039    675   1182       S  
ATOM   5204  N   VAL A 744       4.095  24.069  -6.611  1.00 36.72           N  
ANISOU 5204  N   VAL A 744     7187   4078   2689   2421   1003   1410       N  
ATOM   5205  CA  VAL A 744       3.091  23.024  -6.400  1.00 53.23           C  
ANISOU 5205  CA  VAL A 744     9451   5974   4801   2387   1204   1499       C  
ATOM   5206  C   VAL A 744       3.245  22.385  -5.023  1.00 57.86           C  
ANISOU 5206  C   VAL A 744    10199   6542   5241   2614   1320   1600       C  
ATOM   5207  O   VAL A 744       2.260  22.179  -4.313  1.00 43.63           O  
ANISOU 5207  O   VAL A 744     8490   4646   3442   2598   1444   1655       O  
ATOM   5208  CB  VAL A 744       3.160  21.909  -7.474  1.00 56.31           C  
ANISOU 5208  CB  VAL A 744     9931   6216   5249   2320   1305   1523       C  
ATOM   5209  CG1 VAL A 744       2.138  20.830  -7.177  1.00 50.04           C  
ANISOU 5209  CG1 VAL A 744     9318   5213   4483   2285   1529   1609       C  
ATOM   5210  CG2 VAL A 744       2.933  22.475  -8.865  1.00 44.95           C  
ANISOU 5210  CG2 VAL A 744     8347   4786   3947   2100   1201   1428       C  
ATOM   5211  N   GLN A 745       4.489  22.069  -4.666  1.00 65.78           N  
ANISOU 5211  N   GLN A 745    11238   7638   6117   2830   1282   1623       N  
ATOM   5212  CA  GLN A 745       4.835  21.532  -3.350  1.00 64.07           C  
ANISOU 5212  CA  GLN A 745    11168   7440   5736   3085   1367   1716       C  
ATOM   5213  C   GLN A 745       4.371  22.463  -2.236  1.00 81.01           C  
ANISOU 5213  C   GLN A 745    13262   9686   7834   3124   1313   1702       C  
ATOM   5214  O   GLN A 745       3.545  22.098  -1.403  1.00 74.51           O  
ANISOU 5214  O   GLN A 745    12568   8766   6978   3161   1454   1780       O  
ATOM   5215  CB  GLN A 745       6.350  21.347  -3.243  1.00 91.49           C  
ANISOU 5215  CB  GLN A 745    14630  11049   9083   3301   1278   1712       C  
ATOM   5216  CG  GLN A 745       6.925  20.273  -4.148  1.00123.95           C  
ANISOU 5216  CG  GLN A 745    18826  15060  13208   3317   1351   1746       C  
ATOM   5217  CD  GLN A 745       6.872  18.898  -3.517  1.00141.98           C  
ANISOU 5217  CD  GLN A 745    21355  17198  15391   3494   1563   1882       C  
ATOM   5218  NE2 GLN A 745       7.331  17.891  -4.252  1.00146.94           N  
ANISOU 5218  NE2 GLN A 745    22076  17724  16030   3515   1646   1920       N  
ATOM   5219  OE1 GLN A 745       6.428  18.741  -2.380  1.00143.86           O  
ANISOU 5219  OE1 GLN A 745    21705  17413  15543   3614   1656   1954       O  
ATOM   5220  N   ARG A 746       4.933  23.665  -2.223  1.00 65.56           N  
ANISOU 5220  N   ARG A 746    11117   7919   5873   3117   1115   1601       N  
ATOM   5221  CA  ARG A 746       4.536  24.695  -1.279  1.00 64.60           C  
ANISOU 5221  CA  ARG A 746    10920   7905   5720   3133   1042   1568       C  
ATOM   5222  C   ARG A 746       3.014  24.762  -1.184  1.00 72.41           C  
ANISOU 5222  C   ARG A 746    11951   8754   6808   2960   1153   1597       C  
ATOM   5223  O   ARG A 746       2.443  24.672  -0.098  1.00 75.26           O  
ANISOU 5223  O   ARG A 746    12410   9088   7098   3048   1243   1661       O  
ATOM   5224  CB  ARG A 746       5.103  26.044  -1.726  1.00 55.74           C  
ANISOU 5224  CB  ARG A 746     9565   6960   4652   3047    827   1434       C  
ATOM   5225  CG  ARG A 746       5.141  27.115  -0.653  1.00 69.49           C  
ANISOU 5225  CG  ARG A 746    11219   8857   6325   3126    725   1387       C  
ATOM   5226  CD  ARG A 746       6.196  28.160  -0.978  1.00 75.34           C  
ANISOU 5226  CD  ARG A 746    11762   9788   7076   3125    529   1264       C  
ATOM   5227  NE  ARG A 746       6.138  29.303  -0.072  1.00105.36           N  
ANISOU 5227  NE  ARG A 746    15461  13731  10839   3160    428   1200       N  
ATOM   5228  CZ  ARG A 746       6.993  30.321  -0.097  1.00116.38           C  
ANISOU 5228  CZ  ARG A 746    16686  15300  12235   3172    266   1087       C  
ATOM   5229  NH1 ARG A 746       7.980  30.338  -0.983  1.00115.52           N1+
ANISOU 5229  NH1 ARG A 746    16489  15244  12161   3154    189   1028       N1+
ATOM   5230  NH2 ARG A 746       6.862  31.322   0.766  1.00 91.53           N  
ANISOU 5230  NH2 ARG A 746    13456  12269   9053   3200    187   1031       N  
ATOM   5231  N   ALA A 747       2.364  24.901  -2.333  1.00 61.54           N  
ANISOU 5231  N   ALA A 747    10501   7290   5591   2719   1150   1551       N  
ATOM   5232  CA  ALA A 747       0.908  24.961  -2.405  1.00 66.91           C  
ANISOU 5232  CA  ALA A 747    11203   7840   6380   2535   1249   1567       C  
ATOM   5233  C   ALA A 747       0.237  23.794  -1.688  1.00 78.06           C  
ANISOU 5233  C   ALA A 747    12833   9078   7746   2611   1480   1688       C  
ATOM   5234  O   ALA A 747      -0.702  23.992  -0.919  1.00 66.93           O  
ANISOU 5234  O   ALA A 747    11466   7624   6340   2589   1559   1721       O  
ATOM   5235  CB  ALA A 747       0.457  25.013  -3.860  1.00 53.73           C  
ANISOU 5235  CB  ALA A 747     9447   6095   4874   2294   1225   1506       C  
ATOM   5236  N   GLU A 748       0.711  22.580  -1.956  1.00 78.28           N  
ANISOU 5236  N   GLU A 748    13004   9002   7738   2699   1598   1754       N  
ATOM   5237  CA  GLU A 748       0.180  21.389  -1.300  1.00 85.52           C  
ANISOU 5237  CA  GLU A 748    14144   9739   8610   2785   1837   1874       C  
ATOM   5238  C   GLU A 748       0.235  21.560   0.205  1.00 84.37           C  
ANISOU 5238  C   GLU A 748    14082   9662   8313   2998   1870   1939       C  
ATOM   5239  O   GLU A 748      -0.750  21.321   0.905  1.00 84.26           O  
ANISOU 5239  O   GLU A 748    14173   9537   8306   2982   2024   2002       O  
ATOM   5240  CB  GLU A 748       0.975  20.144  -1.695  1.00 97.28           C  
ANISOU 5240  CB  GLU A 748    15772  11140  10049   2902   1936   1936       C  
ATOM   5241  CG  GLU A 748       0.601  19.548  -3.038  1.00120.89           C  
ANISOU 5241  CG  GLU A 748    18760  13983  13191   2695   2000   1907       C  
ATOM   5242  CD  GLU A 748       1.466  18.352  -3.393  1.00137.63           C  
ANISOU 5242  CD  GLU A 748    21016  16023  15253   2823   2092   1967       C  
ATOM   5243  OE1 GLU A 748       2.330  17.983  -2.570  1.00137.12           O  
ANISOU 5243  OE1 GLU A 748    21051  16019  15028   3079   2110   2036       O  
ATOM   5244  OE2 GLU A 748       1.281  17.786  -4.492  1.00138.96           O1-
ANISOU 5244  OE2 GLU A 748    21193  16072  15533   2673   2146   1943       O1-
ATOM   5245  N   GLY A 749       1.399  21.975   0.695  1.00 71.66           N  
ANISOU 5245  N   GLY A 749    12422   8239   6566   3197   1727   1919       N  
ATOM   5246  CA  GLY A 749       1.600  22.191   2.114  1.00 70.25           C  
ANISOU 5246  CA  GLY A 749    12311   8155   6224   3422   1731   1969       C  
ATOM   5247  C   GLY A 749       0.543  23.103   2.698  1.00 71.02           C  
ANISOU 5247  C   GLY A 749    12345   8271   6370   3313   1717   1943       C  
ATOM   5248  O   GLY A 749      -0.183  22.725   3.617  1.00 84.55           O  
ANISOU 5248  O   GLY A 749    14202   9892   8033   3381   1875   2030       O  
ATOM   5249  N   TYR A 750       0.452  24.311   2.157  1.00 67.55           N  
ANISOU 5249  N   TYR A 750    11692   7947   6027   3147   1534   1825       N  
ATOM   5250  CA  TYR A 750      -0.532  25.281   2.620  1.00 58.50           C  
ANISOU 5250  CA  TYR A 750    10465   6828   4935   3032   1504   1790       C  
ATOM   5251  C   TYR A 750      -1.939  24.685   2.643  1.00 66.95           C  
ANISOU 5251  C   TYR A 750    11650   7687   6100   2892   1713   1859       C  
ATOM   5252  O   TYR A 750      -2.664  24.842   3.621  1.00 75.48           O  
ANISOU 5252  O   TYR A 750    12796   8742   7140   2932   1798   1906       O  
ATOM   5253  CB  TYR A 750      -0.478  26.557   1.769  1.00 47.15           C  
ANISOU 5253  CB  TYR A 750     8788   5511   3616   2842   1299   1656       C  
ATOM   5254  CG  TYR A 750       0.674  27.481   2.115  1.00 90.47           C  
ANISOU 5254  CG  TYR A 750    14141  11222   9012   2971   1098   1576       C  
ATOM   5255  CD1 TYR A 750       0.442  28.731   2.672  1.00101.87           C  
ANISOU 5255  CD1 TYR A 750    15459  12793  10456   2944    981   1507       C  
ATOM   5256  CD2 TYR A 750       1.991  27.097   1.897  1.00118.44           C  
ANISOU 5256  CD2 TYR A 750    17683  14847  12472   3120   1032   1564       C  
ATOM   5257  CE1 TYR A 750       1.488  29.577   2.994  1.00103.45           C  
ANISOU 5257  CE1 TYR A 750    15532  13192  10581   3052    806   1423       C  
ATOM   5258  CE2 TYR A 750       3.044  27.937   2.218  1.00122.54           C  
ANISOU 5258  CE2 TYR A 750    18072  15572  12915   3231    855   1481       C  
ATOM   5259  CZ  TYR A 750       2.784  29.175   2.766  1.00112.59           C  
ANISOU 5259  CZ  TYR A 750    16686  14431  11662   3194    744   1408       C  
ATOM   5260  OH  TYR A 750       3.823  30.015   3.087  1.00100.57           O  
ANISOU 5260  OH  TYR A 750    15030  13109  10072   3296    576   1314       O  
ATOM   5261  N   PHE A 751      -2.319  23.986   1.579  1.00 74.17           N  
ANISOU 5261  N   PHE A 751    12590   8451   7141   2730   1801   1861       N  
ATOM   5262  CA  PHE A 751      -3.660  23.415   1.507  1.00 71.77           C  
ANISOU 5262  CA  PHE A 751    12377   7944   6946   2576   2002   1909       C  
ATOM   5263  C   PHE A 751      -3.902  22.373   2.590  1.00 78.17           C  
ANISOU 5263  C   PHE A 751    13425   8623   7654   2750   2235   2040       C  
ATOM   5264  O   PHE A 751      -5.022  22.225   3.078  1.00 79.08           O  
ANISOU 5264  O   PHE A 751    13608   8616   7822   2676   2391   2079       O  
ATOM   5265  CB  PHE A 751      -3.930  22.798   0.138  1.00 77.23           C  
ANISOU 5265  CB  PHE A 751    13052   8503   7787   2380   2053   1877       C  
ATOM   5266  CG  PHE A 751      -5.308  22.221   0.007  1.00 70.27           C  
ANISOU 5266  CG  PHE A 751    12232   7420   7047   2206   2256   1884       C  
ATOM   5267  CD1 PHE A 751      -6.387  23.035  -0.291  1.00 60.24           C  
ANISOU 5267  CD1 PHE A 751    10820   6156   5914   1994   2212   1801       C  
ATOM   5268  CD2 PHE A 751      -5.528  20.870   0.193  1.00 57.01           C  
ANISOU 5268  CD2 PHE A 751    10749   5545   5367   2257   2497   1967       C  
ATOM   5269  CE1 PHE A 751      -7.659  22.510  -0.409  1.00 63.89           C  
ANISOU 5269  CE1 PHE A 751    11322   6440   6513   1832   2397   1793       C  
ATOM   5270  CE2 PHE A 751      -6.799  20.338   0.078  1.00 72.87           C  
ANISOU 5270  CE2 PHE A 751    12804   7365   7518   2089   2692   1959       C  
ATOM   5271  CZ  PHE A 751      -7.865  21.160  -0.223  1.00 69.28           C  
ANISOU 5271  CZ  PHE A 751    12195   6927   7202   1875   2638   1868       C  
ATOM   5272  N   ARG A 752      -2.847  21.647   2.951  1.00 90.78           N  
ANISOU 5272  N   ARG A 752    15144  10241   9107   2984   2264   2106       N  
ATOM   5273  CA  ARG A 752      -2.914  20.642   4.009  1.00104.15           C  
ANISOU 5273  CA  ARG A 752    17076  11819  10676   3190   2483   2241       C  
ATOM   5274  C   ARG A 752      -3.119  21.296   5.373  1.00104.91           C  
ANISOU 5274  C   ARG A 752    17195  12018  10648   3338   2466   2272       C  
ATOM   5275  O   ARG A 752      -3.952  20.856   6.166  1.00 83.32           O  
ANISOU 5275  O   ARG A 752    14610   9153   7896   3371   2665   2359       O  
ATOM   5276  CB  ARG A 752      -1.636  19.799   4.021  1.00116.13           C  
ANISOU 5276  CB  ARG A 752    18704  13362  12057   3421   2492   2297       C  
ATOM   5277  CG  ARG A 752      -1.501  18.850   5.206  1.00120.41           C  
ANISOU 5277  CG  ARG A 752    19496  13821  12433   3689   2694   2441       C  
ATOM   5278  CD  ARG A 752      -1.824  17.425   4.802  1.00140.64           C  
ANISOU 5278  CD  ARG A 752    22251  16131  15053   3661   2953   2530       C  
ATOM   5279  NE  ARG A 752      -1.374  17.150   3.442  1.00164.98           N  
ANISOU 5279  NE  ARG A 752    25249  19190  18245   3522   2882   2463       N  
ATOM   5280  CZ  ARG A 752      -1.446  15.962   2.853  1.00166.21           C  
ANISOU 5280  CZ  ARG A 752    25541  19148  18462   3484   3067   2515       C  
ATOM   5281  NH1 ARG A 752      -1.945  14.923   3.510  1.00183.59           N1+
ANISOU 5281  NH1 ARG A 752    27974  21150  20631   3574   3344   2636       N1+
ATOM   5282  NH2 ARG A 752      -1.015  15.813   1.607  1.00120.52           N  
ANISOU 5282  NH2 ARG A 752    19664  13359  12771   3357   2982   2446       N  
ATOM   5283  N   LYS A 753      -2.350  22.346   5.642  1.00119.38           N  
ANISOU 5283  N   LYS A 753    18881  14082  12398   3425   2232   2197       N  
ATOM   5284  CA  LYS A 753      -2.480  23.090   6.889  1.00111.27           C  
ANISOU 5284  CA  LYS A 753    17851  13175  11252   3560   2186   2207       C  
ATOM   5285  C   LYS A 753      -3.874  23.694   7.018  1.00102.89           C  
ANISOU 5285  C   LYS A 753    16737  12041  10316   3353   2241   2187       C  
ATOM   5286  O   LYS A 753      -4.351  23.952   8.121  1.00101.06           O  
ANISOU 5286  O   LYS A 753    16573  11823  10004   3447   2303   2233       O  
ATOM   5287  CB  LYS A 753      -1.427  24.197   6.962  1.00106.60           C  
ANISOU 5287  CB  LYS A 753    17076  12843  10584   3643   1913   2102       C  
ATOM   5288  CG  LYS A 753       0.002  23.694   7.022  1.00113.96           C  
ANISOU 5288  CG  LYS A 753    18051  13879  11371   3879   1847   2117       C  
ATOM   5289  CD  LYS A 753       0.988  24.847   7.065  1.00135.95           C  
ANISOU 5289  CD  LYS A 753    20634  16917  14102   3935   1582   1995       C  
ATOM   5290  CE  LYS A 753       2.417  24.342   7.166  1.00139.71           C  
ANISOU 5290  CE  LYS A 753    21147  17506  14429   4178   1517   2005       C  
ATOM   5291  NZ  LYS A 753       3.409  25.450   7.155  1.00126.38           N1+
ANISOU 5291  NZ  LYS A 753    19251  16064  12704   4219   1266   1873       N1+
ATOM   5292  N   TRP A 754      -4.525  23.909   5.882  1.00 84.28           N  
ANISOU 5292  N   TRP A 754    14260   9611   8153   3076   2220   2117       N  
ATOM   5293  CA  TRP A 754      -5.825  24.566   5.848  1.00 78.34           C  
ANISOU 5293  CA  TRP A 754    13425   8807   7533   2861   2248   2080       C  
ATOM   5294  C   TRP A 754      -6.982  23.572   5.825  1.00 85.87           C  
ANISOU 5294  C   TRP A 754    14518   9514   8596   2751   2520   2142       C  
ATOM   5295  O   TRP A 754      -8.107  23.918   6.173  1.00 96.22           O  
ANISOU 5295  O   TRP A 754    15805  10763   9989   2634   2598   2130       O  
ATOM   5296  CB  TRP A 754      -5.908  25.500   4.639  1.00 61.33           C  
ANISOU 5296  CB  TRP A 754    11039   6733   5529   2627   2055   1950       C  
ATOM   5297  CG  TRP A 754      -7.238  26.155   4.453  1.00 43.68           C  
ANISOU 5297  CG  TRP A 754     8700   4447   3448   2399   2076   1894       C  
ATOM   5298  CD1 TRP A 754      -7.694  27.273   5.079  1.00 51.44           C  
ANISOU 5298  CD1 TRP A 754     9588   5536   4421   2378   1988   1856       C  
ATOM   5299  CD2 TRP A 754      -8.284  25.736   3.567  1.00 61.03           C  
ANISOU 5299  CD2 TRP A 754    10870   6482   5838   2161   2189   1856       C  
ATOM   5300  CE2 TRP A 754      -9.345  26.646   3.714  1.00 64.59           C  
ANISOU 5300  CE2 TRP A 754    11205   6953   6384   2012   2161   1799       C  
ATOM   5301  CE3 TRP A 754      -8.423  24.677   2.665  1.00 73.17           C  
ANISOU 5301  CE3 TRP A 754    12466   7861   7474   2063   2311   1860       C  
ATOM   5302  NE1 TRP A 754      -8.961  27.574   4.644  1.00 65.20           N  
ANISOU 5302  NE1 TRP A 754    11247   7191   6335   2148   2041   1804       N  
ATOM   5303  CZ2 TRP A 754     -10.531  26.532   2.994  1.00 70.49           C  
ANISOU 5303  CZ2 TRP A 754    11887   7576   7319   1773   2245   1743       C  
ATOM   5304  CZ3 TRP A 754      -9.603  24.566   1.950  1.00 78.28           C  
ANISOU 5304  CZ3 TRP A 754    13049   8385   8311   1820   2394   1798       C  
ATOM   5305  CH2 TRP A 754     -10.640  25.487   2.118  1.00 66.95           C  
ANISOU 5305  CH2 TRP A 754    11492   6982   6965   1680   2358   1739       C  
ATOM   5306  N   LYS A 755      -6.709  22.343   5.404  1.00 92.47           N  
ANISOU 5306  N   LYS A 755    15489  10204   9441   2784   2666   2199       N  
ATOM   5307  CA  LYS A 755      -7.719  21.294   5.445  1.00107.80           C  
ANISOU 5307  CA  LYS A 755    17576  11899  11483   2698   2947   2254       C  
ATOM   5308  C   LYS A 755      -7.842  20.807   6.880  1.00115.42           C  
ANISOU 5308  C   LYS A 755    18751  12805  12297   2925   3131   2383       C  
ATOM   5309  O   LYS A 755      -8.941  20.691   7.423  1.00101.43           O  
ANISOU 5309  O   LYS A 755    17040  10910  10590   2857   3305   2410       O  
ATOM   5310  CB  LYS A 755      -7.328  20.130   4.536  1.00109.14           C  
ANISOU 5310  CB  LYS A 755    17830  11931  11708   2668   3049   2271       C  
ATOM   5311  CG  LYS A 755      -8.334  18.991   4.525  1.00 94.61           C  
ANISOU 5311  CG  LYS A 755    16139   9825   9984   2570   3352   2317       C  
ATOM   5312  CD  LYS A 755      -7.718  17.713   3.983  1.00105.19           C  
ANISOU 5312  CD  LYS A 755    17622  11031  11315   2632   3480   2369       C  
ATOM   5313  CE  LYS A 755      -8.689  16.549   4.081  1.00117.44           C  
ANISOU 5313  CE  LYS A 755    19338  12306  12976   2550   3804   2417       C  
ATOM   5314  NZ  LYS A 755      -8.058  15.256   3.689  1.00115.98           N1+
ANISOU 5314  NZ  LYS A 755    19319  11980  12767   2638   3953   2481       N1+
ATOM   5315  N   GLU A 756      -6.692  20.536   7.487  1.00114.22           N  
ANISOU 5315  N   GLU A 756    18708  12749  11942   3203   3090   2460       N  
ATOM   5316  CA  GLU A 756      -6.620  20.091   8.868  1.00100.46           C  
ANISOU 5316  CA  GLU A 756    17173  10978  10019   3465   3242   2588       C  
ATOM   5317  C   GLU A 756      -6.820  21.265   9.819  1.00104.87           C  
ANISOU 5317  C   GLU A 756    17650  11705  10490   3528   3114   2564       C  
ATOM   5318  O   GLU A 756      -6.469  21.186  10.994  1.00122.62           O  
ANISOU 5318  O   GLU A 756    20031  14012  12547   3785   3156   2650       O  
ATOM   5319  CB  GLU A 756      -5.254  19.454   9.134  1.00101.08           C  
ANISOU 5319  CB  GLU A 756    17376  11128   9902   3752   3215   2662       C  
ATOM   5320  CG  GLU A 756      -4.839  18.402   8.114  1.00117.40           C  
ANISOU 5320  CG  GLU A 756    19504  13063  12040   3702   3297   2677       C  
ATOM   5321  CD  GLU A 756      -3.394  17.959   8.287  1.00125.01           C  
ANISOU 5321  CD  GLU A 756    20540  14138  12820   3981   3221   2719       C  
ATOM   5322  OE1 GLU A 756      -2.657  18.621   9.046  1.00115.07           O  
ANISOU 5322  OE1 GLU A 756    19237  13088  11395   4184   3058   2707       O  
ATOM   5323  OE2 GLU A 756      -2.997  16.952   7.658  1.00116.67           O1-
ANISOU 5323  OE2 GLU A 756    19581  12962  11787   3996   3324   2758       O1-
ATOM   5324  N   SER A 757      -7.388  22.352   9.309  1.00101.22           N  
ANISOU 5324  N   SER A 757    16971  11321  10166   3301   2961   2446       N  
ATOM   5325  CA  SER A 757      -7.450  23.601  10.065  1.00 92.10           C  
ANISOU 5325  CA  SER A 757    15708  10350   8937   3347   2801   2403       C  
ATOM   5326  C   SER A 757      -8.613  23.704  11.057  1.00107.50           C  
ANISOU 5326  C   SER A 757    17741  12207  10895   3338   2972   2453       C  
ATOM   5327  O   SER A 757      -8.381  23.976  12.235  1.00163.91           O  
ANISOU 5327  O   SER A 757    24968  19444  17866   3552   2967   2509       O  
ATOM   5328  CB  SER A 757      -7.420  24.814   9.129  1.00114.41           C  
ANISOU 5328  CB  SER A 757    18266  13319  11887   3135   2547   2256       C  
ATOM   5329  OG  SER A 757      -7.352  26.017   9.871  1.00114.94           O  
ANISOU 5329  OG  SER A 757    18230  13568  11873   3196   2388   2210       O  
ATOM   5330  N   ASN A 758      -9.853  23.500  10.612  1.00 68.20           N  
ANISOU 5330  N   ASN A 758    12742   7057   6116   3099   3121   2429       N  
ATOM   5331  CA  ASN A 758     -10.196  23.207   9.227  1.00 98.20           C  
ANISOU 5331  CA  ASN A 758    16436  10754  10120   2844   3122   2351       C  
ATOM   5332  C   ASN A 758     -10.811  24.439   8.585  1.00116.35           C  
ANISOU 5332  C   ASN A 758    18489  13151  12568   2603   2941   2218       C  
ATOM   5333  O   ASN A 758     -11.845  24.934   9.030  1.00106.48           O  
ANISOU 5333  O   ASN A 758    17200  11871  11386   2507   2999   2202       O  
ATOM   5334  CB  ASN A 758     -11.177  22.039   9.156  1.00119.89           C  
ANISOU 5334  CB  ASN A 758    19331  13232  12989   2745   3430   2407       C  
ATOM   5335  CG  ASN A 758     -12.494  22.342   9.849  1.00115.74           C  
ANISOU 5335  CG  ASN A 758    18813  12622  12541   2650   3572   2412       C  
ATOM   5336  ND2 ASN A 758     -12.570  22.029  11.137  1.00116.53           N  
ANISOU 5336  ND2 ASN A 758    19099  12681  12496   2859   3729   2527       N  
ATOM   5337  OD1 ASN A 758     -13.433  22.849   9.234  1.00 95.63           O  
ANISOU 5337  OD1 ASN A 758    16108  10049  10178   2399   3544   2314       O  
ATOM   5338  N   GLY A 759     -10.170  24.935   7.537  1.00133.25           N  
ANISOU 5338  N   GLY A 759    20466  15407  14757   2512   2728   2127       N  
ATOM   5339  CA  GLY A 759     -10.560  26.205   6.973  1.00129.45           C  
ANISOU 5339  CA  GLY A 759    19754  15045  14384   2324   2533   2007       C  
ATOM   5340  C   GLY A 759     -10.598  27.251   8.074  1.00124.18           C  
ANISOU 5340  C   GLY A 759    19051  14526  13607   2433   2440   2009       C  
ATOM   5341  O   GLY A 759     -11.192  28.319   7.886  1.00110.93           O  
ANISOU 5341  O   GLY A 759    17209  12921  12018   2285   2327   1926       O  
ATOM   5342  N   ASN A 760      -9.987  26.957   9.226  1.00132.81           N  
ANISOU 5342  N   ASN A 760    20297  15661  14502   2696   2488   2102       N  
ATOM   5343  CA  ASN A 760      -9.944  27.939  10.304  1.00137.51           C  
ANISOU 5343  CA  ASN A 760    20863  16408  14978   2817   2392   2098       C  
ATOM   5344  C   ASN A 760      -8.829  28.979  10.147  1.00112.37           C  
ANISOU 5344  C   ASN A 760    17524  13462  11708   2885   2109   2015       C  
ATOM   5345  O   ASN A 760      -9.111  30.174  10.127  1.00108.06           O  
ANISOU 5345  O   ASN A 760    16817  13030  11211   2785   1964   1930       O  
ATOM   5346  CB  ASN A 760      -9.941  27.306  11.721  1.00154.49           C  
ANISOU 5346  CB  ASN A 760    23239  18510  16951   3068   2569   2225       C  
ATOM   5347  CG  ASN A 760      -9.823  28.381  12.839  1.00160.78           C  
ANISOU 5347  CG  ASN A 760    23996  19484  17609   3204   2449   2209       C  
ATOM   5348  ND2 ASN A 760     -10.390  28.145  14.033  1.00151.81           N  
ANISOU 5348  ND2 ASN A 760    23013  18287  16381   3333   2616   2297       N  
ATOM   5349  OD1 ASN A 760      -9.224  29.415  12.588  1.00172.31           O  
ANISOU 5349  OD1 ASN A 760    25286  21131  19052   3186   2211   2114       O  
ATOM   5350  N   LEU A 761      -7.578  28.543  10.025  1.00 85.73           N  
ANISOU 5350  N   LEU A 761    14190  10162   8222   3050   2036   2028       N  
