CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 21051323292462246

Job options:

ID        	=	 21051323292462246
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:


REMARK AtomGroup 4C5Y
ATOM      1  N   ASP A  45      19.073  -7.187 -30.818  1.00115.71           N  
ANISOU    1  N   ASP A  45    10748  16892  16324    565   1695  -1859       N  
ATOM      2  CA  ASP A  45      19.077  -6.937 -32.301  1.00120.19           C  
ANISOU    2  CA  ASP A  45    10914  17750  17003    568   1807  -1896       C  
ATOM      3  C   ASP A  45      17.989  -5.924 -32.736  1.00117.70           C  
ANISOU    3  C   ASP A  45    10612  17575  16532    261   1981  -2004       C  
ATOM      4  O   ASP A  45      18.322  -4.830 -33.210  1.00119.92           O  
ANISOU    4  O   ASP A  45    10814  17905  16846    290   2234  -2136       O  
ATOM      5  CB  ASP A  45      19.054  -8.261 -33.148  1.00121.64           C  
ANISOU    5  CB  ASP A  45    10772  18147  17299    610   1578  -1744       C  
ATOM      6  CG  ASP A  45      17.873  -9.203 -32.822  1.00119.05           C  
ANISOU    6  CG  ASP A  45    10568  17859  16806    340   1342  -1635       C  
ATOM      7  OD1 ASP A  45      17.159  -8.996 -31.820  1.00114.74           O  
ANISOU    7  OD1 ASP A  45    10366  17146  16083    167   1328  -1656       O  
ATOM      8  OD2 ASP A  45      17.662 -10.172 -33.590  1.00120.45           O1-
ANISOU    8  OD2 ASP A  45    10492  18240  17033    299   1169  -1523       O1-
ATOM      9  N   GLU A  46      16.715  -6.278 -32.553  1.00109.25           N  
ANISOU    9  N   GLU A  46     9660  16558  15290    -33   1853  -1950       N  
ATOM     10  CA  GLU A  46      15.584  -5.472 -33.039  1.00103.94           C  
ANISOU   10  CA  GLU A  46     8997  16030  14463   -347   1981  -2027       C  
ATOM     11  C   GLU A  46      14.497  -5.355 -31.982  1.00 98.27           C  
ANISOU   11  C   GLU A  46     8663  15145  13530   -588   1908  -2011       C  
ATOM     12  O   GLU A  46      14.101  -6.356 -31.396  1.00 97.37           O  
ANISOU   12  O   GLU A  46     8672  14954  13371   -623   1694  -1903       O  
ATOM     13  CB  GLU A  46      14.969  -6.115 -34.293  1.00104.37           C  
ANISOU   13  CB  GLU A  46     8717  16398  14542   -497   1893  -1964       C  
ATOM     14  CG  GLU A  46      15.921  -6.574 -35.377  1.00107.35           C  
ANISOU   14  CG  GLU A  46     8665  16978  15146   -264   1887  -1927       C  
ATOM     15  CD  GLU A  46      16.329  -5.477 -36.346  1.00109.56           C  
ANISOU   15  CD  GLU A  46     8692  17425  15512   -220   2168  -2060       C  
ATOM     16  OE1 GLU A  46      16.870  -4.440 -35.908  1.00108.37           O  
ANISOU   16  OE1 GLU A  46     8699  17114  15363   -119   2383  -2185       O  
ATOM     17  OE2 GLU A  46      16.112  -5.663 -37.558  1.00109.90           O1-
ANISOU   17  OE2 GLU A  46     8375  17767  15615   -298   2177  -2041       O1-
ATOM     18  N   ALA A  47      13.982  -4.152 -31.755  1.00 95.69           N  
ANISOU   18  N   ALA A  47     8521  14766  13067   -761   2087  -2115       N  
ATOM     19  CA  ALA A  47      12.930  -3.952 -30.747  1.00 92.24           C  
ANISOU   19  CA  ALA A  47     8444  14170  12434   -980   2024  -2094       C  
ATOM     20  C   ALA A  47      11.600  -4.645 -31.104  1.00 91.31           C  
ANISOU   20  C   ALA A  47     8316  14175  12203  -1247   1879  -2017       C  
ATOM     21  O   ALA A  47      11.174  -4.613 -32.254  1.00 93.68           O  
ANISOU   21  O   ALA A  47     8379  14713  12501  -1390   1923  -2034       O  
ATOM     22  CB  ALA A  47      12.694  -2.467 -30.541  1.00 91.47           C  
ANISOU   22  CB  ALA A  47     8526  14011  12216  -1114   2245  -2214       C  
ATOM     23  N   LYS A  48      10.942  -5.251 -30.112  1.00 87.08           N  
ANISOU   23  N   LYS A  48     8044  13474  11570  -1320   1716  -1937       N  
ATOM     24  CA  LYS A  48       9.642  -5.906 -30.308  1.00 84.66           C  
ANISOU   24  CA  LYS A  48     7788  13236  11141  -1574   1587  -1870       C  
ATOM     25  C   LYS A  48       8.512  -4.904 -30.082  1.00 81.35           C  
ANISOU   25  C   LYS A  48     7603  12764  10543  -1840   1693  -1922       C  
ATOM     26  O   LYS A  48       8.258  -4.498 -28.955  1.00 74.85           O  
ANISOU   26  O   LYS A  48     7076  11724   9639  -1847   1693  -1918       O  
ATOM     27  CB  LYS A  48       9.488  -7.078 -29.348  1.00 83.20           C  
ANISOU   27  CB  LYS A  48     7774  12894  10944  -1515   1375  -1764       C  
ATOM     28  CG  LYS A  48       8.283  -7.970 -29.614  1.00 84.48           C  
ANISOU   28  CG  LYS A  48     7971  13127  10999  -1749   1234  -1693       C  
ATOM     29  CD  LYS A  48       8.098  -8.980 -28.492  1.00 86.98           C  
ANISOU   29  CD  LYS A  48     8508  13254  11285  -1697   1060  -1607       C  
ATOM     30  CE  LYS A  48       8.094 -10.423 -28.997  1.00 90.54           C  
ANISOU   30  CE  LYS A  48     8802  13825  11773  -1706    873  -1515       C  
ATOM     31  NZ  LYS A  48       7.003 -11.196 -28.349  1.00 88.04           N1+
ANISOU   31  NZ  LYS A  48     8733  13395  11324  -1875    755  -1460       N1+
ATOM     32  N   VAL A  49       7.838  -4.517 -31.165  1.00 83.03           N  
ANISOU   32  N   VAL A  49     7675  13180  10692  -2063   1777  -1963       N  
ATOM     33  CA  VAL A  49       6.836  -3.446 -31.133  1.00 81.96           C  
ANISOU   33  CA  VAL A  49     7739  13012  10388  -2324   1897  -2018       C  
ATOM     34  C   VAL A  49       5.401  -3.986 -31.203  1.00 78.62           C  
ANISOU   34  C   VAL A  49     7456  12595   9820  -2597   1782  -1954       C  
ATOM     35  O   VAL A  49       5.089  -4.883 -31.985  1.00 78.91           O  
ANISOU   35  O   VAL A  49     7316  12796   9869  -2685   1684  -1908       O  
ATOM     36  CB  VAL A  49       7.068  -2.415 -32.269  1.00 86.19           C  
ANISOU   36  CB  VAL A  49     8058  13758  10929  -2412   2111  -2126       C  
ATOM     37  CG1 VAL A  49       6.049  -1.280 -32.196  1.00 86.63           C  
ANISOU   37  CG1 VAL A  49     8346  13773  10794  -2695   2230  -2176       C  
ATOM     38  CG2 VAL A  49       8.478  -1.841 -32.211  1.00 87.98           C  
ANISOU   38  CG2 VAL A  49     8165  13965  11297  -2140   2251  -2202       C  
ATOM     39  N   THR A  50       4.545  -3.440 -30.346  1.00 75.39           N  
ANISOU   39  N   THR A  50     7377  11994   9274  -2727   1791  -1946       N  
ATOM     40  CA  THR A  50       3.137  -3.798 -30.299  1.00 73.08           C  
ANISOU   40  CA  THR A  50     7272  11656   8837  -2980   1707  -1894       C  
ATOM     41  C   THR A  50       2.337  -2.500 -30.323  1.00 73.11           C  
ANISOU   41  C   THR A  50     7467  11618   8693  -3205   1843  -1944       C  
ATOM     42  O   THR A  50       2.659  -1.548 -29.596  1.00 71.22           O  
ANISOU   42  O   THR A  50     7381  11243   8436  -3133   1928  -1975       O  
ATOM     43  CB  THR A  50       2.806  -4.605 -29.022  1.00 69.65           C  
ANISOU   43  CB  THR A  50     7088  10982   8392  -2887   1550  -1809       C  
ATOM     44  CG2 THR A  50       1.335  -4.941 -28.967  1.00 69.02           C  
ANISOU   44  CG2 THR A  50     7221  10834   8168  -3137   1485  -1764       C  
ATOM     45  OG1 THR A  50       3.571  -5.816 -29.005  1.00 68.12           O  
ANISOU   45  OG1 THR A  50     6729  10828   8323  -2693   1421  -1760       O  
ATOM     46  N   ILE A  51       1.313  -2.451 -31.169  1.00 74.08           N  
ANISOU   46  N   ILE A  51     7588  11860   8699  -3489   1860  -1948       N  
ATOM     47  CA  ILE A  51       0.470  -1.269 -31.253  1.00 73.62           C  
ANISOU   47  CA  ILE A  51     7724  11762   8484  -3731   1976  -1985       C  
ATOM     48  C   ILE A  51      -0.898  -1.627 -30.735  1.00 71.85           C  
ANISOU   48  C   ILE A  51     7803  11365   8129  -3909   1872  -1911       C  
ATOM     49  O   ILE A  51      -1.413  -2.700 -31.034  1.00 71.92           O  
ANISOU   49  O   ILE A  51     7784  11412   8129  -3980   1758  -1865       O  
ATOM     50  CB  ILE A  51       0.365  -0.727 -32.691  1.00 76.61           C  
ANISOU   50  CB  ILE A  51     7876  12416   8815  -3947   2114  -2060       C  
ATOM     51  CG1 ILE A  51       1.777  -0.601 -33.293  1.00 78.26           C  
ANISOU   51  CG1 ILE A  51     7735  12813   9189  -3733   2214  -2131       C  
ATOM     52  CG2 ILE A  51      -0.382   0.613 -32.695  1.00 77.48           C  
ANISOU   52  CG2 ILE A  51     8210  12472   8759  -4190   2246  -2101       C  
ATOM     53  CD1 ILE A  51       1.910   0.300 -34.510  1.00 80.96           C  
ANISOU   53  CD1 ILE A  51     7859  13404   9498  -3895   2409  -2229       C  
ATOM     54  N   ILE A  52      -1.470  -0.727 -29.945  1.00 70.94           N  
ANISOU   54  N   ILE A  52     7982  11056   7917  -3976   1908  -1896       N  
ATOM     55  CA  ILE A  52      -2.801  -0.920 -29.400  1.00 70.89           C  
ANISOU   55  CA  ILE A  52     8284  10858   7792  -4130   1826  -1824       C  
ATOM     56  C   ILE A  52      -3.683   0.309 -29.631  1.00 73.27           C  
ANISOU   56  C   ILE A  52     8785  11125   7931  -4395   1926  -1839       C  
ATOM     57  O   ILE A  52      -3.381   1.396 -29.124  1.00 72.25           O  
ANISOU   57  O   ILE A  52     8757  10919   7776  -4360   2003  -1855       O  
ATOM     58  CB  ILE A  52      -2.758  -1.174 -27.893  1.00 68.14           C  
ANISOU   58  CB  ILE A  52     8151  10245   7493  -3918   1728  -1752       C  
ATOM     59  CG1 ILE A  52      -1.757  -2.278 -27.546  1.00 66.37           C  
ANISOU   59  CG1 ILE A  52     7751  10040   7425  -3647   1635  -1737       C  
ATOM     60  CG2 ILE A  52      -4.148  -1.546 -27.399  1.00 68.17           C  
ANISOU   60  CG2 ILE A  52     8446  10057   7398  -4054   1644  -1676       C  
ATOM     61  CD1 ILE A  52      -1.411  -2.320 -26.071  1.00 63.75           C  
ANISOU   61  CD1 ILE A  52     7584   9484   7151  -3421   1570  -1683       C  
ATOM     62  N   TYR A  53      -4.777   0.122 -30.377  1.00 73.95           N  
ANISOU   62  N   TYR A  53     8942  11261   7895  -4672   1918  -1830       N  
ATOM     63  CA  TYR A  53      -5.754   1.177 -30.595  1.00 73.30           C  
ANISOU   63  CA  TYR A  53     9085  11124   7643  -4948   1995  -1830       C  
ATOM     64  C   TYR A  53      -6.860   1.008 -29.573  1.00 70.06           C  
ANISOU   64  C   TYR A  53     9036  10417   7168  -4967   1892  -1733       C  
ATOM     65  O   TYR A  53      -7.280  -0.108 -29.274  1.00 67.13           O  
ANISOU   65  O   TYR A  53     8722   9953   6831  -4910   1782  -1686       O  
ATOM     66  CB  TYR A  53      -6.346   1.106 -31.992  1.00 76.22           C  
ANISOU   66  CB  TYR A  53     9345  11709   7906  -5256   2050  -1874       C  
ATOM     67  CG  TYR A  53      -5.322   1.044 -33.102  1.00 78.06           C  
ANISOU   67  CG  TYR A  53     9174  12262   8222  -5232   2139  -1961       C  
ATOM     68  CD1 TYR A  53      -4.757  -0.171 -33.493  1.00 77.93           C  
ANISOU   68  CD1 TYR A  53     8891  12387   8330  -5098   2055  -1957       C  
ATOM     69  CD2 TYR A  53      -4.946   2.196 -33.795  1.00 79.73           C  
ANISOU   69  CD2 TYR A  53     9268  12640   8384  -5351   2309  -2044       C  
ATOM     70  CE1 TYR A  53      -3.831  -0.228 -34.535  1.00 79.22           C  
ANISOU   70  CE1 TYR A  53     8666  12851   8585  -5063   2131  -2024       C  
ATOM     71  CE2 TYR A  53      -4.020   2.147 -34.840  1.00 80.66           C  
ANISOU   71  CE2 TYR A  53     8998  13059   8592  -5316   2406  -2126       C  
ATOM     72  CZ  TYR A  53      -3.461   0.940 -35.217  1.00 79.89           C  
ANISOU   72  CZ  TYR A  53     8621  13099   8633  -5165   2314  -2111       C  
ATOM     73  OH  TYR A  53      -2.523   0.901 -36.244  1.00 78.33           O  
ANISOU   73  OH  TYR A  53     8020  13198   8542  -5108   2405  -2180       O  
ATOM     74  N   ALA A  54      -7.342   2.130 -29.066  1.00 69.46           N  
ANISOU   74  N   ALA A  54     9203  10194   6995  -5054   1933  -1702       N  
ATOM     75  CA  ALA A  54      -8.270   2.127 -27.953  1.00 68.71           C  
ANISOU   75  CA  ALA A  54     9439   9804   6864  -5023   1839  -1598       C  
ATOM     76  C   ALA A  54      -9.424   3.058 -28.223  1.00 70.73           C  
ANISOU   76  C   ALA A  54     9960   9973   6943  -5314   1880  -1566       C  
ATOM     77  O   ALA A  54      -9.206   4.179 -28.682  1.00 72.72           O  
ANISOU   77  O   ALA A  54    10193  10328   7110  -5459   1985  -1608       O  
ATOM     78  CB  ALA A  54      -7.560   2.578 -26.707  1.00 67.08           C  
ANISOU   78  CB  ALA A  54     9280   9462   6744  -4768   1811  -1558       C  
ATOM     79  N   GLY A  55     -10.641   2.598 -27.928  1.00 70.76           N  
ANISOU   79  N   GLY A  55    10222   9777   6887  -5401   1802  -1492       N  
ATOM     80  CA  GLY A  55     -11.838   3.430 -28.049  1.00 71.87           C  
ANISOU   80  CA  GLY A  55    10664   9781   6861  -5662   1821  -1440       C  
ATOM     81  C   GLY A  55     -11.767   4.572 -27.067  1.00 71.10           C  
ANISOU   81  C   GLY A  55    10737   9527   6748  -5583   1813  -1369       C  
ATOM     82  O   GLY A  55     -12.062   5.730 -27.396  1.00 71.23           O  
ANISOU   82  O   GLY A  55    10873   9562   6631  -5796   1877  -1365       O  
ATOM     83  N   LEU A  56     -11.331   4.220 -25.863  1.00 70.12           N  
ANISOU   83  N   LEU A  56    10618   9267   6760  -5284   1729  -1311       N  
ATOM     84  CA  LEU A  56     -11.092   5.162 -24.781  1.00 68.49           C  
ANISOU   84  CA  LEU A  56    10532   8925   6563  -5167   1700  -1235       C  
ATOM     85  C   LEU A  56      -9.774   4.808 -24.109  1.00 65.22           C  
ANISOU   85  C   LEU A  56     9900   8574   6304  -4868   1681  -1264       C  
ATOM     86  O   LEU A  56      -9.548   3.651 -23.746  1.00 62.42           O  
ANISOU   86  O   LEU A  56     9452   8191   6075  -4671   1618  -1262       O  
ATOM     87  CB  LEU A  56     -12.199   5.035 -23.751  1.00 68.42           C  
ANISOU   87  CB  LEU A  56    10823   8617   6556  -5106   1590  -1096       C  
ATOM     88  CG  LEU A  56     -12.145   5.980 -22.558  1.00 67.77           C  
ANISOU   88  CG  LEU A  56    10891   8380   6480  -4999   1530   -985       C  
ATOM     89  CD1 LEU A  56     -12.363   7.425 -22.998  1.00 69.46           C  
ANISOU   89  CD1 LEU A  56    11234   8633   6525  -5259   1588   -974       C  
ATOM     90  CD2 LEU A  56     -13.186   5.542 -21.538  1.00 66.34           C  
ANISOU   90  CD2 LEU A  56    10943   7915   6348  -4879   1417   -850       C  
ATOM     91  N   LEU A  57      -8.916   5.802 -23.937  1.00 63.78           N  
ANISOU   91  N   LEU A  57     9656   8469   6107  -4846   1739  -1291       N  
ATOM     92  CA  LEU A  57      -7.636   5.569 -23.304  1.00 60.94           C  
ANISOU   92  CA  LEU A  57     9115   8157   5881  -4580   1729  -1320       C  
ATOM     93  C   LEU A  57      -7.519   6.427 -22.068  1.00 61.94           C  
ANISOU   93  C   LEU A  57     9408   8129   5996  -4494   1673  -1225       C  
ATOM     94  O   LEU A  57      -7.460   7.654 -22.143  1.00 63.56           O  
ANISOU   94  O   LEU A  57     9708   8355   6087  -4645   1729  -1224       O  
ATOM     95  CB  LEU A  57      -6.500   5.856 -24.267  1.00 60.00           C  
ANISOU   95  CB  LEU A  57     8733   8292   5774  -4606   1863  -1459       C  
ATOM     96  CG  LEU A  57      -5.135   5.536 -23.678  1.00 57.57           C  
ANISOU   96  CG  LEU A  57     8242   8023   5608  -4325   1857  -1495       C  
ATOM     97  CD1 LEU A  57      -4.217   4.961 -24.739  1.00 57.66           C  
ANISOU   97  CD1 LEU A  57     7939   8267   5702  -4274   1944  -1618       C  
ATOM     98  CD2 LEU A  57      -4.515   6.762 -23.018  1.00 57.65           C  
ANISOU   98  CD2 LEU A  57     8341   7993   5568  -4311   1900  -1487       C  
ATOM     99  N   ILE A  58      -7.466   5.765 -20.920  1.00 62.65           N  
ANISOU   99  N   ILE A  58     9530   8074   6200  -4259   1560  -1144       N  
ATOM    100  CA  ILE A  58      -7.399   6.438 -19.633  1.00 63.83           C  
ANISOU  100  CA  ILE A  58     9823   8076   6351  -4162   1482  -1033       C  
ATOM    101  C   ILE A  58      -5.958   6.373 -19.151  1.00 62.67           C  
ANISOU  101  C   ILE A  58     9499   8014   6297  -3963   1498  -1087       C  
ATOM    102  O   ILE A  58      -5.470   5.294 -18.889  1.00 59.82           O  
ANISOU  102  O   ILE A  58     9000   7663   6066  -3762   1460  -1109       O  
ATOM    103  CB  ILE A  58      -8.312   5.754 -18.601  1.00 64.27           C  
ANISOU  103  CB  ILE A  58    10027   7914   6478  -4028   1351   -901       C  
ATOM    104  CG1 ILE A  58      -9.753   5.709 -19.122  1.00 65.33           C  
ANISOU  104  CG1 ILE A  58    10353   7942   6526  -4215   1343   -855       C  
ATOM    105  CG2 ILE A  58      -8.255   6.500 -17.275  1.00 65.33           C  
ANISOU  105  CG2 ILE A  58    10289   7917   6617  -3937   1261   -772       C  
ATOM    106  CD1 ILE A  58     -10.660   4.741 -18.395  1.00 64.98           C  
ANISOU  106  CD1 ILE A  58    10423   7698   6568  -4077   1252   -765       C  
ATOM    107  N   PRO A  59      -5.285   7.527 -19.015  1.00 64.68           N  
ANISOU  107  N   PRO A  59     9779   8320   6479  -4028   1553  -1108       N  
ATOM    108  CA  PRO A  59      -3.838   7.452 -18.931  1.00 64.41           C  
ANISOU  108  CA  PRO A  59     9560   8394   6519  -3874   1611  -1200       C  
ATOM    109  C   PRO A  59      -3.290   7.381 -17.512  1.00 62.22           C  
ANISOU  109  C   PRO A  59     9324   8005   6313  -3675   1508  -1116       C  
ATOM    110  O   PRO A  59      -2.143   6.994 -17.341  1.00 60.19           O  
ANISOU  110  O   PRO A  59     8919   7808   6143  -3509   1533  -1183       O  
ATOM    111  CB  PRO A  59      -3.395   8.748 -19.624  1.00 67.28           C  
ANISOU  111  CB  PRO A  59     9939   8875   6750  -4073   1751  -1286       C  
ATOM    112  CG  PRO A  59      -4.566   9.691 -19.504  1.00 68.32           C  
ANISOU  112  CG  PRO A  59    10323   8907   6727  -4306   1713  -1184       C  
ATOM    113  CD  PRO A  59      -5.744   8.927 -18.960  1.00 66.96           C  
ANISOU  113  CD  PRO A  59    10267   8569   6606  -4248   1571  -1054       C  
ATOM    114  N   GLY A  60      -4.090   7.758 -16.517  1.00 62.91           N  
ANISOU  114  N   GLY A  60     9606   7933   6362  -3693   1393   -968       N  
ATOM    115  CA  GLY A  60      -3.668   7.719 -15.120  1.00 62.33           C  
ANISOU  115  CA  GLY A  60     9569   7764   6351  -3523   1286   -871       C  
ATOM    116  C   GLY A  60      -3.776   9.107 -14.529  1.00 63.87           C  
ANISOU  116  C   GLY A  60     9943   7910   6414  -3667   1255   -784       C  
ATOM    117  O   GLY A  60      -4.487   9.321 -13.551  1.00 63.36           O  
ANISOU  117  O   GLY A  60    10016   7714   6344  -3651   1127   -627       O  
ATOM    118  N   ASP A  61      -3.054  10.046 -15.128  1.00 65.78           N  
ANISOU  118  N   ASP A  61    10180   8264   6551  -3809   1373   -883       N  
ATOM    119  CA  ASP A  61      -3.179  11.452 -14.780  1.00 69.27           C  
ANISOU  119  CA  ASP A  61    10808   8679   6833  -4004   1363   -816       C  
ATOM    120  C   ASP A  61      -3.552  12.188 -16.054  1.00 71.04           C  
ANISOU  120  C   ASP A  61    11076   8994   6919  -4260   1496   -903       C  
ATOM    121  O   ASP A  61      -3.124  11.793 -17.135  1.00 72.09           O  
ANISOU  121  O   ASP A  61    11049   9255   7085  -4262   1630  -1056       O  
ATOM    122  CB  ASP A  61      -1.860  11.974 -14.230  1.00 70.69           C  
ANISOU  122  CB  ASP A  61    10963   8905   6990  -3958   1398   -864       C  
ATOM    123  CG  ASP A  61      -2.015  13.217 -13.388  1.00 73.82           C  
ANISOU  123  CG  ASP A  61    11567   9240   7242  -4114   1320   -743       C  
ATOM    124  OD1 ASP A  61      -3.152  13.672 -13.120  1.00 76.74           O  
ANISOU  124  OD1 ASP A  61    12096   9521   7541  -4235   1217   -598       O  
ATOM    125  OD2 ASP A  61      -0.961  13.731 -12.966  1.00 77.21           O1-
ANISOU  125  OD2 ASP A  61    12004   9704   7625  -4114   1355   -786       O1-
ATOM    126  N   GLY A  62      -4.354  13.240 -15.934  1.00 72.21           N  
ANISOU  126  N   GLY A  62    11439   9080   6915  -4480   1454   -804       N  
ATOM    127  CA  GLY A  62      -4.862  13.961 -17.111  1.00 75.70           C  
ANISOU  127  CA  GLY A  62    11955   9598   7208  -4754   1572   -872       C  
ATOM    128  C   GLY A  62      -6.069  13.307 -17.784  1.00 74.22           C  
ANISOU  128  C   GLY A  62    11787   9368   7044  -4806   1550   -845       C  
ATOM    129  O   GLY A  62      -6.291  12.107 -17.636  1.00 69.45           O  
ANISOU  129  O   GLY A  62    11080   8719   6590  -4612   1492   -832       O  
ATOM    130  N   GLU A  63      -6.827  14.108 -18.537  1.00 75.90           N  
ANISOU  130  N   GLU A  63    12145   9597   7095  -5086   1602   -840       N  
ATOM    131  CA  GLU A  63      -8.049  13.648 -19.205  1.00 77.55           C  
ANISOU  131  CA  GLU A  63    12423   9753   7290  -5189   1585   -810       C  
ATOM    132  C   GLU A  63      -7.873  12.366 -20.040  1.00 76.85           C  
ANISOU  132  C   GLU A  63    12105   9765   7330  -5073   1656   -937       C  
ATOM    133  O   GLU A  63      -6.799  12.147 -20.614  1.00 77.30           O  
ANISOU  133  O   GLU A  63    11940   9993   7436  -5011   1780  -1087       O  
ATOM    134  CB  GLU A  63      -8.644  14.762 -20.104  1.00 81.10           C  
ANISOU  134  CB  GLU A  63    13037  10250   7527  -5542   1671   -829       C  
ATOM    135  CG  GLU A  63      -9.281  15.927 -19.357  1.00 82.82           C  
ANISOU  135  CG  GLU A  63    13540  10330   7598  -5701   1559   -659       C  
ATOM    136  CD  GLU A  63     -10.375  15.432 -18.407  1.00 83.16           C  
ANISOU  136  CD  GLU A  63    13731  10141   7725  -5566   1361   -459       C  
ATOM    137  OE1 GLU A  63     -11.391  14.898 -18.911  1.00 85.14           O  
ANISOU  137  OE1 GLU A  63    14051  10315   7984  -5617   1346   -437       O  
ATOM    138  OE2 GLU A  63     -10.221  15.531 -17.165  1.00 79.67           O1-
ANISOU  138  OE2 GLU A  63    13330   9595   7347  -5404   1225   -329       O1-
ATOM    139  N   PRO A  64      -8.933  11.519 -20.107  1.00 74.39           N  
ANISOU  139  N   PRO A  64    11854   9341   7070  -5044   1580   -871       N  
ATOM    140  CA  PRO A  64      -8.927  10.348 -20.969  1.00 74.19           C  
ANISOU  140  CA  PRO A  64    11645   9410   7133  -4991   1637   -978       C  
ATOM    141  C   PRO A  64      -9.061  10.716 -22.441  1.00 77.45           C  
ANISOU  141  C   PRO A  64    12004   9998   7423  -5264   1784  -1098       C  
ATOM    142  O   PRO A  64      -9.593  11.774 -22.762  1.00 79.84           O  
ANISOU  142  O   PRO A  64    12485  10290   7559  -5518   1819  -1070       O  
ATOM    143  CB  PRO A  64     -10.157   9.570 -20.503  1.00 73.32           C  
ANISOU  143  CB  PRO A  64    11689   9097   7074  -4929   1514   -857       C  
ATOM    144  CG  PRO A  64     -11.088  10.598 -19.993  1.00 73.83           C  
ANISOU  144  CG  PRO A  64    12041   8995   7018  -5077   1437   -709       C  
ATOM    145  CD  PRO A  64     -10.193  11.613 -19.342  1.00 74.06           C  
ANISOU  145  CD  PRO A  64    12064   9069   7007  -5058   1434   -689       C  
ATOM    146  N   LEU A  65      -8.587   9.842 -23.321  1.00 78.76           N  
ANISOU  146  N   LEU A  65    11926  10330   7668  -5215   1863  -1225       N  
ATOM    147  CA  LEU A  65      -8.558  10.121 -24.748  1.00 82.49           C  
ANISOU  147  CA  LEU A  65    12286  11011   8044  -5455   2012  -1349       C  
ATOM    148  C   LEU A  65      -9.503   9.234 -25.533  1.00 83.66           C  
ANISOU  148  C   LEU A  65    12438  11168   8182  -5568   1993  -1354       C  
ATOM    149  O   LEU A  65      -9.759   8.088 -25.155  1.00 82.97           O  
ANISOU  149  O   LEU A  65    12325  10989   8211  -5397   1897  -1314       O  
ATOM    150  CB  LEU A  65      -7.152   9.947 -25.302  1.00 85.29           C  
ANISOU  150  CB  LEU A  65    12324  11592   8489  -5336   2137  -1500       C  
ATOM    151  CG  LEU A  65      -6.207  11.127 -25.193  1.00 88.64           C  
ANISOU  151  CG  LEU A  65    12734  12093   8852  -5367   2249  -1562       C  
ATOM    152  CD1 LEU A  65      -6.202  11.717 -23.789  1.00 88.76           C  
ANISOU  152  CD1 LEU A  65    12967  11908   8849  -5275   2136  -1439       C  
ATOM    153  CD2 LEU A  65      -4.831  10.675 -25.678  1.00 88.99           C  
ANISOU  153  CD2 LEU A  65    12453  12326   9031  -5183   2361  -1705       C  
ATOM    154  N   ARG A  66      -9.978   9.786 -26.651  1.00 85.25           N  
ANISOU  154  N   ARG A  66    12669  11490   8234  -5876   2096  -1409       N  
ATOM    155  CA  ARG A  66     -10.954   9.163 -27.525  1.00 84.40           C  
ANISOU  155  CA  ARG A  66    12599  11403   8067  -6066   2093  -1418       C  
ATOM    156  C   ARG A  66     -10.256   8.622 -28.767  1.00 82.05           C  
ANISOU  156  C   ARG A  66    11963  11399   7812  -6109   2209  -1564       C  
ATOM    157  O   ARG A  66      -9.455   9.309 -29.390  1.00 80.41           O  
ANISOU  157  O   ARG A  66    11583  11395   7573  -6180   2348  -1666       O  
ATOM    158  CB  ARG A  66     -12.017  10.197 -27.925  1.00 88.76           C  
ANISOU  158  CB  ARG A  66    13432  11888   8406  -6411   2121  -1368       C  
ATOM    159  CG  ARG A  66     -13.104  10.406 -26.886  1.00 91.36           C  
ANISOU  159  CG  ARG A  66    14115  11901   8697  -6394   1976  -1198       C  
ATOM    160  CD  ARG A  66     -14.049   9.217 -26.875  1.00 96.10           C  
ANISOU  160  CD  ARG A  66    14806  12358   9350  -6354   1889  -1150       C  
ATOM    161  NE  ARG A  66     -14.828   9.161 -25.635  1.00100.44           N  
ANISOU  161  NE  ARG A  66    15625  12596   9943  -6206   1747   -990       N  
ATOM    162  CZ  ARG A  66     -15.415   8.065 -25.138  1.00104.46           C  
ANISOU  162  CZ  ARG A  66    16204  12931  10555  -6042   1659   -937       C  
ATOM    163  NH1 ARG A  66     -15.365   6.891 -25.774  1.00104.31           N1+
ANISOU  163  NH1 ARG A  66    16030  13011  10592  -6026   1684  -1024       N1+
ATOM    164  NH2 ARG A  66     -16.079   8.144 -23.984  1.00104.48           N  
ANISOU  164  NH2 ARG A  66    16437  12658  10603  -5897   1544   -790       N  
ATOM    165  N   ASN A  67     -10.554   7.376 -29.115  1.00 81.47           N  
ANISOU  165  N   ASN A  67    11794  11349   7811  -6062   2153  -1571       N  
ATOM    166  CA  ASN A  67     -10.009   6.769 -30.330  1.00 82.42           C  
ANISOU  166  CA  ASN A  67    11591  11756   7971  -6119   2237  -1688       C  
ATOM    167  C   ASN A  67      -8.506   6.982 -30.392  1.00 80.20           C  
ANISOU  167  C   ASN A  67    11005  11657   7810  -5916   2328  -1782       C  
ATOM    168  O   ASN A  67      -7.971   7.524 -31.350  1.00 82.05           O  
ANISOU  168  O   ASN A  67    11042  12125   8006  -6042   2474  -1886       O  
ATOM    169  CB  ASN A  67     -10.707   7.348 -31.573  1.00 84.95           C  
ANISOU  169  CB  ASN A  67    11947  12223   8106  -6510   2341  -1737       C  
ATOM    170  CG  ASN A  67     -12.208   7.113 -31.563  1.00 83.77           C  
ANISOU  170  CG  ASN A  67    12121  11878   7830  -6723   2255  -1647       C  
ATOM    171  ND2 ASN A  67     -12.977   8.197 -31.540  1.00 84.61           N  
ANISOU  171  ND2 ASN A  67    12508  11874   7765  -6962   2283  -1598       N  
ATOM    172  OD1 ASN A  67     -12.669   5.972 -31.536  1.00 80.67           O  
ANISOU  172  OD1 ASN A  67    11744  11418   7490  -6671   2165  -1618       O  
ATOM    173  N   ALA A  68      -7.835   6.577 -29.333  1.00 77.90           N  
ANISOU  173  N   ALA A  68    10688  11246   7664  -5600   2247  -1744       N  
ATOM    174  CA  ALA A  68      -6.407   6.804 -29.223  1.00 78.08           C  
ANISOU  174  CA  ALA A  68    10474  11392   7802  -5386   2324  -1823       C  
ATOM    175  C   ALA A  68      -5.637   5.542 -29.578  1.00 78.07           C  
ANISOU  175  C   ALA A  68    10163  11528   7971  -5175   2293  -1869       C  
ATOM    176  O   ALA A  68      -6.237   4.487 -29.852  1.00 79.63           O  
ANISOU  176  O   ALA A  68    10343  11724   8189  -5205   2202  -1835       O  
ATOM    177  CB  ALA A  68      -6.061   7.277 -27.818  1.00 75.77           C  
ANISOU  177  CB  ALA A  68    10356  10888   7544  -5191   2260  -1752       C  
ATOM    178  N   ALA A  69      -4.310   5.669 -29.579  1.00 77.04           N  
ANISOU  178  N   ALA A  69     9803  11511   7956  -4973   2368  -1944       N  
ATOM    179  CA  ALA A  69      -3.408   4.547 -29.813  1.00 76.84           C  
ANISOU  179  CA  ALA A  69     9484  11604   8108  -4736   2331  -1976       C  
ATOM    180  C   ALA A  69      -2.179   4.631 -28.909  1.00 74.36           C  
ANISOU  180  C   ALA A  69     9116  11214   7924  -4428   2329  -1988       C  
ATOM    181  O   ALA A  69      -1.745   5.719 -28.553  1.00 74.41           O  
ANISOU  181  O   ALA A  69     9210  11181   7882  -4432   2423  -2021       O  
ATOM    182  CB  ALA A  69      -2.983   4.517 -31.266  1.00 79.68           C  
ANISOU  182  CB  ALA A  69     9525  12266   8485  -4844   2457  -2080       C  
ATOM    183  N   LEU A  70      -1.641   3.472 -28.545  1.00 72.29           N  
ANISOU  183  N   LEU A  70     8726  10930   7812  -4183   2221  -1959       N  
ATOM    184  CA  LEU A  70      -0.479   3.382 -27.667  1.00 70.43           C  
ANISOU  184  CA  LEU A  70     8446  10612   7701  -3888   2201  -1962       C  
ATOM    185  C   LEU A  70       0.514   2.398 -28.266  1.00 71.00           C  
ANISOU  185  C   LEU A  70     8193  10845   7937  -3691   2193  -2007       C  
ATOM    186  O   LEU A  70       0.117   1.368 -28.820  1.00 71.30           O  
ANISOU  186  O   LEU A  70     8114  10970   8007  -3728   2109  -1980       O  
ATOM    187  CB  LEU A  70      -0.902   2.914 -26.272  1.00 67.93           C  
ANISOU  187  CB  LEU A  70     8367  10044   7400  -3765   2042  -1849       C  
ATOM    188  CG  LEU A  70       0.175   2.812 -25.174  1.00 67.17           C  
ANISOU  188  CG  LEU A  70     8275   9834   7412  -3484   2001  -1833       C  
ATOM    189  CD1 LEU A  70      -0.399   3.185 -23.805  1.00 66.20           C  
ANISOU  189  CD1 LEU A  70     8449   9474   7229  -3474   1908  -1731       C  
ATOM    190  CD2 LEU A  70       0.835   1.437 -25.096  1.00 65.82           C  
ANISOU  190  CD2 LEU A  70     7921   9692   7397  -3254   1902  -1820       C  
ATOM    191  N   VAL A  71       1.803   2.705 -28.147  1.00 70.84           N  
ANISOU  191  N   VAL A  71     8038  10860   8018  -3489   2274  -2070       N  
ATOM    192  CA  VAL A  71       2.844   1.826 -28.668  1.00 71.36           C  
ANISOU  192  CA  VAL A  71     7796  11062   8254  -3274   2263  -2103       C  
ATOM    193  C   VAL A  71       3.743   1.331 -27.554  1.00 70.71           C  
ANISOU  193  C   VAL A  71     7761  10819   8287  -2982   2172  -2063       C  
ATOM    194  O   VAL A  71       3.952   2.014 -26.557  1.00 70.18           O  
ANISOU  194  O   VAL A  71     7901  10585   8179  -2932   2187  -2053       O  
ATOM    195  CB  VAL A  71       3.713   2.531 -29.707  1.00 73.56           C  
ANISOU  195  CB  VAL A  71     7825  11546   8578  -3266   2459  -2224       C  
ATOM    196  CG1 VAL A  71       4.680   1.555 -30.366  1.00 74.24           C  
ANISOU  196  CG1 VAL A  71     7571  11788   8849  -3048   2434  -2241       C  
ATOM    197  CG2 VAL A  71       2.824   3.163 -30.760  1.00 76.56           C  
ANISOU  197  CG2 VAL A  71     8177  12089   8823  -3582   2566  -2269       C  
ATOM    198  N   ILE A  72       4.246   0.116 -27.739  1.00 70.97           N  
ANISOU  198  N   ILE A  72     7604  10909   8453  -2809   2069  -2033       N  
ATOM    199  CA  ILE A  72       5.137  -0.523 -26.800  1.00 69.16           C  
ANISOU  199  CA  ILE A  72     7393  10546   8338  -2537   1973  -1993       C  
ATOM    200  C   ILE A  72       6.373  -0.943 -27.550  1.00 70.87           C  
ANISOU  200  C   ILE A  72     7301  10912   8715  -2337   2016  -2043       C  
ATOM    201  O   ILE A  72       6.305  -1.847 -28.380  1.00 73.49           O  
ANISOU  201  O   ILE A  72     7413  11399   9110  -2339   1950  -2021       O  
ATOM    202  CB  ILE A  72       4.505  -1.809 -26.215  1.00 67.18           C  
ANISOU  202  CB  ILE A  72     7229  10200   8096  -2513   1775  -1886       C  
ATOM    203  CG1 ILE A  72       3.299  -1.460 -25.346  1.00 65.40           C  
ANISOU  203  CG1 ILE A  72     7316   9798   7735  -2669   1728  -1826       C  
ATOM    204  CG2 ILE A  72       5.538  -2.598 -25.409  1.00 66.34           C  
ANISOU  204  CG2 ILE A  72     7097   9993   8117  -2234   1676  -1848       C  
ATOM    205  CD1 ILE A  72       2.563  -2.674 -24.811  1.00 64.69           C  
ANISOU  205  CD1 ILE A  72     7325   9609   7644  -2663   1562  -1734       C  
ATOM    206  N   SER A  73       7.501  -0.317 -27.254  1.00 71.72           N  
ANISOU  206  N   SER A  73     7393  10967   8887  -2163   2122  -2105       N  
ATOM    207  CA  SER A  73       8.780  -0.853 -27.700  1.00 73.95           C  
ANISOU  207  CA  SER A  73     7421  11330   9346  -1908   2136  -2133       C  
ATOM    208  C   SER A  73       9.349  -1.637 -26.533  1.00 72.84           C  
ANISOU  208  C   SER A  73     7406  10999   9273  -1696   1986  -2057       C  
ATOM    209  O   SER A  73       9.598  -1.057 -25.484  1.00 72.39           O  
ANISOU  209  O   SER A  73     7576  10761   9166  -1655   2006  -2061       O  
ATOM    210  CB  SER A  73       9.738   0.262 -28.138  1.00 75.80           C  
ANISOU  210  CB  SER A  73     7566  11614   9620  -1835   2360  -2258       C  
ATOM    211  OG  SER A  73      10.897  -0.265 -28.747  1.00 76.62           O  
ANISOU  211  OG  SER A  73     7392  11812   9908  -1589   2385  -2283       O  
ATOM    212  N   ASP A  74       9.520  -2.947 -26.730  1.00 74.38           N  
ANISOU  212  N   ASP A  74     7453  11244   9566  -1586   1832  -1985       N  
ATOM    213  CA  ASP A  74      10.056  -3.876 -25.719  1.00 73.47           C  
ANISOU  213  CA  ASP A  74     7433  10969   9515  -1394   1675  -1906       C  
ATOM    214  C   ASP A  74       9.337  -3.745 -24.380  1.00 70.96           C  
ANISOU  214  C   ASP A  74     7438  10446   9077  -1477   1602  -1852       C  
ATOM    215  O   ASP A  74       8.138  -3.992 -24.298  1.00 67.50           O  
ANISOU  215  O   ASP A  74     7100  10004   8541  -1660   1535  -1805       O  
ATOM    216  CB  ASP A  74      11.571  -3.677 -25.563  1.00 75.11           C  
ANISOU  216  CB  ASP A  74     7568  11117   9852  -1128   1744  -1951       C  
ATOM    217  CG  ASP A  74      12.340  -4.063 -26.805  1.00 78.17           C  
ANISOU  217  CG  ASP A  74     7613  11696  10391   -992   1781  -1976       C  
ATOM    218  OD1 ASP A  74      12.343  -5.269 -27.133  1.00 79.45           O  
ANISOU  218  OD1 ASP A  74     7625  11934  10626   -936   1622  -1894       O  
ATOM    219  OD2 ASP A  74      12.952  -3.172 -27.444  1.00 79.90           O1-
ANISOU  219  OD2 ASP A  74     7710  11989  10661   -941   1970  -2078       O1-
ATOM    220  N   LYS A  75      10.068  -3.308 -23.357  1.00 72.00           N  
ANISOU  220  N   LYS A  75     7731  10410   9216  -1348   1624  -1860       N  
ATOM    221  CA  LYS A  75       9.578  -3.234 -21.988  1.00 71.48           C  
ANISOU  221  CA  LYS A  75     7944  10154   9060  -1389   1545  -1797       C  
ATOM    222  C   LYS A  75       8.859  -1.928 -21.659  1.00 70.39           C  
ANISOU  222  C   LYS A  75     7997   9963   8783  -1577   1646  -1826       C  
ATOM    223  O   LYS A  75       8.170  -1.840 -20.648  1.00 67.06           O  
ANISOU  223  O   LYS A  75     7789   9410   8279  -1648   1573  -1760       O  
ATOM    224  CB  LYS A  75      10.759  -3.438 -21.035  1.00 74.82           C  
ANISOU  224  CB  LYS A  75     8443  10434   9552  -1173   1506  -1782       C  
ATOM    225  CG  LYS A  75      11.382  -4.822 -21.257  1.00 78.32           C  
ANISOU  225  CG  LYS A  75     8727  10910  10119   -999   1377  -1731       C  
ATOM    226  CD  LYS A  75      12.675  -5.127 -20.492  1.00 80.01           C  
ANISOU  226  CD  LYS A  75     8994  10993  10414   -775   1338  -1717       C  
ATOM    227  CE  LYS A  75      12.933  -6.631 -20.366  1.00 81.68           C  
ANISOU  227  CE  LYS A  75     9133  11200  10703   -659   1160  -1630       C  
ATOM    228  NZ  LYS A  75      13.752  -6.953 -19.154  1.00 82.06           N1+
ANISOU  228  NZ  LYS A  75     9343  11070  10766   -518   1088  -1588       N1+
ATOM    229  N   ILE A  76       8.993  -0.919 -22.520  1.00 72.72           N  
ANISOU  229  N   ILE A  76     8213  10366   9052  -1661   1813  -1920       N  
ATOM    230  CA  ILE A  76       8.467   0.426 -22.214  1.00 71.19           C  
ANISOU  230  CA  ILE A  76     8211  10120   8717  -1843   1917  -1951       C  
ATOM    231  C   ILE A  76       7.543   1.030 -23.269  1.00 68.73           C  
ANISOU  231  C   ILE A  76     7844   9953   8318  -2077   2014  -1995       C  
ATOM    232  O   ILE A  76       7.481   0.593 -24.423  1.00 67.02           O  
ANISOU  232  O   ILE A  76     7398   9910   8156  -2100   2043  -2028       O  
ATOM    233  CB  ILE A  76       9.606   1.425 -21.891  1.00 74.02           C  
ANISOU  233  CB  ILE A  76     8634  10415   9076  -1755   2054  -2032       C  
ATOM    234  CG1 ILE A  76      10.572   1.586 -23.070  1.00 77.18           C  
ANISOU  234  CG1 ILE A  76     8786  10959   9580  -1650   2209  -2145       C  
ATOM    235  CG2 ILE A  76      10.373   0.959 -20.655  1.00 74.47           C  
ANISOU  235  CG2 ILE A  76     8812  10303   9181  -1571   1949  -1976       C  
ATOM    236  CD1 ILE A  76      10.237   2.717 -24.017  1.00 79.32           C  
ANISOU  236  CD1 ILE A  76     9009  11361   9767  -1839   2400  -2244       C  
ATOM    237  N   ILE A  77       6.821   2.046 -22.825  1.00 66.07           N  
ANISOU  237  N   ILE A  77     7724   9543   7838  -2262   2055  -1985       N  
ATOM    238  CA  ILE A  77       5.828   2.710 -23.629  1.00 66.45           C  
ANISOU  238  CA  ILE A  77     7785   9691   7772  -2516   2135  -2011       C  
ATOM    239  C   ILE A  77       6.470   3.717 -24.567  1.00 68.44           C  
ANISOU  239  C   ILE A  77     7917  10080   8008  -2569   2347  -2141       C  
ATOM    240  O   ILE A  77       7.075   4.689 -24.129  1.00 68.38           O  
ANISOU  240  O   ILE A  77     8026  10003   7953  -2561   2450  -2193       O  
ATOM    241  CB  ILE A  77       4.810   3.439 -22.732  1.00 65.60           C  
ANISOU  241  CB  ILE A  77     7974   9437   7514  -2688   2086  -1936       C  
ATOM    242  CG1 ILE A  77       3.995   2.409 -21.941  1.00 62.54           C  
ANISOU  242  CG1 ILE A  77     7688   8929   7145  -2651   1896  -1813       C  
ATOM    243  CG2 ILE A  77       3.911   4.348 -23.569  1.00 67.79           C  
ANISOU  243  CG2 ILE A  77     8294   9807   7655  -2967   2191  -1973       C  
ATOM    244  CD1 ILE A  77       2.857   2.988 -21.133  1.00 61.24           C  
ANISOU  244  CD1 ILE A  77     7791   8624   6855  -2806   1834  -1722       C  
ATOM    245  N   ALA A  78       6.270   3.507 -25.863  1.00 69.95           N  
ANISOU  245  N   ALA A  78     7880  10470   8228  -2648   2417  -2194       N  
ATOM    246  CA  ALA A  78       6.925   4.299 -26.892  1.00 71.54           C  
ANISOU  246  CA  ALA A  78     7907  10833   8443  -2676   2630  -2325       C  
ATOM    247  C   ALA A  78       6.076   5.471 -27.429  1.00 71.76           C  
ANISOU  247  C   ALA A  78     8036  10933   8296  -2985   2763  -2374       C  
ATOM    248  O   ALA A  78       6.627   6.496 -27.846  1.00 72.91           O  
ANISOU  248  O   ALA A  78     8158  11143   8403  -3033   2960  -2485       O  
ATOM    249  CB  ALA A  78       7.347   3.376 -28.023  1.00 73.34           C  
ANISOU  249  CB  ALA A  78     7785  11261   8821  -2564   2634  -2353       C  
ATOM    250  N   PHE A  79       4.753   5.325 -27.434  1.00 70.29           N  
ANISOU  250  N   PHE A  79     7974  10732   7999  -3197   2663  -2294       N  
ATOM    251  CA  PHE A  79       3.881   6.402 -27.908  1.00 71.60           C  
ANISOU  251  CA  PHE A  79     8266  10952   7989  -3506   2770  -2325       C  
ATOM    252  C   PHE A  79       2.488   6.352 -27.278  1.00 71.05           C  
ANISOU  252  C   PHE A  79     8467  10738   7791  -3686   2620  -2203       C  
ATOM    253  O   PHE A  79       1.921   5.275 -27.077  1.00 70.63           O  
ANISOU  253  O   PHE A  79     8411  10639   7786  -3638   2460  -2116       O  
ATOM    254  CB  PHE A  79       3.764   6.348 -29.438  1.00 73.89           C  
ANISOU  254  CB  PHE A  79     8281  11504   8290  -3635   2893  -2408       C  
ATOM    255  CG  PHE A  79       2.678   7.228 -29.999  1.00 75.32           C  
ANISOU  255  CG  PHE A  79     8589  11749   8280  -3983   2973  -2422       C  
ATOM    256  CD1 PHE A  79       2.933   8.568 -30.290  1.00 77.32           C  
ANISOU  256  CD1 PHE A  79     8904  12052   8421  -4132   3174  -2522       C  
ATOM    257  CD2 PHE A  79       1.396   6.726 -30.231  1.00 74.64           C  
ANISOU  257  CD2 PHE A  79     8583  11664   8114  -4178   2852  -2339       C  
ATOM    258  CE1 PHE A  79       1.935   9.390 -30.796  1.00 77.82           C  
ANISOU  258  CE1 PHE A  79     9100  12171   8296  -4468   3244  -2530       C  
ATOM    259  CE2 PHE A  79       0.393   7.542 -30.735  1.00 76.17           C  
ANISOU  259  CE2 PHE A  79     8917  11901   8124  -4507   2922  -2346       C  
ATOM    260  CZ  PHE A  79       0.662   8.880 -31.015  1.00 78.03           C  
ANISOU  260  CZ  PHE A  79     9209  12192   8248  -4655   3114  -2438       C  
ATOM    261  N   VAL A  80       1.962   7.533 -26.954  1.00 71.92           N  
ANISOU  261  N   VAL A  80     8820  10771   7735  -3889   2676  -2195       N  
ATOM    262  CA  VAL A  80       0.550   7.724 -26.614  1.00 72.33           C  
ANISOU  262  CA  VAL A  80     9125  10710   7648  -4107   2571  -2089       C  
ATOM    263  C   VAL A  80       0.032   9.003 -27.277  1.00 76.63           C  
ANISOU  263  C   VAL A  80     9774  11332   8010  -4416   2717  -2142       C  
ATOM    264  O   VAL A  80       0.701  10.047 -27.247  1.00 77.34           O  
ANISOU  264  O   VAL A  80     9901  11445   8041  -4452   2858  -2219       O  
ATOM    265  CB  VAL A  80       0.312   7.882 -25.105  1.00 69.65           C  
ANISOU  265  CB  VAL A  80     9057  10124   7280  -4026   2429  -1970       C  
ATOM    266  CG1 VAL A  80      -1.173   7.736 -24.788  1.00 68.29           C  
ANISOU  266  CG1 VAL A  80     9104   9827   7014  -4188   2298  -1847       C  
ATOM    267  CG2 VAL A  80       1.127   6.869 -24.328  1.00 69.22           C  
ANISOU  267  CG2 VAL A  80     8911   9995   7393  -3715   2323  -1940       C  
ATOM    268  N   GLY A  81      -1.175   8.919 -27.834  1.00 79.45           N  
ANISOU  268  N   GLY A  81    10203  11718   8267  -4650   2682  -2099       N  
ATOM    269  CA  GLY A  81      -1.776  10.012 -28.617  1.00 84.52           C  
ANISOU  269  CA  GLY A  81    10934  12453   8726  -4978   2814  -2147       C  
ATOM    270  C   GLY A  81      -2.947   9.490 -29.434  1.00 87.52           C  
ANISOU  270  C   GLY A  81    11310  12901   9044  -5190   2768  -2112       C  
ATOM    271  O   GLY A  81      -3.274   8.293 -29.342  1.00 91.98           O  
ANISOU  271  O   GLY A  81    11812  13429   9705  -5077   2632  -2053       O  
ATOM    272  N   SER A  82      -3.580  10.342 -30.246  1.00 86.92           N  
ANISOU  272  N   SER A  82    11305  12922   8798  -5510   2880  -2151       N  
ATOM    273  CA  SER A  82      -4.744   9.875 -30.999  1.00 86.10           C  
ANISOU  273  CA  SER A  82    11231  12868   8615  -5740   2832  -2114       C  
ATOM    274  C   SER A  82      -4.265   8.975 -32.141  1.00 86.37           C  
ANISOU  274  C   SER A  82    10891  13160   8766  -5692   2889  -2202       C  
ATOM    275  O   SER A  82      -3.145   9.133 -32.662  1.00 85.67           O  
ANISOU  275  O   SER A  82    10526  13254   8770  -5576   3029  -2314       O  
ATOM    276  CB  SER A  82      -5.619  11.027 -31.501  1.00 87.83           C  
ANISOU  276  CB  SER A  82    11661  13105   8606  -6115   2921  -2118       C  
ATOM    277  OG  SER A  82      -5.026  11.691 -32.602  1.00 91.36           O  
ANISOU  277  OG  SER A  82    11896  13811   9007  -6259   3138  -2261       O  
ATOM    278  N   GLU A  83      -5.116   8.020 -32.504  1.00 86.41           N  
ANISOU  278  N   GLU A  83    10893  13171   8767  -5778   2778  -2145       N  
ATOM    279  CA  GLU A  83      -4.799   7.014 -33.532  1.00 86.84           C  
ANISOU  279  CA  GLU A  83    10606  13463   8925  -5748   2787  -2198       C  
ATOM    280  C   GLU A  83      -4.171   7.600 -34.802  1.00 88.20           C  
ANISOU  280  C   GLU A  83    10481  13946   9086  -5873   2994  -2330       C  
ATOM    281  O   GLU A  83      -3.235   7.026 -35.361  1.00 87.09           O  
ANISOU  281  O   GLU A  83     9989  13999   9102  -5697   3036  -2392       O  
ATOM    282  CB  GLU A  83      -6.067   6.242 -33.883  1.00 86.66           C  
ANISOU  282  CB  GLU A  83    10703  13406   8818  -5955   2668  -2125       C  
ATOM    283  CG  GLU A  83      -5.956   5.377 -35.113  1.00 88.23           C  
ANISOU  283  CG  GLU A  83    10578  13879   9066  -6034   2682  -2173       C  
ATOM    284  CD  GLU A  83      -7.162   4.495 -35.291  1.00 88.98           C  
ANISOU  284  CD  GLU A  83    10826  13905   9079  -6216   2547  -2097       C  
ATOM    285  OE1 GLU A  83      -7.976   4.363 -34.342  1.00 90.16           O  
ANISOU  285  OE1 GLU A  83    11313  13767   9178  -6203   2432  -2005       O  
ATOM    286  OE2 GLU A  83      -7.281   3.922 -36.388  1.00 89.59           O1-
ANISOU  286  OE2 GLU A  83    10680  14215   9145  -6370   2558  -2128       O1-
ATOM    287  N   ALA A  84      -4.678   8.751 -35.233  1.00 89.75           N  
ANISOU  287  N   ALA A  84    10817  14185   9098  -6173   3124  -2370       N  
ATOM    288  CA  ALA A  84      -4.136   9.459 -36.399  1.00 92.16           C  
ANISOU  288  CA  ALA A  84    10864  14781   9373  -6318   3348  -2504       C  
ATOM    289  C   ALA A  84      -2.626   9.736 -36.295  1.00 93.63           C  
ANISOU  289  C   ALA A  84    10806  15048   9719  -6024   3482  -2605       C  
ATOM    290  O   ALA A  84      -1.884   9.521 -37.253  1.00 93.72           O  
ANISOU  290  O   ALA A  84    10448  15323   9838  -5963   3605  -2698       O  
ATOM    291  CB  ALA A  84      -4.882  10.765 -36.602  1.00 93.08           C  
ANISOU  291  CB  ALA A  84    11243  14874   9250  -6672   3461  -2523       C  
ATOM    292  N   ASP A  85      -2.172  10.170 -35.115  1.00 93.79           N  
ANISOU  292  N   ASP A  85    11032  14842   9761  -5835   3452  -2580       N  
ATOM    293  CA  ASP A  85      -0.822  10.733 -34.952  1.00 93.83           C  
ANISOU  293  CA  ASP A  85    10899  14887   9866  -5617   3610  -2686       C  
ATOM    294  C   ASP A  85       0.292   9.701 -34.614  1.00 89.59           C  
ANISOU  294  C   ASP A  85    10118  14342   9579  -5211   3537  -2685       C  
ATOM    295  O   ASP A  85       1.409  10.089 -34.275  1.00 86.19           O  
ANISOU  295  O   ASP A  85     9627  13886   9237  -4998   3642  -2757       O  
ATOM    296  CB  ASP A  85      -0.865  11.899 -33.927  1.00 95.14           C  
ANISOU  296  CB  ASP A  85    11424  14832   9894  -5675   3636  -2668       C  
ATOM    297  CG  ASP A  85      -1.727  13.110 -34.412  1.00 99.47           C  
ANISOU  297  CG  ASP A  85    12180  15424  10189  -6084   3755  -2693       C  
ATOM    298  OD1 ASP A  85      -1.785  13.420 -35.630  1.00103.16           O  
ANISOU  298  OD1 ASP A  85    12455  16140  10601  -6291   3925  -2792       O  
ATOM    299  OD2 ASP A  85      -2.355  13.772 -33.556  1.00 99.84           O1-
ANISOU  299  OD2 ASP A  85    12586  15257  10088  -6206   3674  -2607       O1-
ATOM    300  N   ILE A  86      -0.000   8.403 -34.737  1.00 87.55           N  
ANISOU  300  N   ILE A  86     9733  14108   9424  -5118   3365  -2607       N  
ATOM    301  CA  ILE A  86       1.025   7.354 -34.557  1.00 87.59           C  
ANISOU  301  CA  ILE A  86     9490  14132   9660  -4758   3289  -2600       C  
ATOM    302  C   ILE A  86       2.240   7.629 -35.467  1.00 89.61           C  
ANISOU  302  C   ILE A  86     9381  14624  10045  -4626   3497  -2733       C  
ATOM    303  O   ILE A  86       2.071   7.900 -36.638  1.00 91.18           O  
ANISOU  303  O   ILE A  86     9371  15068  10204  -4815   3631  -2804       O  
ATOM    304  CB  ILE A  86       0.459   5.928 -34.864  1.00 87.23           C  
ANISOU  304  CB  ILE A  86     9323  14141   9681  -4749   3095  -2507       C  
ATOM    305  CG1 ILE A  86      -0.631   5.530 -33.862  1.00 84.78           C  
ANISOU  305  CG1 ILE A  86     9368  13569   9276  -4816   2896  -2379       C  
ATOM    306  CG2 ILE A  86       1.553   4.856 -34.845  1.00 85.84           C  
ANISOU  306  CG2 ILE A  86     8860  14019   9735  -4403   3022  -2499       C  
ATOM    307  CD1 ILE A  86      -1.459   4.333 -34.288  1.00 84.42           C  
ANISOU  307  CD1 ILE A  86     9271  13575   9229  -4915   2740  -2304       C  
ATOM    308  N   PRO A  87       3.466   7.553 -34.929  1.00 91.46           N  
ANISOU  308  N   PRO A  87     9536  14779  10434  -4300   3528  -2769       N  
ATOM    309  CA  PRO A  87       4.631   7.622 -35.816  1.00 95.16           C  
ANISOU  309  CA  PRO A  87     9635  15461  11059  -4130   3711  -2886       C  
ATOM    310  C   PRO A  87       4.651   6.485 -36.830  1.00 97.79           C  
ANISOU  310  C   PRO A  87     9593  16034  11530  -4079   3634  -2854       C  
ATOM    311  O   PRO A  87       4.374   5.327 -36.479  1.00 93.80           O  
ANISOU  311  O   PRO A  87     9090  15462  11088  -3985   3407  -2738       O  
ATOM    312  CB  PRO A  87       5.831   7.480 -34.871  1.00 94.67           C  
ANISOU  312  CB  PRO A  87     9611  15213  11144  -3769   3695  -2895       C  
ATOM    313  CG  PRO A  87       5.325   7.740 -33.499  1.00 91.60           C  
ANISOU  313  CG  PRO A  87     9636  14533  10633  -3807   3562  -2811       C  
ATOM    314  CD  PRO A  87       3.832   7.568 -33.499  1.00 90.76           C  
ANISOU  314  CD  PRO A  87     9714  14403  10368  -4098   3424  -2713       C  
ATOM    315  N   LYS A  88       4.966   6.820 -38.078  1.00104.09           N  
ANISOU  315  N   LYS A  88    10068  17116  12366  -4153   3824  -2953       N  
ATOM    316  CA  LYS A  88       4.975   5.819 -39.150  1.00106.75           C  
ANISOU  316  CA  LYS A  88    10014  17721  12824  -4137   3756  -2919       C  
ATOM    317  C   LYS A  88       6.129   4.851 -38.960  1.00104.79           C  
ANISOU  317  C   LYS A  88     9529  17458  12830  -3731   3663  -2883       C  
ATOM    318  O   LYS A  88       6.038   3.698 -39.374  1.00103.99           O  
ANISOU  318  O   LYS A  88     9212  17475  12825  -3677   3494  -2794       O  
ATOM    319  CB  LYS A  88       4.994   6.453 -40.556  1.00111.47           C  
ANISOU  319  CB  LYS A  88    10304  18651  13399  -4332   3988  -3030       C  
ATOM    320  CG  LYS A  88       6.074   7.495 -40.850  1.00114.07           C  
ANISOU  320  CG  LYS A  88    10496  19046  13798  -4197   4286  -3187       C  
ATOM    321  CD  LYS A  88       5.996   7.906 -42.334  1.00118.12           C  
ANISOU  321  CD  LYS A  88    10651  19926  14302  -4398   4494  -3283       C  
ATOM    322  CE  LYS A  88       6.078   9.412 -42.607  1.00119.38           C  
ANISOU  322  CE  LYS A  88    10907  20129  14322  -4587   4805  -3441       C  
ATOM    323  NZ  LYS A  88       7.317  10.033 -42.074  1.00119.83           N1+
ANISOU  323  NZ  LYS A  88    11002  20038  14488  -4288   4984  -3549       N1+
ATOM    324  N   LYS A  89       7.188   5.337 -38.316  1.00103.30           N  
ANISOU  324  N   LYS A  89     9406  17112  12733  -3464   3770  -2949       N  
ATOM    325  CA  LYS A  89       8.303   4.530 -37.842  1.00102.50           C  
ANISOU  325  CA  LYS A  89     9186  16910  12848  -3070   3674  -2909       C  
ATOM    326  C   LYS A  89       7.811   3.192 -37.256  1.00 98.99           C  
ANISOU  326  C   LYS A  89     8827  16357  12426  -3020   3363  -2749       C  
ATOM    327  O   LYS A  89       8.328   2.103 -37.576  1.00 97.51           O  
ANISOU  327  O   LYS A  89     8377  16262  12411  -2817   3234  -2682       O  
ATOM    328  CB  LYS A  89       9.072   5.383 -36.797  1.00103.22           C  
ANISOU  328  CB  LYS A  89     9549  16740  12930  -2904   3790  -2980       C  
ATOM    329  CG  LYS A  89      10.039   4.657 -35.866  1.00103.68           C  
ANISOU  329  CG  LYS A  89     9655  16588  13149  -2540   3657  -2923       C  
ATOM    330  CD  LYS A  89      10.875   5.620 -35.024  1.00103.25           C  
ANISOU  330  CD  LYS A  89     9837  16317  13078  -2407   3812  -3016       C  
ATOM    331  CE  LYS A  89      11.717   4.855 -34.007  1.00100.84           C  
ANISOU  331  CE  LYS A  89     9623  15787  12905  -2085   3656  -2945       C  
ATOM    332  NZ  LYS A  89      12.836   5.665 -33.475  1.00100.83           N1+
ANISOU  332  NZ  LYS A  89     9749  15623  12939  -1902   3836  -3052       N1+
ATOM    333  N   TYR A  90       6.786   3.286 -36.413  1.00 96.82           N  
ANISOU  333  N   TYR A  90     8924  15890  11973  -3212   3245  -2686       N  
ATOM    334  CA  TYR A  90       6.281   2.134 -35.662  1.00 93.90           C  
ANISOU  334  CA  TYR A  90     8704  15369  11603  -3170   2974  -2548       C  
ATOM    335  C   TYR A  90       5.310   1.283 -36.470  1.00 93.47           C  
ANISOU  335  C   TYR A  90     8519  15499  11498  -3393   2842  -2474       C  
ATOM    336  O   TYR A  90       5.312   0.048 -36.360  1.00 94.12           O  
ANISOU  336  O   TYR A  90     8524  15577  11659  -3290   2641  -2376       O  
ATOM    337  CB  TYR A  90       5.659   2.583 -34.319  1.00 91.46           C  
ANISOU  337  CB  TYR A  90     8847  14757  11145  -3244   2908  -2508       C  
ATOM    338  CG  TYR A  90       6.678   3.154 -33.330  1.00 89.81           C  
ANISOU  338  CG  TYR A  90     8785  14342  10994  -3001   2979  -2551       C  
ATOM    339  CD1 TYR A  90       7.881   2.479 -33.063  1.00 89.65           C  
ANISOU  339  CD1 TYR A  90     8613  14281  11170  -2659   2931  -2540       C  
ATOM    340  CD2 TYR A  90       6.443   4.363 -32.673  1.00 87.74           C  
ANISOU  340  CD2 TYR A  90     8823  13931  10584  -3126   3088  -2597       C  
ATOM    341  CE1 TYR A  90       8.811   2.996 -32.181  1.00 89.34           C  
ANISOU  341  CE1 TYR A  90     8723  14050  11171  -2457   3000  -2582       C  
ATOM    342  CE2 TYR A  90       7.367   4.887 -31.787  1.00 88.03           C  
ANISOU  342  CE2 TYR A  90     9002  13789  10658  -2932   3150  -2637       C  
ATOM    343  CZ  TYR A  90       8.550   4.202 -31.547  1.00 88.90           C  
ANISOU  343  CZ  TYR A  90     8963  13856  10958  -2600   3111  -2634       C  
ATOM    344  OH  TYR A  90       9.483   4.718 -30.672  1.00 88.80           O  
ANISOU  344  OH  TYR A  90     9108  13657  10973  -2421   3176  -2676       O  
ATOM    345  N   LEU A  91       4.480   1.942 -37.269  1.00 92.95           N  
ANISOU  345  N   LEU A  91     8443  15588  11285  -3715   2953  -2522       N  
ATOM    346  CA  LEU A  91       3.601   1.238 -38.191  1.00 93.04           C  
ANISOU  346  CA  LEU A  91     8310  15806  11236  -3962   2856  -2467       C  
ATOM    347  C   LEU A  91       4.391   0.273 -39.058  1.00 93.88           C  
ANISOU  347  C   LEU A  91     7976  16156  11536  -3784   2797  -2440       C  
ATOM    348  O   LEU A  91       3.927  -0.827 -39.341  1.00 93.38           O  
ANISOU  348  O   LEU A  91     7834  16173  11474  -3857   2610  -2345       O  
ATOM    349  CB  LEU A  91       2.842   2.229 -39.073  1.00 94.95           C  
ANISOU  349  CB  LEU A  91     8549  16217  11308  -4319   3030  -2544       C  
ATOM    350  CG  LEU A  91       1.794   3.059 -38.321  1.00 94.36           C  
ANISOU  350  CG  LEU A  91     8927  15914  11013  -4559   3045  -2540       C  
ATOM    351  CD1 LEU A  91       1.268   4.206 -39.171  1.00 96.18           C  
ANISOU  351  CD1 LEU A  91     9154  16308  11083  -4887   3249  -2631       C  
ATOM    352  CD2 LEU A  91       0.647   2.179 -37.837  1.00 92.63           C  
ANISOU  352  CD2 LEU A  91     8958  15544  10692  -4699   2819  -2421       C  
ATOM    353  N   ARG A  92       5.583   0.686 -39.472  1.00 95.80           N  
ANISOU  353  N   ARG A  92     7941  16514  11943  -3551   2955  -2519       N  
ATOM    354  CA  ARG A  92       6.408  -0.142 -40.349  1.00 98.97           C  
ANISOU  354  CA  ARG A  92     7894  17159  12551  -3358   2911  -2488       C  
ATOM    355  C   ARG A  92       6.984  -1.348 -39.598  1.00 96.81           C  
ANISOU  355  C   ARG A  92     7638  16729  12417  -3064   2682  -2376       C  
ATOM    356  O   ARG A  92       7.127  -2.425 -40.173  1.00 97.39           O  
ANISOU  356  O   ARG A  92     7445  16970  12588  -3014   2526  -2287       O  
ATOM    357  CB  ARG A  92       7.531   0.696 -41.016  1.00102.68           C  
ANISOU  357  CB  ARG A  92     8061  17784  13168  -3175   3171  -2612       C  
ATOM    358  CG  ARG A  92       7.741   0.418 -42.518  1.00107.82           C  
ANISOU  358  CG  ARG A  92     8210  18830  13927  -3224   3227  -2619       C  
ATOM    359  CD  ARG A  92       8.751   1.345 -43.222  1.00110.87           C  
ANISOU  359  CD  ARG A  92     8298  19376  14451  -3063   3523  -2757       C  
ATOM    360  NE  ARG A  92       8.336   2.755 -43.329  1.00111.97           N  
ANISOU  360  NE  ARG A  92     8612  19515  14418  -3305   3783  -2897       N  
ATOM    361  CZ  ARG A  92       8.580   3.723 -42.438  1.00109.90           C  
ANISOU  361  CZ  ARG A  92     8683  18993  14080  -3252   3923  -2985       C  
ATOM    362  NH1 ARG A  92       9.236   3.478 -41.305  1.00107.04           N1+
ANISOU  362  NH1 ARG A  92     8534  18337  13798  -2964   3834  -2955       N1+
ATOM    363  NH2 ARG A  92       8.131   4.958 -42.669  1.00110.14           N  
ANISOU  363  NH2 ARG A  92     8848  19061  13939  -3515   4148  -3104       N  
ATOM    364  N   SER A  93       7.293  -1.173 -38.316  1.00 94.07           N  
ANISOU  364  N   SER A  93     7608  16068  12067  -2889   2655  -2375       N  
ATOM    365  CA  SER A  93       8.085  -2.160 -37.582  1.00 91.49           C  
ANISOU  365  CA  SER A  93     7284  15588  11889  -2572   2480  -2289       C  
ATOM    366  C   SER A  93       7.277  -3.157 -36.751  1.00 88.93           C  
ANISOU  366  C   SER A  93     7228  15088  11469  -2655   2232  -2171       C  
ATOM    367  O   SER A  93       7.743  -4.272 -36.523  1.00 89.18           O  
ANISOU  367  O   SER A  93     7177  15095  11612  -2470   2051  -2078       O  
ATOM    368  CB  SER A  93       9.098  -1.445 -36.688  1.00 89.68           C  
ANISOU  368  CB  SER A  93     7207  15129  11735  -2300   2602  -2360       C  
ATOM    369  OG  SER A  93       8.459  -0.472 -35.884  1.00 87.46           O  
ANISOU  369  OG  SER A  93     7302  14653  11274  -2468   2688  -2411       O  
ATOM    370  N   THR A  94       6.087  -2.769 -36.292  1.00 86.36           N  
ANISOU  370  N   THR A  94     7229  14643  10943  -2925   2226  -2172       N  
ATOM    371  CA  THR A  94       5.271  -3.623 -35.394  1.00 83.17           C  
ANISOU  371  CA  THR A  94     7117  14040  10444  -2996   2019  -2072       C  
ATOM    372  C   THR A  94       5.026  -5.053 -35.880  1.00 84.95           C  
ANISOU  372  C   THR A  94     7178  14398  10702  -3036   1811  -1968       C  
ATOM    373  O   THR A  94       4.952  -5.282 -37.079  1.00 89.80           O  
ANISOU  373  O   THR A  94     7492  15290  11336  -3160   1819  -1966       O  
ATOM    374  CB  THR A  94       3.886  -3.006 -35.131  1.00 80.96           C  
ANISOU  374  CB  THR A  94     7159  13657   9942  -3318   2053  -2085       C  
ATOM    375  CG2 THR A  94       3.202  -2.618 -36.432  1.00 83.81           C  
ANISOU  375  CG2 THR A  94     7352  14282  10208  -3627   2149  -2127       C  
ATOM    376  OG1 THR A  94       3.066  -3.956 -34.438  1.00 77.62           O  
ANISOU  376  OG1 THR A  94     6973  13075   9443  -3388   1860  -1990       O  
ATOM    377  N   GLN A  95       4.867  -5.993 -34.948  1.00 83.20           N  
ANISOU  377  N   GLN A  95     7157  13983  10471  -2954   1629  -1883       N  
ATOM    378  CA  GLN A  95       4.499  -7.378 -35.286  1.00 84.75           C  
ANISOU  378  CA  GLN A  95     7267  14273  10661  -3034   1424  -1782       C  
ATOM    379  C   GLN A  95       3.289  -7.822 -34.484  1.00 81.87           C  
ANISOU  379  C   GLN A  95     7275  13701  10129  -3220   1319  -1738       C  
ATOM    380  O   GLN A  95       3.082  -9.016 -34.253  1.00 82.15           O  
ANISOU  380  O   GLN A  95     7355  13703  10156  -3224   1143  -1656       O  
ATOM    381  CB  GLN A  95       5.634  -8.372 -35.014  1.00 86.42           C  
ANISOU  381  CB  GLN A  95     7317  14470  11047  -2725   1282  -1710       C  
ATOM    382  CG  GLN A  95       7.029  -7.839 -35.217  1.00 89.46           C  
ANISOU  382  CG  GLN A  95     7459  14907  11623  -2423   1395  -1757       C  
ATOM    383  CD  GLN A  95       7.530  -7.152 -33.978  1.00 88.59           C  
ANISOU  383  CD  GLN A  95     7616  14514  11531  -2227   1477  -1804       C  
ATOM    384  NE2 GLN A  95       7.946  -5.899 -34.139  1.00 91.16           N  
ANISOU  384  NE2 GLN A  95     7909  14849  11879  -2182   1692  -1911       N  
ATOM    385  OE1 GLN A  95       7.553  -7.733 -32.883  1.00 86.97           O  
ANISOU  385  OE1 GLN A  95     7644  14088  11313  -2127   1354  -1748       O  
ATOM    386  N   SER A  96       2.472  -6.872 -34.072  1.00 80.05           N  
ANISOU  386  N   SER A  96     7317  13333   9766  -3379   1431  -1789       N  
ATOM    387  CA  SER A  96       1.336  -7.197 -33.248  1.00 78.73           C  
ANISOU  387  CA  SER A  96     7513  12945   9456  -3525   1351  -1748       C  
ATOM    388  C   SER A  96       0.442  -5.987 -33.150  1.00 79.78           C  
ANISOU  388  C   SER A  96     7876  12992   9446  -3733   1491  -1804       C  
ATOM    389  O   SER A  96       0.928  -4.856 -33.062  1.00 82.00           O  
ANISOU  389  O   SER A  96     8142  13262   9753  -3660   1637  -1870       O  