ATOM   5351  CA  LEU A 761      -6.473  29.493   9.878  1.00 94.92           C  
ANISOU 5351  CA  LEU A 761    15191  11548   9327   3115   1777   1924       C  
ATOM   5352  C   LEU A 761      -6.560  30.269   8.564  1.00114.32           C  
ANISOU 5352  C   LEU A 761    17432  14043  11960   2865   1621   1806       C  
ATOM   5353  O   LEU A 761      -6.796  29.690   7.505  1.00 95.57           O  
ANISOU 5353  O   LEU A 761    15052  11550   9709   2714   1676   1806       O  
ATOM   5354  CB  LEU A 761      -5.113  28.798  10.015  1.00 90.62           C  
ANISOU 5354  CB  LEU A 761    14727  11071   8633   3350   1742   1954       C  
ATOM   5355  CG  LEU A 761      -4.741  27.676   9.047  1.00103.60           C  
ANISOU 5355  CG  LEU A 761    16439  12591  10332   3316   1823   1990       C  
ATOM   5356  CD1 LEU A 761      -4.225  28.227   7.721  1.00 72.16           C  
ANISOU 5356  CD1 LEU A 761    12258   8684   6476   3146   1638   1873       C  
ATOM   5357  CD2 LEU A 761      -3.698  26.773   9.685  1.00110.52           C  
ANISOU 5357  CD2 LEU A 761    17478  13496  11019   3609   1875   2071       C  
ATOM   5358  N   SER A 762      -6.371  31.582   8.641  1.00137.06           N  
ANISOU 5358  N   SER A 762    20140  17088  14848   2826   1431   1706       N  
ATOM   5359  CA  SER A 762      -6.500  32.442   7.469  1.00120.48           C  
ANISOU 5359  CA  SER A 762    17838  15030  12908   2599   1286   1597       C  
ATOM   5360  C   SER A 762      -5.481  32.116   6.387  1.00119.78           C  
ANISOU 5360  C   SER A 762    17689  14969  12852   2584   1193   1551       C  
ATOM   5361  O   SER A 762      -4.364  31.685   6.670  1.00124.72           O  
ANISOU 5361  O   SER A 762    18368  15666  13356   2774   1157   1565       O  
ATOM   5362  CB  SER A 762      -6.400  33.920   7.854  1.00112.30           C  
ANISOU 5362  CB  SER A 762    16642  14164  11863   2584   1110   1500       C  
ATOM   5363  OG  SER A 762      -7.640  34.410   8.335  1.00114.59           O  
ANISOU 5363  OG  SER A 762    16931  14404  12202   2487   1182   1517       O  
ATOM   5364  N   LEU A 763      -5.886  32.337   5.143  1.00 98.99           N  
ANISOU 5364  N   LEU A 763    14946  12285  10382   2361   1154   1496       N  
ATOM   5365  CA  LEU A 763      -5.048  32.064   3.989  1.00 95.13           C  
ANISOU 5365  CA  LEU A 763    14394  11809   9943   2317   1073   1451       C  
ATOM   5366  C   LEU A 763      -5.062  33.287   3.078  1.00103.84           C  
ANISOU 5366  C   LEU A 763    15285  13002  11166   2139    901   1334       C  
ATOM   5367  O   LEU A 763      -6.130  33.758   2.685  1.00 94.81           O  
ANISOU 5367  O   LEU A 763    14079  11805  10139   1958    917   1314       O  
ATOM   5368  CB  LEU A 763      -5.577  30.830   3.255  1.00 92.02           C  
ANISOU 5368  CB  LEU A 763    14113  11224   9628   2224   1238   1516       C  
ATOM   5369  CG  LEU A 763      -4.873  30.323   1.999  1.00115.59           C  
ANISOU 5369  CG  LEU A 763    17063  14185  12670   2166   1193   1485       C  
ATOM   5370  CD1 LEU A 763      -3.442  29.917   2.289  1.00129.03           C  
ANISOU 5370  CD1 LEU A 763    18812  15978  14237   2384   1138   1497       C  
ATOM   5371  CD2 LEU A 763      -5.651  29.159   1.404  1.00101.24           C  
ANISOU 5371  CD2 LEU A 763    15362  12164  10940   2055   1378   1547       C  
ATOM   5372  N   PRO A 764      -3.872  33.817   2.751  1.00 83.94           N  
ANISOU 5372  N   PRO A 764    12655  10620   8619   2196    741   1256       N  
ATOM   5373  CA  PRO A 764      -3.733  35.019   1.920  1.00 68.97           C  
ANISOU 5373  CA  PRO A 764    10562   8814   6829   2048    582   1144       C  
ATOM   5374  C   PRO A 764      -4.480  34.898   0.598  1.00 69.84           C  
ANISOU 5374  C   PRO A 764    10626   8816   7095   1828    607   1130       C  
ATOM   5375  O   PRO A 764      -4.248  33.952  -0.152  1.00 76.56           O  
ANISOU 5375  O   PRO A 764    11538   9582   7970   1809    663   1160       O  
ATOM   5376  CB  PRO A 764      -2.225  35.097   1.671  1.00 50.93           C  
ANISOU 5376  CB  PRO A 764     8217   6649   4487   2160    464   1087       C  
ATOM   5377  CG  PRO A 764      -1.621  34.412   2.849  1.00 50.45           C  
ANISOU 5377  CG  PRO A 764     8289   6625   4256   2402    518   1150       C  
ATOM   5378  CD  PRO A 764      -2.566  33.303   3.201  1.00 48.77           C  
ANISOU 5378  CD  PRO A 764     8259   6246   4025   2414    711   1270       C  
ATOM   5379  N   VAL A 765      -5.359  35.856   0.317  1.00 50.73           N  
ANISOU 5379  N   VAL A 765     8098   6403   4772   1671    563   1084       N  
ATOM   5380  CA  VAL A 765      -6.213  35.803  -0.869  1.00 68.79           C  
ANISOU 5380  CA  VAL A 765    10339   8598   7199   1467    586   1071       C  
ATOM   5381  C   VAL A 765      -5.436  35.720  -2.185  1.00 67.56           C  
ANISOU 5381  C   VAL A 765    10111   8458   7102   1407    502   1017       C  
ATOM   5382  O   VAL A 765      -5.927  35.160  -3.167  1.00 91.42           O  
ANISOU 5382  O   VAL A 765    13149  11381  10207   1284    552   1027       O  
ATOM   5383  CB  VAL A 765      -7.192  36.997  -0.921  1.00 64.72           C  
ANISOU 5383  CB  VAL A 765     9707   8115   6767   1329    533   1024       C  
ATOM   5384  CG1 VAL A 765      -8.345  36.784   0.047  1.00 74.33           C  
ANISOU 5384  CG1 VAL A 765    11016   9260   7967   1329    664   1091       C  
ATOM   5385  CG2 VAL A 765      -6.462  38.296  -0.620  1.00 75.47           C  
ANISOU 5385  CG2 VAL A 765    10938   9631   8104   1376    380    942       C  
ATOM   5386  N   ASP A 766      -4.230  36.278  -2.202  1.00 37.35           N  
ANISOU 5386  N   ASP A 766     6202   4755   3234   1491    379    956       N  
ATOM   5387  CA  ASP A 766      -3.385  36.231  -3.391  1.00 74.39           C  
ANISOU 5387  CA  ASP A 766    10826   9466   7974   1447    304    905       C  
ATOM   5388  C   ASP A 766      -3.012  34.798  -3.760  1.00 69.95           C  
ANISOU 5388  C   ASP A 766    10392   8807   7377   1502    398    968       C  
ATOM   5389  O   ASP A 766      -2.898  34.456  -4.939  1.00 76.45           O  
ANISOU 5389  O   ASP A 766    11195   9582   8271   1409    390    951       O  
ATOM   5390  CB  ASP A 766      -2.115  37.060  -3.182  1.00 91.80           C  
ANISOU 5390  CB  ASP A 766    12925  11819  10134   1539    175    830       C  
ATOM   5391  CG  ASP A 766      -2.397  38.549  -3.068  1.00 94.92           C  
ANISOU 5391  CG  ASP A 766    13179  12302  10587   1460     80    753       C  
ATOM   5392  OD1 ASP A 766      -3.582  38.928  -2.946  1.00 63.66           O  
ANISOU 5392  OD1 ASP A 766     9212   8297   6678   1361    113    769       O  
ATOM   5393  OD2 ASP A 766      -1.431  39.340  -3.103  1.00103.80           O1-
ANISOU 5393  OD2 ASP A 766    14198  13536  11705   1496    -22    677       O1-
ATOM   5394  N   VAL A 767      -2.835  33.961  -2.744  1.00 57.66           N  
ANISOU 5394  N   VAL A 767     8975   7222   5710   1659    493   1044       N  
ATOM   5395  CA  VAL A 767      -2.361  32.597  -2.950  1.00 58.32           C  
ANISOU 5395  CA  VAL A 767     9194   7218   5746   1743    591   1109       C  
ATOM   5396  C   VAL A 767      -3.485  31.561  -2.934  1.00 59.44           C  
ANISOU 5396  C   VAL A 767     9477   7185   5922   1678    769   1193       C  
ATOM   5397  O   VAL A 767      -3.324  30.467  -3.462  1.00 69.74           O  
ANISOU 5397  O   VAL A 767    10878   8386   7233   1681    859   1236       O  
ATOM   5398  CB  VAL A 767      -1.302  32.211  -1.896  1.00 59.75           C  
ANISOU 5398  CB  VAL A 767     9454   7476   5772   1982    593   1144       C  
ATOM   5399  CG1 VAL A 767      -0.271  33.316  -1.754  1.00 48.64           C  
ANISOU 5399  CG1 VAL A 767     7898   6248   4334   2042    424   1051       C  
ATOM   5400  CG2 VAL A 767      -1.958  31.932  -0.560  1.00 59.06           C  
ANISOU 5400  CG2 VAL A 767     9488   7352   5598   2086    704   1222       C  
ATOM   5401  N   THR A 768      -4.619  31.904  -2.332  1.00 59.50           N  
ANISOU 5401  N   THR A 768     9495   7156   5957   1616    829   1214       N  
ATOM   5402  CA  THR A 768      -5.704  30.941  -2.161  1.00 77.52           C  
ANISOU 5402  CA  THR A 768    11912   9269   8274   1558   1018   1292       C  
ATOM   5403  C   THR A 768      -6.180  30.368  -3.488  1.00 74.94           C  
ANISOU 5403  C   THR A 768    11571   8828   8076   1383   1064   1267       C  
ATOM   5404  O   THR A 768      -6.647  29.234  -3.548  1.00 95.49           O  
ANISOU 5404  O   THR A 768    14292  11280  10710   1362   1228   1311       O  
ATOM   5405  CB  THR A 768      -6.924  31.547  -1.432  1.00 76.00           C  
ANISOU 5405  CB  THR A 768    11700   9060   8116   1489   1066   1298       C  
ATOM   5406  CG2 THR A 768      -6.533  32.094  -0.075  1.00 68.50           C  
ANISOU 5406  CG2 THR A 768    10772   8219   7038   1662   1030   1320       C  
ATOM   5407  OG1 THR A 768      -7.479  32.606  -2.220  1.00108.11           O  
ANISOU 5407  OG1 THR A 768    15599  13178  12300   1313    953   1210       O  
ATOM   5408  N   LEU A 769      -6.071  31.159  -4.547  1.00 67.59           N  
ANISOU 5408  N   LEU A 769    10491   7966   7223   1260    923   1185       N  
ATOM   5409  CA  LEU A 769      -6.544  30.728  -5.856  1.00 48.41           C  
ANISOU 5409  CA  LEU A 769     8027   5448   4919   1093    947   1140       C  
ATOM   5410  C   LEU A 769      -5.713  29.552  -6.335  1.00 56.27           C  
ANISOU 5410  C   LEU A 769     9129   6374   5878   1163   1006   1177       C  
ATOM   5411  O   LEU A 769      -6.246  28.572  -6.856  1.00 71.10           O  
ANISOU 5411  O   LEU A 769    11075   8113   7827   1081   1131   1182       O  
ATOM   5412  CB  LEU A 769      -6.474  31.876  -6.863  1.00 76.35           C  
ANISOU 5412  CB  LEU A 769    11392   9089   8528    976    777   1051       C  
ATOM   5413  CG  LEU A 769      -7.426  31.746  -8.055  1.00 72.50           C  
ANISOU 5413  CG  LEU A 769    10841   8525   8181    780    797    990       C  
ATOM   5414  CD1 LEU A 769      -8.865  31.627  -7.567  1.00 35.99           C  
ANISOU 5414  CD1 LEU A 769     6230   3815   3630    687    914    988       C  
ATOM   5415  CD2 LEU A 769      -7.272  32.928  -8.998  1.00 93.70           C  
ANISOU 5415  CD2 LEU A 769    13367  11318  10915    693    629    913       C  
ATOM   5416  N   ALA A 770      -4.400  29.656  -6.141  1.00 62.17           N  
ANISOU 5416  N   ALA A 770     9880   7221   6519   1315    919   1191       N  
ATOM   5417  CA  ALA A 770      -3.469  28.596  -6.509  1.00 55.04           C  
ANISOU 5417  CA  ALA A 770     9073   6271   5570   1409    965   1224       C  
ATOM   5418  C   ALA A 770      -3.604  27.392  -5.582  1.00 49.61           C  
ANISOU 5418  C   ALA A 770     8580   5464   4806   1534   1151   1327       C  
ATOM   5419  O   ALA A 770      -3.724  26.257  -6.035  1.00 45.29           O  
ANISOU 5419  O   ALA A 770     8141   4779   4290   1509   1280   1362       O  
ATOM   5420  CB  ALA A 770      -2.044  29.120  -6.482  1.00 36.81           C  
ANISOU 5420  CB  ALA A 770     6688   4116   3183   1541    819   1182       C  
ATOM   5421  N   VAL A 771      -3.583  27.656  -4.281  1.00 78.87           N  
ANISOU 5421  N   VAL A 771    12329   9223   8417   1671   1171   1368       N  
ATOM   5422  CA  VAL A 771      -3.667  26.606  -3.272  1.00 78.49           C  
ANISOU 5422  CA  VAL A 771    12472   9073   8278   1818   1349   1473       C  
ATOM   5423  C   VAL A 771      -4.917  25.737  -3.425  1.00 76.86           C  
ANISOU 5423  C   VAL A 771    12363   8667   8174   1686   1550   1506       C  
ATOM   5424  O   VAL A 771      -4.824  24.514  -3.455  1.00 72.76           O  
ANISOU 5424  O   VAL A 771    11992   8012   7643   1737   1707   1566       O  
ATOM   5425  CB  VAL A 771      -3.608  27.198  -1.856  1.00 47.49           C  
ANISOU 5425  CB  VAL A 771     8560   5244   4238   1971   1328   1500       C  
ATOM   5426  CG1 VAL A 771      -3.827  26.118  -0.823  1.00 48.39           C  
ANISOU 5426  CG1 VAL A 771     8884   5241   4261   2119   1530   1617       C  
ATOM   5427  CG2 VAL A 771      -2.272  27.887  -1.637  1.00 56.76           C  
ANISOU 5427  CG2 VAL A 771     9642   6610   5315   2119   1150   1450       C  
ATOM   5428  N   PHE A 772      -6.081  26.370  -3.520  1.00 70.61           N  
ANISOU 5428  N   PHE A 772    11478   7857   7493   1518   1550   1452       N  
ATOM   5429  CA  PHE A 772      -7.316  25.631  -3.740  1.00 62.62           C  
ANISOU 5429  CA  PHE A 772    10521   6667   6604   1371   1731   1448       C  
ATOM   5430  C   PHE A 772      -7.219  24.818  -5.020  1.00 56.67           C  
ANISOU 5430  C   PHE A 772     9774   5817   5943   1260   1766   1409       C  
ATOM   5431  O   PHE A 772      -7.599  23.652  -5.059  1.00 71.27           O  
ANISOU 5431  O   PHE A 772    11751   7498   7832   1240   1955   1443       O  
ATOM   5432  CB  PHE A 772      -8.521  26.571  -3.813  1.00 80.61           C  
ANISOU 5432  CB  PHE A 772    12664   8969   8996   1197   1690   1377       C  
ATOM   5433  CG  PHE A 772      -8.916  27.165  -2.489  1.00 78.33           C  
ANISOU 5433  CG  PHE A 772    12395   8728   8638   1284   1712   1419       C  
ATOM   5434  CD1 PHE A 772      -8.172  26.916  -1.347  1.00 57.07           C  
ANISOU 5434  CD1 PHE A 772     9828   6070   5785   1509   1748   1511       C  
ATOM   5435  CD2 PHE A 772     -10.034  27.981  -2.389  1.00 75.05           C  
ANISOU 5435  CD2 PHE A 772    11872   8328   8315   1147   1693   1366       C  
ATOM   5436  CE1 PHE A 772      -8.533  27.468  -0.132  1.00 60.42           C  
ANISOU 5436  CE1 PHE A 772    10273   6543   6139   1594   1766   1546       C  
ATOM   5437  CE2 PHE A 772     -10.400  28.533  -1.177  1.00 69.60           C  
ANISOU 5437  CE2 PHE A 772    11202   7682   7562   1226   1715   1404       C  
ATOM   5438  CZ  PHE A 772      -9.648  28.276  -0.047  1.00 75.59           C  
ANISOU 5438  CZ  PHE A 772    12090   8474   8159   1449   1752   1494       C  
ATOM   5439  N   ALA A 773      -6.709  25.444  -6.074  1.00 74.77           N  
ANISOU 5439  N   ALA A 773    11930   8212   8269   1189   1590   1335       N  
ATOM   5440  CA  ALA A 773      -6.552  24.767  -7.358  1.00 79.14           C  
ANISOU 5440  CA  ALA A 773    12478   8691   8901   1087   1603   1290       C  
ATOM   5441  C   ALA A 773      -5.782  23.457  -7.179  1.00 76.66           C  
ANISOU 5441  C   ALA A 773    12342   8275   8510   1228   1735   1372       C  
ATOM   5442  O   ALA A 773      -6.225  22.396  -7.621  1.00 66.46           O  
ANISOU 5442  O   ALA A 773    11136   6822   7292   1152   1890   1371       O  
ATOM   5443  CB  ALA A 773      -5.855  25.681  -8.365  1.00 41.48           C  
ANISOU 5443  CB  ALA A 773     7554   4065   4141   1041   1388   1218       C  
ATOM   5444  N   VAL A 774      -4.633  23.542  -6.518  1.00 74.86           N  
ANISOU 5444  N   VAL A 774    12167   8143   8134   1435   1676   1438       N  
ATOM   5445  CA  VAL A 774      -3.814  22.375  -6.232  1.00 66.24           C  
ANISOU 5445  CA  VAL A 774    11247   6975   6948   1603   1792   1525       C  
ATOM   5446  C   VAL A 774      -4.568  21.383  -5.360  1.00 66.52           C  
ANISOU 5446  C   VAL A 774    11458   6837   6979   1645   2035   1604       C  
ATOM   5447  O   VAL A 774      -4.551  20.178  -5.609  1.00 68.89           O  
ANISOU 5447  O   VAL A 774    11894   6982   7299   1655   2200   1643       O  
ATOM   5448  CB  VAL A 774      -2.522  22.776  -5.504  1.00 57.87           C  
ANISOU 5448  CB  VAL A 774    10197   6073   5719   1834   1674   1575       C  
ATOM   5449  CG1 VAL A 774      -1.803  21.544  -4.967  1.00 43.13           C  
ANISOU 5449  CG1 VAL A 774     8527   4124   3736   2037   1816   1680       C  
ATOM   5450  CG2 VAL A 774      -1.622  23.578  -6.427  1.00 77.23           C  
ANISOU 5450  CG2 VAL A 774    12487   8677   8181   1803   1460   1491       C  
ATOM   5451  N   GLY A 775      -5.227  21.901  -4.330  1.00 66.72           N  
ANISOU 5451  N   GLY A 775    11485   6885   6980   1670   2066   1629       N  
ATOM   5452  CA  GLY A 775      -5.939  21.071  -3.378  1.00 57.11           C  
ANISOU 5452  CA  GLY A 775    10437   5512   5751   1723   2300   1711       C  
ATOM   5453  C   GLY A 775      -7.043  20.248  -4.003  1.00 55.52           C  
ANISOU 5453  C   GLY A 775    10271   5111   5715   1526   2482   1672       C  
ATOM   5454  O   GLY A 775      -7.256  19.100  -3.630  1.00 65.52           O  
ANISOU 5454  O   GLY A 775    11712   6204   6978   1577   2706   1742       O  
ATOM   5455  N   ALA A 776      -7.744  20.834  -4.964  1.00 51.34           N  
ANISOU 5455  N   ALA A 776     9574   4604   5329   1303   2389   1557       N  
ATOM   5456  CA  ALA A 776      -8.870  20.168  -5.607  1.00 71.86           C  
ANISOU 5456  CA  ALA A 776    12174   7034   8096   1097   2540   1494       C  
ATOM   5457  C   ALA A 776      -8.442  18.979  -6.465  1.00 88.47           C  
ANISOU 5457  C   ALA A 776    14369   9010  10236   1077   2639   1491       C  
ATOM   5458  O   ALA A 776      -9.283  18.274  -7.022  1.00 98.32           O  
ANISOU 5458  O   ALA A 776    15632  10105  11620    914   2780   1433       O  
ATOM   5459  CB  ALA A 776      -9.661  21.162  -6.441  1.00 77.90           C  
ANISOU 5459  CB  ALA A 776    12727   7882   8990    883   2393   1367       C  
ATOM   5460  N   GLN A 777      -7.137  18.760  -6.574  1.00 83.40           N  
ANISOU 5460  N   GLN A 777    13783   8432   9473   1240   2565   1545       N  
ATOM   5461  CA  GLN A 777      -6.627  17.674  -7.405  1.00 85.86           C  
ANISOU 5461  CA  GLN A 777    14181   8633   9808   1234   2645   1544       C  
ATOM   5462  C   GLN A 777      -6.820  16.305  -6.758  1.00106.72           C  
ANISOU 5462  C   GLN A 777    17048  11065  12436   1318   2928   1636       C  
ATOM   5463  O   GLN A 777      -7.054  15.314  -7.450  1.00 83.97           O  
ANISOU 5463  O   GLN A 777    14232   8025   9647   1223   3067   1606       O  
ATOM   5464  CB  GLN A 777      -5.159  17.911  -7.770  1.00 75.66           C  
ANISOU 5464  CB  GLN A 777    12868   7482   8397   1380   2472   1568       C  
ATOM   5465  CG  GLN A 777      -4.966  19.065  -8.738  1.00 89.23           C  
ANISOU 5465  CG  GLN A 777    14373   9369  10161   1264   2223   1463       C  
ATOM   5466  CD  GLN A 777      -5.828  18.926  -9.977  1.00 91.81           C  
ANISOU 5466  CD  GLN A 777    14607   9620  10657   1020   2233   1347       C  
ATOM   5467  NE2 GLN A 777      -6.454  20.022 -10.394  1.00 50.52           N  
ANISOU 5467  NE2 GLN A 777     9200   4494   5501    877   2088   1258       N  
ATOM   5468  OE1 GLN A 777      -5.932  17.845 -10.554  1.00 95.52           O  
ANISOU 5468  OE1 GLN A 777    15165   9942  11187    964   2369   1335       O  
ATOM   5469  N   SER A 778      -6.725  16.252  -5.432  1.00130.07           N  
ANISOU 5469  N   SER A 778    20126  14018  15276   1499   3017   1746       N  
ATOM   5470  CA  SER A 778      -7.021  15.027  -4.695  1.00113.39           C  
ANISOU 5470  CA  SER A 778    18237  11699  13148   1585   3304   1843       C  
ATOM   5471  C   SER A 778      -8.527  14.889  -4.503  1.00 93.63           C  
ANISOU 5471  C   SER A 778    15724   9051  10799   1397   3475   1795       C  
ATOM   5472  O   SER A 778      -9.220  15.872  -4.252  1.00102.10           O  
ANISOU 5472  O   SER A 778    16663  10217  11913   1307   3380   1744       O  
ATOM   5473  CB  SER A 778      -6.301  15.012  -3.345  1.00111.55           C  
ANISOU 5473  CB  SER A 778    18146  11523  12716   1872   3335   1983       C  
ATOM   5474  OG  SER A 778      -6.644  16.144  -2.566  1.00127.79           O  
ANISOU 5474  OG  SER A 778    20106  13720  14728   1893   3219   1979       O  
ATOM   5475  N   THR A 779      -9.030  13.666  -4.625  1.00105.74           N  
ANISOU 5475  N   THR A 779    17397  10357  12423   1335   3733   1806       N  
ATOM   5476  CA  THR A 779     -10.466  13.416  -4.548  1.00117.94           C  
ANISOU 5476  CA  THR A 779    18929  11748  14135   1137   3915   1744       C  
ATOM   5477  C   THR A 779     -11.060  13.715  -3.169  1.00105.47           C  
ANISOU 5477  C   THR A 779    17420  10152  12504   1226   4025   1825       C  
ATOM   5478  O   THR A 779     -12.267  13.909  -3.037  1.00 81.06           O  
ANISOU 5478  O   THR A 779    14262   6994   9542   1060   4111   1762       O  
ATOM   5479  CB  THR A 779     -10.807  11.969  -4.963  1.00116.90           C  
ANISOU 5479  CB  THR A 779    18941  11361  14113   1057   4188   1735       C  
ATOM   5480  CG2 THR A 779      -9.822  10.992  -4.346  1.00130.94           C  
ANISOU 5480  CG2 THR A 779    20962  13048  15742   1309   4339   1888       C  
ATOM   5481  OG1 THR A 779     -12.132  11.641  -4.527  1.00 74.61           O  
ANISOU 5481  OG1 THR A 779    13614   5841   8894    918   4411   1705       O  
ATOM   5482  N   GLU A 780     -10.213  13.753  -2.147  1.00102.06           N  
ANISOU 5482  N   GLU A 780    17117   9785  11877   1492   4019   1962       N  
ATOM   5483  CA  GLU A 780     -10.663  14.082  -0.800  1.00 94.53           C  
ANISOU 5483  CA  GLU A 780    16237   8834  10847   1605   4107   2046       C  
ATOM   5484  C   GLU A 780     -10.620  15.589  -0.580  1.00 91.26           C  
ANISOU 5484  C   GLU A 780    15633   8661  10381   1604   3836   2002       C  
ATOM   5485  O   GLU A 780     -11.519  16.164   0.033  1.00 79.29           O  
ANISOU 5485  O   GLU A 780    14067   7153   8905   1541   3864   1988       O  
ATOM   5486  CB  GLU A 780      -9.795  13.376   0.240  1.00102.46           C  
ANISOU 5486  CB  GLU A 780    17481   9795  11655   1908   4239   2213       C  
ATOM   5487  CG  GLU A 780      -8.342  13.804   0.214  1.00130.88           C  
ANISOU 5487  CG  GLU A 780    21058  13599  15072   2115   4006   2255       C  
ATOM   5488  CD  GLU A 780      -7.393  12.638   0.377  1.00167.63           C  
ANISOU 5488  CD  GLU A 780    25929  18156  19608   2328   4146   2369       C  
ATOM   5489  OE1 GLU A 780      -7.848  11.556   0.803  1.00181.37           O  
ANISOU 5489  OE1 GLU A 780    27866  19672  21374   2361   4440   2444       O  
ATOM   5490  OE2 GLU A 780      -6.193  12.803   0.077  1.00178.61           O1-
ANISOU 5490  OE2 GLU A 780    27291  19690  20882   2464   3969   2382       O1-
ATOM   5491  N   GLY A 781      -9.563  16.219  -1.084  1.00 69.58           N  
ANISOU 5491  N   GLY A 781    12783   6105   7547   1672   3581   1978       N  
ATOM   5492  CA  GLY A 781      -9.445  17.663  -1.050  1.00 72.03           C  
ANISOU 5492  CA  GLY A 781    12902   6643   7823   1654   3315   1921       C  
ATOM   5493  C   GLY A 781     -10.534  18.316  -1.879  1.00 70.28           C  
ANISOU 5493  C   GLY A 781    12482   6430   7790   1373   3242   1782       C  
ATOM   5494  O   GLY A 781     -11.072  19.351  -1.509  1.00 53.07           O  
ANISOU 5494  O   GLY A 781    10182   4356   5624   1323   3140   1746       O  
ATOM   5495  N   TRP A 782     -10.863  17.708  -3.011  1.00 61.15           N  
ANISOU 5495  N   TRP A 782    11290   5168   6778   1195   3294   1699       N  
ATOM   5496  CA  TRP A 782     -11.936  18.213  -3.842  1.00 74.90           C  
ANISOU 5496  CA  TRP A 782    12849   6912   8698    935   3237   1561       C  
ATOM   5497  C   TRP A 782     -13.232  18.250  -3.044  1.00 89.78           C  
ANISOU 5497  C   TRP A 782    14749   8699  10665    854   3405   1560       C  
ATOM   5498  O   TRP A 782     -13.961  19.240  -3.071  1.00 88.62           O  
ANISOU 5498  O   TRP A 782    14443   8646  10583    738   3294   1488       O  
ATOM   5499  CB  TRP A 782     -12.111  17.341  -5.081  1.00 86.57           C  
ANISOU 5499  CB  TRP A 782    14317   8265  10310    774   3307   1477       C  
ATOM   5500  CG  TRP A 782     -12.994  17.946  -6.124  1.00 85.42           C  
ANISOU 5500  CG  TRP A 782    13962   8166  10326    526   3194   1322       C  
ATOM   5501  CD1 TRP A 782     -12.597  18.611  -7.245  1.00 87.30           C  
ANISOU 5501  CD1 TRP A 782    14040   8545  10583    449   2964   1233       C  
ATOM   5502  CD2 TRP A 782     -14.425  17.943  -6.146  1.00 76.46           C  
ANISOU 5502  CD2 TRP A 782    12756   6942   9353    331   3308   1235       C  
ATOM   5503  CE2 TRP A 782     -14.826  18.624  -7.312  1.00 75.41           C  
ANISOU 5503  CE2 TRP A 782    12415   6911   9324    149   3127   1094       C  
ATOM   5504  CE3 TRP A 782     -15.407  17.429  -5.294  1.00 72.07           C  
ANISOU 5504  CE3 TRP A 782    12290   6230   8865    296   3549   1262       C  
ATOM   5505  NE1 TRP A 782     -13.691  19.021  -7.965  1.00 77.07           N  
ANISOU 5505  NE1 TRP A 782    12582   7258   9442    227   2923   1100       N  
ATOM   5506  CZ2 TRP A 782     -16.166  18.807  -7.647  1.00 70.73           C  
ANISOU 5506  CZ2 TRP A 782    11697   6281   8897    -60   3170    975       C  
ATOM   5507  CZ3 TRP A 782     -16.737  17.612  -5.629  1.00 63.91           C  
ANISOU 5507  CZ3 TRP A 782    11127   5152   8006     77   3597   1140       C  
ATOM   5508  CH2 TRP A 782     -17.104  18.295  -6.794  1.00 75.94           C  
ANISOU 5508  CH2 TRP A 782    12437   6790   9626    -97   3403    996       C  
ATOM   5509  N   ASP A 783     -13.511  17.167  -2.324  1.00107.96           N  
ANISOU 5509  N   ASP A 783    17248  10807  12964    920   3680   1644       N  
ATOM   5510  CA  ASP A 783     -14.737  17.058  -1.537  1.00113.00           C  
ANISOU 5510  CA  ASP A 783    17923  11326  13687    847   3877   1650       C  
ATOM   5511  C   ASP A 783     -14.755  18.018  -0.353  1.00 99.44           C  
ANISOU 5511  C   ASP A 783    16198   9735  11848    983   3803   1720       C  
ATOM   5512  O   ASP A 783     -15.775  18.647  -0.076  1.00 85.81           O  
ANISOU 5512  O   ASP A 783    14372   8025  10208    866   3807   1668       O  
ATOM   5513  CB  ASP A 783     -14.957  15.621  -1.059  1.00130.07           C  
ANISOU 5513  CB  ASP A 783    20314  13235  15871    897   4209   1729       C  
ATOM   5514  CG  ASP A 783     -15.546  14.732  -2.137  1.00140.64           C  
ANISOU 5514  CG  ASP A 783    21628  14408  17401    679   4339   1620       C  
ATOM   5515  OD1 ASP A 783     -14.824  14.402  -3.101  1.00146.08           O  
ANISOU 5515  OD1 ASP A 783    22299  15117  18088    665   4249   1584       O  
ATOM   5516  OD2 ASP A 783     -16.734  14.363  -2.021  1.00135.07           O1-
ANISOU 5516  OD2 ASP A 783    20918  13552  16849    520   4535   1564       O1-
ATOM   5517  N   PHE A 784     -13.629  18.124   0.344  1.00 91.89           N  
ANISOU 5517  N   PHE A 784    15347   8875  10692   1234   3733   1833       N  
ATOM   5518  CA  PHE A 784     -13.509  19.077   1.441  1.00 95.00           C  
ANISOU 5518  CA  PHE A 784    15729   9412  10954   1378   3637   1892       C  
ATOM   5519  C   PHE A 784     -13.911  20.467   0.964  1.00 93.86           C  
ANISOU 5519  C   PHE A 784    15340   9445  10879   1229   3393   1777       C  
ATOM   5520  O   PHE A 784     -14.737  21.131   1.582  1.00100.15           O  
ANISOU 5520  O   PHE A 784    16080  10268  11705   1183   3404   1764       O  
ATOM   5521  CB  PHE A 784     -12.081  19.106   1.989  1.00 84.07           C  
ANISOU 5521  CB  PHE A 784    14445   8149   9347   1656   3534   1994       C  
ATOM   5522  CG  PHE A 784     -11.875  20.104   3.093  1.00112.63           C  
ANISOU 5522  CG  PHE A 784    18044  11930  12822   1811   3419   2042       C  
ATOM   5523  CD1 PHE A 784     -11.879  19.703   4.416  1.00100.98           C  
ANISOU 5523  CD1 PHE A 784    16757  10395  11215   2012   3587   2166       C  
ATOM   5524  CD2 PHE A 784     -11.688  21.446   2.806  1.00134.40           C  
ANISOU 5524  CD2 PHE A 784    20597  14897  15574   1757   3148   1959       C  
ATOM   5525  CE1 PHE A 784     -11.694  20.620   5.434  1.00101.10           C  
ANISOU 5525  CE1 PHE A 784    16754  10566  11095   2158   3478   2201       C  
ATOM   5526  CE2 PHE A 784     -11.505  22.368   3.822  1.00118.45           C  
ANISOU 5526  CE2 PHE A 784    18556  13024  13425   1894   3045   1993       C  
ATOM   5527  CZ  PHE A 784     -11.508  21.954   5.136  1.00110.03           C  
ANISOU 5527  CZ  PHE A 784    17675  11906  12228   2094   3206   2111       C  
ATOM   5528  N   LEU A 785     -13.317  20.900  -0.142  1.00 79.85           N  
ANISOU 5528  N   LEU A 785    13425   7788   9128   1159   3180   1697       N  
ATOM   5529  CA  LEU A 785     -13.631  22.196  -0.727  1.00 88.72           C  
ANISOU 5529  CA  LEU A 785    14319   9074  10316   1020   2950   1589       C  
ATOM   5530  C   LEU A 785     -15.116  22.321  -1.028  1.00 93.53           C  
ANISOU 5530  C   LEU A 785    14826   9598  11112    789   3036   1496       C  
ATOM   5531  O   LEU A 785     -15.708  23.373  -0.814  1.00 90.39           O  
ANISOU 5531  O   LEU A 785    14296   9302  10744    724   2932   1450       O  
ATOM   5532  CB  LEU A 785     -12.818  22.423  -2.001  1.00 83.22           C  
ANISOU 5532  CB  LEU A 785    13510   8477   9633    969   2751   1518       C  
ATOM   5533  CG  LEU A 785     -11.329  22.695  -1.790  1.00 66.05           C  
ANISOU 5533  CG  LEU A 785    11370   6445   7281   1180   2597   1580       C  
ATOM   5534  CD1 LEU A 785     -10.565  22.508  -3.080  1.00 49.54           C  
ANISOU 5534  CD1 LEU A 785     9216   4389   5219   1127   2477   1523       C  
ATOM   5535  CD2 LEU A 785     -11.118  24.091  -1.229  1.00 71.67           C  
ANISOU 5535  CD2 LEU A 785    11965   7354   7913   1242   2401   1570       C  
ATOM   5536  N   TYR A 786     -15.718  21.245  -1.521  1.00 98.17           N  
ANISOU 5536  N   TYR A 786    15471  10000  11828    664   3228   1463       N  
ATOM   5537  CA  TYR A 786     -17.129  21.286  -1.877  1.00 92.64           C  
ANISOU 5537  CA  TYR A 786    14663   9220  11317    436   3314   1358       C  
ATOM   5538  C   TYR A 786     -18.023  21.487  -0.659  1.00114.30           C  
ANISOU 5538  C   TYR A 786    17455  11910  14065    459   3461   1406       C  
ATOM   5539  O   TYR A 786     -19.065  22.135  -0.748  1.00113.32           O  
ANISOU 5539  O   TYR A 786    17187  11814  14054    308   3434   1322       O  
ATOM   5540  CB  TYR A 786     -17.553  20.033  -2.637  1.00 79.30           C  
ANISOU 5540  CB  TYR A 786    13028   7338   9767    299   3502   1302       C  
ATOM   5541  CG  TYR A 786     -19.005  20.071  -3.041  1.00102.24           C  
ANISOU 5541  CG  TYR A 786    15804  10170  12872     60   3583   1175       C  
ATOM   5542  CD1 TYR A 786     -19.432  20.890  -4.076  1.00109.67           C  
ANISOU 5542  CD1 TYR A 786    16524  11238  13909   -106   3384   1038       C  
ATOM   5543  CD2 TYR A 786     -19.952  19.303  -2.379  1.00 81.97           C  
ANISOU 5543  CD2 TYR A 786    13336   7413  10398      6   3863   1189       C  
ATOM   5544  CE1 TYR A 786     -20.761  20.939  -4.447  1.00115.87           C  
ANISOU 5544  CE1 TYR A 786    17180  11971  14872   -316   3449    914       C  
ATOM   5545  CE2 TYR A 786     -21.284  19.342  -2.744  1.00 82.44           C  
ANISOU 5545  CE2 TYR A 786    13264   7412  10646   -216   3937   1062       C  
ATOM   5546  CZ  TYR A 786     -21.684  20.162  -3.778  1.00108.16           C  
ANISOU 5546  CZ  TYR A 786    16294  10809  13993   -374   3723    922       C  
ATOM   5547  OH  TYR A 786     -23.009  20.208  -4.147  1.00115.32           O  
ANISOU 5547  OH  TYR A 786    17062  11671  15085   -586   3788    787       O  
ATOM   5548  N   SER A 787     -17.623  20.928   0.478  1.00122.32           N  
ANISOU 5548  N   SER A 787    18674  12849  14956    653   3619   1542       N  
ATOM   5549  CA  SER A 787     -18.357  21.147   1.716  1.00116.41           C  
ANISOU 5549  CA  SER A 787    17988  12058  14186    705   3756   1602       C  
ATOM   5550  C   SER A 787     -18.132  22.581   2.193  1.00117.09           C  
ANISOU 5550  C   SER A 787    17957  12362  14172    779   3524   1605       C  
ATOM   5551  O   SER A 787     -19.081  23.309   2.482  1.00127.50           O  
ANISOU 5551  O   SER A 787    19169  13713  15563    681   3512   1557       O  
ATOM   5552  CB  SER A 787     -17.921  20.154   2.794  1.00 98.73           C  
ANISOU 5552  CB  SER A 787    16011   9682  11822    915   3987   1754       C  
ATOM   5553  OG  SER A 787     -16.588  20.394   3.204  1.00 96.33           O  
ANISOU 5553  OG  SER A 787    15781   9512  11309   1154   3846   1846       O  
ATOM   5554  N   LYS A 788     -16.864  22.975   2.258  1.00 97.85           N  
ANISOU 5554  N   LYS A 788    15536  10073  11571    951   3342   1654       N  
ATOM   5555  CA  LYS A 788     -16.481  24.326   2.638  1.00 87.66           C  
ANISOU 5555  CA  LYS A 788    14132   8994  10181   1027   3111   1648       C  
ATOM   5556  C   LYS A 788     -17.077  25.336   1.662  1.00 95.49           C  
ANISOU 5556  C   LYS A 788    14884  10091  11308    817   2927   1512       C  
ATOM   5557  O   LYS A 788     -17.073  26.542   1.909  1.00 93.72           O  
ANISOU 5557  O   LYS A 788    14542  10023  11044    830   2756   1486       O  
ATOM   5558  CB  LYS A 788     -14.957  24.450   2.634  1.00 96.37           C  
ANISOU 5558  CB  LYS A 788    15277  10230  11111   1221   2949   1699       C  
ATOM   5559  CG  LYS A 788     -14.407  25.523   3.552  1.00132.88           C  
ANISOU 5559  CG  LYS A 788    19873  15036  15580   1385   2792   1736       C  
ATOM   5560  CD  LYS A 788     -14.618  25.154   5.011  1.00159.49           C  
ANISOU 5560  CD  LYS A 788    23422  18338  18837   1558   2974   1850       C  
ATOM   5561  CE  LYS A 788     -13.928  26.139   5.943  1.00179.65           C  
ANISOU 5561  CE  LYS A 788    25960  21083  21216   1745   2813   1883       C  
ATOM   5562  NZ  LYS A 788     -14.460  27.523   5.804  1.00180.50           N1+
ANISOU 5562  NZ  LYS A 788    25867  21325  21390   1617   2639   1791       N1+
ATOM   5563  N   TYR A 789     -17.598  24.822   0.555  1.00 99.89           N  
ANISOU 5563  N   TYR A 789    15374  10558  12022    628   2969   1423       N  
ATOM   5564  CA  TYR A 789     -18.109  25.642  -0.536  1.00102.01           C  
ANISOU 5564  CA  TYR A 789    15423  10920  12415    435   2797   1291       C  
ATOM   5565  C   TYR A 789     -19.450  26.297  -0.216  1.00134.90           C  
ANISOU 5565  C   TYR A 789    19478  15086  16691    304   2832   1233       C  
ATOM   5566  O   TYR A 789     -19.898  27.189  -0.933  1.00121.39           O  
ANISOU 5566  O   TYR A 789    17582  13480  15061    173   2673   1134       O  
ATOM   5567  CB  TYR A 789     -18.236  24.784  -1.794  1.00107.28           C  
ANISOU 5567  CB  TYR A 789    16065  11490  13208    288   2841   1212       C  
ATOM   5568  CG  TYR A 789     -18.893  25.474  -2.958  1.00120.72           C  
ANISOU 5568  CG  TYR A 789    17552  13271  15046     87   2692   1070       C  
ATOM   5569  CD1 TYR A 789     -18.179  26.352  -3.760  1.00127.75           C  
ANISOU 5569  CD1 TYR A 789    18318  14329  15892     92   2442   1027       C  
ATOM   5570  CD2 TYR A 789     -20.224  25.238  -3.264  1.00124.07           C  
ANISOU 5570  CD2 TYR A 789    17898  13603  15640   -103   2807    977       C  
ATOM   5571  CE1 TYR A 789     -18.775  26.982  -4.829  1.00106.90           C  
ANISOU 5571  CE1 TYR A 789    15491  11762  13364    -76   2310    905       C  
ATOM   5572  CE2 TYR A 789     -20.829  25.863  -4.331  1.00120.29           C  
ANISOU 5572  CE2 TYR A 789    17222  13207  15275   -272   2665    846       C  
ATOM   5573  CZ  TYR A 789     -20.099  26.734  -5.110  1.00106.82           C  
ANISOU 5573  CZ  TYR A 789    15406  11667  13513   -252   2417    815       C  
ATOM   5574  OH  TYR A 789     -20.700  27.358  -6.175  1.00 83.98           O  
ANISOU 5574  OH  TYR A 789    12327   8858  10723   -405   2280    690       O  
ATOM   5575  N   GLN A 790     -20.085  25.854   0.861  1.00186.29           N  
ANISOU 5575  N   GLN A 790    26105  21478  23201    345   3044   1298       N  
ATOM   5576  CA  GLN A 790     -21.391  26.372   1.244  1.00211.67           C  
ANISOU 5576  CA  GLN A 790    29227  24674  26522    226   3106   1249       C  
ATOM   5577  C   GLN A 790     -21.253  27.454   2.299  1.00204.75           C  
ANISOU 5577  C   GLN A 790    28343  23929  25524    356   3011   1308       C  
ATOM   5578  O   GLN A 790     -22.002  28.431   2.321  1.00218.83           O  
ANISOU 5578  O   GLN A 790    29982  25795  27369    266   2926   1246       O  
ATOM   5579  CB  GLN A 790     -22.250  25.237   1.784  1.00238.01           C  
ANISOU 5579  CB  GLN A 790    32694  27791  29947    180   3415   1277       C  
ATOM   5580  CG  GLN A 790     -22.549  24.174   0.756  1.00257.32           C  
ANISOU 5580  CG  GLN A 790    35136  30097  32538     26   3528   1198       C  
ATOM   5581  CD  GLN A 790     -23.324  24.728  -0.413  1.00270.97           C  
ANISOU 5581  CD  GLN A 790    36635  31896  34426   -195   3393   1038       C  
ATOM   5582  NE2 GLN A 790     -23.009  24.257  -1.610  1.00272.37           N  
ANISOU 5582  NE2 GLN A 790    36765  32061  34662   -283   3334    963       N  
ATOM   5583  OE1 GLN A 790     -24.199  25.574  -0.242  1.00280.03           O  
ANISOU 5583  OE1 GLN A 790    37649  33110  35638   -278   3343    983       O  
ATOM   5584  N   PHE A 791     -20.280  27.259   3.176  1.00168.27           N  
ANISOU 5584  N   PHE A 791    23880  19328  20727    575   3028   1425       N  
ATOM   5585  CA  PHE A 791     -19.989  28.197   4.240  1.00156.22           C  
ANISOU 5585  CA  PHE A 791    22365  17929  19062    725   2939   1484       C  
ATOM   5586  C   PHE A 791     -18.941  29.189   3.744  1.00157.49           C  
ANISOU 5586  C   PHE A 791    22412  18292  19134    782   2655   1451       C  
ATOM   5587  O   PHE A 791     -18.136  29.711   4.514  1.00153.41           O  
ANISOU 5587  O   PHE A 791    21941  17890  18459    959   2562   1509       O  
ATOM   5588  CB  PHE A 791     -19.488  27.418   5.453  1.00150.95           C  
ANISOU 5588  CB  PHE A 791    21931  17180  18244    943   3112   1621       C  
ATOM   5589  CG  PHE A 791     -19.245  28.259   6.659  1.00161.96           C  
ANISOU 5589  CG  PHE A 791    23357  18692  19487   1111   3049   1683       C  
ATOM   5590  CD1 PHE A 791     -20.300  28.731   7.419  1.00175.22           C  
ANISOU 5590  CD1 PHE A 791    25015  20348  21211   1067   3136   1683       C  
ATOM   5591  CD2 PHE A 791     -17.955  28.560   7.048  1.00156.89           C  
ANISOU 5591  CD2 PHE A 791    22766  18187  18659   1315   2905   1736       C  
ATOM   5592  CE1 PHE A 791     -20.072  29.501   8.538  1.00176.19           C  
ANISOU 5592  CE1 PHE A 791    25172  20581  21192   1224   3079   1736       C  
ATOM   5593  CE2 PHE A 791     -17.720  29.328   8.162  1.00161.59           C  
ANISOU 5593  CE2 PHE A 791    23387  18897  19113   1471   2843   1781       C  
ATOM   5594  CZ  PHE A 791     -18.779  29.798   8.910  1.00169.24           C  
ANISOU 5594  CZ  PHE A 791    24340  19839  20123   1426   2930   1783       C  
ATOM   5595  N   SER A 792     -18.960  29.444   2.440  1.00158.84           N  
ANISOU 5595  N   SER A 792    22434  18509  19411    629   2521   1351       N  
ATOM   5596  CA  SER A 792     -17.997  30.346   1.823  1.00176.21           C  
ANISOU 5596  CA  SER A 792    24521  20884  21547    663   2266   1312       C  
ATOM   5597  C   SER A 792     -18.354  31.804   2.085  1.00186.03           C  
ANISOU 5597  C   SER A 792    25619  22273  22790    635   2111   1267       C  
ATOM   5598  O   SER A 792     -17.572  32.705   1.787  1.00203.28           O  
ANISOU 5598  O   SER A 792    27714  24609  24913    678   1908   1240       O  
ATOM   5599  CB  SER A 792     -17.906  30.080   0.319  1.00190.41           C  
ANISOU 5599  CB  SER A 792    26221  22671  23453    517   2189   1226       C  
ATOM   5600  OG  SER A 792     -19.183  30.155  -0.288  1.00202.55           O  
ANISOU 5600  OG  SER A 792    27643  24153  25163    313   2235   1135       O  
ATOM   5601  N   LEU A 793     -19.545  32.027   2.634  1.00165.98           N  
ANISOU 5601  N   LEU A 793    23056  19683  20326    560   2217   1257       N  
ATOM   5602  CA  LEU A 793     -19.963  33.357   3.072  1.00155.88           C  
ANISOU 5602  CA  LEU A 793    21661  18526  19040    548   2102   1227       C  
ATOM   5603  C   LEU A 793     -20.239  34.329   1.935  1.00164.29           C  
ANISOU 5603  C   LEU A 793    22522  19694  20206    399   1917   1118       C  
ATOM   5604  O   LEU A 793     -19.995  35.527   2.078  1.00127.99           O  
ANISOU 5604  O   LEU A 793    17831  15236  15563    430   1757   1097       O  
ATOM   5605  CB  LEU A 793     -18.905  33.964   3.990  1.00143.15           C  
ANISOU 5605  CB  LEU A 793    20106  17038  17245    751   1998   1289       C  
ATOM   5606  CG  LEU A 793     -18.687  33.249   5.316  1.00139.59           C  
ANISOU 5606  CG  LEU A 793    19855  16517  16668    930   2164   1401       C  
ATOM   5607  CD1 LEU A 793     -17.398  33.727   5.954  1.00123.81           C  
ANISOU 5607  CD1 LEU A 793    17900  14659  14482   1136   2029   1444       C  
ATOM   5608  CD2 LEU A 793     -19.877  33.478   6.234  1.00129.05           C  
ANISOU 5608  CD2 LEU A 793    18536  15124  15375    899   2301   1418       C  
ATOM   5609  N   SER A 794     -20.750  33.825   0.817  1.00205.09           N  
ANISOU 5609  N   SER A 794    27623  24795  25508    241   1942   1048       N  
ATOM   5610  CA  SER A 794     -21.017  34.672  -0.338  1.00211.64           C  
ANISOU 5610  CA  SER A 794    28267  25721  26427    109   1771    946       C  
ATOM   5611  C   SER A 794     -19.843  35.619  -0.537  1.00208.94           C  
ANISOU 5611  C   SER A 794    27878  25534  25978    205   1560    951       C  
ATOM   5612  O   SER A 794     -20.015  36.796  -0.849  1.00207.75           O  
ANISOU 5612  O   SER A 794    27591  25496  25848    161   1414    899       O  
ATOM   5613  CB  SER A 794     -22.304  35.467  -0.129  1.00207.83           C  
ANISOU 5613  CB  SER A 794    27666  25260  26041      3   1779    893       C  
ATOM   5614  OG  SER A 794     -23.400  34.601   0.101  1.00203.51           O  
ANISOU 5614  OG  SER A 794    27157  24568  25601    -89   1984    882       O  
ATOM   5615  N   SER A 795     -18.644  35.082  -0.346  1.00188.90           N  
ANISOU 5615  N   SER A 795    25452  22997  23324    340   1552   1012       N  
ATOM   5616  CA  SER A 795     -17.435  35.881  -0.289  1.00150.25           C  
ANISOU 5616  CA  SER A 795    20532  18243  18313    456   1377   1024       C  
ATOM   5617  C   SER A 795     -16.771  35.945  -1.653  1.00134.63           C  
ANISOU 5617  C   SER A 795    18474  16312  16368    397   1243    968       C  
ATOM   5618  O   SER A 795     -17.362  35.564  -2.664  1.00112.79           O  
ANISOU 5618  O   SER A 795    15651  13488  13715    258   1264    911       O  
ATOM   5619  CB  SER A 795     -16.469  35.263   0.724  1.00114.30           C  
ANISOU 5619  CB  SER A 795    16143  13677  13608    652   1440   1118       C  
ATOM   5620  OG  SER A 795     -15.577  36.225   1.250  1.00111.76           O  
ANISOU 5620  OG  SER A 795    15792  13503  13170    775   1294   1125       O  
ATOM   5621  N   THR A 796     -15.541  36.445  -1.674  1.00138.06           N  
ANISOU 5621  N   THR A 796    18899  16855  16700    505   1106    979       N  
ATOM   5622  CA  THR A 796     -14.690  36.313  -2.840  1.00126.34           C  
ANISOU 5622  CA  THR A 796    17376  15403  15224    484   1003    945       C  
ATOM   5623  C   THR A 796     -14.172  34.883  -2.840  1.00117.84           C  
ANISOU 5623  C   THR A 796    16446  14220  14108    548   1123   1000       C  
ATOM   5624  O   THR A 796     -13.917  34.297  -3.893  1.00103.85           O  
ANISOU 5624  O   THR A 796    14667  12406  12384    486   1114    972       O  
ATOM   5625  CB  THR A 796     -13.498  37.287  -2.787  1.00123.40           C  
ANISOU 5625  CB  THR A 796    16950  15178  14759    583    831    937       C  
ATOM   5626  CG2 THR A 796     -13.984  38.724  -2.741  1.00119.44           C  
ANISOU 5626  CG2 THR A 796    16314  14775  14295    526    724    885       C  
ATOM   5627  OG1 THR A 796     -12.713  37.025  -1.620  1.00106.57           O  
ANISOU 5627  OG1 THR A 796    14930  13071  12490    760    863   1005       O  
ATOM   5628  N   GLU A 797     -14.041  34.324  -1.639  1.00114.29           N  
ANISOU 5628  N   GLU A 797    16134  13723  13569    678   1242   1081       N  
ATOM   5629  CA  GLU A 797     -13.539  32.967  -1.450  1.00 79.10           C  
ANISOU 5629  CA  GLU A 797    11838   9159   9058    767   1375   1149       C  
ATOM   5630  C   GLU A 797     -14.369  31.924  -2.181  1.00 93.35           C  
ANISOU 5630  C   GLU A 797    13671  10808  10990    626   1518   1125       C  
ATOM   5631  O   GLU A 797     -13.825  30.959  -2.714  1.00116.18           O  
ANISOU 5631  O   GLU A 797    16638  13628  13875    644   1568   1142       O  
ATOM   5632  CB  GLU A 797     -13.480  32.614   0.037  1.00 80.61           C  
ANISOU 5632  CB  GLU A 797    12174   9319   9135    930   1497   1241       C  
ATOM   5633  CG  GLU A 797     -13.026  31.186   0.300  1.00 92.91           C  
ANISOU 5633  CG  GLU A 797    13914  10755  10632   1035   1656   1321       C  
ATOM   5634  CD  GLU A 797     -13.070  30.810   1.768  1.00110.66           C  
ANISOU 5634  CD  GLU A 797    16317  12964  12765   1201   1793   1418       C  
ATOM   5635  OE1 GLU A 797     -14.181  30.557   2.286  1.00101.26           O  
ANISOU 5635  OE1 GLU A 797    15170  11668  11637   1142   1950   1437       O  
ATOM   5636  OE2 GLU A 797     -11.995  30.757   2.404  1.00104.71           O1-
ANISOU 5636  OE2 GLU A 797    15641  12286  11856   1397   1748   1474       O1-
ATOM   5637  N   LYS A 798     -15.684  32.103  -2.196  1.00107.58           N  
ANISOU 5637  N   LYS A 798    15411  12556  12908    488   1588   1082       N  
ATOM   5638  CA  LYS A 798     -16.548  31.169  -2.903  1.00127.40           C  
ANISOU 5638  CA  LYS A 798    17928  14925  15552    339   1721   1039       C  
ATOM   5639  C   LYS A 798     -16.139  31.054  -4.365  1.00130.65           C  
ANISOU 5639  C   LYS A 798    18259  15362  16019    249   1612    968       C  
ATOM   5640  O   LYS A 798     -15.928  29.955  -4.875  1.00140.44           O  
ANISOU 5640  O   LYS A 798    19578  16498  17286    230   1704    971       O  
ATOM   5641  CB  LYS A 798     -18.014  31.581  -2.808  0.00191.73           C  
ANISOU 5641  CB  LYS A 798    25980  23044  23824    194   1777    980       C  
ATOM   5642  CG  LYS A 798     -18.914  30.740  -3.693  0.00239.02           C  
ANISOU 5642  CG  LYS A 798    31940  28912  29966     22   1886    905       C  
ATOM   5643  CD  LYS A 798     -20.374  30.870  -3.313  0.00270.25           C  
ANISOU 5643  CD  LYS A 798    35837  32808  34036    -97   1998    862       C  
ATOM   5644  CE  LYS A 798     -21.226  29.922  -4.140  0.00288.96           C  