ATOM    390  CB  SER A  96       1.804  -7.577 -31.852  1.00 76.85           C  
ANISOU  390  CB  SER A  96     7469  12445   9284  -3265   1271  -1708       C  
ATOM    391  OG  SER A  96       0.708  -7.678 -30.966  1.00 75.63           O  
ANISOU  391  OG  SER A  96     7672  12060   9003  -3384   1229  -1679       O  
ATOM    392  N   THR A  97      -0.864  -6.224 -33.174  1.00 79.90           N  
ANISOU  392  N   THR A  97     8117  12939   9304  -3998   1446  -1778       N  
ATOM    393  CA  THR A  97      -1.828  -5.148 -33.109  1.00 78.95           C  
ANISOU  393  CA  THR A  97     8238  12726   9034  -4219   1559  -1815       C  
ATOM    394  C   THR A  97      -3.146  -5.580 -32.489  1.00 77.66           C  
ANISOU  394  C   THR A  97     8432  12341   8734  -4383   1477  -1762       C  
ATOM    395  O   THR A  97      -3.675  -6.639 -32.826  1.00 82.27           O  
ANISOU  395  O   THR A  97     9020  12966   9272  -4506   1370  -1723       O  
ATOM    396  CB  THR A  97      -2.133  -4.694 -34.532  1.00 81.33           C  
ANISOU  396  CB  THR A  97     8337  13303   9260  -4490   1655  -1865       C  
ATOM    397  CG2 THR A  97      -2.904  -3.393 -34.524  1.00 81.61           C  
ANISOU  397  CG2 THR A  97     8594  13262   9151  -4701   1794  -1912       C  
ATOM    398  OG1 THR A  97      -0.907  -4.551 -35.262  1.00 81.89           O  
ANISOU  398  OG1 THR A  97     8021  13615   9479  -4330   1719  -1908       O  
ATOM    399  N   HIS A  98      -3.680  -4.760 -31.597  1.00 74.57           N  
ANISOU  399  N   HIS A  98     8341  11716   8277  -4387   1530  -1760       N  
ATOM    400  CA  HIS A  98      -4.938  -5.071 -30.951  1.00 72.86           C  
ANISOU  400  CA  HIS A  98     8472  11265   7945  -4515   1469  -1709       C  
ATOM    401  C   HIS A  98      -5.808  -3.843 -30.967  1.00 73.65           C  
ANISOU  401  C   HIS A  98     8799  11275   7910  -4719   1573  -1726       C  
ATOM    402  O   HIS A  98      -5.312  -2.712 -30.940  1.00 75.13           O  
ANISOU  402  O   HIS A  98     8943  11493   8108  -4679   1680  -1765       O  
ATOM    403  CB  HIS A  98      -4.708  -5.505 -29.506  1.00 70.35           C  
ANISOU  403  CB  HIS A  98     8325  10696   7709  -4249   1388  -1656       C  
ATOM    404  CG  HIS A  98      -3.668  -6.576 -29.344  1.00 69.89           C  
ANISOU  404  CG  HIS A  98     8056  10708   7791  -4015   1291  -1638       C  
ATOM    405  CD2 HIS A  98      -2.348  -6.492 -29.064  1.00 69.15           C  
ANISOU  405  CD2 HIS A  98     7766  10665   7841  -3751   1293  -1650       C  
ATOM    406  ND1 HIS A  98      -3.951  -7.923 -29.450  1.00 70.18           N  
ANISOU  406  ND1 HIS A  98     8088  10754   7820  -4050   1171  -1600       N  
ATOM    407  CE1 HIS A  98      -2.847  -8.620 -29.255  1.00 69.39           C  
ANISOU  407  CE1 HIS A  98     7794  10719   7853  -3819   1096  -1583       C  
ATOM    408  NE2 HIS A  98      -1.860  -7.775 -29.016  1.00 68.89           N  
ANISOU  408  NE2 HIS A  98     7613  10673   7887  -3628   1170  -1612       N  
ATOM    409  N   ARG A  99      -7.113  -4.052 -31.054  1.00 73.54           N  
ANISOU  409  N   ARG A  99     9036  11148   7758  -4955   1547  -1697       N  
ATOM    410  CA  ARG A  99      -8.051  -2.959 -30.854  1.00 73.56           C  
ANISOU  410  CA  ARG A  99     9320  11000   7629  -5131   1621  -1689       C  
ATOM    411  C   ARG A  99      -8.891  -3.332 -29.659  1.00 69.43           C  
ANISOU  411  C   ARG A  99     9135  10156   7090  -5054   1544  -1616       C  
ATOM    412  O   ARG A  99      -9.434  -4.439 -29.613  1.00 67.95           O  
ANISOU  412  O   ARG A  99     9031   9902   6886  -5089   1465  -1592       O  
ATOM    413  CB  ARG A  99      -8.938  -2.709 -32.090  1.00 77.13           C  
ANISOU  413  CB  ARG A  99     9794  11594   7919  -5507   1676  -1719       C  
ATOM    414  CG  ARG A  99      -9.693  -1.378 -32.029  1.00 78.25           C  
ANISOU  414  CG  ARG A  99    10183  11624   7925  -5696   1770  -1718       C  
ATOM    415  CD  ARG A  99     -10.415  -1.008 -33.321  1.00 80.72           C  
ANISOU  415  CD  ARG A  99    10490  12108   8073  -6079   1843  -1757       C  
ATOM    416  NE  ARG A  99      -9.518  -0.504 -34.359  1.00 82.68           N  
ANISOU  416  NE  ARG A  99    10383  12683   8349  -6133   1947  -1836       N  
ATOM    417  CZ  ARG A  99      -9.074   0.755 -34.456  1.00 82.23           C  
ANISOU  417  CZ  ARG A  99    10279  12689   8276  -6145   2074  -1881       C  
ATOM    418  NH1 ARG A  99      -9.416   1.700 -33.580  1.00 79.94           N1+
ANISOU  418  NH1 ARG A  99    10275  12168   7932  -6119   2099  -1847       N1+
ATOM    419  NH2 ARG A  99      -8.259   1.069 -35.460  1.00 84.08           N  
ANISOU  419  NH2 ARG A  99    10167  13231   8546  -6185   2179  -1961       N  
ATOM    420  N   VAL A 100      -8.975  -2.424 -28.689  1.00 66.50           N  
ANISOU  420  N   VAL A 100     8953   9592   6725  -4947   1570  -1581       N  
ATOM    421  CA  VAL A 100      -9.821  -2.640 -27.531  1.00 64.87           C  
ANISOU  421  CA  VAL A 100     9061   9078   6509  -4868   1507  -1503       C  
ATOM    422  C   VAL A 100     -10.639  -1.406 -27.190  1.00 65.77           C  
ANISOU  422  C   VAL A 100     9445   9026   6520  -4991   1555  -1461       C  
ATOM    423  O   VAL A 100     -10.260  -0.302 -27.534  1.00 66.40           O  
ANISOU  423  O   VAL A 100     9460   9210   6559  -5064   1633  -1489       O  
ATOM    424  CB  VAL A 100      -9.014  -3.073 -26.294  1.00 62.26           C  
ANISOU  424  CB  VAL A 100     8688   8637   6331  -4526   1442  -1467       C  
ATOM    425  CG1 VAL A 100      -8.172  -4.296 -26.622  1.00 62.16           C  
ANISOU  425  CG1 VAL A 100     8418   8783   6417  -4405   1384  -1500       C  
ATOM    426  CG2 VAL A 100      -8.151  -1.940 -25.762  1.00 60.99           C  
ANISOU  426  CG2 VAL A 100     8466   8485   6222  -4383   1489  -1468       C  
ATOM    427  N   PRO A 101     -11.778  -1.608 -26.524  1.00 67.48           N  
ANISOU  427  N   PRO A 101     9971   8979   6690  -5018   1511  -1390       N  
ATOM    428  CA  PRO A 101     -12.678  -0.541 -26.097  1.00 69.16           C  
ANISOU  428  CA  PRO A 101    10471   8994   6808  -5121   1531  -1324       C  
ATOM    429  C   PRO A 101     -12.032   0.478 -25.185  1.00 68.31           C  
ANISOU  429  C   PRO A 101    10362   8832   6761  -4943   1533  -1281       C  
ATOM    430  O   PRO A 101     -12.079   1.674 -25.464  1.00 71.24           O  
ANISOU  430  O   PRO A 101    10785   9241   7042  -5087   1590  -1280       O  
ATOM    431  CB  PRO A 101     -13.769  -1.287 -25.320  1.00 69.95           C  
ANISOU  431  CB  PRO A 101    10853   8808   6915  -5066   1468  -1253       C  
ATOM    432  CG  PRO A 101     -13.773  -2.666 -25.882  1.00 69.89           C  
ANISOU  432  CG  PRO A 101    10744   8891   6921  -5102   1444  -1308       C  
ATOM    433  CD  PRO A 101     -12.368  -2.948 -26.315  1.00 68.85           C  
ANISOU  433  CD  PRO A 101    10242   9037   6881  -4990   1445  -1375       C  
ATOM    434  N   VAL A 102     -11.438  -0.008 -24.103  1.00 66.15           N  
ANISOU  434  N   VAL A 102    10036   8473   6627  -4651   1470  -1246       N  
ATOM    435  CA  VAL A 102     -10.893   0.837 -23.060  1.00 64.79           C  
ANISOU  435  CA  VAL A 102     9887   8220   6509  -4475   1452  -1189       C  
ATOM    436  C   VAL A 102      -9.485   0.375 -22.727  1.00 62.48           C  
ANISOU  436  C   VAL A 102     9330   8055   6354  -4231   1438  -1234       C  
ATOM    437  O   VAL A 102      -9.251  -0.818 -22.541  1.00 62.66           O  
ANISOU  437  O   VAL A 102     9262   8078   6465  -4093   1388  -1247       O  
ATOM    438  CB  VAL A 102     -11.774   0.758 -21.800  1.00 64.80           C  
ANISOU  438  CB  VAL A 102    10149   7927   6542  -4353   1374  -1069       C  
ATOM    439  CG1 VAL A 102     -11.038   1.281 -20.568  1.00 63.30           C  
ANISOU  439  CG1 VAL A 102     9932   7677   6443  -4122   1329  -1006       C  
ATOM    440  CG2 VAL A 102     -13.070   1.525 -22.019  1.00 66.11           C  
ANISOU  440  CG2 VAL A 102    10600   7944   6573  -4579   1387  -1007       C  
ATOM    441  N   LEU A 103      -8.563   1.322 -22.632  1.00 61.30           N  
ANISOU  441  N   LEU A 103     9077   8002   6213  -4186   1482  -1258       N  
ATOM    442  CA  LEU A 103      -7.181   1.023 -22.288  1.00 59.95           C  
ANISOU  442  CA  LEU A 103     8681   7933   6166  -3957   1477  -1300       C  
ATOM    443  C   LEU A 103      -6.743   1.925 -21.144  1.00 61.37           C  
ANISOU  443  C   LEU A 103     8949   8004   6364  -3830   1457  -1238       C  
ATOM    444  O   LEU A 103      -7.022   3.131 -21.147  1.00 62.73           O  
ANISOU  444  O   LEU A 103     9249   8151   6435  -3970   1496  -1214       O  
ATOM    445  CB  LEU A 103      -6.260   1.246 -23.486  1.00 59.59           C  
ANISOU  445  CB  LEU A 103     8376   8149   6117  -4028   1576  -1414       C  
ATOM    446  CG  LEU A 103      -4.872   0.603 -23.392  1.00 57.10           C  
ANISOU  446  CG  LEU A 103     7804   7950   5943  -3791   1568  -1467       C  
ATOM    447  CD1 LEU A 103      -4.961  -0.895 -23.585  1.00 57.07           C  
ANISOU  447  CD1 LEU A 103     7703   7970   6011  -3718   1489  -1466       C  
ATOM    448  CD2 LEU A 103      -3.900   1.191 -24.397  1.00 57.51           C  
ANISOU  448  CD2 LEU A 103     7623   8230   5997  -3835   1687  -1572       C  
ATOM    449  N   MET A 104      -6.041   1.340 -20.174  1.00 61.08           N  
ANISOU  449  N   MET A 104     8849   7912   6445  -3582   1391  -1210       N  
ATOM    450  CA  MET A 104      -5.615   2.063 -18.992  1.00 59.76           C  
ANISOU  450  CA  MET A 104     8762   7644   6300  -3459   1354  -1143       C  
ATOM    451  C   MET A 104      -4.386   1.399 -18.432  1.00 57.50           C  
ANISOU  451  C   MET A 104     8308   7401   6138  -3219   1323  -1169       C  
ATOM    452  O   MET A 104      -4.092   0.257 -18.786  1.00 58.24           O  
ANISOU  452  O   MET A 104     8262   7559   6308  -3134   1306  -1214       O  
ATOM    453  CB  MET A 104      -6.729   2.048 -17.953  1.00 61.77           C  
ANISOU  453  CB  MET A 104     9249   7674   6549  -3432   1264  -1011       C  
ATOM    454  CG  MET A 104      -6.981   0.690 -17.333  1.00 62.99           C  
ANISOU  454  CG  MET A 104     9395   7731   6810  -3258   1191   -979       C  
ATOM    455  SD  MET A 104      -8.335   0.829 -16.153  1.00 69.12           S  
ANISOU  455  SD  MET A 104    10438   8239   7584  -3222   1111   -826       S  
ATOM    456  CE  MET A 104      -7.435   1.391 -14.706  1.00 66.69           C  
ANISOU  456  CE  MET A 104    10098   7895   7345  -3026   1045   -745       C  
ATOM    457  N   PRO A 105      -3.673   2.094 -17.532  1.00 56.24           N  
ANISOU  457  N   PRO A 105     8174   7201   5992  -3121   1308  -1136       N  
ATOM    458  CA  PRO A 105      -2.497   1.464 -16.957  1.00 53.83           C  
ANISOU  458  CA  PRO A 105     7733   6923   5798  -2901   1277  -1158       C  
ATOM    459  C   PRO A 105      -2.845   0.360 -15.980  1.00 50.56           C  
ANISOU  459  C   PRO A 105     7358   6382   5470  -2742   1171  -1081       C  
ATOM    460  O   PRO A 105      -3.940   0.337 -15.425  1.00 49.08           O  
ANISOU  460  O   PRO A 105     7331   6056   5262  -2772   1119   -990       O  
ATOM    461  CB  PRO A 105      -1.787   2.611 -16.225  1.00 54.23           C  
ANISOU  461  CB  PRO A 105     7844   6951   5812  -2882   1291  -1136       C  
ATOM    462  CG  PRO A 105      -2.764   3.737 -16.125  1.00 55.05           C  
ANISOU  462  CG  PRO A 105     8143   6981   5793  -3071   1293  -1066       C  
ATOM    463  CD  PRO A 105      -4.015   3.353 -16.843  1.00 56.62           C  
ANISOU  463  CD  PRO A 105     8405   7154   5954  -3202   1293  -1054       C  
ATOM    464  N   GLY A 106      -1.895  -0.541 -15.785  1.00 49.63           N  
ANISOU  464  N   GLY A 106     7096   6311   5449  -2571   1145  -1117       N  
ATOM    465  CA  GLY A 106      -2.020  -1.616 -14.823  1.00 49.57           C  
ANISOU  465  CA  GLY A 106     7109   6202   5522  -2414   1055  -1056       C  
ATOM    466  C   GLY A 106      -2.276  -1.103 -13.423  1.00 49.93           C  
ANISOU  466  C   GLY A 106     7295   6107   5570  -2348    994   -946       C  
ATOM    467  O   GLY A 106      -1.703  -0.083 -12.999  1.00 50.57           O  
ANISOU  467  O   GLY A 106     7402   6196   5616  -2356   1003   -927       O  
ATOM    468  N   LEU A 107      -3.136  -1.826 -12.711  1.00 50.22           N  
ANISOU  468  N   LEU A 107     7417   6019   5645  -2286    936   -872       N  
ATOM    469  CA  LEU A 107      -3.581  -1.434 -11.379  1.00 51.32           C  
ANISOU  469  CA  LEU A 107     7675   6024   5799  -2218    872   -751       C  
ATOM    470  C   LEU A 107      -2.602  -1.804 -10.288  1.00 50.35           C  
ANISOU  470  C   LEU A 107     7482   5901   5749  -2047    818   -723       C  
ATOM    471  O   LEU A 107      -1.870  -2.807 -10.394  1.00 51.42           O  
ANISOU  471  O   LEU A 107     7502   6092   5941  -1948    814   -783       O  
ATOM    472  CB  LEU A 107      -4.894  -2.108 -11.031  1.00 51.99           C  
ANISOU  472  CB  LEU A 107     7874   5969   5911  -2201    847   -688       C  
ATOM    473  CG  LEU A 107      -6.093  -1.666 -11.841  1.00 53.59           C  
ANISOU  473  CG  LEU A 107     8207   6119   6036  -2375    886   -683       C  
ATOM    474  CD1 LEU A 107      -7.219  -2.666 -11.621  1.00 54.97           C  
ANISOU  474  CD1 LEU A 107     8481   6157   6250  -2336    880   -654       C  
ATOM    475  CD2 LEU A 107      -6.509  -0.260 -11.446  1.00 53.40           C  
ANISOU  475  CD2 LEU A 107     8309   6034   5946  -2459    864   -589       C  
ATOM    476  N   TRP A 108      -2.622  -0.986  -9.236  1.00 48.70           N  
ANISOU  476  N   TRP A 108     7347   5632   5527  -2026    769   -624       N  
ATOM    477  CA  TRP A 108      -1.839  -1.221  -8.033  1.00 48.36           C  
ANISOU  477  CA  TRP A 108     7259   5578   5538  -1887    708   -574       C  
ATOM    478  C   TRP A 108      -2.774  -1.375  -6.860  1.00 50.26           C  
ANISOU  478  C   TRP A 108     7577   5696   5826  -1815    643   -443       C  
ATOM    479  O   TRP A 108      -3.693  -0.546  -6.685  1.00 53.38           O  
ANISOU  479  O   TRP A 108     8083   6018   6182  -1891    622   -354       O  
ATOM    480  CB  TRP A 108      -0.989  -0.016  -7.668  1.00 47.31           C  
ANISOU  480  CB  TRP A 108     7143   5490   5343  -1938    699   -555       C  
ATOM    481  CG  TRP A 108       0.224   0.186  -8.438  1.00 46.61           C  
ANISOU  481  CG  TRP A 108     6972   5511   5227  -1959    764   -674       C  
ATOM    482  CD1 TRP A 108       0.323   0.322  -9.778  1.00 47.76           C  
ANISOU  482  CD1 TRP A 108     7069   5737   5340  -2047    851   -781       C  
ATOM    483  CD2 TRP A 108       1.541   0.366  -7.909  1.00 45.88           C  
ANISOU  483  CD2 TRP A 108     6838   5457   5135  -1896    755   -696       C  
ATOM    484  CE2 TRP A 108       2.397   0.568  -8.999  1.00 45.84           C  
ANISOU  484  CE2 TRP A 108     6761   5544   5111  -1928    846   -824       C  
ATOM    485  CE3 TRP A 108       2.079   0.339  -6.622  1.00 44.75           C  
ANISOU  485  CE3 TRP A 108     6711   5280   5012  -1816    680   -622       C  
ATOM    486  NE1 TRP A 108       1.628   0.533 -10.130  1.00 48.07           N  
ANISOU  486  NE1 TRP A 108     7027   5860   5376  -2019    903   -871       N  
ATOM    487  CZ2 TRP A 108       3.752   0.757  -8.851  1.00 45.40           C  
ANISOU  487  CZ2 TRP A 108     6667   5526   5054  -1874    871   -881       C  
ATOM    488  CZ3 TRP A 108       3.416   0.524  -6.478  1.00 45.51           C  
ANISOU  488  CZ3 TRP A 108     6778   5420   5094  -1785    699   -678       C  
ATOM    489  CH2 TRP A 108       4.247   0.735  -7.587  1.00 45.94           C  
ANISOU  489  CH2 TRP A 108     6780   5545   5130  -1807    796   -809       C  
ATOM    490  N   ASP A 109      -2.513  -2.382  -6.026  1.00 48.58           N  
ANISOU  490  N   ASP A 109     7302   5460   5694  -1670    609   -425       N  
ATOM    491  CA  ASP A 109      -2.959  -2.297  -4.655  1.00 47.46           C  
ANISOU  491  CA  ASP A 109     7193   5239   5601  -1583    542   -293       C  
ATOM    492  C   ASP A 109      -1.775  -1.992  -3.768  1.00 46.22           C  
ANISOU  492  C   ASP A 109     6974   5147   5440  -1537    490   -263       C  
ATOM    493  O   ASP A 109      -0.740  -2.626  -3.890  1.00 46.07           O  
ANISOU  493  O   ASP A 109     6875   5194   5437  -1487    504   -344       O  
ATOM    494  CB  ASP A 109      -3.643  -3.551  -4.187  1.00 46.28           C  
ANISOU  494  CB  ASP A 109     7035   5010   5540  -1464    550   -279       C  
ATOM    495  CG  ASP A 109      -4.331  -3.328  -2.887  1.00 46.85           C  
ANISOU  495  CG  ASP A 109     7137   4995   5669  -1378    496   -135       C  
ATOM    496  OD1 ASP A 109      -3.655  -3.378  -1.842  1.00 47.11           O  
ANISOU  496  OD1 ASP A 109     7098   5067   5734  -1301    444    -81       O  
ATOM    497  OD2 ASP A 109      -5.527  -3.008  -2.899  1.00 48.17           O1-
ANISOU  497  OD2 ASP A 109     7400   5056   5847  -1395    500    -67       O1-
ATOM    498  N   CYS A 110      -1.948  -1.038  -2.865  1.00 47.30           N  
ANISOU  498  N   CYS A 110     7155   5262   5555  -1561    424   -140       N  
ATOM    499  CA  CYS A 110      -0.844  -0.533  -2.071  1.00 49.62           C  
ANISOU  499  CA  CYS A 110     7416   5622   5816  -1564    371   -107       C  
ATOM    500  C   CYS A 110      -0.810  -1.027  -0.623  1.00 50.05           C  
ANISOU  500  C   CYS A 110     7413   5661   5941  -1448    300     -2       C  
ATOM    501  O   CYS A 110       0.074  -0.606   0.118  1.00 51.47           O  
ANISOU  501  O   CYS A 110     7572   5896   6086  -1466    248     36       O  
ATOM    502  CB  CYS A 110      -0.873   0.990  -2.037  1.00 52.17           C  
ANISOU  502  CB  CYS A 110     7826   5959   6036  -1709    337    -39       C  
ATOM    503  SG  CYS A 110      -0.623   1.790  -3.619  1.00 55.71           S  
ANISOU  503  SG  CYS A 110     8334   6455   6378  -1872    434   -168       S  
ATOM    504  N   HIS A 111      -1.746  -1.888  -0.207  1.00 48.85           N  
ANISOU  504  N   HIS A 111     7240   5437   5884  -1338    304     43       N  
ATOM    505  CA  HIS A 111      -1.695  -2.510   1.124  1.00 46.95           C  
ANISOU  505  CA  HIS A 111     6922   5195   5721  -1218    257    126       C  
ATOM    506  C   HIS A 111      -2.141  -3.950   0.955  1.00 46.13           C  
ANISOU  506  C   HIS A 111     6785   5042   5699  -1108    324     56       C  
ATOM    507  O   HIS A 111      -3.313  -4.239   0.891  1.00 46.12           O  
ANISOU  507  O   HIS A 111     6824   4946   5752  -1062    357     86       O  
ATOM    508  CB  HIS A 111      -2.597  -1.775   2.113  1.00 47.98           C  
ANISOU  508  CB  HIS A 111     7066   5281   5885  -1200    183    303       C  
ATOM    509  CG  HIS A 111      -2.399  -2.174   3.535  1.00 49.44           C  
ANISOU  509  CG  HIS A 111     7147   5498   6138  -1099    127    400       C  
ATOM    510  CD2 HIS A 111      -2.177  -3.379   4.118  1.00 52.00           C  
ANISOU  510  CD2 HIS A 111     7383   5834   6536   -984    159    369       C  
ATOM    511  ND1 HIS A 111      -2.415  -1.258   4.555  1.00 52.68           N  
ANISOU  511  ND1 HIS A 111     7533   5947   6536  -1129     23    559       N  
ATOM    512  CE1 HIS A 111      -2.188  -1.872   5.704  1.00 55.55           C  
ANISOU  512  CE1 HIS A 111     7784   6354   6969  -1034     -4    618       C  
ATOM    513  NE2 HIS A 111      -2.062  -3.165   5.471  1.00 55.58           N  
ANISOU  513  NE2 HIS A 111     7753   6339   7027   -943     82    503       N  
ATOM    514  N   MET A 112      -1.187  -4.851   0.861  1.00 44.68           N  
ANISOU  514  N   MET A 112     6544   4915   5518  -1074    346    -38       N  
ATOM    515  CA  MET A 112      -1.489  -6.240   0.672  1.00 45.47           C  
ANISOU  515  CA  MET A 112     6621   4980   5675   -994    405   -110       C  
ATOM    516  C   MET A 112      -0.692  -7.015   1.689  1.00 46.64           C  
ANISOU  516  C   MET A 112     6690   5178   5855   -918    379    -99       C  
ATOM    517  O   MET A 112       0.283  -6.517   2.205  1.00 45.79           O  
ANISOU  517  O   MET A 112     6552   5139   5709   -947    323    -69       O  
ATOM    518  CB  MET A 112      -1.076  -6.632  -0.721  1.00 46.47           C  
ANISOU  518  CB  MET A 112     6763   5135   5756  -1055    451   -248       C  
ATOM    519  CG  MET A 112      -1.885  -5.952  -1.806  1.00 48.57           C  
ANISOU  519  CG  MET A 112     7106   5364   5983  -1150    488   -270       C  
ATOM    520  SD  MET A 112      -3.574  -6.578  -1.917  1.00 52.08           S  
ANISOU  520  SD  MET A 112     7633   5673   6481  -1116    545   -250       S  
ATOM    521  CE  MET A 112      -3.264  -8.311  -2.249  1.00 50.80           C  
ANISOU  521  CE  MET A 112     7430   5528   6343  -1066    594   -366       C  
ATOM    522  N   HIS A 113      -1.086  -8.244   1.965  1.00 49.46           N  
ANISOU  522  N   HIS A 113     7024   5498   6268   -837    426   -127       N  
ATOM    523  CA  HIS A 113      -0.479  -9.002   3.037  1.00 50.62           C  
ANISOU  523  CA  HIS A 113     7099   5689   6444   -772    410   -106       C  
ATOM    524  C   HIS A 113      -0.163 -10.405   2.533  1.00 48.54           C  
ANISOU  524  C   HIS A 113     6838   5427   6177   -755    459   -220       C  
ATOM    525  O   HIS A 113      -1.026 -11.283   2.577  1.00 51.17           O  
ANISOU  525  O   HIS A 113     7191   5698   6554   -706    526   -243       O  
ATOM    526  CB  HIS A 113      -1.444  -9.057   4.242  1.00 56.08           C  
ANISOU  526  CB  HIS A 113     7751   6336   7221   -680    420      7       C  
ATOM    527  CG  HIS A 113      -1.508  -7.783   5.052  1.00 65.55           C  
ANISOU  527  CG  HIS A 113     8918   7564   8424   -695    339    149       C  
ATOM    528  CD2 HIS A 113      -2.566  -7.138   5.608  1.00 73.47           C  
ANISOU  528  CD2 HIS A 113     9913   8513   9488   -648    322    273       C  
ATOM    529  ND1 HIS A 113      -0.392  -7.054   5.426  1.00 69.43           N  
ANISOU  529  ND1 HIS A 113     9382   8149   8847   -770    257    184       N  
ATOM    530  CE1 HIS A 113      -0.761  -6.003   6.144  1.00 71.42           C  
ANISOU  530  CE1 HIS A 113     9614   8416   9108   -786    188    322       C  
ATOM    531  NE2 HIS A 113      -2.077  -6.027   6.274  1.00 72.11           N  
ANISOU  531  NE2 HIS A 113     9704   8416   9279   -706    219    386       N  
ATOM    532  N   PHE A 114       1.069 -10.627   2.075  1.00 45.54           N  
ANISOU  532  N   PHE A 114     6444   5115   5743   -795    427   -288       N  
ATOM    533  CA  PHE A 114       1.488 -11.956   1.571  1.00 45.74           C  
ANISOU  533  CA  PHE A 114     6470   5152   5756   -788    451   -383       C  
ATOM    534  C   PHE A 114       1.612 -13.017   2.663  1.00 45.50           C  
ANISOU  534  C   PHE A 114     6408   5128   5750   -732    463   -365       C  
ATOM    535  O   PHE A 114       2.723 -13.384   3.061  1.00 43.43           O  
ANISOU  535  O   PHE A 114     6121   4921   5457   -738    417   -371       O  
ATOM    536  CB  PHE A 114       2.826 -11.865   0.846  1.00 44.93           C  
ANISOU  536  CB  PHE A 114     6356   5114   5601   -828    405   -446       C  
ATOM    537  CG  PHE A 114       2.710 -11.445  -0.572  1.00 47.51           C  
ANISOU  537  CG  PHE A 114     6700   5446   5905   -882    423   -512       C  
ATOM    538  CD1 PHE A 114       2.109 -10.242  -0.910  1.00 50.51           C  
ANISOU  538  CD1 PHE A 114     7107   5808   6276   -927    437   -483       C  
ATOM    539  CD2 PHE A 114       3.206 -12.236  -1.589  1.00 48.20           C  
ANISOU  539  CD2 PHE A 114     6772   5567   5976   -897    422   -598       C  
ATOM    540  CE1 PHE A 114       2.003  -9.839  -2.241  1.00 49.03           C  
ANISOU  540  CE1 PHE A 114     6929   5639   6061   -992    463   -549       C  
ATOM    541  CE2 PHE A 114       3.099 -11.835  -2.917  1.00 47.59           C  
ANISOU  541  CE2 PHE A 114     6687   5515   5881   -952    441   -656       C  
ATOM    542  CZ  PHE A 114       2.500 -10.635  -3.240  1.00 46.68           C  
ANISOU  542  CZ  PHE A 114     6598   5385   5754  -1002    468   -637       C  
ATOM    543  N   GLY A 115       0.477 -13.536   3.120  1.00 47.06           N  
ANISOU  543  N   GLY A 115     6617   5263   6001   -683    531   -346       N  
ATOM    544  CA  GLY A 115       0.458 -14.463   4.245  1.00 50.97           C  
ANISOU  544  CA  GLY A 115     7074   5766   6525   -629    564   -325       C  
ATOM    545  C   GLY A 115       0.337 -15.933   3.858  1.00 53.32           C  
ANISOU  545  C   GLY A 115     7417   6041   6800   -641    625   -420       C  
ATOM    546  O   GLY A 115       1.049 -16.788   4.386  1.00 54.69           O  
ANISOU  546  O   GLY A 115     7571   6260   6946   -648    616   -437       O  
ATOM    547  N   GLY A 116      -0.602 -16.237   2.972  1.00 53.67           N  
ANISOU  547  N   GLY A 116     7534   6012   6846   -661    687   -478       N  
ATOM    548  CA  GLY A 116      -0.859 -17.629   2.620  1.00 52.87           C  
ANISOU  548  CA  GLY A 116     7494   5884   6712   -692    749   -565       C  
ATOM    549  C   GLY A 116      -1.129 -18.547   3.804  1.00 51.48           C  
ANISOU  549  C   GLY A 116     7306   5693   6563   -639    825   -558       C  
ATOM    550  O   GLY A 116      -0.772 -19.707   3.781  1.00 49.75           O  
ANISOU  550  O   GLY A 116     7118   5494   6292   -683    844   -618       O  
ATOM    551  N   ASP A 117      -1.802 -18.013   4.820  1.00 52.40           N  
ANISOU  551  N   ASP A 117     7372   5775   6762   -548    871   -479       N  
ATOM    552  CA  ASP A 117      -2.022 -18.710   6.084  1.00 56.29           C  
ANISOU  552  CA  ASP A 117     7816   6272   7298   -483    950   -458       C  
ATOM    553  C   ASP A 117      -2.855 -19.980   5.898  1.00 54.86           C  
ANISOU  553  C   ASP A 117     7732   6007   7104   -491   1084   -553       C  
ATOM    554  O   ASP A 117      -3.709 -20.013   5.039  1.00 55.65           O  
ANISOU  554  O   ASP A 117     7933   6012   7200   -511   1134   -603       O  
ATOM    555  CB  ASP A 117      -2.718 -17.756   7.090  1.00 60.97           C  
ANISOU  555  CB  ASP A 117     8322   6845   8000   -371    968   -342       C  
ATOM    556  CG  ASP A 117      -1.956 -16.401   7.251  1.00 63.78           C  
ANISOU  556  CG  ASP A 117     8602   7281   8351   -388    830   -243       C  
ATOM    557  OD1 ASP A 117      -0.742 -16.416   7.549  1.00 66.43           O  
ANISOU  557  OD1 ASP A 117     8892   7718   8630   -442    750   -234       O  
ATOM    558  OD2 ASP A 117      -2.553 -15.321   7.031  1.00 63.08           O1-
ANISOU  558  OD2 ASP A 117     8518   7147   8303   -362    803   -179       O1-
ATOM    559  N   ASP A 118      -2.596 -21.011   6.706  1.00 54.31           N  
ANISOU  559  N   ASP A 118     7644   5974   7019   -491   1146   -581       N  
ATOM    560  CA  ASP A 118      -3.517 -22.141   6.837  1.00 55.84           C  
ANISOU  560  CA  ASP A 118     7924   6080   7211   -484   1305   -663       C  
ATOM    561  C   ASP A 118      -4.792 -21.601   7.490  1.00 58.85           C  
ANISOU  561  C   ASP A 118     8277   6360   7722   -342   1416   -610       C  
ATOM    562  O   ASP A 118      -4.750 -20.641   8.273  1.00 61.28           O  
ANISOU  562  O   ASP A 118     8459   6709   8117   -250   1369   -497       O  
ATOM    563  CB  ASP A 118      -2.926 -23.290   7.691  1.00 55.82           C  
ANISOU  563  CB  ASP A 118     7897   6149   7161   -518   1355   -698       C  
ATOM    564  CG  ASP A 118      -1.704 -23.960   7.050  1.00 53.12           C  
ANISOU  564  CG  ASP A 118     7604   5890   6690   -657   1244   -745       C  
ATOM    565  OD1 ASP A 118      -1.505 -23.804   5.841  1.00 53.43           O  
ANISOU  565  OD1 ASP A 118     7708   5917   6677   -725   1163   -776       O  
ATOM    566  OD2 ASP A 118      -0.943 -24.639   7.755  1.00 48.64           O1-
ANISOU  566  OD2 ASP A 118     7007   5400   6074   -698   1237   -746       O1-
ATOM    567  N   ASP A 119      -5.922 -22.225   7.182  1.00 62.61           N  
ANISOU  567  N   ASP A 119     8878   6702   8210   -325   1561   -687       N  
ATOM    568  CA  ASP A 119      -7.229 -21.760   7.672  1.00 64.77           C  
ANISOU  568  CA  ASP A 119     9152   6844   8612   -179   1676   -643       C  
ATOM    569  C   ASP A 119      -7.563 -22.231   9.084  1.00 61.54           C  
ANISOU  569  C   ASP A 119     8640   6442   8299    -52   1809   -618       C  
ATOM    570  O   ASP A 119      -8.709 -22.121   9.524  1.00 61.77           O  
ANISOU  570  O   ASP A 119     8681   6348   8442     84   1939   -599       O  
ATOM    571  CB  ASP A 119      -8.338 -22.221   6.716  1.00 69.13           C  
ANISOU  571  CB  ASP A 119     9906   7227   9132   -220   1787   -742       C  
ATOM    572  CG  ASP A 119      -9.581 -21.358   6.799  1.00 73.29           C  
ANISOU  572  CG  ASP A 119    10465   7603   9779    -89   1847   -678       C  
ATOM    573  OD1 ASP A 119      -9.464 -20.182   7.230  1.00 74.91           O  
ANISOU  573  OD1 ASP A 119    10546   7850  10068     -2   1747   -547       O  
ATOM    574  OD2 ASP A 119     -10.669 -21.859   6.423  1.00 77.08           O1-
ANISOU  574  OD2 ASP A 119    11111   7916  10261    -82   1989   -755       O1-
ATOM    575  N   TYR A 120      -6.567 -22.737   9.797  1.00 58.31           N  
ANISOU  575  N   TYR A 120     8129   6177   7848    -95   1779   -615       N  
ATOM    576  CA  TYR A 120      -6.798 -23.321  11.105  1.00 59.74           C  
ANISOU  576  CA  TYR A 120     8207   6390   8103     -1   1916   -606       C  
ATOM    577  C   TYR A 120      -7.009 -22.303  12.226  1.00 59.58           C  
ANISOU  577  C   TYR A 120     7984   6420   8233    157   1888   -453       C  
ATOM    578  O   TYR A 120      -7.996 -22.386  12.965  1.00 60.17           O  
ANISOU  578  O   TYR A 120     8004   6420   8437    310   2034   -431       O  
ATOM    579  CB  TYR A 120      -5.655 -24.244  11.466  1.00 59.03           C  
ANISOU  579  CB  TYR A 120     8091   6439   7900   -125   1892   -654       C  
ATOM    580  CG  TYR A 120      -5.984 -25.111  12.640  1.00 60.65           C  
ANISOU  580  CG  TYR A 120     8226   6666   8151    -64   2071   -685       C  
ATOM    581  CD1 TYR A 120      -6.847 -26.197  12.512  1.00 61.81           C  
ANISOU  581  CD1 TYR A 120     8513   6694   8280    -65   2276   -812       C  
ATOM    582  CD2 TYR A 120      -5.440 -24.839  13.885  1.00 61.62           C  
ANISOU  582  CD2 TYR A 120     8147   6933   8332    -14   2044   -589       C  
ATOM    583  CE1 TYR A 120      -7.136 -26.997  13.593  1.00 64.08           C  
ANISOU  583  CE1 TYR A 120     8734   7005   8609    -10   2460   -850       C  
ATOM    584  CE2 TYR A 120      -5.723 -25.637  14.979  1.00 63.55           C  
ANISOU  584  CE2 TYR A 120     8309   7217   8621     37   2220   -618       C  
ATOM    585  CZ  TYR A 120      -6.569 -26.714  14.831  1.00 65.51           C  
ANISOU  585  CZ  TYR A 120     8693   7344   8855     45   2433   -752       C  
ATOM    586  OH  TYR A 120      -6.847 -27.500  15.928  1.00 69.71           O  
ANISOU  586  OH  TYR A 120     9139   7917   9432     97   2625   -789       O  
ATOM    587  N   TYR A 121      -6.096 -21.348  12.346  1.00 58.31           N  
ANISOU  587  N   TYR A 121     7715   6385   8057    119   1702   -348       N  
ATOM    588  CA  TYR A 121      -6.189 -20.342  13.397  1.00 59.73           C  
ANISOU  588  CA  TYR A 121     7699   6637   8359    237   1645   -189       C  
ATOM    589  C   TYR A 121      -6.848 -19.051  12.869  1.00 63.51           C  
ANISOU  589  C   TYR A 121     8202   7023   8905    303   1559    -95       C  
ATOM    590  O   TYR A 121      -6.502 -18.550  11.791  1.00 64.04           O  
ANISOU  590  O   TYR A 121     8377   7068   8887    202   1449   -117       O  
ATOM    591  CB  TYR A 121      -4.798 -20.009  13.934  1.00 56.80           C  
ANISOU  591  CB  TYR A 121     7208   6457   7917    136   1492   -121       C  
ATOM    592  CG  TYR A 121      -4.121 -21.073  14.781  1.00 54.52           C  
ANISOU  592  CG  TYR A 121     6853   6284   7577     78   1559   -167       C  
ATOM    593  CD1 TYR A 121      -4.650 -21.467  16.002  1.00 55.40           C  
ANISOU  593  CD1 TYR A 121     6818   6437   7794    187   1695   -134       C  
ATOM    594  CD2 TYR A 121      -2.916 -21.648  14.379  1.00 51.30           C  
ANISOU  594  CD2 TYR A 121     6523   5951   7016    -87   1481   -237       C  
ATOM    595  CE1 TYR A 121      -4.010 -22.419  16.783  1.00 54.20           C  
ANISOU  595  CE1 TYR A 121     6606   6404   7584    115   1760   -177       C  
ATOM    596  CE2 TYR A 121      -2.276 -22.593  15.149  1.00 49.89           C  
ANISOU  596  CE2 TYR A 121     6301   5877   6778   -157   1533   -273       C  
ATOM    597  CZ  TYR A 121      -2.819 -22.981  16.344  1.00 51.86           C  
ANISOU  597  CZ  TYR A 121     6412   6173   7121    -67   1675   -247       C  
ATOM    598  OH  TYR A 121      -2.158 -23.930  17.096  1.00 51.25           O  
ANISOU  598  OH  TYR A 121     6294   6207   6969   -157   1731   -286       O  
ATOM    599  N   ASN A 122      -7.764 -18.486  13.652  1.00 68.69           N  
ANISOU  599  N   ASN A 122     8748   7634   9715    471   1605     16       N  
ATOM    600  CA  ASN A 122      -8.440 -17.240  13.269  1.00 70.98           C  
ANISOU  600  CA  ASN A 122     9062   7835  10073    535   1518    125       C  
ATOM    601  C   ASN A 122      -7.555 -15.998  13.394  1.00 69.17           C  
ANISOU  601  C   ASN A 122     8735   7744   9803    458   1303    254       C  
ATOM    602  O   ASN A 122      -7.571 -15.132  12.518  1.00 68.59           O  
ANISOU  602  O   ASN A 122     8758   7622   9683    396   1200    278       O  
ATOM    603  CB  ASN A 122      -9.707 -17.081  14.098  1.00 75.85           C  
ANISOU  603  CB  ASN A 122     9594   8351  10875    751   1632    214       C  
ATOM    604  CG  ASN A 122     -10.622 -18.282  13.982  1.00 81.42           C  
ANISOU  604  CG  ASN A 122    10417   8898  11619    830   1865     75       C  
ATOM    605  ND2 ASN A 122     -10.869 -18.756  12.755  1.00 82.69           N  
ANISOU  605  ND2 ASN A 122    10812   8930  11677    729   1913    -65       N  
ATOM    606  OD1 ASN A 122     -11.054 -18.820  14.998  1.00 84.24           O  
ANISOU  606  OD1 ASN A 122    10653   9263  12089    966   2006     86       O  
ATOM    607  N   ASP A 123      -6.747 -15.931  14.447  1.00 69.22           N  
ANISOU  607  N   ASP A 123     8563   7924   9812    441   1243    332       N  
ATOM    608  CA  ASP A 123      -5.913 -14.754  14.696  1.00 68.26           C  
ANISOU  608  CA  ASP A 123     8354   7936   9647    357   1048    460       C  
ATOM    609  C   ASP A 123      -4.517 -14.886  14.049  1.00 66.24           C  
ANISOU  609  C   ASP A 123     8182   7768   9219    167    951    373       C  
ATOM    610  O   ASP A 123      -4.275 -15.770  13.215  1.00 64.79           O  
ANISOU  610  O   ASP A 123     8133   7531   8954    102   1014    224       O  
ATOM    611  CB  ASP A 123      -5.815 -14.473  16.207  1.00 68.10           C  
ANISOU  611  CB  ASP A 123     8094   8062   9718    428   1017    610       C  
ATOM    612  CG  ASP A 123      -5.104 -15.588  16.976  1.00 69.49           C  
ANISOU  612  CG  ASP A 123     8183   8363   9859    386   1096    542       C  
ATOM    613  OD1 ASP A 123      -4.841 -16.665  16.381  1.00 69.21           O  
ANISOU  613  OD1 ASP A 123     8277   8278   9740    324   1191    379       O  
ATOM    614  OD2 ASP A 123      -4.829 -15.385  18.184  1.00 69.04           O1-
ANISOU  614  OD2 ASP A 123     7924   8457   9852    404   1059    657       O1-
ATOM    615  N   TYR A 124      -3.622 -13.977  14.429  1.00 64.22           N  
ANISOU  615  N   TYR A 124     7850   7642   8910     79    796    472       N  
ATOM    616  CA  TYR A 124      -2.255 -13.951  13.937  1.00 60.13           C  
ANISOU  616  CA  TYR A 124     7403   7201   8243    -85    700    409       C  
ATOM    617  C   TYR A 124      -1.447 -15.224  14.218  1.00 57.06           C  
ANISOU  617  C   TYR A 124     7017   6877   7786   -145    761    307       C  
ATOM    618  O   TYR A 124      -0.380 -15.426  13.624  1.00 55.43           O  
ANISOU  618  O   TYR A 124     6902   6699   7459   -266    700    231       O  
ATOM    619  CB  TYR A 124      -1.526 -12.764  14.565  1.00 61.47           C  
ANISOU  619  CB  TYR A 124     7485   7497   8376   -164    541    548       C  
ATOM    620  CG  TYR A 124      -1.899 -11.401  14.037  1.00 62.82           C  
ANISOU  620  CG  TYR A 124     7702   7620   8548   -178    442    632       C  
ATOM    621  CD1 TYR A 124      -2.518 -11.239  12.789  1.00 62.61           C  
ANISOU  621  CD1 TYR A 124     7822   7451   8516   -162    477    558       C  
ATOM    622  CD2 TYR A 124      -1.558 -10.258  14.762  1.00 64.43           C  
ANISOU  622  CD2 TYR A 124     7815   7929   8737   -234    306    786       C  
ATOM    623  CE1 TYR A 124      -2.818  -9.982  12.305  1.00 62.59           C  
ANISOU  623  CE1 TYR A 124     7871   7411   8499   -197    387    634       C  
ATOM    624  CE2 TYR A 124      -1.841  -8.999  14.278  1.00 64.27           C  
ANISOU  624  CE2 TYR A 124     7853   7870   8697   -272    211    863       C  
ATOM    625  CZ  TYR A 124      -2.477  -8.865  13.052  1.00 63.52           C  
ANISOU  625  CZ  TYR A 124     7904   7631   8601   -250    256    786       C  
ATOM    626  OH  TYR A 124      -2.757  -7.615  12.571  1.00 60.07           O  
ANISOU  626  OH  TYR A 124     7532   7158   8133   -303    166    861       O  
ATOM    627  N   THR A 125      -1.932 -16.068  15.124  1.00 54.23           N  
ANISOU  627  N   THR A 125     6559   6542   7503    -62    880    306       N  
ATOM    628  CA  THR A 125      -1.278 -17.335  15.408  1.00 52.57           C  
ANISOU  628  CA  THR A 125     6363   6388   7224   -127    952    208       C  
ATOM    629  C   THR A 125      -1.037 -18.125  14.132  1.00 50.62           C  
ANISOU  629  C   THR A 125     6308   6046   6881   -197    985     52       C  
ATOM    630  O   THR A 125      -0.024 -18.777  13.995  1.00 49.16           O  
ANISOU  630  O   THR A 125     6178   5914   6586   -307    953    -13       O  
ATOM    631  CB  THR A 125      -2.112 -18.183  16.391  1.00 54.29           C  
ANISOU  631  CB  THR A 125     6467   6613   7548    -11   1120    206       C  
ATOM    632  CG2 THR A 125      -1.340 -19.384  16.865  1.00 53.07           C  
ANISOU  632  CG2 THR A 125     6312   6546   7308   -105   1182    124       C  
ATOM    633  OG1 THR A 125      -2.454 -17.387  17.527  1.00 56.47           O  
ANISOU  633  OG1 THR A 125     6541   6979   7935     72   1084    367       O  
ATOM    634  N   SER A 126      -1.966 -18.059  13.191  1.00 52.75           N  
ANISOU  634  N   SER A 126     6680   6175   7187   -139   1039      1       N  
ATOM    635  CA  SER A 126      -1.779 -18.708  11.891  1.00 54.45           C  
ANISOU  635  CA  SER A 126     7067   6311   7309   -218   1053   -134       C  
ATOM    636  C   SER A 126      -0.466 -18.248  11.222  1.00 53.28           C  
ANISOU  636  C   SER A 126     6968   6227   7049   -342    898   -142       C  
ATOM    637  O   SER A 126       0.258 -19.047  10.626  1.00 51.58           O  
ANISOU  637  O   SER A 126     6840   6020   6739   -429    884   -233       O  
ATOM    638  CB  SER A 126      -2.982 -18.446  10.959  1.00 55.81           C  
ANISOU  638  CB  SER A 126     7340   6331   7533   -156   1113   -167       C  
ATOM    639  OG  SER A 126      -2.961 -17.125  10.443  1.00 56.88           O  
ANISOU  639  OG  SER A 126     7481   6455   7675   -165    997    -94       O  
ATOM    640  N   GLY A 127      -0.180 -16.954  11.317  1.00 53.07           N  
ANISOU  640  N   GLY A 127     6889   6240   7034   -347    785    -43       N  
ATOM    641  CA  GLY A 127       1.072 -16.395  10.814  1.00 52.25           C  
ANISOU  641  CA  GLY A 127     6828   6191   6832   -453    654    -46       C  
ATOM    642  C   GLY A 127       2.313 -17.158  11.243  1.00 49.60           C  
ANISOU  642  C   GLY A 127     6496   5940   6409   -538    619    -78       C  
ATOM    643  O   GLY A 127       3.170 -17.494  10.424  1.00 49.20           O  
ANISOU  643  O   GLY A 127     6539   5881   6274   -609    570   -151       O  
ATOM    644  N   LEU A 128       2.404 -17.442  12.526  1.00 48.63           N  
ANISOU  644  N   LEU A 128     6269   5899   6307   -530    644    -18       N  
ATOM    645  CA  LEU A 128       3.532 -18.195  13.036  1.00 48.63           C  
ANISOU  645  CA  LEU A 128     6281   5979   6219   -624    616    -42       C  
ATOM    646  C   LEU A 128       3.416 -19.702  12.746  1.00 47.25           C  
ANISOU  646  C   LEU A 128     6181   5766   6007   -639    714   -154       C  
ATOM    647  O   LEU A 128       4.390 -20.342  12.347  1.00 46.96           O  
ANISOU  647  O   LEU A 128     6233   5738   5871   -728    666   -212       O  
ATOM    648  CB  LEU A 128       3.683 -17.937  14.533  1.00 51.39           C  
ANISOU  648  CB  LEU A 128     6484   6449   6594   -633    607     67       C  
ATOM    649  CG  LEU A 128       4.746 -18.722  15.314  1.00 53.53           C  
ANISOU  649  CG  LEU A 128     6752   6815   6772   -742    591     57       C  
ATOM    650  CD1 LEU A 128       4.933 -18.083  16.677  1.00 54.45           C  
ANISOU  650  CD1 LEU A 128     6714   7064   6908   -771    548    187       C  
ATOM    651  CD2 LEU A 128       4.443 -20.216  15.489  1.00 55.57           C  
ANISOU  651  CD2 LEU A 128     7032   7062   7020   -738    721    -32       C  
ATOM    652  N   ALA A 129       2.242 -20.274  12.940  1.00 47.03           N  
ANISOU  652  N   ALA A 129     6126   5689   6055   -557    853   -184       N  
ATOM    653  CA  ALA A 129       2.109 -21.730  12.850  1.00 48.43           C  
ANISOU  653  CA  ALA A 129     6375   5840   6183   -592    960   -288       C  
ATOM    654  C   ALA A 129       2.229 -22.285  11.414  1.00 47.56           C  
ANISOU  654  C   ALA A 129     6425   5646   6001   -646    939   -393       C  
ATOM    655  O   ALA A 129       2.713 -23.410  11.212  1.00 44.00           O  
ANISOU  655  O   ALA A 129     6059   5202   5459   -731    952   -465       O  
ATOM    656  CB  ALA A 129       0.792 -22.167  13.453  1.00 50.59           C  
ANISOU  656  CB  ALA A 129     6590   6074   6560   -486   1132   -300       C  
ATOM    657  N   THR A 130       1.783 -21.484  10.437  1.00 46.72           N  
ANISOU  657  N   THR A 130     6354   5467   5930   -606    901   -394       N  
ATOM    658  CA  THR A 130       1.807 -21.877   9.030  1.00 44.48           C  
ANISOU  658  CA  THR A 130     6195   5118   5588   -657    877   -482       C  
ATOM    659  C   THR A 130       3.220 -21.989   8.489  1.00 40.89           C  
ANISOU  659  C   THR A 130     5786   4713   5037   -747    743   -494       C  
ATOM    660  O   THR A 130       4.020 -21.055   8.591  1.00 39.04           O  
ANISOU  660  O   THR A 130     5511   4521   4799   -750    640   -434       O  
ATOM    661  CB  THR A 130       1.067 -20.868   8.148  1.00 44.88           C  
ANISOU  661  CB  THR A 130     6260   5096   5695   -606    863   -471       C  
ATOM    662  CG2 THR A 130       1.023 -21.345   6.718  1.00 45.03           C  
ANISOU  662  CG2 THR A 130     6391   5063   5653   -671    848   -561       C  
ATOM    663  OG1 THR A 130      -0.272 -20.720   8.619  1.00 48.32           O  
ANISOU  663  OG1 THR A 130     6667   5463   6227   -511    983   -451       O  
ATOM    664  N   HIS A 131       3.505 -23.138   7.894  1.00 38.59           N  
ANISOU  664  N   HIS A 131     5588   4409   4666   -821    745   -571       N  
ATOM    665  CA  HIS A 131       4.812 -23.382   7.355  1.00 37.79           C  
ANISOU  665  CA  HIS A 131     5534   4342   4481   -893    619   -578       C  
ATOM    666  C   HIS A 131       4.937 -22.581   6.074  1.00 37.49           C  
ANISOU  666  C   HIS A 131     5508   4276   4460   -875    542   -588       C  
ATOM    667  O   HIS A 131       4.022 -22.586   5.258  1.00 36.72           O  
ANISOU  667  O   HIS A 131     5437   4127   4386   -864    591   -632       O  
ATOM    668  CB  HIS A 131       5.005 -24.870   7.080  1.00 38.39           C  
ANISOU  668  CB  HIS A 131     5706   4416   4466   -982    635   -644       C  
ATOM    669  CG  HIS A 131       6.413 -25.231   6.754  1.00 37.73           C  
ANISOU  669  CG  HIS A 131     5669   4366   4299  -1049    499   -633       C  
ATOM    670  CD2 HIS A 131       7.296 -26.036   7.382  1.00 39.14           C  
ANISOU  670  CD2 HIS A 131     5891   4582   4396  -1123    462   -620       C  
ATOM    671  ND1 HIS A 131       7.067 -24.730   5.656  1.00 36.82           N  
ANISOU  671  ND1 HIS A 131     5565   4242   4184  -1037    387   -631       N  
ATOM    672  CE1 HIS A 131       8.288 -25.220   5.607  1.00 37.48           C  
ANISOU  672  CE1 HIS A 131     5697   4345   4197  -1087    283   -614       C  
ATOM    673  NE2 HIS A 131       8.455 -26.017   6.647  1.00 38.62           N  
ANISOU  673  NE2 HIS A 131     5872   4516   4286  -1147    320   -606       N  
ATOM    674  N   PRO A 132       6.072 -21.904   5.878  1.00 36.88           N  
ANISOU  674  N   PRO A 132     5417   4230   4365   -879    429   -553       N  
ATOM    675  CA  PRO A 132       6.142 -20.974   4.751  1.00 36.56           C  
ANISOU  675  CA  PRO A 132     5370   4171   4352   -854    378   -563       C  
ATOM    676  C   PRO A 132       5.991 -21.623   3.398  1.00 36.50           C  
ANISOU  676  C   PRO A 132     5407   4143   4317   -888    362   -630       C  
ATOM    677  O   PRO A 132       5.591 -20.951   2.465  1.00 37.07           O  
ANISOU  677  O   PRO A 132     5465   4200   4421   -872    361   -649       O  
ATOM    678  CB  PRO A 132       7.520 -20.352   4.868  1.00 36.71           C  
ANISOU  678  CB  PRO A 132     5384   4219   4345   -857    275   -525       C  
ATOM    679  CG  PRO A 132       7.927 -20.579   6.283  1.00 37.44           C  
ANISOU  679  CG  PRO A 132     5466   4348   4412   -880    279   -474       C  
ATOM    680  CD  PRO A 132       7.250 -21.824   6.748  1.00 37.25           C  
ANISOU  680  CD  PRO A 132     5457   4325   4371   -906    360   -503       C  
ATOM    681  N   ALA A 133       6.326 -22.901   3.278  1.00 36.43           N  
ANISOU  681  N   ALA A 133     5455   4144   4243   -947    343   -662       N  
ATOM    682  CA  ALA A 133       6.011 -23.670   2.068  1.00 36.15           C  
ANISOU  682  CA  ALA A 133     5464   4100   4171  -1001    329   -719       C  
ATOM    683  C   ALA A 133       4.519 -23.669   1.775  1.00 36.17           C  
ANISOU  683  C   ALA A 133     5487   4055   4201  -1009    442   -761       C  
ATOM    684  O   ALA A 133       4.105 -23.465   0.643  1.00 35.52           O  
ANISOU  684  O   ALA A 133     5407   3966   4123  -1032    432   -794       O  
ATOM    685  CB  ALA A 133       6.533 -25.105   2.160  1.00 36.17           C  
ANISOU  685  CB  ALA A 133     5537   4120   4084  -1083    291   -736       C  
ATOM    686  N   SER A 134       3.701 -23.914   2.786  1.00 36.85           N  
ANISOU  686  N   SER A 134     5588   4106   4305   -990    555   -762       N  
ATOM    687  CA  SER A 134       2.271 -23.905   2.547  1.00 38.02           C  
ANISOU  687  CA  SER A 134     5775   4185   4485   -985    671   -801       C  
ATOM    688  C   SER A 134       1.900 -22.509   2.085  1.00 38.27           C  
ANISOU  688  C   SER A 134     5756   4198   4589   -926    658   -771       C  
ATOM    689  O   SER A 134       1.224 -22.346   1.085  1.00 38.15           O  
ANISOU  689  O   SER A 134     5776   4148   4570   -959    675   -808       O  
ATOM    690  CB  SER A 134       1.495 -24.311   3.786  1.00 38.13           C  
ANISOU  690  CB  SER A 134     5800   4160   4529   -947    804   -801       C  
ATOM    691  OG  SER A 134       1.963 -25.552   4.265  1.00 38.07           O  
ANISOU  691  OG  SER A 134     5840   4181   4442  -1016    817   -830       O  
ATOM    692  N   SER A 135       2.400 -21.503   2.780  1.00 40.25           N  
ANISOU  692  N   SER A 135     5930   4475   4888   -858    619   -701       N  
ATOM    693  CA  SER A 135       2.139 -20.125   2.393  1.00 42.56           C  
ANISOU  693  CA  SER A 135     6182   4755   5233   -818    599   -666       C  
ATOM    694  C   SER A 135       2.583 -19.815   0.978  1.00 42.30           C  
ANISOU  694  C   SER A 135     6151   4749   5171   -864    528   -703       C  
ATOM    695  O   SER A 135       1.863 -19.186   0.220  1.00 42.42           O  
ANISOU  695  O   SER A 135     6177   4735   5205   -876    553   -717       O  
ATOM    696  CB  SER A 135       2.847 -19.175   3.329  1.00 43.63           C  
ANISOU  696  CB  SER A 135     6247   4933   5399   -769    548   -586       C  
ATOM    697  OG  SER A 135       2.411 -19.396   4.648  1.00 47.10           O  
ANISOU  697  OG  SER A 135     6656   5367   5875   -725    612   -542       O  
ATOM    698  N   GLY A 136       3.775 -20.256   0.622  1.00 42.32           N  
ANISOU  698  N   GLY A 136     6141   4808   5130   -891    440   -714       N  
ATOM    699  CA  GLY A 136       4.307 -19.980  -0.699  1.00 42.46           C  
ANISOU  699  CA  GLY A 136     6133   4865   5135   -918    371   -743       C  
ATOM    700  C   GLY A 136       3.421 -20.545  -1.775  1.00 42.86           C  
ANISOU  700  C   GLY A 136     6222   4904   5160   -989    405   -801       C  
ATOM    701  O   GLY A 136       3.049 -19.829  -2.702  1.00 45.95           O  
ANISOU  701  O   GLY A 136     6591   5302   5566  -1009    410   -819       O  
ATOM    702  N   ALA A 137       3.051 -21.816  -1.634  1.00 42.22           N  
ANISOU  702  N   ALA A 137     6206   4805   5030  -1045    434   -833       N  
ATOM    703  CA  ALA A 137       2.160 -22.485  -2.578  1.00 41.82           C  
ANISOU  703  CA  ALA A 137     6216   4738   4934  -1140    469   -890       C  
ATOM    704  C   ALA A 137       0.885 -21.675  -2.774  1.00 42.30           C  
ANISOU  704  C   ALA A 137     6309   4730   5033  -1137    562   -901       C  
ATOM    705  O   ALA A 137       0.493 -21.370  -3.904  1.00 41.50           O  
ANISOU  705  O   ALA A 137     6208   4643   4916  -1201    555   -929       O  
ATOM    706  CB  ALA A 137       1.816 -23.867  -2.075  1.00 41.99           C  
ANISOU  706  CB  ALA A 137     6330   4730   4893  -1200    517   -921       C  
ATOM    707  N   ARG A 138       0.251 -21.313  -1.665  1.00 42.68           N  
ANISOU  707  N   ARG A 138     6380   4706   5131  -1064    646   -871       N  
ATOM    708  CA  ARG A 138      -0.980 -20.538  -1.746  1.00 43.87           C  
ANISOU  708  CA  ARG A 138     6573   4772   5324  -1047    729   -867       C  
ATOM    709  C   ARG A 138      -0.751 -19.173  -2.395  1.00 44.53           C  
ANISOU  709  C   ARG A 138     6594   4890   5436  -1038    675   -835       C  
ATOM    710  O   ARG A 138      -1.575 -18.721  -3.191  1.00 46.19           O  
ANISOU  710  O   ARG A 138     6848   5062   5639  -1091    709   -857       O  
ATOM    711  CB  ARG A 138      -1.634 -20.351  -0.382  1.00 42.83           C  
ANISOU  711  CB  ARG A 138     6453   4562   5258   -948    817   -822       C  
ATOM    712  CG  ARG A 138      -2.172 -21.627   0.217  1.00 44.23           C  
ANISOU  712  CG  ARG A 138     6709   4685   5412   -959    915   -867       C  
ATOM    713  CD  ARG A 138      -3.143 -21.378   1.385  1.00 45.94           C  
ANISOU  713  CD  ARG A 138     6936   4807   5714   -850   1032   -830       C  
ATOM    714  NE  ARG A 138      -3.345 -22.610   2.160  1.00 46.14           N  
ANISOU  714  NE  ARG A 138     7007   4807   5719   -849   1128   -873       N  
ATOM    715  CZ  ARG A 138      -2.591 -23.001   3.186  1.00 44.80           C  
ANISOU  715  CZ  ARG A 138     6765   4703   5552   -813   1116   -844       C  
ATOM    716  NH1 ARG A 138      -1.593 -22.244   3.641  1.00 43.31           N1+
ANISOU  716  NH1 ARG A 138     6462   4604   5391   -770   1010   -767       N1+
ATOM    717  NH2 ARG A 138      -2.850 -24.172   3.762  1.00 46.28           N  
ANISOU  717  NH2 ARG A 138     7010   4868   5708   -834   1219   -897       N  
ATOM    718  N   LEU A 139       0.370 -18.525  -2.085  1.00 42.79           N  
ANISOU  718  N   LEU A 139     6284   4736   5235   -985    600   -793       N  
ATOM    719  CA  LEU A 139       0.615 -17.180  -2.600  1.00 42.18           C  
ANISOU  719  CA  LEU A 139     6158   4689   5180   -981    565   -769       C  
ATOM    720  C   LEU A 139       0.792 -17.190  -4.118  1.00 42.00           C  
ANISOU  720  C   LEU A 139     6114   4726   5119  -1065    534   -826       C  
ATOM    721  O   LEU A 139       0.600 -16.172  -4.786  1.00 40.85           O  
ANISOU  721  O   LEU A 139     5949   4594   4978  -1093    539   -827       O  
ATOM    722  CB  LEU A 139       1.829 -16.569  -1.911  1.00 41.64           C  
ANISOU  722  CB  LEU A 139     6020   4673   5129   -918    500   -720       C  
ATOM    723  CG  LEU A 139       1.532 -16.106  -0.490  1.00 42.02           C  
ANISOU  723  CG  LEU A 139     6068   4680   5219   -850    525   -645       C  
ATOM    724  CD1 LEU A 139       2.796 -15.866   0.305  1.00 41.82           C  
ANISOU  724  CD1 LEU A 139     5992   4708   5188   -815    458   -603       C  
ATOM    725  CD2 LEU A 139       0.698 -14.845  -0.504  1.00 42.54           C  
ANISOU  725  CD2 LEU A 139     6146   4701   5316   -845    552   -599       C  
ATOM    726  N   ALA A 140       1.150 -18.355  -4.656  1.00 42.44           N  
ANISOU  726  N   ALA A 140     6168   4826   5133  -1115    499   -869       N  
ATOM    727  CA  ALA A 140       1.242 -18.538  -6.100  1.00 43.42           C  
ANISOU  727  CA  ALA A 140     6256   5022   5221  -1204    463   -916       C  
ATOM    728  C   ALA A 140      -0.113 -18.335  -6.729  1.00 43.52           C  
ANISOU  728  C   ALA A 140     6344   4983   5209  -1295    537   -946       C  
ATOM    729  O   ALA A 140      -0.244 -17.534  -7.645  1.00 44.37           O  
ANISOU  729  O   ALA A 140     6414   5132   5314  -1345    537   -959       O  
ATOM    730  CB  ALA A 140       1.777 -19.928  -6.451  1.00 42.65           C  
ANISOU  730  CB  ALA A 140     6152   4978   5076  -1250    402   -940       C  
ATOM    731  N   ARG A 141      -1.106 -19.071  -6.241  1.00 43.39           N  
ANISOU  731  N   ARG A 141     6442   4872   5171  -1322    607   -960       N  
ATOM    732  CA  ARG A 141      -2.447 -18.972  -6.776  1.00 43.74           C  
ANISOU  732  CA  ARG A 141     6593   4840   5185  -1412    685   -990       C  
ATOM    733  C   ARG A 141      -2.934 -17.544  -6.709  1.00 44.23           C  
ANISOU  733  C   ARG A 141     6657   4856   5293  -1378    718   -952       C  
ATOM    734  O   ARG A 141      -3.517 -17.028  -7.664  1.00 45.77           O  
ANISOU  734  O   ARG A 141     6882   5053   5457  -1475    735   -974       O  
ATOM    735  CB  ARG A 141      -3.408 -19.879  -6.016  1.00 44.11           C  
ANISOU  735  CB  ARG A 141     6776   4764   5220  -1412    777  -1011       C  
ATOM    736  CG  ARG A 141      -4.855 -19.774  -6.482  1.00 45.02           C  
ANISOU  736  CG  ARG A 141     7035   4766   5306  -1497    871  -1043       C  
ATOM    737  CD  ARG A 141      -4.987 -20.234  -7.914  1.00 45.30           C  
ANISOU  737  CD  ARG A 141     7090   4873   5249  -1675    838  -1101       C  
ATOM    738  NE  ARG A 141      -6.332 -20.102  -8.441  1.00 46.55           N  
ANISOU  738  NE  ARG A 141     7402   4922   5364  -1782    924  -1135       N  
ATOM    739  CZ  ARG A 141      -7.333 -20.921  -8.150  1.00 48.18           C  
ANISOU  739  CZ  ARG A 141     7781   4995   5531  -1827   1023  -1178       C  
ATOM    740  NH1 ARG A 141      -7.141 -21.917  -7.295  1.00 47.52           N1+
ANISOU  740  NH1 ARG A 141     7725   4881   5447  -1771   1056  -1194       N1+
ATOM    741  NH2 ARG A 141      -8.532 -20.741  -8.719  1.00 49.42           N  
ANISOU  741  NH2 ARG A 141     8093   5043   5642  -1935   1099  -1209       N  
ATOM    742  N   GLY A 142      -2.683 -16.901  -5.579  1.00 44.24           N  
ANISOU  742  N   GLY A 142     6631   4821   5356  -1256    719   -890       N  
ATOM    743  CA  GLY A 142      -3.099 -15.525  -5.377  1.00 45.01           C  
ANISOU  743  CA  GLY A 142     6735   4875   5491  -1226    735   -835       C  
ATOM    744  C   GLY A 142      -2.478 -14.550  -6.357  1.00 45.94           C  
ANISOU  744  C   GLY A 142     6776   5092   5588  -1282    688   -846       C  
ATOM    745  O   GLY A 142      -3.156 -13.678  -6.886  1.00 48.04           O  
ANISOU  745  O   GLY A 142     7085   5329   5839  -1346    716   -839       O  
ATOM    746  N   CYS A 143      -1.184 -14.689  -6.606  1.00 46.48           N  
ANISOU  746  N   CYS A 143     6733   5272   5655  -1260    622   -862       N  
ATOM    747  CA  CYS A 143      -0.506 -13.794  -7.526  1.00 47.68           C  
ANISOU  747  CA  CYS A 143     6800   5518   5796  -1298    594   -881       C  
ATOM    748  C   CYS A 143      -1.024 -13.948  -8.946  1.00 47.63           C  
ANISOU  748  C   CYS A 143     6791   5563   5741  -1429    612   -940       C  
ATOM    749  O   CYS A 143      -1.182 -12.954  -9.652  1.00 50.35           O  
ANISOU  749  O   CYS A 143     7119   5943   6070  -1494    634   -949       O  
ATOM    750  CB  CYS A 143       0.993 -14.012  -7.470  1.00 49.19           C  
ANISOU  750  CB  CYS A 143     6884   5800   6006  -1228    527   -888       C  
ATOM    751  SG  CYS A 143       1.738 -13.261  -6.007  1.00 50.69           S  
ANISOU  751  SG  CYS A 143     7072   5955   6233  -1113    504   -818       S  
ATOM    752  N   TRP A 144      -1.304 -15.183  -9.347  1.00 46.55           N  
ANISOU  752  N   TRP A 144     6677   5436   5572  -1487    605   -977       N  
ATOM    753  CA  TRP A 144      -1.939 -15.473 -10.622  1.00 46.32           C  
ANISOU  753  CA  TRP A 144     6663   5452   5484  -1639    620  -1027       C  
ATOM    754  C   TRP A 144      -3.233 -14.680 -10.762  1.00 48.13           C  
ANISOU  754  C   TRP A 144     7015   5585   5687  -1718    695  -1021       C  
ATOM    755  O   TRP A 144      -3.412 -13.911 -11.718  1.00 48.59           O  
ANISOU  755  O   TRP A 144     7045   5703   5716  -1817    709  -1040       O  
ATOM    756  CB  TRP A 144      -2.221 -16.979 -10.741  1.00 45.89           C  
ANISOU  756  CB  TRP A 144     6661   5390   5384  -1699    606  -1058       C  
ATOM    757  CG  TRP A 144      -2.720 -17.384 -12.076  1.00 47.46           C  
ANISOU  757  CG  TRP A 144     6862   5659   5510  -1873    602  -1105       C  
ATOM    758  CD1 TRP A 144      -1.965 -17.690 -13.181  1.00 48.34           C  
ANISOU  758  CD1 TRP A 144     6827   5935   5604  -1936    529  -1125       C  
ATOM    759  CD2 TRP A 144      -4.093 -17.490 -12.486  1.00 48.00           C  
ANISOU  759  CD2 TRP A 144     7082   5643   5511  -2016    672  -1134       C  
ATOM    760  CE2 TRP A 144      -4.094 -17.864 -13.849  1.00 49.14           C  
ANISOU  760  CE2 TRP A 144     7165   5919   5588  -2182    634  -1172       C  
ATOM    761  CE3 TRP A 144      -5.320 -17.298 -11.839  1.00 47.70           C  
ANISOU  761  CE3 TRP A 144     7229   5429   5467  -2017    763  -1127       C  
ATOM    762  NE1 TRP A 144      -2.786 -17.983 -14.248  1.00 49.50           N  
ANISOU  762  NE1 TRP A 144     7014   6121   5671  -2123    544  -1162       N  
ATOM    763  CZ2 TRP A 144      -5.270 -18.064 -14.569  1.00 49.76           C  
ANISOU  763  CZ2 TRP A 144     7374   5956   5577  -2369    683  -1208       C  
ATOM    764  CZ3 TRP A 144      -6.499 -17.500 -12.561  1.00 49.10           C  
ANISOU  764  CZ3 TRP A 144     7547   5544   5563  -2187    819  -1165       C  
ATOM    765  CH2 TRP A 144      -6.459 -17.879 -13.913  1.00 50.06           C  
ANISOU  765  CH2 TRP A 144     7617   5800   5602  -2371    779  -1208       C  
ATOM    766  N   GLU A 145      -4.135 -14.875  -9.810  1.00 49.75           N  
ANISOU  766  N   GLU A 145     7357   5639   5907  -1674    747   -992       N  
ATOM    767  CA  GLU A 145      -5.469 -14.281  -9.884  1.00 51.98           C  
ANISOU  767  CA  GLU A 145     7785   5798   6168  -1739    817   -978       C  
ATOM    768  C   GLU A 145      -5.311 -12.763  -9.953  1.00 51.72           C  
ANISOU  768  C   GLU A 145     7715   5786   6150  -1733    810   -935       C  
ATOM    769  O   GLU A 145      -5.991 -12.098 -10.734  1.00 53.97           O  
ANISOU  769  O   GLU A 145     8058   6059   6387  -1854    840   -944       O  
ATOM    770  CB  GLU A 145      -6.327 -14.684  -8.676  1.00 52.20           C  
ANISOU  770  CB  GLU A 145     7944   5654   6237  -1645    876   -942       C  
ATOM    771  CG  GLU A 145      -6.600 -16.177  -8.528  1.00 53.17           C  
ANISOU  771  CG  GLU A 145     8135   5735   6332  -1664    907   -994       C  
ATOM    772  CD  GLU A 145      -7.737 -16.679  -9.403  1.00 57.98           C  
ANISOU  772  CD  GLU A 145     8899   6273   6858  -1827    968  -1052       C  
ATOM    773  OE1 GLU A 145      -8.390 -15.855 -10.090  1.00 61.00           O  
ANISOU  773  OE1 GLU A 145     9342   6627   7210  -1923    989  -1048       O  
ATOM    774  OE2 GLU A 145      -7.982 -17.912  -9.403  1.00 60.34           O1-
ANISOU  774  OE2 GLU A 145     9271   6541   7113  -1876    998  -1103       O1-
ATOM    775  N   ALA A 146      -4.420 -12.227  -9.124  1.00 49.58           N  
ANISOU  775  N   ALA A 146     7358   5545   5935  -1607    771   -887       N  
ATOM    776  CA  ALA A 146      -4.122 -10.803  -9.129  1.00 51.49           C  
ANISOU  776  CA  ALA A 146     7568   5817   6180  -1608    761   -848       C  
ATOM    777  C   ALA A 146      -3.865 -10.330 -10.544  1.00 52.90           C  
ANISOU  777  C   ALA A 146     7683   6116   6302  -1743    767   -909       C  
ATOM    778  O   ALA A 146      -4.514  -9.416 -11.034  1.00 54.58           O  
ANISOU  778  O   ALA A 146     7959   6306   6471  -1845    801   -900       O  
ATOM    779  CB  ALA A 146      -2.897 -10.508  -8.272  1.00 51.40           C  
ANISOU  779  CB  ALA A 146     7456   5858   6215  -1484    709   -814       C  