ANISOU 5644  CE  LYS A 798    38181  35052  36559   -264   2121    778       C  
ATOM   5645  NZ  LYS A 798     -22.644  29.910  -3.694  0.00297.78           N1+
ANISOU 5645  NZ  LYS A 798    39250  36098  37796   -377   2257    733       N1+
ATOM   5646  N   SER A 799     -16.027  32.196  -5.033  1.00102.29           N  
ANISOU 5646  N   SER A 799    14517  11905  12444    199   1422    905       N  
ATOM   5647  CA  SER A 799     -15.662  32.228  -6.445  1.00 88.95           C  
ANISOU 5647  CA  SER A 799    12744  10252  10802    118   1308    837       C  
ATOM   5648  C   SER A 799     -14.285  31.613  -6.691  1.00 87.73           C  
ANISOU 5648  C   SER A 799    12683  10098  10554    234   1282    885       C  
ATOM   5649  O   SER A 799     -14.018  31.086  -7.771  1.00 71.28           O  
ANISOU 5649  O   SER A 799    10589   7983   8512    174   1263    845       O  
ATOM   5650  CB  SER A 799     -15.702  33.662  -6.979  1.00 94.65           C  
ANISOU 5650  CB  SER A 799    13303  11122  11540     72   1115    777       C  
ATOM   5651  OG  SER A 799     -15.341  33.701  -8.347  1.00117.06           O  
ANISOU 5651  OG  SER A 799    16068  13994  14415      5   1010    716       O  
ATOM   5652  N   GLN A 800     -13.418  31.687  -5.688  1.00 78.37           N  
ANISOU 5652  N   GLN A 800    11586   8952   9238    404   1279    966       N  
ATOM   5653  CA  GLN A 800     -12.092  31.084  -5.775  1.00 71.31           C  
ANISOU 5653  CA  GLN A 800    10786   8065   8245    534   1261   1017       C  
ATOM   5654  C   GLN A 800     -12.187  29.560  -5.748  1.00 79.84           C  
ANISOU 5654  C   GLN A 800    12017   8980   9340    545   1453   1060       C  
ATOM   5655  O   GLN A 800     -11.545  28.873  -6.543  1.00 80.60           O  
ANISOU 5655  O   GLN A 800    12150   9040   9437    546   1450   1054       O  
ATOM   5656  CB  GLN A 800     -11.187  31.586  -4.646  1.00 64.74           C  
ANISOU 5656  CB  GLN A 800    10000   7331   7265    722   1205   1083       C  
ATOM   5657  CG  GLN A 800     -10.893  33.076  -4.711  1.00 71.51           C  
ANISOU 5657  CG  GLN A 800    10713   8352   8104    720   1015   1036       C  
ATOM   5658  CD  GLN A 800      -9.880  33.519  -3.678  1.00 75.52           C  
ANISOU 5658  CD  GLN A 800    11259   8966   8468    905    951   1083       C  
ATOM   5659  NE2 GLN A 800      -8.853  34.236  -4.124  1.00 60.40           N  
ANISOU 5659  NE2 GLN A 800     9262   7175   6513    946    790   1048       N  
ATOM   5660  OE1 GLN A 800     -10.018  33.226  -2.492  1.00 78.98           O  
ANISOU 5660  OE1 GLN A 800    11798   9378   8831   1013   1047   1147       O  
ATOM   5661  N   ILE A 801     -12.992  29.035  -4.830  1.00 74.73           N  
ANISOU 5661  N   ILE A 801    11461   8225   8707    552   1627   1104       N  
ATOM   5662  CA  ILE A 801     -13.258  27.604  -4.790  1.00 85.81           C  
ANISOU 5662  CA  ILE A 801    13008   9451  10146    542   1836   1139       C  
ATOM   5663  C   ILE A 801     -13.914  27.175  -6.096  1.00 89.33           C  
ANISOU 5663  C   ILE A 801    13376   9823  10740    348   1854   1041       C  
ATOM   5664  O   ILE A 801     -13.380  26.340  -6.821  1.00 80.35           O  
ANISOU 5664  O   ILE A 801    12294   8624   9610    344   1884   1036       O  
ATOM   5665  CB  ILE A 801     -14.181  27.234  -3.623  1.00 83.64           C  
ANISOU 5665  CB  ILE A 801    12828   9069   9883    559   2029   1191       C  
ATOM   5666  CG1 ILE A 801     -13.603  27.751  -2.305  1.00 69.98           C  
ANISOU 5666  CG1 ILE A 801    11165   7425   7998    755   2000   1280       C  
ATOM   5667  CG2 ILE A 801     -14.386  25.729  -3.567  1.00 99.19           C  
ANISOU 5667  CG2 ILE A 801    14958  10842  11889    556   2262   1232       C  
ATOM   5668  CD1 ILE A 801     -14.406  27.344  -1.090  1.00 66.19           C  
ANISOU 5668  CD1 ILE A 801    10801   6838   7509    798   2200   1346       C  
ATOM   5669  N   GLU A 802     -15.075  27.754  -6.383  1.00 64.67           N  
ANISOU 5669  N   GLU A 802    10125   6713   7734    192   1835    959       N  
ATOM   5670  CA  GLU A 802     -15.778  27.508  -7.636  1.00 60.63           C  
ANISOU 5670  CA  GLU A 802     9514   6161   7361      6   1827    848       C  
ATOM   5671  C   GLU A 802     -14.790  27.281  -8.781  1.00 79.46           C  
ANISOU 5671  C   GLU A 802    11886   8584   9721     14   1716    822       C  
ATOM   5672  O   GLU A 802     -15.003  26.424  -9.635  1.00 81.76           O  
ANISOU 5672  O   GLU A 802    12191   8783  10092    -81   1784    767       O  
ATOM   5673  CB  GLU A 802     -16.716  28.681  -7.944  1.00 60.68           C  
ANISOU 5673  CB  GLU A 802     9340   6269   7447   -115   1709    762       C  
ATOM   5674  CG  GLU A 802     -17.042  28.884  -9.416  1.00108.13           C  
ANISOU 5674  CG  GLU A 802    15210  12321  13553   -262   1598    645       C  
ATOM   5675  CD  GLU A 802     -17.714  30.224  -9.685  1.00139.67           C  
ANISOU 5675  CD  GLU A 802    19033  16447  17590   -335   1450    579       C  
ATOM   5676  OE1 GLU A 802     -17.303  30.921 -10.638  1.00135.42           O  
ANISOU 5676  OE1 GLU A 802    18394  16018  17040   -354   1279    533       O  
ATOM   5677  OE2 GLU A 802     -18.646  30.584  -8.936  1.00147.76           O1-
ANISOU 5677  OE2 GLU A 802    20025  17461  18655   -369   1511    576       O1-
ATOM   5678  N   PHE A 803     -13.700  28.043  -8.784  1.00 61.73           N  
ANISOU 5678  N   PHE A 803     9615   6473   7368    129   1552    857       N  
ATOM   5679  CA  PHE A 803     -12.662  27.894  -9.795  1.00 62.83           C  
ANISOU 5679  CA  PHE A 803     9744   6656   7473    153   1446    841       C  
ATOM   5680  C   PHE A 803     -11.885  26.603  -9.585  1.00 64.59           C  
ANISOU 5680  C   PHE A 803    10138   6767   7636    257   1577    913       C  
ATOM   5681  O   PHE A 803     -11.763  25.785 -10.497  1.00 59.63           O  
ANISOU 5681  O   PHE A 803     9536   6062   7057    195   1618    877       O  
ATOM   5682  CB  PHE A 803     -11.704  29.086  -9.763  1.00 55.55           C  
ANISOU 5682  CB  PHE A 803     8745   5904   6457    249   1249    858       C  
ATOM   5683  CG  PHE A 803     -10.593  28.996 -10.769  1.00 72.04           C  
ANISOU 5683  CG  PHE A 803    10821   8041   8510    280   1142    843       C  
ATOM   5684  CD1 PHE A 803     -10.759  29.495 -12.051  1.00 88.84           C  
ANISOU 5684  CD1 PHE A 803    12825  10224  10707    163   1023    756       C  
ATOM   5685  CD2 PHE A 803      -9.382  28.406 -10.439  1.00 73.75           C  
ANISOU 5685  CD2 PHE A 803    11151   8250   8621    433   1162    917       C  
ATOM   5686  CE1 PHE A 803      -9.738  29.410 -12.989  1.00 67.56           C  
ANISOU 5686  CE1 PHE A 803    10121   7569   7979    192    933    744       C  
ATOM   5687  CE2 PHE A 803      -8.356  28.317 -11.373  1.00 77.81           C  
ANISOU 5687  CE2 PHE A 803    11649   8807   9106    459   1068    902       C  
ATOM   5688  CZ  PHE A 803      -8.537  28.821 -12.649  1.00 34.75           C  
ANISOU 5688  CZ  PHE A 803     6075   3403   3727    336    956    816       C  
ATOM   5689  N   ALA A 804     -11.355  26.432  -8.377  1.00 57.34           N  
ANISOU 5689  N   ALA A 804     9337   5843   6606    423   1641   1016       N  
ATOM   5690  CA  ALA A 804     -10.550  25.259  -8.038  1.00 66.92           C  
ANISOU 5690  CA  ALA A 804    10725   6961   7742    555   1765   1099       C  
ATOM   5691  C   ALA A 804     -11.285  23.952  -8.319  1.00 72.58           C  
ANISOU 5691  C   ALA A 804    11537   7482   8559    457   1976   1084       C  
ATOM   5692  O   ALA A 804     -10.693  22.983  -8.792  1.00 84.47           O  
ANISOU 5692  O   ALA A 804    13137   8906  10053    489   2043   1102       O  
ATOM   5693  CB  ALA A 804     -10.116  25.320  -6.580  1.00 44.98           C  
ANISOU 5693  CB  ALA A 804     8056   4206   4830    748   1816   1207       C  
ATOM   5694  N   LEU A 805     -12.579  23.929  -8.019  1.00 63.11           N  
ANISOU 5694  N   LEU A 805    10311   6206   7462    336   2086   1047       N  
ATOM   5695  CA  LEU A 805     -13.393  22.746  -8.259  1.00 86.42           C  
ANISOU 5695  CA  LEU A 805    13337   8968  10529    223   2297   1015       C  
ATOM   5696  C   LEU A 805     -13.468  22.406  -9.743  1.00 79.05           C  
ANISOU 5696  C   LEU A 805    12323   8015   9695     75   2245    906       C  
ATOM   5697  O   LEU A 805     -13.397  21.240 -10.124  1.00 73.66           O  
ANISOU 5697  O   LEU A 805    11742   7193   9055     48   2386    901       O  
ATOM   5698  CB  LEU A 805     -14.802  22.938  -7.693  1.00 97.46           C  
ANISOU 5698  CB  LEU A 805    14693  10309  12031    109   2407    979       C  
ATOM   5699  CG  LEU A 805     -14.939  22.980  -6.169  1.00 67.90           C  
ANISOU 5699  CG  LEU A 805    11061   6533   8205    242   2525   1087       C  
ATOM   5700  CD1 LEU A 805     -16.376  23.267  -5.783  1.00 65.76           C  
ANISOU 5700  CD1 LEU A 805    10718   6214   8052    106   2617   1034       C  
ATOM   5701  CD2 LEU A 805     -14.463  21.675  -5.547  1.00 63.78           C  
ANISOU 5701  CD2 LEU A 805    10761   5852   7621    371   2740   1192       C  
ATOM   5702  N   CYS A 806     -13.613  23.427 -10.580  1.00 54.08           N  
ANISOU 5702  N   CYS A 806     8986   4993   6570    -16   2046    819       N  
ATOM   5703  CA  CYS A 806     -13.720  23.216 -12.020  1.00 69.25           C  
ANISOU 5703  CA  CYS A 806    10820   6915   8576   -151   1979    709       C  
ATOM   5704  C   CYS A 806     -12.371  22.860 -12.638  1.00 62.06           C  
ANISOU 5704  C   CYS A 806     9971   6031   7580    -52   1907    746       C  
ATOM   5705  O   CYS A 806     -12.293  22.491 -13.809  1.00 54.15           O  
ANISOU 5705  O   CYS A 806     8930   5011   6632   -140   1872    669       O  
ATOM   5706  CB  CYS A 806     -14.293  24.458 -12.703  1.00 75.49           C  
ANISOU 5706  CB  CYS A 806    11411   7851   9420   -261   1791    613       C  
ATOM   5707  SG  CYS A 806     -15.992  24.832 -12.248  1.00 75.74           S  
ANISOU 5707  SG  CYS A 806    11345   7855   9577   -406   1867    541       S  
ATOM   5708  N   ARG A 807     -11.316  22.964 -11.837  1.00 46.13           N  
ANISOU 5708  N   ARG A 807     8045   4057   5425    136   1885    859       N  
ATOM   5709  CA  ARG A 807      -9.957  22.795 -12.329  1.00 74.52           C  
ANISOU 5709  CA  ARG A 807    11681   7704   8928    248   1796    896       C  
ATOM   5710  C   ARG A 807      -9.429  21.375 -12.110  1.00 76.58           C  
ANISOU 5710  C   ARG A 807    12130   7813   9155    335   1977    965       C  
ATOM   5711  O   ARG A 807      -8.354  21.022 -12.590  1.00 74.21           O  
ANISOU 5711  O   ARG A 807    11876   7529   8789    420   1931    992       O  
ATOM   5712  CB  ARG A 807      -9.035  23.836 -11.678  1.00 92.40           C  
ANISOU 5712  CB  ARG A 807    13913  10131  11064    402   1642    961       C  
ATOM   5713  CG  ARG A 807      -7.596  23.819 -12.168  1.00127.51           C  
ANISOU 5713  CG  ARG A 807    18377  14653  15417    519   1532    991       C  
ATOM   5714  CD  ARG A 807      -7.500  24.004 -13.678  1.00124.86           C  
ANISOU 5714  CD  ARG A 807    17936  14354  15150    396   1419    896       C  
ATOM   5715  NE  ARG A 807      -6.122  23.875 -14.145  1.00133.04           N  
ANISOU 5715  NE  ARG A 807    19001  15446  16103    507   1337    927       N  
ATOM   5716  CZ  ARG A 807      -5.779  23.662 -15.411  1.00130.28           C  
ANISOU 5716  CZ  ARG A 807    18613  15095  15790    441   1279    869       C  
ATOM   5717  NH1 ARG A 807      -6.714  23.550 -16.342  1.00124.02           N1+
ANISOU 5717  NH1 ARG A 807    17755  14257  15111    268   1289    774       N1+
ATOM   5718  NH2 ARG A 807      -4.502  23.551 -15.749  1.00137.53           N  
ANISOU 5718  NH2 ARG A 807    19560  16064  16630    550   1213    902       N  
ATOM   5719  N   THR A 808     -10.192  20.558 -11.396  1.00 59.13           N  
ANISOU 5719  N   THR A 808    10028   5449   6990    316   2190    995       N  
ATOM   5720  CA  THR A 808      -9.795  19.177 -11.147  1.00 77.53           C  
ANISOU 5720  CA  THR A 808    12550   7615   9295    397   2389   1064       C  
ATOM   5721  C   THR A 808      -9.695  18.410 -12.464  1.00 77.52           C  
ANISOU 5721  C   THR A 808    12543   7537   9375    285   2408    983       C  
ATOM   5722  O   THR A 808     -10.326  18.781 -13.451  1.00 68.52           O  
ANISOU 5722  O   THR A 808    11262   6434   8340    114   2321    862       O  
ATOM   5723  CB  THR A 808     -10.794  18.463 -10.206  1.00 91.37           C  
ANISOU 5723  CB  THR A 808    14413   9199  11105    371   2635   1098       C  
ATOM   5724  CG2 THR A 808     -12.035  18.011 -10.971  1.00 60.88           C  
ANISOU 5724  CG2 THR A 808    10485   5221   7425    137   2735    970       C  
ATOM   5725  OG1 THR A 808     -10.166  17.329  -9.590  1.00 88.75           O  
ANISOU 5725  OG1 THR A 808    14292   8735  10694    525   2817   1209       O  
ATOM   5726  N   GLN A 809      -8.899  17.344 -12.481  1.00 86.40           N  
ANISOU 5726  N   GLN A 809    13823   8559  10445    390   2521   1048       N  
ATOM   5727  CA  GLN A 809      -8.749  16.517 -13.677  1.00 80.01           C  
ANISOU 5727  CA  GLN A 809    13029   7664   9706    296   2557    977       C  
ATOM   5728  C   GLN A 809      -9.722  15.338 -13.660  1.00 92.66           C  
ANISOU 5728  C   GLN A 809    14726   9048  11435    176   2811    937       C  
ATOM   5729  O   GLN A 809      -9.838  14.599 -14.638  1.00 82.04           O  
ANISOU 5729  O   GLN A 809    13387   7612  10173     66   2866    856       O  
ATOM   5730  CB  GLN A 809      -7.313  16.010 -13.806  1.00 59.64           C  
ANISOU 5730  CB  GLN A 809    10561   5095   7006    471   2536   1062       C  
ATOM   5731  CG  GLN A 809      -6.270  17.107 -13.917  1.00 69.94           C  
ANISOU 5731  CG  GLN A 809    11767   6610   8197    583   2293   1087       C  
ATOM   5732  CD  GLN A 809      -6.304  17.805 -15.257  1.00 94.37           C  
ANISOU 5732  CD  GLN A 809    14690   9811  11355    443   2106    971       C  
ATOM   5733  NE2 GLN A 809      -6.503  19.118 -15.241  1.00 97.08           N  
ANISOU 5733  NE2 GLN A 809    14879  10313  11693    411   1929    936       N  
ATOM   5734  OE1 GLN A 809      -6.148  17.170 -16.298  1.00 99.74           O  
ANISOU 5734  OE1 GLN A 809    15381  10430  12086    371   2125    913       O  
ATOM   5735  N   ASN A 810     -10.414  15.167 -12.541  1.00 76.36           N  
ANISOU 5735  N   ASN A 810    12734   6895   9383    197   2971    991       N  
ATOM   5736  CA  ASN A 810     -11.442  14.143 -12.420  1.00 91.37           C  
ANISOU 5736  CA  ASN A 810    14715   8585  11416     72   3226    948       C  
ATOM   5737  C   ASN A 810     -12.646  14.462 -13.302  1.00 81.51           C  
ANISOU 5737  C   ASN A 810    13286   7346  10336   -177   3181    776       C  
ATOM   5738  O   ASN A 810     -13.461  15.317 -12.960  1.00 88.28           O  
ANISOU 5738  O   ASN A 810    14025   8282  11236   -248   3118    737       O  
ATOM   5739  CB  ASN A 810     -11.879  14.020 -10.964  1.00121.54           C  
ANISOU 5739  CB  ASN A 810    18650  12326  15203    165   3399   1053       C  
ATOM   5740  CG  ASN A 810     -12.781  12.831 -10.727  1.00115.93           C  
ANISOU 5740  CG  ASN A 810    18057  11372  14618     66   3700   1030       C  
ATOM   5741  ND2 ASN A 810     -12.755  12.308  -9.516  1.00130.50           N  
ANISOU 5741  ND2 ASN A 810    20082  13102  16401    205   3901   1159       N  
ATOM   5742  OD1 ASN A 810     -13.490  12.386 -11.624  1.00 78.90           O  
ANISOU 5742  OD1 ASN A 810    13299   6598  10080   -132   3757    896       O  
ATOM   5743  N   LYS A 811     -12.760  13.769 -14.431  1.00 64.39           N  
ANISOU 5743  N   LYS A 811    11099   5104   8262   -305   3213    669       N  
ATOM   5744  CA  LYS A 811     -13.821  14.058 -15.393  1.00 65.49           C  
ANISOU 5744  CA  LYS A 811    11060   5273   8552   -532   3149    491       C  
ATOM   5745  C   LYS A 811     -15.214  13.746 -14.858  1.00 72.54           C  
ANISOU 5745  C   LYS A 811    11936   6039   9586   -673   3340    426       C  
ATOM   5746  O   LYS A 811     -16.197  14.369 -15.258  1.00 78.98           O  
ANISOU 5746  O   LYS A 811    12578   6929  10502   -828   3256    301       O  
ATOM   5747  CB  LYS A 811     -13.593  13.308 -16.706  1.00 71.07           C  
ANISOU 5747  CB  LYS A 811    11760   5924   9320   -628   3149    387       C  
ATOM   5748  CG  LYS A 811     -12.302  13.653 -17.416  1.00 69.13           C  
ANISOU 5748  CG  LYS A 811    11505   5808   8952   -516   2952    427       C  
ATOM   5749  CD  LYS A 811     -12.362  13.243 -18.876  1.00 66.22           C  
ANISOU 5749  CD  LYS A 811    11068   5431   8663   -652   2900    285       C  
ATOM   5750  CE  LYS A 811     -11.047  12.636 -19.323  1.00102.86           C  
ANISOU 5750  CE  LYS A 811    15828  10046  13208   -526   2891    355       C  
ATOM   5751  NZ  LYS A 811     -10.914  12.622 -20.804  1.00130.19           N1+
ANISOU 5751  NZ  LYS A 811    19194  13565  16709   -630   2764    227       N1+
ATOM   5752  N   GLU A 812     -15.303  12.774 -13.962  1.00 86.78           N  
ANISOU 5752  N   GLU A 812    13922   7652  11399   -616   3602    511       N  
ATOM   5753  CA  GLU A 812     -16.584  12.417 -13.377  1.00118.08           C  
ANISOU 5753  CA  GLU A 812    17888  11479  15500   -742   3812    459       C  
ATOM   5754  C   GLU A 812     -17.030  13.512 -12.418  1.00 96.39           C  
ANISOU 5754  C   GLU A 812    15068   8846  12709   -695   3733    513       C  
ATOM   5755  O   GLU A 812     -18.202  13.878 -12.381  1.00 79.57           O  
ANISOU 5755  O   GLU A 812    12811   6722  10701   -846   3753    412       O  
ATOM   5756  CB  GLU A 812     -16.485  11.076 -12.650  1.00147.81           C  
ANISOU 5756  CB  GLU A 812    21887  14997  19277   -676   4129    549       C  
ATOM   5757  CG  GLU A 812     -17.809  10.560 -12.135  1.00172.68           C  
ANISOU 5757  CG  GLU A 812    25047  17975  22590   -822   4380    483       C  
ATOM   5758  CD  GLU A 812     -18.796  10.311 -13.250  1.00196.09           C  
ANISOU 5758  CD  GLU A 812    27851  20906  25748  -1081   4386    265       C  
ATOM   5759  OE1 GLU A 812     -18.374  10.276 -14.424  1.00189.06           O  
ANISOU 5759  OE1 GLU A 812    26886  20087  24861  -1134   4240    176       O  
ATOM   5760  OE2 GLU A 812     -19.995  10.146 -12.950  1.00218.52           O1-
ANISOU 5760  OE2 GLU A 812    30638  23653  28737  -1230   4540    176       O1-
ATOM   5761  N   LYS A 813     -16.079  14.032 -11.647  1.00 84.76           N  
ANISOU 5761  N   LYS A 813    13672   7469  11063   -483   3643    668       N  
ATOM   5762  CA  LYS A 813     -16.346  15.121 -10.713  1.00 72.66           C  
ANISOU 5762  CA  LYS A 813    12079   6060   9468   -416   3553    728       C  
ATOM   5763  C   LYS A 813     -16.658  16.420 -11.454  1.00 77.40           C  
ANISOU 5763  C   LYS A 813    12445   6871  10094   -516   3279    621       C  
ATOM   5764  O   LYS A 813     -17.340  17.296 -10.923  1.00 59.23           O  
ANISOU 5764  O   LYS A 813    10045   4650   7808   -544   3224    611       O  
ATOM   5765  CB  LYS A 813     -15.169  15.326  -9.759  1.00 90.15           C  
ANISOU 5765  CB  LYS A 813    14433   8334  11485   -158   3515    907       C  
ATOM   5766  CG  LYS A 813     -14.963  14.197  -8.762  1.00120.83           C  
ANISOU 5766  CG  LYS A 813    18560  12025  15324    -26   3792   1035       C  
ATOM   5767  CD  LYS A 813     -13.766  14.473  -7.863  1.00137.04           C  
ANISOU 5767  CD  LYS A 813    20733  14167  17167    243   3726   1201       C  
ATOM   5768  CE  LYS A 813     -13.444  13.280  -6.979  1.00139.88           C  
ANISOU 5768  CE  LYS A 813    21347  14337  17465    397   3997   1334       C  
ATOM   5769  NZ  LYS A 813     -14.604  12.880  -6.144  1.00117.84           N1+
ANISOU 5769  NZ  LYS A 813    18625  11381  14767    329   4248   1343       N1+
ATOM   5770  N   LEU A 814     -16.154  16.550 -12.677  1.00 62.28           N  
ANISOU 5770  N   LEU A 814    10444   5041   8178   -561   3113    546       N  
ATOM   5771  CA  LEU A 814     -16.507  17.693 -13.511  1.00 81.71           C  
ANISOU 5771  CA  LEU A 814    12688   7686  10672   -663   2871    436       C  
ATOM   5772  C   LEU A 814     -17.922  17.526 -14.043  1.00 89.52           C  
ANISOU 5772  C   LEU A 814    13550   8622  11843   -887   2939    271       C  
ATOM   5773  O   LEU A 814     -18.799  18.338 -13.755  1.00 69.09           O  
ANISOU 5773  O   LEU A 814    10837   6110   9305   -955   2885    225       O  
ATOM   5774  CB  LEU A 814     -15.517  17.863 -14.664  1.00 62.24           C  
ANISOU 5774  CB  LEU A 814    10180   5325   8145   -634   2683    409       C  
ATOM   5775  CG  LEU A 814     -14.104  18.255 -14.238  1.00 67.25           C  
ANISOU 5775  CG  LEU A 814    10897   6054   8603   -420   2572    552       C  
ATOM   5776  CD1 LEU A 814     -13.226  18.491 -15.452  1.00 51.25           C  
ANISOU 5776  CD1 LEU A 814     8807   4131   6532   -412   2387    511       C  
ATOM   5777  CD2 LEU A 814     -14.147  19.488 -13.342  1.00 55.89           C  
ANISOU 5777  CD2 LEU A 814     9393   4755   7089   -337   2454    616       C  
ATOM   5778  N   GLN A 815     -18.139  16.465 -14.815  1.00109.76           N  
ANISOU 5778  N   GLN A 815    16143  11055  14506   -999   3058    176       N  
ATOM   5779  CA  GLN A 815     -19.467  16.146 -15.321  1.00105.87           C  
ANISOU 5779  CA  GLN A 815    15534  10497  14195  -1215   3145      4       C  
ATOM   5780  C   GLN A 815     -20.491  16.276 -14.206  1.00 93.65           C  
ANISOU 5780  C   GLN A 815    13984   8883  12717  -1254   3295     21       C  
ATOM   5781  O   GLN A 815     -21.617  16.726 -14.424  1.00 81.41           O  
ANISOU 5781  O   GLN A 815    12271   7380  11282  -1401   3265   -105       O  
ATOM   5782  CB  GLN A 815     -19.500  14.725 -15.883  1.00 85.83           C  
ANISOU 5782  CB  GLN A 815    13091   7769  11751  -1302   3338    -67       C  
ATOM   5783  CG  GLN A 815     -20.863  14.311 -16.411  1.00 88.77           C  
ANISOU 5783  CG  GLN A 815    13340   8067  12320  -1533   3440   -262       C  
ATOM   5784  CD  GLN A 815     -21.340  15.197 -17.547  1.00 97.13           C  
ANISOU 5784  CD  GLN A 815    14167   9318  13419  -1646   3194   -419       C  
ATOM   5785  NE2 GLN A 815     -22.620  15.542 -17.529  1.00 78.46           N  
ANISOU 5785  NE2 GLN A 815    11649   6980  11182  -1793   3207   -546       N  
ATOM   5786  OE1 GLN A 815     -20.565  15.563 -18.432  1.00112.49           O  
ANISOU 5786  OE1 GLN A 815    16075  11386  15280  -1597   2997   -425       O  
ATOM   5787  N   TRP A 816     -20.084  15.880 -13.005  1.00 87.21           N  
ANISOU 5787  N   TRP A 816    13351   7960  11825  -1112   3459    178       N  
ATOM   5788  CA  TRP A 816     -20.960  15.905 -11.844  1.00 99.56           C  
ANISOU 5788  CA  TRP A 816    14947   9441  13442  -1126   3630    215       C  
ATOM   5789  C   TRP A 816     -21.352  17.331 -11.488  1.00103.19           C  
ANISOU 5789  C   TRP A 816    15255  10089  13864  -1112   3439    219       C  
ATOM   5790  O   TRP A 816     -22.524  17.621 -11.269  1.00 95.44           O  
ANISOU 5790  O   TRP A 816    14164   9101  12997  -1237   3490    135       O  
ATOM   5791  CB  TRP A 816     -20.281  15.231 -10.656  1.00125.38           C  
ANISOU 5791  CB  TRP A 816    18458  12574  16605   -942   3825    399       C  
ATOM   5792  CG  TRP A 816     -21.202  14.970  -9.516  1.00136.26           C  
ANISOU 5792  CG  TRP A 816    19902  13818  18051   -964   4059    435       C  
ATOM   5793  CD1 TRP A 816     -22.007  13.883  -9.346  1.00143.78           C  
ANISOU 5793  CD1 TRP A 816    20929  14550  19152  -1081   4347    380       C  
ATOM   5794  CD2 TRP A 816     -21.417  15.812  -8.381  1.00130.51           C  
ANISOU 5794  CD2 TRP A 816    19174  13163  17249   -866   4035    531       C  
ATOM   5795  CE2 TRP A 816     -22.366  15.170  -7.561  1.00129.76           C  
ANISOU 5795  CE2 TRP A 816    19159  12884  17260   -927   4318    535       C  
ATOM   5796  CE3 TRP A 816     -20.899  17.044  -7.977  1.00115.98           C  
ANISOU 5796  CE3 TRP A 816    17276  11524  15267   -735   3809    609       C  
ATOM   5797  NE1 TRP A 816     -22.711  13.995  -8.173  1.00136.10           N  
ANISOU 5797  NE1 TRP A 816    20005  13506  18201  -1061   4508    441       N  
ATOM   5798  CZ2 TRP A 816     -22.809  15.721  -6.361  1.00114.44           C  
ANISOU 5798  CZ2 TRP A 816    17244  10956  15280   -856   4376    619       C  
ATOM   5799  CZ3 TRP A 816     -21.339  17.589  -6.786  1.00120.52           C  
ANISOU 5799  CZ3 TRP A 816    17874  12114  15805   -668   3863    687       C  
ATOM   5800  CH2 TRP A 816     -22.285  16.928  -5.992  1.00104.27           C  
ANISOU 5800  CH2 TRP A 816    15898   9873  13847   -725   4142    694       C  
ATOM   5801  N   LEU A 817     -20.368  18.221 -11.431  1.00105.41           N  
ANISOU 5801  N   LEU A 817    15527  10536  13987   -962   3224    312       N  
ATOM   5802  CA  LEU A 817     -20.643  19.631 -11.191  1.00 92.73           C  
ANISOU 5802  CA  LEU A 817    13776   9117  12341   -946   3028    311       C  
ATOM   5803  C   LEU A 817     -21.612  20.177 -12.235  1.00 89.62           C  
ANISOU 5803  C   LEU A 817    13160   8818  12074  -1134   2900    132       C  
ATOM   5804  O   LEU A 817     -22.427  21.047 -11.937  1.00 79.97           O  
ANISOU 5804  O   LEU A 817    11812   7682  10892  -1185   2838     94       O  
ATOM   5805  CB  LEU A 817     -19.349  20.447 -11.200  1.00102.55           C  
ANISOU 5805  CB  LEU A 817    15033  10523  13409   -772   2810    413       C  
ATOM   5806  CG  LEU A 817     -18.441  20.353  -9.973  1.00104.96           C  
ANISOU 5806  CG  LEU A 817    15516  10804  13561   -558   2874    592       C  
ATOM   5807  CD1 LEU A 817     -17.133  21.090 -10.222  1.00104.72           C  
ANISOU 5807  CD1 LEU A 817    15472  10938  13378   -412   2648    658       C  
ATOM   5808  CD2 LEU A 817     -19.148  20.903  -8.745  1.00100.72           C  
ANISOU 5808  CD2 LEU A 817    14979  10271  13020   -528   2943    644       C  
ATOM   5809  N   LEU A 818     -21.523  19.662 -13.459  1.00 89.97           N  
ANISOU 5809  N   LEU A 818    13157   8849  12177  -1230   2861     22       N  
ATOM   5810  CA  LEU A 818     -22.372  20.120 -14.559  1.00 80.08           C  
ANISOU 5810  CA  LEU A 818    11696   7698  11032  -1395   2729   -156       C  
ATOM   5811  C   LEU A 818     -23.854  19.853 -14.314  1.00 91.11           C  
ANISOU 5811  C   LEU A 818    13006   9013  12600  -1562   2881   -275       C  
ATOM   5812  O   LEU A 818     -24.672  20.773 -14.349  1.00120.11           O  
ANISOU 5812  O   LEU A 818    16516  12804  16317  -1626   2774   -345       O  
ATOM   5813  CB  LEU A 818     -21.939  19.475 -15.877  1.00 78.07           C  
ANISOU 5813  CB  LEU A 818    11432   7431  10801  -1455   2679   -249       C  
ATOM   5814  CG  LEU A 818     -20.724  20.094 -16.566  1.00 74.64           C  
ANISOU 5814  CG  LEU A 818    10991   7144  10226  -1338   2450   -193       C  
ATOM   5815  CD1 LEU A 818     -20.199  19.184 -17.662  1.00 91.36           C  
ANISOU 5815  CD1 LEU A 818    13151   9201  12360  -1378   2462   -259       C  
ATOM   5816  CD2 LEU A 818     -21.065  21.470 -17.123  1.00 74.22           C  
ANISOU 5816  CD2 LEU A 818    10744   7299  10156  -1365   2205   -257       C  
ATOM   5817  N   ASP A 819     -24.194  18.592 -14.076  1.00 69.41           N  
ANISOU 5817  N   ASP A 819    10365   6059   9950  -1632   3137   -302       N  
ATOM   5818  CA  ASP A 819     -25.581  18.199 -13.845  1.00 94.62           C  
ANISOU 5818  CA  ASP A 819    13480   9149  13320  -1801   3313   -425       C  
ATOM   5819  C   ASP A 819     -26.164  18.862 -12.601  1.00108.52           C  
ANISOU 5819  C   ASP A 819    15236  10922  15074  -1758   3370   -345       C  
ATOM   5820  O   ASP A 819     -27.278  19.382 -12.633  1.00125.46           O  
ANISOU 5820  O   ASP A 819    17219  13127  17325  -1876   3346   -455       O  
ATOM   5821  CB  ASP A 819     -25.698  16.678 -13.716  1.00 95.60           C  
ANISOU 5821  CB  ASP A 819    13751   9028  13545  -1867   3605   -447       C  
ATOM   5822  CG  ASP A 819     -25.225  15.948 -14.957  1.00116.51           C  
ANISOU 5822  CG  ASP A 819    16401  11651  16217  -1926   3568   -544       C  
ATOM   5823  OD1 ASP A 819     -25.188  16.568 -16.040  1.00152.03           O  
ANISOU 5823  OD1 ASP A 819    20745  16318  20703  -1970   3334   -646       O  
ATOM   5824  OD2 ASP A 819     -24.893  14.748 -14.852  1.00 86.55           O1-
ANISOU 5824  OD2 ASP A 819    12769   7665  12451  -1924   3779   -516       O1-
ATOM   5825  N   GLU A 820     -25.407  18.842 -11.509  1.00 99.88           N  
ANISOU 5825  N   GLU A 820    14320   9778  13852  -1583   3444   -156       N  
ATOM   5826  CA  GLU A 820     -25.906  19.317 -10.222  1.00 99.27           C  
ANISOU 5826  CA  GLU A 820    14272   9686  13759  -1529   3533    -67       C  
ATOM   5827  C   GLU A 820     -26.201  20.817 -10.226  1.00108.94           C  
ANISOU 5827  C   GLU A 820    15324  11128  14941  -1515   3292    -83       C  
ATOM   5828  O   GLU A 820     -27.139  21.271  -9.569  1.00122.14           O  
ANISOU 5828  O   GLU A 820    16926  12806  16675  -1563   3348   -102       O  
ATOM   5829  CB  GLU A 820     -24.926  18.970  -9.096  1.00 96.06           C  
ANISOU 5829  CB  GLU A 820    14100   9194  13203  -1323   3646    139       C  
ATOM   5830  CG  GLU A 820     -24.364  17.552  -9.158  1.00130.51           C  
ANISOU 5830  CG  GLU A 820    18656  13361  17573  -1295   3855    180       C  
ATOM   5831  CD  GLU A 820     -25.437  16.480  -9.125  1.00139.85           C  
ANISOU 5831  CD  GLU A 820    19856  14333  18947  -1465   4137     76       C  
ATOM   5832  OE1 GLU A 820     -26.491  16.711  -8.497  1.00148.75           O  
ANISOU 5832  OE1 GLU A 820    20923  15425  20169  -1543   4244     40       O  
ATOM   5833  OE2 GLU A 820     -25.221  15.401  -9.721  1.00120.73           O1-
ANISOU 5833  OE2 GLU A 820    17510  11777  16586  -1522   4259     26       O1-
ATOM   5834  N   SER A 821     -25.404  21.583 -10.964  1.00110.28           N  
ANISOU 5834  N   SER A 821    15427  11469  15004  -1449   3034    -75       N  
ATOM   5835  CA  SER A 821     -25.619  23.027 -11.063  1.00110.18           C  
ANISOU 5835  CA  SER A 821    15253  11661  14948  -1432   2803    -90       C  
ATOM   5836  C   SER A 821     -26.743  23.330 -12.044  1.00108.73           C  
ANISOU 5836  C   SER A 821    14853  11553  14907  -1614   2722   -282       C  
ATOM   5837  O   SER A 821     -27.057  24.487 -12.313  1.00 73.70           O  
ANISOU 5837  O   SER A 821    10265   7284  10452  -1619   2532   -320       O  
ATOM   5838  CB  SER A 821     -24.335  23.746 -11.481  1.00 88.58           C  
ANISOU 5838  CB  SER A 821    12531   9074  12051  -1292   2572    -10       C  
ATOM   5839  OG  SER A 821     -23.882  23.298 -12.747  1.00 86.55           O  
ANISOU 5839  OG  SER A 821    12247   8830  11807  -1341   2492    -89       O  
ATOM   5840  N   PHE A 822     -27.338  22.271 -12.576  1.00116.65           N  
ANISOU 5840  N   PHE A 822    15843  12430  16050  -1758   2870   -407       N  
ATOM   5841  CA  PHE A 822     -28.485  22.384 -13.461  1.00131.30           C  
ANISOU 5841  CA  PHE A 822    17494  14342  18053  -1938   2822   -609       C  
ATOM   5842  C   PHE A 822     -29.722  22.020 -12.648  1.00143.47           C  
ANISOU 5842  C   PHE A 822    19009  15763  19741  -2047   3044   -663       C  
ATOM   5843  O   PHE A 822     -30.830  22.470 -12.939  1.00138.57           O  
ANISOU 5843  O   PHE A 822    18202  15217  19230  -2168   3000   -801       O  
ATOM   5844  CB  PHE A 822     -28.321  21.424 -14.638  1.00130.45           C  
ANISOU 5844  CB  PHE A 822    17378  14176  18009  -2034   2840   -732       C  
ATOM   5845  CG  PHE A 822     -29.112  21.802 -15.853  1.00144.53           C  
ANISOU 5845  CG  PHE A 822    18939  16092  19882  -2170   2685   -932       C  
ATOM   5846  CD1 PHE A 822     -28.477  22.036 -17.061  1.00135.11           C  
ANISOU 5846  CD1 PHE A 822    17695  15019  18620  -2148   2482   -979       C  
ATOM   5847  CD2 PHE A 822     -30.489  21.920 -15.794  1.00166.94           C  
ANISOU 5847  CD2 PHE A 822    21619  18939  22870  -2313   2743  -1076       C  
ATOM   5848  CE1 PHE A 822     -29.200  22.378 -18.185  1.00135.49           C  
ANISOU 5848  CE1 PHE A 822    17545  15197  18739  -2258   2338  -1162       C  
ATOM   5849  CE2 PHE A 822     -31.217  22.265 -16.915  1.00166.86           C  
ANISOU 5849  CE2 PHE A 822    21401  19065  22935  -2425   2594  -1265       C  
ATOM   5850  CZ  PHE A 822     -30.571  22.494 -18.112  1.00148.51           C  
ANISOU 5850  CZ  PHE A 822    19034  16863  20532  -2393   2390  -1307       C  
ATOM   5851  N   LYS A 823     -29.512  21.203 -11.621  1.00141.08           N  
ANISOU 5851  N   LYS A 823    18895  15274  19434  -1996   3285   -550       N  
ATOM   5852  CA  LYS A 823     -30.578  20.802 -10.709  1.00126.94           C  
ANISOU 5852  CA  LYS A 823    17114  13345  17773  -2080   3528   -574       C  
ATOM   5853  C   LYS A 823     -31.016  21.972  -9.841  1.00148.69           C  
ANISOU 5853  C   LYS A 823    19803  16209  20481  -2019   3454   -507       C  
ATOM   5854  O   LYS A 823     -30.301  22.962  -9.709  1.00138.19           O  
ANISOU 5854  O   LYS A 823    18476  15029  19001  -1881   3254   -403       O  
ATOM   5855  CB  LYS A 823     -30.107  19.664  -9.800  0.00 99.89           C  
ANISOU 5855  CB  LYS A 823    13936   9691  14328  -2008   3807   -445       C  
ATOM   5856  CG  LYS A 823     -29.831  18.345 -10.498  0.00 96.94           C  
ANISOU 5856  CG  LYS A 823    13645   9163  14026  -2084   3946   -514       C  
ATOM   5857  CD  LYS A 823     -29.396  17.302  -9.479  0.00106.79           C  
ANISOU 5857  CD  LYS A 823    15148  10183  15245  -1992   4233   -368       C  
ATOM   5858  CE  LYS A 823     -29.239  15.926 -10.099  0.00110.24           C  
ANISOU 5858  CE  LYS A 823    15674  10439  15773  -2079   4411   -441       C  
ATOM   5859  NZ  LYS A 823     -28.871  14.911  -9.072  0.00112.42           N1+
ANISOU 5859  NZ  LYS A 823    16208  10484  16023  -1982   4709   -293       N1+
ATOM   5860  N   GLY A 824     -32.191  21.843  -9.236  1.00179.31           N  
ANISOU 5860  N   GLY A 824    23625  20008  24497  -2123   3626   -570       N  
ATOM   5861  CA  GLY A 824     -32.703  22.871  -8.353  1.00194.89           C  
ANISOU 5861  CA  GLY A 824    25542  22067  26442  -2074   3586   -511       C  
ATOM   5862  C   GLY A 824     -32.114  22.789  -6.960  1.00207.22           C  
ANISOU 5862  C   GLY A 824    27319  23534  27883  -1907   3724   -304       C  
ATOM   5863  O   GLY A 824     -31.843  23.807  -6.324  1.00221.86           O  
ANISOU 5863  O   GLY A 824    29175  25504  29616  -1784   3601   -199       O  
ATOM   5864  N   ASP A 825     -31.904  21.563  -6.496  1.00202.80           N  
ANISOU 5864  N   ASP A 825    26944  22761  27350  -1898   3983   -249       N  
ATOM   5865  CA  ASP A 825     -31.499  21.304  -5.119  1.00201.82           C  
ANISOU 5865  CA  ASP A 825    27036  22518  27127  -1745   4163    -62       C  
ATOM   5866  C   ASP A 825     -30.247  22.054  -4.674  1.00194.55           C  
ANISOU 5866  C   ASP A 825    26217  21724  25978  -1522   3980    110       C  
ATOM   5867  O   ASP A 825     -30.281  22.810  -3.703  1.00197.49           O  
ANISOU 5867  O   ASP A 825    26617  22156  26266  -1417   3958    210       O  
ATOM   5868  CB  ASP A 825     -31.295  19.802  -4.907  1.00210.28           C  
ANISOU 5868  CB  ASP A 825    28302  23345  28251  -1756   4453    -30       C  
ATOM   5869  CG  ASP A 825     -32.558  19.003  -5.152  1.00221.30           C  
ANISOU 5869  CG  ASP A 825    29615  24588  29882  -1975   4679   -197       C  
ATOM   5870  OD1 ASP A 825     -33.650  19.610  -5.185  1.00229.29           O  
ANISOU 5870  OD1 ASP A 825    30439  25671  31008  -2097   4645   -311       O  
ATOM   5871  OD2 ASP A 825     -32.462  17.769  -5.310  1.00221.81           O1-
ANISOU 5871  OD2 ASP A 825    29798  24460  30021  -2027   4895   -217       O1-
ATOM   5872  N   LYS A 826     -29.143  21.841  -5.381  1.00173.66           N  
ANISOU 5872  N   LYS A 826    23625  19122  23236  -1451   3853    139       N  
ATOM   5873  CA  LYS A 826     -27.841  22.302  -4.908  1.00159.70           C  
ANISOU 5873  CA  LYS A 826    21982  17441  21256  -1233   3723    305       C  
ATOM   5874  C   LYS A 826     -27.419  23.667  -5.450  1.00190.21           C  
ANISOU 5874  C   LYS A 826    25694  21547  25029  -1190   3399    289       C  
ATOM   5875  O   LYS A 826     -26.716  24.417  -4.772  1.00204.66           O  
ANISOU 5875  O   LYS A 826    27579  23475  26707  -1029   3291    410       O  
ATOM   5876  CB  LYS A 826     -26.780  21.241  -5.191  1.00119.95           C  
ANISOU 5876  CB  LYS A 826    17120  12299  16155  -1153   3798    370       C  
ATOM   5877  CG  LYS A 826     -27.071  19.933  -4.483  1.00110.14           C  
ANISOU 5877  CG  LYS A 826    16064  10809  14976  -1158   4135    418       C  
ATOM   5878  CD  LYS A 826     -26.072  18.848  -4.831  1.00130.07           C  
ANISOU 5878  CD  LYS A 826    18756  13220  17444  -1085   4217    474       C  
ATOM   5879  CE  LYS A 826     -26.367  17.580  -4.043  1.00123.44           C  
ANISOU 5879  CE  LYS A 826    18117  12123  16661  -1075   4570    536       C  
ATOM   5880  NZ  LYS A 826     -25.426  16.479  -4.373  1.00120.60           N1+
ANISOU 5880  NZ  LYS A 826    17930  11642  16251  -1002   4667    592       N1+
ATOM   5881  N   ILE A 827     -27.849  23.980  -6.667  1.00195.96           N  
ANISOU 5881  N   ILE A 827    26235  22369  25851  -1332   3250    137       N  
ATOM   5882  CA  ILE A 827     -27.631  25.298  -7.259  1.00186.51           C  
ANISOU 5882  CA  ILE A 827    24881  21394  24591  -1311   2959    106       C  
ATOM   5883  C   ILE A 827     -28.176  25.301  -8.684  1.00193.83           C  
ANISOU 5883  C   ILE A 827    25626  22385  25636  -1475   2847    -73       C  
ATOM   5884  O   ILE A 827     -28.157  24.273  -9.358  1.00224.06           O  
ANISOU 5884  O   ILE A 827    29485  26110  29539  -1557   2939   -146       O  
ATOM   5885  CB  ILE A 827     -26.146  25.712  -7.231  1.00190.59           C  
ANISOU 5885  CB  ILE A 827    25492  22006  24919  -1128   2797    232       C  
ATOM   5886  CG1 ILE A 827     -26.005  27.203  -7.544  1.00193.62           C  
ANISOU 5886  CG1 ILE A 827    25727  22604  25237  -1094   2530    219       C  
ATOM   5887  CG2 ILE A 827     -25.328  24.855  -8.183  1.00198.94           C  
ANISOU 5887  CG2 ILE A 827    26611  23016  25962  -1132   2783    210       C  
ATOM   5888  CD1 ILE A 827     -24.833  27.854  -6.853  1.00202.05           C  
ANISOU 5888  CD1 ILE A 827    26889  23756  26123   -899   2423    364       C  
ATOM   5889  N   LYS A 828     -28.665  26.451  -9.141  1.00160.60           N  
ANISOU 5889  N   LYS A 828    21232  18347  21441  -1516   2651   -147       N  
ATOM   5890  CA  LYS A 828     -29.467  26.485 -10.363  1.00149.09           C  
ANISOU 5890  CA  LYS A 828    19585  16952  20108  -1677   2567   -331       C  
ATOM   5891  C   LYS A 828     -29.018  27.467 -11.437  1.00137.53           C  
ANISOU 5891  C   LYS A 828    17997  15686  18574  -1649   2284   -371       C  
ATOM   5892  O   LYS A 828     -28.147  27.171 -12.252  1.00117.72           O  
ANISOU 5892  O   LYS A 828    15528  13195  16007  -1618   2197   -370       O  
ATOM   5893  CB  LYS A 828     -30.923  26.799 -10.022  1.00149.11           C  
ANISOU 5893  CB  LYS A 828    19448  16959  20249  -1798   2640   -430       C  
ATOM   5894  CG  LYS A 828     -31.647  25.698  -9.293  0.00141.32           C  
ANISOU 5894  CG  LYS A 828    18540  15767  19387  -1883   2936   -449       C  
ATOM   5895  CD  LYS A 828     -33.145  25.943  -9.313  0.00135.13           C  
ANISOU 5895  CD  LYS A 828    17574  15003  18768  -2036   2987   -596       C  
ATOM   5896  CE  LYS A 828     -33.677  25.961 -10.737  0.00130.58           C  
ANISOU 5896  CE  LYS A 828    16801  14526  18289  -2173   2852   -794       C  
ATOM   5897  NZ  LYS A 828     -35.157  26.109 -10.773  0.00129.26           N1+
ANISOU 5897  NZ  LYS A 828    16446  14377  18289  -2325   2909   -952       N1+
ATOM   5898  N   THR A 829     -29.659  28.630 -11.442  1.00174.75           N  
ANISOU 5898  N   THR A 829    22560  20541  23295  -1662   2150   -409       N  
ATOM   5899  CA  THR A 829     -29.506  29.600 -12.516  1.00204.20           C  
ANISOU 5899  CA  THR A 829    26149  24455  26982  -1655   1899   -469       C  
ATOM   5900  C   THR A 829     -28.373  30.576 -12.243  1.00199.24           C  
ANISOU 5900  C   THR A 829    25582  23931  26188  -1491   1740   -329       C  
ATOM   5901  O   THR A 829     -27.740  31.083 -13.169  1.00209.76           O  
ANISOU 5901  O   THR A 829    26870  25377  27454  -1453   1558   -342       O  
ATOM   5902  CB  THR A 829     -30.804  30.409 -12.710  1.00216.92           C  
ANISOU 5902  CB  THR A 829    27560  26174  28688  -1746   1832   -586       C  
ATOM   5903  CG2 THR A 829     -31.942  29.497 -13.120  1.00214.34           C  
ANISOU 5903  CG2 THR A 829    27142  25765  28535  -1918   1968   -753       C  
ATOM   5904  OG1 THR A 829     -31.150  31.059 -11.484  1.00220.80           O  
ANISOU 5904  OG1 THR A 829    28069  26665  29159  -1692   1886   -498       O  
ATOM   5905  N   GLN A 830     -28.119  30.829 -10.966  1.00179.01           N  
ANISOU 5905  N   GLN A 830    23124  21332  23561  -1394   1816   -201       N  
ATOM   5906  CA  GLN A 830     -27.189  31.875 -10.560  1.00165.91           C  
ANISOU 5906  CA  GLN A 830    21502  19781  21756  -1246   1671    -82       C  
ATOM   5907  C   GLN A 830     -25.727  31.564 -10.867  1.00174.87           C  
ANISOU 5907  C   GLN A 830    22758  20912  22772  -1138   1610     -1       C  
ATOM   5908  O   GLN A 830     -24.888  32.465 -10.849  1.00190.01           O  
ANISOU 5908  O   GLN A 830    24679  22939  24578  -1031   1459     68       O  
ATOM   5909  CB  GLN A 830     -27.341  32.161  -9.067  1.00151.34           C  
ANISOU 5909  CB  GLN A 830    19737  17894  19873  -1169   1778     23       C  
ATOM   5910  CG  GLN A 830     -26.968  30.986  -8.182  1.00165.80           C  
ANISOU 5910  CG  GLN A 830    21757  19554  21684  -1121   1992    111       C  
ATOM   5911  CD  GLN A 830     -26.889  31.364  -6.718  1.00162.08           C  
ANISOU 5911  CD  GLN A 830    21382  19064  21138  -1009   2070    232       C  
ATOM   5912  NE2 GLN A 830     -26.477  30.416  -5.884  1.00159.77           N  
ANISOU 5912  NE2 GLN A 830    21269  18632  20804   -937   2251    324       N  
ATOM   5913  OE1 GLN A 830     -27.192  32.495  -6.340  1.00148.20           O  
ANISOU 5913  OE1 GLN A 830    19541  17413  19353   -981   1972    242       O  
ATOM   5914  N   GLU A 831     -25.411  30.303 -11.145  1.00154.04           N  
ANISOU 5914  N   GLU A 831    20219  18148  20161  -1167   1731    -11       N  
ATOM   5915  CA  GLU A 831     -24.006  29.928 -11.292  1.00141.97           C  
ANISOU 5915  CA  GLU A 831    18820  16604  18516  -1053   1695     78       C  
ATOM   5916  C   GLU A 831     -23.662  29.037 -12.486  1.00135.32           C  
ANISOU 5916  C   GLU A 831    17987  15718  17709  -1115   1690      5       C  
ATOM   5917  O   GLU A 831     -22.565  29.138 -13.034  1.00168.16           O  
ANISOU 5917  O   GLU A 831    22186  19930  21778  -1037   1576     44       O  
ATOM   5918  CB  GLU A 831     -23.484  29.293 -10.004  1.00142.87           C  
ANISOU 5918  CB  GLU A 831    19120  16601  18562   -942   1861    210       C  
ATOM   5919  CG  GLU A 831     -22.030  28.875 -10.093  1.00166.90           C  
ANISOU 5919  CG  GLU A 831    22298  19633  21484   -813   1829    302       C  
ATOM   5920  CD  GLU A 831     -21.421  28.592  -8.741  1.00173.50           C  
ANISOU 5920  CD  GLU A 831    23302  20404  22217   -663   1943    443       C  
ATOM   5921  OE1 GLU A 831     -22.112  28.809  -7.724  1.00172.65           O  
ANISOU 5921  OE1 GLU A 831    23207  20265  22126   -657   2039    474       O  
ATOM   5922  OE2 GLU A 831     -20.251  28.159  -8.696  1.00171.20           O1-
ANISOU 5922  OE2 GLU A 831    23129  20096  21823   -546   1936    521       O1-
ATOM   5923  N   PHE A 832     -24.584  28.169 -12.883  1.00 95.97           N  
ANISOU 5923  N   PHE A 832    12967  10638  12860  -1256   1815   -107       N  
ATOM   5924  CA  PHE A 832     -24.315  27.212 -13.956  1.00 96.27           C  
ANISOU 5924  CA  PHE A 832    13023  10617  12939  -1322   1834   -185       C  
ATOM   5925  C   PHE A 832     -23.531  27.799 -15.136  1.00123.88           C  
ANISOU 5925  C   PHE A 832    16456  14251  16361  -1285   1613   -208       C  
ATOM   5926  O   PHE A 832     -22.530  27.222 -15.560  1.00136.59           O  
ANISOU 5926  O   PHE A 832    18164  15825  17911  -1230   1607   -169       O  
ATOM   5927  CB  PHE A 832     -25.610  26.564 -14.453  1.00 79.36           C  
ANISOU 5927  CB  PHE A 832    10780   8408  10966  -1503   1940   -347       C  
ATOM   5928  CG  PHE A 832     -25.411  25.603 -15.591  1.00 90.00           C  
ANISOU 5928  CG  PHE A 832    12134   9701  12362  -1581   1956   -446       C  
ATOM   5929  CD1 PHE A 832     -24.975  24.307 -15.354  1.00 97.35           C  
ANISOU 5929  CD1 PHE A 832    13225  10456  13309  -1578   2145   -409       C  
ATOM   5930  CD2 PHE A 832     -25.666  25.993 -16.898  1.00 81.89           C  
ANISOU 5930  CD2 PHE A 832    10956   8797  11361  -1651   1787   -576       C  
ATOM   5931  CE1 PHE A 832     -24.792  23.419 -16.399  1.00 96.68           C  
ANISOU 5931  CE1 PHE A 832    13147  10316  13270  -1652   2164   -504       C  
ATOM   5932  CE2 PHE A 832     -25.487  25.110 -17.947  1.00 70.97           C  
ANISOU 5932  CE2 PHE A 832     9579   7367  10019  -1721   1800   -672       C  
ATOM   5933  CZ  PHE A 832     -25.048  23.822 -17.698  1.00 90.59           C  
ANISOU 5933  CZ  PHE A 832    12221   9673  12524  -1726   1989   -639       C  
ATOM   5934  N   PRO A 833     -23.984  28.948 -15.666  1.00128.22           N  
ANISOU 5934  N   PRO A 833    16848  14957  16914  -1309   1438   -268       N  
ATOM   5935  CA  PRO A 833     -23.353  29.596 -16.825  1.00119.68           C  
ANISOU 5935  CA  PRO A 833    15698  14008  15766  -1276   1233   -295       C  
ATOM   5936  C   PRO A 833     -21.857  29.839 -16.650  1.00104.90           C  
ANISOU 5936  C   PRO A 833    13941  12162  13754  -1126   1161   -163       C  
ATOM   5937  O   PRO A 833     -21.113  29.824 -17.630  1.00 89.44           O  
ANISOU 5937  O   PRO A 833    11984  10251  11749  -1102   1057   -178       O  
ATOM   5938  CB  PRO A 833     -24.080  30.945 -16.911  1.00 90.65           C  