ATOM    780  N   LEU A 147      -2.919 -10.975 -11.210  1.00 52.89           N  
ANISOU  780  N   LEU A 147     7550   6244   6301  -1744    737   -966       N  
ATOM    781  CA  LEU A 147      -2.544 -10.580 -12.560  1.00 52.79           C  
ANISOU  781  CA  LEU A 147     7435   6370   6251  -1854    746  -1023       C  
ATOM    782  C   LEU A 147      -3.746 -10.732 -13.489  1.00 53.58           C  
ANISOU  782  C   LEU A 147     7624   6453   6280  -2029    788  -1053       C  
ATOM    783  O   LEU A 147      -4.075  -9.829 -14.267  1.00 52.36           O  
ANISOU  783  O   LEU A 147     7475   6341   6078  -2150    826  -1069       O  
ATOM    784  CB  LEU A 147      -1.386 -11.441 -13.051  1.00 53.16           C  
ANISOU  784  CB  LEU A 147     7322   6548   6326  -1805    694  -1065       C  
ATOM    785  CG  LEU A 147      -0.470 -10.802 -14.088  1.00 54.31           C  
ANISOU  785  CG  LEU A 147     7308   6850   6479  -1830    700  -1110       C  
ATOM    786  CD1 LEU A 147      -0.031  -9.393 -13.693  1.00 52.24           C  
ANISOU  786  CD1 LEU A 147     7049   6573   6226  -1787    738  -1094       C  
ATOM    787  CD2 LEU A 147       0.730 -11.713 -14.319  1.00 54.86           C  
ANISOU  787  CD2 LEU A 147     7229   7018   6598  -1734    634  -1128       C  
ATOM    788  N   GLN A 148      -4.410 -11.873 -13.371  1.00 52.19           N  
ANISOU  788  N   GLN A 148     7534   6209   6088  -2055    786  -1062       N  
ATOM    789  CA  GLN A 148      -5.587 -12.129 -14.140  1.00 52.57           C  
ANISOU  789  CA  GLN A 148     7700   6215   6058  -2228    827  -1090       C  
ATOM    790  C   GLN A 148      -6.613 -11.044 -13.982  1.00 53.15           C  
ANISOU  790  C   GLN A 148     7924   6166   6104  -2286    882  -1053       C  
ATOM    791  O   GLN A 148      -7.471 -10.918 -14.825  1.00 56.37           O  
ANISOU  791  O   GLN A 148     8421   6562   6437  -2457    919  -1078       O  
ATOM    792  CB  GLN A 148      -6.232 -13.441 -13.714  1.00 54.60           C  
ANISOU  792  CB  GLN A 148     8076   6367   6301  -2227    835  -1100       C  
ATOM    793  CG  GLN A 148      -6.672 -14.341 -14.878  1.00 56.69           C  
ANISOU  793  CG  GLN A 148     8361   6702   6478  -2418    832  -1161       C  
ATOM    794  CD  GLN A 148      -5.503 -14.795 -15.738  1.00 57.50           C  
ANISOU  794  CD  GLN A 148     8245   7020   6583  -2440    756  -1190       C  
ATOM    795  NE2 GLN A 148      -5.795 -15.522 -16.804  1.00 60.10           N  
ANISOU  795  NE2 GLN A 148     8559   7442   6833  -2617    736  -1230       N  
ATOM    796  OE1 GLN A 148      -4.355 -14.498 -15.443  1.00 56.29           O  
ANISOU  796  OE1 GLN A 148     7940   6946   6501  -2300    714  -1172       O  
ATOM    797  N   ASN A 149      -6.566 -10.282 -12.899  1.00 54.38           N  
ANISOU  797  N   ASN A 149     8119   6228   6314  -2157    881   -985       N  
ATOM    798  CA  ASN A 149      -7.514  -9.158 -12.692  1.00 58.15           C  
ANISOU  798  CA  ASN A 149     8741   6585   6767  -2207    916   -927       C  
ATOM    799  C   ASN A 149      -6.986  -7.776 -13.107  1.00 57.21           C  
ANISOU  799  C   ASN A 149     8552   6563   6621  -2262    914   -918       C  
ATOM    800  O   ASN A 149      -7.636  -6.765 -12.840  1.00 58.47           O  
ANISOU  800  O   ASN A 149     8827   6631   6757  -2299    927   -858       O  
ATOM    801  CB  ASN A 149      -7.915  -9.053 -11.214  1.00 60.07           C  
ANISOU  801  CB  ASN A 149     9077   6664   7083  -2043    910   -840       C  
ATOM    802  CG  ASN A 149      -9.054  -9.950 -10.829  1.00 62.35           C  
ANISOU  802  CG  ASN A 149     9525   6783   7381  -2027    955   -835       C  
ATOM    803  ND2 ASN A 149     -10.221  -9.349 -10.652  1.00 64.41           N  
ANISOU  803  ND2 ASN A 149     9957   6885   7630  -2060    990   -781       N  
ATOM    804  OD1 ASN A 149      -8.878 -11.154 -10.612  1.00 63.25           O  
ANISOU  804  OD1 ASN A 149     9618   6899   7514  -1976    960   -877       O  
ATOM    805  N   GLY A 150      -5.812  -7.722 -13.725  1.00 55.56           N  
ANISOU  805  N   GLY A 150     8162   6531   6415  -2263    900   -974       N  
ATOM    806  CA  GLY A 150      -5.216  -6.451 -14.121  1.00 55.86           C  
ANISOU  806  CA  GLY A 150     8131   6665   6428  -2311    917   -981       C  
ATOM    807  C   GLY A 150      -4.473  -5.718 -13.015  1.00 54.05           C  
ANISOU  807  C   GLY A 150     7883   6408   6247  -2172    888   -922       C  
ATOM    808  O   GLY A 150      -4.265  -4.508 -13.097  1.00 57.33           O  
ANISOU  808  O   GLY A 150     8309   6851   6623  -2227    907   -908       O  
ATOM    809  N   TYR A 151      -4.095  -6.432 -11.968  1.00 51.05           N  
ANISOU  809  N   TYR A 151     7483   5974   5938  -2011    842   -888       N  
ATOM    810  CA  TYR A 151      -3.248  -5.866 -10.950  1.00 49.41           C  
ANISOU  810  CA  TYR A 151     7241   5762   5769  -1891    806   -838       C  
ATOM    811  C   TYR A 151      -1.831  -6.263 -11.290  1.00 49.15           C  
ANISOU  811  C   TYR A 151     7046   5862   5768  -1823    794   -905       C  
ATOM    812  O   TYR A 151      -1.474  -7.440 -11.237  1.00 46.99           O  
ANISOU  812  O   TYR A 151     6710   5608   5536  -1749    765   -930       O  
ATOM    813  CB  TYR A 151      -3.659  -6.351  -9.569  1.00 48.38           C  
ANISOU  813  CB  TYR A 151     7181   5502   5698  -1762    767   -755       C  
ATOM    814  CG  TYR A 151      -4.847  -5.592  -9.072  1.00 48.10           C  
ANISOU  814  CG  TYR A 151     7294   5335   5647  -1797    771   -665       C  
ATOM    815  CD1 TYR A 151      -6.123  -5.978  -9.422  1.00 48.17           C  
ANISOU  815  CD1 TYR A 151     7423   5240   5639  -1863    806   -662       C  
ATOM    816  CD2 TYR A 151      -4.686  -4.445  -8.299  1.00 47.61           C  
ANISOU  816  CD2 TYR A 151     7261   5250   5578  -1779    737   -578       C  
ATOM    817  CE1 TYR A 151      -7.225  -5.263  -9.000  1.00 50.00           C  
ANISOU  817  CE1 TYR A 151     7802   5335   5860  -1887    806   -572       C  
ATOM    818  CE2 TYR A 151      -5.779  -3.729  -7.848  1.00 48.89           C  
ANISOU  818  CE2 TYR A 151     7556   5290   5729  -1809    724   -478       C  
ATOM    819  CZ  TYR A 151      -7.054  -4.137  -8.198  1.00 50.60           C  
ANISOU  819  CZ  TYR A 151     7892   5391   5941  -1853    760   -473       C  
ATOM    820  OH  TYR A 151      -8.171  -3.427  -7.761  1.00 51.77           O  
ANISOU  820  OH  TYR A 151     8185   5400   6086  -1872    745   -365       O  
ATOM    821  N   THR A 152      -1.037  -5.259 -11.650  1.00 49.81           N  
ANISOU  821  N   THR A 152     7070   6027   5826  -1853    820   -934       N  
ATOM    822  CA  THR A 152       0.330  -5.458 -12.117  1.00 49.71           C  
ANISOU  822  CA  THR A 152     6908   6133   5846  -1787    825  -1003       C  
ATOM    823  C   THR A 152       1.391  -4.997 -11.100  1.00 47.67           C  
ANISOU  823  C   THR A 152     6646   5853   5612  -1675    798   -973       C  
ATOM    824  O   THR A 152       2.597  -5.183 -11.314  1.00 46.05           O  
ANISOU  824  O   THR A 152     6339   5717   5442  -1598    799  -1024       O  
ATOM    825  CB  THR A 152       0.547  -4.703 -13.448  1.00 52.19           C  
ANISOU  825  CB  THR A 152     7145   6568   6115  -1907    901  -1081       C  
ATOM    826  CG2 THR A 152      -0.491  -5.138 -14.457  1.00 52.32           C  
ANISOU  826  CG2 THR A 152     7169   6617   6095  -2043    924  -1108       C  
ATOM    827  OG1 THR A 152       0.450  -3.283 -13.235  1.00 51.73           O  
ANISOU  827  OG1 THR A 152     7174   6487   5995  -1984    943  -1061       O  
ATOM    828  N   SER A 153       0.940  -4.395 -10.005  1.00 45.17           N  
ANISOU  828  N   SER A 153     6445   5441   5278  -1671    770   -886       N  
ATOM    829  CA  SER A 153       1.833  -4.013  -8.946  1.00 43.64           C  
ANISOU  829  CA  SER A 153     6261   5225   5096  -1588    733   -846       C  
ATOM    830  C   SER A 153       1.143  -4.150  -7.588  1.00 42.77           C  
ANISOU  830  C   SER A 153     6237   5010   5004  -1538    670   -733       C  
ATOM    831  O   SER A 153       0.003  -3.766  -7.409  1.00 41.60           O  
ANISOU  831  O   SER A 153     6176   4793   4837  -1595    669   -670       O  
ATOM    832  CB  SER A 153       2.321  -2.587  -9.167  1.00 43.89           C  
ANISOU  832  CB  SER A 153     6324   5293   5059  -1673    779   -864       C  
ATOM    833  OG  SER A 153       3.384  -2.550 -10.091  1.00 44.18           O  
ANISOU  833  OG  SER A 153     6258   5426   5103  -1658    839   -969       O  
ATOM    834  N   TYR A 154       1.858  -4.725  -6.640  1.00 42.74           N  
ANISOU  834  N   TYR A 154     6203   4994   5043  -1427    621   -704       N  
ATOM    835  CA  TYR A 154       1.387  -4.860  -5.281  1.00 44.12           C  
ANISOU  835  CA  TYR A 154     6425   5092   5245  -1368    565   -599       C  
ATOM    836  C   TYR A 154       2.440  -4.278  -4.327  1.00 45.65           C  
ANISOU  836  C   TYR A 154     6620   5305   5420  -1340    522   -558       C  
ATOM    837  O   TYR A 154       3.651  -4.425  -4.557  1.00 48.29           O  
ANISOU  837  O   TYR A 154     6909   5689   5750  -1310    529   -623       O  
ATOM    838  CB  TYR A 154       1.216  -6.343  -4.936  1.00 44.31           C  
ANISOU  838  CB  TYR A 154     6414   5089   5333  -1272    549   -605       C  
ATOM    839  CG  TYR A 154      -0.123  -6.991  -5.238  1.00 44.82           C  
ANISOU  839  CG  TYR A 154     6524   5088   5417  -1288    578   -601       C  
ATOM    840  CD1 TYR A 154      -1.300  -6.239  -5.431  1.00 45.02           C  
ANISOU  840  CD1 TYR A 154     6637   5048   5419  -1363    601   -556       C  
ATOM    841  CD2 TYR A 154      -0.219  -8.380  -5.260  1.00 43.97           C  
ANISOU  841  CD2 TYR A 154     6391   4970   5346  -1234    582   -639       C  
ATOM    842  CE1 TYR A 154      -2.505  -6.878  -5.677  1.00 45.15           C  
ANISOU  842  CE1 TYR A 154     6719   4984   5453  -1376    635   -557       C  
ATOM    843  CE2 TYR A 154      -1.421  -9.023  -5.518  1.00 44.27           C  
ANISOU  843  CE2 TYR A 154     6493   4936   5393  -1258    620   -645       C  
ATOM    844  CZ  TYR A 154      -2.558  -8.284  -5.719  1.00 44.78           C  
ANISOU  844  CZ  TYR A 154     6647   4927   5437  -1323    650   -607       C  
ATOM    845  OH  TYR A 154      -3.729  -8.978  -5.963  1.00 44.48           O  
ANISOU  845  OH  TYR A 154     6695   4800   5407  -1346    695   -620       O  
ATOM    846  N   ARG A 155       1.992  -3.644  -3.245  1.00 43.48           N  
ANISOU  846  N   ARG A 155     6399   4988   5135  -1351    474   -444       N  
ATOM    847  CA  ARG A 155       2.897  -3.296  -2.179  1.00 41.19           C  
ANISOU  847  CA  ARG A 155     6108   4717   4826  -1332    420   -392       C  
ATOM    848  C   ARG A 155       2.537  -4.185  -1.015  1.00 41.34           C  
ANISOU  848  C   ARG A 155     6092   4702   4911  -1234    371   -313       C  
ATOM    849  O   ARG A 155       1.498  -4.003  -0.403  1.00 44.42           O  
ANISOU  849  O   ARG A 155     6503   5044   5330  -1223    347   -214       O  
ATOM    850  CB  ARG A 155       2.772  -1.824  -1.824  1.00 41.00           C  
ANISOU  850  CB  ARG A 155     6159   4694   4725  -1441    393   -316       C  
ATOM    851  CG  ARG A 155       3.850  -1.370  -0.872  1.00 39.93           C  
ANISOU  851  CG  ARG A 155     6037   4590   4544  -1457    342   -278       C  
ATOM    852  CD  ARG A 155       3.711   0.091  -0.545  1.00 40.09           C  
ANISOU  852  CD  ARG A 155     6142   4617   4471  -1590    309   -199       C  
ATOM    853  NE  ARG A 155       2.537   0.350   0.282  1.00 40.50           N  
ANISOU  853  NE  ARG A 155     6203   4634   4551  -1589    236    -49       N  
ATOM    854  CZ  ARG A 155       2.342   1.454   1.008  1.00 41.31           C  
ANISOU  854  CZ  ARG A 155     6363   4745   4587  -1687    162     73       C  
ATOM    855  NH1 ARG A 155       3.255   2.413   1.027  1.00 41.79           N1+
ANISOU  855  NH1 ARG A 155     6493   4850   4535  -1811    158     54       N1+
ATOM    856  NH2 ARG A 155       1.217   1.611   1.714  1.00 41.56           N  
ANISOU  856  NH2 ARG A 155     6388   4739   4665  -1661     92    220       N  
ATOM    857  N   ASP A 156       3.360  -5.188  -0.749  1.00 41.63           N  
ANISOU  857  N   ASP A 156     6079   4761   4978  -1159    363   -356       N  
ATOM    858  CA  ASP A 156       3.111  -6.133   0.344  1.00 42.38           C  
ANISOU  858  CA  ASP A 156     6136   4836   5131  -1073    331   -295       C  
ATOM    859  C   ASP A 156       3.668  -5.554   1.632  1.00 41.79           C  
ANISOU  859  C   ASP A 156     6059   4789   5030  -1087    265   -200       C  
ATOM    860  O   ASP A 156       4.867  -5.407   1.767  1.00 41.33           O  
ANISOU  860  O   ASP A 156     6010   4768   4925  -1111    244   -231       O  
ATOM    861  CB  ASP A 156       3.759  -7.490   0.038  1.00 43.11           C  
ANISOU  861  CB  ASP A 156     6187   4944   5250  -1009    347   -381       C  
ATOM    862  CG  ASP A 156       4.064  -8.298   1.290  1.00 43.55           C  
ANISOU  862  CG  ASP A 156     6210   5004   5333   -947    310   -329       C  
ATOM    863  OD1 ASP A 156       3.259  -8.264   2.228  1.00 46.41           O  
ANISOU  863  OD1 ASP A 156     6556   5344   5731   -919    301   -239       O  
ATOM    864  OD2 ASP A 156       5.130  -8.946   1.355  1.00 42.64           O1-
ANISOU  864  OD2 ASP A 156     6082   4917   5204   -925    292   -374       O1-
ATOM    865  N   LEU A 157       2.793  -5.222   2.576  1.00 43.42           N  
ANISOU  865  N   LEU A 157     6254   4977   5266  -1075    229    -78       N  
ATOM    866  CA  LEU A 157       3.222  -4.603   3.824  1.00 44.16           C  
ANISOU  866  CA  LEU A 157     6332   5115   5332  -1107    153     31       C  
ATOM    867  C   LEU A 157       3.622  -5.576   4.907  1.00 43.80           C  
ANISOU  867  C   LEU A 157     6216   5100   5326  -1039    130     62       C  
ATOM    868  O   LEU A 157       4.424  -5.210   5.724  1.00 48.48           O  
ANISOU  868  O   LEU A 157     6803   5746   5870  -1090     72    112       O  
ATOM    869  CB  LEU A 157       2.177  -3.654   4.364  1.00 44.91           C  
ANISOU  869  CB  LEU A 157     6434   5192   5439  -1134    107    168       C  
ATOM    870  CG  LEU A 157       1.926  -2.474   3.427  1.00 45.13           C  
ANISOU  870  CG  LEU A 157     6550   5200   5396  -1241    117    153       C  
ATOM    871  CD1 LEU A 157       0.837  -1.587   4.051  1.00 47.96           C  
ANISOU  871  CD1 LEU A 157     6921   5533   5768  -1264     53    312       C  
ATOM    872  CD2 LEU A 157       3.216  -1.734   3.155  1.00 44.42           C  
ANISOU  872  CD2 LEU A 157     6514   5164   5198  -1350    108     95       C  
ATOM    873  N   ALA A 158       3.114  -6.796   4.933  1.00 41.55           N  
ANISOU  873  N   ALA A 158     5887   4785   5114   -944    178     28       N  
ATOM    874  CA  ALA A 158       3.690  -7.824   5.819  1.00 41.07           C  
ANISOU  874  CA  ALA A 158     5770   4762   5073   -898    168     31       C  
ATOM    875  C   ALA A 158       3.597  -9.202   5.187  1.00 41.34           C  
ANISOU  875  C   ALA A 158     5806   4761   5141   -835    235    -76       C  
ATOM    876  O   ALA A 158       2.555  -9.563   4.664  1.00 46.28           O  
ANISOU  876  O   ALA A 158     6441   5329   5815   -794    292   -100       O  
ATOM    877  CB  ALA A 158       3.013  -7.812   7.175  1.00 41.42           C  
ANISOU  877  CB  ALA A 158     5732   4830   5175   -854    143    161       C  
ATOM    878  N   GLY A 159       4.667  -9.987   5.225  1.00 42.01           N  
ANISOU  878  N   GLY A 159     5894   4876   5193   -840    225   -135       N  
ATOM    879  CA  GLY A 159       4.640 -11.336   4.641  1.00 42.29           C  
ANISOU  879  CA  GLY A 159     5935   4887   5247   -798    272   -227       C  
ATOM    880  C   GLY A 159       5.874 -11.769   3.872  1.00 42.91           C  
ANISOU  880  C   GLY A 159     6049   4979   5275   -820    248   -315       C  
ATOM    881  O   GLY A 159       6.984 -11.272   4.081  1.00 44.27           O  
ANISOU  881  O   GLY A 159     6245   5178   5399   -855    201   -309       O  
ATOM    882  N   TYR A 160       5.666 -12.706   2.959  1.00 42.84           N  
ANISOU  882  N   TYR A 160     6049   4949   5279   -799    282   -395       N  
ATOM    883  CA  TYR A 160       6.764 -13.338   2.252  1.00 44.36           C  
ANISOU  883  CA  TYR A 160     6260   5155   5440   -801    252   -466       C  
ATOM    884  C   TYR A 160       7.005 -12.748   0.859  1.00 44.15           C  
ANISOU  884  C   TYR A 160     6237   5131   5407   -816    258   -530       C  
ATOM    885  O   TYR A 160       7.677 -13.354   0.010  1.00 41.99           O  
ANISOU  885  O   TYR A 160     5956   4869   5128   -803    240   -592       O  
ATOM    886  CB  TYR A 160       6.488 -14.840   2.170  1.00 45.50           C  
ANISOU  886  CB  TYR A 160     6405   5291   5592   -785    270   -504       C  
ATOM    887  CG  TYR A 160       6.376 -15.499   3.519  1.00 46.85           C  
ANISOU  887  CG  TYR A 160     6568   5470   5764   -776    279   -453       C  
ATOM    888  CD1 TYR A 160       7.459 -15.513   4.403  1.00 48.95           C  
ANISOU  888  CD1 TYR A 160     6840   5767   5991   -793    225   -416       C  
ATOM    889  CD2 TYR A 160       5.202 -16.110   3.921  1.00 47.72           C  
ANISOU  889  CD2 TYR A 160     6667   5555   5910   -755    349   -446       C  
ATOM    890  CE1 TYR A 160       7.365 -16.116   5.649  1.00 50.87           C  
ANISOU  890  CE1 TYR A 160     7063   6032   6230   -798    238   -370       C  
ATOM    891  CE2 TYR A 160       5.107 -16.732   5.159  1.00 50.09           C  
ANISOU  891  CE2 TYR A 160     6943   5872   6215   -743    371   -406       C  
ATOM    892  CZ  TYR A 160       6.189 -16.733   6.019  1.00 51.45           C  
ANISOU  892  CZ  TYR A 160     7107   6092   6348   -769    315   -366       C  
ATOM    893  OH  TYR A 160       6.091 -17.343   7.248  1.00 52.20           O  
ANISOU  893  OH  TYR A 160     7167   6221   6445   -771    344   -325       O  
ATOM    894  N   GLY A 161       6.479 -11.546   0.647  1.00 45.24           N  
ANISOU  894  N   GLY A 161     6379   5264   5546   -845    281   -509       N  
ATOM    895  CA  GLY A 161       6.606 -10.864  -0.632  1.00 45.71           C  
ANISOU  895  CA  GLY A 161     6435   5335   5596   -872    304   -571       C  
ATOM    896  C   GLY A 161       8.005 -10.957  -1.210  1.00 45.07           C  
ANISOU  896  C   GLY A 161     6349   5276   5499   -851    280   -629       C  
ATOM    897  O   GLY A 161       8.169 -11.265  -2.376  1.00 47.80           O  
ANISOU  897  O   GLY A 161     6657   5644   5860   -839    294   -695       O  
ATOM    898  N   CYS A 162       9.017 -10.695  -0.400  1.00 43.19           N  
ANISOU  898  N   CYS A 162     6147   5031   5231   -846    243   -602       N  
ATOM    899  CA  CYS A 162      10.368 -10.797  -0.882  1.00 43.02           C  
ANISOU  899  CA  CYS A 162     6139   5007   5199   -812    225   -654       C  
ATOM    900  C   CYS A 162      10.703 -12.190  -1.345  1.00 42.09           C  
ANISOU  900  C   CYS A 162     5989   4893   5109   -757    191   -685       C  
ATOM    901  O   CYS A 162      11.250 -12.356  -2.419  1.00 42.67           O  
ANISOU  901  O   CYS A 162     6026   4980   5205   -719    191   -741       O  
ATOM    902  CB  CYS A 162      11.331 -10.388   0.207  1.00 45.80           C  
ANISOU  902  CB  CYS A 162     6563   5336   5503   -830    189   -612       C  
ATOM    903  SG  CYS A 162      11.135  -8.657   0.682  1.00 48.79           S  
ANISOU  903  SG  CYS A 162     6993   5718   5826   -920    213   -572       S  
ATOM    904  N   GLU A 163      10.359 -13.196  -0.548  1.00 42.16           N  
ANISOU  904  N   GLU A 163     6006   4896   5114   -758    162   -645       N  
ATOM    905  CA  GLU A 163      10.733 -14.588  -0.846  1.00 41.48           C  
ANISOU  905  CA  GLU A 163     5911   4814   5036   -728    120   -664       C  
ATOM    906  C   GLU A 163       9.958 -15.155  -2.028  1.00 42.42           C  
ANISOU  906  C   GLU A 163     5973   4962   5182   -733    138   -709       C  
ATOM    907  O   GLU A 163      10.415 -16.074  -2.714  1.00 42.84           O  
ANISOU  907  O   GLU A 163     6002   5033   5242   -713     94   -734       O  
ATOM    908  CB  GLU A 163      10.501 -15.474   0.364  1.00 41.22           C  
ANISOU  908  CB  GLU A 163     5911   4773   4979   -748    101   -616       C  
ATOM    909  CG  GLU A 163      11.459 -15.239   1.532  1.00 42.76           C  
ANISOU  909  CG  GLU A 163     6163   4951   5132   -761     63   -569       C  
ATOM    910  CD  GLU A 163      11.430 -13.833   2.146  1.00 41.63           C  
ANISOU  910  CD  GLU A 163     6035   4809   4974   -792     83   -532       C  
ATOM    911  OE1 GLU A 163      10.377 -13.133   2.105  1.00 42.13           O  
ANISOU  911  OE1 GLU A 163     6062   4885   5060   -808    127   -515       O  
ATOM    912  OE2 GLU A 163      12.472 -13.458   2.724  1.00 40.49           O1-
ANISOU  912  OE2 GLU A 163     5951   4647   4786   -812     49   -512       O1-
ATOM    913  N   VAL A 164       8.766 -14.628  -2.258  1.00 42.47           N  
ANISOU  913  N   VAL A 164     5963   4974   5200   -770    197   -713       N  
ATOM    914  CA  VAL A 164       7.939 -15.111  -3.350  1.00 43.45           C  
ANISOU  914  CA  VAL A 164     6049   5124   5336   -801    220   -756       C  
ATOM    915  C   VAL A 164       8.269 -14.375  -4.628  1.00 43.35           C  
ANISOU  915  C   VAL A 164     5974   5154   5342   -800    234   -805       C  
ATOM    916  O   VAL A 164       8.183 -14.946  -5.712  1.00 44.23           O  
ANISOU  916  O   VAL A 164     6029   5313   5464   -815    221   -842       O  
ATOM    917  CB  VAL A 164       6.443 -14.939  -3.035  1.00 44.86           C  
ANISOU  917  CB  VAL A 164     6256   5272   5517   -845    283   -738       C  
ATOM    918  CG1 VAL A 164       5.589 -15.406  -4.193  1.00 45.35           C  
ANISOU  918  CG1 VAL A 164     6301   5354   5577   -898    309   -787       C  
ATOM    919  CG2 VAL A 164       6.069 -15.731  -1.795  1.00 45.71           C  
ANISOU  919  CG2 VAL A 164     6407   5343   5618   -834    287   -697       C  
ATOM    920  N   ALA A 165       8.657 -13.108  -4.511  1.00 43.81           N  
ANISOU  920  N   ALA A 165     6042   5205   5399   -793    263   -804       N  
ATOM    921  CA  ALA A 165       8.926 -12.293  -5.688  1.00 44.30           C  
ANISOU  921  CA  ALA A 165     6045   5311   5475   -798    302   -858       C  
ATOM    922  C   ALA A 165      10.070 -12.888  -6.493  1.00 45.33           C  
ANISOU  922  C   ALA A 165     6108   5477   5639   -728    261   -895       C  
ATOM    923  O   ALA A 165      10.240 -12.584  -7.679  1.00 48.75           O  
ANISOU  923  O   ALA A 165     6454   5968   6100   -722    289   -945       O  
ATOM    924  CB  ALA A 165       9.231 -10.863  -5.297  1.00 44.02           C  
ANISOU  924  CB  ALA A 165     6055   5255   5417   -814    344   -853       C  
ATOM    925  N   LYS A 166      10.856 -13.746  -5.863  1.00 44.50           N  
ANISOU  925  N   LYS A 166     6035   5340   5534   -675    191   -864       N  
ATOM    926  CA  LYS A 166      11.905 -14.418  -6.625  1.00 45.88           C  
ANISOU  926  CA  LYS A 166     6149   5538   5747   -599    136   -883       C  
ATOM    927  C   LYS A 166      11.429 -15.583  -7.436  1.00 46.40           C  
ANISOU  927  C   LYS A 166     6143   5665   5823   -625     87   -885       C  
ATOM    928  O   LYS A 166      12.106 -15.929  -8.367  1.00 50.11           O  
ANISOU  928  O   LYS A 166     6524   6180   6334   -571     47   -898       O  
ATOM    929  CB  LYS A 166      13.121 -14.837  -5.812  1.00 45.51           C  
ANISOU  929  CB  LYS A 166     6173   5426   5691   -532     74   -851       C  
ATOM    930  CG  LYS A 166      12.894 -15.332  -4.414  1.00 45.04           C  
ANISOU  930  CG  LYS A 166     6213   5320   5581   -573     44   -796       C  
ATOM    931  CD  LYS A 166      14.234 -15.571  -3.737  1.00 45.21           C  
ANISOU  931  CD  LYS A 166     6313   5278   5586   -520    -13   -771       C  
ATOM    932  CE  LYS A 166      15.125 -14.334  -3.682  1.00 45.52           C  
ANISOU  932  CE  LYS A 166     6394   5273   5629   -482     31   -796       C  
ATOM    933  NZ  LYS A 166      16.242 -14.527  -2.724  1.00 46.41           N1+
ANISOU  933  NZ  LYS A 166     6623   5308   5703   -463    -17   -763       N1+
ATOM    934  N   ALA A 167      10.291 -16.177  -7.108  1.00 45.29           N  
ANISOU  934  N   ALA A 167     6040   5524   5645   -707     92   -869       N  
ATOM    935  CA  ALA A 167       9.737 -17.227  -7.937  1.00 46.09           C  
ANISOU  935  CA  ALA A 167     6091   5685   5738   -763     53   -877       C  
ATOM    936  C   ALA A 167       8.979 -16.593  -9.104  1.00 48.34           C  
ANISOU  936  C   ALA A 167     6294   6039   6035   -823    112   -922       C  
ATOM    937  O   ALA A 167       8.866 -17.183 -10.191  1.00 47.98           O  
ANISOU  937  O   ALA A 167     6160   6076   5995   -862     75   -936       O  
ATOM    938  CB  ALA A 167       8.834 -18.135  -7.123  1.00 45.72           C  
ANISOU  938  CB  ALA A 167     6137   5598   5638   -833     53   -855       C  
ATOM    939  N   ILE A 168       8.463 -15.383  -8.875  1.00 50.15           N  
ANISOU  939  N   ILE A 168     6554   6241   6260   -846    197   -937       N  
ATOM    940  CA  ILE A 168       7.962 -14.518  -9.957  1.00 52.81           C  
ANISOU  940  CA  ILE A 168     6818   6642   6604   -902    262   -982       C  
ATOM    941  C   ILE A 168       9.115 -14.157 -10.894  1.00 52.98           C  
ANISOU  941  C   ILE A 168     6716   6734   6681   -826    256  -1014       C  
ATOM    942  O   ILE A 168       9.040 -14.378 -12.091  1.00 51.89           O  
ANISOU  942  O   ILE A 168     6458   6694   6563   -855    250  -1041       O  
ATOM    943  CB  ILE A 168       7.357 -13.198  -9.415  1.00 53.89           C  
ANISOU  943  CB  ILE A 168     7030   6727   6720   -939    345   -981       C  
ATOM    944  CG1 ILE A 168       5.954 -13.444  -8.853  1.00 55.56           C  
ANISOU  944  CG1 ILE A 168     7338   6879   6892  -1018    369   -954       C  
ATOM    945  CG2 ILE A 168       7.290 -12.133 -10.501  1.00 55.32           C  
ANISOU  945  CG2 ILE A 168     7137   6975   6906   -982    414  -1032       C  
ATOM    946  CD1 ILE A 168       5.351 -12.258  -8.121  1.00 55.44           C  
ANISOU  946  CD1 ILE A 168     7403   6800   6858  -1042    426   -926       C  
ATOM    947  N   ASN A 169      10.191 -13.628 -10.324  1.00 53.34           N  
ANISOU  947  N   ASN A 169     6790   6727   6750   -728    260  -1011       N  
ATOM    948  CA  ASN A 169      11.239 -13.012 -11.122  1.00 52.54           C  
ANISOU  948  CA  ASN A 169     6591   6667   6705   -644    291  -1053       C  
ATOM    949  C   ASN A 169      12.080 -13.944 -11.909  1.00 51.04           C  
ANISOU  949  C   ASN A 169     6282   6534   6576   -557    213  -1045       C  
ATOM    950  O   ASN A 169      12.649 -13.508 -12.896  1.00 52.70           O  
ANISOU  950  O   ASN A 169     6366   6810   6847   -499    250  -1085       O  
ATOM    951  CB  ASN A 169      12.136 -12.136 -10.279  1.00 52.39           C  
ANISOU  951  CB  ASN A 169     6663   6560   6682   -576    328  -1058       C  
ATOM    952  CG  ASN A 169      11.568 -10.763 -10.124  1.00 54.99           C  
ANISOU  952  CG  ASN A 169     7046   6878   6968   -655    429  -1086       C  
ATOM    953  ND2 ASN A 169      12.434  -9.822  -9.838  1.00 57.88           N  
ANISOU  953  ND2 ASN A 169     7463   7197   7330   -611    482  -1113       N  
ATOM    954  OD1 ASN A 169      10.344 -10.537 -10.256  1.00 55.89           O  
ANISOU  954  OD1 ASN A 169     7171   7019   7045   -764    458  -1082       O  
ATOM    955  N   ASP A 170      12.181 -15.204 -11.500  1.00 48.79           N  
ANISOU  955  N   ASP A 170     6031   6228   6279   -548    107   -992       N  
ATOM    956  CA  ASP A 170      12.860 -16.187 -12.342  1.00 50.57           C  
ANISOU  956  CA  ASP A 170     6137   6520   6556   -485     10   -966       C  
ATOM    957  C   ASP A 170      11.867 -16.816 -13.304  1.00 50.67           C  
ANISOU  957  C   ASP A 170     6052   6650   6548   -603    -19   -968       C  
ATOM    958  O   ASP A 170      12.246 -17.667 -14.099  1.00 51.79           O  
ANISOU  958  O   ASP A 170     6081   6873   6724   -582   -111   -938       O  
ATOM    959  CB  ASP A 170      13.621 -17.257 -11.541  1.00 50.12           C  
ANISOU  959  CB  ASP A 170     6165   6388   6489   -424   -103   -905       C  
ATOM    960  CG  ASP A 170      12.724 -18.079 -10.637  1.00 49.62           C  
ANISOU  960  CG  ASP A 170     6226   6287   6339   -536   -137   -873       C  
ATOM    961  OD1 ASP A 170      11.490 -17.911 -10.713  1.00 51.54           O  
ANISOU  961  OD1 ASP A 170     6484   6558   6540   -649    -79   -896       O  
ATOM    962  OD2 ASP A 170      13.257 -18.896  -9.846  1.00 48.28           O1-
ANISOU  962  OD2 ASP A 170     6145   6055   6143   -511   -213   -826       O1-
ATOM    963  N   GLY A 171      10.609 -16.385 -13.223  1.00 48.73           N  
ANISOU  963  N   GLY A 171     5862   6409   6244   -733     56   -995       N  
ATOM    964  CA  GLY A 171       9.586 -16.786 -14.168  1.00 49.63           C  
ANISOU  964  CA  GLY A 171     5907   6625   6324   -869     51  -1008       C  
ATOM    965  C   GLY A 171       9.058 -18.176 -13.913  1.00 50.68           C  
ANISOU  965  C   GLY A 171     6109   6751   6395   -955    -39   -966       C  
ATOM    966  O   GLY A 171       8.492 -18.799 -14.797  1.00 51.59           O  
ANISOU  966  O   GLY A 171     6159   6963   6481  -1065    -77   -966       O  
ATOM    967  N   THR A 172       9.242 -18.674 -12.701  1.00 52.19           N  
ANISOU  967  N   THR A 172     6437   6834   6558   -918    -68   -935       N  
ATOM    968  CA  THR A 172       8.735 -19.980 -12.350  1.00 52.01           C  
ANISOU  968  CA  THR A 172     6501   6795   6465  -1006   -134   -905       C  
ATOM    969  C   THR A 172       7.226 -19.878 -12.162  1.00 51.52           C  
ANISOU  969  C   THR A 172     6540   6699   6336  -1143    -47   -938       C  
ATOM    970  O   THR A 172       6.493 -20.858 -12.325  1.00 52.46           O  
ANISOU  970  O   THR A 172     6715   6830   6387  -1262    -75   -937       O  
ATOM    971  CB  THR A 172       9.405 -20.518 -11.078  1.00 50.92           C  
ANISOU  971  CB  THR A 172     6477   6556   6314   -932   -178   -864       C  
ATOM    972  CG2 THR A 172       8.804 -21.833 -10.727  1.00 52.32           C  
ANISOU  972  CG2 THR A 172     6751   6719   6409  -1040   -225   -846       C  
ATOM    973  OG1 THR A 172      10.801 -20.725 -11.320  1.00 50.19           O  
ANISOU  973  OG1 THR A 172     6309   6481   6279   -811   -269   -830       O  
ATOM    974  N   ILE A 173       6.767 -18.685 -11.813  1.00 49.32           N  
ANISOU  974  N   ILE A 173     6298   6368   6071  -1130     55   -965       N  
ATOM    975  CA  ILE A 173       5.346 -18.414 -11.744  1.00 49.81           C  
ANISOU  975  CA  ILE A 173     6454   6389   6084  -1245    140   -990       C  
ATOM    976  C   ILE A 173       5.171 -16.987 -12.190  1.00 49.53           C  
ANISOU  976  C   ILE A 173     6369   6374   6077  -1244    220  -1019       C  
ATOM    977  O   ILE A 173       6.139 -16.335 -12.542  1.00 49.42           O  
ANISOU  977  O   ILE A 173     6253   6409   6117  -1160    214  -1026       O  
ATOM    978  CB  ILE A 173       4.794 -18.586 -10.325  1.00 49.66           C  
ANISOU  978  CB  ILE A 173     6590   6240   6040  -1228    183   -971       C  
ATOM    979  CG1 ILE A 173       5.454 -17.577  -9.373  1.00 49.74           C  
ANISOU  979  CG1 ILE A 173     6611   6191   6096  -1110    210   -949       C  
ATOM    980  CG2 ILE A 173       5.029 -20.006  -9.845  1.00 50.82           C  
ANISOU  980  CG2 ILE A 173     6791   6370   6148  -1239    115   -950       C  
ATOM    981  CD1 ILE A 173       4.826 -17.529  -8.001  1.00 47.58           C  
ANISOU  981  CD1 ILE A 173     6460   5810   5810  -1094    259   -922       C  
ATOM    982  N   VAL A 174       3.941 -16.498 -12.158  1.00 48.50           N  
ANISOU  982  N   VAL A 174     6324   6196   5907  -1339    298  -1035       N  
ATOM    983  CA  VAL A 174       3.660 -15.182 -12.672  1.00 48.33           C  
ANISOU  983  CA  VAL A 174     6272   6199   5893  -1372    371  -1061       C  
ATOM    984  C   VAL A 174       2.952 -14.416 -11.584  1.00 47.18           C  
ANISOU  984  C   VAL A 174     6263   5926   5736  -1360    436  -1037       C  
ATOM    985  O   VAL A 174       2.354 -15.004 -10.679  1.00 46.63           O  
ANISOU  985  O   VAL A 174     6304   5762   5651  -1354    438  -1010       O  
ATOM    986  CB  VAL A 174       2.793 -15.247 -13.948  1.00 49.68           C  
ANISOU  986  CB  VAL A 174     6404   6453   6018  -1531    396  -1097       C  
ATOM    987  CG1 VAL A 174       3.391 -16.221 -14.962  1.00 50.15           C  
ANISOU  987  CG1 VAL A 174     6322   6649   6085  -1555    311  -1103       C  
ATOM    988  CG2 VAL A 174       1.362 -15.642 -13.628  1.00 50.14           C  
ANISOU  988  CG2 VAL A 174     6627   6413   6010  -1644    436  -1096       C  
ATOM    989  N   GLY A 175       3.042 -13.102 -11.648  1.00 46.23           N  
ANISOU  989  N   GLY A 175     6132   5808   5626  -1355    489  -1042       N  
ATOM    990  CA  GLY A 175       2.374 -12.310 -10.662  1.00 44.55           C  
ANISOU  990  CA  GLY A 175     6039   5485   5401  -1350    533  -1004       C  
ATOM    991  C   GLY A 175       2.649 -10.870 -10.909  1.00 44.62           C  
ANISOU  991  C   GLY A 175     6027   5518   5406  -1364    580  -1013       C  
ATOM    992  O   GLY A 175       3.384 -10.532 -11.813  1.00 44.21           O  
ANISOU  992  O   GLY A 175     5865   5565   5366  -1366    592  -1059       O  
ATOM    993  N   PRO A 176       2.050 -10.006 -10.096  1.00 45.90           N  
ANISOU  993  N   PRO A 176     6293   5594   5551  -1375    609   -966       N  
ATOM    994  CA  PRO A 176       2.304  -8.588 -10.262  1.00 46.23           C  
ANISOU  994  CA  PRO A 176     6337   5657   5572  -1409    651   -972       C  
ATOM    995  C   PRO A 176       3.727  -8.258  -9.910  1.00 46.32           C  
ANISOU  995  C   PRO A 176     6291   5698   5608  -1312    635   -982       C  
ATOM    996  O   PRO A 176       4.464  -9.118  -9.445  1.00 44.89           O  
ANISOU  996  O   PRO A 176     6079   5512   5465  -1216    582   -974       O  
ATOM    997  CB  PRO A 176       1.353  -7.905  -9.260  1.00 46.31           C  
ANISOU  997  CB  PRO A 176     6479   5555   5560  -1431    659   -893       C  
ATOM    998  CG  PRO A 176       0.501  -8.973  -8.681  1.00 47.59           C  
ANISOU  998  CG  PRO A 176     6702   5636   5743  -1402    639   -859       C  
ATOM    999  CD  PRO A 176       1.097 -10.307  -9.014  1.00 46.90           C  
ANISOU  999  CD  PRO A 176     6538   5602   5679  -1358    605   -905       C  
ATOM   1000  N   ASN A 177       4.114  -7.009 -10.155  1.00 48.42           N  
ANISOU 1000  N   ASN A 177     6558   5990   5847  -1349    685  -1003       N  
ATOM   1001  CA  ASN A 177       5.356  -6.473  -9.600  1.00 46.01           C  
ANISOU 1001  CA  ASN A 177     6251   5679   5550  -1273    682  -1006       C  
ATOM   1002  C   ASN A 177       5.166  -6.407  -8.107  1.00 45.11           C  
ANISOU 1002  C   ASN A 177     6239   5475   5426  -1241    629   -918       C  
ATOM   1003  O   ASN A 177       4.148  -5.901  -7.635  1.00 44.13           O  
ANISOU 1003  O   ASN A 177     6197   5300   5272  -1303    630   -858       O  
ATOM   1004  CB  ASN A 177       5.652  -5.085 -10.166  1.00 46.10           C  
ANISOU 1004  CB  ASN A 177     6268   5732   5515  -1346    763  -1053       C  
ATOM   1005  CG  ASN A 177       6.184  -5.148 -11.572  1.00 45.44           C  
ANISOU 1005  CG  ASN A 177     6051   5757   5459  -1348    824  -1147       C  
ATOM   1006  ND2 ASN A 177       5.493  -4.504 -12.500  1.00 45.71           N  
ANISOU 1006  ND2 ASN A 177     6069   5849   5451  -1472    893  -1183       N  
ATOM   1007  OD1 ASN A 177       7.184  -5.803 -11.824  1.00 44.71           O  
ANISOU 1007  OD1 ASN A 177     5866   5697   5426  -1238    805  -1180       O  
ATOM   1008  N   VAL A 178       6.105  -6.954  -7.353  1.00 45.53           N  
ANISOU 1008  N   VAL A 178     6286   5508   5507  -1144    579   -902       N  
ATOM   1009  CA  VAL A 178       5.949  -6.971  -5.909  1.00 46.64           C  
ANISOU 1009  CA  VAL A 178     6501   5580   5639  -1119    528   -815       C  
ATOM   1010  C   VAL A 178       6.980  -6.092  -5.220  1.00 45.99           C  
ANISOU 1010  C   VAL A 178     6465   5487   5522  -1114    521   -800       C  
ATOM   1011  O   VAL A 178       8.172  -6.215  -5.460  1.00 46.45           O  
ANISOU 1011  O   VAL A 178     6499   5561   5588  -1060    526   -852       O  
ATOM   1012  CB  VAL A 178       6.010  -8.411  -5.389  1.00 48.19           C  
ANISOU 1012  CB  VAL A 178     6675   5758   5879  -1040    473   -795       C  
ATOM   1013  CG1 VAL A 178       6.212  -8.431  -3.879  1.00 48.60           C  
ANISOU 1013  CG1 VAL A 178     6778   5762   5925  -1005    425   -714       C  
ATOM   1014  CG2 VAL A 178       4.731  -9.146  -5.791  1.00 47.55           C  
ANISOU 1014  CG2 VAL A 178     6592   5663   5812  -1072    486   -794       C  
ATOM   1015  N   TYR A 179       6.486  -5.196  -4.373  1.00 46.14           N  
ANISOU 1015  N   TYR A 179     6561   5474   5497  -1175    507   -724       N  
ATOM   1016  CA  TYR A 179       7.317  -4.292  -3.562  1.00 46.04           C  
ANISOU 1016  CA  TYR A 179     6614   5449   5427  -1205    490   -693       C  
ATOM   1017  C   TYR A 179       6.991  -4.599  -2.095  1.00 45.98           C  
ANISOU 1017  C   TYR A 179     6632   5410   5427  -1185    412   -581       C  
ATOM   1018  O   TYR A 179       6.005  -4.099  -1.557  1.00 47.34           O  
ANISOU 1018  O   TYR A 179     6833   5566   5590  -1232    390   -495       O  
ATOM   1019  CB  TYR A 179       7.001  -2.825  -3.877  1.00 45.68           C  
ANISOU 1019  CB  TYR A 179     6633   5414   5309  -1327    534   -691       C  
ATOM   1020  CG  TYR A 179       7.220  -2.437  -5.320  1.00 45.64           C  
ANISOU 1020  CG  TYR A 179     6593   5454   5294  -1360    627   -801       C  
ATOM   1021  CD1 TYR A 179       6.228  -2.633  -6.288  1.00 45.40           C  
ANISOU 1021  CD1 TYR A 179     6516   5449   5285  -1395    664   -828       C  
ATOM   1022  CD2 TYR A 179       8.406  -1.860  -5.716  1.00 46.09           C  
ANISOU 1022  CD2 TYR A 179     6663   5527   5320  -1363    687   -883       C  
ATOM   1023  CE1 TYR A 179       6.432  -2.272  -7.616  1.00 45.62           C  
ANISOU 1023  CE1 TYR A 179     6493   5538   5302  -1436    752   -929       C  
ATOM   1024  CE2 TYR A 179       8.623  -1.496  -7.038  1.00 47.55           C  
ANISOU 1024  CE2 TYR A 179     6796   5765   5506  -1385    787   -988       C  
ATOM   1025  CZ  TYR A 179       7.642  -1.709  -7.986  1.00 46.94           C  
ANISOU 1025  CZ  TYR A 179     6652   5732   5450  -1424    816  -1008       C  
ATOM   1026  OH  TYR A 179       7.904  -1.332  -9.275  1.00 47.02           O  
ANISOU 1026  OH  TYR A 179     6593   5810   5460  -1454    918  -1111       O  
ATOM   1027  N   SER A 180       7.809  -5.443  -1.468  1.00 44.67           N  
ANISOU 1027  N   SER A 180     6452   5239   5283  -1115    371   -578       N  
ATOM   1028  CA  SER A 180       7.513  -6.015  -0.156  1.00 41.51           C  
ANISOU 1028  CA  SER A 180     6046   4824   4901  -1086    309   -485       C  
ATOM   1029  C   SER A 180       8.264  -5.235   0.932  1.00 40.77           C  
ANISOU 1029  C   SER A 180     6011   4737   4743  -1143    262   -422       C  
ATOM   1030  O   SER A 180       9.254  -4.562   0.677  1.00 41.23           O  
ANISOU 1030  O   SER A 180     6126   4795   4743  -1185    280   -470       O  
ATOM   1031  CB  SER A 180       7.904  -7.500  -0.167  1.00 40.90           C  
ANISOU 1031  CB  SER A 180     5923   4745   4874   -997    294   -522       C  
ATOM   1032  OG  SER A 180       7.809  -8.118   1.107  1.00 42.27           O  
ANISOU 1032  OG  SER A 180     6089   4914   5058   -973    247   -446       O  
ATOM   1033  N   SER A 181       7.773  -5.314   2.150  1.00 40.79           N  
ANISOU 1033  N   SER A 181     6000   4747   4753  -1149    207   -314       N  
ATOM   1034  CA  SER A 181       8.434  -4.700   3.279  1.00 41.75           C  
ANISOU 1034  CA  SER A 181     6163   4890   4808  -1218    149   -240       C  
ATOM   1035  C   SER A 181       9.156  -5.744   4.095  1.00 42.60           C  
ANISOU 1035  C   SER A 181     6252   5007   4929  -1172    112   -231       C  
ATOM   1036  O   SER A 181       9.674  -5.423   5.173  1.00 46.09           O  
ANISOU 1036  O   SER A 181     6720   5476   5316  -1235     57   -161       O  
ATOM   1037  CB  SER A 181       7.404  -4.041   4.179  1.00 42.47           C  
ANISOU 1037  CB  SER A 181     6233   5004   4902  -1263     99   -105       C  
ATOM   1038  OG  SER A 181       6.577  -5.040   4.738  1.00 43.18           O  
ANISOU 1038  OG  SER A 181     6237   5091   5078  -1172     91    -54       O  
ATOM   1039  N   GLY A 182       9.191  -6.978   3.582  1.00 41.34           N  
ANISOU 1039  N   GLY A 182     6051   4828   4827  -1080    139   -297       N  
ATOM   1040  CA  GLY A 182       9.524  -8.133   4.387  1.00 41.41           C  
ANISOU 1040  CA  GLY A 182     6032   4846   4854  -1039    108   -276       C  
ATOM   1041  C   GLY A 182       8.517  -8.144   5.511  1.00 41.89           C  
ANISOU 1041  C   GLY A 182     6029   4939   4946  -1042     85   -164       C  
ATOM   1042  O   GLY A 182       7.312  -8.050   5.268  1.00 43.31           O  
ANISOU 1042  O   GLY A 182     6168   5107   5182  -1009    114   -140       O  
ATOM   1043  N   ALA A 183       9.012  -8.209   6.740  1.00 41.95           N  
ANISOU 1043  N   ALA A 183     6031   4989   4921  -1083     34    -92       N  
ATOM   1044  CA  ALA A 183       8.166  -8.124   7.930  1.00 42.42           C  
ANISOU 1044  CA  ALA A 183     6007   5098   5014  -1086      5     28       C  
ATOM   1045  C   ALA A 183       7.776  -6.691   8.316  1.00 43.47           C  
ANISOU 1045  C   ALA A 183     6143   5260   5115  -1164    -40    128       C  
ATOM   1046  O   ALA A 183       8.542  -5.723   8.153  1.00 44.96           O  
ANISOU 1046  O   ALA A 183     6415   5452   5214  -1262    -70    120       O  
ATOM   1047  CB  ALA A 183       8.860  -8.788   9.115  1.00 42.33           C  
ANISOU 1047  CB  ALA A 183     5971   5139   4974  -1115    -31     71       C  
ATOM   1048  N   ALA A 184       6.582  -6.580   8.881  1.00 42.77           N  
ANISOU 1048  N   ALA A 184     5966   5189   5097  -1121    -47    227       N  
ATOM   1049  CA  ALA A 184       6.184  -5.380   9.570  1.00 42.55           C  
ANISOU 1049  CA  ALA A 184     5917   5207   5044  -1194   -118    359       C  
ATOM   1050  C   ALA A 184       6.914  -5.323  10.884  1.00 42.70           C  
ANISOU 1050  C   ALA A 184     5897   5316   5011  -1273   -191    446       C  
ATOM   1051  O   ALA A 184       6.981  -6.299  11.620  1.00 44.08           O  
ANISOU 1051  O   ALA A 184     5992   5530   5225  -1226   -180    460       O  
ATOM   1052  CB  ALA A 184       4.700  -5.391   9.824  1.00 44.81           C  
ANISOU 1052  CB  ALA A 184     6111   5476   5437  -1102   -106    448       C  
ATOM   1053  N   LEU A 185       7.450  -4.160  11.190  1.00 44.06           N  
ANISOU 1053  N   LEU A 185     6130   5530   5081  -1412   -264    507       N  
ATOM   1054  CA  LEU A 185       8.145  -3.947  12.440  1.00 44.10           C  
ANISOU 1054  CA  LEU A 185     6109   5631   5014  -1524   -346    601       C  
ATOM   1055  C   LEU A 185       7.133  -3.515  13.452  1.00 43.52           C  
ANISOU 1055  C   LEU A 185     5894   5639   5001  -1516   -416    777       C  
ATOM   1056  O   LEU A 185       6.364  -2.585  13.221  1.00 43.42           O  
ANISOU 1056  O   LEU A 185     5884   5614   5000  -1529   -450    850       O  
ATOM   1057  CB  LEU A 185       9.172  -2.835  12.292  1.00 47.45           C  
ANISOU 1057  CB  LEU A 185     6684   6058   5288  -1696   -392    585       C  
ATOM   1058  CG  LEU A 185      10.512  -3.092  11.608  1.00 47.83           C  
ANISOU 1058  CG  LEU A 185     6883   6038   5254  -1733   -342    434       C  
ATOM   1059  CD1 LEU A 185      10.326  -3.594  10.195  1.00 48.53           C  
ANISOU 1059  CD1 LEU A 185     7002   6027   5409  -1605   -243    293       C  
ATOM   1060  CD2 LEU A 185      11.359  -1.822  11.622  1.00 49.14           C  
ANISOU 1060  CD2 LEU A 185     7199   6203   5266  -1915   -381    438       C  
ATOM   1061  N   SER A 186       7.148  -4.177  14.592  1.00 39.13           N  
ANISOU 1061  N   SER A 186     5107   3710   6049   -267    861    -94       N  
ATOM   1062  CA  SER A 186       6.253  -3.838  15.692  1.00 39.21           C  
ANISOU 1062  CA  SER A 186     5208   3684   6004   -108    858    -71       C  
ATOM   1063  C   SER A 186       7.052  -3.875  16.995  1.00 38.54           C  
ANISOU 1063  C   SER A 186     5008   3784   5850     -2    850    -95       C  
ATOM   1064  O   SER A 186       7.995  -4.654  17.116  1.00 36.43           O  
ANISOU 1064  O   SER A 186     4643   3610   5586    -47    834   -152       O  
ATOM   1065  CB  SER A 186       5.106  -4.838  15.756  1.00 38.52           C  
ANISOU 1065  CB  SER A 186     5256   3454   5927    -56    824   -131       C  
ATOM   1066  OG  SER A 186       4.298  -4.610  16.884  1.00 37.91           O  
ANISOU 1066  OG  SER A 186     5261   3370   5773    138    815   -120       O  
ATOM   1067  N   GLN A 187       6.684  -3.020  17.952  1.00 39.15           N  
ANISOU 1067  N   GLN A 187     5100   3922   5854    128    861    -52       N  
ATOM   1068  CA  GLN A 187       7.204  -3.152  19.308  1.00 38.12           C  
ANISOU 1068  CA  GLN A 187     4863   3982   5638    223    849    -87       C  
ATOM   1069  C   GLN A 187       6.592  -4.395  19.957  1.00 38.14           C  
ANISOU 1069  C   GLN A 187     4892   3992   5606    320    814   -161       C  
ATOM   1070  O   GLN A 187       5.617  -4.946  19.465  1.00 38.99           O  
ANISOU 1070  O   GLN A 187     5127   3940   5748    349    796   -181       O  
ATOM   1071  CB  GLN A 187       6.908  -1.916  20.152  1.00 38.31           C  
ANISOU 1071  CB  GLN A 187     4878   4103   5574    348    868    -30       C  
ATOM   1072  CG  GLN A 187       5.428  -1.595  20.281  1.00 40.80           C  
ANISOU 1072  CG  GLN A 187     5352   4300   5852    504    868      9       C  
ATOM   1073  CD  GLN A 187       5.106  -0.752  21.509  1.00 41.99           C  
ANISOU 1073  CD  GLN A 187     5467   4617   5871    693    873     35       C  
ATOM   1074  NE2 GLN A 187       4.669  -1.424  22.570  1.00 43.06           N  
ANISOU 1074  NE2 GLN A 187     5578   4867   5914    845    844    -25       N  
ATOM   1075  OE1 GLN A 187       5.235   0.476  21.506  1.00 40.32           O  
ANISOU 1075  OE1 GLN A 187     5240   4451   5628    711    902    104       O  
ATOM   1076  N   THR A 188       7.210  -4.850  21.036  1.00 38.09           N  
ANISOU 1076  N   THR A 188     4767   4177   5528    356    801   -206       N  
ATOM   1077  CA  THR A 188       6.623  -5.849  21.905  1.00 38.79           C  
ANISOU 1077  CA  THR A 188     4852   4342   5546    482    772   -268       C  
ATOM   1078  C   THR A 188       5.284  -5.268  22.347  1.00 41.18           C  
ANISOU 1078  C   THR A 188     5265   4603   5778    680    767   -243       C  
ATOM   1079  O   THR A 188       5.171  -4.058  22.573  1.00 41.28           O  
ANISOU 1079  O   THR A 188     5282   4650   5752    733    791   -179       O  
ATOM   1080  CB  THR A 188       7.537  -6.103  23.127  1.00 37.59           C  
ANISOU 1080  CB  THR A 188     4534   4449   5300    473    772   -298       C  
ATOM   1081  CG2 THR A 188       6.768  -6.744  24.272  1.00 38.93           C  
ANISOU 1081  CG2 THR A 188     4674   4771   5349    649    749   -347       C  
ATOM   1082  OG1 THR A 188       8.634  -6.941  22.755  1.00 35.00           O  
ANISOU 1082  OG1 THR A 188     4148   4127   5024    317    772   -327       O  
ATOM   1083  N   ALA A 189       4.266  -6.111  22.456  1.00 42.81           N  
ANISOU 1083  N   ALA A 189     5575   4731   5959    809    735   -292       N  
ATOM   1084  CA  ALA A 189       2.927  -5.624  22.811  1.00 44.86           C  
ANISOU 1084  CA  ALA A 189     5987   4915   6142   1027    725   -270       C  
ATOM   1085  C   ALA A 189       2.364  -4.646  21.769  1.00 44.49           C  
ANISOU 1085  C   ALA A 189     6115   4618   6171    975    751   -185       C  
ATOM   1086  O   ALA A 189       1.403  -3.924  22.033  1.00 44.47           O  
ANISOU 1086  O   ALA A 189     6251   4545   6100   1144    756   -138       O  
ATOM   1087  CB  ALA A 189       2.960  -4.976  24.184  1.00 45.04           C  
ANISOU 1087  CB  ALA A 189     5894   5210   6011   1197    731   -258       C  
ATOM   1088  N   GLY A 190       2.981  -4.619  20.595  1.00 43.45           N  
ANISOU 1088  N   GLY A 190     5974   4369   6166    745    769   -165       N  
ATOM   1089  CA  GLY A 190       2.516  -3.782  19.507  1.00 45.14           C  
ANISOU 1089  CA  GLY A 190     6332   4369   6451    653    798    -85       C  
ATOM   1090  C   GLY A 190       1.439  -4.461  18.683  1.00 47.36           C  
ANISOU 1090  C   GLY A 190     6825   4382   6788    624    775   -115       C  
ATOM   1091  O   GLY A 190       1.037  -5.595  18.955  1.00 46.24           O  
ANISOU 1091  O   GLY A 190     6722   4219   6630    698    732   -207       O  
ATOM   1092  N   HIS A 191       0.960  -3.739  17.676  1.00 50.57           N  
ANISOU 1092  N   HIS A 191     7374   4589   7251    509    805    -38       N  
ATOM   1093  CA  HIS A 191      -0.122  -4.227  16.830  1.00 54.70           C  
ANISOU 1093  CA  HIS A 191     8129   4832   7824    446    787    -57       C  
ATOM   1094  C   HIS A 191       0.297  -5.499  16.127  1.00 54.61           C  
ANISOU 1094  C   HIS A 191     8044   4812   7894    280    755   -164       C  
ATOM   1095  O   HIS A 191      -0.504  -6.392  15.901  1.00 58.37           O  
ANISOU 1095  O   HIS A 191     8667   5130   8381    293    714   -241       O  
ATOM   1096  CB  HIS A 191      -0.537  -3.168  15.822  1.00 56.66           C  
ANISOU 1096  CB  HIS A 191     8514   4899   8114    297    835     56       C  
ATOM   1097  CG  HIS A 191      -1.462  -3.682  14.773  1.00 59.18           C  
ANISOU 1097  CG  HIS A 191     9053   4936   8497    145    822     31       C  
ATOM   1098  CD2 HIS A 191      -1.259  -3.919  13.455  1.00 60.63           C  
ANISOU 1098  CD2 HIS A 191     9218   5044   8773   -141    833     21       C  
ATOM   1099  ND1 HIS A 191      -2.760  -4.057  15.040  1.00 61.18           N  
ANISOU 1099  ND1 HIS A 191     9583   4956   8706    284    788      1       N  
ATOM   1100  CE1 HIS A 191      -3.322  -4.487  13.923  1.00 63.68           C  
ANISOU 1100  CE1 HIS A 191    10057   5042   9095     68    780    -26       C  
ATOM   1101  NE2 HIS A 191      -2.431  -4.416  12.947  1.00 62.00           N  
ANISOU 1101  NE2 HIS A 191     9654   4938   8964   -199    808    -15       N  
ATOM   1102  N   GLY A 192       1.577  -5.597  15.815  1.00 54.52           N  
ANISOU 1102  N   GLY A 192     7809   4979   7927    142    769   -173       N  
ATOM   1103  CA  GLY A 192       2.131  -6.834  15.271  1.00 55.08           C  
ANISOU 1103  CA  GLY A 192     7781   5094   8054     21    738   -274       C  
ATOM   1104  C   GLY A 192       2.061  -8.050  16.190  1.00 53.04           C  
ANISOU 1104  C   GLY A 192     7488   4921   7743    176    690   -378       C  
ATOM   1105  O   GLY A 192       1.933  -9.178  15.727  1.00 55.38           O  
ANISOU 1105  O   GLY A 192     7796   5172   8072    119    654   -471       O  
ATOM   1106  N   ASP A 193       2.085  -7.821  17.491  1.00 51.39           N  
ANISOU 1106  N   ASP A 193     7234   4851   7442    374    689   -365       N  
ATOM   1107  CA  ASP A 193       2.259  -8.906  18.443  1.00 49.01           C  
ANISOU 1107  CA  ASP A 193     6844   4705   7073    506    653   -451       C  
ATOM   1108  C   ASP A 193       1.095  -9.907  18.489  1.00 47.77           C  
ANISOU 1108  C   ASP A 193     6851   4411   6889    626    600   -543       C  
ATOM   1109  O   ASP A 193      -0.066  -9.552  18.266  1.00 49.40           O  
ANISOU 1109  O   ASP A 193     7278   4402   7088    695    590   -529       O  
ATOM   1110  CB  ASP A 193       2.501  -8.335  19.837  1.00 49.42           C  
ANISOU 1110  CB  ASP A 193     6796   4971   7012    678    666   -415       C  
ATOM   1111  CG  ASP A 193       3.208  -9.296  20.719  1.00 48.25           C  
ANISOU 1111  CG  ASP A 193     6477   5054   6801    723    648   -480       C  
ATOM   1112  OD1 ASP A 193       3.075 -10.519  20.441  1.00 48.58           O  
ANISOU 1112  OD1 ASP A 193     6531   5064   6863    711    614   -562       O  
ATOM   1113  OD2 ASP A 193       3.876  -8.847  21.701  1.00 48.25           O1-
ANISOU 1113  OD2 ASP A 193     6332   5276   6724    764    668   -450       O1-
ATOM   1114  N   ILE A 194       1.436 -11.169  18.746  1.00 45.80           N  
ANISOU 1114  N   ILE A 194     6504   4277   6622    646    567   -636       N  
ATOM   1115  CA  ILE A 194       0.460 -12.266  18.902  1.00 44.15           C  
ANISOU 1115  CA  ILE A 194     6420   3985   6371    782    509   -743       C  
ATOM   1116  C   ILE A 194       0.201 -12.444  20.373  1.00 41.45           C  
ANISOU 1116  C   ILE A 194     6026   3839   5884   1045    494   -762       C  
ATOM   1117  O   ILE A 194       0.891 -13.197  21.022  1.00 38.09           O  
ANISOU 1117  O   ILE A 194     5422   3644   5405   1074    488   -800       O  
ATOM   1118  CB  ILE A 194       0.991 -13.619  18.356  1.00 43.05           C  
ANISOU 1118  CB  ILE A 194     6183   3898   6276    672    480   -840       C  
ATOM   1119  CG1 ILE A 194       1.461 -13.483  16.905  1.00 42.82           C  
ANISOU 1119  CG1 ILE A 194     6143   3755   6370    406    497   -827       C  
ATOM   1120  CG2 ILE A 194      -0.080 -14.683  18.458  1.00 44.37           C  
ANISOU 1120  CG2 ILE A 194     6495   3967   6395    814    417   -956       C  
ATOM   1121  CD1 ILE A 194       2.287 -14.656  16.407  1.00 41.58           C  
ANISOU 1121  CD1 ILE A 194     5844   3714   6241    304    480   -902       C  
ATOM   1122  N   PHE A 195      -0.827 -11.783  20.883  1.00 42.20           N  
ANISOU 1122  N   PHE A 195     6284   3850   5901   1243    487   -735       N  
ATOM   1123  CA  PHE A 195      -1.041 -11.701  22.321  1.00 42.76           C  
ANISOU 1123  CA  PHE A 195     6280   4157   5809   1508    478   -740       C  
ATOM   1124  C   PHE A 195      -1.471 -13.012  22.923  1.00 43.48           C  
ANISOU 1124  C   PHE A 195     6359   4359   5804   1687    424   -855       C  
ATOM   1125  O   PHE A 195      -1.248 -13.258  24.090  1.00 43.20           O  
ANISOU 1125  O   PHE A 195     6163   4618   5633   1843    421   -872       O  
ATOM   1126  CB  PHE A 195      -2.080 -10.649  22.652  1.00 44.31           C  
ANISOU 1126  CB  PHE A 195     6671   4235   5929   1707    482   -682       C  
ATOM   1127  CG  PHE A 195      -1.587  -9.261  22.484  1.00 45.03           C  
ANISOU 1127  CG  PHE A 195     6717   4330   6061   1598    539   -560       C  
ATOM   1128  CD1 PHE A 195      -1.546  -8.671  21.236  1.00 46.87           C  
ANISOU 1128  CD1 PHE A 195     7063   4313   6432   1374    568   -497       C  
ATOM   1129  CD2 PHE A 195      -1.133  -8.541  23.568  1.00 45.77           C  
ANISOU 1129  CD2 PHE A 195     6643   4704   6046   1709    565   -512       C  
ATOM   1130  CE1 PHE A 195      -1.071  -7.372  21.073  1.00 46.91           C  
ANISOU 1130  CE1 PHE A 195     7018   4341   6465   1283    621   -383       C  
ATOM   1131  CE2 PHE A 195      -0.654  -7.243  23.417  1.00 45.88           C  
ANISOU 1131  CE2 PHE A 195     6611   4733   6090   1615    614   -407       C  
ATOM   1132  CZ  PHE A 195      -0.621  -6.661  22.169  1.00 46.18           C  
ANISOU 1132  CZ  PHE A 195     6766   4515   6266   1411    643   -342       C  
ATOM   1133  N   ALA A 196      -2.071 -13.870  22.121  1.00 44.90           N  
ANISOU 1133  N   ALA A 196     6696   4321   6042   1654    381   -941       N  
ATOM   1134  CA  ALA A 196      -2.572 -15.123  22.640  1.00 46.38           C  
ANISOU 1134  CA  ALA A 196     6891   4599   6130   1844    323  -1060       C  
ATOM   1135  C   ALA A 196      -1.453 -16.142  22.879  1.00 44.96           C  
ANISOU 1135  C   ALA A 196     6445   4688   5949   1739    329  -1097       C  
ATOM   1136  O   ALA A 196      -1.707 -17.212  23.438  1.00 46.29           O  
ANISOU 1136  O   ALA A 196     6569   5003   6017   1897    289  -1188       O  
ATOM   1137  CB  ALA A 196      -3.630 -15.693  21.716  1.00 48.33           C  
ANISOU 1137  CB  ALA A 196     7415   4516   6432   1847    269  -1151       C  
ATOM   1138  N   LEU A 197      -0.231 -15.817  22.473  1.00 42.13           N  
ANISOU 1138  N   LEU A 197     5924   4395   5688   1490    379  -1026       N  
ATOM   1139  CA  LEU A 197       0.891 -16.694  22.737  1.00 41.42           C  
ANISOU 1139  CA  LEU A 197     5608   4544   5586   1393    392  -1042       C  
ATOM   1140  C   LEU A 197       1.825 -16.132  23.786  1.00 41.44           C  
ANISOU 1140  C   LEU A 197     5404   4830   5511   1379    440   -961       C  
ATOM   1141  O   LEU A 197       1.895 -14.921  23.978  1.00 40.95           O  
ANISOU 1141  O   LEU A 197     5349   4755   5453   1364    472   -882       O  
ATOM   1142  CB  LEU A 197       1.677 -16.976  21.454  1.00 39.93           C  
ANISOU 1142  CB  LEU A 197     5397   4228   5547   1127    405  -1040       C  
ATOM   1143  CG  LEU A 197       1.018 -17.929  20.441  1.00 40.41           C  
ANISOU 1143  CG  LEU A 197     5592   4094   5668   1098    353  -1148       C  
ATOM   1144  CD1 LEU A 197       1.871 -17.986  19.189  1.00 38.50           C  
ANISOU 1144  CD1 LEU A 197     5296   3775   5555    835    373  -1133       C  
ATOM   1145  CD2 LEU A 197       0.765 -19.339  21.011  1.00 41.04           C  
ANISOU 1145  CD2 LEU A 197     5621   4328   5644   1259    306  -1256       C  
ATOM   1146  N   PRO A 198       2.532 -17.018  24.493  1.00 42.34           N  
ANISOU 1146  N   PRO A 198     5335   5209   5544   1377    445   -982       N  
ATOM   1147  CA  PRO A 198       3.486 -16.543  25.468  1.00 42.52           C  
ANISOU 1147  CA  PRO A 198     5167   5498   5492   1316    492   -910       C  
ATOM   1148  C   PRO A 198       4.538 -15.687  24.795  1.00 42.76           C  
ANISOU 1148  C   PRO A 198     5174   5424   5648   1072    537   -826       C  
ATOM   1149  O   PRO A 198       4.903 -15.965  23.632  1.00 42.78           O  
ANISOU 1149  O   PRO A 198     5235   5241   5779    925    536   -832       O  
ATOM   1150  CB  PRO A 198       4.078 -17.833  26.001  1.00 42.59           C  
ANISOU 1150  CB  PRO A 198     5023   5740   5419   1302    489   -948       C  
ATOM   1151  CG  PRO A 198       2.940 -18.799  25.926  1.00 44.25           C  
ANISOU 1151  CG  PRO A 198     5332   5907   5575   1512    429  -1053       C  
ATOM   1152  CD  PRO A 198       2.305 -18.468  24.617  1.00 43.70           C  
ANISOU 1152  CD  PRO A 198     5477   5471   5654   1468    405  -1077       C  
ATOM   1153  N   ALA A 199       5.020 -14.660  25.502  1.00 41.88           N  
ANISOU 1153  N   ALA A 199     4973   5447   5490   1038    574   -757       N  
ATOM   1154  CA  ALA A 199       5.967 -13.729  24.884  1.00 40.10           C  
ANISOU 1154  CA  ALA A 199     4743   5121   5374    834    613   -683       C  
ATOM   1155  C   ALA A 199       7.201 -14.425  24.309  1.00 38.13           C  
ANISOU 1155  C   ALA A 199     4435   4859   5194    636    629   -675       C  
ATOM   1156  O   ALA A 199       7.737 -13.992  23.289  1.00 36.87           O  
ANISOU 1156  O   ALA A 199     4326   4534   5150    497    643   -644       O  
ATOM   1157  CB  ALA A 199       6.379 -12.641  25.858  1.00 40.17           C  
ANISOU 1157  CB  ALA A 199     4646   5315   5300    827    645   -626       C  
ATOM   1158  N   GLY A 200       7.658 -15.484  24.968  1.00 37.76           N  
ANISOU 1158  N   GLY A 200     4283   5001   5063    633    629   -701       N  
ATOM   1159  CA  GLY A 200       8.877 -16.151  24.549  1.00 36.94           C  
ANISOU 1159  CA  GLY A 200     4138   4898   5000    466    648   -684       C  
ATOM   1160  C   GLY A 200       8.723 -16.819  23.199  1.00 36.17           C  
ANISOU 1160  C   GLY A 200     4134   4598   5011    443    622   -727       C  
ATOM   1161  O   GLY A 200       9.636 -16.818  22.369  1.00 34.07           O  
ANISOU 1161  O   GLY A 200     3883   4243   4821    308    637   -701       O  
ATOM   1162  N   GLU A 201       7.567 -17.394  22.961  1.00 36.64           N  
ANISOU 1162  N   GLU A 201     4262   4592   5067    580    580   -801       N  
ATOM   1163  CA  GLU A 201       7.400 -18.089  21.710  1.00 37.66           C  
ANISOU 1163  CA  GLU A 201     4467   4556   5286    542    551   -857       C  
ATOM   1164  C   GLU A 201       7.474 -17.111  20.580  1.00 37.64           C  
ANISOU 1164  C   GLU A 201     4545   4351   5407    426    563   -823       C  
ATOM   1165  O   GLU A 201       8.053 -17.401  19.525  1.00 35.95           O  
ANISOU 1165  O   GLU A 201     4332   4062   5264    314    563   -830       O  
ATOM   1166  CB  GLU A 201       6.090 -18.840  21.675  1.00 39.75           C  
ANISOU 1166  CB  GLU A 201     4811   4772   5522    704    497   -954       C  
ATOM   1167  CG  GLU A 201       6.211 -20.238  22.216  1.00 42.12           C  
ANISOU 1167  CG  GLU A 201     5026   5253   5723    785    479  -1010       C  
ATOM   1168  CD  GLU A 201       6.516 -20.342  23.690  1.00 44.29           C  
ANISOU 1168  CD  GLU A 201     5169   5803   5854    856    504   -972       C  
ATOM   1169  OE1 GLU A 201       6.461 -19.359  24.487  1.00 43.55           O  
ANISOU 1169  OE1 GLU A 201     5044   5790   5715    878    528   -919       O  
ATOM   1170  OE2 GLU A 201       6.855 -21.493  24.018  1.00 49.97           O1-