ANISOU 5938  CB  PRO A 833    11865  10480  12097  -1288   1093   -334       C  
ATOM   5939  CG  PRO A 833     -24.825  31.087 -15.614  1.00107.76           C  
ANISOU 5939  CG  PRO A 833    14041  12596  14307  -1296   1215   -294       C  
ATOM   5940  CD  PRO A 833     -25.167  29.698 -15.215  1.00121.65           C  
ANISOU 5940  CD  PRO A 833    15891  14180  16149  -1368   1434   -316       C  
ATOM   5941  N   GLN A 834     -21.428  30.075 -15.417  1.00 86.92           N  
ANISOU 5941  N   GLN A 834    11756   9861  11410  -1024   1216    -40       N  
ATOM   5942  CA  GLN A 834     -20.035  30.398 -15.149  1.00 90.22           C  
ANISOU 5942  CA  GLN A 834    12266  10318  11695   -877   1141     78       C  
ATOM   5943  C   GLN A 834     -19.195  29.149 -14.928  1.00 95.60           C  
ANISOU 5943  C   GLN A 834    13113  10871  12341   -822   1270    141       C  
ATOM   5944  O   GLN A 834     -18.021  29.108 -15.292  1.00102.12           O  
ANISOU 5944  O   GLN A 834    13996  11725  13079   -734   1197    192       O  
ATOM   5945  CB  GLN A 834     -19.937  31.349 -13.957  1.00113.21           C  
ANISOU 5945  CB  GLN A 834    15186  13287  14542   -783   1117    170       C  
ATOM   5946  CG  GLN A 834     -20.603  32.688 -14.224  1.00144.49           C  
ANISOU 5946  CG  GLN A 834    18991  17385  18525   -818    976    119       C  
ATOM   5947  CD  GLN A 834     -20.607  33.602 -13.019  1.00158.05           C  
ANISOU 5947  CD  GLN A 834    20714  19150  20189   -737    965    200       C  
ATOM   5948  NE2 GLN A 834     -20.643  34.905 -13.267  1.00152.87           N  
ANISOU 5948  NE2 GLN A 834    19951  18625  19507   -718    813    189       N  
ATOM   5949  OE1 GLN A 834     -20.587  33.143 -11.877  1.00160.92           O  
ANISOU 5949  OE1 GLN A 834    21180  19431  20531   -687   1097    271       O  
ATOM   5950  N   ILE A 835     -19.805  28.128 -14.338  1.00 96.65           N  
ANISOU 5950  N   ILE A 835    13321  10858  12543   -873   1468    136       N  
ATOM   5951  CA  ILE A 835     -19.144  26.843 -14.170  1.00 81.62           C  
ANISOU 5951  CA  ILE A 835    11580   8813  10618   -830   1615    188       C  
ATOM   5952  C   ILE A 835     -18.853  26.239 -15.536  1.00 78.54           C  
ANISOU 5952  C   ILE A 835    11170   8411  10261   -897   1571    103       C  
ATOM   5953  O   ILE A 835     -17.723  25.845 -15.823  1.00 90.43           O  
ANISOU 5953  O   ILE A 835    12767   9904  11688   -810   1548    160       O  
ATOM   5954  CB  ILE A 835     -20.015  25.865 -13.370  1.00 84.65           C  
ANISOU 5954  CB  ILE A 835    12041   9031  11091   -892   1854    184       C  
ATOM   5955  CG1 ILE A 835     -20.488  26.523 -12.069  1.00 87.67           C  
ANISOU 5955  CG1 ILE A 835    12427   9431  11452   -840   1897    254       C  
ATOM   5956  CG2 ILE A 835     -19.254  24.577 -13.095  1.00 73.83           C  
ANISOU 5956  CG2 ILE A 835    10858   7510   9685   -823   2015    258       C  
ATOM   5957  CD1 ILE A 835     -21.458  25.677 -11.267  1.00 73.74           C  
ANISOU 5957  CD1 ILE A 835    10728   7507   9785   -908   2137    246       C  
ATOM   5958  N   LEU A 836     -19.882  26.180 -16.377  1.00 77.94           N  
ANISOU 5958  N   LEU A 836    10969   8345  10300  -1048   1557    -38       N  
ATOM   5959  CA  LEU A 836     -19.766  25.603 -17.711  1.00 78.13           C  
ANISOU 5959  CA  LEU A 836    10961   8360  10363  -1124   1517   -140       C  
ATOM   5960  C   LEU A 836     -18.537  26.114 -18.449  1.00 79.95           C  
ANISOU 5960  C   LEU A 836    11198   8697  10480  -1025   1342    -95       C  
ATOM   5961  O   LEU A 836     -17.792  25.334 -19.041  1.00 89.87           O  
ANISOU 5961  O   LEU A 836    12534   9898  11713  -1006   1365    -92       O  
ATOM   5962  CB  LEU A 836     -21.011  25.909 -18.542  1.00 85.24           C  
ANISOU 5962  CB  LEU A 836    11686   9324  11376  -1275   1457   -303       C  
ATOM   5963  CG  LEU A 836     -20.961  25.395 -19.983  1.00 81.49           C  
ANISOU 5963  CG  LEU A 836    11164   8862  10937  -1353   1398   -425       C  
ATOM   5964  CD1 LEU A 836     -21.176  23.895 -20.004  1.00 46.42           C  
ANISOU 5964  CD1 LEU A 836     6815   4239   6583  -1436   1603   -476       C  
ATOM   5965  CD2 LEU A 836     -21.991  26.095 -20.854  1.00 84.69           C  
ANISOU 5965  CD2 LEU A 836    11377   9393  11408  -1456   1269   -570       C  
ATOM   5966  N   THR A 837     -18.333  27.428 -18.417  1.00 70.63           N  
ANISOU 5966  N   THR A 837     9933   7666   9236   -965   1176    -62       N  
ATOM   5967  CA  THR A 837     -17.210  28.043 -19.115  1.00 72.41           C  
ANISOU 5967  CA  THR A 837    10152   7997   9363   -876   1011    -24       C  
ATOM   5968  C   THR A 837     -15.890  27.724 -18.422  1.00 71.26           C  
ANISOU 5968  C   THR A 837    10153   7810   9112   -731   1050    110       C  
ATOM   5969  O   THR A 837     -14.874  27.505 -19.081  1.00 78.13           O  
ANISOU 5969  O   THR A 837    11067   8694   9923   -676    993    130       O  
ATOM   5970  CB  THR A 837     -17.375  29.569 -19.225  1.00 80.99           C  
ANISOU 5970  CB  THR A 837    11111   9245  10416   -852    839    -26       C  
ATOM   5971  CG2 THR A 837     -18.734  29.916 -19.810  1.00 72.32           C  
ANISOU 5971  CG2 THR A 837     9866   8196   9416   -979    802   -154       C  
ATOM   5972  OG1 THR A 837     -17.247  30.163 -17.929  1.00 82.14           O  
ANISOU 5972  OG1 THR A 837    11289   9405  10514   -769    861     73       O  
ATOM   5973  N   LEU A 838     -15.914  27.696 -17.092  1.00 40.42           N  
ANISOU 5973  N   LEU A 838     6321   3857   5179   -665   1148    198       N  
ATOM   5974  CA  LEU A 838     -14.734  27.336 -16.312  1.00 47.69           C  
ANISOU 5974  CA  LEU A 838     7385   4741   5996   -516   1195    323       C  
ATOM   5975  C   LEU A 838     -14.249  25.927 -16.633  1.00 70.62           C  
ANISOU 5975  C   LEU A 838    10416   7510   8905   -511   1323    331       C  
ATOM   5976  O   LEU A 838     -13.048  25.686 -16.725  1.00 73.35           O  
ANISOU 5976  O   LEU A 838    10844   7864   9163   -400   1294    398       O  
ATOM   5977  CB  LEU A 838     -15.015  27.454 -14.818  1.00 62.87           C  
ANISOU 5977  CB  LEU A 838     9367   6628   7892   -450   1295    405       C  
ATOM   5978  CG  LEU A 838     -15.045  28.871 -14.256  1.00 59.83           C  
ANISOU 5978  CG  LEU A 838     8894   6380   7458   -399   1166    435       C  
ATOM   5979  CD1 LEU A 838     -15.054  28.835 -12.736  1.00 59.69           C  
ANISOU 5979  CD1 LEU A 838     8969   6323   7389   -302   1271    532       C  
ATOM   5980  CD2 LEU A 838     -13.849  29.649 -14.768  1.00 55.10           C  
ANISOU 5980  CD2 LEU A 838     8262   5906   6768   -309    992    462       C  
ATOM   5981  N   ILE A 839     -15.185  24.998 -16.788  1.00 56.94           N  
ANISOU 5981  N   ILE A 839     8701   5654   7281   -630   1470    259       N  
ATOM   5982  CA  ILE A 839     -14.839  23.636 -17.162  1.00 61.17           C  
ANISOU 5982  CA  ILE A 839     9354   6050   7838   -643   1604    253       C  
ATOM   5983  C   ILE A 839     -14.470  23.582 -18.639  1.00 65.71           C  
ANISOU 5983  C   ILE A 839     9867   6676   8422   -696   1486    168       C  
ATOM   5984  O   ILE A 839     -13.612  22.801 -19.045  1.00 75.47           O  
ANISOU 5984  O   ILE A 839    11202   7853   9622   -647   1522    195       O  
ATOM   5985  CB  ILE A 839     -15.985  22.654 -16.868  1.00 72.22           C  
ANISOU 5985  CB  ILE A 839    10788   7291   9363   -764   1812    191       C  
ATOM   5986  CG1 ILE A 839     -16.268  22.613 -15.364  1.00 60.39           C  
ANISOU 5986  CG1 ILE A 839     9376   5727   7844   -695   1951    290       C  
ATOM   5987  CG2 ILE A 839     -15.639  21.267 -17.382  1.00 53.32           C  
ANISOU 5987  CG2 ILE A 839     8510   4750   7000   -789   1950    170       C  
ATOM   5988  CD1 ILE A 839     -17.444  21.737 -14.975  1.00 67.33           C  
ANISOU 5988  CD1 ILE A 839    10284   6445   8852   -815   2170    233       C  
ATOM   5989  N   GLY A 840     -15.115  24.435 -19.429  1.00 60.97           N  
ANISOU 5989  N   GLY A 840     9108   6191   7868   -787   1345     68       N  
ATOM   5990  CA  GLY A 840     -14.851  24.524 -20.852  1.00 44.90           C  
ANISOU 5990  CA  GLY A 840     7004   4222   5835   -832   1220    -16       C  
ATOM   5991  C   GLY A 840     -13.447  25.013 -21.144  1.00 70.88           C  
ANISOU 5991  C   GLY A 840    10329   7598   9006   -700   1092     67       C  
ATOM   5992  O   GLY A 840     -13.021  25.062 -22.299  1.00 58.40           O  
ANISOU 5992  O   GLY A 840     8712   6067   7409   -714    994     17       O  
ATOM   5993  N   ARG A 841     -12.727  25.372 -20.086  1.00 73.91           N  
ANISOU 5993  N   ARG A 841    10778   7999   9303   -570   1096    190       N  
ATOM   5994  CA  ARG A 841     -11.366  25.872 -20.215  1.00 47.32           C  
ANISOU 5994  CA  ARG A 841     7436   4717   5826   -439    981    268       C  
ATOM   5995  C   ARG A 841     -10.361  24.917 -19.596  1.00 63.97           C  
ANISOU 5995  C   ARG A 841     9706   6732   7867   -320   1093    367       C  
ATOM   5996  O   ARG A 841      -9.154  25.094 -19.743  1.00 87.61           O  
ANISOU 5996  O   ARG A 841    12734   9780  10774   -209   1018    425       O  
ATOM   5997  CB  ARG A 841     -11.241  27.253 -19.586  1.00 55.27           C  
ANISOU 5997  CB  ARG A 841     8366   5854   6780   -373    862    316       C  
ATOM   5998  CG  ARG A 841     -12.097  28.300 -20.267  1.00 78.71           C  
ANISOU 5998  CG  ARG A 841    11177   8928   9800   -468    737    228       C  
ATOM   5999  CD  ARG A 841     -11.844  29.673 -19.692  1.00111.59           C  
ANISOU 5999  CD  ARG A 841    15275  13216  13909   -397    623    279       C  
ATOM   6000  NE  ARG A 841     -12.622  30.690 -20.387  1.00135.87           N  
ANISOU 6000  NE  ARG A 841    18207  16390  17027   -475    506    202       N  
ATOM   6001  CZ  ARG A 841     -12.567  31.987 -20.111  1.00142.72           C  
ANISOU 6001  CZ  ARG A 841    18997  17367  17863   -435    399    225       C  
ATOM   6002  NH1 ARG A 841     -11.766  32.429 -19.150  1.00142.63           N1+
ANISOU 6002  NH1 ARG A 841    19029  17386  17780   -325    389    314       N1+
ATOM   6003  NH2 ARG A 841     -13.311  32.843 -20.795  1.00139.17           N  
ANISOU 6003  NH2 ARG A 841    18426  17000  17451   -501    304    156       N  
ATOM   6004  N   ASN A 842     -10.866  23.909 -18.894  1.00 64.13           N  
ANISOU 6004  N   ASN A 842     9827   6610   7929   -339   1278    385       N  
ATOM   6005  CA  ASN A 842     -10.034  22.813 -18.426  1.00 60.27           C  
ANISOU 6005  CA  ASN A 842     9505   6010   7386   -233   1409    471       C  
ATOM   6006  C   ASN A 842      -9.707  21.923 -19.618  1.00 70.49           C  
ANISOU 6006  C   ASN A 842    10834   7239   8711   -286   1432    411       C  
ATOM   6007  O   ASN A 842     -10.612  21.478 -20.322  1.00 71.41           O  
ANISOU 6007  O   ASN A 842    10906   7294   8931   -433   1481    303       O  
ATOM   6008  CB  ASN A 842     -10.766  22.016 -17.347  1.00 62.47           C  
ANISOU 6008  CB  ASN A 842     9885   6146   7705   -243   1617    507       C  
ATOM   6009  CG  ASN A 842      -9.847  21.081 -16.581  1.00 76.79           C  
ANISOU 6009  CG  ASN A 842    11882   7862   9434    -90   1748    625       C  
ATOM   6010  ND2 ASN A 842     -10.362  20.509 -15.503  1.00 59.19           N  
ANISOU 6010  ND2 ASN A 842     9754   5518   7218    -65   1927    680       N  
ATOM   6011  OD1 ASN A 842      -8.692  20.878 -16.948  1.00100.30           O  
ANISOU 6011  OD1 ASN A 842    14910  10868  12333     10   1694    668       O  
ATOM   6012  N   PRO A 843      -8.411  21.671 -19.856  1.00 65.93           N  
ANISOU 6012  N   PRO A 843    10329   6677   8045   -167   1395    475       N  
ATOM   6013  CA  PRO A 843      -7.936  20.870 -20.991  1.00 74.75           C  
ANISOU 6013  CA  PRO A 843    11486   7740   9176   -198   1408    428       C  
ATOM   6014  C   PRO A 843      -8.604  19.504 -21.072  1.00 84.56           C  
ANISOU 6014  C   PRO A 843    12823   8800  10507   -288   1608    383       C  
ATOM   6015  O   PRO A 843      -8.675  18.913 -22.150  1.00 90.90           O  
ANISOU 6015  O   PRO A 843    13621   9556  11361   -374   1619    298       O  
ATOM   6016  CB  PRO A 843      -6.440  20.689 -20.694  1.00 61.03           C  
ANISOU 6016  CB  PRO A 843     9846   6024   7319    -20   1388    539       C  
ATOM   6017  CG  PRO A 843      -6.264  21.105 -19.255  1.00 67.09           C  
ANISOU 6017  CG  PRO A 843    10653   6823   8017    103   1411    642       C  
ATOM   6018  CD  PRO A 843      -7.295  22.151 -19.031  1.00 31.41           C  
ANISOU 6018  CD  PRO A 843     6002   2383   3551     10   1337    591       C  
ATOM   6019  N   VAL A 844      -9.087  19.012 -19.938  1.00 79.40           N  
ANISOU 6019  N   VAL A 844    12257   8041   9872   -268   1772    437       N  
ATOM   6020  CA  VAL A 844      -9.684  17.686 -19.867  1.00 70.26           C  
ANISOU 6020  CA  VAL A 844    11206   6691   8800   -343   1992    405       C  
ATOM   6021  C   VAL A 844     -11.186  17.783 -19.610  1.00 88.70           C  
ANISOU 6021  C   VAL A 844    13462   8982  11258   -498   2068    316       C  
ATOM   6022  O   VAL A 844     -11.884  16.773 -19.529  1.00114.80           O  
ANISOU 6022  O   VAL A 844    16833  12127  14659   -589   2258    269       O  
ATOM   6023  CB  VAL A 844      -8.998  16.845 -18.776  1.00 75.45           C  
ANISOU 6023  CB  VAL A 844    12055   7232   9380   -186   2159    544       C  
ATOM   6024  CG1 VAL A 844      -9.592  15.454 -18.715  1.00112.58           C  
ANISOU 6024  CG1 VAL A 844    16879  11720  14177   -263   2406    515       C  
ATOM   6025  CG2 VAL A 844      -7.502  16.766 -19.039  1.00 80.08           C  
ANISOU 6025  CG2 VAL A 844    12707   7875   9846    -28   2077    625       C  
ATOM   6026  N   GLY A 845     -11.680  19.013 -19.503  1.00 85.97           N  
ANISOU 6026  N   GLY A 845    12973   8779  10915   -530   1921    289       N  
ATOM   6027  CA  GLY A 845     -13.084  19.247 -19.222  1.00 72.97           C  
ANISOU 6027  CA  GLY A 845    11234   7112   9377   -666   1974    208       C  
ATOM   6028  C   GLY A 845     -13.848  19.950 -20.328  1.00 82.88           C  
ANISOU 6028  C   GLY A 845    12305   8479  10706   -809   1822     61       C  
ATOM   6029  O   GLY A 845     -15.072  20.054 -20.269  1.00 96.28           O  
ANISOU 6029  O   GLY A 845    13912  10161  12508   -937   1865    -31       O  
ATOM   6030  N   TYR A 846     -13.140  20.439 -21.341  1.00 82.19           N  
ANISOU 6030  N   TYR A 846    12159   8507  10563   -782   1648     39       N  
ATOM   6031  CA  TYR A 846     -13.812  21.121 -22.445  1.00 84.45           C  
ANISOU 6031  CA  TYR A 846    12277   8907  10902   -897   1499    -95       C  
ATOM   6032  C   TYR A 846     -14.743  20.208 -23.248  1.00 88.09           C  
ANISOU 6032  C   TYR A 846    12705   9275  11488  -1062   1592   -249       C  
ATOM   6033  O   TYR A 846     -15.829  20.633 -23.642  1.00 84.85           O  
ANISOU 6033  O   TYR A 846    12155   8924  11159  -1180   1540   -369       O  
ATOM   6034  CB  TYR A 846     -12.817  21.854 -23.359  1.00 71.19           C  
ANISOU 6034  CB  TYR A 846    10554   7366   9131   -824   1302    -79       C  
ATOM   6035  CG  TYR A 846     -11.998  20.981 -24.288  1.00 64.59           C  
ANISOU 6035  CG  TYR A 846     9797   6474   8272   -809   1320    -97       C  
ATOM   6036  CD1 TYR A 846     -12.499  20.583 -25.521  1.00 65.60           C  
ANISOU 6036  CD1 TYR A 846     9862   6596   8467   -928   1296   -238       C  
ATOM   6037  CD2 TYR A 846     -10.712  20.579 -23.947  1.00 68.34           C  
ANISOU 6037  CD2 TYR A 846    10403   6909   8654   -669   1353     23       C  
ATOM   6038  CE1 TYR A 846     -11.751  19.798 -26.379  1.00 77.25           C  
ANISOU 6038  CE1 TYR A 846    11412   8021   9920   -914   1312   -256       C  
ATOM   6039  CE2 TYR A 846      -9.956  19.795 -24.799  1.00 68.79           C  
ANISOU 6039  CE2 TYR A 846    10531   6915   8690   -652   1370      9       C  
ATOM   6040  CZ  TYR A 846     -10.481  19.407 -26.015  1.00 85.14           C  
ANISOU 6040  CZ  TYR A 846    12544   8973  10830   -777   1352   -130       C  
ATOM   6041  OH  TYR A 846      -9.736  18.626 -26.872  1.00 82.23           O  
ANISOU 6041  OH  TYR A 846    12250   8554  10441   -760   1371   -147       O  
ATOM   6042  N   PRO A 847     -14.335  18.946 -23.482  1.00 83.75           N  
ANISOU 6042  N   PRO A 847    12280   8582  10958  -1068   1733   -253       N  
ATOM   6043  CA  PRO A 847     -15.210  18.064 -24.259  1.00 83.86           C  
ANISOU 6043  CA  PRO A 847    12259   8506  11098  -1231   1825   -414       C  
ATOM   6044  C   PRO A 847     -16.546  17.856 -23.562  1.00102.47           C  
ANISOU 6044  C   PRO A 847    14570  10785  13578  -1349   1965   -481       C  
ATOM   6045  O   PRO A 847     -17.566  17.734 -24.235  1.00113.40           O  
ANISOU 6045  O   PRO A 847    15835  12179  15071  -1500   1961   -645       O  
ATOM   6046  CB  PRO A 847     -14.437  16.742 -24.294  1.00 74.40           C  
ANISOU 6046  CB  PRO A 847    11236   7143   9889  -1190   1986   -368       C  
ATOM   6047  CG  PRO A 847     -13.027  17.103 -23.994  1.00 64.53           C  
ANISOU 6047  CG  PRO A 847    10076   5950   8491  -1004   1905   -208       C  
ATOM   6048  CD  PRO A 847     -13.108  18.253 -23.050  1.00 73.20           C  
ANISOU 6048  CD  PRO A 847    11120   7158   9535   -929   1819   -120       C  
ATOM   6049  N   LEU A 848     -16.535  17.821 -22.232  1.00 97.57           N  
ANISOU 6049  N   LEU A 848    14040  10093  12940  -1278   2086   -360       N  
ATOM   6050  CA  LEU A 848     -17.748  17.575 -21.453  1.00 81.82           C  
ANISOU 6050  CA  LEU A 848    12020   8006  11061  -1380   2244   -407       C  
ATOM   6051  C   LEU A 848     -18.738  18.725 -21.555  1.00 80.65           C  
ANISOU 6051  C   LEU A 848    11679   8009  10956  -1456   2103   -491       C  
ATOM   6052  O   LEU A 848     -19.935  18.507 -21.726  1.00 86.50           O  
ANISOU 6052  O   LEU A 848    12321   8717  11827  -1607   2169   -629       O  
ATOM   6053  CB  LEU A 848     -17.409  17.326 -19.983  1.00 77.26           C  
ANISOU 6053  CB  LEU A 848    11598   7326  10433  -1260   2401   -241       C  
ATOM   6054  CG  LEU A 848     -16.322  16.295 -19.691  1.00101.83           C  
ANISOU 6054  CG  LEU A 848    14915  10301  13474  -1142   2538   -126       C  
ATOM   6055  CD1 LEU A 848     -16.165  16.110 -18.191  1.00 81.76           C  
ANISOU 6055  CD1 LEU A 848    12515   7668  10882  -1022   2694     28       C  
ATOM   6056  CD2 LEU A 848     -16.638  14.973 -20.373  1.00 97.11           C  
ANISOU 6056  CD2 LEU A 848    14371   9537  12987  -1264   2705   -236       C  
ATOM   6057  N   ALA A 849     -18.231  19.950 -21.440  1.00101.84           N  
ANISOU 6057  N   ALA A 849    14308  10856  13530  -1349   1912   -409       N  
ATOM   6058  CA  ALA A 849     -19.070  21.145 -21.504  1.00 93.80           C  
ANISOU 6058  CA  ALA A 849    13116   9988  12536  -1398   1768   -469       C  
ATOM   6059  C   ALA A 849     -19.655  21.325 -22.902  1.00 94.83           C  
ANISOU 6059  C   ALA A 849    13093  10213  12724  -1515   1640   -643       C  
ATOM   6060  O   ALA A 849     -20.772  21.817 -23.062  1.00 81.82           O  
ANISOU 6060  O   ALA A 849    11297   8635  11155  -1614   1596   -754       O  
ATOM   6061  CB  ALA A 849     -18.271  22.372 -21.095  1.00 67.81           C  
ANISOU 6061  CB  ALA A 849     9816   6837   9111  -1251   1604   -339       C  
ATOM   6062  N   TRP A 850     -18.885  20.924 -23.908  1.00 89.99           N  
ANISOU 6062  N   TRP A 850    12517   9608  12068  -1495   1580   -668       N  
ATOM   6063  CA  TRP A 850     -19.340  20.948 -25.291  1.00 87.82           C  
ANISOU 6063  CA  TRP A 850    12118   9415  11836  -1593   1468   -834       C  
ATOM   6064  C   TRP A 850     -20.360  19.833 -25.510  1.00105.72           C  
ANISOU 6064  C   TRP A 850    14360  11555  14254  -1758   1633   -992       C  
ATOM   6065  O   TRP A 850     -21.478  20.078 -25.966  1.00105.81           O  
ANISOU 6065  O   TRP A 850    14217  11634  14354  -1876   1588  -1146       O  
ATOM   6066  CB  TRP A 850     -18.142  20.784 -26.229  1.00 90.56           C  
ANISOU 6066  CB  TRP A 850    12531   9793  12087  -1514   1373   -802       C  
ATOM   6067  CG  TRP A 850     -18.436  20.911 -27.706  1.00115.03           C  
ANISOU 6067  CG  TRP A 850    15513  12995  15199  -1585   1235   -956       C  
ATOM   6068  CD1 TRP A 850     -17.655  20.453 -28.732  1.00112.22           C  
ANISOU 6068  CD1 TRP A 850    15207  12638  14794  -1561   1188   -981       C  
ATOM   6069  CD2 TRP A 850     -19.574  21.538 -28.319  1.00123.48           C  
ANISOU 6069  CD2 TRP A 850    16402  14189  16326  -1678   1125  -1105       C  
ATOM   6070  CE2 TRP A 850     -19.412  21.418 -29.717  1.00100.81           C  
ANISOU 6070  CE2 TRP A 850    13483  11390  13431  -1701   1013  -1214       C  
ATOM   6071  CE3 TRP A 850     -20.710  22.185 -27.826  1.00129.78           C  
ANISOU 6071  CE3 TRP A 850    17074  15048  17190  -1739   1110  -1156       C  
ATOM   6072  NE1 TRP A 850     -18.235  20.752 -29.941  1.00101.45           N  
ANISOU 6072  NE1 TRP A 850    13709  11390  13450  -1632   1057  -1135       N  
ATOM   6073  CZ2 TRP A 850     -20.343  21.919 -30.624  1.00 86.58           C  
ANISOU 6073  CZ2 TRP A 850    11512   9723  11661  -1774    884  -1374       C  
ATOM   6074  CZ3 TRP A 850     -21.634  22.682 -28.727  1.00122.96           C  
ANISOU 6074  CZ3 TRP A 850    16038  14316  16363  -1814    983  -1315       C  
ATOM   6075  CH2 TRP A 850     -21.445  22.547 -30.110  1.00107.77           C  
ANISOU 6075  CH2 TRP A 850    14071  12468  14408  -1827    869  -1422       C  
ATOM   6076  N   GLN A 851     -19.972  18.609 -25.165  1.00105.54           N  
ANISOU 6076  N   GLN A 851    14490  11348  14262  -1764   1829   -956       N  
ATOM   6077  CA  GLN A 851     -20.871  17.463 -25.252  1.00111.86           C  
ANISOU 6077  CA  GLN A 851    15289  11998  15215  -1921   2022  -1098       C  
ATOM   6078  C   GLN A 851     -22.105  17.669 -24.381  1.00 77.77           C  
ANISOU 6078  C   GLN A 851    10891   7653  11007  -2010   2121  -1143       C  
ATOM   6079  O   GLN A 851     -23.071  16.916 -24.478  1.00106.59           O  
ANISOU 6079  O   GLN A 851    14493  11204  14802  -2161   2264  -1289       O  
ATOM   6080  CB  GLN A 851     -20.150  16.175 -24.836  1.00145.70           C  
ANISOU 6080  CB  GLN A 851    19780  16076  19503  -1885   2236  -1017       C  
ATOM   6081  CG  GLN A 851     -19.057  15.724 -25.799  1.00167.81           C  
ANISOU 6081  CG  GLN A 851    22658  18876  22224  -1826   2172  -1005       C  
ATOM   6082  CD  GLN A 851     -18.297  14.508 -25.298  1.00165.28           C  
ANISOU 6082  CD  GLN A 851    22550  18354  21895  -1770   2385   -906       C  
ATOM   6083  NE2 GLN A 851     -17.685  13.772 -26.220  1.00161.18           N  
ANISOU 6083  NE2 GLN A 851    22091  17789  21363  -1776   2390   -952       N  
ATOM   6084  OE1 GLN A 851     -18.257  14.235 -24.097  1.00157.80           O  
ANISOU 6084  OE1 GLN A 851    21715  17294  20947  -1713   2545   -787       O  
ATOM   6085  N   PHE A 852     -22.065  18.690 -23.529  1.00 59.63           N  