ANISOU 1170  OE2 GLU A 201     5808   6682   6499    879    500   -999       O1-
ATOM   1171  N   VAL A 202       6.880 -15.948  20.817  1.00 40.23           N  
ANISOU 1171  N   VAL A 202     4930   4611   5744    463    572   -783       N  
ATOM   1172  CA  VAL A 202       6.786 -14.896  19.812  1.00 42.44           C  
ANISOU 1172  CA  VAL A 202     5292   4708   6127    365    587   -741       C  
ATOM   1173  C   VAL A 202       8.138 -14.261  19.549  1.00 41.92           C  
ANISOU 1173  C   VAL A 202     5145   4687   6094    220    628   -670       C  
ATOM   1174  O   VAL A 202       8.477 -14.044  18.395  1.00 43.44           O  
ANISOU 1174  O   VAL A 202     5361   4778   6368    110    633   -662       O  
ATOM   1175  CB  VAL A 202       5.796 -13.777  20.232  1.00 45.27           C  
ANISOU 1175  CB  VAL A 202     5742   4992   6467    465    591   -704       C  
ATOM   1176  CG1 VAL A 202       5.713 -12.687  19.178  1.00 43.64           C  
ANISOU 1176  CG1 VAL A 202     5616   4608   6358    349    612   -648       C  
ATOM   1177  CG2 VAL A 202       4.408 -14.347  20.490  1.00 48.30           C  
ANISOU 1177  CG2 VAL A 202     6244   5303   6803    638    546   -777       C  
ATOM   1178  N   LEU A 203       8.906 -13.947  20.595  1.00 41.56           N  
ANISOU 1178  N   LEU A 203     5011   4802   5978    218    654   -624       N  
ATOM   1179  CA  LEU A 203      10.178 -13.272  20.369  1.00 41.15           C  
ANISOU 1179  CA  LEU A 203     4916   4768   5951     89    688   -563       C  
ATOM   1180  C   LEU A 203      11.269 -14.194  19.889  1.00 40.30           C  
ANISOU 1180  C   LEU A 203     4778   4686   5850      9    690   -576       C  
ATOM   1181  O   LEU A 203      12.159 -13.759  19.160  1.00 43.54           O  
ANISOU 1181  O   LEU A 203     5195   5047   6302    -79    706   -544       O  
ATOM   1182  CB  LEU A 203      10.632 -12.476  21.569  1.00 42.99           C  
ANISOU 1182  CB  LEU A 203     5086   5142   6108     87    714   -515       C  
ATOM   1183  CG  LEU A 203      10.057 -11.057  21.493  1.00 45.95           C  
ANISOU 1183  CG  LEU A 203     5501   5450   6506    118    725   -472       C  
ATOM   1184  CD1 LEU A 203       8.829 -10.860  22.406  1.00 48.31           C  
ANISOU 1184  CD1 LEU A 203     5813   5813   6731    283    712   -486       C  
ATOM   1185  CD2 LEU A 203      11.153 -10.052  21.794  1.00 44.88           C  
ANISOU 1185  CD2 LEU A 203     5316   5379   6357     22    756   -419       C  
ATOM   1186  N   GLY A 204      11.185 -15.465  20.254  1.00 39.05           N  
ANISOU 1186  N   GLY A 204     4589   4608   5639     57    672   -622       N  
ATOM   1187  CA  GLY A 204      12.000 -16.491  19.623  1.00 37.77           C  
ANISOU 1187  CA  GLY A 204     4417   4454   5480     14    668   -641       C  
ATOM   1188  C   GLY A 204      11.806 -16.534  18.117  1.00 37.91           C  
ANISOU 1188  C   GLY A 204     4477   4343   5585    -17    649   -677       C  
ATOM   1189  O   GLY A 204      12.766 -16.598  17.360  1.00 40.12           O  
ANISOU 1189  O   GLY A 204     4750   4613   5879    -76    658   -662       O  
ATOM   1190  N   SER A 205      10.569 -16.484  17.662  1.00 38.51           N  
ANISOU 1190  N   SER A 205     4600   4324   5707     20    622   -727       N  
ATOM   1191  CA  SER A 205      10.326 -16.507  16.235  1.00 40.05           C  
ANISOU 1191  CA  SER A 205     4825   4415   5976    -44    605   -766       C  
ATOM   1192  C   SER A 205      10.705 -15.173  15.593  1.00 40.45           C  
ANISOU 1192  C   SER A 205     4885   4403   6080   -134    634   -700       C  
ATOM   1193  O   SER A 205      11.317 -15.143  14.536  1.00 41.74           O  
ANISOU 1193  O   SER A 205     5022   4570   6269   -203    637   -703       O  
ATOM   1194  CB  SER A 205       8.867 -16.866  15.930  1.00 41.40           C  
ANISOU 1194  CB  SER A 205     5072   4481   6177     -4    566   -842       C  
ATOM   1195  OG  SER A 205       8.607 -18.240  16.158  1.00 40.82           O  
ANISOU 1195  OG  SER A 205     4982   4473   6056     75    531   -924       O  
ATOM   1196  N   TYR A 206      10.363 -14.062  16.220  1.00 41.37           N  
ANISOU 1196  N   TYR A 206     5032   4487   6201   -120    655   -643       N  
ATOM   1197  CA  TYR A 206      10.387 -12.799  15.496  1.00 41.46           C  
ANISOU 1197  CA  TYR A 206     5064   4426   6264   -196    678   -588       C  
ATOM   1198  C   TYR A 206      11.275 -11.699  16.051  1.00 39.60           C  
ANISOU 1198  C   TYR A 206     4797   4247   6004   -208    712   -511       C  
ATOM   1199  O   TYR A 206      11.356 -10.628  15.475  1.00 39.29           O  
ANISOU 1199  O   TYR A 206     4764   4167   5996   -259    732   -463       O  
ATOM   1200  CB  TYR A 206       8.958 -12.311  15.330  1.00 42.53           C  
ANISOU 1200  CB  TYR A 206     5295   4428   6438   -182    669   -592       C  
ATOM   1201  CG  TYR A 206       8.064 -13.280  14.570  1.00 43.99           C  
ANISOU 1201  CG  TYR A 206     5536   4524   6654   -203    631   -678       C  
ATOM   1202  CD1 TYR A 206       8.459 -13.828  13.361  1.00 44.79           C  
ANISOU 1202  CD1 TYR A 206     5590   4642   6785   -304    620   -724       C  
ATOM   1203  CD2 TYR A 206       6.796 -13.611  15.054  1.00 46.12           C  
ANISOU 1203  CD2 TYR A 206     5913   4700   6912   -112    603   -722       C  
ATOM   1204  CE1 TYR A 206       7.617 -14.687  12.658  1.00 47.74           C  
ANISOU 1204  CE1 TYR A 206     6011   4945   7181   -342    581   -816       C  
ATOM   1205  CE2 TYR A 206       5.949 -14.466  14.369  1.00 47.11           C  
ANISOU 1205  CE2 TYR A 206     6112   4726   7063   -138    562   -813       C  
ATOM   1206  CZ  TYR A 206       6.356 -15.002  13.173  1.00 48.83           C  
ANISOU 1206  CZ  TYR A 206     6272   4964   7317   -266    552   -862       C  
ATOM   1207  OH  TYR A 206       5.508 -15.852  12.501  1.00 50.23           O  
ANISOU 1207  OH  TYR A 206     6518   5053   7514   -308    508   -965       O  
ATOM   1208  N   GLY A 207      12.007 -11.983  17.108  1.00 39.85           N  
ANISOU 1208  N   GLY A 207     4790   4379   5971   -177    719   -500       N  
ATOM   1209  CA  GLY A 207      12.950 -11.003  17.646  1.00 42.25           C  
ANISOU 1209  CA  GLY A 207     5072   4736   6244   -208    747   -441       C  
ATOM   1210  C   GLY A 207      14.215 -10.804  16.810  1.00 41.59           C  
ANISOU 1210  C   GLY A 207     4984   4650   6167   -270    757   -424       C  
ATOM   1211  O   GLY A 207      14.511 -11.603  15.958  1.00 44.21           O  
ANISOU 1211  O   GLY A 207     5313   4975   6510   -277    743   -458       O  
ATOM   1212  N   VAL A 208      14.953  -9.732  17.068  1.00 41.88           N  
ANISOU 1212  N   VAL A 208     5023   4705   6185   -297    777   -379       N  
ATOM   1213  CA  VAL A 208      16.194  -9.425  16.359  1.00 42.11           C  
ANISOU 1213  CA  VAL A 208     5064   4732   6201   -324    784   -365       C  
ATOM   1214  C   VAL A 208      17.432  -9.781  17.175  1.00 43.21           C  
ANISOU 1214  C   VAL A 208     5241   4906   6270   -344    788   -360       C  
ATOM   1215  O   VAL A 208      18.504  -9.253  16.956  1.00 43.35           O  
ANISOU 1215  O   VAL A 208     5302   4911   6260   -357    794   -343       O  
ATOM   1216  CB  VAL A 208      16.270  -7.927  16.017  1.00 42.52           C  
ANISOU 1216  CB  VAL A 208     5113   4774   6268   -337    800   -323       C  
ATOM   1217  CG1 VAL A 208      15.160  -7.570  15.040  1.00 42.03           C  
ANISOU 1217  CG1 VAL A 208     5033   4667   6268   -345    801   -316       C  
ATOM   1218  CG2 VAL A 208      16.206  -7.067  17.283  1.00 42.55           C  
ANISOU 1218  CG2 VAL A 208     5115   4816   6238   -340    813   -295       C  
ATOM   1219  N   MET A 209      17.276 -10.705  18.102  1.00 46.16           N  
ANISOU 1219  N   MET A 209     5607   5322   6608   -348    786   -373       N  
ATOM   1220  CA  MET A 209      18.323 -11.131  19.028  1.00 48.54           C  
ANISOU 1220  CA  MET A 209     5948   5659   6834   -399    796   -360       C  
ATOM   1221  C   MET A 209      18.429 -12.643  18.903  1.00 47.79           C  
ANISOU 1221  C   MET A 209     5863   5581   6714   -373    787   -382       C  
ATOM   1222  O   MET A 209      17.487 -13.292  18.493  1.00 49.29           O  
ANISOU 1222  O   MET A 209     6008   5780   6939   -319    771   -417       O  
ATOM   1223  CB  MET A 209      17.832 -10.835  20.430  1.00 53.79           C  
ANISOU 1223  CB  MET A 209     6561   6419   7458   -434    806   -352       C  
ATOM   1224  CG  MET A 209      16.569 -11.679  20.694  1.00 60.17           C  
ANISOU 1224  CG  MET A 209     7308   7282   8273   -364    794   -382       C  
ATOM   1225  SD  MET A 209      15.157 -11.096  21.632  1.00 71.86           S  
ANISOU 1225  SD  MET A 209     8715   8852   9736   -297    791   -388       S  
ATOM   1226  CE  MET A 209      14.555  -9.616  20.846  1.00 69.95           C  
ANISOU 1226  CE  MET A 209     8497   8513   9568   -262    793   -366       C  
ATOM   1227  N   ASN A 210      19.540 -13.232  19.293  1.00 49.19           N  
ANISOU 1227  N   ASN A 210     6109   5759   6823   -413    798   -362       N  
ATOM   1228  CA  ASN A 210      19.654 -14.704  19.243  1.00 49.28           C  
ANISOU 1228  CA  ASN A 210     6129   5800   6796   -380    794   -373       C  
ATOM   1229  C   ASN A 210      19.464 -15.292  17.871  1.00 43.95           C  
ANISOU 1229  C   ASN A 210     5445   5097   6157   -288    771   -411       C  
ATOM   1230  O   ASN A 210      18.507 -16.011  17.586  1.00 42.14           O  
ANISOU 1230  O   ASN A 210     5149   4905   5955   -239    752   -456       O  
ATOM   1231  CB  ASN A 210      18.725 -15.369  20.242  1.00 52.95           C  
ANISOU 1231  CB  ASN A 210     6509   6374   7234   -382    794   -388       C  
ATOM   1232  CG  ASN A 210      18.950 -14.856  21.635  1.00 60.02           C  
ANISOU 1232  CG  ASN A 210     7386   7349   8068   -480    818   -354       C  
ATOM   1233  ND2 ASN A 210      18.031 -15.152  22.519  1.00 63.35           N  
ANISOU 1233  ND2 ASN A 210     7713   7900   8459   -463    817   -371       N  
ATOM   1234  OD1 ASN A 210      19.968 -14.222  21.921  1.00 66.23           O  
ANISOU 1234  OD1 ASN A 210     8246   8093   8824   -572    834   -322       O  
ATOM   1235  N   PRO A 211      20.395 -14.986  16.992  1.00 41.99           N  
ANISOU 1235  N   PRO A 211     5264   4794   5896   -258    769   -402       N  
ATOM   1236  CA  PRO A 211      20.328 -15.661  15.723  1.00 42.58           C  
ANISOU 1236  CA  PRO A 211     5313   4889   5978   -170    747   -443       C  
ATOM   1237  C   PRO A 211      20.366 -17.194  15.877  1.00 40.51           C  
ANISOU 1237  C   PRO A 211     5051   4679   5661   -124    741   -459       C  
ATOM   1238  O   PRO A 211      20.946 -17.714  16.826  1.00 38.13           O  
ANISOU 1238  O   PRO A 211     4813   4380   5293   -156    761   -417       O  
ATOM   1239  CB  PRO A 211      21.595 -15.159  15.020  1.00 42.90           C  
ANISOU 1239  CB  PRO A 211     5444   4887   5970   -123    749   -421       C  
ATOM   1240  CG  PRO A 211      22.515 -14.784  16.136  1.00 41.48           C  
ANISOU 1240  CG  PRO A 211     5382   4640   5738   -191    772   -368       C  
ATOM   1241  CD  PRO A 211      21.592 -14.141  17.094  1.00 40.48           C  
ANISOU 1241  CD  PRO A 211     5178   4536   5665   -287    782   -363       C  
ATOM   1242  N   ARG A 212      19.797 -17.888  14.901  1.00 37.90           N  
ANISOU 1242  N   ARG A 212     4651   4399   5349    -57    714   -520       N  
ATOM   1243  CA  ARG A 212      19.646 -19.317  14.971  1.00 36.39           C  
ANISOU 1243  CA  ARG A 212     4440   4278   5110     -2    704   -549       C  
ATOM   1244  C   ARG A 212      19.349 -19.914  13.598  1.00 35.07           C  
ANISOU 1244  C   ARG A 212     4203   4175   4946     74    672   -624       C  
ATOM   1245  O   ARG A 212      18.961 -19.203  12.657  1.00 34.40           O  
ANISOU 1245  O   ARG A 212     4066   4089   4917     55    658   -658       O  
ATOM   1246  CB  ARG A 212      18.480 -19.632  15.912  1.00 36.39           C  
ANISOU 1246  CB  ARG A 212     4376   4308   5141    -38    700   -572       C  
ATOM   1247  CG  ARG A 212      17.208 -18.846  15.607  1.00 36.31           C  
ANISOU 1247  CG  ARG A 212     4304   4262   5228    -68    682   -616       C  
ATOM   1248  CD  ARG A 212      15.933 -19.448  16.208  1.00 36.51           C  
ANISOU 1248  CD  ARG A 212     4282   4322   5268    -45    663   -666       C  
ATOM   1249  NE  ARG A 212      14.774 -18.611  15.883  1.00 37.33           N  
ANISOU 1249  NE  ARG A 212     4372   4355   5457    -69    648   -698       N  
ATOM   1250  CZ  ARG A 212      14.197 -18.531  14.671  1.00 39.32           C  
ANISOU 1250  CZ  ARG A 212     4609   4563   5767    -85    624   -754       C  
ATOM   1251  NH1 ARG A 212      14.618 -19.262  13.642  1.00 40.41           N1+
ANISOU 1251  NH1 ARG A 212     4717   4751   5885    -67    606   -800       N1+
ATOM   1252  NH2 ARG A 212      13.176 -17.719  14.462  1.00 40.33           N  
ANISOU 1252  NH2 ARG A 212     4753   4607   5966   -123    617   -766       N  
ATOM   1253  N   PRO A 213      19.490 -21.238  13.486  1.00 33.99           N  
ANISOU 1253  N   PRO A 213     4057   4115   4742    150    659   -651       N  
ATOM   1254  CA  PRO A 213      18.920 -21.889  12.320  1.00 34.74           C  
ANISOU 1254  CA  PRO A 213     4057   4299   4842    203    622   -746       C  
ATOM   1255  C   PRO A 213      17.368 -21.722  12.238  1.00 35.31           C  
ANISOU 1255  C   PRO A 213     4050   4354   5014    130    596   -820       C  
ATOM   1256  O   PRO A 213      16.738 -21.379  13.226  1.00 32.60           O  
ANISOU 1256  O   PRO A 213     3725   3948   4715     81    606   -798       O  
ATOM   1257  CB  PRO A 213      19.329 -23.356  12.511  1.00 34.14           C  
ANISOU 1257  CB  PRO A 213     3993   4311   4666    303    617   -754       C  
ATOM   1258  CG  PRO A 213      20.373 -23.358  13.543  1.00 33.16           C  
ANISOU 1258  CG  PRO A 213     3993   4130   4474    301    658   -649       C  
ATOM   1259  CD  PRO A 213      20.043 -22.214  14.429  1.00 32.91           C  
ANISOU 1259  CD  PRO A 213     3981   4003   4518    179    679   -605       C  
ATOM   1260  N   GLY A 214      16.791 -21.926  11.051  1.00 37.87           N  
ANISOU 1260  N   GLY A 214     4295   4733   5363    122    563   -908       N  
ATOM   1261  CA  GLY A 214      15.341 -21.785  10.824  1.00 39.43           C  
ANISOU 1261  CA  GLY A 214     4451   4883   5647     41    536   -984       C  
ATOM   1262  C   GLY A 214      14.893 -20.394  10.346  1.00 40.74           C  
ANISOU 1262  C   GLY A 214     4617   4964   5897    -69    547   -961       C  
ATOM   1263  O   GLY A 214      13.834 -19.861  10.786  1.00 44.33           O  
ANISOU 1263  O   GLY A 214     5106   5310   6425   -133    546   -964       O  
ATOM   1264  N   TYR A 215      15.698 -19.794   9.466  1.00 39.18           N  
ANISOU 1264  N   TYR A 215     4387   4824   5675    -75    560   -938       N  
ATOM   1265  CA  TYR A 215      15.313 -18.584   8.717  1.00 38.37           C  
ANISOU 1265  CA  TYR A 215     4254   4692   5632   -181    569   -926       C  
ATOM   1266  C   TYR A 215      15.015 -17.418   9.641  1.00 35.68           C  
ANISOU 1266  C   TYR A 215     3988   4214   5356   -229    599   -844       C  
ATOM   1267  O   TYR A 215      14.095 -16.651   9.449  1.00 35.80           O  
ANISOU 1267  O   TYR A 215     4010   4151   5441   -323    603   -840       O  
ATOM   1268  CB  TYR A 215      14.159 -18.904   7.733  1.00 39.88           C  
ANISOU 1268  CB  TYR A 215     4382   4907   5865   -286    537  -1025       C  
ATOM   1269  CG  TYR A 215      14.464 -20.155   6.896  1.00 42.37           C  
ANISOU 1269  CG  TYR A 215     4608   5392   6100   -230    502  -1120       C  
ATOM   1270  CD1 TYR A 215      15.406 -20.104   5.846  1.00 43.84           C  
ANISOU 1270  CD1 TYR A 215     4701   5754   6201   -185    503  -1129       C  
ATOM   1271  CD2 TYR A 215      13.881 -21.397   7.179  1.00 41.88           C  
ANISOU 1271  CD2 TYR A 215     4548   5336   6026   -193    467  -1203       C  
ATOM   1272  CE1 TYR A 215      15.719 -21.232   5.091  1.00 44.15           C  
ANISOU 1272  CE1 TYR A 215     4650   5978   6148   -112    471  -1217       C  
ATOM   1273  CE2 TYR A 215      14.204 -22.531   6.424  1.00 42.11           C  
ANISOU 1273  CE2 TYR A 215     4488   5542   5970   -129    434  -1291       C  
ATOM   1274  CZ  TYR A 215      15.111 -22.440   5.384  1.00 42.92           C  
ANISOU 1274  CZ  TYR A 215     4496   5823   5990    -89    438  -1297       C  
ATOM   1275  OH  TYR A 215      15.434 -23.524   4.605  1.00 42.69           O  
ANISOU 1275  OH  TYR A 215     4367   5995   5858     -9    405  -1387       O  
ATOM   1276  N   TRP A 216      15.821 -17.320  10.668  1.00 34.40           N  
ANISOU 1276  N   TRP A 216     3885   4026   5158   -165    621   -777       N  
ATOM   1277  CA  TRP A 216      15.807 -16.176  11.516  1.00 35.00           C  
ANISOU 1277  CA  TRP A 216     4014   4015   5270   -199    650   -702       C  
ATOM   1278  C   TRP A 216      15.772 -14.931  10.644  1.00 34.43           C  
ANISOU 1278  C   TRP A 216     3914   3937   5232   -262    663   -675       C  
ATOM   1279  O   TRP A 216      16.418 -14.869   9.606  1.00 33.92           O  
ANISOU 1279  O   TRP A 216     3798   3963   5127   -246    660   -690       O  
ATOM   1280  CB  TRP A 216      17.077 -16.212  12.355  1.00 36.69           C  
ANISOU 1280  CB  TRP A 216     4289   4237   5416   -142    671   -641       C  
ATOM   1281  CG  TRP A 216      17.149 -15.200  13.401  1.00 38.76           C  
ANISOU 1281  CG  TRP A 216     4597   4434   5695   -180    696   -576       C  
ATOM   1282  CD1 TRP A 216      16.492 -15.208  14.566  1.00 39.09           C  
ANISOU 1282  CD1 TRP A 216     4650   4451   5750   -198    702   -564       C  
ATOM   1283  CD2 TRP A 216      17.971 -14.020  13.404  1.00 41.00           C  
ANISOU 1283  CD2 TRP A 216     4917   4694   5968   -195    717   -521       C  
ATOM   1284  CE2 TRP A 216      17.736 -13.360  14.603  1.00 39.78           C  
ANISOU 1284  CE2 TRP A 216     4788   4500   5826   -236    735   -480       C  
ATOM   1285  CE3 TRP A 216      18.862 -13.447  12.490  1.00 41.65           C  
ANISOU 1285  CE3 TRP A 216     5004   4801   6018   -164    720   -509       C  
ATOM   1286  NE1 TRP A 216      16.838 -14.111  15.307  1.00 40.11           N  
ANISOU 1286  NE1 TRP A 216     4810   4553   5879   -231    726   -506       N  
ATOM   1287  CZ2 TRP A 216      18.357 -12.165  14.924  1.00 40.39           C  
ANISOU 1287  CZ2 TRP A 216     4901   4553   5893   -261    753   -434       C  
ATOM   1288  CZ3 TRP A 216      19.479 -12.254  12.817  1.00 39.61           C  
ANISOU 1288  CZ3 TRP A 216     4793   4508   5749   -178    738   -461       C  
ATOM   1289  CH2 TRP A 216      19.226 -11.631  14.017  1.00 38.63           C  
ANISOU 1289  CH2 TRP A 216     4697   4334   5646   -231    754   -425       C  
ATOM   1290  N   GLY A 217      14.997 -13.941  11.062  1.00 34.77           N  
ANISOU 1290  N   GLY A 217     3983   3892   5336   -320    679   -638       N  
ATOM   1291  CA  GLY A 217      14.973 -12.648  10.398  1.00 35.31           C  
ANISOU 1291  CA  GLY A 217     4030   3957   5429   -381    699   -595       C  
ATOM   1292  C   GLY A 217      14.122 -12.600   9.158  1.00 36.52           C  
ANISOU 1292  C   GLY A 217     4130   4128   5618   -478    690   -635       C  
ATOM   1293  O   GLY A 217      14.047 -11.571   8.490  1.00 36.08           O  
ANISOU 1293  O   GLY A 217     4044   4092   5575   -544    711   -597       O  
ATOM   1294  N   ALA A 218      13.485 -13.718   8.831  1.00 38.49           N  
ANISOU 1294  N   ALA A 218     4365   4382   5877   -499    660   -716       N  
ATOM   1295  CA  ALA A 218      12.715 -13.811   7.582  1.00 40.57           C  
ANISOU 1295  CA  ALA A 218     4576   4674   6163   -623    646   -771       C  
ATOM   1296  C   ALA A 218      11.291 -14.324   7.821  1.00 41.29           C  
ANISOU 1296  C   ALA A 218     4746   4627   6314   -685    623   -826       C  
ATOM   1297  O   ALA A 218      10.909 -15.321   7.226  1.00 43.80           O  
ANISOU 1297  O   ALA A 218     5033   4985   6625   -722    588   -921       O  
ATOM   1298  CB  ALA A 218      13.453 -14.687   6.553  1.00 40.54           C  
ANISOU 1298  CB  ALA A 218     4459   4856   6087   -598    624   -843       C  
ATOM   1299  N   GLY A 219      10.536 -13.640   8.687  1.00 40.38           N  
ANISOU 1299  N   GLY A 219     4737   4359   6247   -680    637   -771       N  
ATOM   1300  CA  GLY A 219       9.130 -13.951   8.941  1.00 40.76           C  
ANISOU 1300  CA  GLY A 219     4897   4249   6340   -713    615   -815       C  
ATOM   1301  C   GLY A 219       8.183 -12.847   8.486  1.00 41.20           C  
ANISOU 1301  C   GLY A 219     5036   4172   6445   -839    638   -763       C  
ATOM   1302  O   GLY A 219       8.581 -11.936   7.792  1.00 39.51           O  
ANISOU 1302  O   GLY A 219     4763   4018   6231   -925    671   -702       O  
ATOM   1303  N   PRO A 220       6.898 -12.945   8.852  1.00 43.71           N  
ANISOU 1303  N   PRO A 220     5504   4307   6798   -844    620   -785       N  
ATOM   1304  CA  PRO A 220       5.948 -11.892   8.516  1.00 45.90           C  
ANISOU 1304  CA  PRO A 220     5901   4425   7113   -954    646   -721       C  
ATOM   1305  C   PRO A 220       6.005 -10.717   9.445  1.00 45.68           C  
ANISOU 1305  C   PRO A 220     5923   4354   7078   -852    684   -605       C  
ATOM   1306  O   PRO A 220       5.441  -9.667   9.155  1.00 47.13           O  
ANISOU 1306  O   PRO A 220     6189   4438   7282   -929    717   -526       O  
ATOM   1307  CB  PRO A 220       4.579 -12.561   8.689  1.00 47.54           C  
ANISOU 1307  CB  PRO A 220     6287   4436   7342   -954    605   -796       C  
ATOM   1308  CG  PRO A 220       4.838 -14.013   8.837  1.00 47.38           C  
ANISOU 1308  CG  PRO A 220     6202   4505   7296   -879    556   -917       C  
ATOM   1309  CD  PRO A 220       6.220 -14.130   9.402  1.00 45.37           C  
ANISOU 1309  CD  PRO A 220     5788   4449   6999   -757    572   -882       C  
ATOM   1310  N   LEU A 221       6.726 -10.896  10.535  1.00 46.65           N  
ANISOU 1310  N   LEU A 221     5991   4569   7166   -690    682   -595       N  
ATOM   1311  CA  LEU A 221       6.690 -10.004  11.664  1.00 47.18           C  
ANISOU 1311  CA  LEU A 221     6102   4614   7210   -569    707   -513       C  
ATOM   1312  C   LEU A 221       8.069  -9.887  12.281  1.00 43.69           C  
ANISOU 1312  C   LEU A 221     5531   4343   6727   -497    721   -486       C  
ATOM   1313  O   LEU A 221       8.872 -10.814  12.250  1.00 40.86           O  
ANISOU 1313  O   LEU A 221     5089   4089   6348   -480    703   -540       O  
ATOM   1314  CB  LEU A 221       5.749 -10.591  12.692  1.00 52.25           C  
ANISOU 1314  CB  LEU A 221     6858   5165   7829   -428    675   -556       C  
ATOM   1315  CG  LEU A 221       5.595  -9.870  14.036  1.00 56.90           C  
ANISOU 1315  CG  LEU A 221     7480   5770   8367   -268    691   -492       C  
ATOM   1316  CD1 LEU A 221       4.816  -8.561  13.876  1.00 59.94           C  
ANISOU 1316  CD1 LEU A 221     7985   6025   8763   -283    723   -402       C  
ATOM   1317  CD2 LEU A 221       4.911 -10.787  15.043  1.00 58.91           C  
ANISOU 1317  CD2 LEU A 221     7795   6015   8571   -105    651   -562       C  
ATOM   1318  N   CYS A 222       8.336  -8.735  12.856  1.00 43.47           N  
ANISOU 1318  N   CYS A 222     5499   4337   6681   -454    753   -400       N  
ATOM   1319  CA  CYS A 222       9.632  -8.482  13.421  1.00 43.07           C  
ANISOU 1319  CA  CYS A 222     5351   4426   6589   -409    767   -376       C  
ATOM   1320  C   CYS A 222       9.472  -7.594  14.625  1.00 41.67           C  
ANISOU 1320  C   CYS A 222     5199   4261   6374   -314    784   -319       C  
ATOM   1321  O   CYS A 222       8.984  -6.458  14.499  1.00 41.23           O  
ANISOU 1321  O   CYS A 222     5188   4153   6324   -320    810   -252       O  
ATOM   1322  CB  CYS A 222      10.519  -7.811  12.386  1.00 45.34           C  
ANISOU 1322  CB  CYS A 222     5564   4782   6882   -496    790   -341       C  
ATOM   1323  SG  CYS A 222      12.182  -7.458  12.979  1.00 46.34           S  
ANISOU 1323  SG  CYS A 222     5613   5043   6951   -440    801   -319       S  
ATOM   1324  N   ILE A 223       9.886  -8.117  15.780  1.00 39.80           N  
ANISOU 1324  N   ILE A 223     4926   4111   6085   -231    772   -345       N  
ATOM   1325  CA  ILE A 223       9.686  -7.447  17.025  1.00 39.61           C  
ANISOU 1325  CA  ILE A 223     4903   4142   6005   -139    783   -310       C  
ATOM   1326  C   ILE A 223      10.975  -6.901  17.551  1.00 39.22           C  
ANISOU 1326  C   ILE A 223     4773   4216   5913   -162    800   -284       C  
ATOM   1327  O   ILE A 223      11.913  -7.629  17.902  1.00 42.04           O  
ANISOU 1327  O   ILE A 223     5082   4649   6242   -185    793   -315       O  
ATOM   1328  CB  ILE A 223       9.006  -8.361  18.029  1.00 40.87           C  
ANISOU 1328  CB  ILE A 223     5081   4334   6115    -28    757   -361       C  
ATOM   1329  CG1 ILE A 223       7.642  -8.711  17.456  1.00 43.13           C  
ANISOU 1329  CG1 ILE A 223     5487   4461   6440      2    736   -388       C  
ATOM   1330  CG2 ILE A 223       8.936  -7.697  19.404  1.00 41.52           C  
ANISOU 1330  CG2 ILE A 223     5125   4538   6111     71    767   -332       C  
ATOM   1331  CD1 ILE A 223       6.627  -9.251  18.406  1.00 45.19           C  
ANISOU 1331  CD1 ILE A 223     5807   4725   6639    159    709   -429       C  
ATOM   1332  N   ALA A 224      11.013  -5.582  17.601  1.00 38.79           N  
ANISOU 1332  N   ALA A 224     4717   4172   5849   -160    824   -224       N  
ATOM   1333  CA  ALA A 224      12.176  -4.891  18.087  1.00 38.71           C  
ANISOU 1333  CA  ALA A 224     4647   4267   5796   -185    838   -205       C  
ATOM   1334  C   ALA A 224      11.771  -3.881  19.145  1.00 37.41           C  
ANISOU 1334  C   ALA A 224     4467   4179   5568   -110    849   -172       C  
ATOM   1335  O   ALA A 224      10.770  -3.199  19.008  1.00 37.20           O  
ANISOU 1335  O   ALA A 224     4488   4098   5546    -47    859   -130       O  
ATOM   1336  CB  ALA A 224      12.902  -4.209  16.937  1.00 38.28           C  
ANISOU 1336  CB  ALA A 224     4584   4187   5775   -254    852   -176       C  
ATOM   1337  N   ASP A 225      12.586  -3.788  20.189  1.00 36.02           N  
ANISOU 1337  N   ASP A 225     4228   4134   5323   -122    848   -190       N  
ATOM   1338  CA  ASP A 225      12.420  -2.782  21.198  1.00 35.26           C  
ANISOU 1338  CA  ASP A 225     4089   4158   5151    -65    857   -170       C  
ATOM   1339  C   ASP A 225      13.745  -2.051  21.388  1.00 34.10           C  
ANISOU 1339  C   ASP A 225     3901   4083   4972   -150    864   -173       C  
ATOM   1340  O   ASP A 225      14.775  -2.668  21.607  1.00 33.94           O  
ANISOU 1340  O   ASP A 225     3873   4084   4939   -237    856   -208       O  
ATOM   1341  CB  ASP A 225      11.949  -3.430  22.486  1.00 35.49           C  
ANISOU 1341  CB  ASP A 225     4069   4318   5098      2    844   -208       C  
ATOM   1342  CG  ASP A 225      10.629  -4.193  22.317  1.00 36.02           C  
ANISOU 1342  CG  ASP A 225     4199   4305   5184    112    830   -218       C  
ATOM   1343  OD1 ASP A 225       9.614  -3.557  21.976  1.00 36.52           O  
ANISOU 1343  OD1 ASP A 225     4333   4281   5260    204    835   -179       O  
ATOM   1344  OD2 ASP A 225      10.604  -5.417  22.553  1.00 35.95           O1-
ANISOU 1344  OD2 ASP A 225     4178   4315   5168    110    813   -265       O1-
ATOM   1345  N   GLY A 226      13.716  -0.733  21.265  1.00 33.34           N  
ANISOU 1345  N   GLY A 226     3796   4012   4859   -120    878   -133       N  
ATOM   1346  CA  GLY A 226      14.898   0.063  21.505  1.00 33.46           C  
ANISOU 1346  CA  GLY A 226     3782   4100   4833   -185    879   -146       C  
ATOM   1347  C   GLY A 226      15.655   0.428  20.240  1.00 33.49           C  
ANISOU 1347  C   GLY A 226     3827   4007   4889   -225    883   -130       C  
ATOM   1348  O   GLY A 226      15.505  -0.173  19.204  1.00 31.66           O  
ANISOU 1348  O   GLY A 226     3632   3672   4724   -237    884   -119       O  
ATOM   1349  N   VAL A 227      16.460   1.467  20.335  1.00 35.17           N  
ANISOU 1349  N   VAL A 227     4027   4276   5058   -241    884   -133       N  
ATOM   1350  CA  VAL A 227      17.056   2.055  19.155  1.00 36.24           C  
ANISOU 1350  CA  VAL A 227     4190   4361   5220   -241    889   -112       C  
ATOM   1351  C   VAL A 227      18.001   1.060  18.527  1.00 37.62           C  
ANISOU 1351  C   VAL A 227     4417   4456   5420   -293    873   -150       C  
ATOM   1352  O   VAL A 227      18.114   0.989  17.314  1.00 38.21           O  
ANISOU 1352  O   VAL A 227     4505   4483   5532   -278    877   -133       O  
ATOM   1353  CB  VAL A 227      17.765   3.390  19.500  1.00 36.44           C  
ANISOU 1353  CB  VAL A 227     4194   4477   5174   -229    886   -122       C  
ATOM   1354  CG1 VAL A 227      18.546   3.901  18.321  1.00 36.92           C  
ANISOU 1354  CG1 VAL A 227     4281   4505   5241   -214    886   -114       C  
ATOM   1355  CG2 VAL A 227      16.757   4.451  19.925  1.00 36.79           C  
ANISOU 1355  CG2 VAL A 227     4182   4610   5184   -149    905    -72       C  
ATOM   1356  N   GLU A 228      18.675   0.279  19.361  1.00 41.90           N  
ANISOU 1356  N   GLU A 228     4989   5000   5931   -354    857   -199       N  
ATOM   1357  CA  GLU A 228      19.662  -0.675  18.868  1.00 43.69           C  
ANISOU 1357  CA  GLU A 228     5289   5147   6165   -390    843   -229       C  
ATOM   1358  C   GLU A 228      18.944  -1.746  18.091  1.00 42.82           C  
ANISOU 1358  C   GLU A 228     5169   4981   6121   -367    846   -217       C  
ATOM   1359  O   GLU A 228      19.361  -2.107  17.004  1.00 41.40           O  
ANISOU 1359  O   GLU A 228     5014   4756   5959   -346    840   -221       O  
ATOM   1360  CB  GLU A 228      20.456  -1.303  20.010  1.00 45.69           C  
ANISOU 1360  CB  GLU A 228     5590   5407   6363   -479    830   -271       C  
ATOM   1361  CG  GLU A 228      21.238  -0.299  20.852  1.00 49.46           C  
ANISOU 1361  CG  GLU A 228     6086   5941   6766   -536    823   -300       C  
ATOM   1362  CD  GLU A 228      22.347   0.359  20.064  1.00 53.82           C  
ANISOU 1362  CD  GLU A 228     6727   6425   7294   -504    809   -317       C  
ATOM   1363  OE1 GLU A 228      23.345  -0.350  19.752  1.00 62.02           O  
ANISOU 1363  OE1 GLU A 228     7885   7364   8315   -521    796   -339       O  
ATOM   1364  OE2 GLU A 228      22.224   1.567  19.753  1.00 56.15           O1-
ANISOU 1364  OE2 GLU A 228     6984   6773   7578   -445    810   -307       O1-
ATOM   1365  N   GLU A 229      17.863  -2.267  18.651  1.00 43.53           N  
ANISOU 1365  N   GLU A 229     5220   5086   6232   -363    850   -210       N  
ATOM   1366  CA  GLU A 229      17.163  -3.365  17.996  1.00 43.79           C  
ANISOU 1366  CA  GLU A 229     5254   5062   6323   -349    847   -214       C  
ATOM   1367  C   GLU A 229      16.459  -2.963  16.689  1.00 45.41           C  
ANISOU 1367  C   GLU A 229     5446   5223   6585   -324    857   -182       C  
ATOM   1368  O   GLU A 229      16.375  -3.771  15.757  1.00 47.57           O  
ANISOU 1368  O   GLU A 229     5724   5456   6895   -335    850   -199       O  
ATOM   1369  CB  GLU A 229      16.176  -4.015  18.953  1.00 43.88           C  
ANISOU 1369  CB  GLU A 229     5240   5102   6328   -332    845   -224       C  
ATOM   1370  CG  GLU A 229      16.793  -5.077  19.830  1.00 44.49           C  
ANISOU 1370  CG  GLU A 229     5323   5221   6360   -377    835   -260       C  
ATOM   1371  CD  GLU A 229      15.756  -5.917  20.586  1.00 47.38           C  
ANISOU 1371  CD  GLU A 229     5652   5638   6714   -337    830   -277       C  
ATOM   1372  OE1 GLU A 229      14.647  -6.298  20.061  1.00 47.21           O  
ANISOU 1372  OE1 GLU A 229     5637   5558   6740   -274    823   -279       O  
ATOM   1373  OE2 GLU A 229      16.094  -6.225  21.747  1.00 46.74           O1-
ANISOU 1373  OE2 GLU A 229     5538   5659   6560   -376    830   -292       O1-
ATOM   1374  N   VAL A 230      15.935  -1.741  16.611  1.00 44.93           N  
ANISOU 1374  N   VAL A 230     5366   5182   6523   -301    875   -135       N  
ATOM   1375  CA  VAL A 230      15.204  -1.338  15.405  1.00 44.52           C  
ANISOU 1375  CA  VAL A 230     5306   5091   6516   -307    892    -92       C  
ATOM   1376  C   VAL A 230      16.167  -1.215  14.233  1.00 45.75           C  
ANISOU 1376  C   VAL A 230     5441   5280   6664   -324    890   -100       C  
ATOM   1377  O   VAL A 230      15.757  -1.330  13.083  1.00 48.97           O  
ANISOU 1377  O   VAL A 230     5824   5679   7102   -357    898    -86       O  
ATOM   1378  CB  VAL A 230      14.391  -0.018  15.554  1.00 45.12           C  
ANISOU 1378  CB  VAL A 230     5377   5181   6582   -273    918    -23       C  
ATOM   1379  CG1 VAL A 230      13.311  -0.150  16.598  1.00 46.74           C  
ANISOU 1379  CG1 VAL A 230     5613   5365   6781   -220    917    -16       C  
ATOM   1380  CG2 VAL A 230      15.272   1.165  15.913  1.00 47.51           C  
ANISOU 1380  CG2 VAL A 230     5651   5576   6823   -245    922    -13       C  
ATOM   1381  N   ARG A 231      17.436  -0.933  14.515  1.00 43.57           N  
ANISOU 1381  N   ARG A 231     5175   5047   6331   -301    879   -126       N  
ATOM   1382  CA  ARG A 231      18.416  -0.837  13.458  1.00 42.67           C  
ANISOU 1382  CA  ARG A 231     5054   4975   6183   -276    872   -141       C  
ATOM   1383  C   ARG A 231      18.571  -2.161  12.752  1.00 39.69           C  
ANISOU 1383  C   ARG A 231     4678   4580   5823   -284    856   -180       C  
ATOM   1384  O   ARG A 231      18.572  -2.208  11.526  1.00 42.52           O  
ANISOU 1384  O   ARG A 231     4984   4993   6177   -281    859   -180       O  
ATOM   1385  CB  ARG A 231      19.763  -0.407  13.992  1.00 43.88           C  
ANISOU 1385  CB  ARG A 231     5261   5145   6266   -237    855   -172       C  
ATOM   1386  CG  ARG A 231      19.841   1.052  14.338  1.00 45.50           C  
ANISOU 1386  CG  ARG A 231     5447   5405   6434   -214    866   -145       C  
ATOM   1387  CD  ARG A 231      21.284   1.407  14.595  1.00 47.63           C  
ANISOU 1387  CD  ARG A 231     5793   5679   6626   -175    842   -191       C  
ATOM   1388  NE  ARG A 231      21.413   2.769  15.083  1.00 48.58           N  
ANISOU 1388  NE  ARG A 231     5898   5859   6703   -155    845   -183       N  
ATOM   1389  CZ  ARG A 231      21.301   3.847  14.326  1.00 46.26           C  
ANISOU 1389  CZ  ARG A 231     5546   5649   6384    -97    859   -149       C  
ATOM   1390  NH1 ARG A 231      21.032   3.728  13.045  1.00 47.28           N1+
ANISOU 1390  NH1 ARG A 231     5618   5822   6526    -71    873   -118       N1+
ATOM   1391  NH2 ARG A 231      21.463   5.045  14.854  1.00 46.72           N  
ANISOU 1391  NH2 ARG A 231     5592   5769   6392    -70    859   -148       N  
ATOM   1392  N   ARG A 232      18.712  -3.229  13.514  1.00 36.23           N  
ANISOU 1392  N   ARG A 232     4286   4088   5391   -294    840   -214       N  
ATOM   1393  CA  ARG A 232      18.793  -4.534  12.918  1.00 35.71           C  
ANISOU 1393  CA  ARG A 232     4220   4014   5334   -291    825   -254       C  
ATOM   1394  C   ARG A 232      17.479  -4.919  12.219  1.00 36.35           C  
ANISOU 1394  C   ARG A 232     4245   4086   5482   -340    830   -250       C  
ATOM   1395  O   ARG A 232      17.484  -5.515  11.129  1.00 36.21           O  
ANISOU 1395  O   ARG A 232     4184   4111   5463   -348    823   -278       O  
ATOM   1396  CB  ARG A 232      19.163  -5.572  13.958  1.00 36.40           C  
ANISOU 1396  CB  ARG A 232     4369   4055   5407   -296    812   -282       C  
ATOM   1397  CG  ARG A 232      19.098  -6.975  13.394  1.00 38.33           C  
ANISOU 1397  CG  ARG A 232     4606   4299   5657   -283    796   -320       C  
ATOM   1398  CD  ARG A 232      20.329  -7.776  13.716  1.00 40.16           C  
ANISOU 1398  CD  ARG A 232     4921   4514   5822   -245    785   -340       C  
ATOM   1399  NE  ARG A 232      20.559  -7.901  15.150  1.00 40.27           N  
ANISOU 1399  NE  ARG A 232     4995   4490   5817   -293    790   -330       N  
ATOM   1400  CZ  ARG A 232      21.666  -7.527  15.784  1.00 41.07           C  
ANISOU 1400  CZ  ARG A 232     5189   4559   5857   -307    791   -322       C  
ATOM   1401  NH1 ARG A 232      22.710  -6.964  15.155  1.00 41.94           N1+
ANISOU 1401  NH1 ARG A 232     5368   4652   5916   -248    783   -325       N1+
ATOM   1402  NH2 ARG A 232      21.729  -7.726  17.081  1.00 42.15           N  
ANISOU 1402  NH2 ARG A 232     5354   4687   5971   -382    798   -316       N  
ATOM   1403  N   ALA A 233      16.351  -4.577  12.834  1.00 36.95           N  
ANISOU 1403  N   ALA A 233     4328   4110   5603   -371    844   -221       N  
ATOM   1404  CA  ALA A 233      15.062  -4.880  12.232  1.00 37.29           C  
ANISOU 1404  CA  ALA A 233     4360   4106   5705   -424    847   -219       C  
ATOM   1405  C   ALA A 233      14.952  -4.291  10.824  1.00 37.46           C  
ANISOU 1405  C   ALA A 233     4323   4181   5728   -479    863   -194       C  
ATOM   1406  O   ALA A 233      14.546  -4.993   9.900  1.00 40.85           O  
ANISOU 1406  O   ALA A 233     4721   4621   6178   -539    855   -228       O  
ATOM   1407  CB  ALA A 233      13.924  -4.385  13.110  1.00 37.55           C  
ANISOU 1407  CB  ALA A 233     4437   4066   5763   -417    859   -181       C  
ATOM   1408  N   VAL A 234      15.300  -3.017  10.649  1.00 35.87           N  
ANISOU 1408  N   VAL A 234     4098   4035   5495   -466    886   -141       N  
ATOM   1409  CA  VAL A 234      15.184  -2.386   9.334  1.00 36.04           C  
ANISOU 1409  CA  VAL A 234     4048   4143   5503   -525    907   -109       C  
ATOM   1410  C   VAL A 234      16.104  -3.130   8.411  1.00 34.52           C  
ANISOU 1410  C   VAL A 234     3790   4064   5263   -502    886   -168       C  
ATOM   1411  O   VAL A 234      15.742  -3.500   7.314  1.00 35.61           O  
ANISOU 1411  O   VAL A 234     3859   4271   5402   -578    887   -187       O  
ATOM   1412  CB  VAL A 234      15.569  -0.885   9.322  1.00 36.17           C  
ANISOU 1412  CB  VAL A 234     4039   4231   5473   -489    932    -45       C  
ATOM   1413  CG1 VAL A 234      15.608  -0.361   7.903  1.00 36.71           C  
ANISOU 1413  CG1 VAL A 234     4010   4435   5504   -545    954    -17       C  
ATOM   1414  CG2 VAL A 234      14.571  -0.055  10.116  1.00 36.25           C  
ANISOU 1414  CG2 VAL A 234     4108   4152   5515   -497    958     23       C  
ATOM   1415  N   ARG A 235      17.309  -3.355   8.881  1.00 33.75           N  
ANISOU 1415  N   ARG A 235     3720   3990   5112   -397    864   -202       N  
ATOM   1416  CA  ARG A 235      18.322  -3.954   8.050  1.00 34.02           C  
ANISOU 1416  CA  ARG A 235     3713   4138   5074   -329    844   -253       C  
ATOM   1417  C   ARG A 235      17.968  -5.386   7.696  1.00 34.68           C  
ANISOU 1417  C   ARG A 235     3780   4216   5183   -361    824   -312       C  
ATOM   1418  O   ARG A 235      18.122  -5.782   6.554  1.00 36.13           O  
ANISOU 1418  O   ARG A 235     3874   4533   5322   -364    816   -347       O  
ATOM   1419  CB  ARG A 235      19.683  -3.844   8.728  1.00 34.21           C  
ANISOU 1419  CB  ARG A 235     3820   4145   5032   -206    827   -269       C  
ATOM   1420  CG  ARG A 235      20.166  -2.391   8.821  1.00 34.13           C  
ANISOU 1420  CG  ARG A 235     3812   4179   4977   -161    840   -230       C  
ATOM   1421  CD  ARG A 235      21.295  -2.248   9.814  1.00 33.86           C  
ANISOU 1421  CD  ARG A 235     3899   4071   4895    -81    822   -250       C  
ATOM   1422  NE  ARG A 235      21.749  -0.880   9.924  1.00 35.54           N  
ANISOU 1422  NE  ARG A 235     4117   4326   5059    -35    829   -227       N  
ATOM   1423  CZ  ARG A 235      22.681  -0.456  10.782  1.00 37.70           C  
ANISOU 1423  CZ  ARG A 235     4499   4539   5286     13    813   -246       C  
ATOM   1424  NH1 ARG A 235      23.277  -1.286  11.636  1.00 37.68           N1+
ANISOU 1424  NH1 ARG A 235     4615   4425   5278      5    794   -280       N1+
ATOM   1425  NH2 ARG A 235      23.022   0.829  10.801  1.00 39.57           N  
ANISOU 1425  NH2 ARG A 235     4729   4830   5475     57    816   -234       N  
ATOM   1426  N   LEU A 236      17.425  -6.161   8.626  1.00 35.53           N  
ANISOU 1426  N   LEU A 236     3955   4197   5349   -383    814   -327       N  
ATOM   1427  CA  LEU A 236      16.970  -7.524   8.275  1.00 35.29           C  
ANISOU 1427  CA  LEU A 236     3904   4165   5338   -414    791   -388       C  
ATOM   1428  C   LEU A 236      15.995  -7.583   7.101  1.00 36.59           C  
ANISOU 1428  C   LEU A 236     3983   4386   5532   -534    796   -406       C  
ATOM   1429  O   LEU A 236      16.062  -8.494   6.303  1.00 37.27           O  
ANISOU 1429  O   LEU A 236     4006   4565   5590   -545    775   -470       O  
ATOM   1430  CB  LEU A 236      16.358  -8.221   9.474  1.00 34.07           C  
ANISOU 1430  CB  LEU A 236     3827   3880   5237   -420    782   -400       C  
ATOM   1431  CG  LEU A 236      17.435  -8.649  10.456  1.00 34.17           C  
ANISOU 1431  CG  LEU A 236     3908   3873   5202   -329    772   -404       C  
ATOM   1432  CD1 LEU A 236      16.826  -9.094  11.767  1.00 32.69           C  
ANISOU 1432  CD1 LEU A 236     3776   3595   5050   -341    771   -402       C  
ATOM   1433  CD2 LEU A 236      18.269  -9.767   9.852  1.00 35.39           C  
ANISOU 1433  CD2 LEU A 236     4051   4102   5294   -261    751   -455       C  
ATOM   1434  N   GLN A 237      15.110  -6.609   6.971  1.00 37.33           N  
ANISOU 1434  N   GLN A 237     4081   4432   5671   -632    824   -350       N  
ATOM   1435  CA  GLN A 237      14.203  -6.590   5.832  1.00 39.06           C  
ANISOU 1435  CA  GLN A 237     4236   4696   5910   -782    833   -358       C  
ATOM   1436  C   GLN A 237      14.942  -6.228   4.553  1.00 38.96           C  
ANISOU 1436  C   GLN A 237     4082   4910   5809   -790    840   -364       C  
ATOM   1437  O   GLN A 237      14.729  -6.847   3.505  1.00 42.56           O  
ANISOU 1437  O   GLN A 237     4442   5490   6239   -875    830   -421       O  
ATOM   1438  CB  GLN A 237      13.036  -5.624   6.055  1.00 40.71           C  
ANISOU 1438  CB  GLN A 237     4515   4772   6180   -886    866   -281       C  
ATOM   1439  CG  GLN A 237      12.368  -5.736   7.421  1.00 40.54           C  
ANISOU 1439  CG  GLN A 237     4629   4556   6217   -830    859   -265       C  
ATOM   1440  CD  GLN A 237      12.270  -7.158   7.927  1.00 40.38           C  
ANISOU 1440  CD  GLN A 237     4646   4483   6216   -784    820   -350       C  
ATOM   1441  NE2 GLN A 237      12.815  -7.388   9.103  1.00 39.93           N  
ANISOU 1441  NE2 GLN A 237     4628   4399   6145   -663    810   -352       N  
ATOM   1442  OE1 GLN A 237      11.710  -8.042   7.267  1.00 41.42           O  
ANISOU 1442  OE1 GLN A 237     4765   4608   6365   -864    799   -415       O  
ATOM   1443  N   ILE A 238      15.831  -5.251   4.615  1.00 36.79           N  
ANISOU 1443  N   ILE A 238     3786   4716   5476   -694    857   -316       N  
ATOM   1444  CA  ILE A 238      16.583  -4.887   3.421  1.00 36.99           C  
ANISOU 1444  CA  ILE A 238     3672   4988   5395   -665    862   -325       C  
ATOM   1445  C   ILE A 238      17.325  -6.129   2.903  1.00 36.35           C  
ANISOU 1445  C   ILE A 238     3533   5037   5243   -573    823   -420       C  
ATOM   1446  O   ILE A 238      17.276  -6.457   1.729  1.00 36.06           O  
ANISOU 1446  O   ILE A 238     3357   5201   5143   -628    818   -463       O  
ATOM   1447  CB  ILE A 238      17.580  -3.742   3.714  1.00 36.66           C  
ANISOU 1447  CB  ILE A 238     3642   5000   5286   -528    874   -277       C  
ATOM   1448  CG1 ILE A 238      16.909  -2.454   4.277  1.00 37.84           C  
ANISOU 1448  CG1 ILE A 238     3844   5044   5492   -594    912   -183       C  
ATOM   1449  CG2 ILE A 238      18.442  -3.444   2.501  1.00 37.12           C  
ANISOU 1449  CG2 ILE A 238     3558   5336   5211   -451    872   -298       C  
ATOM   1450  CD1 ILE A 238      16.013  -1.633   3.379  1.00 39.12           C  
ANISOU 1450  CD1 ILE A 238     3921   5288   5655   -756    954   -118       C  
ATOM   1451  N   ARG A 239      17.921  -6.878   3.812  1.00 36.14           N  
ANISOU 1451  N   ARG A 239     3612   4897   5222   -446    796   -448       N  
ATOM   1452  CA  ARG A 239      18.556  -8.155   3.488  1.00 36.46           C  
ANISOU 1452  CA  ARG A 239     3628   5027   5195   -345    762   -528       C  
ATOM   1453  C   ARG A 239      17.720  -9.098   2.640  1.00 38.07           C  
ANISOU 1453  C   ARG A 239     3731   5320   5415   -469    748   -597       C  
ATOM   1454  O   ARG A 239      18.248  -9.815   1.796  1.00 40.19           O  
ANISOU 1454  O   ARG A 239     3900   5785   5586   -399    725   -663       O  
ATOM   1455  CB  ARG A 239      18.858  -8.896   4.765  1.00 35.74           C  
ANISOU 1455  CB  ARG A 239     3685   4749   5144   -263    746   -533       C  
ATOM   1456  CG  ARG A 239      20.030  -9.842   4.660  1.00 35.94           C  
ANISOU 1456  CG  ARG A 239     3739   4849   5067    -90    718   -579       C  
ATOM   1457  CD  ARG A 239      20.149 -10.592   5.972  1.00 35.51           C  
ANISOU 1457  CD  ARG A 239     3827   4607   5057    -57    711   -573       C  
ATOM   1458  NE  ARG A 239      20.337 -11.995   5.696  1.00 36.50           N  
ANISOU 1458  NE  ARG A 239     3938   4795   5135      5    684   -634       N  
ATOM   1459  CZ  ARG A 239      21.515 -12.541   5.440  1.00 35.95           C  
ANISOU 1459  CZ  ARG A 239     3908   4803   4949    177    669   -651       C  
ATOM   1460  NH1 ARG A 239      22.587 -11.788   5.487  1.00 35.67           N1+
ANISOU 1460  NH1 ARG A 239     3948   4767   4838    293    674   -617       N1+
ATOM   1461  NH2 ARG A 239      21.619 -13.842   5.178  1.00 36.01           N  
ANISOU 1461  NH2 ARG A 239     3897   4880   4907    242    646   -706       N  
ATOM   1462  N   ARG A 240      16.418  -9.107   2.875  1.00 38.02           N  
ANISOU 1462  N   ARG A 240     3758   5169   5518   -644    757   -588       N  
ATOM   1463  CA  ARG A 240      15.524  -9.963   2.123  1.00 39.13           C  
ANISOU 1463  CA  ARG A 240     3827   5361   5679   -790    740   -662       C  
ATOM   1464  C   ARG A 240      15.204  -9.343   0.773  1.00 39.91           C  
ANISOU 1464  C   ARG A 240     3772   5665   5728   -944    760   -661       C  
ATOM   1465  O   ARG A 240      14.577  -9.955  -0.062  1.00 41.11           O  
ANISOU 1465  O   ARG A 240     3837   5911   5871  -1090    747   -730       O  
ATOM   1466  CB  ARG A 240      14.247 -10.184   2.923  1.00 39.67           C  
ANISOU 1466  CB  ARG A 240     4026   5174   5873   -905    738   -655       C  
ATOM   1467  CG  ARG A 240      14.524 -10.630   4.347  1.00 39.89           C  
ANISOU 1467  CG  ARG A 240     4187   5030   5938   -762    727   -643       C  
ATOM   1468  CD  ARG A 240      13.297 -10.490   5.230  1.00 41.15           C  
ANISOU 1468  CD  ARG A 240     4475   4959   6201   -838    733   -617       C  
ATOM   1469  NE  ARG A 240      12.255 -11.437   4.833  1.00 43.37           N  
ANISOU 1469  NE  ARG A 240     4767   5192   6521   -948    704   -699       N  
ATOM   1470  CZ  ARG A 240      11.071 -11.572   5.432  1.00 43.59           C  
ANISOU 1470  CZ  ARG A 240     4919   5020   6623  -1003    698   -704       C  
ATOM   1471  NH1 ARG A 240      10.746 -10.812   6.473  1.00 42.80           N1+
ANISOU 1471  NH1 ARG A 240     4930   4770   6563   -951    719   -626       N1+
ATOM   1472  NH2 ARG A 240      10.208 -12.477   4.983  1.00 44.91           N  
ANISOU 1472  NH2 ARG A 240     5103   5147   6812  -1099    665   -794       N  
ATOM   1473  N   GLY A 241      15.630  -8.115   0.555  1.00 39.92           N  
ANISOU 1473  N   GLY A 241     3733   5747   5686   -922    793   -585       N  
ATOM   1474  CA  GLY A 241      15.291  -7.428  -0.677  1.00 40.91           C  
ANISOU 1474  CA  GLY A 241     3705   6084   5755  -1085    821   -568       C  
ATOM   1475  C   GLY A 241      14.120  -6.477  -0.581  1.00 40.67           C  
ANISOU 1475  C   GLY A 241     3741   5894   5815  -1296    864   -480       C  
ATOM   1476  O   GLY A 241      13.688  -5.974  -1.603  1.00 41.81           O  
ANISOU 1476  O   GLY A 241     3770   6196   5918  -1477    892   -460       O  
ATOM   1477  N   ALA A 242      13.637  -6.168   0.620  1.00 39.22           N  
ANISOU 1477  N   ALA A 242     3741   5422   5739  -1269    873   -422       N  
ATOM   1478  CA  ALA A 242      12.472  -5.271   0.754  1.00 40.48           C  
ANISOU 1478  CA  ALA A 242     3994   5411   5973  -1443    914   -332       C  
ATOM   1479  C   ALA A 242      12.642  -3.877   0.155  1.00 42.06           C  
ANISOU 1479  C   ALA A 242     4108   5760   6112  -1497    964   -234       C  
ATOM   1480  O   ALA A 242      13.671  -3.244   0.326  1.00 42.17           O  
ANISOU 1480  O   ALA A 242     4069   5894   6059  -1326    969   -205       O  
ATOM   1481  CB  ALA A 242      12.099  -5.125   2.197  1.00 39.11           C  
ANISOU 1481  CB  ALA A 242     4014   4955   5891  -1345    912   -289       C  
ATOM   1482  N   LYS A 243      11.616  -3.399  -0.533  1.00 44.56           N  
ANISOU 1482  N   LYS A 243     4422   6062   6445  -1739   1001   -183       N  
ATOM   1483  CA  LYS A 243      11.662  -2.085  -1.194  1.00 47.32           C  
ANISOU 1483  CA  LYS A 243     4679   6574   6727  -1823   1057    -79       C  
ATOM   1484  C   LYS A 243      10.803  -0.994  -0.499  1.00 47.21           C  
ANISOU 1484  C   LYS A 243     4836   6320   6782  -1872   1103     52       C  
ATOM   1485  O   LYS A 243      10.584   0.128  -1.006  1.00 46.55           O  
ANISOU 1485  O   LYS A 243     4707   6329   6652  -1974   1157    156       O  
ATOM   1486  CB  LYS A 243      11.277  -2.240  -2.667  1.00 50.59           C  
ANISOU 1486  CB  LYS A 243     4927   7226   7070  -2080   1075   -105       C  
ATOM   1487  CG  LYS A 243      12.254  -3.106  -3.447  1.00 51.42           C  
ANISOU 1487  CG  LYS A 243     4822   7648   7066  -1993   1034   -225       C  
ATOM   1488  CD  LYS A 243      12.159  -2.908  -4.945  1.00 54.42           C  
ANISOU 1488  CD  LYS A 243     4973   8378   7326  -2209   1060   -237       C  
ATOM   1489  CE  LYS A 243      13.158  -3.803  -5.659  1.00 56.42           C  
ANISOU 1489  CE  LYS A 243     5018   8969   7451  -2075   1014   -365       C  
ATOM   1490  NZ  LYS A 243      13.106  -3.665  -7.149  1.00 60.15           N1+
ANISOU 1490  NZ  LYS A 243     5227   9847   7779  -2279   1037   -391       N1+
ATOM   1491  N   VAL A 244      10.360  -1.325   0.698  1.00 46.39           N  
ANISOU 1491  N   VAL A 244     4923   5927   6774  -1777   1081     47       N  
ATOM   1492  CA  VAL A 244       9.658  -0.374   1.519  1.00 46.98           C  
ANISOU 1492  CA  VAL A 244     5164   5787   6898  -1757   1116    160       C  
ATOM   1493  C   VAL A 244       9.723  -0.898   2.953  1.00 44.99           C  
ANISOU 1493  C   VAL A 244     5050   5332   6711  -1557   1076    119       C  
ATOM   1494  O   VAL A 244       9.949  -2.082   3.148  1.00 45.33           O  
ANISOU 1494  O   VAL A 244     5089   5354   6778  -1509   1028     13       O  
ATOM   1495  CB  VAL A 244       8.214  -0.220   1.019  1.00 48.99           C  
ANISOU 1495  CB  VAL A 244     5545   5873   7196  -2014   1150    219       C  
ATOM   1496  CG1 VAL A 244       7.474  -1.540   1.117  1.00 48.93           C  
ANISOU 1496  CG1 VAL A 244     5649   5681   7261  -2093   1104    114       C  
ATOM   1497  CG2 VAL A 244       7.504   0.874   1.803  1.00 50.60           C  
ANISOU 1497  CG2 VAL A 244     5928   5873   7426  -1967   1191    350       C  
ATOM   1498  N   ILE A 245       9.568  -0.038   3.951  1.00 44.14           N  
ANISOU 1498  N   ILE A 245     5048   5106   6618  -1438   1095    199       N  
ATOM   1499  CA  ILE A 245       9.559  -0.519   5.321  1.00 43.97           C  
ANISOU 1499  CA  ILE A 245     5139   4925   6642  -1267   1060    160       C  
ATOM   1500  C   ILE A 245       8.228  -0.242   5.972  1.00 45.80           C  
ANISOU 1500  C   ILE A 245     5568   4910   6922  -1283   1075    222       C  
ATOM   1501  O   ILE A 245       7.694   0.865   5.849  1.00 46.13           O  
ANISOU 1501  O   ILE A 245     5667   4914   6946  -1328   1122    333       O  
ATOM   1502  CB  ILE A 245      10.681   0.115   6.149  1.00 42.73           C  
ANISOU 1502  CB  ILE A 245     4929   4867   6440  -1072   1056    173       C  
ATOM   1503  CG1 ILE A 245      12.062  -0.315   5.624  1.00 43.00           C  
ANISOU 1503  CG1 ILE A 245     4812   5110   6417  -1012   1030     98       C  
ATOM   1504  CG2 ILE A 245      10.551  -0.292   7.602  1.00 41.97           C  
ANISOU 1504  CG2 ILE A 245     4941   4627   6379   -929   1027    143       C  
ATOM   1505  CD1 ILE A 245      12.381  -1.801   5.741  1.00 42.94           C  
ANISOU 1505  CD1 ILE A 245     4801   5083   6432   -981    982    -14       C  
ATOM   1506  N   VAL A 247       6.019  -0.050   9.528  1.00 48.00           N  
ANISOU 1506  N   VAL A 247     6314   4683   7240   -882   1048    280       N  
ATOM   1507  CA  VAL A 247       5.964   0.046  10.996  1.00 46.78           C  
ANISOU 1507  CA  VAL A 247     6207   4514   7055   -668   1030    273       C  
ATOM   1508  C   VAL A 247       4.541   0.090  11.505  1.00 48.38           C  
ANISOU 1508  C   VAL A 247     6626   4504   7251   -595   1030    310       C  
ATOM   1509  O   VAL A 247       3.681   0.684  10.870  1.00 51.67           O  
ANISOU 1509  O   VAL A 247     7175   4786   7671   -687   1065    394       O  
ATOM   1510  CB  VAL A 247       6.583   1.337  11.556  1.00 44.80           C  
ANISOU 1510  CB  VAL A 247     5881   4398   6744   -562   1060    349       C  
ATOM   1511  CG1 VAL A 247       8.073   1.199  11.608  1.00 44.50           C  
ANISOU 1511  CG1 VAL A 247     5662   4555   6690   -548   1043    289       C  
ATOM   1512  CG2 VAL A 247       6.156   2.562  10.769  1.00 44.84           C  
ANISOU 1512  CG2 VAL A 247     5924   4385   6727   -648   1115    473       C  
ATOM   1513  N   MET A 248       4.318  -0.489  12.677  1.00 46.75           N  
ANISOU 1513  N   MET A 248     6461   4279   7020   -421    993    251       N  
ATOM   1514  CA  MET A 248       3.080  -0.323  13.383  1.00 47.37           C  
ANISOU 1514  CA  MET A 248     6740   4197   7060   -277    990    283       C  
ATOM   1515  C   MET A 248       3.310   0.828  14.345  1.00 46.56           C  
ANISOU 1515  C   MET A 248     6594   4220   6877   -105   1013    356       C  
ATOM   1516  O   MET A 248       3.994   0.653  15.358  1.00 44.35           O  
ANISOU 1516  O   MET A 248     6188   4108   6555     17    990    302       O  
ATOM   1517  CB  MET A 248       2.749  -1.585  14.155  1.00 48.75           C  
ANISOU 1517  CB  MET A 248     6956   4337   7230   -158    934    172       C  
ATOM   1518  CG  MET A 248       2.854  -2.872  13.352  1.00 50.40           C  
ANISOU 1518  CG  MET A 248     7144   4495   7510   -309    901     70       C  
ATOM   1519  SD  MET A 248       1.817  -2.882  11.886  1.00 54.92           S  
ANISOU 1519  SD  MET A 248     7901   4823   8143   -539    917     99       S  
ATOM   1520  CE  MET A 248       1.790  -4.618  11.447  1.00 55.86           C  
ANISOU 1520  CE  MET A 248     8001   4909   8314   -626    856    -60       C  
ATOM   1521  N   ALA A 249       2.771   2.007  14.015  1.00 46.72           N  
ANISOU 1521  N   ALA A 249     6712   4171   6868   -111   1060    478       N  
ATOM   1522  CA  ALA A 249       3.014   3.227  14.795  1.00 46.44           C  
ANISOU 1522  CA  ALA A 249     6624   4275   6747     44   1086    552       C  
ATOM   1523  C   ALA A 249       1.838   3.575  15.687  1.00 48.03           C  
ANISOU 1523  C   ALA A 249     7013   4373   6863    267   1085    599       C  
ATOM   1524  O   ALA A 249       1.824   4.635  16.332  1.00 49.48           O  
ANISOU 1524  O   ALA A 249     7179   4664   6958    417   1108    668       O  
ATOM   1525  CB  ALA A 249       3.359   4.390  13.881  1.00 46.50           C  
ANISOU 1525  CB  ALA A 249     6583   4330   6755    -82   1141    661       C  
ATOM   1526  N   SER A 250       0.874   2.660  15.750  1.00 49.64           N  
ANISOU 1526  N   SER A 250     7396   4383   7080    309   1054    552       N  
ATOM   1527  CA  SER A 250      -0.314   2.806  16.609  1.00 51.76           C  
ANISOU 1527  CA  SER A 250     7874   4538   7252    559   1042    578       C  
ATOM   1528  C   SER A 250      -1.010   1.459  16.812  1.00 51.98           C  
ANISOU 1528  C   SER A 250     8033   4420   7298    615    987    470       C  
ATOM   1529  O   SER A 250      -0.722   0.491  16.121  1.00 48.74           O  
ANISOU 1529  O   SER A 250     7581   3955   6983    431    965    391       O  
ATOM   1530  CB  SER A 250      -1.276   3.851  16.011  1.00 53.99           C  
ANISOU 1530  CB  SER A 250     8394   4614   7508    548   1094    727       C  
ATOM   1531  OG  SER A 250      -2.621   3.411  15.957  1.00 55.04           O  
ANISOU 1531  OG  SER A 250     8838   4455   7621    625   1077    734       O  
ATOM   1532  N   GLY A 251      -1.878   1.390  17.815  1.00 56.28           N  
ANISOU 1532  N   GLY A 251     8716   4932   7734    893    961    458       N  
ATOM   1533  CA  GLY A 251      -2.609   0.162  18.095  1.00 60.93           C  
ANISOU 1533  CA  GLY A 251     9442   5393   8315    992    905    352       C  
ATOM   1534  C   GLY A 251      -3.495  -0.222  16.921  1.00 67.79           C  
ANISOU 1534  C   GLY A 251    10580   5911   9267    815    906    364       C  
ATOM   1535  O   GLY A 251      -3.880   0.642  16.150  1.00 70.76           O  
ANISOU 1535  O   GLY A 251    11101   6123   9663    694    954    480       O  
ATOM   1536  N   GLY A 252      -3.827  -1.507  16.773  1.00 73.51           N  
ANISOU 1536  N   GLY A 252    11374   6526  10031    788    853    243       N  
ATOM   1537  CA  GLY A 252      -4.739  -1.944  15.706  1.00 77.45           C  
ANISOU 1537  CA  GLY A 252    12145   6684  10598    613    844    233       C  
ATOM   1538  C   GLY A 252      -5.929  -2.822  16.086  1.00 82.18           C  
ANISOU 1538  C   GLY A 252    13024   7058  11141    800    783    144       C  
ATOM   1539  O   GLY A 252      -6.106  -3.226  17.251  1.00 81.05           O  
ANISOU 1539  O   GLY A 252    12857   7045  10895   1103    742     78       O  
ATOM   1540  N   VAL A 253      -6.788  -3.063  15.095  1.00 85.62           N  
ANISOU 1540  N   VAL A 253    13740   7157  11633    619    779    144       N  
ATOM   1541  CA  VAL A 253      -8.041  -3.766  15.331  1.00 88.15           C  
ANISOU 1541  CA  VAL A 253    14398   7199  11897    788    721     66       C  
ATOM   1542  C   VAL A 253      -7.831  -5.279  15.227  1.00 88.38           C  
ANISOU 1542  C   VAL A 253    14327   7275  11978    732    653   -115       C  
ATOM   1543  O   VAL A 253      -8.415  -6.034  16.007  1.00 85.00           O  
ANISOU 1543  O   VAL A 253    14010   6821  11465   1000    591   -216       O  
ATOM   1544  CB  VAL A 253      -9.156  -3.289  14.369  1.00 89.36           C  
ANISOU 1544  CB  VAL A 253    14952   6931  12071    620    746    151       C  
ATOM   1545  CG1 VAL A 253     -10.374  -4.197  14.460  1.00 93.36           C  
ANISOU 1545  CG1 VAL A 253    15820   7119  12532    749    675     40       C  
ATOM   1546  CG2 VAL A 253      -9.564  -1.850  14.681  1.00 90.50           C  
ANISOU 1546  CG2 VAL A 253    15250   7010  12125    765    806    333       C  
ATOM   1547  N   MET A 254      -7.015  -5.722  14.267  1.00 91.10           N  
ANISOU 1547  N   MET A 254    14463   7705  12446    403    663   -157       N  
ATOM   1548  CA  MET A 254      -6.734  -7.183  14.074  1.00 95.99           C  
ANISOU 1548  CA  MET A 254    14967   8391  13113    333    600   -328       C  
ATOM   1549  C   MET A 254      -5.974  -7.879  15.239  1.00 90.42           C  
ANISOU 1549  C   MET A 254    13988   8018  12349    575    567   -412       C  
ATOM   1550  O   MET A 254      -6.111  -9.091  15.441  1.00 85.51           O  
ANISOU 1550  O   MET A 254    13355   7419  11715    646    506   -551       O  
ATOM   1551  CB  MET A 254      -5.908  -7.439  12.795  1.00101.11           C  
ANISOU 1551  CB  MET A 254    15415   9113  13887    -53    623   -348       C  
ATOM   1552  CG  MET A 254      -6.603  -8.096  11.606  1.00106.68           C  
ANISOU 1552  CG  MET A 254    16315   9557  14660   -325    595   -429       C  
ATOM   1553  SD  MET A 254      -8.269  -7.562  11.185  1.00113.80           S  
ANISOU 1553  SD  MET A 254    17733   9974  15532   -370    597   -370       S  
ATOM   1554  CE  MET A 254      -8.227  -7.927   9.427  1.00111.44           C  
ANISOU 1554  CE  MET A 254    17423   9573  15347   -884    607   -417       C  
ATOM   1555  N   SER A 255      -5.134  -7.124  15.953  1.00 86.63           N  
ANISOU 1555  N   SER A 255    12395  10552   9966   1054   2189  -1873       N  
ATOM   1556  CA  SER A 255      -4.410  -7.656  17.109  1.00 82.44           C  
ANISOU 1556  CA  SER A 255    11620  10335   9369   1131   2418  -1742       C  
ATOM   1557  C   SER A 255      -5.361  -7.631  18.306  1.00 84.95           C  
ANISOU 1557  C   SER A 255    11802  10633   9838   1447   2627  -1799       C  
ATOM   1558  O   SER A 255      -6.213  -6.738  18.430  1.00 82.65           O  
ANISOU 1558  O   SER A 255    11497  10098   9807   1554   2537  -1822       O  
ATOM   1559  CB  SER A 255      -3.153  -6.847  17.392  1.00 76.86           C  
ANISOU 1559  CB  SER A 255    10652   9748   8803    944   2316  -1447       C  
ATOM   1560  OG  SER A 255      -3.443  -5.470  17.377  1.00 72.28           O  
ANISOU 1560  OG  SER A 255    10004   8965   8496    927   2149  -1363       O  
ATOM   1561  N   ARG A 256      -5.224  -8.615  19.186  1.00 86.39           N  
ANISOU 1561  N   ARG A 256    11875  11083   9866   1603   2911  -1806       N  
ATOM   1562  CA  ARG A 256      -6.277  -8.888  20.190  1.00 89.47           C  
ANISOU 1562  CA  ARG A 256    12182  11465  10348   1956   3165  -1931       C  
ATOM   1563  C   ARG A 256      -6.401  -7.859  21.379  1.00 91.53           C  
ANISOU 1563  C   ARG A 256    12064  11701  11009   2081   3192  -1701       C  
ATOM   1564  O   ARG A 256      -7.528  -7.456  21.753  1.00 91.86           O  
ANISOU 1564  O   ARG A 256    12096  11530  11278   2322   3219  -1811       O  
ATOM   1565  CB  ARG A 256      -6.199 -10.383  20.659  1.00 87.89           C  
ANISOU 1565  CB  ARG A 256    12019  11580   9796   2108   3500  -2042       C  
ATOM   1566  CG  ARG A 256      -6.133 -10.609  22.149  1.00 87.22           C  
ANISOU 1566  CG  ARG A 256    11560  11762   9814   2333   3825  -1876       C  
ATOM   1567  CD  ARG A 256      -6.897 -11.865  22.510  1.00 89.77           C  
ANISOU 1567  CD  ARG A 256    12024  12238   9848   2644   4177  -2146       C  
ATOM   1568  NE  ARG A 256      -6.250 -12.750  23.467  1.00 90.97           N  
ANISOU 1568  NE  ARG A 256    11923  12833   9809   2711   4519  -1964       N  
ATOM   1569  CZ  ARG A 256      -5.531 -12.393  24.529  1.00 89.66           C  
ANISOU 1569  CZ  ARG A 256    11305  12889   9874   2675   4618  -1591       C  
ATOM   1570  NH1 ARG A 256      -5.310 -11.123  24.841  1.00 86.66           N1+
ANISOU 1570  NH1 ARG A 256    10672  12333   9923   2574   4390  -1361       N1+
ATOM   1571  NH2 ARG A 256      -5.016 -13.343  25.297  1.00 92.35           N  
ANISOU 1571  NH2 ARG A 256    11447  13643   9999   2730   4943  -1431       N  
ATOM   1572  N   ASP A 257      -5.265  -7.428  21.941  1.00 89.98           N  
ANISOU 1572  N   ASP A 257    11574  11698  10918   1912   3151  -1383       N  
ATOM   1573  CA  ASP A 257      -5.252  -6.684  23.232  1.00 89.43           C  
ANISOU 1573  CA  ASP A 257    11114  11669  11197   2023   3194  -1134       C  
ATOM   1574  C   ASP A 257      -5.102  -5.183  23.071  1.00 84.54           C  
ANISOU 1574  C   ASP A 257    10434  10822  10864   1865   2864   -975       C  
ATOM   1575  O   ASP A 257      -5.535  -4.445  23.942  1.00 83.66           O  
ANISOU 1575  O   ASP A 257    10093  10630  11066   1993   2839   -844       O  
ATOM   1576  CB  ASP A 257      -4.099  -7.117  24.174  1.00 90.08           C  
ANISOU 1576  CB  ASP A 257    10862  12103  11263   1940   3337   -839       C  
ATOM   1577  CG  ASP A 257      -4.479  -8.205  25.155  1.00 92.99           C  
ANISOU 1577  CG  ASP A 257    11053  12736  11540   2213   3739   -855       C  
ATOM   1578  OD1 ASP A 257      -5.287  -9.090  24.772  1.00 94.47           O  
ANISOU 1578  OD1 ASP A 257    11499  12919  11477   2406   3934  -1162       O  
ATOM   1579  OD2 ASP A 257      -3.919  -8.184  26.291  1.00 89.78           O1-
ANISOU 1579  OD2 ASP A 257    10250  12552  11310   2224   3852   -551       O1-
ATOM   1580  N   ASP A 258      -4.461  -4.739  21.987  1.00 81.03           N  
ANISOU 1580  N   ASP A 258    10183  10294  10310   1593   2620   -974       N  
ATOM   1581  CA  ASP A 258      -3.966  -3.352  21.896  1.00 77.41           C  
ANISOU 1581  CA  ASP A 258     9648   9711  10054   1411   2330   -784       C  
ATOM   1582  C   ASP A 258      -4.972  -2.314  21.361  1.00 73.92           C  
ANISOU 1582  C   ASP A 258     9364   8954   9769   1443   2136   -864       C  
ATOM   1583  O   ASP A 258      -5.892  -2.643  20.593  1.00 73.40           O  
ANISOU 1583  O   ASP A 258     9551   8718   9620   1520   2150  -1089       O  
ATOM   1584  CB  ASP A 258      -2.613  -3.299  21.148  1.00 74.23           C  
ANISOU 1584  CB  ASP A 258     9312   9409   9484   1117   2180   -700       C  
ATOM   1585  CG  ASP A 258      -2.674  -3.822  19.695  1.00 73.54           C  
ANISOU 1585  CG  ASP A 258     9555   9252   9135   1004   2137   -910       C  
ATOM   1586  OD1 ASP A 258      -3.684  -4.408  19.269  1.00 78.32           O  
ANISOU 1586  OD1 ASP A 258    10360   9754   9644   1136   2228  -1131       O  
ATOM   1587  OD2 ASP A 258      -1.669  -3.667  18.962  1.00 70.38           O1-
ANISOU 1587  OD2 ASP A 258     9213   8892   8637    780   1998   -851       O1-
ATOM   1588  N   ASN A 259      -4.810  -1.072  21.826  1.00 72.12           N  
ANISOU 1588  N   ASN A 259     8985   8645   9773   1382   1941   -663       N  
ATOM   1589  CA  ASN A 259      -5.814  -0.007  21.627  1.00 72.23           C  
ANISOU 1589  CA  ASN A 259     9082   8383   9978   1432   1761   -665       C  
ATOM   1590  C   ASN A 259      -5.373   0.964  20.524  1.00 69.25           C  
ANISOU 1590  C   ASN A 259     8896   7910   9504   1181   1510   -627       C  
ATOM   1591  O   ASN A 259      -4.278   1.530  20.580  1.00 67.03           O  
ANISOU 1591  O   ASN A 259     8542   7740   9187   1006   1389   -480       O  
ATOM   1592  CB  ASN A 259      -6.100   0.743  22.946  1.00 71.81           C  
ANISOU 1592  CB  ASN A 259     8732   8300  10250   1555   1706   -453       C  
ATOM   1593  CG  ASN A 259      -7.070   1.912  22.787  1.00 69.24           C  
ANISOU 1593  CG  ASN A 259     8483   7695  10129   1583   1484   -407       C  
ATOM   1594  ND2 ASN A 259      -7.541   2.426  23.906  1.00 70.28           N  
ANISOU 1594  ND2 ASN A 259     8368   7769  10568   1726   1439   -245       N  
ATOM   1595  OD1 ASN A 259      -7.371   2.360  21.685  1.00 66.47           O  
ANISOU 1595  OD1 ASN A 259     8389   7190   9674   1466   1344   -486       O  
ATOM   1596  N   PRO A 260      -6.234   1.144  19.509  1.00 68.00           N  
ANISOU 1596  N   PRO A 260     8984   7543   9310   1170   1433   -759       N  
ATOM   1597  CA  PRO A 260      -5.865   1.998  18.391  1.00 63.06           C  
ANISOU 1597  CA  PRO A 260     8525   6856   8580    942   1238   -711       C  
ATOM   1598  C   PRO A 260      -5.705   3.491  18.671  1.00 59.17           C  
ANISOU 1598  C   PRO A 260     7962   6313   8208    852   1023   -500       C  
ATOM   1599  O   PRO A 260      -5.099   4.191  17.877  1.00 56.86           O  
ANISOU 1599  O   PRO A 260     7772   6048   7785    666    902   -446       O  
ATOM   1600  CB  PRO A 260      -7.004   1.746  17.394  1.00 65.96           C  
ANISOU 1600  CB  PRO A 260     9133   6996   8932    972   1211   -874       C  
ATOM   1601  CG  PRO A 260      -7.478   0.354  17.706  1.00 67.93           C  
ANISOU 1601  CG  PRO A 260     9411   7264   9134   1165   1424  -1084       C  
ATOM   1602  CD  PRO A 260      -7.417   0.306  19.192  1.00 69.68           C  
ANISOU 1602  CD  PRO A 260     9357   7600   9519   1349   1549   -988       C  
ATOM   1603  N   ASN A 261      -6.246   3.996  19.760  1.00 58.79           N  
ANISOU 1603  N   ASN A 261     7746   6193   8396    985    973   -379       N  
ATOM   1604  CA  ASN A 261      -6.017   5.396  20.082  1.00 58.20           C  
ANISOU 1604  CA  ASN A 261     7619   6090   8404    884    741   -168       C  
ATOM   1605  C   ASN A 261      -4.578   5.786  20.367  1.00 55.86           C  
ANISOU 1605  C   ASN A 261     7238   5984   8000    730    663    -65       C  
ATOM   1606  O   ASN A 261      -4.177   6.922  20.095  1.00 53.38           O  
ANISOU 1606  O   ASN A 261     7003   5663   7614    589    470     38       O  
ATOM   1607  CB  ASN A 261      -6.827   5.779  21.296  1.00 62.54           C  
ANISOU 1607  CB  ASN A 261     7972   6529   9261   1057    682    -39       C  
ATOM   1608  CG  ASN A 261      -8.279   5.915  20.975  1.00 65.78           C  
ANISOU 1608  CG  ASN A 261     8491   6680   9823   1180    644    -90       C  
ATOM   1609  ND2 ASN A 261      -9.126   5.292  21.782  1.00 69.01           N  
ANISOU 1609  ND2 ASN A 261     8758   6999  10465   1433    770   -145       N  
ATOM   1610  OD1 ASN A 261      -8.644   6.585  20.001  1.00 67.42           O  
ANISOU 1610  OD1 ASN A 261     8901   6763   9950   1054    503    -71       O  
ATOM   1611  N   PHE A 262      -3.815   4.850  20.928  1.00 55.62           N  
ANISOU 1611  N   PHE A 262     7057   6122   7955    759    808    -89       N  
ATOM   1612  CA  PHE A 262      -2.477   5.140  21.454  1.00 53.92           C  
ANISOU 1612  CA  PHE A 262     6717   6055   7715    632    709     32       C  
ATOM   1613  C   PHE A 262      -1.374   4.912  20.427  1.00 51.77           C  
ANISOU 1613  C   PHE A 262     6595   5883   7191    465    719    -65       C  
ATOM   1614  O   PHE A 262      -1.512   4.073  19.534  1.00 50.65           O  
ANISOU 1614  O   PHE A 262     6579   5759   6906    463    868   -216       O  
ATOM   1615  CB  PHE A 262      -2.186   4.266  22.676  1.00 55.06           C  
ANISOU 1615  CB  PHE A 262     6575   6330   8014    736    843    114       C  
ATOM   1616  CG  PHE A 262      -3.238   4.340  23.771  1.00 57.15           C  
ANISOU 1616  CG  PHE A 262     6632   6514   8567    937    876    214       C  
ATOM   1617  CD1 PHE A 262      -4.026   5.485  23.962  1.00 57.45           C  
ANISOU 1617  CD1 PHE A 262     6692   6370   8764    963    671    312       C  
ATOM   1618  CD2 PHE A 262      -3.421   3.263  24.637  1.00 58.20           C  
ANISOU 1618  CD2 PHE A 262     6531   6766   8818   1106   1117    229       C  
ATOM   1619  CE1 PHE A 262      -4.982   5.540  24.970  1.00 59.01           C  
ANISOU 1619  CE1 PHE A 262     6676   6478   9267   1159    688    417       C  
ATOM   1620  CE2 PHE A 262      -4.376   3.318  25.644  1.00 60.52           C  
ANISOU 1620  CE2 PHE A 262     6602   6989   9402   1318   1169    320       C  
ATOM   1621  CZ  PHE A 262      -5.154   4.457  25.810  1.00 61.09           C  
ANISOU 1621  CZ  PHE A 262     6691   6853   9668   1346    945    414       C  
ATOM   1622  N   ALA A 263      -0.276   5.657  20.579  1.00 50.99           N  
ANISOU 1622  N   ALA A 263     6482   5836   7054    331    542     22       N  
ATOM   1623  CA  ALA A 263       0.879   5.527  19.687  1.00 49.50           C  
ANISOU 1623  CA  ALA A 263     6412   5729   6667    191    534    -62       C  
ATOM   1624  C   ALA A 263       1.668   4.286  20.048  1.00 49.45           C  
ANISOU 1624  C   ALA A 263     6260   5857   6669    182    661    -65       C  
ATOM   1625  O   ALA A 263       1.422   3.671  21.092  1.00 49.66           O  
ANISOU 1625  O   ALA A 263     6082   5940   6847    275    748     23       O  
ATOM   1626  CB  ALA A 263       1.778   6.754  19.768  1.00 49.32           C  
ANISOU 1626  CB  ALA A 263     6443   5695   6600     78    295      2       C  
ATOM   1627  N   GLN A 264       2.591   3.910  19.160  1.00 48.59           N  
ANISOU 1627  N   GLN A 264     6249   5809   6404     74    679   -149       N  
ATOM   1628  CA  GLN A 264       3.492   2.774  19.392  1.00 48.06           C  
ANISOU 1628  CA  GLN A 264     6062   5871   6327     28    763   -124       C  
ATOM   1629  C   GLN A 264       4.842   3.091  18.838  1.00 45.33           C  
ANISOU 1629  C   GLN A 264     5777   5533   5913   -110    623   -139       C  
ATOM   1630  O   GLN A 264       4.962   3.898  17.914  1.00 45.62           O  
ANISOU 1630  O   GLN A 264     5985   5504   5843   -151    548   -227       O  
ATOM   1631  CB  GLN A 264       2.987   1.480  18.766  1.00 47.85           C  
ANISOU 1631  CB  GLN A 264     6100   5907   6175     74    985   -239       C  
ATOM   1632  CG  GLN A 264       1.730   0.970  19.418  1.00 50.32           C  
ANISOU 1632  CG  GLN A 264     6347   6217   6556    245   1150   -253       C  
ATOM   1633  CD  GLN A 264       1.293  -0.378  18.894  1.00 52.31           C  
ANISOU 1633  CD  GLN A 264     6687   6536   6651    297   1358   -390       C  
ATOM   1634  NE2 GLN A 264       0.226  -0.898  19.488  1.00 55.14           N  
ANISOU 1634  NE2 GLN A 264     7000   6893   7056    478   1522   -436       N  
ATOM   1635  OE1 GLN A 264       1.874  -0.941  17.964  1.00 50.59           O  
ANISOU 1635  OE1 GLN A 264     6586   6363   6272    185   1363   -459       O  
ATOM   1636  N   PHE A 265       5.847   2.436  19.412  1.00 43.29           N  
ANISOU 1636  N   PHE A 265     5367   5356   5723   -174    594    -42       N  
ATOM   1637  CA  PHE A 265       7.235   2.855  19.280  1.00 41.48           C  
ANISOU 1637  CA  PHE A 265     5148   5096   5516   -292    398    -22       C  
ATOM   1638  C   PHE A 265       7.464   4.243  19.881  1.00 40.48           C  
ANISOU 1638  C   PHE A 265     5039   4863   5479   -304    155     22       C  
ATOM   1639  O   PHE A 265       6.533   5.028  20.071  1.00 39.75           O  
ANISOU 1639  O   PHE A 265     4998   4718   5387   -236    135     20       O  
ATOM   1640  CB  PHE A 265       7.682   2.832  17.820  1.00 40.61           C  
ANISOU 1640  CB  PHE A 265     5223   4965   5242   -342    422   -177       C  
ATOM   1641  CG  PHE A 265       8.036   1.471  17.319  1.00 40.45           C  
ANISOU 1641  CG  PHE A 265     5170   5037   5162   -390    550   -181       C  
ATOM   1642  CD1 PHE A 265       9.058   0.769  17.910  1.00 42.22           C  
ANISOU 1642  CD1 PHE A 265     5242   5320   5481   -469    487    -52       C  
ATOM   1643  CD2 PHE A 265       7.380   0.906  16.246  1.00 40.23           C  
ANISOU 1643  CD2 PHE A 265     5268   5030   4987   -374    701   -295       C  
ATOM   1644  CE1 PHE A 265       9.401  -0.498  17.469  1.00 42.97           C  
ANISOU 1644  CE1 PHE A 265     5312   5512   5500   -528    587    -28       C  
ATOM   1645  CE2 PHE A 265       7.722  -0.355  15.792  1.00 40.58           C  
ANISOU 1645  CE2 PHE A 265     5300   5161   4959   -433    785   -291       C  
ATOM   1646  CZ  PHE A 265       8.730  -1.065  16.409  1.00 41.11           C  
ANISOU 1646  CZ  PHE A 265     5219   5306   5096   -508    735   -156       C  
ATOM   1647  N   SER A 266       8.710   4.525  20.214  1.00 39.40           N  
ANISOU 1647  N   SER A 266     4866   4681   5424   -396    -55     68       N  
ATOM   1648  CA  SER A 266       9.068   5.856  20.680  1.00 39.77           C  
ANISOU 1648  CA  SER A 266     4983   4613   5517   -420   -325     75       C  
ATOM   1649  C   SER A 266       9.308   6.732  19.463  1.00 38.36           C  
ANISOU 1649  C   SER A 266     5071   4382   5124   -409   -350   -127       C  
ATOM   1650  O   SER A 266       9.639   6.214  18.418  1.00 37.94           O  
ANISOU 1650  O   SER A 266     5084   4363   4967   -414   -217   -234       O  
ATOM   1651  CB  SER A 266      10.343   5.770  21.499  1.00 40.59           C  
ANISOU 1651  CB  SER A 266     4959   4660   5805   -525   -568    190       C  
ATOM   1652  OG  SER A 266      11.350   5.073  20.785  1.00 39.98           O  
ANISOU 1652  OG  SER A 266     4906   4590   5695   -583   -542    126       O  
ATOM   1653  N   PRO A 267       9.195   8.054  19.597  1.00 38.09           N  
ANISOU 1653  N   PRO A 267     5179   4275   5018   -396   -521   -166       N  
ATOM   1654  CA  PRO A 267       9.669   8.944  18.563  1.00 38.52           C  
ANISOU 1654  CA  PRO A 267     5474   4303   4860   -382   -553   -347       C  
ATOM   1655  C   PRO A 267      11.117   8.653  18.210  1.00 39.99           C  
ANISOU 1655  C   PRO A 267     5678   4441   5077   -421   -640   -442       C  
ATOM   1656  O   PRO A 267      11.497   8.687  17.027  1.00 38.59           O  
ANISOU 1656  O   PRO A 267     5617   4285   4761   -388   -523   -592       O  
ATOM   1657  CB  PRO A 267       9.577  10.307  19.228  1.00 39.79           C  
ANISOU 1657  CB  PRO A 267     5753   4392   4975   -385   -801   -328       C  
ATOM   1658  CG  PRO A 267       8.476  10.185  20.180  1.00 39.82           C  
ANISOU 1658  CG  PRO A 267     5601   4403   5125   -373   -805   -145       C  
ATOM   1659  CD  PRO A 267       8.582   8.792  20.700  1.00 39.91           C  
ANISOU 1659  CD  PRO A 267     5355   4459   5351   -388   -689    -33       C  
ATOM   1660  N   GLU A 268      11.903   8.385  19.256  1.00 43.51           N  
ANISOU 1660  N   GLU A 268     5990   4810   5733   -491   -857   -335       N  
ATOM   1661  CA  GLU A 268      13.292   7.957  19.148  1.00 46.14           C  
ANISOU 1661  CA  GLU A 268     6296   5061   6173   -546   -987   -376       C  
ATOM   1662  C   GLU A 268      13.437   6.736  18.219  1.00 43.95           C  
ANISOU 1662  C   GLU A 268     5944   4870   5887   -548   -747   -392       C  
ATOM   1663  O   GLU A 268      14.190   6.785  17.242  1.00 45.71           O  
ANISOU 1663  O   GLU A 268     6269   5053   6045   -523   -730   -541       O  
ATOM   1664  CB  GLU A 268      13.850   7.641  20.533  1.00 51.30           C  
ANISOU 1664  CB  GLU A 268     6753   5636   7103   -649  -1239   -175       C  
ATOM   1665  CG  GLU A 268      13.815   8.835  21.512  1.00 59.32           C  
ANISOU 1665  CG  GLU A 268     7835   6539   8164   -673  -1547   -139       C  
ATOM   1666  CD  GLU A 268      12.640   8.883  22.563  1.00 65.47           C  
ANISOU 1666  CD  GLU A 268     8439   7385   9050   -675  -1532     78       C  
ATOM   1667  OE1 GLU A 268      12.619   8.033  23.490  1.00 69.39           O  
ANISOU 1667  OE1 GLU A 268     8652   7922   9793   -738  -1534    311       O  
ATOM   1668  OE2 GLU A 268      11.743   9.795  22.525  1.00 64.98           O1-
ANISOU 1668  OE2 GLU A 268     8506   7337   8847   -617  -1530     39       O1-
ATOM   1669  N   GLU A 269      12.685   5.669  18.473  1.00 41.41           N  
ANISOU 1669  N   GLU A 269     5453   4666   5614   -566   -558   -250       N  
ATOM   1670  CA  GLU A 269      12.774   4.476  17.645  1.00 38.89           C  
ANISOU 1670  CA  GLU A 269     5083   4433   5261   -585   -360   -254       C  
ATOM   1671  C   GLU A 269      12.376   4.728  16.195  1.00 38.03           C  
ANISOU 1671  C   GLU A 269     5142   4354   4955   -520   -185   -429       C  
ATOM   1672  O   GLU A 269      13.047   4.269  15.270  1.00 36.35           O  
ANISOU 1672  O   GLU A 269     4946   4135   4730   -537   -148   -494       O  
ATOM   1673  CB  GLU A 269      11.939   3.374  18.230  1.00 38.14           C  
ANISOU 1673  CB  GLU A 269     4818   4470   5205   -596   -185    -97       C  
ATOM   1674  CG  GLU A 269      12.636   2.724  19.387  1.00 39.66           C  
ANISOU 1674  CG  GLU A 269     4791   4674   5605   -686   -311    117       C  
ATOM   1675  CD  GLU A 269      11.675   1.974  20.289  1.00 41.54           C  
ANISOU 1675  CD  GLU A 269     4843   5054   5884   -658   -137    284       C  
ATOM   1676  OE1 GLU A 269      10.817   2.644  20.928  1.00 41.05           O  
ANISOU 1676  OE1 GLU A 269     4760   4981   5855   -587   -139    307       O  
ATOM   1677  OE2 GLU A 269      11.777   0.710  20.328  1.00 40.08           O1-
ANISOU 1677  OE2 GLU A 269     4538   5001   5689   -698      7    390       O1-
ATOM   1678  N   LEU A 270      11.289   5.464  15.995  1.00 39.63           N  
ANISOU 1678  N   LEU A 270     5447   4584   5024   -455    -92   -480       N  
ATOM   1679  CA  LEU A 270      10.792   5.761  14.630  1.00 40.90           C  
ANISOU 1679  CA  LEU A 270     5745   4782   5012   -410     74   -602       C  
ATOM   1680  C   LEU A 270      11.759   6.628  13.817  1.00 43.37           C  
ANISOU 1680  C   LEU A 270     6183   5046   5250   -374      8   -749       C  
ATOM   1681  O   LEU A 270      11.943   6.374  12.617  1.00 41.38           O  
ANISOU 1681  O   LEU A 270     5954   4826   4943   -362    136   -818       O  
ATOM   1682  CB  LEU A 270       9.439   6.474  14.653  1.00 41.17           C  
ANISOU 1682  CB  LEU A 270     5862   4840   4940   -360    153   -591       C  
ATOM   1683  CG  LEU A 270       8.273   5.738  15.321  1.00 41.88           C  
ANISOU 1683  CG  LEU A 270     5850   4964   5096   -348    252   -485       C  
ATOM   1684  CD1 LEU A 270       7.083   6.677  15.441  1.00 42.41           C  
ANISOU 1684  CD1 LEU A 270     6006   5007   5101   -295    259   -465       C  
ATOM   1685  CD2 LEU A 270       7.912   4.464  14.572  1.00 41.69           C  
ANISOU 1685  CD2 LEU A 270     5797   4998   5048   -367    434   -502       C  
ATOM   1686  N   LYS A 271      12.371   7.640  14.455  1.00 44.31           N  
ANISOU 1686  N   LYS A 271     6384   5084   5367   -351   -193   -799       N  
ATOM   1687  CA  LYS A 271      13.346   8.475  13.765  1.00 45.01           C  
ANISOU 1687  CA  LYS A 271     6612   5120   5368   -286   -253   -974       C  
ATOM   1688  C   LYS A 271      14.441   7.608  13.148  1.00 43.06           C  
ANISOU 1688  C   LYS A 271     6278   4826   5256   -298   -250  -1014       C  
ATOM   1689  O   LYS A 271      14.850   7.808  11.998  1.00 42.47           O  
ANISOU 1689  O   LYS A 271     6254   4768   5115   -230   -140  -1135       O  
ATOM   1690  CB  LYS A 271      13.957   9.481  14.714  1.00 48.94           C  
ANISOU 1690  CB  LYS A 271     7219   5507   5868   -273   -526  -1028       C  
ATOM   1691  CG  LYS A 271      14.964  10.413  14.061  1.00 53.02           C  
ANISOU 1691  CG  LYS A 271     7921   5961   6262   -174   -589  -1253       C  
ATOM   1692  CD  LYS A 271      15.541  11.388  15.078  1.00 57.88           C  
ANISOU 1692  CD  LYS A 271     8681   6444   6866   -172   -908  -1321       C  
ATOM   1693  CE  LYS A 271      17.043  11.562  14.874  1.00 63.22           C  
ANISOU 1693  CE  LYS A 271     9444   6958   7620   -110  -1081  -1514       C  
ATOM   1694  NZ  LYS A 271      17.654  12.622  15.723  1.00 69.16           N1+
ANISOU 1694  NZ  LYS A 271    10397   7556   8326    -98  -1417  -1632       N1+
ATOM   1695  N   VAL A 272      14.907   6.651  13.932  1.00 41.51           N  
ANISOU 1695  N   VAL A 272     5931   4577   5262   -387   -371   -888       N  
ATOM   1696  CA  VAL A 272      15.950   5.744  13.501  1.00 40.47           C  
ANISOU 1696  CA  VAL A 272     5701   4388   5286   -425   -414   -877       C  
ATOM   1697  C   VAL A 272      15.456   4.862  12.384  1.00 38.17           C  
ANISOU 1697  C   VAL A 272     5349   4208   4944   -440   -182   -848       C  
ATOM   1698  O   VAL A 272      16.133   4.669  11.388  1.00 38.53           O  
ANISOU 1698  O   VAL A 272     5385   4224   5030   -410   -151   -919       O  
ATOM   1699  CB  VAL A 272      16.415   4.884  14.675  1.00 40.35           C  
ANISOU 1699  CB  VAL A 272     5524   4323   5486   -543   -590   -689       C  
ATOM   1700  CG1 VAL A 272      17.302   3.728  14.211  1.00 40.55           C  
ANISOU 1700  CG1 VAL A 272     5425   4319   5662   -611   -615   -615       C  
ATOM   1701  CG2 VAL A 272      17.122   5.769  15.696  1.00 41.48           C  
ANISOU 1701  CG2 VAL A 272     5721   4308   5729   -547   -886   -714       C  
ATOM   1702  N   ILE A 273      14.271   4.322  12.537  1.00 36.58           N  
ANISOU 1702  N   ILE A 273     5108   4122   4669   -480    -35   -748       N  
ATOM   1703  CA  ILE A 273      13.742   3.457  11.500  1.00 35.88           C  
ANISOU 1703  CA  ILE A 273     4987   4119   4527   -509    146   -725       C  
ATOM   1704  C   ILE A 273      13.666   4.181  10.169  1.00 37.10           C  
ANISOU 1704  C   ILE A 273     5228   4287   4583   -437    262   -848       C  
ATOM   1705  O   ILE A 273      14.016   3.623   9.151  1.00 37.06           O  
ANISOU 1705  O   ILE A 273     5169   4290   4622   -456    317   -851       O  
ATOM   1706  CB  ILE A 273      12.352   2.950  11.879  1.00 34.95           C  
ANISOU 1706  CB  ILE A 273     4860   4094   4323   -536    280   -644       C  
ATOM   1707  CG1 ILE A 273      12.461   1.966  13.034  1.00 35.30           C  
ANISOU 1707  CG1 ILE A 273     4777   4173   4462   -602    225   -499       C  
ATOM   1708  CG2 ILE A 273      11.687   2.265  10.707  1.00 34.47           C  
ANISOU 1708  CG2 ILE A 273     4818   4094   4184   -565    436   -653       C  
ATOM   1709  CD1 ILE A 273      11.137   1.721  13.704  1.00 35.69           C  
ANISOU 1709  CD1 ILE A 273     4817   4298   4445   -576    348   -445       C  
ATOM   1710  N   VAL A 274      13.192   5.425  10.186  1.00 39.97           N  
ANISOU 1710  N   VAL A 274     5711   4664   4812   -360    298   -926       N  
ATOM   1711  CA  VAL A 274      13.120   6.253   8.967  1.00 40.62           C  
ANISOU 1711  CA  VAL A 274     5865   4792   4777   -283    433  -1019       C  
ATOM   1712  C   VAL A 274      14.495   6.472   8.353  1.00 41.81           C  
ANISOU 1712  C   VAL A 274     5998   4880   5008   -206    386  -1136       C  
ATOM   1713  O   VAL A 274      14.684   6.258   7.167  1.00 43.36           O  
ANISOU 1713  O   VAL A 274     6131   5113   5233   -184    507  -1148       O  
ATOM   1714  CB  VAL A 274      12.447   7.611   9.262  1.00 41.12           C  
ANISOU 1714  CB  VAL A 274     6076   4896   4654   -220    456  -1062       C  
ATOM   1715  CG1 VAL A 274      12.696   8.628   8.155  1.00 42.05           C  
ANISOU 1715  CG1 VAL A 274     6270   5080   4628   -121    586  -1164       C  
ATOM   1716  CG2 VAL A 274      10.956   7.395   9.454  1.00 41.45           C  
ANISOU 1716  CG2 VAL A 274     6120   4990   4639   -279    540   -945       C  
ATOM   1717  N   GLU A 275      15.445   6.888   9.183  1.00 42.80           N  
ANISOU 1717  N   GLU A 275     6173   4894   5195   -165    195  -1216       N  
ATOM   1718  CA  GLU A 275      16.811   7.159   8.762  1.00 43.54           C  
ANISOU 1718  CA  GLU A 275     6274   4881   5389    -68    111  -1358       C  
ATOM   1719  C   GLU A 275      17.480   5.942   8.160  1.00 42.77           C  
ANISOU 1719  C   GLU A 275     6007   4734   5508   -122     94  -1283       C  
ATOM   1720  O   GLU A 275      18.173   6.056   7.169  1.00 41.25           O  
ANISOU 1720  O   GLU A 275     5775   4513   5384    -28    154  -1370       O  
ATOM   1721  CB  GLU A 275      17.619   7.643   9.953  1.00 45.81           C  
ANISOU 1721  CB  GLU A 275     6649   5014   5742    -52   -158  -1431       C  
ATOM   1722  CG  GLU A 275      17.248   9.050  10.371  1.00 48.52           C  
ANISOU 1722  CG  GLU A 275     7196   5385   5855     28   -180  -1549       C  
ATOM   1723  CD  GLU A 275      17.845   9.454  11.699  1.00 51.44           C  
ANISOU 1723  CD  GLU A 275     7650   5596   6300      0   -495  -1580       C  
ATOM   1724  OE1 GLU A 275      18.282   8.581  12.484  1.00 51.42           O  
ANISOU 1724  OE1 GLU A 275     7514   5489   6533   -112   -678  -1451       O  
ATOM   1725  OE2 GLU A 275      17.882  10.673  11.970  1.00 57.97           O1-
ANISOU 1725  OE2 GLU A 275     8679   6405   6942     81   -574  -1721       O1-
ATOM   1726  N   GLU A 276      17.266   4.784   8.781  1.00 43.75           N  
ANISOU 1726  N   GLU A 276     6027   4856   5738   -269     15  -1112       N  
ATOM   1727  CA  GLU A 276      17.774   3.500   8.264  1.00 44.09           C  
ANISOU 1727  CA  GLU A 276     5919   4877   5956   -356    -17   -998       C  
ATOM   1728  C   GLU A 276      17.208   3.172   6.902  1.00 42.88           C  
ANISOU 1728  C   GLU A 276     5713   4826   5753   -359    178   -974       C  
ATOM   1729  O   GLU A 276      17.916   2.665   6.044  1.00 45.52           O  
ANISOU 1729  O   GLU A 276     5941   5116   6238   -357    158   -954       O  
ATOM   1730  CB  GLU A 276      17.432   2.345   9.205  1.00 42.50           C  
ANISOU 1730  CB  GLU A 276     5639   4714   5796   -513    -91   -806       C  
ATOM   1731  CG  GLU A 276      18.274   2.301  10.454  1.00 43.00           C  
ANISOU 1731  CG  GLU A 276     5672   4660   6007   -555   -327   -750       C  
ATOM   1732  CD  GLU A 276      19.703   1.904  10.193  1.00 44.27           C  
ANISOU 1732  CD  GLU A 276     5754   4661   6407   -566   -518   -738       C  
ATOM   1733  OE1 GLU A 276      20.029   1.284   9.157  1.00 44.15           O  
ANISOU 1733  OE1 GLU A 276     5663   4647   6465   -575   -474   -713       O  
ATOM   1734  OE2 GLU A 276      20.522   2.254  11.050  1.00 47.00           O1-
ANISOU 1734  OE2 GLU A 276     6109   4856   6891   -567   -742   -748       O1-
ATOM   1735  N   ALA A 277      15.925   3.417   6.730  1.00 40.68           N  
ANISOU 1735  N   ALA A 277     5494   4668   5294   -377    339   -952       N  
ATOM   1736  CA  ALA A 277      15.302   3.222   5.450  1.00 40.37           C  
ANISOU 1736  CA  ALA A 277     5409   4712   5219   -396    500   -915       C  
ATOM   1737  C   ALA A 277      15.862   4.228   4.452  1.00 40.61           C  
ANISOU 1737  C   ALA A 277     5425   4747   5258   -250    604  -1028       C  
ATOM   1738  O   ALA A 277      16.245   3.859   3.357  1.00 42.28           O  
ANISOU 1738  O   ALA A 277     5511   4960   5594   -245    651   -993       O  
ATOM   1739  CB  ALA A 277      13.814   3.399   5.582  1.00 40.84           C  
ANISOU 1739  CB  ALA A 277     5551   4863   5103   -442    617   -871       C  
ATOM   1740  N   ALA A 278      15.922   5.492   4.855  1.00 39.25           N  
ANISOU 1740  N   ALA A 278     5380   4583   4949   -128    636  -1160       N  
ATOM   1741  CA  ALA A 278      16.336   6.579   3.977  1.00 40.43           C  
ANISOU 1741  CA  ALA A 278     5547   4779   5034     36    781  -1285       C  
ATOM   1742  C   ALA A 278      17.720   6.380   3.355  1.00 43.35           C  
ANISOU 1742  C   ALA A 278     5806   5048   5619    144    736  -1369       C  
ATOM   1743  O   ALA A 278      17.993   6.807   2.227  1.00 43.88           O  
ANISOU 1743  O   ALA A 278     5788   5175   5708    262    905  -1411       O  
ATOM   1744  CB  ALA A 278      16.298   7.882   4.746  1.00 41.01           C  
ANISOU 1744  CB  ALA A 278     5819   4866   4899    140    767  -1424       C  
ATOM   1745  N   ARG A 279      18.587   5.714   4.108  1.00 45.74           N  
ANISOU 1745  N   ARG A 279     6089   5191   6100    103    504  -1374       N  
ATOM   1746  CA  ARG A 279      19.992   5.506   3.733  1.00 46.84           C  
ANISOU 1746  CA  ARG A 279     6136   5175   6485    205    394  -1456       C  
ATOM   1747  C   ARG A 279      20.094   4.477   2.642  1.00 44.39           C  
ANISOU 1747  C   ARG A 279     5612   4880   6374    134    434  -1303       C  
ATOM   1748  O   ARG A 279      21.039   4.484   1.905  1.00 44.26           O  
ANISOU 1748  O   ARG A 279     5482   4780   6555    253    429  -1360       O  
ATOM   1749  CB  ARG A 279      20.782   5.033   4.954  1.00 47.99           C  
ANISOU 1749  CB  ARG A 279     6319   5137   6780    136     95  -1449       C  
ATOM   1750  CG  ARG A 279      22.272   5.019   4.763  1.00 51.74           C  
ANISOU 1750  CG  ARG A 279     6743   5397   7516    256    -69  -1561       C  
ATOM   1751  CD  ARG A 279      23.007   5.334   6.053  1.00 53.75           C  
ANISOU 1751  CD  ARG A 279     7127   5461   7834    258   -349  -1649       C  
ATOM   1752  NE  ARG A 279      22.544   4.498   7.158  1.00 54.78           N  
ANISOU 1752  NE  ARG A 279     7228   5608   7976     33   -497  -1433       N  
ATOM   1753  CZ  ARG A 279      21.985   4.939   8.292  1.00 56.51           C  
ANISOU 1753  CZ  ARG A 279     7566   5858   8045    -27   -562  -1426       C  
ATOM   1754  NH1 ARG A 279      21.803   6.243   8.541  1.00 58.55           N1+
ANISOU 1754  NH1 ARG A 279     8014   6124   8107    102   -530  -1622       N1+
ATOM   1755  NH2 ARG A 279      21.613   4.054   9.203  1.00 53.90           N  
ANISOU 1755  NH2 ARG A 279     7159   5561   7760   -216   -663  -1207       N  
ATOM   1756  N   GLN A 280      19.104   3.599   2.552  1.00 42.61           N  
ANISOU 1756  N   GLN A 280     5339   4753   6099    -55    458  -1115       N  
ATOM   1757  CA  GLN A 280      19.025   2.621   1.471  1.00 44.10           C  
ANISOU 1757  CA  GLN A 280     5346   4968   6442   -152    475   -954       C  
ATOM   1758  C   GLN A 280      17.950   3.032   0.448  1.00 45.88           C  
ANISOU 1758  C   GLN A 280     5535   5354   6544   -158    707   -900       C  
ATOM   1759  O   GLN A 280      17.580   2.262  -0.445  1.00 46.42           O  
ANISOU 1759  O   GLN A 280     5471   5457   6707   -274    714   -745       O  
ATOM   1760  CB  GLN A 280      18.717   1.226   2.039  1.00 42.14           C  
ANISOU 1760  CB  GLN A 280     5088   4706   6218   -373    307   -779       C  
ATOM   1761  CG  GLN A 280      19.692   0.765   3.115  1.00 42.00           C  
ANISOU 1761  CG  GLN A 280     5083   4551   6322   -404     75   -769       C  
ATOM   1762  CD  GLN A 280      21.123   0.732   2.653  1.00 43.40           C  
ANISOU 1762  CD  GLN A 280     5141   4562   6788   -305    -57   -805       C  
ATOM   1763  NE2 GLN A 280      21.368   0.244   1.436  1.00 44.49           N  
ANISOU 1763  NE2 GLN A 280     5111   4697   7095   -311    -35   -718       N  
ATOM   1764  OE1 GLN A 280      21.999   1.203   3.369  1.00 43.63           O  
ANISOU 1764  OE1 GLN A 280     5225   4449   6905   -214   -189   -916       O  
ATOM   1765  N   ASN A 281      17.458   4.258   0.584  1.00 47.00           N  
ANISOU 1765  N   ASN A 281     5796   5586   6475    -47    873  -1011       N  
ATOM   1766  CA  ASN A 281      16.524   4.837  -0.351  1.00 48.33           C  
ANISOU 1766  CA  ASN A 281     5925   5908   6529    -43   1096   -944       C  
ATOM   1767  C   ASN A 281      15.172   4.207  -0.343  1.00 47.08           C  
ANISOU 1767  C   ASN A 281     5800   5804   6284   -243   1085   -787       C  
ATOM   1768  O   ASN A 281      14.446   4.234  -1.352  1.00 52.10           O  
ANISOU 1768  O   ASN A 281     6343   6523   6929   -306   1200   -661       O  
ATOM   1769  CB  ASN A 281      17.101   4.795  -1.756  1.00 51.70           C  
ANISOU 1769  CB  ASN A 281     6120   6361   7164     34   1204   -888       C  
ATOM   1770  CG  ASN A 281      17.182   6.160  -2.371  1.00 54.77           C  
ANISOU 1770  CG  ASN A 281     6495   6881   7432    235   1467   -982       C  
ATOM   1771  ND2 ASN A 281      17.194   6.200  -3.682  1.00 57.49           N  
ANISOU 1771  ND2 ASN A 281     6613   7315   7916    267   1627   -864       N  
ATOM   1772  OD1 ASN A 281      17.279   7.171  -1.669  1.00 58.94           O  
ANISOU 1772  OD1 ASN A 281     7213   7439   7744    362   1520  -1152       O  
ATOM   1773  N   ARG A 282      14.823   3.645   0.794  1.00 44.70           N  
ANISOU 1773  N   ARG A 282     5625   5447   5909   -340    944   -789       N  
ATOM   1774  CA  ARG A 282      13.462   3.232   1.035  1.00 44.99           C  
ANISOU 1774  CA  ARG A 282     5747   5524   5822   -482    948   -697       C  
ATOM   1775  C   ARG A 282      12.752   4.346   1.762  1.00 44.89           C  
ANISOU 1775  C   ARG A 282     5891   5564   5600   -415   1031   -766       C  
ATOM   1776  O   ARG A 282      13.364   5.283   2.230  1.00 46.09           O  
ANISOU 1776  O   ARG A 282     6109   5718   5685   -282   1050   -887       O  
ATOM   1777  CB  ARG A 282      13.423   1.974   1.891  1.00 42.97           C  
ANISOU 1777  CB  ARG A 282     5532   5205   5590   -604    779   -657       C  
ATOM   1778  CG  ARG A 282      13.477   0.691   1.090  1.00 43.05           C  
ANISOU 1778  CG  ARG A 282     5437   5192   5728   -743    687   -533       C  
ATOM   1779  CD  ARG A 282      14.794   0.510   0.378  1.00 43.57           C  
ANISOU 1779  CD  ARG A 282     5334   5205   6016   -697    626   -514       C  
ATOM   1780  NE  ARG A 282      14.942  -0.856  -0.083  1.00 43.60           N  
ANISOU 1780  NE  ARG A 282     5258   5175   6131   -854    475   -379       N  
ATOM   1781  CZ  ARG A 282      15.987  -1.300  -0.770  1.00 45.27           C  
ANISOU 1781  CZ  ARG A 282     5304   5325   6571   -854    374   -312       C  
ATOM   1782  NH1 ARG A 282      17.003  -0.492  -1.081  1.00 45.13           N1+
ANISOU 1782  NH1 ARG A 282     5177   5263   6707   -682    427   -391       N1+
ATOM   1783  NH2 ARG A 282      16.018  -2.575  -1.143  1.00 46.24           N  
ANISOU 1783  NH2 ARG A 282     5380   5426   6764  -1022    210   -170       N  
ATOM   1784  N   ILE A 283      11.441   4.223   1.848  1.00 44.57           N  
ANISOU 1784  N   ILE A 283     5923   5548   5461   -511   1058   -688       N  
ATOM   1785  CA  ILE A 283      10.653   5.069   2.721  1.00 43.23           C  
ANISOU 1785  CA  ILE A 283     5904   5402   5119   -474   1088   -722       C  
ATOM   1786  C   ILE A 283       9.875   4.164   3.667  1.00 42.17           C  
ANISOU 1786  C   ILE A 283     5842   5208   4971   -564    987   -696       C  
ATOM   1787  O   ILE A 283       9.751   2.949   3.436  1.00 40.03           O  
ANISOU 1787  O   ILE A 283     5528   4903   4777   -664    926   -646       O  
ATOM   1788  CB  ILE A 283       9.628   5.906   1.937  1.00 43.46           C  
ANISOU 1788  CB  ILE A 283     5950   5510   5052   -491   1227   -633       C  
ATOM   1789  CG1 ILE A 283       8.800   5.003   1.004  1.00 43.71           C  
ANISOU 1789  CG1 ILE A 283     5907   5512   5188   -640   1215   -497       C  
ATOM   1790  CG2 ILE A 283      10.326   7.000   1.158  1.00 44.17           C  
ANISOU 1790  CG2 ILE A 283     5981   5706   5096   -369   1376   -662       C  
ATOM   1791  CD1 ILE A 283       7.345   5.400   0.951  1.00 44.55           C  
ANISOU 1791  CD1 ILE A 283     6102   5612   5214   -709   1242   -402       C  
ATOM   1792  N   VAL A 284       9.302   4.777   4.695  1.00 40.36           N  
ANISOU 1792  N   VAL A 284     5724   4975   4635   -522    975   -724       N  
ATOM   1793  CA  VAL A 284       8.588   4.038   5.692  1.00 37.58           C  
ANISOU 1793  CA  VAL A 284     5422   4579   4278   -566    910   -708       C  
ATOM   1794  C   VAL A 284       7.110   4.280   5.546  1.00 36.86           C  
ANISOU 1794  C   VAL A 284     5410   4471   4126   -597    960   -654       C  
ATOM   1795  O   VAL A 284       6.686   5.419   5.422  1.00 36.10           O  
ANISOU 1795  O   VAL A 284     5364   4400   3951   -559   1008   -629       O  
ATOM   1796  CB  VAL A 284       9.032   4.465   7.086  1.00 37.76           C  
ANISOU 1796  CB  VAL A 284     5477   4586   4283   -496    828   -755       C  
ATOM   1797  CG1 VAL A 284       8.222   3.741   8.150  1.00 39.20           C  
ANISOU 1797  CG1 VAL A 284     5677   4744   4473   -519    798   -720       C  
ATOM   1798  CG2 VAL A 284      10.512   4.182   7.268  1.00 37.33           C  
ANISOU 1798  CG2 VAL A 284     5349   4509   4324   -478    738   -800       C  
ATOM   1799  N   SER A 285       6.345   3.190   5.553  1.00 37.50           N  
ANISOU 1799  N   SER A 285     5512   4502   4235   -665    938   -636       N  
ATOM   1800  CA  SER A 285       4.901   3.268   5.596  1.00 39.93           C  
ANISOU 1800  CA  SER A 285     5911   4745   4518   -682    950   -606       C  
ATOM   1801  C   SER A 285       4.422   2.871   6.962  1.00 39.14           C  
ANISOU 1801  C   SER A 285     5854   4611   4406   -618    926   -650       C  
ATOM   1802  O   SER A 285       4.705   1.784   7.435  1.00 37.47           O  
ANISOU 1802  O   SER A 285     5621   4413   4203   -625    911   -686       O  
ATOM   1803  CB  SER A 285       4.237   2.353   4.565  1.00 43.25           C  
ANISOU 1803  CB  SER A 285     6350   5103   4979   -791    927   -578       C  
ATOM   1804  OG  SER A 285       2.823   2.403   4.689  1.00 44.73           O  
ANISOU 1804  OG  SER A 285     6644   5187   5165   -796    910   -568       O  
ATOM   1805  N   ALA A 286       3.629   3.751   7.550  1.00 39.52           N  
ANISOU 1805  N   ALA A 286     5956   4621   4438   -559    925   -625       N  
ATOM   1806  CA  ALA A 286       3.201   3.611   8.916  1.00 39.69           C  
ANISOU 1806  CA  ALA A 286     5981   4615   4483   -476    907   -644       C  
ATOM   1807  C   ALA A 286       1.723   3.328   9.017  1.00 39.52           C  
ANISOU 1807  C   ALA A 286     6041   4481   4496   -449    916   -649       C  
ATOM   1808  O   ALA A 286       0.915   3.995   8.410  1.00 42.71           O  
ANISOU 1808  O   ALA A 286     6506   4812   4907   -477    898   -596       O  
ATOM   1809  CB  ALA A 286       3.529   4.880   9.668  1.00 41.25           C  
ANISOU 1809  CB  ALA A 286     6170   4840   4664   -417    858   -605       C  
ATOM   1810  N   HIS A 287       1.388   2.317   9.793  1.00 39.75           N  
ANISOU 1810  N   HIS A 287     6064   4495   4546   -388    946   -711       N  
ATOM   1811  CA  HIS A 287       0.019   1.955  10.089  1.00 40.97           C  
ANISOU 1811  CA  HIS A 287     6297   4525   4743   -317    961   -757       C  
ATOM   1812  C   HIS A 287      -0.376   2.749  11.285  1.00 39.58           C  
ANISOU 1812  C   HIS A 287     6067   4324   4646   -205    946   -703       C  
ATOM   1813  O   HIS A 287       0.286   2.663  12.303  1.00 38.93           O  
ANISOU 1813  O   HIS A 287     5874   4334   4585   -153    961   -682       O  
ATOM   1814  CB  HIS A 287      -0.026   0.465  10.397  1.00 43.61           C  
ANISOU 1814  CB  HIS A 287     6649   4892   5029   -281   1029   -863       C  
ATOM   1815  CG  HIS A 287      -1.108   0.058  11.339  1.00 47.24           C  
ANISOU 1815  CG  HIS A 287     7137   5276   5535   -128   1090   -932       C  
ATOM   1816  CD2 HIS A 287      -1.379   0.456  12.604  1.00 47.40           C  
ANISOU 1816  CD2 HIS A 287     7057   5305   5649      5   1127   -892       C  
ATOM   1817  ND1 HIS A 287      -2.041  -0.917  11.015  1.00 53.13           N  
ANISOU 1817  ND1 HIS A 287     8025   5923   6239    -88   1116  -1069       N  
ATOM   1818  CE1 HIS A 287      -2.833  -1.092  12.061  1.00 54.48           C  
ANISOU 1818  CE1 HIS A 287     8179   6050   6472     90   1194  -1125       C  
ATOM   1819  NE2 HIS A 287      -2.462  -0.264  13.026  1.00 51.99           N  
ANISOU 1819  NE2 HIS A 287     7700   5800   6254    145   1203  -1003       N  
ATOM   1820  N   VAL A 288      -1.429   3.543  11.169  1.00 39.90           N  
ANISOU 1820  N   VAL A 288     6173   4236   4752   -182    892   -653       N  
ATOM   1821  CA  VAL A 288      -1.819   4.441  12.256  1.00 40.10           C  
ANISOU 1821  CA  VAL A 288     6142   4225   4867    -89    840   -569       C  
ATOM   1822  C   VAL A 288      -3.305   4.664  12.308  1.00 42.61           C  
ANISOU 1822  C   VAL A 288     6534   4353   5305    -21    796   -553       C  
ATOM   1823  O   VAL A 288      -3.964   4.764  11.286  1.00 43.66           O  
ANISOU 1823  O   VAL A 288     6775   4375   5437    -95    756   -543       O  
ATOM   1824  CB  VAL A 288      -1.175   5.828  12.134  1.00 39.35           C  
ANISOU 1824  CB  VAL A 288     6041   4200   4710   -158    755   -455       C  
ATOM   1825  CG1 VAL A 288       0.294   5.774  12.509  1.00 38.79           C  
ANISOU 1825  CG1 VAL A 288     5885   4277   4575   -180    757   -474       C  
ATOM   1826  CG2 VAL A 288      -1.341   6.372  10.729  1.00 39.21           C  
ANISOU 1826  CG2 VAL A 288     6118   4168   4610   -273    747   -408       C  
ATOM   1827  N   HIS A 289      -3.828   4.746  13.523  1.00 44.73           N  
ANISOU 1827  N   HIS A 289     6723   4569   5705    120    789   -532       N  
ATOM   1828  CA  HIS A 289      -5.223   5.050  13.745  1.00 46.92           C  
ANISOU 1828  CA  HIS A 289     7046   4639   6142    211    726   -504       C  
ATOM   1829  C   HIS A 289      -5.340   6.344  14.583  1.00 46.97           C  
ANISOU 1829  C   HIS A 289     6973   4631   6243    235    600   -325       C  
ATOM   1830  O   HIS A 289      -5.767   7.385  14.083  1.00 45.22           O  
ANISOU 1830  O   HIS A 289     6828   4338   6015    152    479   -196       O  
ATOM   1831  CB  HIS A 289      -5.908   3.870  14.437  1.00 48.59           C  
ANISOU 1831  CB  HIS A 289     7233   4776   6454    395    839   -654       C  
ATOM   1832  CG  HIS A 289      -6.153   2.694  13.544  1.00 50.62           C  
ANISOU 1832  CG  HIS A 289     7635   4986   6614    373    910   -834       C  
ATOM   1833  CD2 HIS A 289      -5.931   1.373  13.727  1.00 53.12           C  
ANISOU 1833  CD2 HIS A 289     7963   5386   6835    445   1052   -997       C  
ATOM   1834  ND1 HIS A 289      -6.750   2.806  12.308  1.00 53.22           N  
ANISOU 1834  ND1 HIS A 289     8126   5160   6934    258    811   -846       N  
ATOM   1835  CE1 HIS A 289      -6.882   1.606  11.767  1.00 54.28           C  
ANISOU 1835  CE1 HIS A 289     8376   5264   6982    257    863  -1022       C  
ATOM   1836  NE2 HIS A 289      -6.392   0.718  12.608  1.00 54.38           N  
ANISOU 1836  NE2 HIS A 289     8313   5429   6919    373   1016  -1123       N  
ATOM   1837  N   GLY A 290      -4.960   6.268  15.852  1.00 48.01           N  
ANISOU 1837  N   GLY A 290     6945   4838   6460    336    616   -298       N  
ATOM   1838  CA  GLY A 290      -5.129   7.406  16.756  1.00 50.80           C  
ANISOU 1838  CA  GLY A 290     7214   5158   6929    362    461   -123       C  
ATOM   1839  C   GLY A 290      -4.334   8.585  16.256  1.00 49.98           C  
ANISOU 1839  C   GLY A 290     7191   5154   6646    199    337    -19       C  
ATOM   1840  O   GLY A 290      -3.354   8.389  15.549  1.00 48.77           O  
ANISOU 1840  O   GLY A 290     7087   5132   6312    102    402    -92       O  
ATOM   1841  N   LYS A 291      -4.730   9.804  16.628  1.00 51.03           N  
ANISOU 1841  N   LYS A 291     7341   5231   6818    176    160    149       N  
ATOM   1842  CA  LYS A 291      -3.984  10.992  16.189  1.00 51.56           C  
ANISOU 1842  CA  LYS A 291     7513   5413   6665     37     50    235       C  
ATOM   1843  C   LYS A 291      -2.544  10.981  16.719  1.00 50.96           C  
ANISOU 1843  C   LYS A 291     7374   5493   6493     10     34    181       C  
ATOM   1844  O   LYS A 291      -1.587  11.266  15.983  1.00 51.37           O  
ANISOU 1844  O   LYS A 291     7521   5668   6330    -79     63    118       O  
ATOM   1845  CB  LYS A 291      -4.679  12.273  16.629  1.00 54.65           C  
ANISOU 1845  CB  LYS A 291     7944   5724   7098     17   -161    439       C  
ATOM   1846  CG  LYS A 291      -4.271  13.501  15.839  1.00 55.10           C  
ANISOU 1846  CG  LYS A 291     8171   5894   6871   -125   -236    528       C  
ATOM   1847  CD  LYS A 291      -4.861  14.751  16.453  1.00 58.31           C  
ANISOU 1847  CD  LYS A 291     8618   6243   7295   -152   -474    747       C  
ATOM   1848  CE  LYS A 291      -4.876  15.880  15.445  1.00 61.02           C  
ANISOU 1848  CE  LYS A 291     9151   6687   7346   -287   -504    863       C  
ATOM   1849  NZ  LYS A 291      -4.704  17.207  16.098  1.00 64.78           N1+
ANISOU 1849  NZ  LYS A 291     9713   7221   7679   -341   -742   1022       N1+
ATOM   1850  N   ALA A 292      -2.399  10.620  17.989  1.00 50.46           N  
ANISOU 1850  N   ALA A 292     7139   5417   6617     92    -13    210       N  
ATOM   1851  CA  ALA A 292      -1.085  10.433  18.601  1.00 48.80           C  
ANISOU 1851  CA  ALA A 292     6837   5321   6381     63    -50    178       C  
ATOM   1852  C   ALA A 292      -0.054   9.681  17.719  1.00 46.61           C  
ANISOU 1852  C   ALA A 292     6609   5157   5944      5    101     19       C  
ATOM   1853  O   ALA A 292       1.083  10.130  17.581  1.00 46.22           O  
ANISOU 1853  O   ALA A 292     6614   5185   5763    -70     23    -15       O  
ATOM   1854  CB  ALA A 292      -1.250   9.720  19.932  1.00 49.81           C  
ANISOU 1854  CB  ALA A 292     6723   5426   6777    170    -41    239       C  
ATOM   1855  N   GLY A 293      -0.444   8.534  17.157  1.00 45.47           N  
ANISOU 1855  N   GLY A 293     6451   5006   5820     45    296    -81       N  
ATOM   1856  CA  GLY A 293       0.454   7.722  16.335  1.00 43.54           C  
ANISOU 1856  CA  GLY A 293     6235   4856   5452    -14    421   -206       C  
ATOM   1857  C   GLY A 293       0.696   8.389  14.999  1.00 43.73           C  
ANISOU 1857  C   GLY A 293     6425   4909   5282   -106    426   -243       C  
ATOM   1858  O   GLY A 293       1.825   8.417  14.504  1.00 42.63           O  
ANISOU 1858  O   GLY A 293     6311   4857   5028   -165    436   -306       O  
ATOM   1859  N   ILE A 294      -0.382   8.916  14.416  1.00 44.26           N  
ANISOU 1859  N   ILE A 294     6589   4896   5331   -114    423   -188       N  
ATOM   1860  CA  ILE A 294      -0.326   9.662  13.162  1.00 44.29           C  
ANISOU 1860  CA  ILE A 294     6725   4942   5161   -204    442   -168       C  
ATOM   1861  C   ILE A 294       0.701  10.792  13.217  1.00 43.88           C  
ANISOU 1861  C   ILE A 294     6735   5002   4937   -242    354   -153       C  
ATOM   1862  O   ILE A 294       1.562  10.867  12.356  1.00 43.35           O  
ANISOU 1862  O   ILE A 294     6709   5032   4729   -282    429   -225       O  
ATOM   1863  CB  ILE A 294      -1.695  10.285  12.825  1.00 47.80           C  
ANISOU 1863  CB  ILE A 294     7246   5275   5643   -218    395    -42       C  
ATOM   1864  CG1 ILE A 294      -2.735   9.202  12.547  1.00 48.65           C  
ANISOU 1864  CG1 ILE A 294     7339   5238   5906   -179    468    -92       C  
ATOM   1865  CG2 ILE A 294      -1.600  11.183  11.596  1.00 50.01           C  
ANISOU 1865  CG2 ILE A 294     7634   5636   5729   -322    423     31       C  
ATOM   1866  CD1 ILE A 294      -4.126   9.735  12.259  1.00 50.24           C  
ANISOU 1866  CD1 ILE A 294     7611   5276   6200   -191    388     35       C  
ATOM   1867  N   MET A 295       0.609  11.668  14.215  1.00 43.72           N  
ANISOU 1867  N   MET A 295     6725   4959   4928   -221    187    -66       N  
ATOM   1868  CA  MET A 295       1.552  12.781  14.332  1.00 44.69           C  
ANISOU 1868  CA  MET A 295     6949   5172   4859   -251     70    -76       C  
ATOM   1869  C   MET A 295       2.999  12.323  14.653  1.00 43.58           C  
ANISOU 1869  C   MET A 295     6758   5079   4722   -242     49   -212       C  
ATOM   1870  O   MET A 295       3.972  12.984  14.266  1.00 43.47           O  
ANISOU 1870  O   MET A 295     6853   5140   4525   -254     19   -296       O  
ATOM   1871  CB  MET A 295       1.092  13.763  15.395  1.00 47.38           C  
ANISOU 1871  CB  MET A 295     7320   5459   5224   -247   -153     60       C  
ATOM   1872  CG  MET A 295      -0.299  14.315  15.165  1.00 50.04           C  
ANISOU 1872  CG  MET A 295     7707   5728   5578   -262   -179    225       C  
ATOM   1873  SD  MET A 295      -0.464  15.458  13.774  1.00 52.78           S  
ANISOU 1873  SD  MET A 295     8254   6201   5600   -348   -107    295       S  
ATOM   1874  CE  MET A 295       0.377  16.899  14.445  1.00 53.99           C  
ANISOU 1874  CE  MET A 295     8569   6455   5489   -369   -327    308       C  
ATOM   1875  N   ALA A 296       3.144  11.209  15.365  1.00 41.15           N  
ANISOU 1875  N   ALA A 296     6288   4726   4621   -214     64   -228       N  
ATOM   1876  CA  ALA A 296       4.461  10.701  15.655  1.00 41.18           C  
ANISOU 1876  CA  ALA A 296     6226   4759   4660   -225     30   -317       C  
ATOM   1877  C   ALA A 296       5.094  10.166  14.385  1.00 41.14           C  
ANISOU 1877  C   ALA A 296     6254   4817   4557   -245    194   -437       C  
ATOM   1878  O   ALA A 296       6.329  10.219  14.216  1.00 42.98           O  
ANISOU 1878  O   ALA A 296     6506   5076   4747   -254    150   -531       O  
ATOM   1879  CB  ALA A 296       4.402   9.612  16.717  1.00 41.48           C  
ANISOU 1879  CB  ALA A 296     6062   4763   4934   -200     27   -261       C  
ATOM   1880  N   ALA A 297       4.266   9.609  13.503  1.00 39.50           N  
ANISOU 1880  N   ALA A 297     6047   4614   4345   -252    360   -431       N  
ATOM   1881  CA  ALA A 297       4.775   9.013  12.271  1.00 38.19           C  
ANISOU 1881  CA  ALA A 297     5885   4502   4125   -284    500   -514       C  
ATOM   1882  C   ALA A 297       5.205  10.107  11.329  1.00 38.15           C  
ANISOU 1882  C   ALA A 297     5996   4570   3929   -290    529   -546       C  
ATOM   1883  O   ALA A 297       6.225   9.986  10.665  1.00 37.89           O  
ANISOU 1883  O   ALA A 297     5957   4586   3852   -286    580   -637       O  
ATOM   1884  CB  ALA A 297       3.717   8.145  11.617  1.00 38.35           C  
ANISOU 1884  CB  ALA A 297     5885   4486   4201   -304    627   -490       C  
ATOM   1885  N   ILE A 298       4.419  11.175  11.289  1.00 39.03           N  
ANISOU 1885  N   ILE A 298     6208   4693   3928   -292    502   -460       N  
ATOM   1886  CA  ILE A 298       4.722  12.337  10.473  1.00 41.21           C  
ANISOU 1886  CA  ILE A 298     6605   5077   3977   -289    551   -467       C  
ATOM   1887  C   ILE A 298       5.988  13.069  10.948  1.00 42.30           C  
ANISOU 1887  C   ILE A 298     6830   5251   3992   -236    438   -590       C  
ATOM   1888  O   ILE A 298       6.791  13.569  10.127  1.00 41.71           O  
ANISOU 1888  O   ILE A 298     6821   5271   3757   -196    529   -688       O  
ATOM   1889  CB  ILE A 298       3.536  13.333  10.479  1.00 43.41           C  
ANISOU 1889  CB  ILE A 298     6978   5364   4151   -319    517   -308       C  
ATOM   1890  CG1 ILE A 298       2.348  12.751   9.701  1.00 42.28           C  
ANISOU 1890  CG1 ILE A 298     6777   5169   4117   -377    625   -196       C  
ATOM   1891  CG2 ILE A 298       3.947  14.695   9.882  1.00 46.18           C  
ANISOU 1891  CG2 ILE A 298     7477   5865   4204   -308    556   -305       C  
ATOM   1892  CD1 ILE A 298       1.096  13.599   9.747  1.00 43.20           C  
ANISOU 1892  CD1 ILE A 298     6967   5253   4194   -417    563     -9       C  
ATOM   1893  N   LYS A 299       6.150  13.148  12.267  1.00 42.24           N  
ANISOU 1893  N   LYS A 299     6818   5159   4069   -231    234   -584       N  
ATOM   1894  CA  LYS A 299       7.321  13.788  12.832  1.00 43.95           C  
ANISOU 1894  CA  LYS A 299     7131   5364   4205   -196     65   -702       C  
ATOM   1895  C   LYS A 299       8.578  13.006  12.534  1.00 41.60           C  
ANISOU 1895  C   LYS A 299     6758   5041   4006   -170     97   -845       C  
ATOM   1896  O   LYS A 299       9.606  13.565  12.248  1.00 40.74           O  
ANISOU 1896  O   LYS A 299     6756   4947   3778   -115     62   -992       O  
ATOM   1897  CB  LYS A 299       7.190  13.921  14.324  1.00 46.47           C  
ANISOU 1897  CB  LYS A 299     7421   5581   4655   -221   -188   -626       C  
ATOM   1898  CG  LYS A 299       8.256  14.834  14.878  1.00 50.27           C  
ANISOU 1898  CG  LYS A 299     8054   6030   5018   -203   -417   -737       C  
ATOM   1899  CD  LYS A 299       7.597  16.127  15.296  1.00 56.39           C  
ANISOU 1899  CD  LYS A 299     8996   6828   5598   -220   -569   -650       C  
ATOM   1900  CE  LYS A 299       8.588  17.145  15.836  1.00 61.72           C  
ANISOU 1900  CE  LYS A 299     9877   7469   6106   -207   -833   -777       C  
ATOM   1901  NZ  LYS A 299       9.247  16.642  17.072  1.00 63.34           N1+
ANISOU 1901  NZ  LYS A 299     9963   7514   6589   -251  -1101   -765       N1+
ATOM   1902  N   ALA A 300       8.476  11.691  12.584  1.00 41.38           N  
ANISOU 1902  N   ALA A 300     6556   4971   4195   -205    162   -803       N  
ATOM   1903  CA  ALA A 300       9.616  10.821  12.279  1.00 41.21           C  
ANISOU 1903  CA  ALA A 300     6444   4921   4291   -201    180   -898       C  
ATOM   1904  C   ALA A 300      10.056  10.846  10.811  1.00 41.69           C  
ANISOU 1904  C   ALA A 300     6525   5058   4258   -161    366   -988       C  
ATOM   1905  O   ALA A 300      11.186  10.490  10.506  1.00 42.12           O  
ANISOU 1905  O   ALA A 300     6541   5078   4385   -131    348  -1090       O  
ATOM   1906  CB  ALA A 300       9.311   9.399  12.705  1.00 39.12           C  
ANISOU 1906  CB  ALA A 300     6000   4623   4239   -257    208   -806       C  
ATOM   1907  N   GLY A 301       9.166  11.242   9.906  1.00 43.56           N  
ANISOU 1907  N   GLY A 301     6798   5387   4363   -165    536   -929       N  
ATOM   1908  CA  GLY A 301       9.476  11.297   8.475  1.00 44.72           C  
ANISOU 1908  CA  GLY A 301     6922   5625   4443   -133    730   -971       C  
ATOM   1909  C   GLY A 301       8.885  10.165   7.655  1.00 44.72           C  
ANISOU 1909  C   GLY A 301     6781   5628   4581   -210    857   -877       C  
ATOM   1910  O   GLY A 301       9.365   9.885   6.563  1.00 45.74           O  
ANISOU 1910  O   GLY A 301     6834   5802   4742   -198    976   -900       O  
ATOM   1911  N   CYS A 302       7.841   9.514   8.159  1.00 44.95           N  
ANISOU 1911  N   CYS A 302     6778   5602   4699   -280    824   -776       N  
ATOM   1912  CA  CYS A 302       7.171   8.472   7.395  1.00 45.59           C  
ANISOU 1912  CA  CYS A 302     6771   5667   4882   -356    915   -706       C  
ATOM   1913  C   CYS A 302       6.469   9.152   6.239  1.00 46.30           C  
ANISOU 1913  C   CYS A 302     6884   5830   4876   -383   1044   -617       C  
ATOM   1914  O   CYS A 302       6.106  10.320   6.351  1.00 45.88           O  
ANISOU 1914  O   CYS A 302     6926   5832   4673   -356   1055   -575       O  
ATOM   1915  CB  CYS A 302       6.157   7.729   8.257  1.00 45.99           C  
ANISOU 1915  CB  CYS A 302     6814   5636   5023   -392    856   -650       C  
ATOM   1916  SG  CYS A 302       6.901   6.849   9.646  1.00 47.84           S  
ANISOU 1916  SG  CYS A 302     6974   5822   5380   -374    735   -695       S  
ATOM   1917  N   LYS A 303       6.320   8.447   5.124  1.00 47.41           N  
ANISOU 1917  N   LYS A 303     6933   5977   5103   -449   1128   -568       N  
ATOM   1918  CA  LYS A 303       5.818   9.070   3.901  1.00 50.88           C  
ANISOU 1918  CA  LYS A 303     7348   6499   5485   -489   1255   -450       C  
ATOM   1919  C   LYS A 303       4.564   8.424   3.358  1.00 50.34           C  
ANISOU 1919  C   LYS A 303     7257   6348   5523   -612   1240   -320       C  
ATOM   1920  O   LYS A 303       3.970   8.946   2.423  1.00 54.10           O  
ANISOU 1920  O   LYS A 303     7705   6872   5980   -673   1316   -177       O  
ATOM   1921  CB  LYS A 303       6.883   9.064   2.816  1.00 53.90           C  
ANISOU 1921  CB  LYS A 303     7613   6973   5895   -454   1369   -480       C  
ATOM   1922  CG  LYS A 303       8.153   9.817   3.149  1.00 57.02           C  
ANISOU 1922  CG  LYS A 303     8047   7433   6183   -311   1392   -631       C  
ATOM   1923  CD  LYS A 303       7.991  11.314   3.348  1.00 60.75           C  
ANISOU 1923  CD  LYS A 303     8654   8020   6407   -236   1454   -631       C  
ATOM   1924  CE  LYS A 303       7.593  12.024   2.092  1.00 63.88           C  
ANISOU 1924  CE  LYS A 303     8990   8575   6706   -248   1656   -490       C  
ATOM   1925  NZ  LYS A 303       7.631  13.486   2.336  1.00 68.97           N1+
ANISOU 1925  NZ  LYS A 303     9789   9360   7057   -160   1723   -509       N1+
ATOM   1926  N   SER A 304       4.145   7.317   3.947  1.00 46.61           N  
ANISOU 1926  N   SER A 304     6802   5750   5155   -645   1140   -368       N  
ATOM   1927  CA  SER A 304       2.870   6.720   3.635  1.00 45.02           C  
ANISOU 1927  CA  SER A 304     6632   5431   5043   -738   1091   -291       C  
ATOM   1928  C   SER A 304       2.186   6.448   4.960  1.00 43.20           C  
ANISOU 1928  C   SER A 304     6493   5098   4825   -683   1008   -352       C  
ATOM   1929  O   SER A 304       2.831   5.980   5.877  1.00 43.60           O  
ANISOU 1929  O   SER A 304     6530   5160   4876   -618    982   -454       O  
ATOM   1930  CB  SER A 304       3.109   5.418   2.876  1.00 44.73           C  
ANISOU 1930  CB  SER A 304     6526   5350   5119   -823   1064   -314       C  
ATOM   1931  OG  SER A 304       1.894   4.730   2.640  1.00 46.44           O  
ANISOU 1931  OG  SER A 304     6810   5422   5412   -908    982   -280       O  
ATOM   1932  N   LEU A 305       0.893   6.719   5.073  1.00 42.74           N  
ANISOU 1932  N   LEU A 305     6506   4932   4799   -704    961   -274       N  
ATOM   1933  CA  LEU A 305       0.132   6.322   6.267  1.00 40.66           C  
ANISOU 1933  CA  LEU A 305     6307   4551   4591   -632    892   -334       C  
ATOM   1934  C   LEU A 305      -1.022   5.412   5.874  1.00 42.08           C  
ANISOU 1934  C   LEU A 305     6549   4560   4879   -680    840   -348       C  
ATOM   1935  O   LEU A 305      -1.664   5.632   4.846  1.00 43.94           O  
ANISOU 1935  O   LEU A 305     6804   4730   5162   -784    809   -241       O  
ATOM   1936  CB  LEU A 305      -0.404   7.542   6.984  1.00 39.71           C  
ANISOU 1936  CB  LEU A 305     6233   4420   4435   -580    850   -245       C  
ATOM   1937  CG  LEU A 305       0.691   8.556   7.284  1.00 38.99           C  
ANISOU 1937  CG  LEU A 305     6127   4486   4203   -540    873   -244       C  
ATOM   1938  CD1 LEU A 305       0.089   9.880   7.705  1.00 40.09           C  
ANISOU 1938  CD1 LEU A 305     6338   4628   4267   -526    812   -119       C  
ATOM   1939  CD2 LEU A 305       1.621   8.031   8.361  1.00 38.09           C  
ANISOU 1939  CD2 LEU A 305     5966   4399   4107   -462    845   -369       C  
ATOM   1940  N   GLU A 306      -1.293   4.398   6.694  1.00 42.83           N  
ANISOU 1940  N   GLU A 306     6677   4583   5014   -604    826   -477       N  
ATOM   1941  CA  GLU A 306      -2.366   3.441   6.406  1.00 44.96           C  
ANISOU 1941  CA  GLU A 306     7046   4678   5359   -621    770   -546       C  
ATOM   1942  C   GLU A 306      -3.525   3.620   7.361  1.00 44.62           C  
ANISOU 1942  C   GLU A 306     7068   4484   5403   -501    732   -571       C  
ATOM   1943  O   GLU A 306      -3.332   3.784   8.553  1.00 42.32           O  
ANISOU 1943  O   GLU A 306     6724   4244   5111   -378    772   -599       O  
ATOM   1944  CB  GLU A 306      -1.858   2.009   6.494  1.00 46.42           C  
ANISOU 1944  CB  GLU A 306     7242   4902   5492   -614    798   -692       C  
ATOM   1945  CG  GLU A 306      -0.428   1.839   6.035  1.00 46.99           C  
ANISOU 1945  CG  GLU A 306     7209   5145   5498   -684    838   -671       C  
ATOM   1946  CD  GLU A 306      -0.250   2.169   4.567  1.00 50.19           C  
ANISOU 1946  CD  GLU A 306     7579   5555   5937   -828    804   -562       C  
ATOM   1947  OE1 GLU A 306      -1.111   1.756   3.764  1.00 50.12           O  
ANISOU 1947  OE1 GLU A 306     7644   5409   5989   -919    719   -544       O  
ATOM   1948  OE2 GLU A 306       0.757   2.835   4.208  1.00 55.31           O1-
ANISOU 1948  OE2 GLU A 306     8117   6337   6560   -846    857   -492       O1-
ATOM   1949  N   HIS A 307      -4.730   3.588   6.817  1.00 46.89           N  
ANISOU 1949  N   HIS A 307     7457   4567   5794   -540    637   -547       N  
ATOM   1950  CA  HIS A 307      -5.964   3.769   7.575  1.00 50.43           C  
ANISOU 1950  CA  HIS A 307     7973   4819   6371   -422    576   -566       C  