ANISOU 6085  N   PHE A 852     8574   5440   8641  -1918   2049  -1022       N  
ATOM   6086  CA  PHE A 852     -23.162  18.973 -22.609  1.00 79.82           C  
ANISOU 6086  CA  PHE A 852    11064   7975  11288  -1983   2140  -1042       C  
ATOM   6087  C   PHE A 852     -24.095  20.032 -23.176  1.00101.98           C  
ANISOU 6087  C   PHE A 852    13652  10969  14128  -2051   1957  -1167       C  
ATOM   6088  O   PHE A 852     -25.317  19.920 -23.069  1.00126.73           O  
ANISOU 6088  O   PHE A 852    16672  14086  17394  -2182   2029  -1299       O  
ATOM   6089  CB  PHE A 852     -22.628  19.434 -21.252  1.00 87.40           C  
ANISOU 6089  CB  PHE A 852    12138   8912  12157  -1840   2185   -838       C  
ATOM   6090  CG  PHE A 852     -23.682  19.529 -20.185  1.00100.58           C  
ANISOU 6090  CG  PHE A 852    13775  10523  13919  -1901   2324   -843       C  
ATOM   6091  CD1 PHE A 852     -23.870  18.494 -19.284  1.00104.06           C  
ANISOU 6091  CD1 PHE A 852    14354  10757  14428  -1923   2590   -799       C  
ATOM   6092  CD2 PHE A 852     -24.485  20.651 -20.081  1.00111.73           C  
ANISOU 6092  CD2 PHE A 852    15024  12080  15349  -1929   2196   -888       C  
ATOM   6093  CE1 PHE A 852     -24.837  18.578 -18.300  1.00 96.92           C  
ANISOU 6093  CE1 PHE A 852    13424   9792  13609  -1977   2727   -801       C  
ATOM   6094  CE2 PHE A 852     -25.455  20.738 -19.100  1.00108.27           C  
ANISOU 6094  CE2 PHE A 852    14554  11586  14996  -1984   2326   -892       C  
ATOM   6095  CZ  PHE A 852     -25.628  19.703 -18.208  1.00101.58           C  
ANISOU 6095  CZ  PHE A 852    13845  10533  14218  -2009   2593   -849       C  
ATOM   6096  N   LEU A 853     -23.511  21.065 -23.769  1.00110.74           N  
ANISOU 6096  N   LEU A 853    14704  12253  15118  -1956   1725  -1125       N  
ATOM   6097  CA  LEU A 853     -24.290  22.115 -24.405  1.00 93.07           C  
ANISOU 6097  CA  LEU A 853    12270  10202  12891  -1996   1538  -1233       C  
ATOM   6098  C   LEU A 853     -25.104  21.514 -25.540  1.00106.21           C  
ANISOU 6098  C   LEU A 853    13814  11878  14661  -2143   1531  -1456       C  
ATOM   6099  O   LEU A 853     -26.201  21.977 -25.843  1.00110.17           O  
ANISOU 6099  O   LEU A 853    14143  12480  15235  -2228   1464  -1594       O  
ATOM   6100  CB  LEU A 853     -23.370  23.216 -24.930  0.00 90.15           C  
ANISOU 6100  CB  LEU A 853    11887   9995  12369  -1859   1310  -1142       C  
ATOM   6101  CG  LEU A 853     -23.751  24.643 -24.534  0.00101.01           C  
ANISOU 6101  CG  LEU A 853    13156  11523  13702  -1804   1172  -1095       C  
ATOM   6102  CD1 LEU A 853     -22.521  25.524 -24.457  0.00101.02           C  
ANISOU 6102  CD1 LEU A 853    13225  11608  13550  -1643   1036   -933       C  
ATOM   6103  CD2 LEU A 853     -24.772  25.227 -25.494  0.00125.04           C  
ANISOU 6103  CD2 LEU A 853    16002  14716  16793  -1883   1031  -1264       C  
ATOM   6104  N   ARG A 854     -24.563  20.470 -26.160  1.00 97.75           N  
ANISOU 6104  N   ARG A 854    12833  10709  13600  -2170   1601  -1497       N  
ATOM   6105  CA  ARG A 854     -25.270  19.769 -27.222  1.00109.69           C  
ANISOU 6105  CA  ARG A 854    14244  12219  15214  -2313   1610  -1718       C  
ATOM   6106  C   ARG A 854     -26.432  18.936 -26.675  1.00123.03           C  
ANISOU 6106  C   ARG A 854    15892  13771  17084  -2474   1825  -1843       C  
ATOM   6107  O   ARG A 854     -27.591  19.187 -27.010  1.00141.23           O  
ANISOU 6107  O   ARG A 854    18017  16160  19485  -2584   1782  -2014       O  
ATOM   6108  CB  ARG A 854     -24.306  18.896 -28.030  1.00127.29           C  
ANISOU 6108  CB  ARG A 854    16589  14377  17398  -2292   1627  -1721       C  
ATOM   6109  CG  ARG A 854     -23.243  19.682 -28.784  1.00 83.87           C  
ANISOU 6109  CG  ARG A 854    11109   9022  11736  -2152   1411  -1633       C  
ATOM   6110  CD  ARG A 854     -22.645  18.850 -29.907  1.00 95.10           C  
ANISOU 6110  CD  ARG A 854    12586  10409  13140  -2169   1402  -1709       C  
ATOM   6111  NE  ARG A 854     -21.947  17.671 -29.410  1.00135.44           N  
ANISOU 6111  NE  ARG A 854    17882  15312  18267  -2161   1606  -1628       N  
ATOM   6112  CZ  ARG A 854     -20.632  17.608 -29.239  1.00151.30           C  
ANISOU 6112  CZ  ARG A 854    20045  17282  20159  -2024   1600  -1458       C  
ATOM   6113  NH1 ARG A 854     -19.880  18.655 -29.531  1.00164.45           N1+
ANISOU 6113  NH1 ARG A 854    21695  19098  21691  -1896   1406  -1358       N1+
ATOM   6114  NH2 ARG A 854     -20.071  16.499 -28.783  1.00143.96           N  
ANISOU 6114  NH2 ARG A 854    19284  16165  19250  -2014   1793  -1392       N  
ATOM   6115  N   LYS A 855     -26.123  17.951 -25.833  1.00116.31           N  
ANISOU 6115  N   LYS A 855    15206  12709  16278  -2483   2060  -1760       N  
ATOM   6116  CA  LYS A 855     -27.154  17.114 -25.227  1.00110.12           C  
ANISOU 6116  CA  LYS A 855    14404  11767  15668  -2631   2296  -1863       C  
ATOM   6117  C   LYS A 855     -28.287  17.959 -24.658  1.00121.62           C  
ANISOU 6117  C   LYS A 855    15705  13315  17190  -2680   2265  -1909       C  
ATOM   6118  O   LYS A 855     -29.376  18.037 -25.227  1.00137.68           O  
ANISOU 6118  O   LYS A 855    17553  15426  19332  -2809   2223  -2111       O  
ATOM   6119  CB  LYS A 855     -26.576  16.267 -24.090  0.00120.81           C  
ANISOU 6119  CB  LYS A 855    15980  12897  17024  -2580   2544  -1700       C  
ATOM   6120  CG  LYS A 855     -25.530  15.248 -24.491  0.00131.55           C  
ANISOU 6120  CG  LYS A 855    17514  14130  18341  -2538   2628  -1652       C  
ATOM   6121  CD  LYS A 855     -25.227  14.329 -23.316  0.00142.67           C  
ANISOU 6121  CD  LYS A 855    19127  15303  19777  -2505   2907  -1517       C  
ATOM   6122  CE  LYS A 855     -23.808  13.791 -23.371  0.00141.91           C  
ANISOU 6122  CE  LYS A 855    19233  15129  19557  -2366   2933  -1365       C  
ATOM   6123  NZ  LYS A 855     -23.572  12.757 -22.326  0.00139.80           N1+
ANISOU 6123  NZ  LYS A 855    19171  14623  19324  -2335   3222  -1252       N1+
ATOM   6124  N   ASN A 856     -28.011  18.590 -23.524  1.00 99.07           N  
ANISOU 6124  N   ASN A 856    12925  10454  14265  -2570   2284  -1722       N  
ATOM   6125  CA  ASN A 856     -29.029  19.304 -22.772  1.00105.52           C  
ANISOU 6125  CA  ASN A 856    13626  11324  15145  -2607   2295  -1738       C  
ATOM   6126  C   ASN A 856     -29.450  20.626 -23.390  1.00120.56           C  
ANISOU 6126  C   ASN A 856    15338  13472  16996  -2582   2031  -1799       C  
ATOM   6127  O   ASN A 856     -30.096  21.438 -22.734  1.00121.28           O  
ANISOU 6127  O   ASN A 856    15346  13632  17103  -2573   2004  -1774       O  
ATOM   6128  CB  ASN A 856     -28.550  19.541 -21.339  1.00116.20           C  
ANISOU 6128  CB  ASN A 856    15132  12590  16429  -2487   2403  -1516       C  
ATOM   6129  CG  ASN A 856     -28.482  18.249 -20.529  1.00126.05           C  
ANISOU 6129  CG  ASN A 856    16554  13585  17756  -2526   2705  -1468       C  
ATOM   6130  ND2 ASN A 856     -27.658  18.252 -19.455  1.00135.33           N  
ANISOU 6130  ND2 ASN A 856    17915  14676  18828  -2381   2790  -1252       N  
ATOM   6131  OD1 ASN A 856     -29.171  17.252 -20.846  1.00127.58           O  
ANISOU 6131  OD1 ASN A 856    16716  13656  18102  -2681   2867  -1627       O  
ATOM   6132  N   TRP A 857     -29.090  20.837 -24.653  1.00135.49           N  
ANISOU 6132  N   TRP A 857    17166  15492  18823  -2564   1843  -1877       N  
ATOM   6133  CA  TRP A 857     -29.397  22.089 -25.350  1.00157.84           C  
ANISOU 6133  CA  TRP A 857    19829  18557  21587  -2520   1588  -1927       C  
ATOM   6134  C   TRP A 857     -30.872  22.470 -25.272  1.00161.38           C  
ANISOU 6134  C   TRP A 857    20075  19084  22158  -2633   1583  -2087       C  
ATOM   6135  O   TRP A 857     -31.214  23.603 -24.922  1.00119.34           O  
ANISOU 6135  O   TRP A 857    14665  13887  16790  -2573   1469  -2036       O  
ATOM   6136  CB  TRP A 857     -28.963  22.007 -26.816  1.00161.93           C  
ANISOU 6136  CB  TRP A 857    20306  19178  22044  -2510   1425  -2026       C  
ATOM   6137  CG  TRP A 857     -29.355  23.205 -27.642  1.00179.87           C  
ANISOU 6137  CG  TRP A 857    22407  21686  24250  -2467   1175  -2096       C  
ATOM   6138  CD1 TRP A 857     -30.184  23.217 -28.726  1.00187.91           C  
ANISOU 6138  CD1 TRP A 857    23250  22827  25319  -2549   1069  -2311       C  
ATOM   6139  CD2 TRP A 857     -28.932  24.564 -27.446  1.00177.34           C  
ANISOU 6139  CD2 TRP A 857    22077  21506  23797  -2323   1006  -1951       C  
ATOM   6140  CE2 TRP A 857     -29.544  25.340 -28.452  1.00151.34           C  
ANISOU 6140  CE2 TRP A 857    18609  18412  20481  -2321    809  -2080       C  
ATOM   6141  CE3 TRP A 857     -28.098  25.196 -26.520  1.00176.75           C  
ANISOU 6141  CE3 TRP A 857    22124  21410  23623  -2194   1005  -1731       C  
ATOM   6142  NE1 TRP A 857     -30.301  24.496 -29.220  1.00172.01           N  
ANISOU 6142  NE1 TRP A 857    21127  21023  23207  -2456    846  -2300       N  
ATOM   6143  CZ2 TRP A 857     -29.345  26.717 -28.558  1.00122.75           C  
ANISOU 6143  CZ2 TRP A 857    14941  14955  16743  -2196    624  -1987       C  
ATOM   6144  CZ3 TRP A 857     -27.902  26.565 -26.625  1.00149.20           C  
ANISOU 6144  CZ3 TRP A 857    18579  18086  20026  -2081    818  -1650       C  
ATOM   6145  CH2 TRP A 857     -28.524  27.309 -27.637  1.00125.27           C  
ANISOU 6145  CH2 TRP A 857    15381  15238  16977  -2083    636  -1774       C  
ATOM   6146  N   ASN A 858     -31.738  21.518 -25.612  1.00159.83           N  
ANISOU 6146  N   ASN A 858    19797  18811  22118  -2797   1707  -2287       N  
ATOM   6147  CA  ASN A 858     -33.179  21.750 -25.612  1.00135.60           C  
ANISOU 6147  CA  ASN A 858    16522  15815  19185  -2920   1712  -2469       C  
ATOM   6148  C   ASN A 858     -33.706  22.283 -24.276  1.00134.26           C  
ANISOU 6148  C   ASN A 858    16351  15608  19054  -2907   1810  -2365       C  
ATOM   6149  O   ASN A 858     -34.265  23.375 -24.215  1.00108.31           O  
ANISOU 6149  O   ASN A 858    12931  12481  15742  -2870   1670  -2372       O  
ATOM   6150  CB  ASN A 858     -33.937  20.483 -26.036  0.00135.05           C  
ANISOU 6150  CB  ASN A 858    16388  15632  19294  -3108   1876  -2696       C  
ATOM   6151  CG  ASN A 858     -33.735  19.319 -25.074  0.00141.46           C  
ANISOU 6151  CG  ASN A 858    17375  16174  20199  -3169   2177  -2626       C  
ATOM   6152  ND2 ASN A 858     -33.703  18.110 -25.609  0.00150.12           N  
ANISOU 6152  ND2 ASN A 858    18510  17144  21387  -3279   2306  -2754       N  
ATOM   6153  OD1 ASN A 858     -33.625  19.503 -23.874  0.00129.60           O  
ANISOU 6153  OD1 ASN A 858    15975  14580  18687  -3116   2296  -2461       O  
ATOM   6154  N   LYS A 859     -33.514  21.520 -23.207  1.00147.35           N  
ANISOU 6154  N   LYS A 859    18165  17054  20767  -2928   2053  -2263       N  
ATOM   6155  CA  LYS A 859     -33.975  21.911 -21.884  1.00137.60           C  
ANISOU 6155  CA  LYS A 859    16951  15763  19568  -2913   2171  -2158       C  
ATOM   6156  C   LYS A 859     -33.113  23.042 -21.335  1.00145.16           C  
ANISOU 6156  C   LYS A 859    17995  16811  20347  -2726   2031  -1931       C  
ATOM   6157  O   LYS A 859     -33.441  23.646 -20.315  1.00145.16           O  
ANISOU 6157  O   LYS A 859    17998  16812  20346  -2687   2072  -1836       O  
ATOM   6158  CB  LYS A 859     -33.943  20.723 -20.919  1.00123.58           C  
ANISOU 6158  CB  LYS A 859    15338  13726  17889  -2974   2481  -2105       C  
ATOM   6159  CG  LYS A 859     -34.627  19.468 -21.431  0.00136.23           C  
ANISOU 6159  CG  LYS A 859    16887  15202  19671  -3161   2652  -2319       C  
ATOM   6160  CD  LYS A 859     -35.635  18.945 -20.430  0.00147.80           C  
ANISOU 6160  CD  LYS A 859    18339  16510  21310  -3282   2916  -2368       C  
ATOM   6161  CE  LYS A 859     -35.975  17.487 -20.687  0.00157.11           C  
ANISOU 6161  CE  LYS A 859    19548  17491  22655  -3446   3155  -2523       C  
ATOM   6162  NZ  LYS A 859     -36.977  16.979 -19.710  0.00162.37           N1+
ANISOU 6162  NZ  LYS A 859    20200  17993  23499  -3568   3429  -2574       N1+
ATOM   6163  N   LEU A 860     -32.009  23.322 -22.022  1.00147.74           N  
ANISOU 6163  N   LEU A 860    18393  17215  20529  -2613   1868  -1851       N  
ATOM   6164  CA  LEU A 860     -31.056  24.334 -21.580  1.00142.25           C  
ANISOU 6164  CA  LEU A 860    17785  16599  19664  -2437   1738  -1644       C  
ATOM   6165  C   LEU A 860     -31.510  25.727 -21.992  1.00145.73           C  
ANISOU 6165  C   LEU A 860    18058  17262  20052  -2391   1509  -1675       C  
ATOM   6166  O   LEU A 860     -31.593  26.634 -21.164  1.00140.16           O  
ANISOU 6166  O   LEU A 860    17349  16605  19301  -2317   1479  -1564       O  
ATOM   6167  CB  LEU A 860     -29.671  24.043 -22.157  1.00125.19           C  
ANISOU 6167  CB  LEU A 860    15766  14423  17377  -2338   1670  -1550       C  
ATOM   6168  CG  LEU A 860     -28.461  24.775 -21.579  1.00127.19           C  
ANISOU 6168  CG  LEU A 860    16153  14708  17465  -2159   1589  -1326       C  
ATOM   6169  CD1 LEU A 860     -27.190  24.002 -21.893  1.00139.16           C  
ANISOU 6169  CD1 LEU A 860    17839  16134  18903  -2093   1621  -1245       C  
ATOM   6170  CD2 LEU A 860     -28.374  26.200 -22.102  1.00 94.24           C  
ANISOU 6170  CD2 LEU A 860    11866  10750  13193  -2074   1338  -1309       C  
ATOM   6171  N   VAL A 861     -31.797  25.891 -23.279  1.00147.54           N  
ANISOU 6171  N   VAL A 861    18151  17626  20283  -2428   1351  -1828       N  
ATOM   6172  CA  VAL A 861     -32.315  27.153 -23.787  1.00138.30           C  
ANISOU 6172  CA  VAL A 861    16815  16668  19067  -2384   1139  -1876       C  
ATOM   6173  C   VAL A 861     -33.538  27.557 -22.977  1.00144.73           C  
ANISOU 6173  C   VAL A 861    17508  17497  19985  -2450   1208  -1925       C  
ATOM   6174  O   VAL A 861     -33.913  28.729 -22.941  1.00132.95           O  
ANISOU 6174  O   VAL A 861    15913  16154  18446  -2388   1068  -1905       O  
ATOM   6175  CB  VAL A 861     -32.698  27.050 -25.275  1.00124.07           C  
ANISOU 6175  CB  VAL A 861    14870  14994  17277  -2437    996  -2071       C  
ATOM   6176  CG1 VAL A 861     -31.491  26.658 -26.102  1.00102.26           C  
ANISOU 6176  CG1 VAL A 861    12228  12217  14410  -2371    930  -2023       C  
ATOM   6177  CG2 VAL A 861     -33.823  26.045 -25.470  1.00112.28           C  
ANISOU 6177  CG2 VAL A 861    13264  13434  15963  -2618   1131  -2291       C  
ATOM   6178  N   GLN A 862     -34.145  26.572 -22.321  1.00150.14           N  
ANISOU 6178  N   GLN A 862    18213  18020  20814  -2572   1433  -1987       N  
ATOM   6179  CA  GLN A 862     -35.321  26.780 -21.485  1.00144.59           C  
ANISOU 6179  CA  GLN A 862    17407  17302  20230  -2650   1538  -2039       C  
ATOM   6180  C   GLN A 862     -35.082  27.867 -20.439  1.00134.53           C  
ANISOU 6180  C   GLN A 862    16186  16066  18865  -2526   1502  -1849       C  
ATOM   6181  O   GLN A 862     -36.028  28.401 -19.857  1.00105.91           O  
ANISOU 6181  O   GLN A 862    12453  12480  15306  -2558   1527  -1880       O  
ATOM   6182  CB  GLN A 862     -35.715  25.469 -20.797  1.00151.88           C  
ANISOU 6182  CB  GLN A 862    18401  18001  21304  -2780   1822  -2086       C  
ATOM   6183  CG  GLN A 862     -37.145  25.431 -20.284  1.00160.04           C  
ANISOU 6183  CG  GLN A 862    19283  19019  22505  -2909   1941  -2219       C  
ATOM   6184  CD  GLN A 862     -38.137  25.004 -21.350  1.00153.80           C  
ANISOU 6184  CD  GLN A 862    18287  18303  21846  -3058   1905  -2492       C  
ATOM   6185  NE2 GLN A 862     -38.997  25.928 -21.763  1.00161.83           N  
ANISOU 6185  NE2 GLN A 862    19098  19515  22875  -3061   1740  -2601       N  
ATOM   6186  OE1 GLN A 862     -38.133  23.856 -21.793  1.00131.43           O  
ANISOU 6186  OE1 GLN A 862    15479  15355  19102  -3165   2024  -2608       O  
ATOM   6187  N   LYS A 863     -33.815  28.184 -20.197  1.00143.37           N  
ANISOU 6187  N   LYS A 863    17467  17172  19834  -2385   1446  -1659       N  
ATOM   6188  CA  LYS A 863     -33.454  29.290 -19.317  1.00118.95           C  
ANISOU 6188  CA  LYS A 863    14424  14134  16639  -2257   1385  -1485       C  
ATOM   6189  C   LYS A 863     -32.313  30.102 -19.919  1.00113.76           C  
ANISOU 6189  C   LYS A 863    13816  13594  15813  -2114   1180  -1378       C  
ATOM   6190  O   LYS A 863     -31.995  29.958 -21.099  1.00102.24           O  
ANISOU 6190  O   LYS A 863    12323  12203  14322  -2116   1064  -1455       O  
ATOM   6191  CB  LYS A 863     -33.062  28.781 -17.929  1.00 96.88           C  
ANISOU 6191  CB  LYS A 863    11807  11160  13844  -2226   1593  -1333       C  
ATOM   6192  CG  LYS A 863     -34.174  28.047 -17.202  1.00123.64           C  
ANISOU 6192  CG  LYS A 863    15162  14419  17399  -2358   1818  -1418       C  
ATOM   6193  CD  LYS A 863     -33.849  27.871 -15.726  1.00139.63           C  
ANISOU 6193  CD  LYS A 863    17355  16300  19398  -2294   1997  -1246       C  
ATOM   6194  CE  LYS A 863     -32.602  27.027 -15.521  1.00129.15           C  
ANISOU 6194  CE  LYS A 863    16246  14837  17989  -2220   2088  -1119       C  
ATOM   6195  NZ  LYS A 863     -32.795  25.619 -15.969  1.00105.00           N1+
ANISOU 6195  NZ  LYS A 863    13221  11628  15045  -2344   2255  -1233       N1+
TER    6196      LYS A 863 
ATOM   6197  N   SER A 868     -31.798  34.904 -23.378  1.00100.95           N  
ANISOU 6197  N   SER A 868    11829  12728  13797  -1753    274  -1389       N  
ATOM   6198  CA  SER A 868     -31.009  34.604 -24.569  1.00126.05           C  
ANISOU 6198  CA  SER A 868    15049  15942  16904  -1719    178  -1415       C  
ATOM   6199  C   SER A 868     -29.974  35.691 -24.857  1.00130.78           C  
ANISOU 6199  C   SER A 868    15711  16625  17355  -1570     36  -1277       C  
ATOM   6200  O   SER A 868     -29.359  35.711 -25.924  1.00102.16           O  
ANISOU 6200  O   SER A 868    12105  13056  13656  -1523    -68  -1292       O  
ATOM   6201  CB  SER A 868     -31.916  34.397 -25.786  1.00107.15           C  
ANISOU 6201  CB  SER A 868    12496  13659  14558  -1785     91  -1617       C  
ATOM   6202  OG  SER A 868     -32.646  33.186 -25.686  1.00 82.88           O  
ANISOU 6202  OG  SER A 868     9379  10488  11622  -1932    232  -1757       O  
ATOM   6203  N   SER A 869     -29.783  36.588 -23.895  1.00151.82           N  
ANISOU 6203  N   SER A 869    18410  19293  19981  -1500     39  -1146       N  
ATOM   6204  CA  SER A 869     -28.827  37.679 -24.048  1.00167.35           C  
ANISOU 6204  CA  SER A 869    20433  21331  21822  -1366    -79  -1018       C  
ATOM   6205  C   SER A 869     -27.613  37.476 -23.149  1.00175.70           C  
ANISOU 6205  C   SER A 869    21657  22274  22826  -1311      0   -860       C  
ATOM   6206  O   SER A 869     -26.520  37.955 -23.449  1.00173.53           O  
ANISOU 6206  O   SER A 869    21457  22024  22452  -1216    -76   -768       O  
ATOM   6207  CB  SER A 869     -29.488  39.023 -23.738  1.00163.72           C  
ANISOU 6207  CB  SER A 869    19876  20984  21348  -1312   -158   -996       C  
ATOM   6208  OG  SER A 869     -29.895  39.093 -22.382  1.00165.47           O  
ANISOU 6208  OG  SER A 869    20112  21135  21625  -1340    -44   -941       O  
ATOM   6209  N   SER A 870     -27.814  36.765 -22.044  1.00178.05           N  
ANISOU 6209  N   SER A 870    22013  22449  23191  -1367    157   -833       N  
ATOM   6210  CA  SER A 870     -26.740  36.500 -21.094  1.00163.74           C  
ANISOU 6210  CA  SER A 870    20358  20529  21325  -1308    242   -690       C  
ATOM   6211  C   SER A 870     -26.205  35.085 -21.260  1.00152.19           C  
ANISOU 6211  C   SER A 870    19000  18939  19885  -1354    350   -705       C  
ATOM   6212  O   SER A 870     -25.196  34.715 -20.662  1.00146.96           O  
ANISOU 6212  O   SER A 870    18477  18191  19169  -1296    413   -593       O  
ATOM   6213  CB  SER A 870     -27.229  36.708 -19.660  1.00150.98           C  
ANISOU 6213  CB  SER A 870    18757  18859  19749  -1314    351   -628       C  
ATOM   6214  OG  SER A 870     -27.648  38.044 -19.456  1.00135.97           O  
ANISOU 6214  OG  SER A 870    16770  17071  17823  -1264    255   -605       O  
ATOM   6215  N   ILE A 871     -26.894  34.296 -22.077  1.00143.55           N  
ANISOU 6215  N   ILE A 871    17836  17835  18870  -1456    370   -849       N  
ATOM   6216  CA  ILE A 871     -26.493  32.916 -22.311  1.00128.83           C  
ANISOU 6216  CA  ILE A 871    16065  15846  17040  -1512    481   -880       C  
ATOM   6217  C   ILE A 871     -25.478  32.819 -23.444  1.00127.33           C  
ANISOU 6217  C   ILE A 871    15921  15695  16763  -1456    374   -874       C  
ATOM   6218  O   ILE A 871     -24.868  31.772 -23.650  1.00127.15           O  
ANISOU 6218  O   ILE A 871    15998  15571  16743  -1475    451   -873       O  
ATOM   6219  CB  ILE A 871     -27.705  32.014 -22.618  1.00135.73           C  
ANISOU 6219  CB  ILE A 871    16845  16676  18051  -1660    573  -1052       C  
ATOM   6220  CG1 ILE A 871     -28.405  32.473 -23.898  1.00125.53           C  
ANISOU 6220  CG1 ILE A 871    15391  15536  16771  -1692    419  -1200       C  
ATOM   6221  CG2 ILE A 871     -28.677  32.002 -21.444  1.00144.15           C  
ANISOU 6221  CG2 ILE A 871    17877  17684  19212  -1720    705  -1054       C  
ATOM   6222  CD1 ILE A 871     -29.496  31.531 -24.363  1.00116.66           C  
ANISOU 6222  CD1 ILE A 871    14164  14381  15779  -1839    495  -1391       C  
ATOM   6223  N   ALA A 872     -25.298  33.913 -24.177  1.00139.88           N  
ANISOU 6223  N   ALA A 872    17443  17427  18277  -1385    203   -869       N  
ATOM   6224  CA  ALA A 872     -24.301  33.949 -25.240  1.00131.15           C  
ANISOU 6224  CA  ALA A 872    16383  16364  17082  -1320    100   -852       C  
ATOM   6225  C   ALA A 872     -22.905  33.743 -24.658  1.00126.70           C  
ANISOU 6225  C   ALA A 872    15980  15717  16445  -1235    147   -702       C  
ATOM   6226  O   ALA A 872     -22.018  33.209 -25.315  1.00130.66           O  
ANISOU 6226  O   ALA A 872    16557  16189  16900  -1209    134   -690       O  
ATOM   6227  CB  ALA A 872     -24.376  35.259 -26.004  1.00112.19           C  
ANISOU 6227  CB  ALA A 872    13890  14124  14612  -1247    -74   -856       C  
ATOM   6228  N   HIS A 873     -22.715  34.170 -23.415  1.00105.65           N  
ANISOU 6228  N   HIS A 873    13362  13018  13764  -1188    201   -591       N  
ATOM   6229  CA  HIS A 873     -21.454  33.939 -22.722  1.00109.60           C  
ANISOU 6229  CA  HIS A 873    14007  13443  14194  -1103    253   -456       C  
ATOM   6230  C   HIS A 873     -21.106  32.448 -22.669  1.00111.57           C  
ANISOU 6230  C   HIS A 873    14365  13550  14476  -1146    390   -467       C  
ATOM   6231  O   HIS A 873     -19.939  32.069 -22.775  1.00126.53           O  
ANISOU 6231  O   HIS A 873    16368  15403  16304  -1079    395   -394       O  
ATOM   6232  CB  HIS A 873     -21.513  34.526 -21.311  1.00105.84           C  
ANISOU 6232  CB  HIS A 873    13556  12952  13707  -1057    303   -358       C  
ATOM   6233  CG  HIS A 873     -20.574  33.878 -20.343  1.00123.08           C  