ATOM   1951  C   HIS A 307      -6.159   5.230   8.010  1.00 51.60           C  
ANISOU 1951  C   HIS A 307     8064   4984   6556   -409    538   -377       C  
ATOM   1952  O   HIS A 307      -7.082   5.937   7.557  1.00 54.15           O  
ANISOU 1952  O   HIS A 307     8436   5158   6981   -474    428   -231       O  
ATOM   1953  CB  HIS A 307      -6.011   2.812   8.759  1.00 51.91           C  
ANISOU 1953  CB  HIS A 307     8162   5009   6553   -237    661   -755       C  
ATOM   1954  CG  HIS A 307      -5.431   1.447   8.477  1.00 53.77           C  
ANISOU 1954  CG  HIS A 307     8436   5326   6666   -256    727   -917       C  
ATOM   1955  CD2 HIS A 307      -4.224   0.910   8.785  1.00 53.78           C  
ANISOU 1955  CD2 HIS A 307     8349   5545   6539   -258    829   -955       C  
ATOM   1956  ND1 HIS A 307      -6.136   0.445   7.845  1.00 56.29           N  
ANISOU 1956  ND1 HIS A 307     8916   5487   6985   -280    663  -1056       N  
ATOM   1957  CE1 HIS A 307      -5.384  -0.639   7.761  1.00 56.73           C  
ANISOU 1957  CE1 HIS A 307     8985   5679   6891   -301    729  -1166       C  
ATOM   1958  NE2 HIS A 307      -4.218  -0.393   8.338  1.00 55.18           N  
ANISOU 1958  NE2 HIS A 307     8628   5712   6625   -288    834  -1097       N  
ATOM   1959  N   VAL A 308      -5.256   5.701   8.848  1.00 50.78           N  
ANISOU 1959  N   VAL A 308     7863   5062   6369   -347    606   -361       N  
ATOM   1960  CA  VAL A 308      -5.255   7.096   9.229  1.00 51.70           C  
ANISOU 1960  CA  VAL A 308     7947   5228   6469   -353    552   -189       C  
ATOM   1961  C   VAL A 308      -6.628   7.482   9.789  1.00 54.04           C  
ANISOU 1961  C   VAL A 308     8286   5302   6945   -278    436   -115       C  
ATOM   1962  O   VAL A 308      -7.137   8.590   9.556  1.00 54.03           O  
ANISOU 1962  O   VAL A 308     8311   5256   6961   -347    337     81       O  
ATOM   1963  CB  VAL A 308      -4.922   8.014   8.044  1.00 51.45           C  
ANISOU 1963  CB  VAL A 308     7926   5300   6324   -513    551    -27       C  
ATOM   1964  CG1 VAL A 308      -4.366   9.321   8.570  1.00 54.55           C  
ANISOU 1964  CG1 VAL A 308     8295   5843   6589   -501    538     88       C  
ATOM   1965  CG2 VAL A 308      -3.904   7.383   7.122  1.00 50.26           C  
ANISOU 1965  CG2 VAL A 308     7737   5286   6075   -592    649   -103       C  
ATOM   1966  N   SER A 309      -7.201   6.570  10.563  1.00 52.47           N  
ANISOU 1966  N   SER A 309     8088   4972   6877   -126    453   -265       N  
ATOM   1967  CA  SER A 309      -8.573   6.704  10.974  1.00 54.81           C  
ANISOU 1967  CA  SER A 309     8429   5009   7386    -28    345   -236       C  
ATOM   1968  C   SER A 309      -8.943   8.042  11.665  1.00 56.33           C  
ANISOU 1968  C   SER A 309     8570   5173   7662    -11    223    -20       C  
ATOM   1969  O   SER A 309     -10.035   8.553  11.439  1.00 59.76           O  
ANISOU 1969  O   SER A 309     9063   5396   8248    -32     81    107       O  
ATOM   1970  CB  SER A 309      -8.977   5.496  11.827  1.00 55.67           C  
ANISOU 1970  CB  SER A 309     8529   5024   7598    178    431   -459       C  
ATOM   1971  OG  SER A 309      -8.665   4.275  11.152  1.00 55.23           O  
ANISOU 1971  OG  SER A 309     8554   5002   7427    144    519   -648       O  
ATOM   1972  N   TYR A 310      -8.071   8.616  12.490  1.00 54.81           N  
ANISOU 1972  N   TYR A 310     8276   5169   7379     14    243     37       N  
ATOM   1973  CA  TYR A 310      -8.450   9.833  13.230  1.00 56.70           C  
ANISOU 1973  CA  TYR A 310     8478   5371   7694     30     92    240       C  
ATOM   1974  C   TYR A 310      -7.837  11.079  12.598  1.00 56.19           C  
ANISOU 1974  C   TYR A 310     8469   5477   7401   -144     37    420       C  
ATOM   1975  O   TYR A 310      -7.594  12.085  13.269  1.00 55.38           O  
ANISOU 1975  O   TYR A 310     8346   5451   7245   -151    -69    556       O  
ATOM   1976  CB  TYR A 310      -8.127   9.709  14.737  1.00 58.34           C  
ANISOU 1976  CB  TYR A 310     8535   5625   8005    188     97    208       C  
ATOM   1977  CG  TYR A 310      -9.075   8.750  15.435  1.00 61.52           C  
ANISOU 1977  CG  TYR A 310     8874   5834   8666    393    144     86       C  
ATOM   1978  CD1 TYR A 310      -8.875   7.368  15.359  1.00 61.44           C  
ANISOU 1978  CD1 TYR A 310     8860   5854   8629    480    329   -148       C  
ATOM   1979  CD2 TYR A 310     -10.206   9.209  16.121  1.00 63.63           C  
ANISOU 1979  CD2 TYR A 310     9096   5883   9198    508      7    199       C  
ATOM   1980  CE1 TYR A 310      -9.760   6.472  15.949  1.00 61.81           C  
ANISOU 1980  CE1 TYR A 310     8875   5740   8872    693    402   -290       C  
ATOM   1981  CE2 TYR A 310     -11.091   8.309  16.723  1.00 63.86           C  
ANISOU 1981  CE2 TYR A 310     9069   5726   9470    732     76     57       C  
ATOM   1982  CZ  TYR A 310     -10.856   6.945  16.624  1.00 62.39           C  
ANISOU 1982  CZ  TYR A 310     8896   5593   9216    830    286   -199       C  
ATOM   1983  OH  TYR A 310     -11.686   6.032  17.183  1.00 62.11           O  
ANISOU 1983  OH  TYR A 310     8829   5402   9369   1070    386   -369       O  
ATOM   1984  N   ALA A 311      -7.612  11.027  11.288  1.00 55.68           N  
ANISOU 1984  N   ALA A 311     8477   5479   7199   -282    106    427       N  
ATOM   1985  CA  ALA A 311      -7.109  12.202  10.586  1.00 55.79           C  
ANISOU 1985  CA  ALA A 311     8541   5673   6983   -427     97    600       C  
ATOM   1986  C   ALA A 311      -8.137  13.315  10.648  1.00 58.19           C  
ANISOU 1986  C   ALA A 311     8897   5868   7346   -485    -76    863       C  
ATOM   1987  O   ALA A 311      -9.343  13.076  10.540  1.00 59.24           O  
ANISOU 1987  O   ALA A 311     9048   5750   7710   -477   -176    930       O  
ATOM   1988  CB  ALA A 311      -6.774  11.873   9.147  1.00 54.95           C  
ANISOU 1988  CB  ALA A 311     8458   5649   6768   -554    216    585       C  
ATOM   1989  N   ASP A 312      -7.641  14.532  10.836  1.00 59.46           N  
ANISOU 1989  N   ASP A 312     9095   6208   7291   -542   -127   1009       N  
ATOM   1990  CA  ASP A 312      -8.481  15.713  10.940  1.00 62.15           C  
ANISOU 1990  CA  ASP A 312     9495   6490   7628   -616   -305   1293       C  
ATOM   1991  C   ASP A 312      -7.811  16.848  10.185  1.00 63.86           C  
ANISOU 1991  C   ASP A 312     9797   6985   7483   -750   -245   1438       C  
ATOM   1992  O   ASP A 312      -6.794  16.630   9.506  1.00 63.83           O  
ANISOU 1992  O   ASP A 312     9789   7180   7282   -769    -57   1305       O  
ATOM   1993  CB  ASP A 312      -8.651  16.094  12.405  1.00 62.53           C  
ANISOU 1993  CB  ASP A 312     9505   6460   7791   -508   -480   1326       C  
ATOM   1994  CG  ASP A 312      -7.381  16.665  13.006  1.00 61.77           C  
ANISOU 1994  CG  ASP A 312     9429   6601   7438   -497   -480   1259       C  
ATOM   1995  OD1 ASP A 312      -6.288  16.404  12.444  1.00 60.52           O  
ANISOU 1995  OD1 ASP A 312     9289   6633   7070   -516   -308   1098       O  
ATOM   1996  OD2 ASP A 312      -7.489  17.388  14.015  1.00 63.16           O1-
ANISOU 1996  OD2 ASP A 312     9606   6755   7637   -472   -675   1372       O1-
ATOM   1997  N   GLU A 313      -8.387  18.046  10.294  1.00 66.70           N  
ANISOU 1997  N   GLU A 313    10230   7360   7751   -833   -399   1715       N  
ATOM   1998  CA  GLU A 313      -7.893  19.207   9.553  1.00 68.54           C  
ANISOU 1998  CA  GLU A 313    10562   7879   7603   -956   -328   1882       C  
ATOM   1999  C   GLU A 313      -6.374  19.375   9.650  1.00 66.85           C  
ANISOU 1999  C   GLU A 313    10391   7933   7076   -895   -184   1659       C  
ATOM   2000  O   GLU A 313      -5.687  19.633   8.659  1.00 65.85           O  
ANISOU 2000  O   GLU A 313    10290   8035   6696   -942     15   1642       O  
ATOM   2001  CB  GLU A 313      -8.611  20.486   9.974  1.00 72.40           C  
ANISOU 2001  CB  GLU A 313    11144   8364   8001  -1038   -550   2197       C  
ATOM   2002  CG  GLU A 313      -8.626  21.546   8.883  1.00 76.22           C  
ANISOU 2002  CG  GLU A 313    11714   9095   8149  -1200   -459   2463       C  
ATOM   2003  CD  GLU A 313      -8.570  22.968   9.417  1.00 80.74           C  
ANISOU 2003  CD  GLU A 313    12439   9835   8402  -1255   -618   2669       C  
ATOM   2004  OE1 GLU A 313      -7.794  23.229  10.360  1.00 83.03           O  
ANISOU 2004  OE1 GLU A 313    12800  10197   8548  -1163   -699   2498       O  
ATOM   2005  OE2 GLU A 313      -9.300  23.836   8.893  1.00 82.96           O1-
ANISOU 2005  OE2 GLU A 313    12775  10177   8569  -1403   -680   3018       O1-
ATOM   2006  N   GLU A 314      -5.851  19.198  10.848  1.00 67.07           N  
ANISOU 2006  N   GLU A 314    10411   7917   7155   -784   -290   1491       N  
ATOM   2007  CA  GLU A 314      -4.425  19.354  11.091  1.00 67.15           C  
ANISOU 2007  CA  GLU A 314    10471   8126   6916   -724   -216   1275       C  
ATOM   2008  C   GLU A 314      -3.589  18.321  10.363  1.00 62.17           C  
ANISOU 2008  C   GLU A 314     9758   7554   6309   -680     21   1040       C  
ATOM   2009  O   GLU A 314      -2.533  18.639   9.860  1.00 62.20           O  
ANISOU 2009  O   GLU A 314     9817   7763   6054   -670    155    927       O  
ATOM   2010  CB  GLU A 314      -4.148  19.240  12.574  1.00 70.45           C  
ANISOU 2010  CB  GLU A 314    10862   8437   7470   -634   -417   1181       C  
ATOM   2011  CG  GLU A 314      -2.885  19.954  12.985  1.00 77.21           C  
ANISOU 2011  CG  GLU A 314    11839   9473   8024   -614   -470   1055       C  
ATOM   2012  CD  GLU A 314      -2.521  19.649  14.434  1.00 80.88           C  
ANISOU 2012  CD  GLU A 314    12229   9814   8687   -541   -675    965       C  
ATOM   2013  OE1 GLU A 314      -3.469  19.395  15.236  1.00 80.97           O  
ANISOU 2013  OE1 GLU A 314    12125   9634   9004   -517   -824   1094       O  
ATOM   2014  OE2 GLU A 314      -1.301  19.675  14.756  1.00 81.11           O1-
ANISOU 2014  OE2 GLU A 314    12302   9929   8587   -506   -692    777       O1-
ATOM   2015  N   VAL A 315      -4.069  17.086  10.318  1.00 59.07           N  
ANISOU 2015  N   VAL A 315     9240   6977   6226   -648     63    961       N  
ATOM   2016  CA  VAL A 315      -3.353  15.993   9.675  1.00 55.25           C  
ANISOU 2016  CA  VAL A 315     8674   6528   5790   -620    252    757       C  
ATOM   2017  C   VAL A 315      -3.319  16.133   8.165  1.00 54.51           C  
ANISOU 2017  C   VAL A 315     8578   6560   5573   -717    428    840       C  
ATOM   2018  O   VAL A 315      -2.306  15.846   7.543  1.00 52.57           O  
ANISOU 2018  O   VAL A 315     8299   6457   5220   -699    589    703       O  
ATOM   2019  CB  VAL A 315      -4.009  14.642  10.014  1.00 54.72           C  
ANISOU 2019  CB  VAL A 315     8504   6233   6055   -565    237    662       C  
ATOM   2020  CG1 VAL A 315      -3.415  13.502   9.188  1.00 53.71           C  
ANISOU 2020  CG1 VAL A 315     8310   6137   5961   -570    409    492       C  
ATOM   2021  CG2 VAL A 315      -3.835  14.350  11.488  1.00 54.38           C  
ANISOU 2021  CG2 VAL A 315     8409   6108   6145   -451    120    567       C  
ATOM   2022  N   TRP A 316      -4.428  16.542   7.568  1.00 55.63           N  
ANISOU 2022  N   TRP A 316     8733   6639   5765   -822    390   1085       N  
ATOM   2023  CA  TRP A 316      -4.473  16.700   6.125  1.00 56.54           C  
ANISOU 2023  CA  TRP A 316     8809   6877   5798   -934    549   1221       C  
ATOM   2024  C   TRP A 316      -3.499  17.788   5.665  1.00 58.92           C  
ANISOU 2024  C   TRP A 316     9167   7497   5721   -932    700   1249       C  
ATOM   2025  O   TRP A 316      -2.724  17.570   4.737  1.00 56.96           O  
ANISOU 2025  O   TRP A 316     8848   7403   5389   -927    901   1177       O  
ATOM   2026  CB  TRP A 316      -5.889  17.039   5.662  1.00 58.81           C  
ANISOU 2026  CB  TRP A 316     9098   7022   6225  -1067    439   1523       C  
ATOM   2027  CG  TRP A 316      -6.946  16.091   6.156  1.00 58.36           C  
ANISOU 2027  CG  TRP A 316     9019   6624   6533  -1044    272   1481       C  
ATOM   2028  CD1 TRP A 316      -6.843  14.731   6.291  1.00 56.06           C  
ANISOU 2028  CD1 TRP A 316     8674   6178   6447   -968    294   1236       C  
ATOM   2029  CD2 TRP A 316      -8.282  16.434   6.557  1.00 60.94           C  
ANISOU 2029  CD2 TRP A 316     9384   6716   7053  -1084     59   1686       C  
ATOM   2030  CE2 TRP A 316      -8.926  15.231   6.933  1.00 60.06           C  
ANISOU 2030  CE2 TRP A 316     9245   6308   7268  -1004    -23   1519       C  
ATOM   2031  CE3 TRP A 316      -9.001  17.642   6.627  1.00 63.71           C  
ANISOU 2031  CE3 TRP A 316     9796   7079   7330  -1177    -75   2002       C  
ATOM   2032  NE1 TRP A 316      -8.028  14.209   6.766  1.00 56.91           N  
ANISOU 2032  NE1 TRP A 316     8798   5980   6845   -939    129   1247       N  
ATOM   2033  CZ2 TRP A 316     -10.240  15.207   7.385  1.00 61.91           C  
ANISOU 2033  CZ2 TRP A 316     9506   6239   7779   -990   -231   1631       C  
ATOM   2034  CZ3 TRP A 316     -10.302  17.617   7.077  1.00 65.00           C  
ANISOU 2034  CZ3 TRP A 316     9975   6937   7786  -1187   -304   2145       C  
ATOM   2035  CH2 TRP A 316     -10.909  16.408   7.452  1.00 64.90           C  
ANISOU 2035  CH2 TRP A 316     9927   6610   8122  -1084   -378   1949       C  
ATOM   2036  N   GLU A 317      -3.526  18.951   6.320  1.00 62.84           N  
ANISOU 2036  N   GLU A 317     9798   8090   5988   -922    598   1345       N  
ATOM   2037  CA  GLU A 317      -2.643  20.063   5.946  1.00 66.46           C  
ANISOU 2037  CA  GLU A 317    10359   8859   6034   -902    736   1349       C  
ATOM   2038  C   GLU A 317      -1.185  19.672   6.065  1.00 64.39           C  
ANISOU 2038  C   GLU A 317    10095   8691   5678   -765    851   1019       C  
ATOM   2039  O   GLU A 317      -0.332  20.146   5.320  1.00 68.11           O  
ANISOU 2039  O   GLU A 317    10587   9399   5894   -721   1056    960       O  
ATOM   2040  CB  GLU A 317      -2.892  21.299   6.814  1.00 71.42           C  
ANISOU 2040  CB  GLU A 317    11169   9547   6419   -914    549   1474       C  
ATOM   2041  CG  GLU A 317      -4.275  21.916   6.673  1.00 77.21           C  
ANISOU 2041  CG  GLU A 317    11921  10214   7200  -1058    419   1845       C  
ATOM   2042  CD  GLU A 317      -4.695  22.116   5.232  1.00 81.44           C  
ANISOU 2042  CD  GLU A 317    12370  10892   7683  -1182    622   2095       C  
ATOM   2043  OE1 GLU A 317      -3.972  22.848   4.521  1.00 84.40           O  
ANISOU 2043  OE1 GLU A 317    12788  11584   7698  -1171    844   2114       O  
ATOM   2044  OE2 GLU A 317      -5.742  21.546   4.819  1.00 82.86           O1-
ANISOU 2044  OE2 GLU A 317    12435  10861   8186  -1286    556   2273       O1-
ATOM   2045  N   LEU A 318      -0.898  18.785   7.001  1.00 61.30           N  
ANISOU 2045  N   LEU A 318     9669   8111   5510   -692    724    814       N  
ATOM   2046  CA  LEU A 318       0.448  18.265   7.151  1.00 59.93           C  
ANISOU 2046  CA  LEU A 318     9474   7981   5316   -581    796    524       C  
ATOM   2047  C   LEU A 318       0.810  17.327   6.007  1.00 60.14           C  
ANISOU 2047  C   LEU A 318     9342   8032   5476   -587   1006    461       C  
ATOM   2048  O   LEU A 318       1.829  17.519   5.354  1.00 64.85           O  
ANISOU 2048  O   LEU A 318     9928   8795   5917   -523   1175    346       O  
ATOM   2049  CB  LEU A 318       0.622  17.528   8.478  1.00 57.12           C  
ANISOU 2049  CB  LEU A 318     9093   7427   5181   -522    602    371       C  
ATOM   2050  CG  LEU A 318       1.145  18.364   9.648  1.00 56.98           C  
ANISOU 2050  CG  LEU A 318     9220   7427   5004   -471    402    305       C  
ATOM   2051  CD1 LEU A 318       0.961  17.584  10.932  1.00 54.97           C  
ANISOU 2051  CD1 LEU A 318     8877   6964   5046   -442    211    254       C  
ATOM   2052  CD2 LEU A 318       2.608  18.720   9.463  1.00 56.96           C  
ANISOU 2052  CD2 LEU A 318     9306   7568   4770   -385    474     81       C  
ATOM   2053  N   MET A 319      -0.014  16.310   5.779  1.00 57.77           N  
ANISOU 2053  N   MET A 319     8926   7556   5470   -656    980    527       N  
ATOM   2054  CA  MET A 319       0.308  15.299   4.788  1.00 54.60           C  
ANISOU 2054  CA  MET A 319     8379   7145   5221   -678   1121    467       C  
ATOM   2055  C   MET A 319       0.555  15.942   3.426  1.00 56.08           C  
ANISOU 2055  C   MET A 319     8508   7552   5246   -720   1335    601       C  
ATOM   2056  O   MET A 319       1.411  15.468   2.672  1.00 54.98           O  
ANISOU 2056  O   MET A 319     8259   7493   5137   -683   1482    500       O  
ATOM   2057  CB  MET A 319      -0.801  14.269   4.731  1.00 54.86           C  
ANISOU 2057  CB  MET A 319     8345   6948   5548   -760   1028    536       C  
ATOM   2058  CG  MET A 319      -0.981  13.519   6.042  1.00 53.27           C  
ANISOU 2058  CG  MET A 319     8169   6560   5511   -687    871    390       C  
ATOM   2059  SD  MET A 319      -2.164  12.152   5.965  1.00 53.52           S  
ANISOU 2059  SD  MET A 319     8152   6324   5860   -735    791    390       S  
ATOM   2060  CE  MET A 319      -1.322  11.093   4.780  1.00 51.50           C  
ANISOU 2060  CE  MET A 319     7786   6132   5649   -780    930    284       C  
ATOM   2061  N   LYS A 320      -0.169  17.035   3.129  1.00 57.48           N  
ANISOU 2061  N   LYS A 320     8747   7836   5256   -793   1354    846       N  
ATOM   2062  CA  LYS A 320       0.074  17.825   1.904  1.00 59.07           C  
ANISOU 2062  CA  LYS A 320     8886   8303   5253   -822   1591   1008       C  
ATOM   2063  C   LYS A 320       1.383  18.559   2.010  1.00 59.77           C  
ANISOU 2063  C   LYS A 320     9064   8619   5027   -662   1733    809       C  
ATOM   2064  O   LYS A 320       2.237  18.403   1.163  1.00 58.35           O  
ANISOU 2064  O   LYS A 320     8771   8576   4823   -593   1941    726       O  
ATOM   2065  CB  LYS A 320      -1.035  18.857   1.636  1.00 61.37           C  
ANISOU 2065  CB  LYS A 320     9230   8674   5415   -951   1569   1351       C  
ATOM   2066  CG  LYS A 320      -2.423  18.269   1.487  1.00 61.59           C  
ANISOU 2066  CG  LYS A 320     9190   8448   5765  -1112   1401   1570       C  
ATOM   2067  CD  LYS A 320      -3.427  19.271   0.935  1.00 65.02           C  
ANISOU 2067  CD  LYS A 320     9630   8976   6099  -1264   1401   1964       C  
ATOM   2068  CE  LYS A 320      -3.700  20.423   1.897  1.00 66.70           C  
ANISOU 2068  CE  LYS A 320    10044   9253   6046  -1243   1273   2043       C  
ATOM   2069  NZ  LYS A 320      -4.458  21.538   1.248  1.00 70.29           N1+
ANISOU 2069  NZ  LYS A 320    10507   9881   6317  -1392   1318   2450       N1+
ATOM   2070  N   GLU A 321       1.511  19.373   3.054  1.00 62.02           N  
ANISOU 2070  N   GLU A 321     9555   8926   5083   -603   1598    735       N  
ATOM   2071  CA  GLU A 321       2.663  20.234   3.244  1.00 65.54           C  
ANISOU 2071  CA  GLU A 321    10148   9567   5185   -453   1687    537       C  
ATOM   2072  C   GLU A 321       3.927  19.397   3.187  1.00 64.27           C  
ANISOU 2072  C   GLU A 321     9907   9351   5159   -320   1748    231       C  
ATOM   2073  O   GLU A 321       4.935  19.840   2.685  1.00 66.20           O  
ANISOU 2073  O   GLU A 321    10175   9771   5208   -189   1930     84       O  
ATOM   2074  CB  GLU A 321       2.551  20.966   4.587  1.00 68.04           C  
ANISOU 2074  CB  GLU A 321    10700   9826   5325   -436   1429    486       C  
ATOM   2075  CG  GLU A 321       3.000  22.424   4.613  1.00 75.51           C  
ANISOU 2075  CG  GLU A 321    11875  11029   5784   -366   1489    469       C  
ATOM   2076  CD  GLU A 321       1.810  23.426   4.790  1.00 79.73           C  
ANISOU 2076  CD  GLU A 321    12527  11640   6125   -504   1383    801       C  
ATOM   2077  OE1 GLU A 321       0.787  23.080   5.459  1.00 78.24           O  
ANISOU 2077  OE1 GLU A 321    12306  11228   6196   -618   1145    961       O  
ATOM   2078  OE2 GLU A 321       1.894  24.567   4.250  1.00 79.23           O1-
ANISOU 2078  OE2 GLU A 321    12588  11867   5648   -492   1543    910       O1-
ATOM   2079  N   LYS A 322       3.861  18.177   3.696  1.00 63.20           N  
ANISOU 2079  N   LYS A 322     9678   8972   5361   -352   1597    142       N  
ATOM   2080  CA  LYS A 322       5.013  17.272   3.716  1.00 63.48           C  
ANISOU 2080  CA  LYS A 322     9629   8931   5558   -254   1613   -110       C  
ATOM   2081  C   LYS A 322       4.987  16.199   2.629  1.00 59.97           C  
ANISOU 2081  C   LYS A 322     8951   8455   5380   -308   1748    -52       C  
ATOM   2082  O   LYS A 322       5.948  15.458   2.476  1.00 58.53           O  
ANISOU 2082  O   LYS A 322     8679   8225   5334   -237   1773   -225       O  
ATOM   2083  CB  LYS A 322       5.146  16.608   5.099  1.00 65.69           C  
ANISOU 2083  CB  LYS A 322     9961   8988   6010   -247   1351   -252       C  
ATOM   2084  CG  LYS A 322       5.852  17.488   6.133  1.00 71.48           C  
ANISOU 2084  CG  LYS A 322    10899   9737   6524   -154   1200   -411       C  
ATOM   2085  CD  LYS A 322       6.086  16.779   7.455  1.00 72.79           C  
ANISOU 2085  CD  LYS A 322    11062   9692   6902   -156    949   -519       C  
ATOM   2086  CE  LYS A 322       6.277  17.795   8.564  1.00 76.15           C  
ANISOU 2086  CE  LYS A 322    11692  10108   7133   -127    730   -568       C  
ATOM   2087  NZ  LYS A 322       7.478  17.467   9.363  1.00 78.54           N1+
ANISOU 2087  NZ  LYS A 322    12021  10297   7524    -56    567   -790       N1+
ATOM   2088  N   GLY A 323       3.902  16.099   1.878  1.00 58.71           N  
ANISOU 2088  N   GLY A 323     8693   8304   5311   -445   1802    204       N  
ATOM   2089  CA  GLY A 323       3.873  15.192   0.738  1.00 56.83           C  
ANISOU 2089  CA  GLY A 323     8236   8046   5310   -514   1908    285       C  
ATOM   2090  C   GLY A 323       3.854  13.731   1.148  1.00 52.28           C  
ANISOU 2090  C   GLY A 323     7601   7233   5029   -557   1746    173       C  
ATOM   2091  O   GLY A 323       4.654  12.912   0.685  1.00 48.46           O  
ANISOU 2091  O   GLY A 323     6993   6730   4691   -527   1789     68       O  
ATOM   2092  N   ILE A 324       2.900  13.417   2.009  1.00 51.44           N  
ANISOU 2092  N   ILE A 324     7583   6954   5007   -624   1562    208       N  
ATOM   2093  CA  ILE A 324       2.742  12.085   2.526  1.00 49.90           C  
ANISOU 2093  CA  ILE A 324     7362   6556   5042   -651   1421    103       C  
ATOM   2094  C   ILE A 324       1.517  11.421   1.924  1.00 49.88           C  
ANISOU 2094  C   ILE A 324     7306   6415   5230   -796   1363    265       C  
ATOM   2095  O   ILE A 324       0.421  11.984   1.926  1.00 51.34           O  
ANISOU 2095  O   ILE A 324     7547   6555   5403   -868   1312    438       O  
ATOM   2096  CB  ILE A 324       2.608  12.139   4.050  1.00 49.37           C  
ANISOU 2096  CB  ILE A 324     7423   6385   4951   -589   1260     -4       C  
ATOM   2097  CG1 ILE A 324       3.862  12.804   4.634  1.00 49.45           C  
ANISOU 2097  CG1 ILE A 324     7501   6502   4787   -463   1269   -167       C  
ATOM   2098  CG2 ILE A 324       2.395  10.741   4.625  1.00 47.84           C  
ANISOU 2098  CG2 ILE A 324     7195   6012   4971   -604   1151   -101       C  
ATOM   2099  CD1 ILE A 324       3.705  13.300   6.048  1.00 48.99           C  
ANISOU 2099  CD1 ILE A 324     7569   6380   4663   -419   1099   -208       C  
ATOM   2100  N   LEU A 325       1.717  10.205   1.434  1.00 48.76           N  
ANISOU 2100  N   LEU A 325     7070   6188   5269   -844   1342    207       N  
ATOM   2101  CA  LEU A 325       0.650   9.406   0.843  1.00 48.78           C  
ANISOU 2101  CA  LEU A 325     7047   6027   5460   -984   1248    316       C  
ATOM   2102  C   LEU A 325      -0.342   8.952   1.902  1.00 47.42           C  
ANISOU 2102  C   LEU A 325     7010   5652   5356   -972   1089    253       C  
ATOM   2103  O   LEU A 325       0.058   8.487   2.970  1.00 46.83           O  
ANISOU 2103  O   LEU A 325     6986   5543   5265   -872   1049     76       O  
ATOM   2104  CB  LEU A 325       1.247   8.169   0.189  1.00 48.57           C  
ANISOU 2104  CB  LEU A 325     6916   5963   5577  -1028   1234    239       C  
ATOM   2105  CG  LEU A 325       0.331   7.362  -0.715  1.00 51.08           C  
ANISOU 2105  CG  LEU A 325     7198   6127   6082  -1193   1125    358       C  
ATOM   2106  CD1 LEU A 325      -0.105   8.208  -1.910  1.00 53.95           C  
ANISOU 2106  CD1 LEU A 325     7443   6574   6482  -1307   1197    632       C  
ATOM   2107  CD2 LEU A 325       1.045   6.094  -1.170  1.00 50.44           C  
ANISOU 2107  CD2 LEU A 325     7040   6015   6110  -1230   1078    259       C  
ATOM   2108  N   TYR A 326      -1.629   9.079   1.590  1.00 46.92           N  
ANISOU 2108  N   TYR A 326     6988   5449   5391  -1071    999    408       N  
ATOM   2109  CA  TYR A 326      -2.711   8.644   2.466  1.00 44.84           C  
ANISOU 2109  CA  TYR A 326     6845   4962   5231  -1044    850    351       C  
ATOM   2110  C   TYR A 326      -3.299   7.422   1.794  1.00 45.60           C  
ANISOU 2110  C   TYR A 326     6951   4872   5504  -1142    748    317       C  
ATOM   2111  O   TYR A 326      -3.658   7.471   0.616  1.00 46.14           O  
ANISOU 2111  O   TYR A 326     6958   4912   5663  -1290    719    487       O  
ATOM   2112  CB  TYR A 326      -3.756   9.754   2.566  1.00 45.63           C  
ANISOU 2112  CB  TYR A 326     7000   5008   5328  -1085    787    560       C  
ATOM   2113  CG  TYR A 326      -4.914   9.530   3.512  1.00 44.81           C  
ANISOU 2113  CG  TYR A 326     7007   4662   5355  -1032    631    524       C  
ATOM   2114  CD1 TYR A 326      -5.804   8.493   3.312  1.00 45.55           C  
ANISOU 2114  CD1 TYR A 326     7157   4507   5645  -1066    509    457       C  
ATOM   2115  CD2 TYR A 326      -5.148  10.399   4.579  1.00 44.50           C  
ANISOU 2115  CD2 TYR A 326     7022   4633   5253   -942    590    561       C  
ATOM   2116  CE1 TYR A 326      -6.879   8.305   4.168  1.00 47.59           C  
ANISOU 2116  CE1 TYR A 326     7513   4530   6037   -983    382    405       C  
ATOM   2117  CE2 TYR A 326      -6.218  10.224   5.440  1.00 45.64           C  
ANISOU 2117  CE2 TYR A 326     7237   4548   5555   -874    450    543       C  
ATOM   2118  CZ  TYR A 326      -7.093   9.173   5.235  1.00 47.97           C  
ANISOU 2118  CZ  TYR A 326     7580   4594   6052   -882    359    457       C  
ATOM   2119  OH  TYR A 326      -8.190   8.954   6.082  1.00 51.29           O  
ANISOU 2119  OH  TYR A 326     8071   4764   6652   -780    231    411       O  
ATOM   2120  N   VAL A 327      -3.358   6.315   2.524  1.00 45.05           N  
ANISOU 2120  N   VAL A 327     6955   4688   5473  -1064    692    106       N  
ATOM   2121  CA  VAL A 327      -3.957   5.086   2.028  1.00 45.92           C  
ANISOU 2121  CA  VAL A 327     7131   4611   5708  -1138    574     28       C  
ATOM   2122  C   VAL A 327      -5.003   4.662   3.033  1.00 46.33           C  
ANISOU 2122  C   VAL A 327     7328   4453   5823  -1030    484   -104       C  
ATOM   2123  O   VAL A 327      -4.664   4.217   4.102  1.00 47.62           O  
ANISOU 2123  O   VAL A 327     7514   4658   5921   -887    542   -271       O  
ATOM   2124  CB  VAL A 327      -2.924   3.962   1.915  1.00 44.92           C  
ANISOU 2124  CB  VAL A 327     6967   4574   5528  -1131    613   -129       C  
ATOM   2125  CG1 VAL A 327      -3.580   2.695   1.366  1.00 46.31           C  
ANISOU 2125  CG1 VAL A 327     7246   4557   5794  -1221    465   -212       C  
ATOM   2126  CG2 VAL A 327      -1.721   4.400   1.085  1.00 44.50           C  
ANISOU 2126  CG2 VAL A 327     6747   4732   5430  -1188    721    -26       C  
ATOM   2127  N   ALA A 328      -6.269   4.786   2.686  1.00 48.41           N  
ANISOU 2127  N   ALA A 328     7675   4484   6232  -1093    341    -19       N  
ATOM   2128  CA  ALA A 328      -7.335   4.568   3.641  1.00 49.50           C  
ANISOU 2128  CA  ALA A 328     7942   4403   6462   -961    259   -133       C  
ATOM   2129  C   ALA A 328      -7.547   3.093   3.993  1.00 50.26           C  
ANISOU 2129  C   ALA A 328     8163   4377   6556   -872    231   -409       C  
ATOM   2130  O   ALA A 328      -7.797   2.776   5.136  1.00 48.68           O  
ANISOU 2130  O   ALA A 328     8008   4140   6347   -687    281   -566       O  
ATOM   2131  CB  ALA A 328      -8.625   5.152   3.104  1.00 53.26           C  
ANISOU 2131  CB  ALA A 328     8478   4636   7124  -1061     86     49       C  
ATOM   2132  N   THR A 329      -7.490   2.196   3.008  1.00 53.12           N  
ANISOU 2132  N   THR A 329     8579   4678   6925  -1002    145   -459       N  
ATOM   2133  CA  THR A 329      -7.793   0.780   3.245  1.00 54.96           C  
ANISOU 2133  CA  THR A 329     8977   4788   7116   -930     95   -725       C  
ATOM   2134  C   THR A 329      -9.197   0.587   3.808  1.00 56.72           C  
ANISOU 2134  C   THR A 329     9374   4710   7468   -799    -11   -856       C  
ATOM   2135  O   THR A 329      -9.395   0.033   4.879  1.00 58.68           O  
ANISOU 2135  O   THR A 329     9690   4946   7659   -590     81  -1065       O  
ATOM   2136  CB  THR A 329      -6.777   0.149   4.205  1.00 54.93           C  
ANISOU 2136  CB  THR A 329     8926   5019   6925   -787    282   -886       C  
ATOM   2137  CG2 THR A 329      -6.832  -1.350   4.119  1.00 57.42           C  
ANISOU 2137  CG2 THR A 329     9399   5285   7134   -772    243  -1113       C  
ATOM   2138  OG1 THR A 329      -5.451   0.587   3.871  1.00 54.89           O  
ANISOU 2138  OG1 THR A 329     8742   5275   6838   -873    381   -752       O  
ATOM   2139  N   ARG A 330     -10.184   1.054   3.068  1.00 57.89           N  
ANISOU 2139  N   ARG A 330     9581   4606   7809   -920   -208   -720       N  
ATOM   2140  CA  ARG A 330     -11.531   1.100   3.566  1.00 58.95           C  
ANISOU 2140  CA  ARG A 330     9861   4421   8117   -796   -334   -805       C  
ATOM   2141  C   ARG A 330     -12.142  -0.272   3.494  1.00 61.59           C  
ANISOU 2141  C   ARG A 330    10437   4529   8434   -728   -445  -1113       C  
ATOM   2142  O   ARG A 330     -12.952  -0.627   4.355  1.00 63.88           O  
ANISOU 2142  O   ARG A 330    10858   4636   8777   -505   -440  -1325       O  
ATOM   2143  CB  ARG A 330     -12.353   2.089   2.749  1.00 59.78           C  
ANISOU 2143  CB  ARG A 330     9941   4321   8450   -976   -535   -517       C  
ATOM   2144  CG  ARG A 330     -13.784   2.276   3.226  1.00 61.26           C  
ANISOU 2144  CG  ARG A 330    10267   4137   8872   -859   -706   -562       C  
ATOM   2145  CD  ARG A 330     -13.925   2.914   4.602  1.00 59.30           C  
ANISOU 2145  CD  ARG A 330     9946   3943   8642   -623   -570   -576       C  
ATOM   2146  NE  ARG A 330     -15.343   2.932   4.954  1.00 61.26           N  
ANISOU 2146  NE  ARG A 330    10333   3789   9155   -504   -760   -640       N  
ATOM   2147  CZ  ARG A 330     -15.878   3.501   6.014  1.00 61.08           C  
ANISOU 2147  CZ  ARG A 330    10267   3680   9263   -310   -738   -621       C  
ATOM   2148  NH1 ARG A 330     -15.124   4.121   6.884  1.00 58.91           N1+
ANISOU 2148  NH1 ARG A 330     9817   3698   8867   -221   -544   -536       N1+
ATOM   2149  NH2 ARG A 330     -17.187   3.433   6.199  1.00 64.46           N  
ANISOU 2149  NH2 ARG A 330    10828   3700   9965   -204   -938   -689       N  
ATOM   2150  N   SER A 331     -11.752  -1.044   2.483  1.00 62.95           N  
ANISOU 2150  N   SER A 331    10672   4718   8529   -908   -547  -1142       N  
ATOM   2151  CA  SER A 331     -12.353  -2.363   2.235  1.00 67.26           C  
ANISOU 2151  CA  SER A 331    11493   5033   9030   -883   -707  -1432       C  
ATOM   2152  C   SER A 331     -12.574  -3.143   3.511  1.00 68.02           C  
ANISOU 2152  C   SER A 331    11724   5145   8977   -573   -536  -1766       C  
ATOM   2153  O   SER A 331     -13.676  -3.596   3.774  1.00 71.56           O  
ANISOU 2153  O   SER A 331    12394   5288   9507   -429   -649  -1989       O  
ATOM   2154  CB  SER A 331     -11.496  -3.202   1.281  1.00 67.42           C  
ANISOU 2154  CB  SER A 331    11525   5195   8899  -1084   -771  -1432       C  
ATOM   2155  OG  SER A 331     -11.609  -2.732  -0.046  1.00 70.00           O  
ANISOU 2155  OG  SER A 331    11770   5412   9414  -1371   -990  -1159       O  
ATOM   2156  N   VAL A 332     -11.529  -3.282   4.311  1.00 66.68           N  
ANISOU 2156  N   VAL A 332    11409   5325   8602   -462   -262  -1792       N  
ATOM   2157  CA  VAL A 332     -11.608  -4.064   5.532  1.00 68.85           C  
ANISOU 2157  CA  VAL A 332    11762   5678   8719   -177    -60  -2067       C  
ATOM   2158  C   VAL A 332     -12.830  -3.654   6.377  1.00 71.04           C  
ANISOU 2158  C   VAL A 332    12095   5694   9202     66    -62  -2165       C  
ATOM   2159  O   VAL A 332     -13.687  -4.511   6.717  1.00 77.23           O  
ANISOU 2159  O   VAL A 332    13109   6273   9959    260    -82  -2469       O  
ATOM   2160  CB  VAL A 332     -10.265  -3.998   6.295  1.00 67.11           C  
ANISOU 2160  CB  VAL A 332    11309   5870   8318   -128    214  -1984       C  
ATOM   2161  CG1 VAL A 332     -10.010  -2.633   6.916  1.00 66.17           C  
ANISOU 2161  CG1 VAL A 332    10941   5853   8348    -90    311  -1748       C  
ATOM   2162  CG2 VAL A 332     -10.201  -5.087   7.351  1.00 69.64           C  
ANISOU 2162  CG2 VAL A 332    11708   6323   8429    115    424  -2246       C  
ATOM   2163  N   ILE A 333     -12.960  -2.357   6.651  1.00 67.91           N  
ANISOU 2163  N   ILE A 333    11508   5282   9011     56    -63  -1915       N  
ATOM   2164  CA  ILE A 333     -14.055  -1.843   7.488  1.00 68.09           C  
ANISOU 2164  CA  ILE A 333    11540   5062   9268    278    -82  -1953       C  
ATOM   2165  C   ILE A 333     -15.422  -2.200   6.884  1.00 68.67           C  
ANISOU 2165  C   ILE A 333    11883   4676   9532    285   -356  -2107       C  
ATOM   2166  O   ILE A 333     -16.239  -2.847   7.529  1.00 70.14           O  
ANISOU 2166  O   ILE A 333    12231   4664   9757    550   -329  -2396       O  
ATOM   2167  CB  ILE A 333     -13.915  -0.324   7.729  1.00 66.74           C  
ANISOU 2167  CB  ILE A 333    11133   4957   9266    208    -89  -1611       C  
ATOM   2168  CG1 ILE A 333     -12.652  -0.059   8.557  1.00 64.10           C  
ANISOU 2168  CG1 ILE A 333    10567   5030   8757    258    167  -1524       C  
ATOM   2169  CG2 ILE A 333     -15.135   0.228   8.454  1.00 69.86           C  
ANISOU 2169  CG2 ILE A 333    11543   5053   9947    405   -173  -1611       C  
ATOM   2170  CD1 ILE A 333     -12.332   1.403   8.763  1.00 63.08           C  
ANISOU 2170  CD1 ILE A 333    10237   5009   8723    174    154  -1209       C  
ATOM   2171  N   GLU A 334     -15.638  -1.835   5.629  1.00105.07           N  
ANISOU 2171  N   GLU A 334    15153  12870  11898   1528   -586   1275       N  
ATOM   2172  CA  GLU A 334     -16.921  -2.111   4.984  1.00103.11           C  
ANISOU 2172  CA  GLU A 334    14964  12614  11600   1538   -564   1323       C  
ATOM   2173  C   GLU A 334     -17.214  -3.605   4.881  1.00102.03           C  
ANISOU 2173  C   GLU A 334    14831  12506  11429   1291   -429   1329       C  
ATOM   2174  O   GLU A 334     -18.368  -3.992   4.998  1.00102.26           O  
ANISOU 2174  O   GLU A 334    14846  12536  11472   1276   -392   1254       O  
ATOM   2175  CB  GLU A 334     -16.990  -1.478   3.595  1.00101.77           C  
ANISOU 2175  CB  GLU A 334    14930  12417  11323   1647   -624   1550       C  
ATOM   2176  CG  GLU A 334     -16.784   0.026   3.580  1.00101.39           C  
ANISOU 2176  CG  GLU A 334    14905  12329  11290   1894   -752   1559       C  
ATOM   2177  CD  GLU A 334     -17.946   0.827   4.058  1.00101.40           C  
ANISOU 2177  CD  GLU A 334    14885  12299  11344   2085   -826   1423       C  
ATOM   2178  OE1 GLU A 334     -18.199   0.926   5.261  1.00101.99           O  
ANISOU 2178  OE1 GLU A 334    14849  12376  11528   2121   -846   1209       O  
ATOM   2179  OE2 GLU A 334     -18.555   1.438   3.200  1.00101.03           O1-
ANISOU 2179  OE2 GLU A 334    14937  12217  11231   2211   -873   1535       O1-
ATOM   2180  N   ILE A 335     -16.189  -4.429   4.638  1.00100.78           N  
ANISOU 2180  N   ILE A 335    14700  12369  11223   1101   -363   1421       N  
ATOM   2181  CA  ILE A 335     -16.380  -5.886   4.522  1.00100.26           C  
ANISOU 2181  CA  ILE A 335    14657  12323  11113    854   -237   1435       C  
ATOM   2182  C   ILE A 335     -16.936  -6.442   5.827  1.00101.06           C  
ANISOU 2182  C   ILE A 335    14642  12438  11318    776   -157   1186       C  
ATOM   2183  O   ILE A 335     -17.805  -7.324   5.821  1.00101.26           O  
ANISOU 2183  O   ILE A 335    14677  12467  11328    658    -71   1146       O  
ATOM   2184  CB  ILE A 335     -15.075  -6.664   4.146  1.00 99.62           C  
ANISOU 2184  CB  ILE A 335    14630  12254  10968    659   -185   1564       C  
ATOM   2185  CG1 ILE A 335     -14.638  -6.371   2.702  1.00 98.36           C  
ANISOU 2185  CG1 ILE A 335    14592  12077  10704    696   -246   1824       C  
ATOM   2186  CG2 ILE A 335     -15.262  -8.177   4.289  1.00 99.79           C  
ANISOU 2186  CG2 ILE A 335    14671  12290  10954    399    -53   1535       C  
ATOM   2187  CD1 ILE A 335     -13.172  -6.665   2.420  1.00 97.93           C  
ANISOU 2187  CD1 ILE A 335    14574  12024  10611    582   -244   1941       C  
ATOM   2188  N   PHE A 336     -16.453  -5.930   6.949  1.00101.22           N  
ANISOU 2188  N   PHE A 336    14549  12459  11450    842   -184   1014       N  
ATOM   2189  CA  PHE A 336     -16.844  -6.522   8.208  1.00102.24           C  
ANISOU 2189  CA  PHE A 336    14559  12596  11691    750    -95    772       C  
ATOM   2190  C   PHE A 336     -18.050  -5.834   8.839  1.00102.00           C  
ANISOU 2190  C   PHE A 336    14443  12547  11765    927   -152    599       C  
ATOM   2191  O   PHE A 336     -18.794  -6.477   9.560  1.00102.83           O  
ANISOU 2191  O   PHE A 336    14476  12654  11943    844    -68    431       O  
ATOM   2192  CB  PHE A 336     -15.646  -6.624   9.130  1.00103.47           C  
ANISOU 2192  CB  PHE A 336    14635  12762  11919    672    -66    670       C  
ATOM   2193  CG  PHE A 336     -14.623  -7.630   8.666  1.00103.97           C  
ANISOU 2193  CG  PHE A 336    14778  12840  11883    444     21    805       C  
ATOM   2194  CD1 PHE A 336     -14.942  -8.997   8.577  1.00104.61           C  
ANISOU 2194  CD1 PHE A 336    14904  12928  11913    208    157    806       C  
ATOM   2195  CD2 PHE A 336     -13.342  -7.222   8.289  1.00103.89           C  
ANISOU 2195  CD2 PHE A 336    14809  12834  11832    462    -37    936       C  
ATOM   2196  CE1 PHE A 336     -14.003  -9.931   8.133  1.00104.42           C  
ANISOU 2196  CE1 PHE A 336    14970  12910  11794     -2    227    935       C  
ATOM   2197  CE2 PHE A 336     -12.398  -8.155   7.853  1.00103.74           C  
ANISOU 2197  CE2 PHE A 336    14867  12822  11724    252     34   1062       C  
ATOM   2198  CZ  PHE A 336     -12.729  -9.508   7.776  1.00103.98           C  
ANISOU 2198  CZ  PHE A 336    14950  12857  11701     21    162   1061       C  
ATOM   2199  N   LEU A 337     -18.268  -4.554   8.545  1.00100.88           N  
ANISOU 2199  N   LEU A 337    14321  12382  11628   1170   -292    640       N  
ATOM   2200  CA  LEU A 337     -19.531  -3.905   8.894  1.00100.74           C  
ANISOU 2200  CA  LEU A 337    14258  12338  11681   1346   -359    513       C  
ATOM   2201  C   LEU A 337     -20.701  -4.682   8.292  1.00100.31           C  
ANISOU 2201  C   LEU A 337    14261  12289  11560   1261   -286    562       C  
ATOM   2202  O   LEU A 337     -21.699  -4.924   8.973  1.00101.03           O  
ANISOU 2202  O   LEU A 337    14274  12373  11739   1264   -253    388       O  
ATOM   2203  CB  LEU A 337     -19.568  -2.457   8.394  1.00100.03           C  
ANISOU 2203  CB  LEU A 337    14227  12216  11565   1606   -519    601       C  
ATOM   2204  CG  LEU A 337     -18.943  -1.409   9.313  1.00100.42           C  
ANISOU 2204  CG  LEU A 337    14192  12243  11721   1766   -625    467       C  
ATOM   2205  CD1 LEU A 337     -18.860  -0.045   8.643  1.00 99.61           C  
ANISOU 2205  CD1 LEU A 337    14181  12103  11560   2001   -772    591       C  
ATOM   2206  CD2 LEU A 337     -19.739  -1.310  10.600  1.00101.68           C  
ANISOU 2206  CD2 LEU A 337    14208  12383  12042   1825   -639    194       C  
ATOM   2207  N   ALA A 338     -20.576  -5.047   7.013  1.00 98.96           N  
ANISOU 2207  N   ALA A 338    14225  12125  11248   1190   -264    796       N  
ATOM   2208  CA  ALA A 338     -21.588  -5.848   6.303  1.00 98.46           C  
ANISOU 2208  CA  ALA A 338    14232  12069  11109   1094   -194    872       C  
ATOM   2209  C   ALA A 338     -21.644  -7.285   6.812  1.00 99.02           C  
ANISOU 2209  C   ALA A 338    14266  12163  11195    838    -39    780       C  
ATOM   2210  O   ALA A 338     -22.703  -7.889   6.894  1.00 98.81           O  
ANISOU 2210  O   ALA A 338    14230  12136  11176    777     26    712       O  
ATOM   2211  CB  ALA A 338     -21.310  -5.838   4.805  1.00 97.18           C  
ANISOU 2211  CB  ALA A 338    14219  11903  10802   1085   -217   1146       C  
ATOM   2212  N   SER A 339     -20.482  -7.831   7.136  1.00 99.58           N  
ANISOU 2212  N   SER A 339    14322  12250  11265    684     21    782       N  
ATOM   2213  CA  SER A 339     -20.383  -9.162   7.731  1.00100.48           C  
ANISOU 2213  CA  SER A 339    14406  12378  11394    434    173    680       C  
ATOM   2214  C   SER A 339     -21.048  -9.197   9.114  1.00101.74           C  
ANISOU 2214  C   SER A 339    14414  12528  11712    450    220    396       C  
ATOM   2215  O   SER A 339     -21.521 -10.236   9.576  1.00102.45           O  
ANISOU 2215  O   SER A 339    14477  12622  11825    276    351    286       O  
ATOM   2216  CB  SER A 339     -18.898  -9.532   7.859  1.00100.61           C  
ANISOU 2216  CB  SER A 339    14438  12406  11385    297    208    734       C  
ATOM   2217  OG  SER A 339     -18.711 -10.882   8.222  1.00101.32           O  
ANISOU 2217  OG  SER A 339    14539  12503  11457     37    359    679       O  
ATOM   2218  N   ASN A 340     -21.094  -8.033   9.751  1.00102.14           N  
ANISOU 2218  N   ASN A 340    14370  12566  11873    664    109    277       N  
ATOM   2219  CA  ASN A 340     -21.468  -7.903  11.152  1.00103.52           C  
ANISOU 2219  CA  ASN A 340    14382  12727  12224    700    130     -2       C  
ATOM   2220  C   ASN A 340     -20.677  -8.838  12.090  1.00104.95           C  
ANISOU 2220  C   ASN A 340    14489  12918  12471    483    269   -139       C  
ATOM   2221  O   ASN A 340     -21.241  -9.423  13.015  1.00105.96           O  
ANISOU 2221  O   ASN A 340    14517  13036  12709    393    369   -346       O  
ATOM   2222  CB  ASN A 340     -22.981  -8.063  11.340  1.00103.64           C  
ANISOU 2222  CB  ASN A 340    14360  12727  12290    741    151   -118       C  
ATOM   2223  CG  ASN A 340     -23.535  -7.042  12.318  1.00104.11           C  
ANISOU 2223  CG  ASN A 340    14282  12756  12517    955     46   -332       C  
ATOM   2224  ND2 ASN A 340     -24.114  -7.510  13.405  1.00105.29           N  
ANISOU 2224  ND2 ASN A 340    14302  12891  12810    892    127   -573       N  
ATOM   2225  OD1 ASN A 340     -23.412  -5.841  12.106  1.00103.34           O  
ANISOU 2225  OD1 ASN A 340    14201  12641  12421   1174   -107   -283       O  
ATOM   2226  N   GLY A 341     -19.371  -8.963  11.830  1.00105.27           N  
ANISOU 2226  N   GLY A 341    14581  12971  12445    399    276    -21       N  
ATOM   2227  CA  GLY A 341     -18.438  -9.733  12.667  1.00106.71           C  
ANISOU 2227  CA  GLY A 341    14705  13160  12677    204    396   -130       C  
ATOM   2228  C   GLY A 341     -18.197 -11.219  12.365  1.00107.53           C  
ANISOU 2228  C   GLY A 341    14904  13274  12678    -87    561    -61       C  
ATOM   2229  O   GLY A 341     -17.473 -11.866  13.123  1.00108.29           O  
ANISOU 2229  O   GLY A 341    14958  13369  12820   -252    669   -167       O  
ATOM   2230  N   GLU A 342     -18.811 -11.778  11.309  1.00107.52           N  
ANISOU 2230  N   GLU A 342    15032  13277  12543   -154    583    105       N  
ATOM   2231  CA  GLU A 342     -18.394 -13.103  10.792  1.00107.71           C  
ANISOU 2231  CA  GLU A 342    15182  13305  12437   -420    708    224       C  
ATOM   2232  C   GLU A 342     -16.946 -13.009  10.301  1.00107.91           C  
ANISOU 2232  C   GLU A 342    15283  13338  12379   -463    663    392       C  
ATOM   2233  O   GLU A 342     -16.567 -12.051   9.610  1.00107.15           O  
ANISOU 2233  O   GLU A 342    15219  13248  12245   -292    525    539       O  
ATOM   2234  CB  GLU A 342     -19.268 -13.626   9.627  1.00106.69           C  
ANISOU 2234  CB  GLU A 342    15187  13176  12175   -465    714    395       C  
ATOM   2235  CG  GLU A 342     -20.370 -14.620   9.966  1.00107.13           C  
ANISOU 2235  CG  GLU A 342    15237  13222  12245   -607    850    273       C  
ATOM   2236  CD  GLU A 342     -21.610 -13.965  10.539  1.00107.60           C  
ANISOU 2236  CD  GLU A 342    15174  13274  12432   -432    813    100       C  
ATOM   2237  OE1 GLU A 342     -21.872 -12.780  10.261  1.00107.06           O  
ANISOU 2237  OE1 GLU A 342    15076  13210  12393   -191    666    139       O  
ATOM   2238  OE2 GLU A 342     -22.357 -14.649  11.260  1.00108.30           O1-
ANISOU 2238  OE2 GLU A 342    15203  13353  12592   -537    932    -77       O1-
ATOM   2239  N   GLY A 343     -16.143 -14.009  10.662  1.00109.03           N  
ANISOU 2239  N   GLY A 343    15459  13476  12492   -694    784    368       N  
ATOM   2240  CA  GLY A 343     -14.752 -14.097  10.212  1.00108.63           C  
ANISOU 2240  CA  GLY A 343    15490  13429  12357   -767    756    524       C  
ATOM   2241  C   GLY A 343     -13.733 -13.584  11.217  1.00109.48           C  
ANISOU 2241  C   GLY A 343    15484  13539  12573   -731    746    391       C  
ATOM   2242  O   GLY A 343     -12.562 -13.965  11.136  1.00109.36           O  
ANISOU 2242  O   GLY A 343    15526  13523  12502   -856    771    468       O  
ATOM   2243  N   LEU A 344     -14.165 -12.726  12.156  1.00110.32           N  
ANISOU 2243  N   LEU A 344    15431  13646  12838   -560    704    193       N  
ATOM   2244  CA  LEU A 344     -13.263 -12.092  13.146  1.00110.91           C  
ANISOU 2244  CA  LEU A 344    15385  13721  13035   -492    677     54       C  
ATOM   2245  C   LEU A 344     -13.313 -12.754  14.524  1.00112.28           C  
ANISOU 2245  C   LEU A 344    15439  13879  13342   -636    828   -212       C  
ATOM   2246  O   LEU A 344     -14.116 -13.644  14.768  1.00112.34           O  
ANISOU 2246  O   LEU A 344    15451  13874  13355   -774    954   -304       O  
ATOM   2247  CB  LEU A 344     -13.594 -10.592  13.312  1.00110.64           C  
ANISOU 2247  CB  LEU A 344    15250  13687  13099   -193    512      5       C  
ATOM   2248  CG  LEU A 344     -13.179  -9.608  12.217  1.00109.44           C  
ANISOU 2248  CG  LEU A 344    15186  13544  12853    -16    351    234       C  
ATOM   2249  CD1 LEU A 344     -13.850  -8.264  12.467  1.00109.37           C  
ANISOU 2249  CD1 LEU A 344    15091  13523  12940    266    210    152       C  
ATOM   2250  CD2 LEU A 344     -11.659  -9.463  12.128  1.00109.12           C  
ANISOU 2250  CD2 LEU A 344    15175  13511  12775    -57    324    330       C  
ATOM   2251  N   VAL A 345     -12.433 -12.292  15.411  1.00113.30           N  
ANISOU 2251  N   VAL A 345    15462  14005  13581   -599    814   -335       N  
ATOM   2252  CA  VAL A 345     -12.468 -12.627  16.835  1.00115.25           C  
ANISOU 2252  CA  VAL A 345    15561  14232  13996   -682    934   -617       C  
ATOM   2253  C   VAL A 345     -13.302 -11.539  17.546  1.00116.22           C  
ANISOU 2253  C   VAL A 345    15519  14345  14297   -438    830   -801       C  
ATOM   2254  O   VAL A 345     -13.312 -10.383  17.120  1.00115.19           O  
ANISOU 2254  O   VAL A 345    15384  14221  14161   -207    658   -716       O  
ATOM   2255  CB  VAL A 345     -11.038 -12.722  17.443  1.00115.40           C  
ANISOU 2255  CB  VAL A 345    15549  14249  14047   -777    975   -658       C  
ATOM   2256  CG1 VAL A 345     -11.059 -13.482  18.764  1.00116.92           C  
ANISOU 2256  CG1 VAL A 345    15631  14415  14380   -946   1153   -924       C  
ATOM   2257  CG2 VAL A 345     -10.077 -13.396  16.465  1.00114.40           C  
ANISOU 2257  CG2 VAL A 345    15606  14135  13727   -940    999   -413       C  
ATOM   2258  N   LYS A 346     -13.992 -11.918  18.626  1.00118.42           N  
ANISOU 2258  N   LYS A 346    15666  14597  14730   -492    938  -1058       N  
ATOM   2259  CA  LYS A 346     -14.986 -11.061  19.328  1.00119.25           C  
ANISOU 2259  CA  LYS A 346    15613  14682  15012   -283    852  -1254       C  
ATOM   2260  C   LYS A 346     -14.439  -9.729  19.885  1.00119.89           C  
ANISOU 2260  C   LYS A 346    15579  14756  15220    -53    690  -1333       C  
ATOM   2261  O   LYS A 346     -15.223  -8.800  20.097  1.00118.93           O  
ANISOU 2261  O   LYS A 346    15376  14617  15196    167    561  -1418       O  
ATOM   2262  CB  LYS A 346     -15.689 -11.872  20.449  1.00120.55           C  
ANISOU 2262  CB  LYS A 346    15653  14815  15333   -424   1023  -1527       C  
ATOM   2263  CG  LYS A 346     -14.764 -12.346  21.577  1.00121.73           C  
ANISOU 2263  CG  LYS A 346    15706  14945  15601   -579   1155  -1710       C  
ATOM   2264  CD  LYS A 346     -15.004 -13.775  22.081  1.00122.73           C  
ANISOU 2264  CD  LYS A 346    15842  15048  15741   -864   1399  -1835       C  
ATOM   2265  CE  LYS A 346     -13.826 -14.246  22.925  1.00123.47           C  
ANISOU 2265  CE  LYS A 346    15889  15127  15895  -1031   1524  -1947       C  
ATOM   2266  NZ  LYS A 346     -13.857 -15.702  23.211  1.00124.40           N1+
ANISOU 2266  NZ  LYS A 346    16070  15220  15975  -1334   1768  -2016       N1+
ATOM   2267  N   GLU A 347     -13.112  -9.651  20.092  1.00121.42           N  
ANISOU 2267  N   GLU A 347    15773  14958  15404   -104    692  -1300       N  
ATOM   2268  CA  GLU A 347     -12.407  -8.432  20.571  1.00122.68           C  
ANISOU 2268  CA  GLU A 347    15838  15109  15664     97    541  -1354       C  
ATOM   2269  C   GLU A 347     -12.075  -7.422  19.449  1.00122.14           C  
ANISOU 2269  C   GLU A 347    15886  15062  15459    288    356  -1105       C  
ATOM   2270  O   GLU A 347     -11.391  -6.419  19.666  1.00121.41           O  
ANISOU 2270  O   GLU A 347    15749  14965  15415    448    227  -1108       O  
ATOM   2271  CB  GLU A 347     -11.089  -8.794  21.293  1.00123.11           C  
ANISOU 2271  CB  GLU A 347    15843  15164  15769    -47    630  -1428       C  
ATOM   2272  CG  GLU A 347     -11.249  -9.569  22.601  1.00124.32           C  
ANISOU 2272  CG  GLU A 347    15853  15287  16096   -207    804  -1711       C  
ATOM   2273  CD  GLU A 347     -10.903 -11.055  22.514  1.00124.27           C  
ANISOU 2273  CD  GLU A 347    15941  15283  15991   -521   1023  -1678       C  
ATOM   2274  OE1 GLU A 347     -10.912 -11.645  21.420  1.00123.35           O  
ANISOU 2274  OE1 GLU A 347    16000  15189  15673   -625   1050  -1453       O  
ATOM   2275  OE2 GLU A 347     -10.613 -11.648  23.562  1.00124.84           O1-
ANISOU 2275  OE2 GLU A 347    15914  15330  16190   -670   1171  -1884       O1-
ATOM   2276  N   SER A 348     -12.543  -7.723  18.246  1.00122.76           N  
ANISOU 2276  N   SER A 348    16117  15161  15367    262    351   -891       N  
ATOM   2277  CA  SER A 348     -12.435  -6.822  17.103  1.00122.23           C  
ANISOU 2277  CA  SER A 348    16164  15105  15172    439    191   -658       C  
ATOM   2278  C   SER A 348     -13.736  -6.018  16.956  1.00124.34           C  
ANISOU 2278  C   SER A 348    16409  15353  15483    656     76   -699       C  
ATOM   2279  O   SER A 348     -14.071  -5.580  15.861  1.00122.97           O  
ANISOU 2279  O   SER A 348    16353  15185  15183    761    -13   -503       O  
ATOM   2280  CB  SER A 348     -12.077  -7.619  15.832  1.00120.63           C  
ANISOU 2280  CB  SER A 348    16143  14927  14761    278    251   -392       C  
ATOM   2281  OG  SER A 348     -10.870  -8.349  16.024  1.00119.67           O  
ANISOU 2281  OG  SER A 348    16046  14818  14604     80    350   -365       O  
ATOM   2282  N   TRP A 349     -14.464  -5.835  18.068  1.00128.37           N  
ANISOU 2282  N   TRP A 349    16765  15834  16175    721     78   -958       N  
ATOM   2283  CA  TRP A 349     -15.493  -4.791  18.193  1.00130.69           C  
ANISOU 2283  CA  TRP A 349    17010  16096  16549    971    -70  -1036       C  
ATOM   2284  C   TRP A 349     -14.775  -3.440  18.342  1.00132.43           C  
ANISOU 2284  C   TRP A 349    17208  16302  16809   1193   -248  -1023       C  
ATOM   2285  O   TRP A 349     -15.425  -2.378  18.279  1.00133.99           O  
ANISOU 2285  O   TRP A 349    17401  16468  17040   1427   -404  -1043       O  
ATOM   2286  CB  TRP A 349     -16.428  -5.064  19.398  1.00132.55           C  
ANISOU 2286  CB  TRP A 349    17078  16298  16984    960    -11  -1331       C  
ATOM   2287  CG  TRP A 349     -17.558  -4.042  19.589  1.00133.66           C  
ANISOU 2287  CG  TRP A 349    17166  16402  17218   1213   -168  -1429       C  
ATOM   2288  CD1 TRP A 349     -18.202  -3.326  18.601  1.00133.15           C  
ANISOU 2288  CD1 TRP A 349    17220  16333  17037   1384   -297  -1263       C  
ATOM   2289  CD2 TRP A 349     -18.175  -3.644  20.832  1.00134.77           C  
ANISOU 2289  CD2 TRP A 349    17127  16495  17586   1318   -214  -1716       C  
ATOM   2290  CE2 TRP A 349     -19.169  -2.678  20.517  1.00134.74           C  
ANISOU 2290  CE2 TRP A 349    17151  16459  17585   1555   -380  -1704       C  
ATOM   2291  CE3 TRP A 349     -17.984  -4.006  22.178  1.00135.05           C  
ANISOU 2291  CE3 TRP A 349    16980  16504  17829   1235   -130  -1986       C  
ATOM   2292  NE1 TRP A 349     -19.164  -2.507  19.156  1.00133.48           N  
ANISOU 2292  NE1 TRP A 349    17177  16328  17211   1588   -421  -1424       N  
ATOM   2293  CZ2 TRP A 349     -19.971  -2.077  21.503  1.00134.80           C  
ANISOU 2293  CZ2 TRP A 349    17013  16410  17794   1712   -475  -1950       C  
ATOM   2294  CZ3 TRP A 349     -18.786  -3.400  23.160  1.00135.57           C  
ANISOU 2294  CZ3 TRP A 349    16890  16514  18107   1392   -222  -2236       C  
ATOM   2295  CH2 TRP A 349     -19.764  -2.453  22.814  1.00135.42           C  
ANISOU 2295  CH2 TRP A 349    16906  16464  18084   1629   -397  -2214       C  
ATOM   2296  N   ALA A 350     -13.442  -3.503  18.547  1.00134.07           N  
ANISOU 2296  N   ALA A 350    17407  16525  17007   1114   -223   -990       N  
ATOM   2297  CA  ALA A 350     -12.531  -2.330  18.594  1.00134.41           C  
ANISOU 2297  CA  ALA A 350    17449  16557  17063   1292   -376   -947       C  
ATOM   2298  C   ALA A 350     -12.831  -1.349  17.455  1.00134.45           C  
ANISOU 2298  C   ALA A 350    17592  16556  16936   1492   -528   -738       C  
ATOM   2299  O   ALA A 350     -12.849  -0.119  17.640  1.00136.30           O  
ANISOU 2299  O   ALA A 350    17810  16757  17221   1723   -691   -772       O  
ATOM   2300  CB  ALA A 350     -11.057  -2.774  18.546  1.00132.44           C  
ANISOU 2300  CB  ALA A 350    17227  16338  16757   1136   -302   -859       C  
ATOM   2301  N   LYS A 351     -13.062  -1.919  16.275  1.00132.15           N  
ANISOU 2301  N   LYS A 351    17443  16291  16475   1398   -469   -523       N  
ATOM   2302  CA  LYS A 351     -13.416  -1.144  15.094  1.00128.81           C  
ANISOU 2302  CA  LYS A 351    17160  15860  15920   1559   -584   -315       C  
ATOM   2303  C   LYS A 351     -14.677  -0.340  15.389  1.00127.39           C  
ANISOU 2303  C   LYS A 351    16943  15639  15820   1769   -696   -436       C  
ATOM   2304  O   LYS A 351     -14.749   0.871  15.115  1.00126.75           O  
ANISOU 2304  O   LYS A 351    16911  15526  15722   1994   -852   -386       O  
ATOM   2305  CB  LYS A 351     -13.620  -2.075  13.908  1.00126.29           C  
ANISOU 2305  CB  LYS A 351    16977  15572  15435   1397   -484   -103       C  
ATOM   2306  CG  LYS A 351     -14.408  -1.495  12.744  1.00124.22           C  
ANISOU 2306  CG  LYS A 351    16844  15297  15057   1540   -570     73       C  
ATOM   2307  CD  LYS A 351     -15.053  -2.609  11.946  1.00122.88           C  
ANISOU 2307  CD  LYS A 351    16756  15149  14781   1369   -451    187       C  
ATOM   2308  CE  LYS A 351     -14.079  -3.752  11.683  1.00121.10           C  
ANISOU 2308  CE  LYS A 351    16572  14958  14482   1115   -323    285       C  
ATOM   2309  NZ  LYS A 351     -14.603  -4.689  10.676  1.00119.70           N1+
ANISOU 2309  NZ  LYS A 351    16508  14796  14177    971   -238    442       N1+
ATOM   2310  N   LEU A 352     -15.659  -1.023  15.970  1.00125.33           N  
ANISOU 2310  N   LEU A 352    16598  15374  15648   1691   -614   -601       N  
ATOM   2311  CA  LEU A 352     -16.809  -0.367  16.530  1.00124.59           C  
ANISOU 2311  CA  LEU A 352    16432  15235  15669   1870   -712   -770       C  
ATOM   2312  C   LEU A 352     -17.458   0.425  15.391  1.00124.33           C  
ANISOU 2312  C   LEU A 352    16550  15186  15503   2046   -827   -582       C  
ATOM   2313  O   LEU A 352     -17.205   0.161  14.205  1.00122.37           O  
ANISOU 2313  O   LEU A 352    16443  14966  15087   1981   -790   -344       O  
ATOM   2314  CB  LEU A 352     -16.372   0.550  17.685  1.00124.15           C  
ANISOU 2314  CB  LEU A 352    16247  15141  15784   2023   -829   -969       C  
ATOM   2315  CG  LEU A 352     -17.122   0.453  19.019  1.00124.72           C  
ANISOU 2315  CG  LEU A 352    16137  15176  16075   2046   -824  -1275       C  
ATOM   2316  CD1 LEU A 352     -16.557   1.430  20.051  1.00124.63           C  
ANISOU 2316  CD1 LEU A 352    16010  15121  16223   2205   -958  -1447       C  
ATOM   2317  CD2 LEU A 352     -18.632   0.619  18.932  1.00124.48           C  
ANISOU 2317  CD2 LEU A 352    16110  15114  16074   2153   -873  -1339       C  
ATOM   2318  N   GLN A 353     -18.289   1.397  15.739  1.00126.34           N  
ANISOU 2318  N   GLN A 353    16779  15390  15834   2267   -968   -691       N  
ATOM   2319  CA  GLN A 353     -18.743   2.385  14.776  1.00125.88           C  
ANISOU 2319  CA  GLN A 353    16866  15302  15659   2464  -1099   -529       C  
ATOM   2320  C   GLN A 353     -18.079   3.760  15.022  1.00126.44           C  
ANISOU 2320  C   GLN A 353    16953  15330  15758   2681  -1271   -538       C  
ATOM   2321  O   GLN A 353     -18.044   4.604  14.110  1.00126.93           O  
ANISOU 2321  O   GLN A 353    17161  15370  15697   2824  -1366   -362       O  
ATOM   2322  CB  GLN A 353     -20.281   2.436  14.776  1.00125.65           C  
ANISOU 2322  CB  GLN A 353    16836  15243  15661   2549  -1129   -610       C  
ATOM   2323  CG  GLN A 353     -20.900   1.754  13.549  1.00123.79           C  
ANISOU 2323  CG  GLN A 353    16730  15040  15266   2448  -1037   -410       C  
ATOM   2324  CD  GLN A 353     -22.033   2.558  12.931  1.00122.90           C  
ANISOU 2324  CD  GLN A 353    16719  14882  15094   2644  -1149   -352       C  
ATOM   2325  NE2 GLN A 353     -23.066   2.817  13.722  1.00123.66           N  
ANISOU 2325  NE2 GLN A 353    16729  14938  15318   2748  -1211   -554       N  
ATOM   2326  OE1 GLN A 353     -21.985   2.937  11.757  1.00120.68           O  
ANISOU 2326  OE1 GLN A 353    16593  14599  14659   2700  -1178   -130       O  
ATOM   2327  N   ALA A 354     -17.541   3.957  16.235  1.00126.96           N  
ANISOU 2327  N   ALA A 354    16874  15380  15984   2700  -1305   -741       N  
ATOM   2328  CA  ALA A 354     -16.737   5.136  16.572  1.00126.01           C  
ANISOU 2328  CA  ALA A 354    16757  15221  15898   2876  -1456   -761       C  
ATOM   2329  C   ALA A 354     -15.530   5.189  15.653  1.00125.03           C  
ANISOU 2329  C   ALA A 354    16751  15134  15623   2818  -1426   -522       C  
ATOM   2330  O   ALA A 354     -15.273   6.216  15.008  1.00123.35           O  
ANISOU 2330  O   ALA A 354    16661  14890  15316   2983  -1542   -385       O  
ATOM   2331  CB  ALA A 354     -16.298   5.096  18.032  1.00126.31           C  
ANISOU 2331  CB  ALA A 354    16606  15245  16143   2859  -1466  -1019       C  
ATOM   2332  N   LEU A 355     -14.809   4.069  15.581  1.00 72.73           N  
ANISOU 2332  N   LEU A 355     9208   9685   8740   1073    403    662       N  
ATOM   2333  CA  LEU A 355     -13.714   3.957  14.641  1.00 69.58           C  
ANISOU 2333  CA  LEU A 355     8893   9307   8237    782    449    623       C  
ATOM   2334  C   LEU A 355     -14.200   3.989  13.187  1.00 68.19           C  
ANISOU 2334  C   LEU A 355     9013   8842   8054    690    482    543       C  
ATOM   2335  O   LEU A 355     -13.636   4.701  12.351  1.00 65.32           O  
ANISOU 2335  O   LEU A 355     8781   8411   7627    469    445    591       O  
ATOM   2336  CB  LEU A 355     -12.898   2.699  14.886  1.00 70.16           C  
ANISOU 2336  CB  LEU A 355     8792   9606   8258    728    572    515       C  
ATOM   2337  CG  LEU A 355     -11.762   2.559  13.855  1.00 70.09           C  
ANISOU 2337  CG  LEU A 355     8876   9598   8159    442    606    476       C  
ATOM   2338  CD1 LEU A 355     -10.522   3.174  14.469  1.00 71.54           C  
ANISOU 2338  CD1 LEU A 355     8906   9981   8296    278    526    600       C  
ATOM   2339  CD2 LEU A 355     -11.520   1.118  13.386  1.00 69.70           C  
ANISOU 2339  CD2 LEU A 355     8815   9602   8065    413    745    316       C  
ATOM   2340  N   ALA A 356     -15.228   3.209  12.868  1.00 67.91           N  
ANISOU 2340  N   ALA A 356     9080   8643   8082    853    554    410       N  