ANISOU 6233  CG  HIS A 873    15888  15027  15849   -995    412   -246       C  
ATOM   6234  CD2 HIS A 873     -20.761  32.869 -19.462  1.00116.37           C  
ANISOU 6234  CD2 HIS A 873    15126  14048  15043  -1025    579   -224       C  
ATOM   6235  ND1 HIS A 873     -19.260  34.271 -20.202  1.00118.00           N  
ANISOU 6235  ND1 HIS A 873    15323  14408  15105   -881    355   -142       N  
ATOM   6236  CE1 HIS A 873     -18.678  33.529 -19.277  1.00104.59           C  
ANISOU 6236  CE1 HIS A 873    13750  12608  13383   -837    471    -63       C  
ATOM   6237  NE2 HIS A 873     -19.567  32.671 -18.811  1.00101.23           N  
ANISOU 6237  NE2 HIS A 873    13338  12084  13041   -919    612   -105       N  
ATOM   6238  N   MET A 874     -22.126  31.608 -22.514  1.00 96.90           N  
ANISOU 6238  N   MET A 874    12477  11616  12725  -1259    506   -561       N  
ATOM   6239  CA  MET A 874     -21.933  30.164 -22.412  1.00113.69           C  
ANISOU 6239  CA  MET A 874    14707  13592  14897  -1311    661   -578       C  
ATOM   6240  C   MET A 874     -21.570  29.538 -23.752  1.00114.52           C  
ANISOU 6240  C   MET A 874    14814  13702  14996  -1341    612   -663       C  
ATOM   6241  O   MET A 874     -20.841  28.551 -23.813  1.00 99.43           O  
ANISOU 6241  O   MET A 874    13020  11684  13073  -1331    698   -633       O  
ATOM   6242  CB  MET A 874     -23.198  29.504 -21.870  1.00116.89           C  
ANISOU 6242  CB  MET A 874    15069  13911  15432  -1432    810   -666       C  
ATOM   6243  CG  MET A 874     -23.651  30.043 -20.529  1.00133.50           C  
ANISOU 6243  CG  MET A 874    17174  16002  17550  -1409    875   -589       C  
ATOM   6244  SD  MET A 874     -25.316  29.495 -20.122  1.00138.84           S  
ANISOU 6244  SD  MET A 874    17754  16609  18390  -1565   1024   -720       S  
ATOM   6245  CE  MET A 874     -25.189  27.751 -20.486  1.00 71.60           C  
ANISOU 6245  CE  MET A 874     9336   7918   9950  -1654   1198   -790       C  
ATOM   6246  N   VAL A 875     -22.090  30.112 -24.828  1.00116.59           N  
ANISOU 6246  N   VAL A 875    14947  14089  15263  -1372    474   -768       N  
ATOM   6247  CA  VAL A 875     -21.842  29.587 -26.159  1.00117.64           C  
ANISOU 6247  CA  VAL A 875    15070  14242  15386  -1400    416   -861       C  
ATOM   6248  C   VAL A 875     -20.445  29.972 -26.647  1.00120.30           C  
ANISOU 6248  C   VAL A 875    15489  14620  15601  -1280    318   -757       C  
ATOM   6249  O   VAL A 875     -19.818  29.231 -27.405  1.00 91.82           O  
ANISOU 6249  O   VAL A 875    11945  10971  11972  -1280    325   -781       O  
ATOM   6250  CB  VAL A 875     -22.878  30.119 -27.138  1.00116.34           C  
ANISOU 6250  CB  VAL A 875    14739  14211  15254  -1457    296  -1008       C  
ATOM   6251  CG1 VAL A 875     -22.727  31.597 -27.235  1.00136.66           C  
ANISOU 6251  CG1 VAL A 875    17252  16928  17745  -1359    141   -941       C  
ATOM   6252  CG2 VAL A 875     -22.710  29.471 -28.495  1.00104.89           C  
ANISOU 6252  CG2 VAL A 875    13278  12778  13796  -1491    246  -1120       C  
ATOM   6253  N   MET A 876     -19.963  31.137 -26.215  1.00126.11           N  
ANISOU 6253  N   MET A 876    16221  15434  16261  -1180    232   -648       N  
ATOM   6254  CA  MET A 876     -18.588  31.542 -26.494  1.00112.97           C  
ANISOU 6254  CA  MET A 876    14637  13799  14489  -1065    157   -542       C  
ATOM   6255  C   MET A 876     -17.635  30.698 -25.658  1.00117.56           C  
ANISOU 6255  C   MET A 876    15367  14251  15049  -1021    280   -439       C  
ATOM   6256  O   MET A 876     -16.782  29.996 -26.194  1.00129.78           O  
ANISOU 6256  O   MET A 876    16997  15749  16562   -997    297   -427       O  
ATOM   6257  CB  MET A 876     -18.369  33.031 -26.185  1.00 97.17           C  
ANISOU 6257  CB  MET A 876    12586  11908  12424   -978     45   -462       C  
ATOM   6258  CG  MET A 876     -18.861  33.998 -27.259  1.00 84.38           C  
ANISOU 6258  CG  MET A 876    10848  10428  10783   -972   -102   -533       C  
ATOM   6259  SD  MET A 876     -18.560  35.732 -26.838  1.00138.04           S  
ANISOU 6259  SD  MET A 876    17602  17335  17512   -869   -209   -432       S  
ATOM   6260  CE  MET A 876     -16.769  35.789 -26.848  1.00218.48           C  
ANISOU 6260  CE  MET A 876    27914  27493  27606   -760   -224   -308       C  
ATOM   6261  N   GLY A 877     -17.801  30.763 -24.341  1.00110.11           N  
ANISOU 6261  N   GLY A 877    14459  13257  14122  -1005    368   -366       N  
ATOM   6262  CA  GLY A 877     -16.917  30.081 -23.413  1.00112.17           C  
ANISOU 6262  CA  GLY A 877    14863  13409  14348   -940    482   -257       C  
ATOM   6263  C   GLY A 877     -16.816  28.579 -23.605  1.00106.60           C  
ANISOU 6263  C   GLY A 877    14252  12565  13685   -992    619   -293       C  
ATOM   6264  O   GLY A 877     -16.071  27.908 -22.890  1.00118.02           O  
ANISOU 6264  O   GLY A 877    15828  13914  15099   -930    722   -202       O  
ATOM   6265  N   THR A 878     -17.558  28.050 -24.572  1.00 79.33           N  
ANISOU 6265  N   THR A 878    10735   9103  10304  -1101    621   -428       N  
ATOM   6266  CA  THR A 878     -17.561  26.616 -24.838  1.00 75.12           C  
ANISOU 6266  CA  THR A 878    10283   8434   9826  -1167    758   -482       C  
ATOM   6267  C   THR A 878     -16.901  26.273 -26.174  1.00 86.84           C  
ANISOU 6267  C   THR A 878    11781   9943  11272  -1160    681   -533       C  
ATOM   6268  O   THR A 878     -16.388  25.170 -26.357  1.00 67.63           O  
ANISOU 6268  O   THR A 878     9452   7398   8845  -1166    780   -531       O  
ATOM   6269  CB  THR A 878     -18.993  26.051 -24.808  1.00 61.23           C  
ANISOU 6269  CB  THR A 878     8447   6618   8198  -1314    857   -617       C  
ATOM   6270  CG2 THR A 878     -18.995  24.573 -25.158  1.00 98.28           C  
ANISOU 6270  CG2 THR A 878    13221  11165  12957  -1390   1004   -685       C  
ATOM   6271  OG1 THR A 878     -19.543  26.220 -23.496  1.00 88.98           O  
ANISOU 6271  OG1 THR A 878    11972  10087  11750  -1317    958   -560       O  
ATOM   6272  N   THR A 879     -16.904  27.225 -27.101  1.00 98.48           N  
ANISOU 6272  N   THR A 879    13155  11561  12703  -1142    510   -573       N  
ATOM   6273  CA  THR A 879     -16.356  26.985 -28.432  1.00 92.15           C  
ANISOU 6273  CA  THR A 879    12358  10794  11861  -1134    430   -627       C  
ATOM   6274  C   THR A 879     -15.326  28.039 -28.824  1.00 93.44           C  
ANISOU 6274  C   THR A 879    12523  11068  11913  -1013    285   -537       C  
ATOM   6275  O   THR A 879     -14.703  27.949 -29.883  1.00 78.29           O  
ANISOU 6275  O   THR A 879    10620   9181   9945   -985    216   -559       O  
ATOM   6276  CB  THR A 879     -17.471  26.973 -29.488  1.00 93.19           C  
ANISOU 6276  CB  THR A 879    12360  10995  12053  -1239    367   -800       C  
ATOM   6277  CG2 THR A 879     -18.456  25.851 -29.208  1.00 83.20           C  
ANISOU 6277  CG2 THR A 879    11087   9614  10910  -1371    519   -910       C  
ATOM   6278  OG1 THR A 879     -18.169  28.222 -29.453  1.00 86.93           O  
ANISOU 6278  OG1 THR A 879    11442  10336  11253  -1229    251   -815       O  
ATOM   6279  N   ASN A 880     -15.150  29.029 -27.955  1.00104.58           N  
ANISOU 6279  N   ASN A 880    13918  12530  13288   -944    248   -440       N  
ATOM   6280  CA  ASN A 880     -14.298  30.185 -28.222  1.00 76.99           C  
ANISOU 6280  CA  ASN A 880    10408   9142   9702   -840    117   -362       C  
ATOM   6281  C   ASN A 880     -12.888  29.833 -28.694  1.00 82.01           C  
ANISOU 6281  C   ASN A 880    11143   9753  10266   -758    106   -298       C  
ATOM   6282  O   ASN A 880     -12.266  30.599 -29.430  1.00 60.01           O  
ANISOU 6282  O   ASN A 880     8332   7052   7416   -697     -5   -278       O  
ATOM   6283  CB  ASN A 880     -14.214  31.062 -26.969  1.00 67.24           C  
ANISOU 6283  CB  ASN A 880     9166   7934   8448   -781    117   -262       C  
ATOM   6284  CG  ASN A 880     -13.675  32.445 -27.258  1.00113.43           C  
ANISOU 6284  CG  ASN A 880    14965  13905  14228   -698    -19   -211       C  
ATOM   6285  ND2 ASN A 880     -12.784  32.924 -26.395  1.00129.28           N  
ANISOU 6285  ND2 ASN A 880    17021  15915  16184   -608    -17   -101       N  
ATOM   6286  OD1 ASN A 880     -14.061  33.083 -28.238  1.00135.29           O  
ANISOU 6286  OD1 ASN A 880    17651  16764  16989   -712   -121   -273       O  
ATOM   6287  N   GLN A 881     -12.389  28.672 -28.279  1.00 87.40           N  
ANISOU 6287  N   GLN A 881    11938  10314  10957   -755    228   -265       N  
ATOM   6288  CA  GLN A 881     -10.979  28.348 -28.474  1.00 59.89           C  
ANISOU 6288  CA  GLN A 881     8554   6801   7401   -662    230   -187       C  
ATOM   6289  C   GLN A 881     -10.704  27.110 -29.333  1.00 75.22           C  
ANISOU 6289  C   GLN A 881    10567   8659   9356   -698    290   -244       C  
ATOM   6290  O   GLN A 881      -9.689  26.436 -29.148  1.00 90.05           O  
ANISOU 6290  O   GLN A 881    12554  10466  11197   -633    352   -175       O  
ATOM   6291  CB  GLN A 881     -10.281  28.220 -27.115  1.00 44.84           C  
ANISOU 6291  CB  GLN A 881     6735   4839   5463   -577    308    -65       C  
ATOM   6292  CG  GLN A 881     -10.415  29.460 -26.238  1.00 59.39           C  
ANISOU 6292  CG  GLN A 881     8515   6767   7285   -531    247     -6       C  
ATOM   6293  CD  GLN A 881     -10.115  29.184 -24.775  1.00 91.53           C  
ANISOU 6293  CD  GLN A 881    12665  10775  11339   -469    345     88       C  
ATOM   6294  NE2 GLN A 881     -10.290  30.198 -23.933  1.00 91.71           N  
ANISOU 6294  NE2 GLN A 881    12636  10865  11346   -433    302    133       N  
ATOM   6295  OE1 GLN A 881      -9.736  28.071 -24.405  1.00 67.89           O  
ANISOU 6295  OE1 GLN A 881     9781   7673   8342   -448    461    121       O  
ATOM   6296  N   PHE A 882     -11.596  26.814 -30.275  1.00 92.57           N  
ANISOU 6296  N   PHE A 882    12699  10867  11604   -797    270   -373       N  
ATOM   6297  CA  PHE A 882     -11.347  25.738 -31.235  1.00 87.79           C  
ANISOU 6297  CA  PHE A 882    12151  10197  11009   -834    311   -443       C  
ATOM   6298  C   PHE A 882     -10.545  26.260 -32.420  1.00 84.59           C  
ANISOU 6298  C   PHE A 882    11733   9881  10525   -771    185   -442       C  
ATOM   6299  O   PHE A 882     -10.712  27.404 -32.832  1.00 71.48           O  
ANISOU 6299  O   PHE A 882     9985   8343   8831   -745     60   -447       O  
ATOM   6300  CB  PHE A 882     -12.653  25.106 -31.718  1.00101.59           C  
ANISOU 6300  CB  PHE A 882    13833  11916  12850   -972    352   -599       C  
ATOM   6301  CG  PHE A 882     -13.306  24.216 -30.702  1.00114.89           C  
ANISOU 6301  CG  PHE A 882    15560  13470  14623  -1045    519   -610       C  
ATOM   6302  CD1 PHE A 882     -14.636  24.391 -30.356  1.00 98.07           C  
ANISOU 6302  CD1 PHE A 882    13330  11354  12578  -1143    541   -695       C  
ATOM   6303  CD2 PHE A 882     -12.585  23.207 -30.086  1.00137.12           C  
ANISOU 6303  CD2 PHE A 882    18518  16147  17436  -1009    661   -532       C  
ATOM   6304  CE1 PHE A 882     -15.239  23.572 -29.418  1.00 79.19           C  
ANISOU 6304  CE1 PHE A 882    10982   8835  10273  -1211    709   -705       C  
ATOM   6305  CE2 PHE A 882     -13.180  22.385 -29.146  1.00129.33           C  
ANISOU 6305  CE2 PHE A 882    17582  15029  16527  -1068    830   -535       C  
ATOM   6306  CZ  PHE A 882     -14.509  22.567 -28.813  1.00 86.73           C  
ANISOU 6306  CZ  PHE A 882    12087   9643  11222  -1173    857   -622       C  
ATOM   6307  N   SER A 883      -9.681  25.416 -32.968  1.00 96.41           N  
ANISOU 6307  N   SER A 883    13324  11313  11994   -743    226   -432       N  
ATOM   6308  CA  SER A 883      -8.759  25.848 -34.013  1.00 71.28           C  
ANISOU 6308  CA  SER A 883    10149   8201   8733   -671    125   -414       C  
ATOM   6309  C   SER A 883      -8.711  24.873 -35.178  1.00 87.41           C  
ANISOU 6309  C   SER A 883    12231  10200  10782   -717    145   -510       C  
ATOM   6310  O   SER A 883      -7.950  25.059 -36.128  1.00 72.24           O  
ANISOU 6310  O   SER A 883    10328   8322   8796   -661     77   -503       O  
ATOM   6311  CB  SER A 883      -7.357  26.016 -33.428  1.00 78.26           C  
ANISOU 6311  CB  SER A 883    11117   9067   9553   -551    139   -274       C  
ATOM   6312  OG  SER A 883      -6.958  24.851 -32.726  1.00 85.92           O  
ANISOU 6312  OG  SER A 883    12198   9906  10542   -542    277   -231       O  
ATOM   6313  N   THR A 884      -9.526  23.828 -35.103  1.00120.93           N  
ANISOU 6313  N   THR A 884    16488  14353  15106   -820    246   -604       N  
ATOM   6314  CA  THR A 884      -9.523  22.790 -36.123  1.00112.64           C  
ANISOU 6314  CA  THR A 884    15479  13247  14073   -874    283   -706       C  
ATOM   6315  C   THR A 884     -10.603  23.044 -37.167  1.00100.76           C  
ANISOU 6315  C   THR A 884    13857  11836  12591   -956    191   -865       C  
ATOM   6316  O   THR A 884     -11.670  23.573 -36.855  1.00 93.03           O  
ANISOU 6316  O   THR A 884    12774  10915  11659  -1013    158   -921       O  
ATOM   6317  CB  THR A 884      -9.737  21.401 -35.496  1.00142.14           C  
ANISOU 6317  CB  THR A 884    19305  16816  17887   -942    464   -728       C  
ATOM   6318  CG2 THR A 884      -9.440  20.306 -36.508  1.00165.62           C  
ANISOU 6318  CG2 THR A 884    22344  19718  20865   -977    511   -811       C  
ATOM   6319  OG1 THR A 884      -8.876  21.251 -34.361  1.00148.91           O  
ANISOU 6319  OG1 THR A 884    20263  17598  18717   -854    548   -576       O  
ATOM   6320  N   ARG A 885     -10.316  22.674 -38.411  1.00121.49           N  
ANISOU 6320  N   ARG A 885    16499  14481  15181   -956    147   -940       N  
ATOM   6321  CA  ARG A 885     -11.294  22.796 -39.484  1.00120.79           C  
ANISOU 6321  CA  ARG A 885    16306  14486  15104  -1024     59  -1103       C  
ATOM   6322  C   ARG A 885     -12.482  21.893 -39.195  1.00124.43           C  
ANISOU 6322  C   ARG A 885    16725  14872  15683  -1166    158  -1242       C  
ATOM   6323  O   ARG A 885     -13.634  22.275 -39.403  1.00 89.93           O  
ANISOU 6323  O   ARG A 885    12229  10587  11353  -1233     98  -1359       O  
ATOM   6324  CB  ARG A 885     -10.665  22.414 -40.824  1.00 97.65           C  
ANISOU 6324  CB  ARG A 885    13422  11574  12108   -991     11  -1154       C  
ATOM   6325  CG  ARG A 885      -9.298  23.024 -41.046  1.00 94.07           C  
ANISOU 6325  CG  ARG A 885    13038  11151  11551   -856    -43  -1010       C  
ATOM   6326  CD  ARG A 885      -9.013  23.215 -42.521  1.00 96.82           C  
ANISOU 6326  CD  ARG A 885    13380  11586  11820   -813   -145  -1073       C  
ATOM   6327  NE  ARG A 885      -8.608  24.587 -42.807  1.00 90.50           N  
ANISOU 6327  NE  ARG A 885    12541  10909  10935   -708   -267   -989       N  
ATOM   6328  CZ  ARG A 885      -8.269  25.029 -44.012  1.00118.10           C  
ANISOU 6328  CZ  ARG A 885    16036  14492  14345   -642   -362  -1011       C  
ATOM   6329  NH1 ARG A 885      -8.283  24.204 -45.050  1.00128.75           N1+
ANISOU 6329  NH1 ARG A 885    17417  15827  15677   -669   -359  -1118       N1+
ATOM   6330  NH2 ARG A 885      -7.915  26.296 -44.180  1.00119.77           N  
ANISOU 6330  NH2 ARG A 885    16218  14802  14488   -548   -452   -927       N  
ATOM   6331  N   THR A 886     -12.184  20.694 -38.703  1.00143.88           N  
ANISOU 6331  N   THR A 886    19292  17173  18201  -1208    318  -1229       N  
ATOM   6332  CA  THR A 886     -13.205  19.707 -38.376  1.00134.59           C  
ANISOU 6332  CA  THR A 886    18095  15894  17148  -1348    447  -1356       C  
ATOM   6333  C   THR A 886     -14.013  20.140 -37.155  1.00118.61           C  
ANISOU 6333  C   THR A 886    16012  13863  15193  -1387    493  -1323       C  
ATOM   6334  O   THR A 886     -15.225  19.928 -37.096  1.00121.40           O  
ANISOU 6334  O   THR A 886    16269  14217  15640  -1503    524  -1459       O  
ATOM   6335  CB  THR A 886     -12.582  18.324 -38.111  1.00129.60           C  
ANISOU 6335  CB  THR A 886    17612  15076  16554  -1368    624  -1330       C  
ATOM   6336  CG2 THR A 886     -11.294  18.157 -38.907  1.00118.64           C  
ANISOU 6336  CG2 THR A 886    16322  13689  15067  -1268    582  -1265       C  
ATOM   6337  OG1 THR A 886     -12.301  18.180 -36.714  1.00139.26           O  
ANISOU 6337  OG1 THR A 886    18916  16195  17803  -1335    748  -1190       O  
ATOM   6338  N   ARG A 887     -13.337  20.745 -36.182  1.00 94.47           N  
ANISOU 6338  N   ARG A 887    13007  10800  12087  -1289    498  -1148       N  
ATOM   6339  CA  ARG A 887     -14.009  21.257 -34.991  1.00 94.20           C  
ANISOU 6339  CA  ARG A 887    12923  10766  12101  -1308    534  -1101       C  
ATOM   6340  C   ARG A 887     -15.044  22.305 -35.383  1.00102.01           C  
ANISOU 6340  C   ARG A 887    13747  11914  13099  -1343    394  -1192       C  
ATOM   6341  O   ARG A 887     -15.944  22.635 -34.604  1.00 90.39           O  
ANISOU 6341  O   ARG A 887    12203  10451  11691  -1394    422  -1209       O  
ATOM   6342  CB  ARG A 887     -12.995  21.847 -34.006  1.00 88.61           C  
ANISOU 6342  CB  ARG A 887    12294  10052  11320  -1179    536   -903       C  
ATOM   6343  CG  ARG A 887     -12.374  20.826 -33.064  1.00 83.01           C  
ANISOU 6343  CG  ARG A 887    11734   9174  10630  -1155    713   -807       C  
ATOM   6344  CD  ARG A 887     -13.411  20.309 -32.085  1.00 89.70           C  
ANISOU 6344  CD  ARG A 887    12573   9922  11586  -1251    859   -845       C  
ATOM   6345  NE  ARG A 887     -12.919  19.194 -31.283  1.00100.66           N  
ANISOU 6345  NE  ARG A 887    14114  11135  12998  -1231   1048   -768       N  
ATOM   6346  CZ  ARG A 887     -13.674  18.495 -30.441  1.00 97.25           C  
ANISOU 6346  CZ  ARG A 887    13712  10577  12661  -1309   1217   -791       C  
ATOM   6347  NH1 ARG A 887     -14.956  18.800 -30.294  1.00 87.54           N1+
ANISOU 6347  NH1 ARG A 887    12359   9381  11519  -1419   1215   -896       N1+
ATOM   6348  NH2 ARG A 887     -13.151  17.491 -29.749  1.00 85.65           N  
ANISOU 6348  NH2 ARG A 887    12396   8946  11200  -1273   1393   -709       N  
ATOM   6349  N   LEU A 888     -14.904  22.821 -36.600  1.00103.61           N  
ANISOU 6349  N   LEU A 888    13894  12240  13231  -1307    246  -1250       N  
ATOM   6350  CA  LEU A 888     -15.855  23.776 -37.154  1.00120.40           C  
ANISOU 6350  CA  LEU A 888    15869  14527  15351  -1324    105  -1345       C  
ATOM   6351  C   LEU A 888     -17.034  23.060 -37.785  1.00142.84           C  
ANISOU 6351  C   LEU A 888    18617  17373  18281  -1457    124  -1557       C  
ATOM   6352  O   LEU A 888     -18.186  23.451 -37.598  1.00147.47           O  
ANISOU 6352  O   LEU A 888    19077  18028  18928  -1521     94  -1649       O  
ATOM   6353  CB  LEU A 888     -15.180  24.668 -38.192  1.00119.48           C  
ANISOU 6353  CB  LEU A 888    15742  14542  15112  -1213    -56  -1309       C  
ATOM   6354  CG  LEU A 888     -14.523  25.900 -37.589  1.00125.07           C  
ANISOU 6354  CG  LEU A 888    16463  15312  15748  -1097   -121  -1141       C  
ATOM   6355  CD1 LEU A 888     -14.546  27.033 -38.586  1.00121.04           C  
ANISOU 6355  CD1 LEU A 888    15878  14962  15148  -1021   -288  -1156       C  
ATOM   6356  CD2 LEU A 888     -15.297  26.284 -36.353  1.00129.32           C  
ANISOU 6356  CD2 LEU A 888    16945  15838  16355  -1138    -74  -1112       C  
ATOM   6357  N   GLU A 889     -16.732  22.011 -38.541  1.00150.76           N  
ANISOU 6357  N   GLU A 889    19681  18307  19295  -1497    174  -1641       N  
ATOM   6358  CA  GLU A 889     -17.755  21.191 -39.166  1.00165.18           C  
ANISOU 6358  CA  GLU A 889    21427  20124  21211  -1631    206  -1856       C  
ATOM   6359  C   GLU A 889     -18.809  20.784 -38.141  1.00165.68           C  
ANISOU 6359  C   GLU A 889    21435  20103  21413  -1752    337  -1916       C  
ATOM   6360  O   GLU A 889     -19.963  20.536 -38.488  1.00176.22           O  
ANISOU 6360  O   GLU A 889    22646  21479  22833  -1864    333  -2102       O  
ATOM   6361  CB  GLU A 889     -17.122  19.952 -39.804  1.00186.00           C  
ANISOU 6361  CB  GLU A 889    24172  22646  23853  -1660    293  -1907       C  
ATOM   6362  CG  GLU A 889     -15.997  20.273 -40.781  1.00203.37           C  
ANISOU 6362  CG  GLU A 889    26440  24911  25918  -1539    182  -1839       C  
ATOM   6363  CD  GLU A 889     -15.338  19.030 -41.353  1.00208.24           C  
ANISOU 6363  CD  GLU A 889    27173  25408  26542  -1565    276  -1881       C  
ATOM   6364  OE1 GLU A 889     -15.711  17.911 -40.944  1.00199.87           O  
ANISOU 6364  OE1 GLU A 889    26149  24202  25591  -1675    437  -1954       O  
ATOM   6365  OE2 GLU A 889     -14.443  19.175 -42.213  1.00214.16           O1-
ANISOU 6365  OE2 GLU A 889    27981  26203  27188  -1474    198  -1840       O1-
ATOM   6366  N   GLU A 890     -18.404  20.725 -36.876  1.00155.89           N  
ANISOU 6366  N   GLU A 890    20287  18750  20195  -1726    456  -1760       N  
ATOM   6367  CA  GLU A 890     -19.322  20.403 -35.791  1.00151.68           C  
ANISOU 6367  CA  GLU A 890    19719  18128  19785  -1825    593  -1789       C  
ATOM   6368  C   GLU A 890     -20.262  21.566 -35.497  1.00143.52           C  
ANISOU 6368  C   GLU A 890    18533  17237  18760  -1826    485  -1812       C  
ATOM   6369  O   GLU A 890     -21.470  21.466 -35.712  1.00170.68           O  
ANISOU 6369  O   GLU A 890    21839  20722  22291  -1935    481  -1981       O  
ATOM   6370  CB  GLU A 890     -18.553  20.022 -34.524  1.00150.22           C  
ANISOU 6370  CB  GLU A 890    19689  17786  19601  -1774    749  -1605       C  
ATOM   6371  CG  GLU A 890     -17.734  18.750 -34.655  1.00145.13           C  
ANISOU 6371  CG  GLU A 890    19200  16978  18965  -1779    889  -1584       C  
ATOM   6372  CD  GLU A 890     -17.110  18.320 -33.342  1.00132.94           C  
ANISOU 6372  CD  GLU A 890    17805  15281  17426  -1726   1054  -1413       C  
ATOM   6373  OE1 GLU A 890     -17.441  18.921 -32.296  1.00133.44           O  
ANISOU 6373  OE1 GLU A 890    17844  15355  17500  -1705   1072  -1330       O  
ATOM   6374  OE2 GLU A 890     -16.289  17.379 -33.357  1.00109.54           O1-
ANISOU 6374  OE2 GLU A 890    14985  12188  14449  -1698   1164  -1362       O1-
ATOM   6375  N   VAL A 891     -19.700  22.667 -35.008  1.00117.41           N  
ANISOU 6375  N   VAL A 891    15247  14003  15362  -1704    399  -1646       N  
ATOM   6376  CA  VAL A 891     -20.489  23.848 -34.665  1.00119.82           C  
ANISOU 6376  CA  VAL A 891    15423  14439  15666  -1689    299  -1645       C  
ATOM   6377  C   VAL A 891     -21.464  24.213 -35.781  1.00143.00           C  
ANISOU 6377  C   VAL A 891    18195  17530  18609  -1735    161  -1830       C  
ATOM   6378  O   VAL A 891     -22.521  24.795 -35.531  1.00135.84           O  
ANISOU 6378  O   VAL A 891    17155  16707  17750  -1775    120  -1899       O  
ATOM   6379  CB  VAL A 891     -19.588  25.056 -34.357  1.00 97.25           C  
ANISOU 6379  CB  VAL A 891    12606  11659  12686  -1539    193  -1458       C  
ATOM   6380  CG1 VAL A 891     -20.433  26.257 -33.950  1.00 68.11