ATOM   2341  CA  ALA A 356     -15.667   3.117  11.476  1.00 65.90           C  
ANISOU 2341  CA  ALA A 356     9094   8123   7823    743    588    323       C  
ATOM   2342  C   ALA A 356     -16.066   4.501  10.948  1.00 66.13           C  
ANISOU 2342  C   ALA A 356     9319   7943   7863    657    470    474       C  
ATOM   2343  O   ALA A 356     -15.681   4.879   9.848  1.00 63.71           O  
ANISOU 2343  O   ALA A 356     9163   7548   7496    428    477    478       O  
ATOM   2344  CB  ALA A 356     -16.811   2.126  11.345  1.00 68.20           C  
ANISOU 2344  CB  ALA A 356     9469   8254   8189    949    664    155       C  
ATOM   2345  N   ASP A 357     -16.808   5.266  11.743  1.00 69.38           N  
ANISOU 2345  N   ASP A 357     9718   8296   8346    835    360    606       N  
ATOM   2346  CA  ASP A 357     -17.262   6.593  11.314  1.00 71.26           C  
ANISOU 2346  CA  ASP A 357    10149   8344   8583    761    237    774       C  
ATOM   2347  C   ASP A 357     -16.102   7.540  11.205  1.00 68.50           C  
ANISOU 2347  C   ASP A 357     9757   8163   8107    517    185    892       C  
ATOM   2348  O   ASP A 357     -15.914   8.160  10.175  1.00 67.83           O  
ANISOU 2348  O   ASP A 357     9848   7973   7953    305    182    925       O  
ATOM   2349  CB  ASP A 357     -18.300   7.197  12.272  1.00 76.11           C  
ANISOU 2349  CB  ASP A 357    10749   8866   9302   1024    109    907       C  
ATOM   2350  CG  ASP A 357     -19.694   6.608  12.083  1.00 81.15           C  
ANISOU 2350  CG  ASP A 357    11536   9215  10080   1254    129    809       C  
ATOM   2351  OD1 ASP A 357     -19.995   6.095  10.982  1.00 81.75           O  
ANISOU 2351  OD1 ASP A 357    11808   9095  10160   1153    207    684       O  
ATOM   2352  OD2 ASP A 357     -20.514   6.698  13.018  1.00 86.08           O1-
ANISOU 2352  OD2 ASP A 357    12090   9797  10821   1538     55    858       O1-
ATOM   2353  N   SER A 358     -15.319   7.651  12.272  1.00 68.55           N  
ANISOU 2353  N   SER A 358     9525   8438   8084    541    147    947       N  
ATOM   2354  CA  SER A 358     -14.125   8.504  12.266  1.00 66.84           C  
ANISOU 2354  CA  SER A 358     9256   8393   7749    313     92   1035       C  
ATOM   2355  C   SER A 358     -13.310   8.269  11.005  1.00 63.57           C  
ANISOU 2355  C   SER A 358     8947   7955   7252     61    191    927       C  
ATOM   2356  O   SER A 358     -12.972   9.210  10.288  1.00 62.78           O  
ANISOU 2356  O   SER A 358     8978   7811   7066   -128    158    988       O  
ATOM   2357  CB  SER A 358     -13.257   8.230  13.492  1.00 66.83           C  
ANISOU 2357  CB  SER A 358     8966   8687   7739    349     73   1051       C  
ATOM   2358  OG  SER A 358     -13.999   8.374  14.696  1.00 70.46           O  
ANISOU 2358  OG  SER A 358     9287   9199   8284    594    -11   1142       O  
ATOM   2359  N   HIS A 359     -13.038   6.996  10.729  1.00 61.54           N  
ANISOU 2359  N   HIS A 359     8629   7734   7019     68    314    766       N  
ATOM   2360  CA  HIS A 359     -12.236   6.612   9.579  1.00 58.27           C  
ANISOU 2360  CA  HIS A 359     8282   7314   6543   -147    403    657       C  
ATOM   2361  C   HIS A 359     -12.765   7.166   8.253  1.00 57.96           C  
ANISOU 2361  C   HIS A 359     8491   7048   6483   -275    414    657       C  
ATOM   2362  O   HIS A 359     -11.992   7.571   7.375  1.00 56.21           O  
ANISOU 2362  O   HIS A 359     8324   6848   6185   -489    439    639       O  
ATOM   2363  CB  HIS A 359     -12.159   5.101   9.466  1.00 56.80           C  
ANISOU 2363  CB  HIS A 359     8022   7170   6388    -89    519    492       C  
ATOM   2364  CG  HIS A 359     -11.357   4.660   8.295  1.00 55.39           C  
ANISOU 2364  CG  HIS A 359     7899   6989   6156   -295    594    388       C  
ATOM   2365  CD2 HIS A 359     -10.033   4.752   8.040  1.00 54.34           C  
ANISOU 2365  CD2 HIS A 359     7690   6995   5961   -474    600    380       C  
ATOM   2366  ND1 HIS A 359     -11.927   4.135   7.164  1.00 56.95           N  
ANISOU 2366  ND1 HIS A 359     8256   7010   6371   -337    660    278       N  
ATOM   2367  CE1 HIS A 359     -10.983   3.861   6.282  1.00 56.11           C  
ANISOU 2367  CE1 HIS A 359     8147   6959   6213   -524    706    208       C  
ATOM   2368  NE2 HIS A 359      -9.824   4.239   6.786  1.00 54.14           N  
ANISOU 2368  NE2 HIS A 359     7760   6889   5919   -602    671    267       N  
ATOM   2369  N   LEU A 360     -14.090   7.140   8.122  1.00 59.16           N  
ANISOU 2369  N   LEU A 360     8787   6979   6712   -140    398    671       N  
ATOM   2370  CA  LEU A 360     -14.766   7.599   6.924  1.00 59.00           C  
ANISOU 2370  CA  LEU A 360     9008   6722   6687   -257    404    685       C  
ATOM   2371  C   LEU A 360     -14.550   9.082   6.784  1.00 60.03           C  
ANISOU 2371  C   LEU A 360     9217   6864   6727   -398    317    855       C  
ATOM   2372  O   LEU A 360     -14.102   9.525   5.729  1.00 59.90           O  
ANISOU 2372  O   LEU A 360     9295   6835   6631   -621    359    845       O  
ATOM   2373  CB  LEU A 360     -16.267   7.273   6.989  1.00 60.71           C  
ANISOU 2373  CB  LEU A 360     9365   6680   7023    -62    382    675       C  
ATOM   2374  CG  LEU A 360     -17.155   7.561   5.774  1.00 60.74           C  
ANISOU 2374  CG  LEU A 360     9634   6393   7050   -175    383    684       C  
ATOM   2375  CD1 LEU A 360     -16.728   6.732   4.572  1.00 59.10           C  
ANISOU 2375  CD1 LEU A 360     9465   6175   6817   -357    500    512       C  
ATOM   2376  CD2 LEU A 360     -18.620   7.313   6.112  1.00 62.30           C  
ANISOU 2376  CD2 LEU A 360     9960   6324   7386     57    333    688       C  
ATOM   2377  N   LYS A 361     -14.861   9.836   7.844  1.00 63.12           N  
ANISOU 2377  N   LYS A 361     9560   7296   7124   -267    199   1008       N  
ATOM   2378  CA  LYS A 361     -14.647  11.296   7.856  1.00 65.63           C  
ANISOU 2378  CA  LYS A 361     9947   7658   7332   -394     99   1182       C  
ATOM   2379  C   LYS A 361     -13.222  11.640   7.480  1.00 63.18           C  
ANISOU 2379  C   LYS A 361     9558   7554   6892   -618    143   1133       C  
ATOM   2380  O   LYS A 361     -12.992  12.563   6.716  1.00 65.19           O  
ANISOU 2380  O   LYS A 361     9934   7799   7036   -809    142   1187       O  
ATOM   2381  CB  LYS A 361     -14.920  11.938   9.223  1.00 69.72           C  
ANISOU 2381  CB  LYS A 361    10362   8263   7865   -221    -47   1339       C  
ATOM   2382  CG  LYS A 361     -16.330  12.463   9.491  1.00 75.15           C  
ANISOU 2382  CG  LYS A 361    11196   8729   8629    -54   -162   1492       C  
ATOM   2383  CD  LYS A 361     -16.389  13.352  10.740  1.00 80.24           C  
ANISOU 2383  CD  LYS A 361    11731   9503   9254     66   -330   1675       C  
ATOM   2384  CE  LYS A 361     -15.842  12.634  11.996  1.00 83.32           C  
ANISOU 2384  CE  LYS A 361    11822  10127   9707    229   -329   1606       C  
ATOM   2385  NZ  LYS A 361     -16.443  11.276  12.282  1.00 85.76           N1+
ANISOU 2385  NZ  LYS A 361    12048  10363  10172    458   -237   1459       N1+
ATOM   2386  N   ALA A 362     -12.269  10.920   8.043  1.00 60.84           N  
ANISOU 2386  N   ALA A 362     9060   7446   6610   -593    179   1033       N  
ATOM   2387  CA  ALA A 362     -10.880  11.146   7.720  1.00 60.93           C  
ANISOU 2387  CA  ALA A 362     8998   7629   6526   -786    214    970       C  
ATOM   2388  C   ALA A 362     -10.648  11.028   6.223  1.00 60.03           C  
ANISOU 2388  C   ALA A 362     9008   7428   6374   -970    323    868       C  
ATOM   2389  O   ALA A 362     -10.041  11.894   5.619  1.00 59.53           O  
ANISOU 2389  O   ALA A 362     8999   7420   6201  -1147    330    880       O  
ATOM   2390  CB  ALA A 362     -10.006  10.141   8.458  1.00 61.97           C  
ANISOU 2390  CB  ALA A 362     8911   7929   6706   -727    243    876       C  
ATOM   2391  N   TYR A 363     -11.123   9.940   5.636  1.00 61.40           N  
ANISOU 2391  N   TYR A 363     9216   7482   6633   -926    410    757       N  
ATOM   2392  CA  TYR A 363     -10.924   9.659   4.208  1.00 61.43           C  
ANISOU 2392  CA  TYR A 363     9309   7413   6618  -1096    512    649       C  
ATOM   2393  C   TYR A 363     -11.598  10.716   3.364  1.00 60.65           C  
ANISOU 2393  C   TYR A 363     9406   7181   6457  -1224    503    746       C  
ATOM   2394  O   TYR A 363     -11.001  11.240   2.445  1.00 60.67           O  
ANISOU 2394  O   TYR A 363     9442   7236   6374  -1416    556    717       O  
ATOM   2395  CB  TYR A 363     -11.520   8.293   3.874  1.00 63.26           C  
ANISOU 2395  CB  TYR A 363     9552   7530   6953  -1006    581    524       C  
ATOM   2396  CG  TYR A 363     -11.111   7.636   2.572  1.00 63.26           C  
ANISOU 2396  CG  TYR A 363     9577   7509   6952  -1160    679    382       C  
ATOM   2397  CD1 TYR A 363     -10.030   8.076   1.801  1.00 62.02           C  
ANISOU 2397  CD1 TYR A 363     9382   7463   6721  -1346    718    343       C  
ATOM   2398  CD2 TYR A 363     -11.809   6.504   2.138  1.00 65.32           C  
ANISOU 2398  CD2 TYR A 363     9887   7643   7289  -1102    729    272       C  
ATOM   2399  CE1 TYR A 363      -9.685   7.411   0.615  1.00 64.10           C  
ANISOU 2399  CE1 TYR A 363     9643   7714   6998  -1469    800    213       C  
ATOM   2400  CE2 TYR A 363     -11.474   5.832   0.971  1.00 65.70           C  
ANISOU 2400  CE2 TYR A 363     9945   7680   7338  -1239    803    142       C  
ATOM   2401  CZ  TYR A 363     -10.423   6.275   0.205  1.00 65.49           C  
ANISOU 2401  CZ  TYR A 363     9867   7768   7250  -1419    835    119       C  
ATOM   2402  OH  TYR A 363     -10.139   5.556  -0.946  1.00 65.25           O  
ANISOU 2402  OH  TYR A 363     9828   7731   7234  -1539    900     -7       O  
ATOM   2403  N   GLN A 364     -12.840  11.036   3.702  1.00 61.87           N  
ANISOU 2403  N   GLN A 364     9685   7167   6655  -1115    434    866       N  
ATOM   2404  CA  GLN A 364     -13.624  12.042   2.968  1.00 63.11           C  
ANISOU 2404  CA  GLN A 364    10048   7174   6756  -1238    411    994       C  
ATOM   2405  C   GLN A 364     -12.986  13.403   2.999  1.00 62.43           C  
ANISOU 2405  C   GLN A 364     9973   7239   6508  -1382    369   1107       C  
ATOM   2406  O   GLN A 364     -12.772  14.010   1.954  1.00 63.50           O  
ANISOU 2406  O   GLN A 364    10196   7388   6545  -1592    432   1110       O  
ATOM   2407  CB  GLN A 364     -15.034  12.168   3.545  1.00 64.09           C  
ANISOU 2407  CB  GLN A 364    10299   7082   6969  -1060    312   1125       C  
ATOM   2408  CG  GLN A 364     -15.870  10.918   3.334  1.00 63.76           C  
ANISOU 2408  CG  GLN A 364    10303   6844   7080   -931    358   1002       C  
ATOM   2409  CD  GLN A 364     -17.218  10.960   4.021  1.00 64.66           C  
ANISOU 2409  CD  GLN A 364    10524   6736   7308   -709    257   1105       C  
ATOM   2410  NE2 GLN A 364     -18.164  10.219   3.478  1.00 65.25           N  
ANISOU 2410  NE2 GLN A 364    10732   6564   7494   -663    288   1021       N  
ATOM   2411  OE1 GLN A 364     -17.408  11.643   5.023  1.00 65.07           O  
ANISOU 2411  OE1 GLN A 364    10539   6832   7352   -579    144   1251       O  
ATOM   2412  N   GLY A 365     -12.692  13.882   4.200  1.00 61.67           N  
ANISOU 2412  N   GLY A 365     9780   7271   6378  -1273    265   1193       N  
ATOM   2413  CA  GLY A 365     -12.069  15.189   4.367  1.00 62.68           C  
ANISOU 2413  CA  GLY A 365     9917   7560   6338  -1400    207   1292       C  
ATOM   2414  C   GLY A 365     -10.688  15.284   3.734  1.00 59.72           C  
ANISOU 2414  C   GLY A 365     9456   7367   5868  -1578    303   1146       C  
ATOM   2415  O   GLY A 365     -10.277  16.358   3.265  1.00 59.66           O  
ANISOU 2415  O   GLY A 365     9513   7453   5701  -1747    313   1184       O  
ATOM   2416  N   ALA A 366      -9.978  14.157   3.712  1.00 56.91           N  
ANISOU 2416  N   ALA A 366     8957   7060   5607  -1535    373    978       N  
ATOM   2417  CA  ALA A 366      -8.654  14.102   3.107  1.00 55.28           C  
ANISOU 2417  CA  ALA A 366     8661   6997   5345  -1674    455    829       C  
ATOM   2418  C   ALA A 366      -8.776  14.321   1.614  1.00 56.27           C  
ANISOU 2418  C   ALA A 366     8894   7066   5421  -1852    570    777       C  
ATOM   2419  O   ALA A 366      -7.998  15.070   1.028  1.00 56.15           O  
ANISOU 2419  O   ALA A 366     8877   7171   5285  -2005    619    732       O  
ATOM   2420  CB  ALA A 366      -7.986  12.775   3.387  1.00 53.03           C  
ANISOU 2420  CB  ALA A 366     8215   6754   5182  -1585    492    689       C  
ATOM   2421  N   ILE A 367      -9.764  13.661   1.019  1.00 56.75           N  
ANISOU 2421  N   ILE A 367     9043   6946   5575  -1833    613    777       N  
ATOM   2422  CA  ILE A 367     -10.104  13.847  -0.383  1.00 57.43           C  
ANISOU 2422  CA  ILE A 367     9237   6958   5627  -2012    711    755       C  
ATOM   2423  C   ILE A 367     -10.447  15.320  -0.635  1.00 58.61           C  
ANISOU 2423  C   ILE A 367     9524   7131   5612  -2152    690    911       C  
ATOM   2424  O   ILE A 367      -9.797  15.993  -1.413  1.00 55.50           O  
ANISOU 2424  O   ILE A 367     9124   6867   5096  -2326    769    867       O  
ATOM   2425  CB  ILE A 367     -11.266  12.891  -0.771  1.00 58.20           C  
ANISOU 2425  CB  ILE A 367     9425   6827   5863  -1953    727    745       C  
ATOM   2426  CG1 ILE A 367     -10.754  11.447  -0.788  1.00 56.71           C  
ANISOU 2426  CG1 ILE A 367     9095   6660   5792  -1865    772    566       C  
ATOM   2427  CG2 ILE A 367     -11.877  13.251  -2.118  1.00 59.23           C  
ANISOU 2427  CG2 ILE A 367     9695   6850   5958  -2155    801    772       C  
ATOM   2428  CD1 ILE A 367     -11.809  10.390  -0.542  1.00 57.36           C  
ANISOU 2428  CD1 ILE A 367     9233   6554   6009  -1717    752    543       C  
ATOM   2429  N   LYS A 368     -11.466  15.809   0.053  1.00 62.52           N  
ANISOU 2429  N   LYS A 368    10141   7511   6105  -2068    581   1094       N  
ATOM   2430  CA  LYS A 368     -11.894  17.197  -0.067  1.00 66.26           C  
ANISOU 2430  CA  LYS A 368    10762   8001   6413  -2192    536   1279       C  
ATOM   2431  C   LYS A 368     -10.737  18.162   0.102  1.00 63.87           C  
ANISOU 2431  C   LYS A 368    10386   7955   5927  -2292    542   1250       C  
ATOM   2432  O   LYS A 368     -10.603  19.116  -0.652  1.00 65.21           O  
ANISOU 2432  O   LYS A 368    10633   8213   5928  -2485    603   1288       O  
ATOM   2433  CB  LYS A 368     -13.017  17.477   0.938  1.00 72.56           C  
ANISOU 2433  CB  LYS A 368    11665   8648   7258  -2029    380   1480       C  
ATOM   2434  CG  LYS A 368     -14.366  16.892   0.483  1.00 79.40           C  
ANISOU 2434  CG  LYS A 368    12682   9220   8268  -1988    377   1537       C  
ATOM   2435  CD  LYS A 368     -15.341  16.497   1.594  1.00 84.64           C  
ANISOU 2435  CD  LYS A 368    13375   9707   9078  -1724    242   1632       C  
ATOM   2436  CE  LYS A 368     -15.409  17.445   2.782  1.00 89.84           C  
ANISOU 2436  CE  LYS A 368    14023  10455   9657  -1616     85   1812       C  
ATOM   2437  NZ  LYS A 368     -15.771  18.856   2.430  1.00 92.68           N1+
ANISOU 2437  NZ  LYS A 368    14559  10819   9835  -1790     27   2027       N1+
ATOM   2438  N   ALA A 369      -9.872  17.898   1.070  1.00 60.71           N  
ANISOU 2438  N   ALA A 369     9833   7680   5555  -2169    485   1170       N  
ATOM   2439  CA  ALA A 369      -8.741  18.782   1.314  1.00 58.71           C  
ANISOU 2439  CA  ALA A 369     9516   7653   5137  -2255    474   1122       C  
ATOM   2440  C   ALA A 369      -7.618  18.631   0.287  1.00 55.74           C  
ANISOU 2440  C   ALA A 369     9056   7397   4727  -2388    623    914       C  
ATOM   2441  O   ALA A 369      -6.647  19.384   0.342  1.00 54.28           O  
ANISOU 2441  O   ALA A 369     8831   7390   4404  -2466    631    843       O  
ATOM   2442  CB  ALA A 369      -8.200  18.553   2.712  1.00 58.64           C  
ANISOU 2442  CB  ALA A 369     9374   7725   5182  -2095    351   1113       C  
ATOM   2443  N   GLY A 370      -7.721  17.647  -0.613  1.00 53.32           N  
ANISOU 2443  N   GLY A 370     8715   6996   4549  -2404    731    805       N  
ATOM   2444  CA  GLY A 370      -6.701  17.433  -1.659  1.00 51.45           C  
ANISOU 2444  CA  GLY A 370     8381   6866   4302  -2515    868    609       C  
ATOM   2445  C   GLY A 370      -5.391  16.750  -1.257  1.00 49.55           C  
ANISOU 2445  C   GLY A 370     7965   6716   4146  -2427    862    432       C  
ATOM   2446  O   GLY A 370      -4.322  17.046  -1.783  1.00 47.63           O  
ANISOU 2446  O   GLY A 370     7648   6602   3846  -2504    932    288       O  
ATOM   2447  N   VAL A 371      -5.467  15.820  -0.316  1.00 49.49           N  
ANISOU 2447  N   VAL A 371     7889   6637   4279  -2263    777    443       N  
ATOM   2448  CA  VAL A 371      -4.306  15.007   0.064  1.00 47.76           C  
ANISOU 2448  CA  VAL A 371     7510   6480   4158  -2189    766    301       C  
ATOM   2449  C   VAL A 371      -4.056  14.007  -1.037  1.00 45.31           C  
ANISOU 2449  C   VAL A 371     7137   6125   3953  -2219    873    162       C  
ATOM   2450  O   VAL A 371      -4.986  13.457  -1.577  1.00 45.59           O  
ANISOU 2450  O   VAL A 371     7229   6042   4051  -2221    913    194       O  
ATOM   2451  CB  VAL A 371      -4.584  14.232   1.371  1.00 48.15           C  
ANISOU 2451  CB  VAL A 371     7497   6479   4317  -2017    657    371       C  
ATOM   2452  CG1 VAL A 371      -3.436  13.299   1.736  1.00 47.04           C  
ANISOU 2452  CG1 VAL A 371     7199   6394   4280  -1960    646    247       C  
ATOM   2453  CG2 VAL A 371      -4.864  15.211   2.497  1.00 49.99           C  
ANISOU 2453  CG2 VAL A 371     7772   6765   4455  -1981    534    516       C  
ATOM   2454  N   THR A 372      -2.811  13.774  -1.380  1.00 44.61           N  
ANISOU 2454  N   THR A 372     6934   6123   3892  -2241    909     10       N  
ATOM   2455  CA  THR A 372      -2.514  12.703  -2.312  1.00 45.64           C  
ANISOU 2455  CA  THR A 372     6983   6218   4139  -2246    983   -112       C  
ATOM   2456  C   THR A 372      -2.970  11.324  -1.792  1.00 46.17           C  
ANISOU 2456  C   THR A 372     7012   6185   4344  -2121    937    -87       C  
ATOM   2457  O   THR A 372      -2.668  10.945  -0.650  1.00 45.97           O  
ANISOU 2457  O   THR A 372     6931   6175   4360  -2015    851    -52       O  
ATOM   2458  CB  THR A 372      -1.020  12.659  -2.597  1.00 45.32           C  
ANISOU 2458  CB  THR A 372     6820   6274   4122  -2259   1001   -271       C  
ATOM   2459  CG2 THR A 372      -0.681  11.479  -3.495  1.00 44.74           C  
ANISOU 2459  CG2 THR A 372     6649   6169   4179  -2249   1053   -383       C  
ATOM   2460  OG1 THR A 372      -0.657  13.878  -3.237  1.00 46.83           O  
ANISOU 2460  OG1 THR A 372     7044   6570   4180  -2372   1071   -325       O  
ATOM   2461  N   ILE A 373      -3.699  10.582  -2.625  1.00 46.53           N  
ANISOU 2461  N   ILE A 373     7086   6141   4452  -2144    995   -108       N  
ATOM   2462  CA  ILE A 373      -4.279   9.338  -2.172  1.00 46.14           C  
ANISOU 2462  CA  ILE A 373     7024   6001   4507  -2030    960    -92       C  
ATOM   2463  C   ILE A 373      -3.932   8.187  -3.084  1.00 47.08           C  
ANISOU 2463  C   ILE A 373     7065   6112   4713  -2052   1008   -217       C  
ATOM   2464  O   ILE A 373      -3.845   8.337  -4.292  1.00 48.04           O  
ANISOU 2464  O   ILE A 373     7181   6244   4828  -2168   1079   -286       O  
ATOM   2465  CB  ILE A 373      -5.808   9.446  -2.033  1.00 46.57           C  
ANISOU 2465  CB  ILE A 373     7223   5915   4556  -2003    950     18       C  
ATOM   2466  CG1 ILE A 373      -6.145  10.359  -0.870  1.00 47.13           C  
ANISOU 2466  CG1 ILE A 373     7348   5997   4563  -1933    869    158       C  
ATOM   2467  CG2 ILE A 373      -6.429   8.083  -1.724  1.00 47.87           C  
ANISOU 2467  CG2 ILE A 373     7377   5987   4825  -1883    934     -8       C  
ATOM   2468  CD1 ILE A 373      -7.591  10.783  -0.819  1.00 48.18           C  
ANISOU 2468  CD1 ILE A 373     7642   5983   4682  -1918    847    287       C  
ATOM   2469  N   ALA A 374      -3.738   7.022  -2.475  1.00 49.38           N  
ANISOU 2469  N   ALA A 374     7284   6399   5078  -1943    964   -238       N  
ATOM   2470  CA  ALA A 374      -3.683   5.755  -3.205  1.00 50.73           C  
ANISOU 2470  CA  ALA A 374     7403   6551   5323  -1948    989   -333       C  
ATOM   2471  C   ALA A 374      -4.546   4.714  -2.506  1.00 51.70           C  
ANISOU 2471  C   ALA A 374     7557   6604   5481  -1831    961   -305       C  
ATOM   2472  O   ALA A 374      -5.140   4.982  -1.445  1.00 51.83           O  
ANISOU 2472  O   ALA A 374     7619   6593   5482  -1734    926   -214       O  
ATOM   2473  CB  ALA A 374      -2.255   5.262  -3.368  1.00 50.25           C  
ANISOU 2473  CB  ALA A 374     7201   6589   5305  -1948    969   -415       C  
ATOM   2474  N   LEU A 375      -4.640   3.546  -3.136  1.00 53.36           N  
ANISOU 2474  N   LEU A 375     7740   6797   5736  -1839    978   -390       N  
ATOM   2475  CA  LEU A 375      -5.661   2.576  -2.767  1.00 55.10           C  
ANISOU 2475  CA  LEU A 375     8020   6939   5976  -1748    974   -398       C  
ATOM   2476  C   LEU A 375      -5.027   1.305  -2.302  1.00 55.50           C  
ANISOU 2476  C   LEU A 375     7962   7084   6042  -1674    947   -440       C  
ATOM   2477  O   LEU A 375      -4.114   0.784  -2.960  1.00 56.59           O  
ANISOU 2477  O   LEU A 375     8013   7292   6198  -1736    940   -502       O  
ATOM   2478  CB  LEU A 375      -6.580   2.281  -3.938  1.00 54.62           C  
ANISOU 2478  CB  LEU A 375     8058   6763   5934  -1839   1013   -465       C  
ATOM   2479  CG  LEU A 375      -7.404   3.465  -4.464  1.00 55.99           C  
ANISOU 2479  CG  LEU A 375     8363   6824   6088  -1936   1042   -405       C  
ATOM   2480  CD1 LEU A 375      -8.444   2.971  -5.467  1.00 56.99           C  
ANISOU 2480  CD1 LEU A 375     8596   6810   6246  -2023   1067   -467       C  
ATOM   2481  CD2 LEU A 375      -8.075   4.254  -3.347  1.00 57.10           C  
ANISOU 2481  CD2 LEU A 375     8589   6901   6203  -1831   1010   -280       C  
ATOM   2482  N   GLY A 376      -5.506   0.834  -1.154  1.00 53.99           N  
ANISOU 2482  N   GLY A 376     7770   6901   5842  -1539    932   -398       N  
ATOM   2483  CA  GLY A 376      -5.052  -0.420  -0.609  1.00 53.07           C  
ANISOU 2483  CA  GLY A 376     7557   6888   5718  -1471    918   -424       C  
ATOM   2484  C   GLY A 376      -6.235  -1.160  -0.038  1.00 53.43           C  
ANISOU 2484  C   GLY A 376     7663   6887   5750  -1346    943   -449       C  
ATOM   2485  O   GLY A 376      -7.123  -0.546   0.525  1.00 53.69           O  
ANISOU 2485  O   GLY A 376     7766   6838   5794  -1263    947   -400       O  
ATOM   2486  N   THR A 377      -6.233  -2.479  -0.203  1.00 55.04           N  
ANISOU 2486  N   THR A 377     7839   7146   5929  -1328    956   -530       N  
ATOM   2487  CA  THR A 377      -7.306  -3.339   0.262  1.00 58.29           C  
ANISOU 2487  CA  THR A 377     8304   7529   6316  -1205    990   -593       C  
ATOM   2488  C   THR A 377      -7.052  -4.005   1.610  1.00 60.60           C  
ANISOU 2488  C   THR A 377     8479   7982   6565  -1078   1001   -550       C  
ATOM   2489  O   THR A 377      -7.998  -4.274   2.349  1.00 64.38           O  
ANISOU 2489  O   THR A 377     8985   8442   7036   -932   1036   -574       O  
ATOM   2490  CB  THR A 377      -7.531  -4.472  -0.741  1.00 57.18           C  
ANISOU 2490  CB  THR A 377     8209   7373   6143  -1270   1002   -727       C  
ATOM   2491  CG2 THR A 377      -8.721  -5.310  -0.348  1.00 59.54           C  
ANISOU 2491  CG2 THR A 377     8589   7622   6412  -1143   1043   -824       C  
ATOM   2492  OG1 THR A 377      -7.757  -3.905  -2.029  1.00 57.83           O  
ANISOU 2492  OG1 THR A 377     8380   7325   6270  -1407    995   -766       O  
ATOM   2493  N   ASP A 378      -5.793  -4.298   1.916  1.00 58.44           N  
ANISOU 2493  N   ASP A 378     8073   7863   6267  -1132    971   -488       N  
ATOM   2494  CA  ASP A 378      -5.472  -5.095   3.091  1.00 58.70           C  
ANISOU 2494  CA  ASP A 378     7983   8072   6246  -1049    985   -442       C  
ATOM   2495  C   ASP A 378      -6.075  -6.497   2.991  1.00 56.06           C  
ANISOU 2495  C   ASP A 378     7672   7796   5832   -993   1038   -555       C  
ATOM   2496  O   ASP A 378      -6.912  -6.871   3.795  1.00 58.56           O  
ANISOU 2496  O   ASP A 378     7983   8148   6118   -852   1094   -589       O  
ATOM   2497  CB  ASP A 378      -5.952  -4.371   4.363  1.00 61.68           C  
ANISOU 2497  CB  ASP A 378     8317   8468   6650   -921    994   -357       C  
ATOM   2498  CG  ASP A 378      -5.434  -4.999   5.648  1.00 64.38           C  
ANISOU 2498  CG  ASP A 378     8495   9022   6946   -864   1007   -281       C  
ATOM   2499  OD1 ASP A 378      -4.948  -6.149   5.618  1.00 65.03           O  
ANISOU 2499  OD1 ASP A 378     8518   9233   6956   -901   1026   -304       O  
ATOM   2500  OD2 ASP A 378      -5.541  -4.334   6.695  1.00 67.32           O1-
ANISOU 2500  OD2 ASP A 378     8792   9440   7348   -788    994   -191       O1-
ATOM   2501  N   THR A 379      -5.643  -7.258   1.997  1.00 53.23           N  
ANISOU 2501  N   THR A 379     7335   7453   5435  -1101   1018   -620       N  
ATOM   2502  CA  THR A 379      -6.010  -8.674   1.857  1.00 52.89           C  
ANISOU 2502  CA  THR A 379     7308   7500   5286  -1077   1053   -726       C  
ATOM   2503  C   THR A 379      -4.876  -9.466   1.222  1.00 51.14           C  
ANISOU 2503  C   THR A 379     7026   7390   5014  -1208    994   -704       C  
ATOM   2504  O   THR A 379      -3.891  -8.890   0.774  1.00 47.73           O  
ANISOU 2504  O   THR A 379     6551   6933   4650  -1306    929   -627       O  
ATOM   2505  CB  THR A 379      -7.250  -8.898   0.962  1.00 52.96           C  
ANISOU 2505  CB  THR A 379     7478   7346   5298  -1063   1079   -890       C  
ATOM   2506  CG2 THR A 379      -8.560  -8.593   1.722  1.00 55.61           C  
ANISOU 2506  CG2 THR A 379     7885   7584   5659   -889   1141   -940       C  
ATOM   2507  OG1 THR A 379      -7.134  -8.105  -0.230  1.00 49.92           O  
ANISOU 2507  OG1 THR A 379     7164   6806   4998  -1190   1031   -898       O  
ATOM   2508  N   ALA A 380      -5.038 -10.789   1.203  1.00 52.08           N  
ANISOU 2508  N   ALA A 380     7145   7633   5010  -1201   1015   -774       N  
ATOM   2509  CA  ALA A 380      -4.126 -11.677   0.498  1.00 54.42           C  
ANISOU 2509  CA  ALA A 380     7405   8030   5244  -1321    946   -760       C  
ATOM   2510  C   ALA A 380      -4.110 -11.402  -1.008  1.00 56.51           C  
ANISOU 2510  C   ALA A 380     7741   8152   5578  -1429    883   -838       C  
ATOM   2511  O   ALA A 380      -5.047 -10.807  -1.556  1.00 58.79           O  
ANISOU 2511  O   ALA A 380     8134   8275   5928  -1421    911   -932       O  
ATOM   2512  CB  ALA A 380      -4.511 -13.123   0.743  1.00 55.33           C  
ANISOU 2512  CB  ALA A 380     7528   8308   5185  -1290    985   -838       C  
ATOM   2513  N   PRO A 381      -3.042 -11.834  -1.691  1.00 56.97           N  
ANISOU 2513  N   PRO A 381     7738   8276   5634  -1537    794   -789       N  
ATOM   2514  CA  PRO A 381      -3.073 -11.685  -3.138  1.00 57.03           C  
ANISOU 2514  CA  PRO A 381     7786   8179   5702  -1637    738   -874       C  
ATOM   2515  C   PRO A 381      -4.150 -12.559  -3.722  1.00 57.16           C  
ANISOU 2515  C   PRO A 381     7907   8183   5626  -1649    757  -1036       C  
ATOM   2516  O   PRO A 381      -4.354 -13.678  -3.226  1.00 60.01           O  
ANISOU 2516  O   PRO A 381     8276   8682   5843  -1611    775  -1068       O  
ATOM   2517  CB  PRO A 381      -1.692 -12.170  -3.559  1.00 58.26           C  
ANISOU 2517  CB  PRO A 381     7838   8436   5863  -1717    631   -781       C  
ATOM   2518  CG  PRO A 381      -0.832 -11.834  -2.368  1.00 56.78           C  
ANISOU 2518  CG  PRO A 381     7566   8312   5694  -1671    631   -623       C  
ATOM   2519  CD  PRO A 381      -1.707 -12.237  -1.221  1.00 56.71           C  
ANISOU 2519  CD  PRO A 381     7588   8382   5577  -1575    729   -639       C  
ATOM   2520  N   GLY A 382      -4.838 -12.037  -4.742  1.00 54.26           N  
ANISOU 2520  N   GLY A 382     7623   7658   5336  -1710    755  -1138       N  
ATOM   2521  CA  GLY A 382      -6.052 -12.659  -5.298  1.00 53.40           C  
ANISOU 2521  CA  GLY A 382     7643   7479   5165  -1728    774  -1311       C  
ATOM   2522  C   GLY A 382      -7.351 -12.245  -4.627  1.00 52.07           C  
ANISOU 2522  C   GLY A 382     7599   7175   5010  -1613    867  -1382       C  
ATOM   2523  O   GLY A 382      -8.434 -12.491  -5.142  1.00 52.12           O  
ANISOU 2523  O   GLY A 382     7738   7059   5007  -1629    879  -1529       O  
ATOM   2524  N   GLY A 383      -7.242 -11.610  -3.471  1.00 50.45           N  
ANISOU 2524  N   GLY A 383     7351   6981   4835  -1495    922  -1278       N  
ATOM   2525  CA  GLY A 383      -8.395 -11.061  -2.796  1.00 50.81           C  
ANISOU 2525  CA  GLY A 383     7495   6889   4919  -1366    997  -1319       C  
ATOM   2526  C   GLY A 383      -9.088  -9.954  -3.582  1.00 50.49           C  
ANISOU 2526  C   GLY A 383     7566   6611   5006  -1429    990  -1341       C  
ATOM   2527  O   GLY A 383      -8.611  -9.528  -4.643  1.00 47.64           O  
ANISOU 2527  O   GLY A 383     7186   6211   4704  -1578    941  -1321       O  
ATOM   2528  N   PRO A 384     -10.213  -9.472  -3.043  1.00 51.44           N  
ANISOU 2528  N   PRO A 384     7796   6576   5170  -1312   1039  -1373       N  
ATOM   2529  CA  PRO A 384     -11.062  -8.499  -3.691  1.00 52.73           C  
ANISOU 2529  CA  PRO A 384     8097   6497   5442  -1366   1033  -1386       C  
ATOM   2530  C   PRO A 384     -10.506  -7.081  -3.618  1.00 52.55           C  
ANISOU 2530  C   PRO A 384     8021   6442   5506  -1408   1025  -1222       C  
ATOM   2531  O   PRO A 384     -11.101  -6.201  -2.987  1.00 52.13           O  
ANISOU 2531  O   PRO A 384     8026   6274   5508  -1314   1046  -1154       O  
ATOM   2532  CB  PRO A 384     -12.347  -8.603  -2.890  1.00 53.44           C  
ANISOU 2532  CB  PRO A 384     8309   6455   5542  -1187   1080  -1461       C  
ATOM   2533  CG  PRO A 384     -11.863  -8.879  -1.519  1.00 52.77           C  
ANISOU 2533  CG  PRO A 384     8087   6565   5397  -1023   1122  -1392       C  
ATOM   2534  CD  PRO A 384     -10.715  -9.816  -1.702  1.00 51.57           C  
ANISOU 2534  CD  PRO A 384     7803   6651   5139  -1111   1103  -1385       C  
ATOM   2535  N   THR A 385      -9.402  -6.851  -4.309  1.00 53.05           N  
ANISOU 2535  N   THR A 385     7977   6601   5578  -1545    990  -1166       N  
ATOM   2536  CA  THR A 385      -8.854  -5.512  -4.396  1.00 54.80           C  
ANISOU 2536  CA  THR A 385     8156   6798   5867  -1601    987  -1040       C  
ATOM   2537  C   THR A 385      -9.777  -4.556  -5.136  1.00 59.55           C  
ANISOU 2537  C   THR A 385     8897   7195   6536  -1689    999  -1042       C  
ATOM   2538  O   THR A 385      -9.878  -3.389  -4.767  1.00 63.95           O  
ANISOU 2538  O   THR A 385     9480   7690   7129  -1670   1011   -936       O  
ATOM   2539  CB  THR A 385      -7.492  -5.504  -5.100  1.00 54.23           C  
ANISOU 2539  CB  THR A 385     7943   6861   5800  -1721    950  -1009       C  
ATOM   2540  CG2 THR A 385      -6.461  -6.152  -4.230  1.00 55.55           C  
ANISOU 2540  CG2 THR A 385     7977   7211   5917  -1643    927   -953       C  
ATOM   2541  OG1 THR A 385      -7.569  -6.240  -6.319  1.00 55.38           O  
ANISOU 2541  OG1 THR A 385     8098   7005   5939  -1845    920  -1117       O  
ATOM   2542  N   ALA A 386     -10.456  -5.042  -6.174  1.00 62.68           N  
ANISOU 2542  N   ALA A 386     9388   7488   6942  -1797    988  -1155       N  
ATOM   2543  CA  ALA A 386     -11.363  -4.201  -6.984  1.00 62.98           C  
ANISOU 2543  CA  ALA A 386     9565   7321   7044  -1918    994  -1150       C  
ATOM   2544  C   ALA A 386     -12.383  -3.395  -6.162  1.00 61.14           C  
ANISOU 2544  C   ALA A 386     9472   6907   6848  -1800   1010  -1076       C  
ATOM   2545  O   ALA A 386     -12.809  -2.317  -6.567  1.00 60.25           O  
ANISOU 2545  O   ALA A 386     9445   6664   6782  -1891   1014   -993       O  
ATOM   2546  CB  ALA A 386     -12.089  -5.074  -7.984  1.00 66.07           C  
ANISOU 2546  CB  ALA A 386    10051   7616   7438  -2031    969  -1298       C  
ATOM   2547  N   LEU A 387     -12.763  -3.930  -5.007  1.00 59.44           N  
ANISOU 2547  N   LEU A 387     9273   6699   6614  -1595   1018  -1100       N  
ATOM   2548  CA  LEU A 387     -13.716  -3.277  -4.116  1.00 60.32           C  
ANISOU 2548  CA  LEU A 387     9496   6652   6772  -1442   1022  -1033       C  
ATOM   2549  C   LEU A 387     -13.292  -1.888  -3.692  1.00 59.71           C  
ANISOU 2549  C   LEU A 387     9376   6599   6712  -1446   1016   -852       C  
ATOM   2550  O   LEU A 387     -14.120  -0.990  -3.566  1.00 60.13           O  
ANISOU 2550  O   LEU A 387     9558   6474   6814  -1427   1000   -767       O  
ATOM   2551  CB  LEU A 387     -13.906  -4.115  -2.840  1.00 59.59           C  
ANISOU 2551  CB  LEU A 387     9355   6642   6644  -1205   1042  -1086       C  
ATOM   2552  CG  LEU A 387     -14.812  -5.332  -2.799  1.00 60.17           C  
ANISOU 2552  CG  LEU A 387     9525   6637   6699  -1108   1057  -1272       C  
ATOM   2553  CD1 LEU A 387     -15.123  -5.734  -1.364  1.00 60.64           C  
ANISOU 2553  CD1 LEU A 387     9532   6770   6739   -846   1093  -1286       C  
ATOM   2554  CD2 LEU A 387     -16.077  -5.043  -3.554  1.00 62.52           C  
ANISOU 2554  CD2 LEU A 387    10046   6630   7079  -1169   1030  -1332       C  
ATOM   2555  N   GLU A 388     -11.998  -1.719  -3.445  1.00 59.87           N  
ANISOU 2555  N   GLU A 388     9224   6836   6690  -1470   1021   -791       N  
ATOM   2556  CA  GLU A 388     -11.483  -0.481  -2.860  1.00 60.02           C  
ANISOU 2556  CA  GLU A 388     9189   6911   6706  -1456   1010   -636       C  
ATOM   2557  C   GLU A 388     -11.847   0.683  -3.771  1.00 58.56           C  
ANISOU 2557  C   GLU A 388     9113   6595   6541  -1620   1010   -566       C  
ATOM   2558  O   GLU A 388     -12.191   1.769  -3.296  1.00 59.91           O  
ANISOU 2558  O   GLU A 388     9346   6702   6716  -1588    993   -439       O  
ATOM   2559  CB  GLU A 388      -9.973  -0.588  -2.625  1.00 59.06           C  
ANISOU 2559  CB  GLU A 388     8877   7022   6543  -1482   1008   -611       C  
ATOM   2560  CG  GLU A 388      -9.347   0.570  -1.886  1.00 62.18           C  
ANISOU 2560  CG  GLU A 388     9207   7492   6925  -1459    989   -475       C  
ATOM   2561  CD  GLU A 388      -9.923   0.765  -0.500  1.00 64.04           C  
ANISOU 2561  CD  GLU A 388     9451   7713   7169  -1271    968   -397       C  
ATOM   2562  OE1 GLU A 388     -10.219  -0.238   0.184  1.00 63.33           O  
ANISOU 2562  OE1 GLU A 388     9324   7661   7079  -1133    979   -454       O  
ATOM   2563  OE2 GLU A 388     -10.080   1.935  -0.107  1.00 68.67           O1-
ANISOU 2563  OE2 GLU A 388    10073   8263   7754  -1262    940   -281       O1-
ATOM   2564  N   LEU A 389     -11.806   0.421  -5.075  1.00 55.65           N  
ANISOU 2564  N   LEU A 389     8765   6199   6179  -1800   1027   -645       N  
ATOM   2565  CA  LEU A 389     -12.213   1.394  -6.078  1.00 53.90           C  
ANISOU 2565  CA  LEU A 389     8642   5867   5971  -1986   1041   -588       C  
ATOM   2566  C   LEU A 389     -13.637   1.836  -5.832  1.00 54.54           C  
ANISOU 2566  C   LEU A 389     8930   5697   6096  -1942   1016   -526       C  
ATOM   2567  O   LEU A 389     -13.932   3.020  -5.728  1.00 53.79           O  
ANISOU 2567  O   LEU A 389     8912   5536   5991  -1981   1008   -385       O  
ATOM   2568  CB  LEU A 389     -12.056   0.805  -7.484  1.00 53.44           C  
ANISOU 2568  CB  LEU A 389     8555   5823   5925  -2177   1059   -702       C  
ATOM   2569  CG  LEU A 389     -10.601   0.832  -7.981  1.00 51.55           C  
ANISOU 2569  CG  LEU A 389     8115   5815   5656  -2259   1080   -724       C  
ATOM   2570  CD1 LEU A 389     -10.269  -0.296  -8.936  1.00 50.87           C  
ANISOU 2570  CD1 LEU A 389     7947   5796   5584  -2349   1069   -861       C  
ATOM   2571  CD2 LEU A 389     -10.269   2.175  -8.619  1.00 52.08           C  
ANISOU 2571  CD2 LEU A 389     8165   5921   5702  -2412   1123   -637       C  
ATOM   2572  N   GLN A 390     -14.519   0.863  -5.723  1.00 56.37           N  
ANISOU 2572  N   GLN A 390     9258   5787   6373  -1853    998   -633       N  
ATOM   2573  CA  GLN A 390     -15.909   1.160  -5.469  1.00 59.30           C  
ANISOU 2573  CA  GLN A 390     9837   5886   6808  -1784    961   -593       C  
ATOM   2574  C   GLN A 390     -16.079   2.080  -4.256  1.00 59.53           C  
ANISOU 2574  C   GLN A 390     9878   5901   6838  -1613    932   -434       C  
ATOM   2575  O   GLN A 390     -16.779   3.078  -4.326  1.00 59.54           O  
ANISOU 2575  O   GLN A 390    10020   5739   6865  -1655    898   -300       O  
ATOM   2576  CB  GLN A 390     -16.679  -0.137  -5.248  1.00 61.66           C  
ANISOU 2576  CB  GLN A 390    10209   6070   7148  -1651    951   -764       C  
ATOM   2577  CG  GLN A 390     -18.180   0.044  -5.299  1.00 64.15           C  
ANISOU 2577  CG  GLN A 390    10768   6052   7554  -1611    907   -762       C  
ATOM   2578  CD  GLN A 390     -18.908  -1.132  -4.718  1.00 65.92           C  
ANISOU 2578  CD  GLN A 390    11053   6181   7812  -1403    900   -935       C  
ATOM   2579  NE2 GLN A 390     -19.951  -0.850  -3.959  1.00 68.41           N  
ANISOU 2579  NE2 GLN A 390    11506   6279   8207  -1211    862   -898       N  
ATOM   2580  OE1 GLN A 390     -18.533  -2.292  -4.937  1.00 65.56           O  
ANISOU 2580  OE1 GLN A 390    10930   6263   7717  -1407    927  -1103       O  
ATOM   2581  N   PHE A 391     -15.417   1.743  -3.154  1.00 58.90           N  
ANISOU 2581  N   PHE A 391     9645   6006   6729  -1432    936   -440       N  
ATOM   2582  CA  PHE A 391     -15.540   2.521  -1.921  1.00 58.73           C  
ANISOU 2582  CA  PHE A 391     9605   6000   6711  -1260    896   -298       C  
ATOM   2583  C   PHE A 391     -14.900   3.905  -2.000  1.00 55.52           C  
ANISOU 2583  C   PHE A 391     9166   5686   6244  -1384    883   -132       C  
ATOM   2584  O   PHE A 391     -15.378   4.838  -1.348  1.00 54.93           O  
ANISOU 2584  O   PHE A 391     9158   5538   6173  -1307    829     15       O  
ATOM   2585  CB  PHE A 391     -14.934   1.758  -0.747  1.00 59.37           C  
ANISOU 2585  CB  PHE A 391     9507   6280   6771  -1063    908   -348       C  
ATOM   2586  CG  PHE A 391     -15.595   0.441  -0.482  1.00 61.42           C  
ANISOU 2586  CG  PHE A 391     9792   6480   7066   -912    931   -511       C  
ATOM   2587  CD1 PHE A 391     -16.934   0.378  -0.144  1.00 63.96           C  
ANISOU 2587  CD1 PHE A 391    10269   6566   7469   -757    903   -534       C  
ATOM   2588  CD2 PHE A 391     -14.872  -0.738  -0.559  1.00 63.15           C  
ANISOU 2588  CD2 PHE A 391     9883   6879   7231   -919    977   -643       C  
ATOM   2589  CE1 PHE A 391     -17.544  -0.837   0.112  1.00 65.97           C  
ANISOU 2589  CE1 PHE A 391    10549   6772   7746   -606    932   -709       C  
ATOM   2590  CE2 PHE A 391     -15.476  -1.962  -0.302  1.00 64.94           C  
ANISOU 2590  CE2 PHE A 391    10135   7076   7461   -784   1004   -803       C  
ATOM   2591  CZ  PHE A 391     -16.815  -2.011   0.036  1.00 66.04           C  
ANISOU 2591  CZ  PHE A 391    10428   6987   7678   -624    989   -849       C  
ATOM   2592  N   ALA A 392     -13.831   4.025  -2.790  1.00 52.33           N  
ANISOU 2592  N   ALA A 392     8659   5445   5780  -1566    927   -162       N  
ATOM   2593  CA  ALA A 392     -13.252   5.332  -3.116  1.00 51.87           C  
ANISOU 2593  CA  ALA A 392     8587   5471   5651  -1714    932    -40       C  
ATOM   2594  C   ALA A 392     -14.346   6.277  -3.588  1.00 54.39           C  
ANISOU 2594  C   ALA A 392     9108   5580   5976  -1812    908     83       C  
ATOM   2595  O   ALA A 392     -14.550   7.363  -3.040  1.00 54.24           O  
ANISOU 2595  O   ALA A 392     9145   5548   5917  -1786    863    242       O  
ATOM   2596  CB  ALA A 392     -12.197   5.204  -4.201  1.00 49.69           C  
ANISOU 2596  CB  ALA A 392     8198   5346   5334  -1903    994   -126       C  
ATOM   2597  N   VAL A 393     -15.061   5.824  -4.603  1.00 56.20           N  
ANISOU 2597  N   VAL A 393     9453   5644   6256  -1932    929     15       N  
ATOM   2598  CA  VAL A 393     -16.099   6.613  -5.222  1.00 58.84           C  
ANISOU 2598  CA  VAL A 393     9991   5762   6605  -2068    908    132       C  
ATOM   2599  C   VAL A 393     -17.275   6.754  -4.291  1.00 61.26           C  
ANISOU 2599  C   VAL A 393    10451   5839   6983  -1872    822    223       C  
ATOM   2600  O   VAL A 393     -17.742   7.854  -4.032  1.00 63.61           O  
ANISOU 2600  O   VAL A 393    10861   6052   7254  -1887    770    407       O  
ATOM   2601  CB  VAL A 393     -16.587   5.940  -6.505  1.00 60.40           C  
ANISOU 2601  CB  VAL A 393    10265   5828   6855  -2249    940     19       C  
ATOM   2602  CG1 VAL A 393     -17.705   6.745  -7.155  1.00 62.74           C  
ANISOU 2602  CG1 VAL A 393    10785   5879   7175  -2414    913    155       C  
ATOM   2603  CG2 VAL A 393     -15.408   5.733  -7.452  1.00 59.88           C  
ANISOU 2603  CG2 VAL A 393    10019   6000   6733  -2425   1019    -79       C  
ATOM   2604  N   GLU A 394     -17.763   5.629  -3.791  1.00 62.12           N  
ANISOU 2604  N   GLU A 394    10571   5852   7181  -1680    804     92       N  
ATOM   2605  CA  GLU A 394     -19.035   5.639  -3.085  1.00 65.07           C  
ANISOU 2605  CA  GLU A 394    11109   5961   7652  -1487    726    144       C  
ATOM   2606  C   GLU A 394     -18.948   6.111  -1.640  1.00 65.26           C  
ANISOU 2606  C   GLU A 394    11054   6071   7671  -1243    668    256       C  
ATOM   2607  O   GLU A 394     -19.920   6.627  -1.122  1.00 68.53           O  
ANISOU 2607  O   GLU A 394    11606   6282   8149  -1119    586    376       O  
ATOM   2608  CB  GLU A 394     -19.727   4.278  -3.195  1.00 65.82           C  
ANISOU 2608  CB  GLU A 394    11267   5901   7843  -1379    734    -61       C  
ATOM   2609  CG  GLU A 394     -20.170   3.991  -4.627  1.00 66.93           C  
ANISOU 2609  CG  GLU A 394    11544   5877   8010  -1632    754   -138       C  
ATOM   2610  CD  GLU A 394     -20.854   2.664  -4.784  1.00 67.85           C  
ANISOU 2610  CD  GLU A 394    11737   5837   8206  -1545    753   -356       C  
ATOM   2611  OE1 GLU A 394     -20.993   1.971  -3.754  1.00 68.76           O  
ANISOU 2611  OE1 GLU A 394    11797   5980   8348  -1275    750   -449       O  
ATOM   2612  OE2 GLU A 394     -21.240   2.325  -5.926  1.00 67.56           O1-
ANISOU 2612  OE2 GLU A 394    11809   5664   8197  -1753    757   -438       O1-
ATOM   2613  N   ARG A 395     -17.799   5.963  -0.993  1.00 63.16           N  
ANISOU 2613  N   ARG A 395    10567   6095   7335  -1180    700    228       N  
ATOM   2614  CA  ARG A 395     -17.693   6.324   0.413  1.00 63.26           C  
ANISOU 2614  CA  ARG A 395    10481   6208   7349   -956    641    324       C  
ATOM   2615  C   ARG A 395     -16.824   7.550   0.608  1.00 62.15           C  
ANISOU 2615  C   ARG A 395    10263   6256   7095  -1067    618    480       C  
ATOM   2616  O   ARG A 395     -17.133   8.434   1.409  1.00 60.61           O  
ANISOU 2616  O   ARG A 395    10093   6046   6889   -970    532    645       O  
ATOM   2617  CB  ARG A 395     -17.165   5.134   1.234  1.00 62.90           C  
ANISOU 2617  CB  ARG A 395    10242   6338   7319   -772    684    173       C  
ATOM   2618  CG  ARG A 395     -18.004   3.860   1.046  1.00 65.52           C  
ANISOU 2618  CG  ARG A 395    10650   6508   7738   -660    717    -10       C  
ATOM   2619  CD  ARG A 395     -19.496   4.190   1.343  1.00 70.84           C  
ANISOU 2619  CD  ARG A 395    11525   6866   8525   -503    639     52       C  
ATOM   2620  NE  ARG A 395     -20.261   3.313   2.255  1.00 74.96           N  
ANISOU 2620  NE  ARG A 395    12031   7311   9139   -205    635    -63       N  
ATOM   2621  CZ  ARG A 395     -20.651   3.598   3.510  1.00 77.57           C  
ANISOU 2621  CZ  ARG A 395    12295   7653   9526     57    579     18       C  
ATOM   2622  NH1 ARG A 395     -20.309   4.722   4.138  1.00 77.90           N1+
ANISOU 2622  NH1 ARG A 395    12266   7796   9534     66    507    225       N1+
ATOM   2623  NH2 ARG A 395     -21.389   2.705   4.171  1.00 79.94           N  
ANISOU 2623  NH2 ARG A 395    12584   7877   9912    320    595   -123       N  
ATOM   2624  N   GLY A 396     -15.714   7.598  -0.105  1.00 61.89           N  
ANISOU 2624  N   GLY A 396    10132   6407   6975  -1261    688    425       N  
ATOM   2625  CA  GLY A 396     -14.818   8.738  -0.001  1.00 62.24           C  
ANISOU 2625  CA  GLY A 396    10108   6637   6902  -1375    675    538       C  
ATOM   2626  C   GLY A 396     -15.373   9.872  -0.823  1.00 64.42           C  
ANISOU 2626  C   GLY A 396    10565   6792   7120  -1563    663    678       C  
ATOM   2627  O   GLY A 396     -15.106  11.050  -0.543  1.00 65.63           O  
ANISOU 2627  O   GLY A 396    10730   7036   7171  -1620    621    823       O  
ATOM   2628  N   GLY A 397     -16.133   9.508  -1.856  1.00 65.30           N  
ANISOU 2628  N   GLY A 397    10817   6707   7287  -1676    698    633       N  
ATOM   2629  CA  GLY A 397     -16.694  10.481  -2.759  1.00 65.83           C  
ANISOU 2629  CA  GLY A 397    11056   6654   7302  -1891    698    767       C  
ATOM   2630  C   GLY A 397     -15.679  10.948  -3.784  1.00 63.72           C  
ANISOU 2630  C   GLY A 397    10704   6592   6916  -2145    796    730       C  
ATOM   2631  O   GLY A 397     -15.514  12.140  -3.973  1.00 65.87           O  
ANISOU 2631  O   GLY A 397    11020   6942   7065  -2280    798    868       O  
ATOM   2632  N   MET A 398     -14.965  10.037  -4.428  1.00 61.32           N  
ANISOU 2632  N   MET A 398    10268   6391   6637  -2203    880    543       N  
ATOM   2633  CA  MET A 398     -14.210  10.438  -5.598  1.00 61.20           C  
ANISOU 2633  CA  MET A 398    10186   6530   6538  -2447    976    501       C  
ATOM   2634  C   MET A 398     -15.040  10.295  -6.846  1.00 62.49           C  
ANISOU 2634  C   MET A 398    10478   6523   6743  -2649   1014    497       C  
ATOM   2635  O   MET A 398     -16.057   9.599  -6.861  1.00 60.48           O  
ANISOU 2635  O   MET A 398    10349   6030   6600  -2592    969    475       O  
ATOM   2636  CB  MET A 398     -12.964   9.592  -5.826  1.00 60.68           C  
ANISOU 2636  CB  MET A 398     9905   6667   6484  -2431   1038    312       C  
ATOM   2637  CG  MET A 398     -12.133   9.221  -4.627  1.00 61.09           C  
ANISOU 2637  CG  MET A 398     9812   6858   6540  -2225    998    267       C  
ATOM   2638  SD  MET A 398     -10.501   8.666  -5.158  1.00 62.29           S  
ANISOU 2638  SD  MET A 398     9734   7257   6677  -2282   1070     94       S  
ATOM   2639  CE  MET A 398      -9.773   8.631  -3.514  1.00 60.57           C  
ANISOU 2639  CE  MET A 398     9405   7159   6449  -2062    995    123       C  
ATOM   2640  N   THR A 399     -14.571  10.957  -7.903  1.00 63.31           N  
ANISOU 2640  N   THR A 399    10540   6758   6754  -2891   1102    509       N  
ATOM   2641  CA  THR A 399     -15.021  10.635  -9.241  1.00 63.99           C  
ANISOU 2641  CA  THR A 399    10671   6760   6883  -3114   1159    462       C  
ATOM   2642  C   THR A 399     -14.321   9.332  -9.603  1.00 62.33           C  
ANISOU 2642  C   THR A 399    10287   6644   6752  -3066   1193    239       C  
ATOM   2643  O   THR A 399     -13.242   9.043  -9.098  1.00 58.20           O  
ANISOU 2643  O   THR A 399     9593   6310   6210  -2939   1204    149       O  
ATOM   2644  CB  THR A 399     -14.700  11.745 -10.277  1.00 64.16           C  
ANISOU 2644  CB  THR A 399    10670   6934   6773  -3393   1257    541       C  
ATOM   2645  CG2 THR A 399     -15.121  13.109  -9.763  1.00 64.85           C  
ANISOU 2645  CG2 THR A 399    10902   7000   6736  -3424   1221    767       C  
ATOM   2646  OG1 THR A 399     -13.301  11.763 -10.566  1.00 62.59           O  
ANISOU 2646  OG1 THR A 399    10241   7030   6512  -3408   1343    409       O  
ATOM   2647  N   PRO A 400     -14.949   8.522 -10.466  1.00 65.08           N  
ANISOU 2647  N   PRO A 400    10687   6848   7191  -3177   1197    154       N  
ATOM   2648  CA  PRO A 400     -14.250   7.348 -10.976  1.00 63.87           C  
ANISOU 2648  CA  PRO A 400    10364   6812   7093  -3171   1225    -46       C  
ATOM   2649  C   PRO A 400     -12.851   7.672 -11.533  1.00 63.25           C  
ANISOU 2649  C   PRO A 400    10056   7035   6943  -3254   1310   -110       C  
ATOM   2650  O   PRO A 400     -11.922   6.885 -11.359  1.00 60.00           O  
ANISOU 2650  O   PRO A 400     9479   6762   6556  -3141   1308   -241       O  
ATOM   2651  CB  PRO A 400     -15.193   6.846 -12.079  1.00 65.36           C  
ANISOU 2651  CB  PRO A 400    10660   6818   7357  -3367   1221    -88       C  
ATOM   2652  CG  PRO A 400     -16.549   7.218 -11.589  1.00 67.25           C  
ANISOU 2652  CG  PRO A 400    11157   6758   7635  -3332   1149     47       C  
ATOM   2653  CD  PRO A 400     -16.380   8.513 -10.836  1.00 67.54           C  
ANISOU 2653  CD  PRO A 400    11230   6858   7573  -3276   1148    233       C  
ATOM   2654  N   LEU A 401     -12.715   8.820 -12.196  1.00 66.07           N  
ANISOU 2654  N   LEU A 401    10406   7489   7208  -3447   1384    -18       N  
ATOM   2655  CA  LEU A 401     -11.452   9.203 -12.820  1.00 65.34           C  
ANISOU 2655  CA  LEU A 401    10099   7675   7050  -3528   1477    -95       C  
ATOM   2656  C   LEU A 401     -10.335   9.356 -11.809  1.00 62.26           C  
ANISOU 2656  C   LEU A 401     9597   7441   6618  -3322   1461   -130       C  
ATOM   2657  O   LEU A 401      -9.216   8.864 -12.007  1.00 58.45           O  
ANISOU 2657  O   LEU A 401     8923   7124   6162  -3268   1484   -265       O  
ATOM   2658  CB  LEU A 401     -11.635  10.512 -13.564  1.00 68.34           C  
ANISOU 2658  CB  LEU A 401    10517   8134   7315  -3761   1568     23       C  
ATOM   2659  CG  LEU A 401     -10.411  10.993 -14.327  1.00 69.65           C  
ANISOU 2659  CG  LEU A 401    10459   8596   7409  -3854   1684    -71       C  
ATOM   2660  CD1 LEU A 401      -9.943   9.949 -15.341  1.00 71.44           C  
ANISOU 2660  CD1 LEU A 401    10498   8903   7743  -3912   1711   -244       C  
ATOM   2661  CD2 LEU A 401     -10.736  12.302 -15.011  1.00 71.29           C  
ANISOU 2661  CD2 LEU A 401    10720   8886   7479  -4094   1784     57       C  
ATOM   2662  N   GLU A 402     -10.666  10.041 -10.720  1.00 62.96           N  
ANISOU 2662  N   GLU A 402     9808   7465   6647  -3212   1409      1       N  
ATOM   2663  CA  GLU A 402      -9.755  10.187  -9.577  1.00 62.69           C  
ANISOU 2663  CA  GLU A 402     9693   7548   6579  -3018   1369    -13       C  
ATOM   2664  C   GLU A 402      -9.448   8.852  -8.854  1.00 60.04           C  
ANISOU 2664  C   GLU A 402     9281   7179   6352  -2813   1300   -117       C  
ATOM   2665  O   GLU A 402      -8.313   8.631  -8.419  1.00 59.40           O  
ANISOU 2665  O   GLU A 402     9056   7244   6271  -2711   1293   -193       O  
ATOM   2666  CB  GLU A 402     -10.325  11.197  -8.572  1.00 63.90           C  
ANISOU 2666  CB  GLU A 402     9998   7633   6647  -2955   1311    165       C  
ATOM   2667  CG  GLU A 402     -10.291  12.640  -9.045  1.00 64.61           C  
ANISOU 2667  CG  GLU A 402    10138   7826   6583  -3136   1375    273       C  
ATOM   2668  CD  GLU A 402     -11.390  13.479  -8.425  1.00 66.71           C  
ANISOU 2668  CD  GLU A 402    10616   7943   6787  -3136   1303    487       C  
ATOM   2669  OE1 GLU A 402     -12.126  12.990  -7.535  1.00 64.46           O  
ANISOU 2669  OE1 GLU A 402    10426   7475   6591  -2967   1199    544       O  
ATOM   2670  OE2 GLU A 402     -11.525  14.646  -8.845  1.00 70.37           O1-
ANISOU 2670  OE2 GLU A 402    11149   8479   7107  -3305   1350    602       O1-
ATOM   2671  N   ALA A 403     -10.454   7.983  -8.712  1.00 58.68           N  
ANISOU 2671  N   ALA A 403     9215   6814   6266  -2756   1250   -121       N  
ATOM   2672  CA  ALA A 403     -10.252   6.663  -8.105  1.00 55.12           C  
ANISOU 2672  CA  ALA A 403     8698   6349   5897  -2580   1199   -225       C  
ATOM   2673  C   ALA A 403      -9.312   5.842  -8.944  1.00 53.48           C  
ANISOU 2673  C   ALA A 403     8318   6278   5724  -2638   1233   -375       C  
ATOM   2674  O   ALA A 403      -8.504   5.113  -8.408  1.00 53.37           O  
ANISOU 2674  O   ALA A 403     8188   6358   5733  -2509   1203   -443       O  
ATOM   2675  CB  ALA A 403     -11.566   5.922  -7.911  1.00 55.45           C  
ANISOU 2675  CB  ALA A 403     8896   6160   6012  -2518   1151   -225       C  
ATOM   2676  N   ILE A 404      -9.405   5.965 -10.259  1.00 55.26           N  
ANISOU 2676  N   ILE A 404     8521   6521   5954  -2836   1290   -416       N  
ATOM   2677  CA  ILE A 404      -8.474   5.275 -11.135  1.00 56.82           C  
ANISOU 2677  CA  ILE A 404     8535   6864   6190  -2892   1314   -551       C  
ATOM   2678  C   ILE A 404      -7.060   5.816 -10.911  1.00 58.32           C  
ANISOU 2678  C   ILE A 404     8564   7252   6340  -2837   1341   -575       C  
ATOM   2679  O   ILE A 404      -6.090   5.050 -10.862  1.00 56.71           O  
ANISOU 2679  O   ILE A 404     8216   7148   6182  -2752   1312   -667       O  
ATOM   2680  CB  ILE A 404      -8.842   5.449 -12.626  1.00 58.74           C  
ANISOU 2680  CB  ILE A 404     8761   7113   6445  -3131   1375   -583       C  
ATOM   2681  CG1 ILE A 404     -10.225   4.863 -12.972  1.00 61.31           C  
ANISOU 2681  CG1 ILE A 404     9253   7219   6823  -3214   1338   -577       C  
ATOM   2682  CG2 ILE A 404      -7.740   4.875 -13.508  1.00 57.75           C  
ANISOU 2682  CG2 ILE A 404     8410   7170   6361  -3171   1396   -716       C  
ATOM   2683  CD1 ILE A 404     -10.405   3.381 -12.731  1.00 61.20           C  
ANISOU 2683  CD1 ILE A 404     9240   7138   6876  -3101   1263   -689       C  
ATOM   2684  N   LYS A 405      -6.957   7.141 -10.788  1.00 61.74           N  
ANISOU 2684  N   LYS A 405     9033   7738   6686  -2890   1389   -492       N  
ATOM   2685  CA  LYS A 405      -5.668   7.809 -10.531  1.00 61.97           C  
ANISOU 2685  CA  LYS A 405     8937   7941   6667  -2842   1414   -525       C  
ATOM   2686  C   LYS A 405      -4.997   7.355  -9.223  1.00 60.66           C  
ANISOU 2686  C   LYS A 405     8737   7786   6525  -2638   1330   -527       C  
ATOM   2687  O   LYS A 405      -3.768   7.230  -9.164  1.00 60.52           O  
ANISOU 2687  O   LYS A 405     8580   7886   6529  -2580   1321   -607       O  
ATOM   2688  CB  LYS A 405      -5.847   9.337 -10.528  1.00 62.93           C  
ANISOU 2688  CB  LYS A 405     9138   8112   6660  -2940   1475   -428       C  
ATOM   2689  CG  LYS A 405      -4.610  10.139 -10.159  1.00 61.62           C  
ANISOU 2689  CG  LYS A 405     8877   8112   6425  -2888   1496   -472       C  
ATOM   2690  CD  LYS A 405      -4.893  11.610 -10.321  1.00 64.36           C  
ANISOU 2690  CD  LYS A 405     9310   8525   6620  -3015   1566   -383       C  
ATOM   2691  CE  LYS A 405      -3.985  12.478  -9.481  1.00 65.60           C  
ANISOU 2691  CE  LYS A 405     9447   8795   6681  -2934   1547   -391       C  
ATOM   2692  NZ  LYS A 405      -4.270  13.912  -9.765  1.00 68.00           N1+
ANISOU 2692  NZ  LYS A 405     9838   9191   6808  -3079   1623   -312       N1+
ATOM   2693  N   ALA A 406      -5.801   7.134  -8.187  1.00 59.01           N  
ANISOU 2693  N   ALA A 406     8650   7453   6317  -2534   1266   -436       N  
ATOM   2694  CA  ALA A 406      -5.292   6.656  -6.919  1.00 56.81           C  
ANISOU 2694  CA  ALA A 406     8332   7195   6060  -2357   1191   -424       C  
ATOM   2695  C   ALA A 406      -4.826   5.186  -7.041  1.00 56.98           C  
ANISOU 2695  C   ALA A 406     8247   7235   6166  -2291   1157   -524       C  
ATOM   2696  O   ALA A 406      -3.906   4.734  -6.367  1.00 57.56           O  
ANISOU 2696  O   ALA A 406     8226   7382   6263  -2190   1110   -544       O  
ATOM   2697  CB  ALA A 406      -6.363   6.799  -5.866  1.00 56.30           C  
ANISOU 2697  CB  ALA A 406     8406   7006   5978  -2261   1141   -307       C  
ATOM   2698  N   ALA A 407      -5.448   4.434  -7.921  1.00 58.18           N  
ANISOU 2698  N   ALA A 407     8421   7325   6361  -2361   1174   -582       N  
ATOM   2699  CA  ALA A 407      -5.011   3.080  -8.147  1.00 58.10           C  
ANISOU 2699  CA  ALA A 407     8316   7351   6410  -2318   1137   -674       C  
ATOM   2700  C   ALA A 407      -3.847   3.010  -9.113  1.00 57.37           C  
ANISOU 2700  C   ALA A 407     8060   7387   6352  -2387   1152   -762       C  
ATOM   2701  O   ALA A 407      -3.192   2.011  -9.160  1.00 60.19           O  
ANISOU 2701  O   ALA A 407     8319   7796   6753  -2334   1103   -818       O  
ATOM   2702  CB  ALA A 407      -6.166   2.240  -8.653  1.00 59.83           C  
ANISOU 2702  CB  ALA A 407     8628   7450   6654  -2363   1132   -713       C  
ATOM   2703  N   THR A 408      -3.579   4.040  -9.898  1.00 57.55           N  
ANISOU 2703  N   THR A 408     8047   7467   6352  -2499   1220   -776       N  
ATOM   2704  CA  THR A 408      -2.553   3.927 -10.950  1.00 56.67           C  
ANISOU 2704  CA  THR A 408     7763   7480   6290  -2553   1242   -879       C  
ATOM   2705  C   THR A 408      -1.415   4.932 -10.812  1.00 53.99           C  
ANISOU 2705  C   THR A 408     7339   7246   5928  -2524   1273   -901       C  
ATOM   2706  O   THR A 408      -0.306   4.566 -10.438  1.00 52.09           O  
ANISOU 2706  O   THR A 408     7000   7054   5736  -2421   1217   -941       O  
ATOM   2707  CB  THR A 408      -3.168   4.084 -12.354  1.00 57.42           C  
ANISOU 2707  CB  THR A 408     7839   7584   6392  -2733   1311   -922       C  
ATOM   2708  CG2 THR A 408      -3.626   2.733 -12.877  1.00 58.24           C  
ANISOU 2708  CG2 THR A 408     7927   7642   6556  -2760   1255   -976       C  
ATOM   2709  OG1 THR A 408      -4.270   4.997 -12.285  1.00 57.88           O  
ANISOU 2709  OG1 THR A 408     8058   7557   6379  -2829   1366   -830       O  
ATOM   2710  N   ALA A 409      -1.701   6.192 -11.146  1.00 50.65           N  
ANISOU 2710  N   ALA A 409     6962   6857   5426  -2625   1361   -877       N  
ATOM   2711  CA  ALA A 409      -0.686   7.227 -11.269  1.00 47.97           C  
ANISOU 2711  CA  ALA A 409     6542   6637   5047  -2624   1413   -932       C  
ATOM   2712  C   ALA A 409      -0.073   7.564  -9.955  1.00 44.42           C  
ANISOU 2712  C   ALA A 409     6133   6176   4569  -2497   1348   -893       C  
ATOM   2713  O   ALA A 409       1.115   7.782  -9.891  1.00 43.05           O  
ANISOU 2713  O   ALA A 409     5862   6072   4422  -2436   1335   -974       O  
ATOM   2714  CB  ALA A 409      -1.281   8.475 -11.888  1.00 49.79           C  
ANISOU 2714  CB  ALA A 409     6831   6919   5168  -2779   1527   -900       C  
ATOM   2715  N   ASN A 410      -0.879   7.616  -8.910  1.00 43.80           N  
ANISOU 2715  N   ASN A 410     6193   6004   4443  -2457   1301   -772       N  
ATOM   2716  CA  ASN A 410      -0.370   7.921  -7.575  1.00 45.42           C  
ANISOU 2716  CA  ASN A 410     6430   6206   4621  -2347   1228   -722       C  
ATOM   2717  C   ASN A 410       0.313   6.754  -6.891  1.00 44.73           C  
ANISOU 2717  C   ASN A 410     6269   6097   4630  -2224   1132   -735       C  
ATOM   2718  O   ASN A 410       1.224   6.979  -6.097  1.00 45.15           O  
ANISOU 2718  O   ASN A 410     6289   6178   4689  -2157   1075   -737       O  
ATOM   2719  CB  ASN A 410      -1.492   8.345  -6.638  1.00 46.62           C  
ANISOU 2719  CB  ASN A 410     6736   6278   4700  -2331   1201   -579       C  
ATOM   2720  CG  ASN A 410      -2.036   9.714  -6.945  1.00 47.61           C  
ANISOU 2720  CG  ASN A 410     6958   6430   4700  -2444   1269   -523       C  
ATOM   2721  ND2 ASN A 410      -3.176  10.026  -6.333  1.00 48.69           N  
ANISOU 2721  ND2 ASN A 410     7238   6475   4787  -2438   1240   -387       N  
ATOM   2722  OD1 ASN A 410      -1.457  10.482  -7.732  1.00 47.94           O  
ANISOU 2722  OD1 ASN A 410     6947   6579   4689  -2532   1346   -599       O  
ATOM   2723  N   ALA A 411      -0.119   5.527  -7.193  1.00 43.76           N  
ANISOU 2723  N   ALA A 411     6128   5928   4572  -2208   1110   -742       N  
ATOM   2724  CA  ALA A 411       0.283   4.337  -6.422  1.00 42.55           C  
ANISOU 2724  CA  ALA A 411     5929   5757   4478  -2102   1021   -722       C  
ATOM   2725  C   ALA A 411       1.799   4.072  -6.286  1.00 41.03           C  
ANISOU 2725  C   ALA A 411     5616   5618   4355  -2047    959   -774       C  
ATOM   2726  O   ALA A 411       2.249   3.621  -5.235  1.00 42.04           O  
ANISOU 2726  O   ALA A 411     5734   5740   4501  -1971    882   -716       O  
ATOM   2727  CB  ALA A 411      -0.421   3.094  -6.965  1.00 43.15           C  
ANISOU 2727  CB  ALA A 411     6008   5795   4591  -2113   1015   -742       C  
ATOM   2728  N   PRO A 412       2.593   4.350  -7.326  1.00 40.04           N  
ANISOU 2728  N   PRO A 412     5396   5541   4275  -2084    988   -879       N  
ATOM   2729  CA  PRO A 412       4.044   4.242  -7.153  1.00 40.58           C  
ANISOU 2729  CA  PRO A 412     5369   5629   4422  -2019    920   -930       C  
ATOM   2730  C   PRO A 412       4.661   5.195  -6.126  1.00 42.26           C  
ANISOU 2730  C   PRO A 412     5623   5837   4597  -1986    889   -909       C  
ATOM   2731  O   PRO A 412       5.812   4.982  -5.748  1.00 44.25           O  
ANISOU 2731  O   PRO A 412     5820   6072   4922  -1931    809   -932       O  
ATOM   2732  CB  PRO A 412       4.612   4.570  -8.539  1.00 40.54           C  
ANISOU 2732  CB  PRO A 412     5255   5682   4467  -2056    978  -1064       C  
ATOM   2733  CG  PRO A 412       3.484   4.391  -9.470  1.00 41.27           C  
ANISOU 2733  CG  PRO A 412     5362   5792   4527  -2151   1055  -1068       C  
ATOM   2734  CD  PRO A 412       2.212   4.631  -8.711  1.00 40.44           C  
ANISOU 2734  CD  PRO A 412     5412   5629   4325  -2183   1077   -956       C  
ATOM   2735  N   LEU A 413       3.955   6.251  -5.706  1.00 43.34           N  
ANISOU 2735  N   LEU A 413     5858   5984   4624  -2029    940   -864       N  
ATOM   2736  CA  LEU A 413       4.455   7.106  -4.614  1.00 43.37           C  
ANISOU 2736  CA  LEU A 413     5907   5993   4580  -2007    891   -833       C  
ATOM   2737  C   LEU A 413       4.583   6.302  -3.350  1.00 41.12           C  
ANISOU 2737  C   LEU A 413     5622   5669   4333  -1941    786   -727       C  
ATOM   2738  O   LEU A 413       5.396   6.633  -2.490  1.00 40.91           O  
ANISOU 2738  O   LEU A 413     5588   5639   4316  -1921    712   -714       O  
ATOM   2739  CB  LEU A 413       3.528   8.282  -4.337  1.00 44.78           C  
ANISOU 2739  CB  LEU A 413     6197   6197   4621  -2064    947   -775       C  
ATOM   2740  CG  LEU A 413       3.499   9.349  -5.423  1.00 45.87           C  
ANISOU 2740  CG  LEU A 413     6342   6402   4683  -2151   1058   -867       C  
ATOM   2741  CD1 LEU A 413       2.300  10.256  -5.236  1.00 46.03           C  
ANISOU 2741  CD1 LEU A 413     6490   6433   4565  -2223   1107   -764       C  
ATOM   2742  CD2 LEU A 413       4.791  10.144  -5.408  1.00 46.82           C  
ANISOU 2742  CD2 LEU A 413     6420   6574   4796  -2139   1049   -990       C  
ATOM   2743  N   SER A 414       3.793   5.239  -3.257  1.00 39.73           N  
ANISOU 2743  N   SER A 414     5450   5473   4172  -1917    783   -658       N  
ATOM   2744  CA  SER A 414       3.844   4.308  -2.123  1.00 40.52           C  
ANISOU 2744  CA  SER A 414     5531   5566   4299  -1857    703   -558       C  
ATOM   2745  C   SER A 414       5.171   3.588  -1.890  1.00 41.56           C  
ANISOU 2745  C   SER A 414     5576   5689   4523  -1832    611   -567       C  
ATOM   2746  O   SER A 414       5.325   2.907  -0.881  1.00 40.73           O  
ANISOU 2746  O   SER A 414     5449   5596   4429  -1802    546   -471       O  
ATOM   2747  CB  SER A 414       2.788   3.215  -2.297  1.00 39.41           C  
ANISOU 2747  CB  SER A 414     5407   5415   4151  -1835    732   -521       C  
ATOM   2748  OG  SER A 414       3.219   2.285  -3.265  1.00 38.11           O  
ANISOU 2748  OG  SER A 414     5178   5253   4050  -1845    726   -588       O  
ATOM   2749  N   VAL A 415       6.103   3.654  -2.827  1.00 44.75           N  
ANISOU 2749  N   VAL A 415     5926   6078   4999  -1841    605   -672       N  
ATOM   2750  CA  VAL A 415       7.427   3.073  -2.578  1.00 47.83           C  
ANISOU 2750  CA  VAL A 415     6250   6431   5492  -1812    499   -670       C  
ATOM   2751  C   VAL A 415       8.538   4.094  -2.838  1.00 50.42           C  
ANISOU 2751  C   VAL A 415     6566   6723   5868  -1812    479   -783       C  
ATOM   2752  O   VAL A 415       9.725   3.751  -2.835  1.00 56.74           O  
ANISOU 2752  O   VAL A 415     7321   7462   6776  -1782    388   -809       O  
ATOM   2753  CB  VAL A 415       7.643   1.764  -3.362  1.00 47.52           C  
ANISOU 2753  CB  VAL A 415     6142   6390   5525  -1791    468   -675       C  
ATOM   2754  CG1 VAL A 415       6.690   0.691  -2.864  1.00 48.49           C  
ANISOU 2754  CG1 VAL A 415     6284   6553   5587  -1787    473   -570       C  
ATOM   2755  CG2 VAL A 415       7.427   1.963  -4.845  1.00 49.72           C  
ANISOU 2755  CG2 VAL A 415     6381   6686   5823  -1805    544   -799       C  
ATOM   2756  N   GLY A 416       8.145   5.355  -3.028  1.00 48.64           N  
ANISOU 2756  N   GLY A 416     6393   6531   5556  -1845    560   -849       N  
ATOM   2757  CA  GLY A 416       9.087   6.442  -3.254  1.00 46.96           C  
ANISOU 2757  CA  GLY A 416     6182   6306   5356  -1845    560   -980       C  
ATOM   2758  C   GLY A 416      10.139   6.164  -4.310  1.00 45.54           C  
ANISOU 2758  C   GLY A 416     5911   6088   5303  -1795    548  -1115       C  
ATOM   2759  O   GLY A 416       9.807   5.847  -5.445  1.00 44.78           O  
ANISOU 2759  O   GLY A 416     5754   6032   5227  -1791    620  -1170       O  
ATOM   2760  N   PRO A 417      11.418   6.276  -3.935  1.00 45.30           N  
ANISOU 2760  N   PRO A 417     5871   5973   5368  -1755    448  -1169       N  
ATOM   2761  CA  PRO A 417      12.488   6.137  -4.907  1.00 46.83           C  
ANISOU 2761  CA  PRO A 417     5980   6114   5698  -1681    428  -1311       C  
ATOM   2762  C   PRO A 417      12.675   4.752  -5.483  1.00 46.54           C  
ANISOU 2762  C   PRO A 417     5856   6046   5782  -1635    367  -1255       C  
ATOM   2763  O   PRO A 417      13.377   4.612  -6.487  1.00 47.50           O  
ANISOU 2763  O   PRO A 417     5885   6145   6016  -1565    361  -1372       O  
ATOM   2764  CB  PRO A 417      13.755   6.525  -4.125  1.00 48.84           C  
ANISOU 2764  CB  PRO A 417     6276   6249   6032  -1655    307  -1358       C  
ATOM   2765  CG  PRO A 417      13.327   7.167  -2.864  1.00 47.73           C  
ANISOU 2765  CG  PRO A 417     6235   6130   5769  -1732    288  -1271       C  
ATOM   2766  CD  PRO A 417      11.884   6.827  -2.649  1.00 46.39           C  
ANISOU 2766  CD  PRO A 417     6082   6064   5481  -1782    361  -1126       C  
ATOM   2767  N   GLN A 418      12.080   3.737  -4.864  1.00 46.28           N  
ANISOU 2767  N   GLN A 418     5843   6020   5721  -1666    319  -1084       N  
ATOM   2768  CA  GLN A 418      12.153   2.367  -5.397  1.00 47.52           C  
ANISOU 2768  CA  GLN A 418     5927   6170   5957  -1636    259  -1019       C  
ATOM   2769  C   GLN A 418      11.254   2.130  -6.607  1.00 49.72           C  
ANISOU 2769  C   GLN A 418     6146   6546   6199  -1651    364  -1074       C  
ATOM   2770  O   GLN A 418      11.296   1.053  -7.208  1.00 49.99           O  
ANISOU 2770  O   GLN A 418     6111   6592   6291  -1631    314  -1043       O  
ATOM   2771  CB  GLN A 418      11.774   1.364  -4.323  1.00 47.55           C  
ANISOU 2771  CB  GLN A 418     5973   6177   5918  -1671    189   -830       C  
ATOM   2772  CG  GLN A 418      12.838   1.183  -3.257  1.00 47.99           C  
ANISOU 2772  CG  GLN A 418     6056   6132   6047  -1671     51   -746       C  
ATOM   2773  CD  GLN A 418      14.154   0.717  -3.843  1.00 48.70           C  
ANISOU 2773  CD  GLN A 418     6090   6109   6306  -1606    -67   -786       C  
ATOM   2774  NE2 GLN A 418      15.245   1.163  -3.256  1.00 49.22           N  
ANISOU 2774  NE2 GLN A 418     6191   6047   6462  -1596   -165   -803       N  
ATOM   2775  OE1 GLN A 418      14.179  -0.015  -4.836  1.00 47.82           O  
ANISOU 2775  OE1 GLN A 418     5904   6018   6247  -1563    -79   -806       O  
ATOM   2776  N   ALA A 419      10.447   3.141  -6.956  1.00 52.39           N  
ANISOU 2776  N   ALA A 419     6514   6957   6434  -1700    500  -1147       N  
ATOM   2777  CA  ALA A 419       9.494   3.094  -8.082  1.00 54.73           C  
ANISOU 2777  CA  ALA A 419     6767   7342   6685  -1748    611  -1195       C  
ATOM   2778  C   ALA A 419      10.123   3.526  -9.383  1.00 55.89           C  
ANISOU 2778  C   ALA A 419     6790   7531   6913  -1715    661  -1359       C  
ATOM   2779  O   ALA A 419      10.820   4.530  -9.412  1.00 60.01           O  
ANISOU 2779  O   ALA A 419     7305   8048   7449  -1683    693  -1470       O  
ATOM   2780  CB  ALA A 419       8.309   4.034  -7.817  1.00 57.08           C  
ANISOU 2780  CB  ALA A 419     7165   7692   6831  -1830    730  -1174       C  
ATOM   2781  N   PRO A 420       9.836   2.813 -10.482  1.00 56.33           N  
ANISOU 2781  N   PRO A 420     6742   7645   7017  -1727    674  -1385       N  
ATOM   2782  CA  PRO A 420      10.281   3.406 -11.733  1.00 56.44           C  
ANISOU 2782  CA  PRO A 420     6619   7733   7092  -1706    752  -1548       C  
ATOM   2783  C   PRO A 420       9.250   4.421 -12.224  1.00 55.16           C  
ANISOU 2783  C   PRO A 420     6485   7678   6795  -1822    924  -1593       C  
ATOM   2784  O   PRO A 420       8.353   4.816 -11.470  1.00 52.82           O  
ANISOU 2784  O   PRO A 420     6332   7368   6369  -1896    966  -1502       O  
ATOM   2785  CB  PRO A 420      10.356   2.200 -12.659  1.00 57.70           C  
ANISOU 2785  CB  PRO A 420     6647   7922   7352  -1686    680  -1540       C  
ATOM   2786  CG  PRO A 420       9.223   1.343 -12.197  1.00 56.39           C  
ANISOU 2786  CG  PRO A 420     6582   7752   7093  -1770    658  -1398       C  
ATOM   2787  CD  PRO A 420       9.111   1.544 -10.704  1.00 55.20           C  
ANISOU 2787  CD  PRO A 420     6589   7520   6865  -1765    628  -1291       C  
ATOM   2788  N   LEU A 421       9.381   4.840 -13.478  1.00 55.20           N  
ANISOU 2788  N   LEU A 421     6350   7791   6833  -1838   1019  -1724       N  
ATOM   2789  CA  LEU A 421       8.332   5.597 -14.123  1.00 55.19           C  
ANISOU 2789  CA  LEU A 421     6358   7904   6709  -1978   1179  -1742       C  
ATOM   2790  C   LEU A 421       7.278   4.630 -14.603  1.00 52.24           C  
ANISOU 2790  C   LEU A 421     5979   7539   6329  -2075   1163  -1654       C  
ATOM   2791  O   LEU A 421       7.535   3.826 -15.497  1.00 52.86           O  
ANISOU 2791  O   LEU A 421     5909   7661   6515  -2057   1117  -1696       O  
ATOM   2792  CB  LEU A 421       8.886   6.376 -15.303  1.00 60.04           C  
ANISOU 2792  CB  LEU A 421     6801   8655   7357  -1971   1296  -1917       C  
ATOM   2793  CG  LEU A 421       9.705   7.624 -14.946  1.00 61.73           C  
ANISOU 2793  CG  LEU A 421     7040   8889   7524  -1907   1360  -2038       C  
ATOM   2794  CD1 LEU A 421      10.076   8.315 -16.246  1.00 65.67           C  
ANISOU 2794  CD1 LEU A 421     7349   9561   8041  -1908   1504  -2218       C  
ATOM   2795  CD2 LEU A 421       8.928   8.571 -14.032  1.00 60.63           C  
ANISOU 2795  CD2 LEU A 421     7100   8742   7191  -2007   1423  -1952       C  
ATOM   2796  N   THR A 422       6.114   4.677 -13.971  1.00 49.80           N  
ANISOU 2796  N   THR A 422     5836   7183   5901  -2167   1187  -1535       N  
ATOM   2797  CA  THR A 422       5.094   3.644 -14.175  1.00 49.01           C  
ANISOU 2797  CA  THR A 422     5773   7053   5795  -2242   1148  -1453       C  
ATOM   2798  C   THR A 422       3.768   4.091 -13.598  1.00 48.77           C  
ANISOU 2798  C   THR A 422     5928   6969   5631  -2341   1210  -1351       C  
ATOM   2799  O   THR A 422       3.670   5.192 -13.046  1.00 50.37           O  
ANISOU 2799  O   THR A 422     6222   7171   5744  -2354   1274  -1331       O  
ATOM   2800  CB  THR A 422       5.512   2.321 -13.514  1.00 47.11           C  
ANISOU 2800  CB  THR A 422     5542   6732   5624  -2140    990  -1387       C  
ATOM   2801  CG2 THR A 422       5.403   2.416 -11.993  1.00 46.66           C  
ANISOU 2801  CG2 THR A 422     5647   6582   5501  -2087    947  -1280       C  
ATOM   2802  OG1 THR A 422       4.704   1.245 -13.994  1.00 45.24           O  
ANISOU 2802  OG1 THR A 422     5303   6498   5387  -2208    953  -1353       O  
ATOM   2803  N   GLY A 423       2.754   3.249 -13.745  1.00 49.15           N  
ANISOU 2803  N   GLY A 423     6035   6972   5667  -2408   1183  -1293       N  
ATOM   2804  CA  GLY A 423       1.415   3.548 -13.252  1.00 49.99           C  
ANISOU 2804  CA  GLY A 423     6324   7000   5671  -2489   1227  -1200       C  
ATOM   2805  C   GLY A 423       0.695   4.590 -14.083  1.00 51.06           C  
ANISOU 2805  C   GLY A 423     6477   7183   5739  -2647   1356  -1210       C  
ATOM   2806  O   GLY A 423      -0.302   5.157 -13.644  1.00 49.04           O  
ANISOU 2806  O   GLY A 423     6383   6856   5394  -2711   1397  -1122       O  
ATOM   2807  N   GLN A 424       1.221   4.859 -15.274  1.00 53.39           N  
ANISOU 2807  N   GLN A 424     6603   7604   6080  -2708   1419  -1312       N  
ATOM   2808  CA  GLN A 424       0.613   5.814 -16.194  1.00 56.68           C  
ANISOU 2808  CA  GLN A 424     7006   8103   6430  -2882   1555  -1322       C  
ATOM   2809  C   GLN A 424       0.886   5.405 -17.632  1.00 60.02           C  
ANISOU 2809  C   GLN A 424     7214   8651   6939  -2964   1585  -1424       C  
ATOM   2810  O   GLN A 424       1.956   4.849 -17.935  1.00 61.94           O  
ANISOU 2810  O   GLN A 424     7286   8958   7291  -2849   1526  -1516       O  
ATOM   2811  CB  GLN A 424       1.193   7.203 -16.032  1.00 58.23           C  
ANISOU 2811  CB  GLN A 424     7191   8393   6540  -2873   1656  -1354       C  
ATOM   2812  CG  GLN A 424       0.990   7.868 -14.693  1.00 58.01           C  
ANISOU 2812  CG  GLN A 424     7354   8277   6409  -2812   1634  -1257       C  
ATOM   2813  CD  GLN A 424       1.332   9.346 -14.761  1.00 59.04           C  
ANISOU 2813  CD  GLN A 424     7489   8525   6418  -2859   1750  -1290       C  
ATOM   2814  NE2 GLN A 424       2.032   9.823 -13.751  1.00 58.11           N  
ANISOU 2814  NE2 GLN A 424     7425   8392   6263  -2740   1706  -1297       N  
ATOM   2815  OE1 GLN A 424       0.983  10.046 -15.722  1.00 60.12           O  
ANISOU 2815  OE1 GLN A 424     7577   8778   6487  -3010   1877  -1311       O  
ATOM   2816  N   LEU A 425      -0.070   5.696 -18.511  1.00 61.56           N  
ANISOU 2816  N   LEU A 425     7415   8879   7095  -3165   1669  -1402       N  
ATOM   2817  CA  LEU A 425       0.082   5.409 -19.924  1.00 64.50           C  
ANISOU 2817  CA  LEU A 425     7571   9394   7544  -3275   1708  -1491       C  
ATOM   2818  C   LEU A 425       0.675   6.648 -20.552  1.00 67.83           C  
ANISOU 2818  C   LEU A 425     7850  10003   7917  -3318   1863  -1565       C  
ATOM   2819  O   LEU A 425      -0.049   7.547 -20.975  1.00 70.14           O  
ANISOU 2819  O   LEU A 425     8192  10351   8108  -3504   1989  -1516       O  
ATOM   2820  CB  LEU A 425      -1.254   5.034 -20.574  1.00 64.54           C  
ANISOU 2820  CB  LEU A 425     7649   9338   7536  -3493   1712  -1431       C  
ATOM   2821  CG  LEU A 425      -1.957   3.781 -20.020  1.00 62.97           C  
ANISOU 2821  CG  LEU A 425     7600   8956   7370  -3458   1568  -1382       C  
ATOM   2822  CD1 LEU A 425      -3.197   3.494 -20.849  1.00 64.09           C  
ANISOU 2822  CD1 LEU A 425     7796   9043   7512  -3691   1577  -1355       C  
ATOM   2823  CD2 LEU A 425      -1.043   2.563 -19.985  1.00 61.12           C  
ANISOU 2823  CD2 LEU A 425     7230   8752   7240  -3299   1435  -1455       C  
ATOM   2824  N   ARG A 426       2.004   6.685 -20.608  1.00 69.43           N  
ANISOU 2824  N   ARG A 426     7883  10302   8194  -3149   1853  -1684       N  
ATOM   2825  CA  ARG A 426       2.729   7.865 -21.089  1.00 71.84           C  
ANISOU 2825  CA  ARG A 426     8052  10792   8453  -3144   2002  -1790       C  
ATOM   2826  C   ARG A 426       4.113   7.448 -21.605  1.00 69.96           C  
ANISOU 2826  C   ARG A 426     7558  10653   8369  -2964   1961  -1950       C  
ATOM   2827  O   ARG A 426       4.665   6.454 -21.157  1.00 68.68           O  
ANISOU 2827  O   ARG A 426     7390  10383   8322  -2807   1802  -1951       O  
ATOM   2828  CB  ARG A 426       2.727   9.012 -20.037  1.00 74.84           C  
ANISOU 2828  CB  ARG A 426     8628  11130   8679  -3111   2061  -1741       C  
ATOM   2829  CG  ARG A 426       1.911  10.216 -20.541  1.00 79.85           C  
ANISOU 2829  CG  ARG A 426     9312  11881   9145  -3333   2236  -1689       C  
ATOM   2830  CD  ARG A 426       1.751  11.349 -19.533  1.00 80.46           C  
ANISOU 2830  CD  ARG A 426     9600  11923   9047  -3328   2280  -1616       C  
ATOM   2831  NE  ARG A 426       3.006  12.067 -19.322  1.00 80.99           N  
ANISOU 2831  NE  ARG A 426     9578  12105   9088  -3181   2329  -1765       N  
ATOM   2832  CZ  ARG A 426       3.621  12.235 -18.153  1.00 77.97           C  
ANISOU 2832  CZ  ARG A 426     9311  11625   8690  -3017   2242  -1774       C  
ATOM   2833  NH1 ARG A 426       3.118  11.759 -17.023  1.00 76.69           N1+
ANISOU 2833  NH1 ARG A 426     9345  11265   8530  -2970   2107  -1635       N1+
ATOM   2834  NH2 ARG A 426       4.755  12.913 -18.114  1.00 78.89           N  
ANISOU 2834  NH2 ARG A 426     9342  11846   8788  -2901   2294  -1933       N  
ATOM   2835  N   GLU A 427       4.628   8.171 -22.598  1.00 71.01           N  
ANISOU 2835  N   GLU A 427     7473  11000   8506  -2993   2102  -2079       N  
ATOM   2836  CA  GLU A 427       5.895   7.818 -23.253  1.00 71.01           C  
ANISOU 2836  CA  GLU A 427     7201  11107   8672  -2817   2071  -2244       C  
ATOM   2837  C   GLU A 427       7.047   7.728 -22.245  1.00 67.87           C  
ANISOU 2837  C   GLU A 427     6869  10578   8339  -2560   1961  -2298       C  
ATOM   2838  O   GLU A 427       7.212   8.606 -21.411  1.00 65.60           O  
ANISOU 2838  O   GLU A 427     6738  10248   7939  -2523   2012  -2300       O  
ATOM   2839  CB  GLU A 427       6.230   8.824 -24.360  1.00 74.90           C  
ANISOU 2839  CB  GLU A 427     7461  11867   9132  -2880   2274  -2387       C  
ATOM   2840  CG  GLU A 427       7.485   8.466 -25.159  1.00 78.80           C  
ANISOU 2840  CG  GLU A 427     7643  12481   9815  -2688   2247  -2567       C  
ATOM   2841  CD  GLU A 427       7.667   9.284 -26.437  1.00 83.93           C  
ANISOU 2841  CD  GLU A 427     8010  13432  10446  -2770   2456  -2711       C  
ATOM   2842  OE1 GLU A 427       6.696   9.930 -26.903  1.00 89.46           O  
ANISOU 2842  OE1 GLU A 427     8732  14262  10996  -3025   2611  -2644       O  
ATOM   2843  OE2 GLU A 427       8.789   9.274 -26.990  1.00 84.48           O1-
ANISOU 2843  OE2 GLU A 427     7829  13613  10656  -2577   2465  -2888       O1-
ATOM   2844  N   GLY A 428       7.808   6.641 -22.321  1.00 66.89           N  
ANISOU 2844  N   GLY A 428     6634  10387   8395  -2399   1797  -2328       N  
ATOM   2845  CA  GLY A 428       8.917   6.383 -21.409  1.00 66.45           C  
ANISOU 2845  CA  GLY A 428     6637  10183   8428  -2169   1666  -2359       C  
ATOM   2846  C   GLY A 428       8.581   5.535 -20.185  1.00 64.99           C  
ANISOU 2846  C   GLY A 428     6685   9781   8227  -2145   1501  -2194       C  
ATOM   2847  O   GLY A 428       9.463   4.896 -19.607  1.00 64.05           O  
ANISOU 2847  O   GLY A 428     6579   9540   8219  -1976   1349  -2189       O  
ATOM   2848  N   TYR A 429       7.308   5.529 -19.781  1.00 64.08           N  
ANISOU 2848  N   TYR A 429     6752   9618   7976  -2311   1530  -2059       N  
ATOM   2849  CA  TYR A 429       6.863   4.780 -18.600  1.00 60.37           C  
ANISOU 2849  CA  TYR A 429     6497   8967   7473  -2292   1398  -1910       C  
ATOM   2850  C   TYR A 429       6.803   3.316 -18.917  1.00 59.31           C  
ANISOU 2850  C   TYR A 429     6294   8795   7443  -2274   1250  -1863       C  
ATOM   2851  O   TYR A 429       6.766   2.904 -20.077  1.00 59.64           O  
ANISOU 2851  O   TYR A 429     6151   8949   7560  -2326   1253  -1918       O  
ATOM   2852  CB  TYR A 429       5.497   5.255 -18.114  1.00 59.70           C  
ANISOU 2852  CB  TYR A 429     6621   8839   7224  -2456   1476  -1792       C  
ATOM   2853  CG  TYR A 429       5.572   6.554 -17.368  1.00 61.08           C  
ANISOU 2853  CG  TYR A 429     6924   9010   7274  -2451   1568  -1792       C  
ATOM   2854  CD1 TYR A 429       6.351   7.608 -17.838  1.00 64.16           C  
ANISOU 2854  CD1 TYR A 429     7200   9529   7647  -2419   1681  -1931       C  
ATOM   2855  CD2 TYR A 429       4.853   6.746 -16.201  1.00 60.58           C  
ANISOU 2855  CD2 TYR A 429     7089   8827   7100  -2476   1540  -1661       C  
ATOM   2856  CE1 TYR A 429       6.416   8.795 -17.159  1.00 65.86           C  
ANISOU 2856  CE1 TYR A 429     7541   9755   7727  -2424   1759  -1937       C  
ATOM   2857  CE2 TYR A 429       4.908   7.939 -15.512  1.00 62.27           C  
ANISOU 2857  CE2 TYR A 429     7420   9050   7191  -2479   1608  -1653       C  
ATOM   2858  CZ  TYR A 429       5.703   8.952 -15.991  1.00 65.85           C  
ANISOU 2858  CZ  TYR A 429     7769   9632   7617  -2458   1713  -1791       C  
ATOM   2859  OH  TYR A 429       5.791  10.148 -15.322  1.00 70.18           O  
ANISOU 2859  OH  TYR A 429     8436  10204   8025  -2468   1773  -1794       O  
ATOM   2860  N   GLU A 430       6.793   2.525 -17.866  1.00 58.58           N  
ANISOU 2860  N   GLU A 430     6349   8562   7348  -2206   1119  -1756       N  
ATOM   2861  CA  GLU A 430       6.884   1.095 -18.026  1.00 58.01           C  
ANISOU 2861  CA  GLU A 430     6227   8459   7356  -2171    963  -1708       C  
ATOM   2862  C   GLU A 430       5.603   0.538 -18.622  1.00 54.29           C  
ANISOU 2862  C   GLU A 430     5782   8022   6825  -2344    981  -1669       C  
ATOM   2863  O   GLU A 430       4.517   0.943 -18.238  1.00 52.52           O  
ANISOU 2863  O   GLU A 430     5722   7750   6484  -2458   1060  -1611       O  
ATOM   2864  CB  GLU A 430       7.213   0.443 -16.685  1.00 59.04           C  
ANISOU 2864  CB  GLU A 430     6509   8450   7475  -2066    835  -1598       C  
ATOM   2865  CG  GLU A 430       8.626   0.750 -16.229  1.00 62.00           C  
ANISOU 2865  CG  GLU A 430     6838   8773   7947  -1900    774  -1640       C  
ATOM   2866  CD  GLU A 430       9.407  -0.503 -15.912  1.00 66.32           C  
ANISOU 2866  CD  GLU A 430     7357   9249   8591  -1792    584  -1568       C  
ATOM   2867  OE1 GLU A 430       9.247  -1.021 -14.776  1.00 66.03           O  
ANISOU 2867  OE1 GLU A 430     7473   9122   8495  -1782    512  -1445       O  
ATOM   2868  OE2 GLU A 430      10.159  -0.972 -16.818  1.00 69.85           O1-
ANISOU 2868  OE2 GLU A 430     7622   9744   9173  -1719    506  -1628       O1-
ATOM   2869  N   ALA A 431       5.746  -0.386 -19.566  1.00 53.29           N  
ANISOU 2869  N   ALA A 431     5493   7969   6784  -2361    893  -1701       N  
ATOM   2870  CA  ALA A 431       4.605  -0.949 -20.279  1.00 52.80           C  
ANISOU 2870  CA  ALA A 431     5436   7945   6681  -2539    897  -1688       C  
ATOM   2871  C   ALA A 431       3.828  -1.935 -19.409  1.00 50.80           C  
ANISOU 2871  C   ALA A 431     5389   7571   6343  -2558    803  -1588       C  
ATOM   2872  O   ALA A 431       3.811  -3.133 -19.670  1.00 50.72           O  
ANISOU 2872  O   ALA A 431     5340   7576   6354  -2560    673  -1575       O  
ATOM   2873  CB  ALA A 431       5.066  -1.613 -21.576  1.00 53.83           C  
ANISOU 2873  CB  ALA A 431     5310   8213   6931  -2552    820  -1761       C  
ATOM   2874  N   ASP A 432       3.202  -1.430 -18.357  1.00 49.22           N  
ANISOU 2874  N   ASP A 432     5402   7261   6039  -2562    868  -1521       N  
ATOM   2875  CA  ASP A 432       2.265  -2.231 -17.595  1.00 48.89           C  
ANISOU 2875  CA  ASP A 432     5551   7115   5908  -2590    814  -1446       C  
ATOM   2876  C   ASP A 432       0.917  -1.658 -17.951  1.00 48.97           C  
ANISOU 2876  C   ASP A 432     5671   7087   5848  -2764    924  -1447       C  
ATOM   2877  O   ASP A 432       0.555  -0.604 -17.434  1.00 47.72           O  
ANISOU 2877  O   ASP A 432     5624   6875   5631  -2779   1028  -1409       O  
ATOM   2878  CB  ASP A 432       2.486  -2.097 -16.085  1.00 48.25           C  
ANISOU 2878  CB  ASP A 432     5625   6935   5773  -2462    800  -1361       C  
ATOM   2879  CG  ASP A 432       3.745  -2.803 -15.579  1.00 47.22           C  
ANISOU 2879  CG  ASP A 432     5423   6812   5706  -2308    672  -1330       C  
ATOM   2880  OD1 ASP A 432       4.547  -3.339 -16.375  1.00 49.43           O  
ANISOU 2880  OD1 ASP A 432     5534   7166   6081  -2275    587  -1372       O  
ATOM   2881  OD2 ASP A 432       3.938  -2.777 -14.346  1.00 44.81           O1-
ANISOU 2881  OD2 ASP A 432     5231   6437   5359  -2222    651  -1253       O1-
ATOM   2882  N   VAL A 433       0.191  -2.349 -18.829  1.00 50.93           N  
ANISOU 2882  N   VAL A 433     5893   7358   6102  -2901    890  -1484       N  
ATOM   2883  CA  VAL A 433      -1.070  -1.856 -19.418  1.00 52.65           C  
ANISOU 2883  CA  VAL A 433     6195   7532   6276  -3101    981  -1490       C  
ATOM   2884  C   VAL A 433      -2.140  -2.936 -19.436  1.00 54.37           C  
ANISOU 2884  C   VAL A 433     6546   7659   6454  -3185    901  -1496       C  
ATOM   2885  O   VAL A 433      -1.837  -4.127 -19.654  1.00 55.23           O  
ANISOU 2885  O   VAL A 433     6586   7816   6581  -3153    776  -1532       O  
ATOM   2886  CB  VAL A 433      -0.880  -1.475 -20.896  1.00 54.57           C  
ANISOU 2886  CB  VAL A 433     6219   7926   6590  -3246   1032  -1563       C  
ATOM   2887  CG1 VAL A 433      -2.103  -0.744 -21.414  1.00 55.68           C  
ANISOU 2887  CG1 VAL A 433     6457   8018   6681  -3469   1142  -1543       C  
ATOM   2888  CG2 VAL A 433       0.379  -0.648 -21.089  1.00 54.61           C  
ANISOU 2888  CG2 VAL A 433     6037   8058   6654  -3139   1094  -1602       C  
ATOM   2889  N   ILE A 434      -3.386  -2.536 -19.217  1.00 55.09           N  
ANISOU 2889  N   ILE A 434     6835   7613   6485  -3292    964  -1464       N  
ATOM   2890  CA  ILE A 434      -4.484  -3.476 -19.307  1.00 57.73           C  
ANISOU 2890  CA  ILE A 434     7309   7838   6786  -3380    896  -1495       C  
ATOM   2891  C   ILE A 434      -5.601  -2.964 -20.171  1.00 62.04           C  
ANISOU 2891  C   ILE A 434     7921   8312   7339  -3615    958  -1505       C  
ATOM   2892  O   ILE A 434      -5.792  -1.752 -20.306  1.00 64.79           O  
ANISOU 2892  O   ILE A 434     8287   8648   7681  -3691   1072  -1449       O  
ATOM   2893  CB  ILE A 434      -5.063  -3.823 -17.931  1.00 57.15           C  
ANISOU 2893  CB  ILE A 434     7463   7613   6637  -3242    878  -1450       C  
ATOM   2894  CG1 ILE A 434      -5.618  -2.586 -17.224  1.00 56.63           C  
ANISOU 2894  CG1 ILE A 434     7551   7427   6540  -3229    985  -1363       C  
ATOM   2895  CG2 ILE A 434      -3.999  -4.501 -17.073  1.00 56.02           C  
ANISOU 2895  CG2 ILE A 434     7256   7547   6481  -3039    805  -1431       C  
ATOM   2896  CD1 ILE A 434      -6.458  -2.941 -16.012  1.00 56.69           C  
ANISOU 2896  CD1 ILE A 434     7780   7271   6488  -3115    966  -1330       C  
ATOM   2897  N   ALA A 435      -6.372  -3.903 -20.713  1.00 63.90           N  
ANISOU 2897  N   ALA A 435     8211   8494   7574  -3738    877  -1572       N  
ATOM   2898  CA  ALA A 435      -7.464  -3.572 -21.601  1.00 65.95           C  
ANISOU 2898  CA  ALA A 435     8538   8667   7852  -3988    911  -1585       C  
ATOM   2899  C   ALA A 435      -8.796  -4.060 -21.057  1.00 68.47           C  
ANISOU 2899  C   ALA A 435     9143   8745   8128  -4014    871  -1600       C  
ATOM   2900  O   ALA A 435      -8.883  -5.130 -20.461  1.00 69.92           O  
ANISOU 2900  O   ALA A 435     9408   8889   8271  -3890    782  -1656       O  
ATOM   2901  CB  ALA A 435      -7.209  -4.179 -22.944  1.00 67.26           C  
ANISOU 2901  CB  ALA A 435     8493   8987   8077  -4153    843  -1670       C  
ATOM   2902  N   LEU A 436      -9.839  -3.274 -21.284  1.00 72.62           N  
ANISOU 2902  N   LEU A 436     9821   9109   8661  -4175    936  -1550       N  
ATOM   2903  CA  LEU A 436     -11.168  -3.606 -20.792  1.00 76.59           C  
ANISOU 2903  CA  LEU A 436    10610   9346   9144  -4193    898  -1565       C  
ATOM   2904  C   LEU A 436     -12.216  -3.763 -21.890  1.00 80.90           C  
ANISOU 2904  C   LEU A 436    11232   9773   9735  -4482    864  -1613       C  
ATOM   2905  O   LEU A 436     -11.974  -3.481 -23.067  1.00 80.83           O  
ANISOU 2905  O   LEU A 436    11043   9900   9770  -4697    884  -1616       O  
ATOM   2906  CB  LEU A 436     -11.628  -2.548 -19.801  1.00 77.07           C  
ANISOU 2906  CB  LEU A 436    10855   9250   9180  -4093    983  -1439       C  
ATOM   2907  CG  LEU A 436     -11.389  -2.907 -18.347  1.00 77.03           C  
ANISOU 2907  CG  LEU A 436    10935   9208   9125  -3800    964  -1429       C  
ATOM   2908  CD1 LEU A 436      -9.939  -3.281 -18.122  1.00 76.23           C  
ANISOU 2908  CD1 LEU A 436    10608   9349   9006  -3649    949  -1448       C  
ATOM   2909  CD2 LEU A 436     -11.759  -1.723 -17.470  1.00 77.98           C  
ANISOU 2909  CD2 LEU A 436    11197   9204   9225  -3718   1041  -1292       C  
ATOM   2910  N   GLU A 437     -13.384  -4.228 -21.459  1.00 82.34           N  
ANISOU 2910  N   GLU A 437    11678   9697   9909  -4480    811  -1658       N  
ATOM   2911  CA  GLU A 437     -14.523  -4.503 -22.320  1.00 85.47           C  
ANISOU 2911  CA  GLU A 437    12208   9914  10351  -4739    755  -1719       C  
ATOM   2912  C   GLU A 437     -15.610  -3.458 -22.084  1.00 84.39           C  
ANISOU 2912  C   GLU A 437    12313   9507  10246  -4826    815  -1598       C  
ATOM   2913  O   GLU A 437     -16.339  -3.095 -23.016  1.00 86.42           O  
ANISOU 2913  O   GLU A 437    12624   9656  10552  -5111    812  -1572       O  
ATOM   2914  CB  GLU A 437     -15.041  -5.919 -22.006  1.00 88.06           C  
ANISOU 2914  CB  GLU A 437    12676  10136  10648  -4658    634  -1886       C  
ATOM   2915  CG  GLU A 437     -16.084  -6.499 -22.954  1.00 93.43           C  
ANISOU 2915  CG  GLU A 437    13476  10653  11370  -4923    541  -2001       C  
ATOM   2916  CD  GLU A 437     -15.530  -6.918 -24.314  1.00 97.52           C  
ANISOU 2916  CD  GLU A 437    13736  11405  11913  -5158    480  -2061       C  
ATOM   2917  OE1 GLU A 437     -14.293  -6.893 -24.524  1.00 95.39           O  
ANISOU 2917  OE1 GLU A 437    13186  11427  11630  -5087    501  -2030       O  
ATOM   2918  OE2 GLU A 437     -16.353  -7.283 -25.189  1.00 99.99           O1-
ANISOU 2918  OE2 GLU A 437    14125  11599  12266  -5417    402  -2143       O1-
ATOM   2919  N   GLU A 438     -15.699  -2.973 -20.843  1.00 81.07           N  
ANISOU 2919  N   GLU A 438    12028   8981   9792  -4589    859  -1515       N  
ATOM   2920  CA  GLU A 438     -16.691  -1.967 -20.442  1.00 81.55           C  
ANISOU 2920  CA  GLU A 438    12326   8781   9877  -4624    902  -1379       C  
ATOM   2921  C   GLU A 438     -16.010  -0.696 -19.897  1.00 76.29           C  
ANISOU 2921  C   GLU A 438    11580   8241   9166  -4525   1011  -1207       C  
ATOM   2922  O   GLU A 438     -14.868  -0.732 -19.491  1.00 72.20           O  
ANISOU 2922  O   GLU A 438    10874   7955   8602  -4358   1043  -1216       O  
ATOM   2923  CB  GLU A 438     -17.631  -2.561 -19.388  1.00 82.58           C  
ANISOU 2923  CB  GLU A 438    12728   8633  10016  -4418    837  -1442       C  
ATOM   2924  CG  GLU A 438     -18.494  -3.711 -19.883  1.00 84.34           C  
ANISOU 2924  CG  GLU A 438    13087   8683  10275  -4523    731  -1623       C  
ATOM   2925  CD  GLU A 438     -19.704  -3.989 -19.003  1.00 85.34           C  
ANISOU 2925  CD  GLU A 438    13525   8465  10434  -4367    682  -1671       C  
ATOM   2926  OE1 GLU A 438     -19.594  -3.861 -17.762  1.00 80.68           O  
ANISOU 2926  OE1 GLU A 438    12983   7859   9813  -4074    713  -1633       O  
ATOM   2927  OE2 GLU A 438     -20.768  -4.348 -19.560  1.00 89.32           O1-
ANISOU 2927  OE2 GLU A 438    14221   8713  11001  -4535    608  -1758       O1-
ATOM   2928  N   ASN A 439     -16.717   0.429 -19.924  1.00 76.25           N  
ANISOU 2928  N   ASN A 439    11726   8078   9168  -4645   1058  -1050       N  
ATOM   2929  CA  ASN A 439     -16.154   1.698 -19.486  1.00 74.33           C  
ANISOU 2929  CA  ASN A 439    11424   7957   8862  -4587   1156   -888       C  
ATOM   2930  C   ASN A 439     -16.329   1.902 -18.001  1.00 72.84           C  
ANISOU 2930  C   ASN A 439    11386   7644   8646  -4291   1139   -825       C  
ATOM   2931  O   ASN A 439     -17.434   2.173 -17.545  1.00 74.09           O  
ANISOU 2931  O   ASN A 439    11796   7521   8836  -4272   1099   -749       O  
ATOM   2932  CB  ASN A 439     -16.808   2.892 -20.186  1.00 76.90           C  
ANISOU 2932  CB  ASN A 439    11839   8198   9182  -4865   1216   -721       C  
ATOM   2933  CG  ASN A 439     -16.294   4.222 -19.662  1.00 75.74           C  
ANISOU 2933  CG  ASN A 439    11659   8177   8943  -4801   1313   -555       C  
ATOM   2934  ND2 ASN A 439     -15.003   4.299 -19.419  1.00 72.93           N  
ANISOU 2934  ND2 ASN A 439    11074   8104   8534  -4655   1368   -603       N  
ATOM   2935  OD1 ASN A 439     -17.057   5.161 -19.455  1.00 78.78           O  
ANISOU 2935  OD1 ASN A 439    12234   8396   9303  -4880   1327   -386       O  
ATOM   2936  N   PRO A 440     -15.229   1.837 -17.245  1.00 70.37           N  
ANISOU 2936  N   PRO A 440    10915   7540   8281  -4064   1165   -846       N  
ATOM   2937  CA  PRO A 440     -15.294   1.991 -15.793  1.00 68.98           C  
ANISOU 2937  CA  PRO A 440    10844   7286   8078  -3784   1146   -789       C  
ATOM   2938  C   PRO A 440     -15.761   3.369 -15.326  1.00 70.40           C  
ANISOU 2938  C   PRO A 440    11163   7362   8223  -3796   1181   -591       C  
ATOM   2939  O   PRO A 440     -16.226   3.504 -14.192  1.00 72.24           O  
ANISOU 2939  O   PRO A 440    11537   7452   8459  -3592   1142   -530       O  
ATOM   2940  CB  PRO A 440     -13.852   1.775 -15.356  1.00 65.89           C  
ANISOU 2940  CB  PRO A 440    10217   7178   7640  -3618   1173   -838       C  
ATOM   2941  CG  PRO A 440     -13.049   2.175 -16.535  1.00 67.01           C  
ANISOU 2941  CG  PRO A 440    10152   7538   7770  -3820   1238   -849       C  
ATOM   2942  CD  PRO A 440     -13.841   1.756 -17.728  1.00 69.08           C  
ANISOU 2942  CD  PRO A 440    10461   7698   8088  -4072   1213   -905       C  
ATOM   2943  N   LEU A 441     -15.631   4.380 -16.180  1.00 69.60           N  
ANISOU 2943  N   LEU A 441    11013   7349   8082  -4030   1254   -487       N  
ATOM   2944  CA  LEU A 441     -16.040   5.723 -15.815  1.00 68.89           C  
ANISOU 2944  CA  LEU A 441    11055   7188   7932  -4069   1286   -286       C  
ATOM   2945  C   LEU A 441     -17.545   5.817 -15.643  1.00 71.46           C  
ANISOU 2945  C   LEU A 441    11677   7154   8322  -4113   1210   -191       C  
ATOM   2946  O   LEU A 441     -18.007   6.597 -14.819  1.00 70.26           O  
ANISOU 2946  O   LEU A 441    11675   6878   8141  -4011   1185    -38       O  
ATOM   2947  CB  LEU A 441     -15.550   6.716 -16.851  1.00 68.71           C  
ANISOU 2947  CB  LEU A 441    10903   7370   7834  -4329   1394   -210       C  
ATOM   2948  CG  LEU A 441     -14.026   6.708 -16.989  1.00 66.53           C  
ANISOU 2948  CG  LEU A 441    10336   7436   7504  -4258   1467   -311       C  
ATOM   2949  CD1 LEU A 441     -13.574   7.738 -18.003  1.00 67.24           C  
ANISOU 2949  CD1 LEU A 441    10290   7741   7514  -4500   1590   -252       C  
ATOM   2950  CD2 LEU A 441     -13.337   6.935 -15.646  1.00 64.78           C  
ANISOU 2950  CD2 LEU A 441    10095   7286   7233  -3972   1450   -291       C  
ATOM   2951  N   GLU A 442     -18.290   4.998 -16.396  1.00 74.94           N  
ANISOU 2951  N   GLU A 442    12201   7421   8853  -4255   1161   -290       N  
ATOM   2952  CA  GLU A 442     -19.743   4.873 -16.236  1.00 78.56           C  
ANISOU 2952  CA  GLU A 442    12955   7492   9400  -4276   1071   -243       C  
ATOM   2953  C   GLU A 442     -20.052   4.003 -15.020  1.00 80.03           C  
ANISOU 2953  C   GLU A 442    13234   7533   9639  -3937    993   -350       C  
ATOM   2954  O   GLU A 442     -20.772   4.432 -14.132  1.00 81.94           O  
ANISOU 2954  O   GLU A 442    13661   7564   9908  -3779    942   -242       O  
ATOM   2955  CB  GLU A 442     -20.425   4.249 -17.461  1.00 80.62           C  
ANISOU 2955  CB  GLU A 442    13279   7609   9743  -4553   1036   -334       C  
ATOM   2956  CG  GLU A 442     -20.087   4.826 -18.807  1.00 82.48           C  
ANISOU 2956  CG  GLU A 442    13373   8025   9941  -4907   1117   -273       C  
ATOM   2957  CD  GLU A 442     -20.804   6.110 -19.060  1.00 85.31           C  
ANISOU 2957  CD  GLU A 442    13899   8245  10270  -5117   1141    -28       C  
ATOM   2958  OE1 GLU A 442     -20.325   7.140 -18.561  1.00 85.78           O  
ANISOU 2958  OE1 GLU A 442    13917   8451  10223  -5049   1206    120       O  
ATOM   2959  OE2 GLU A 442     -21.844   6.080 -19.736  1.00 86.41           O1-
ANISOU 2959  OE2 GLU A 442    14221   8126  10485  -5355   1089     18       O1-
ATOM   2960  N   ASP A 443     -19.523   2.774 -14.990  1.00 80.31           N  
ANISOU 2960  N   ASP A 443    13133   7691   9686  -3826    982   -560       N  
ATOM   2961  CA  ASP A 443     -19.705   1.858 -13.842  1.00 78.70           C  
ANISOU 2961  CA  ASP A 443    12983   7408   9509  -3506    929   -680       C  
ATOM   2962  C   ASP A 443     -18.348   1.398 -13.302  1.00 75.38           C  
ANISOU 2962  C   ASP A 443    12306   7319   9013  -3328    972   -757       C  
ATOM   2963  O   ASP A 443     -17.596   0.706 -13.985  1.00 75.89           O  
ANISOU 2963  O   ASP A 443    12198   7580   9057  -3417    989   -879       O  
ATOM   2964  CB  ASP A 443     -20.564   0.636 -14.219  1.00 79.39           C  
ANISOU 2964  CB  ASP A 443    13207   7282   9676  -3531    858   -874       C  
ATOM   2965  CG  ASP A 443     -21.004  -0.169 -12.997  1.00 79.05           C  
ANISOU 2965  CG  ASP A 443    13260   7119   9658  -3200    814   -987       C  
ATOM   2966  OD1 ASP A 443     -20.996   0.389 -11.880  1.00 76.89           O  
ANISOU 2966  OD1 ASP A 443    13005   6836   9375  -2975    821   -876       O  
ATOM   2967  OD2 ASP A 443     -21.355  -1.361 -13.140  1.00 80.28           O1-
ANISOU 2967  OD2 ASP A 443    13463   7204   9837  -3164    772  -1192       O1-
ATOM   2968  N   ILE A 444     -18.034   1.805 -12.078  1.00 72.85           N  
ANISOU 2968  N   ILE A 444    11963   7057   8659  -3088    980   -675       N  
ATOM   2969  CA  ILE A 444     -16.743   1.500 -11.445  1.00 67.91           C  
ANISOU 2969  CA  ILE A 444    11113   6724   7966  -2925   1014   -717       C  
ATOM   2970  C   ILE A 444     -16.685   0.051 -10.930  1.00 67.16           C  
ANISOU 2970  C   ILE A 444    10983   6657   7879  -2741    982   -898       C  
ATOM   2971  O   ILE A 444     -15.618  -0.520 -10.750  1.00 64.96           O  
ANISOU 2971  O   ILE A 444    10512   6617   7550  -2672    999   -965       O  
ATOM   2972  CB  ILE A 444     -16.500   2.480 -10.282  1.00 66.10           C  
ANISOU 2972  CB  ILE A 444    10880   6538   7695  -2751   1023   -558       C  
ATOM   2973  CG1 ILE A 444     -15.050   2.438  -9.799  1.00 62.70           C  
ANISOU 2973  CG1 ILE A 444    10213   6414   7197  -2651   1060   -573       C  
ATOM   2974  CG2 ILE A 444     -17.460   2.192  -9.134  1.00 67.86           C  
ANISOU 2974  CG2 ILE A 444    11261   6551   7972  -2506    966   -555       C  
ATOM   2975  CD1 ILE A 444     -14.093   3.233 -10.644  1.00 61.65           C  
ANISOU 2975  CD1 ILE A 444     9936   6480   7010  -2841   1122   -524       C  
ATOM   2976  N   LYS A 445     -17.846  -0.543 -10.698  1.00 69.17           N  
ANISOU 2976  N   LYS A 445    11429   6660   8191  -2664    932   -981       N  
ATOM   2977  CA  LYS A 445     -17.912  -1.928 -10.240  1.00 69.77           C  
ANISOU 2977  CA  LYS A 445    11491   6762   8255  -2498    911  -1168       C  
ATOM   2978  C   LYS A 445     -17.464  -2.930 -11.315  1.00 68.95           C  
ANISOU 2978  C   LYS A 445    11290   6785   8123  -2670    898  -1325       C  
ATOM   2979  O   LYS A 445     -17.445  -4.131 -11.085  1.00 67.02           O  
ANISOU 2979  O   LYS A 445    11028   6595   7843  -2569    878  -1485       O  
ATOM   2980  CB  LYS A 445     -19.346  -2.265  -9.778  1.00 74.00           C  
ANISOU 2980  CB  LYS A 445    12274   6978   8866  -2368    864  -1239       C  
ATOM   2981  CG  LYS A 445     -19.780  -1.519  -8.519  1.00 74.84           C  
ANISOU 2981  CG  LYS A 445    12452   6979   9005  -2131    861  -1106       C  
ATOM   2982  CD  LYS A 445     -21.251  -1.669  -8.157  1.00 78.16           C  
ANISOU 2982  CD  LYS A 445    13127   7045   9527  -2003    806  -1158       C  
ATOM   2983  CE  LYS A 445     -22.047  -0.568  -8.834  1.00 81.75           C  
ANISOU 2983  CE  LYS A 445    13772   7231  10059  -2198    763   -998       C  
ATOM   2984  NZ  LYS A 445     -23.366  -0.363  -8.202  1.00 85.60           N1+
ANISOU 2984  NZ  LYS A 445    14498   7368  10658  -2022    697   -973       N1+
ATOM   2985  N   VAL A 446     -17.133  -2.439 -12.502  1.00 68.44           N  
ANISOU 2985  N   VAL A 446    11157   6778   8068  -2933    909  -1279       N  
ATOM   2986  CA  VAL A 446     -16.739  -3.303 -13.598  1.00 67.66           C  
ANISOU 2986  CA  VAL A 446    10951   6801   7954  -3109    884  -1413       C  
ATOM   2987  C   VAL A 446     -15.514  -4.135 -13.249  1.00 63.61           C  
ANISOU 2987  C   VAL A 446    10224   6580   7366  -2983    886  -1481       C  
ATOM   2988  O   VAL A 446     -15.331  -5.246 -13.744  1.00 60.94           O  
ANISOU 2988  O   VAL A 446     9831   6327   6997  -3032    840  -1623       O  
ATOM   2989  CB  VAL A 446     -16.445  -2.425 -14.825  1.00 67.88           C  
ANISOU 2989  CB  VAL A 446    10894   6889   8007  -3394    914  -1321       C  
ATOM   2990  CG1 VAL A 446     -15.336  -1.446 -14.493  1.00 66.60           C  
ANISOU 2990  CG1 VAL A 446    10558   6944   7802  -3341    984  -1179       C  
ATOM   2991  CG2 VAL A 446     -16.089  -3.243 -16.058  1.00 69.13           C  
ANISOU 2991  CG2 VAL A 446    10924   7177   8167  -3595    877  -1450       C  
ATOM   2992  N   PHE A 447     -14.667  -3.576 -12.398  1.00 63.03           N  
ANISOU 2992  N   PHE A 447    10034   6655   7260  -2832    930  -1368       N  
ATOM   2993  CA  PHE A 447     -13.407  -4.231 -12.016  1.00 61.85           C  
ANISOU 2993  CA  PHE A 447     9682   6771   7048  -2721    927  -1397       C  
ATOM   2994  C   PHE A 447     -13.651  -5.499 -11.222  1.00 60.07           C  
ANISOU 2994  C   PHE A 447     9500   6556   6768  -2541    898  -1517       C  
ATOM   2995  O   PHE A 447     -12.825  -6.383 -11.214  1.00 55.01           O  
ANISOU 2995  O   PHE A 447     8724   6112   6067  -2508    875  -1575       O  
ATOM   2996  CB  PHE A 447     -12.520  -3.280 -11.211  1.00 60.31           C  
ANISOU 2996  CB  PHE A 447     9377   6700   6837  -2607    975  -1250       C  
ATOM   2997  CG  PHE A 447     -11.988  -2.127 -12.009  1.00 61.45           C  
ANISOU 2997  CG  PHE A 447     9433   6909   7003  -2775   1016  -1154       C  
ATOM   2998  CD1 PHE A 447     -10.993  -2.326 -12.968  1.00 61.93           C  
ANISOU 2998  CD1 PHE A 447     9304   7160   7067  -2898   1014  -1196       C  
ATOM   2999  CD2 PHE A 447     -12.472  -0.834 -11.804  1.00 63.18           C  
ANISOU 2999  CD2 PHE A 447     9755   7016   7236  -2806   1056  -1022       C  
ATOM   3000  CE1 PHE A 447     -10.486  -1.260 -13.705  1.00 63.14           C  
ANISOU 3000  CE1 PHE A 447     9359   7395   7235  -3040   1068  -1127       C  
ATOM   3001  CE2 PHE A 447     -11.968   0.235 -12.533  1.00 64.17           C  
ANISOU 3001  CE2 PHE A 447     9795   7231   7356  -2965   1108   -941       C  
ATOM   3002  CZ  PHE A 447     -10.975   0.022 -13.488  1.00 64.21           C  
ANISOU 3002  CZ  PHE A 447     9600   7432   7364  -3079   1122  -1003       C  
ATOM   3003  N   GLN A 448     -14.804  -5.569 -10.566  1.00 62.55           N  
ANISOU 3003  N   GLN A 448    10006   6660   7100  -2424    900  -1553       N  
ATOM   3004  CA  GLN A 448     -15.175  -6.749  -9.803  1.00 64.42           C  
ANISOU 3004  CA  GLN A 448    10295   6903   7278  -2245    890  -1688       C  
ATOM   3005  C   GLN A 448     -15.530  -7.954 -10.693  1.00 67.55           C  
ANISOU 3005  C   GLN A 448    10742   7288   7635  -2368    835  -1880       C  
ATOM   3006  O   GLN A 448     -15.811  -9.036 -10.189  1.00 67.78           O  
ANISOU 3006  O   GLN A 448    10814   7350   7590  -2242    827  -2017       O  
ATOM   3007  CB  GLN A 448     -16.295  -6.401  -8.817  1.00 63.93           C  
ANISOU 3007  CB  GLN A 448    10410   6617   7262  -2057    910  -1678       C  
ATOM   3008  CG  GLN A 448     -15.743  -5.608  -7.651  1.00 62.28           C  
ANISOU 3008  CG  GLN A 448    10103   6509   7050  -1884    952  -1514       C  
ATOM   3009  CD  GLN A 448     -16.559  -4.395  -7.302  1.00 62.94           C  
ANISOU 3009  CD  GLN A 448    10325   6369   7221  -1842    953  -1387       C  
ATOM   3010  NE2 GLN A 448     -17.709  -4.619  -6.670  1.00 62.84           N  
ANISOU 3010  NE2 GLN A 448    10476   6148   7254  -1675    943  -1451       N  
ATOM   3011  OE1 GLN A 448     -16.149  -3.253  -7.581  1.00 64.59           O  
ANISOU 3011  OE1 GLN A 448    10492   6596   7452  -1950    961  -1231       O  
ATOM   3012  N   GLU A 449     -15.503  -7.767 -12.007  1.00 79.52           N  
ANISOU 3012  N   GLU A 449    11641   8636   9937  -2754   -160   -478       N  
ATOM   3013  CA  GLU A 449     -15.665  -8.870 -12.921  1.00 80.90           C  
ANISOU 3013  CA  GLU A 449    11786   8906  10046  -2712     53   -759       C  
ATOM   3014  C   GLU A 449     -14.322  -9.131 -13.619  1.00 79.08           C  
ANISOU 3014  C   GLU A 449    11405   9033   9609  -2832    231   -893       C  
ATOM   3015  O   GLU A 449     -13.954  -8.392 -14.532  1.00 77.59           O  
ANISOU 3015  O   GLU A 449    11338   8913   9229  -3138    261   -916       O  
ATOM   3016  CB  GLU A 449     -16.799  -8.574 -13.924  1.00 84.07           C  
ANISOU 3016  CB  GLU A 449    12500   9063  10379  -2932     11   -827       C  
ATOM   3017  CG  GLU A 449     -17.206  -9.774 -14.775  1.00 85.13           C  
ANISOU 3017  CG  GLU A 449    12634   9240  10474  -2884    189  -1103       C  
ATOM   3018  CD  GLU A 449     -16.922 -11.097 -14.089  1.00 86.63           C  
ANISOU 3018  CD  GLU A 449    12563   9566  10787  -2529    327  -1224       C  
ATOM   3019  OE1 GLU A 449     -17.661 -11.445 -13.149  1.00 88.01           O  
ANISOU 3019  OE1 GLU A 449    12716   9538  11188  -2251    284  -1185       O  
ATOM   3020  OE2 GLU A 449     -15.931 -11.775 -14.455  1.00 89.12           O1-
ANISOU 3020  OE2 GLU A 449    12689  10189  10981  -2529    476  -1351       O1-
ATOM   3021  N   PRO A 450     -13.587 -10.185 -13.193  1.00 80.32           N  
ANISOU 3021  N   PRO A 450    11298   9411   9810  -2595    356   -983       N  
ATOM   3022  CA  PRO A 450     -12.279 -10.556 -13.795  1.00 79.46           C  
ANISOU 3022  CA  PRO A 450    11030   9618   9544  -2664    500  -1102       C  
ATOM   3023  C   PRO A 450     -12.281 -10.809 -15.317  1.00 80.28           C  
ANISOU 3023  C   PRO A 450    11194   9814   9493  -2875    619  -1308       C  
ATOM   3024  O   PRO A 450     -11.248 -10.598 -15.969  1.00 78.84           O  
ANISOU 3024  O   PRO A 450    10923   9840   9192  -3008    700  -1366       O  
ATOM   3025  CB  PRO A 450     -11.873 -11.847 -13.051  1.00 78.27           C  
ANISOU 3025  CB  PRO A 450    10638   9616   9483  -2364    586  -1164       C  
ATOM   3026  CG  PRO A 450     -13.052 -12.245 -12.230  1.00 81.45           C  
ANISOU 3026  CG  PRO A 450    11068   9796  10083  -2144    546  -1135       C  
ATOM   3027  CD  PRO A 450     -13.911 -11.033 -12.029  1.00 82.18           C  
ANISOU 3027  CD  PRO A 450    11363   9603  10257  -2251    362   -959       C  
ATOM   3028  N   LYS A 451     -13.414 -11.258 -15.871  1.00 79.61           N  
ANISOU 3028  N   LYS A 451    11250   9572   9425  -2903    627  -1421       N  
ATOM   3029  CA  LYS A 451     -13.548 -11.449 -17.325  1.00 76.60           C  
ANISOU 3029  CA  LYS A 451    10931   9267   8907  -3143    713  -1597       C  
ATOM   3030  C   LYS A 451     -13.559 -10.140 -18.111  1.00 73.35           C  
ANISOU 3030  C   LYS A 451    10681   8818   8370  -3492    694  -1543       C  
ATOM   3031  O   LYS A 451     -13.185 -10.139 -19.271  1.00 69.85           O  
ANISOU 3031  O   LYS A 451    10186   8539   7814  -3700    799  -1673       O  
ATOM   3032  CB  LYS A 451     -14.776 -12.296 -17.625  1.00 80.87           C  
ANISOU 3032  CB  LYS A 451    11613   9629   9484  -3098    714  -1726       C  
ATOM   3033  CG  LYS A 451     -14.470 -13.729 -17.160  1.00 83.01           C  
ANISOU 3033  CG  LYS A 451    11701  10035   9801  -2822    800  -1841       C  
ATOM   3034  CD  LYS A 451     -15.565 -14.773 -17.032  1.00 84.43           C  
ANISOU 3034  CD  LYS A 451    12007  10040  10032  -2684    835  -1979       C  
ATOM   3035  CE  LYS A 451     -14.941 -16.016 -16.432  1.00 83.61           C  
ANISOU 3035  CE  LYS A 451    11704  10129   9935  -2446    937  -2059       C  
ATOM   3036  NZ  LYS A 451     -15.911 -17.132 -16.462  1.00 86.45           N1+
ANISOU 3036  NZ  LYS A 451    12204  10353  10290  -2352   1012  -2239       N1+
ATOM   3037  N   ALA A 452     -13.927  -9.038 -17.443  1.00 71.84           N  
ANISOU 3037  N   ALA A 452    10668   8427   8201  -3560    561  -1345       N  
ATOM   3038  CA  ALA A 452     -13.947  -7.683 -18.024  1.00 71.10           C  
ANISOU 3038  CA  ALA A 452    10780   8280   7954  -3924    536  -1266       C  
ATOM   3039  C   ALA A 452     -12.569  -7.145 -18.387  1.00 69.57           C  
ANISOU 3039  C   ALA A 452    10449   8352   7633  -4056    669  -1298       C  
ATOM   3040  O   ALA A 452     -12.440  -6.219 -19.181  1.00 69.63           O  
ANISOU 3040  O   ALA A 452    10584   8391   7481  -4385    740  -1317       O  
ATOM   3041  CB  ALA A 452     -14.632  -6.712 -17.074  1.00 72.51           C  
ANISOU 3041  CB  ALA A 452    11191   8171   8189  -3950    316  -1016       C  
ATOM   3042  N   VAL A 453     -11.548  -7.703 -17.759  1.00 68.67           N  
ANISOU 3042  N   VAL A 453    10088   8412   7587  -3804    708  -1303       N  
ATOM   3043  CA  VAL A 453     -10.174  -7.457 -18.156  1.00 67.94           C  
ANISOU 3043  CA  VAL A 453     9839   8565   7409  -3866    850  -1376       C  
ATOM   3044  C   VAL A 453      -9.749  -8.485 -19.205  1.00 68.24           C  
ANISOU 3044  C   VAL A 453     9645   8821   7463  -3817    999  -1598       C  
ATOM   3045  O   VAL A 453      -9.723  -9.688 -18.934  1.00 70.55           O  
ANISOU 3045  O   VAL A 453     9781   9175   7852  -3570    980  -1652       O  
ATOM   3046  CB  VAL A 453      -9.253  -7.593 -16.949  1.00 65.68           C  
ANISOU 3046  CB  VAL A 453     9419   8343   7191  -3628    791  -1258       C  
ATOM   3047  CG1 VAL A 453      -7.801  -7.467 -17.380  1.00 64.86           C  
ANISOU 3047  CG1 VAL A 453     9161   8465   7020  -3656    938  -1355       C  
ATOM   3048  CG2 VAL A 453      -9.623  -6.546 -15.916  1.00 66.70           C  
ANISOU 3048  CG2 VAL A 453     9756   8272   7315  -3696    611  -1017       C  
ATOM   3049  N   THR A 454      -9.410  -8.033 -20.399  1.00 67.27           N  
ANISOU 3049  N   THR A 454     9490   8821   7246  -4064   1145  -1726       N  
ATOM   3050  CA  THR A 454      -9.141  -8.964 -21.480  1.00 67.22           C  
ANISOU 3050  CA  THR A 454     9253   9009   7280  -4050   1248  -1917       C  
ATOM   3051  C   THR A 454      -7.684  -9.049 -21.839  1.00 65.40           C  
ANISOU 3051  C   THR A 454     8757   9010   7080  -3973   1373  -2007       C  
ATOM   3052  O   THR A 454      -7.267 -10.026 -22.463  1.00 67.72           O  
ANISOU 3052  O   THR A 454     8808   9468   7453  -3870   1400  -2126       O  
ATOM   3053  CB  THR A 454      -9.875  -8.527 -22.740  1.00 68.48           C  
ANISOU 3053  CB  THR A 454     9506   9160   7352  -4390   1328  -2015       C  
ATOM   3054  CG2 THR A 454     -11.352  -8.810 -22.622  1.00 69.15           C  
ANISOU 3054  CG2 THR A 454     9829   9013   7431  -4441   1194  -1970       C  
ATOM   3055  OG1 THR A 454      -9.662  -7.123 -22.900  1.00 71.15           O  
ANISOU 3055  OG1 THR A 454     9999   9469   7564  -4659   1419  -1969       O  
ATOM   3056  N   HIS A 455      -6.928  -8.012 -21.520  1.00 63.87           N  
ANISOU 3056  N   HIS A 455     8624   8818   6825  -4045   1441  -1954       N  
ATOM   3057  CA  HIS A 455      -5.526  -7.973 -21.890  1.00 64.14           C  
ANISOU 3057  CA  HIS A 455     8437   9034   6901  -3973   1579  -2055       C  
ATOM   3058  C   HIS A 455      -4.720  -7.464 -20.729  1.00 62.16           C  
ANISOU 3058  C   HIS A 455     8274   8724   6621  -3859   1531  -1926       C  
ATOM   3059  O   HIS A 455      -5.107  -6.505 -20.062  1.00 61.61           O  
ANISOU 3059  O   HIS A 455     8466   8503   6441  -4000   1472  -1789       O  
ATOM   3060  CB  HIS A 455      -5.281  -7.059 -23.083  1.00 67.46           C  
ANISOU 3060  CB  HIS A 455     8834   9544   7252  -4262   1802  -2199       C  
ATOM   3061  CG  HIS A 455      -5.930  -7.516 -24.358  1.00 71.31           C  
ANISOU 3061  CG  HIS A 455     9187  10129   7776  -4414   1865  -2335       C  
ATOM   3062  CD2 HIS A 455      -5.404  -8.065 -25.481  1.00 73.17           C  
ANISOU 3062  CD2 HIS A 455     9096  10571   8133  -4400   1975  -2500       C  
ATOM   3063  ND1 HIS A 455      -7.283  -7.391 -24.596  1.00 73.30           N  
ANISOU 3063  ND1 HIS A 455     9649  10258   7944  -4629   1796  -2295       N  
ATOM   3064  CE1 HIS A 455      -7.563  -7.860 -25.800  1.00 75.17           C  
ANISOU 3064  CE1 HIS A 455     9708  10627   8225  -4760   1865  -2433       C  
ATOM   3065  NE2 HIS A 455      -6.439  -8.270 -26.360  1.00 74.89           N  
ANISOU 3065  NE2 HIS A 455     9328  10803   8323  -4624   1971  -2555       N  
ATOM   3066  N   VAL A 456      -3.589  -8.107 -20.492  1.00 60.06           N  
ANISOU 3066  N   VAL A 456     7802   8569   6449  -3622   1532  -1955       N  
ATOM   3067  CA  VAL A 456      -2.748  -7.737 -19.391  1.00 59.44           C  
ANISOU 3067  CA  VAL A 456     7801   8441   6344  -3517   1472  -1833       C  
ATOM   3068  C   VAL A 456      -1.296  -7.756 -19.841  1.00 59.31           C  
ANISOU 3068  C   VAL A 456     7609   8543   6385  -3427   1603  -1957       C  
ATOM   3069  O   VAL A 456      -0.763  -8.782 -20.245  1.00 58.63           O  
ANISOU 3069  O   VAL A 456     7272   8573   6430  -3235   1589  -2036       O  
ATOM   3070  CB  VAL A 456      -2.978  -8.689 -18.204  1.00 59.32           C  
ANISOU 3070  CB  VAL A 456     7755   8389   6397  -3271   1277  -1681       C  
ATOM   3071  CG1 VAL A 456      -2.124  -8.279 -17.001  1.00 58.71           C  
ANISOU 3071  CG1 VAL A 456     7754   8266   6289  -3195   1198  -1532       C  
ATOM   3072  CG2 VAL A 456      -4.454  -8.691 -17.817  1.00 59.64           C  
ANISOU 3072  CG2 VAL A 456     7950   8285   6424  -3325   1168  -1585       C  
ATOM   3073  N   TRP A 457      -0.676  -6.590 -19.790  1.00 60.43           N  
ANISOU 3073  N   TRP A 457     7902   8636   6422  -3579   1724  -1976       N  
ATOM   3074  CA  TRP A 457       0.706  -6.456 -20.168  1.00 62.69           C  
ANISOU 3074  CA  TRP A 457     8063   8987   6767  -3493   1868  -2108       C  
ATOM   3075  C   TRP A 457       1.475  -6.014 -18.947  1.00 64.21           C  
ANISOU 3075  C   TRP A 457     8443   9076   6878  -3444   1776  -1969       C  
ATOM   3076  O   TRP A 457       1.106  -5.009 -18.327  1.00 65.48           O  
ANISOU 3076  O   TRP A 457     8890   9121   6868  -3654   1744  -1855       O  
ATOM   3077  CB  TRP A 457       0.871  -5.383 -21.240  1.00 65.54           C  
ANISOU 3077  CB  TRP A 457     8465   9379   7059  -3741   2150  -2296       C  
ATOM   3078  CG  TRP A 457       0.560  -5.799 -22.661  1.00 66.65           C  
ANISOU 3078  CG  TRP A 457     8332   9669   7326  -3780   2294  -2481       C  
ATOM   3079  CD1 TRP A 457       1.385  -6.459 -23.531  1.00 67.42           C  
ANISOU 3079  CD1 TRP A 457     8081   9899   7635  -3597   2385  -2641       C  
ATOM   3080  CD2 TRP A 457      -0.640  -5.522 -23.377  1.00 65.59           C  
ANISOU 3080  CD2 TRP A 457     8250   9556   7115  -4040   2350  -2512       C  
ATOM   3081  CE2 TRP A 457      -0.489  -6.060 -24.671  1.00 66.42           C  
ANISOU 3081  CE2 TRP A 457     8016   9833   7390  -4014   2480  -2693       C  
ATOM   3082  CE3 TRP A 457      -1.837  -4.887 -23.040  1.00 64.67           C  
ANISOU 3082  CE3 TRP A 457     8438   9319   6814  -4295   2278  -2389       C  
ATOM   3083  NE1 TRP A 457       0.760  -6.616 -24.747  1.00 67.32           N  
ANISOU 3083  NE1 TRP A 457     7876  10012   7690  -3733   2494  -2768       N  
ATOM   3084  CZ2 TRP A 457      -1.481  -5.986 -25.619  1.00 67.71           C  
ANISOU 3084  CZ2 TRP A 457     8139  10063   7524  -4256   2551  -2761       C  
ATOM   3085  CZ3 TRP A 457      -2.824  -4.814 -23.984  1.00 66.62           C  
ANISOU 3085  CZ3 TRP A 457     8674   9609   7030  -4525   2346  -2457       C  
ATOM   3086  CH2 TRP A 457      -2.642  -5.354 -25.267  1.00 67.72           C  
ANISOU 3086  CH2 TRP A 457     8476   9934   7321  -4518   2490  -2645       C  
ATOM   3087  N   LYS A 458       2.532  -6.760 -18.609  1.00 63.34           N  
ANISOU 3087  N   LYS A 458     8185   9000   6881  -3196   1711  -1964       N  
ATOM   3088  CA  LYS A 458       3.461  -6.371 -17.555  1.00 61.30           C  
ANISOU 3088  CA  LYS A 458     8092   8647   6551  -3162   1635  -1854       C  
ATOM   3089  C   LYS A 458       4.865  -6.433 -18.117  1.00 61.36           C  
ANISOU 3089  C   LYS A 458     7983   8669   6661  -3029   1771  -2021       C  
ATOM   3090  O   LYS A 458       5.311  -7.483 -18.591  1.00 59.92           O  
ANISOU 3090  O   LYS A 458     7534   8572   6663  -2802   1734  -2084       O  
ATOM   3091  CB  LYS A 458       3.347  -7.296 -16.348  1.00 60.64           C  
ANISOU 3091  CB  LYS A 458     7975   8563   6504  -2985   1381  -1641       C  
ATOM   3092  CG  LYS A 458       4.221  -6.895 -15.161  1.00 61.51           C  
ANISOU 3092  CG  LYS A 458     8259   8582   6529  -2990   1272  -1492       C  
ATOM   3093  CD  LYS A 458       4.374  -8.016 -14.143  1.00 60.07           C  
ANISOU 3093  CD  LYS A 458     7965   8443   6415  -2792   1064  -1322       C  
ATOM   3094  CE  LYS A 458       5.644  -8.825 -14.368  1.00 60.93           C  
ANISOU 3094  CE  LYS A 458     7933   8591   6625  -2592   1056  -1392       C  
ATOM   3095  NZ  LYS A 458       5.973  -9.701 -13.207  1.00 60.54           N1+
ANISOU 3095  NZ  LYS A 458     7850   8570   6583  -2472    858  -1202       N1+
ATOM   3096  N   GLY A 459       5.554  -5.296 -18.067  1.00 62.01           N  
ANISOU 3096  N   GLY A 459     8283   8654   6624  -3177   1921  -2092       N  
ATOM   3097  CA  GLY A 459       6.879  -5.177 -18.654  1.00 62.64           C  
ANISOU 3097  CA  GLY A 459     8283   8708   6811  -3056   2096  -2286       C  
ATOM   3098  C   GLY A 459       6.835  -5.417 -20.150  1.00 63.02           C  
ANISOU 3098  C   GLY A 459     8025   8877   7043  -2997   2310  -2523       C  
ATOM   3099  O   GLY A 459       7.760  -5.976 -20.720  1.00 62.20           O  
ANISOU 3099  O   GLY A 459     7683   8795   7157  -2766   2355  -2647       O  
ATOM   3100  N   GLY A 460       5.732  -5.011 -20.770  1.00 64.01           N  
ANISOU 3100  N   GLY A 460     8152   9077   7093  -3215   2419  -2570       N  
ATOM   3101  CA  GLY A 460       5.517  -5.188 -22.203  1.00 66.85           C  
ANISOU 3101  CA  GLY A 460     8211   9576   7612  -3220   2619  -2778       C  
ATOM   3102  C   GLY A 460       5.379  -6.624 -22.666  1.00 67.04           C  
ANISOU 3102  C   GLY A 460     7875   9725   7875  -2975   2447  -2758       C  
ATOM   3103  O   GLY A 460       5.489  -6.891 -23.857  1.00 67.28           O  
ANISOU 3103  O   GLY A 460     7598   9873   8092  -2931   2580  -2926       O  
ATOM   3104  N   LYS A 461       5.157  -7.542 -21.725  1.00 67.11           N  
ANISOU 3104  N   LYS A 461     7916   9710   7870  -2834   2154  -2552       N  
ATOM   3105  CA  LYS A 461       4.938  -8.950 -22.017  1.00 67.99           C  
ANISOU 3105  CA  LYS A 461     7758   9930   8144  -2645   1962  -2508       C  
ATOM   3106  C   LYS A 461       3.471  -9.242 -21.707  1.00 65.83           C  
ANISOU 3106  C   LYS A 461     7588   9682   7744  -2780   1843  -2388       C  
ATOM   3107  O   LYS A 461       2.888  -8.665 -20.793  1.00 65.48           O  
ANISOU 3107  O   LYS A 461     7815   9540   7523  -2906   1797  -2259       O  
ATOM   3108  CB  LYS A 461       5.880  -9.808 -21.174  1.00 69.38           C  
ANISOU 3108  CB  LYS A 461     7919  10056   8386  -2392   1747  -2382       C  
ATOM   3109  CG  LYS A 461       5.684 -11.319 -21.281  1.00 73.08           C  
ANISOU 3109  CG  LYS A 461     8177  10624   8964  -2226   1517  -2304       C  
ATOM   3110  CD  LYS A 461       6.452 -12.055 -20.186  1.00 75.37           C  
ANISOU 3110  CD  LYS A 461     8545  10855   9238  -2050   1300  -2137       C  
ATOM   3111  CE  LYS A 461       6.391 -13.560 -20.314  1.00 77.67           C  
ANISOU 3111  CE  LYS A 461     8660  11244   9608  -1912   1078  -2066       C  
ATOM   3112  NZ  LYS A 461       7.367 -14.073 -21.306  1.00 82.68           N1+
ANISOU 3112  NZ  LYS A 461     9029  11909  10478  -1748   1035  -2160       N1+
ATOM   3113  N   LEU A 462       2.875 -10.129 -22.485  1.00 64.51           N  
ANISOU 3113  N   LEU A 462     7204   9631   7677  -2756   1784  -2432       N  
ATOM   3114  CA  LEU A 462       1.453 -10.319 -22.451  1.00 62.46           C  
ANISOU 3114  CA  LEU A 462     7043   9376   7312  -2905   1719  -2374       C  
ATOM   3115  C   LEU A 462       1.142 -11.548 -21.635  1.00 59.65           C  
ANISOU 3115  C   LEU A 462     6694   9019   6949  -2738   1481  -2231       C  
ATOM   3116  O   LEU A 462       1.559 -12.638 -21.986  1.00 58.79           O  
ANISOU 3116  O   LEU A 462     6382   9002   6955  -2587   1372  -2249       O  
ATOM   3117  CB  LEU A 462       0.937 -10.469 -23.874  1.00 64.91           C  
ANISOU 3117  CB  LEU A 462     7140   9812   7712  -3034   1820  -2527       C  
ATOM   3118  CG  LEU A 462      -0.585 -10.464 -24.026  1.00 65.73           C  
ANISOU 3118  CG  LEU A 462     7387   9893   7695  -3245   1787  -2496       C  
ATOM   3119  CD1 LEU A 462      -1.249  -9.287 -23.331  1.00 66.01           C  
ANISOU 3119  CD1 LEU A 462     7765   9777   7538  -3443   1845  -2412       C  
ATOM   3120  CD2 LEU A 462      -0.930 -10.459 -25.497  1.00 67.95           C  
ANISOU 3120  CD2 LEU A 462     7451  10309   8060  -3417   1910  -2654       C  
ATOM   3121  N   PHE A 463       0.414 -11.363 -20.541  1.00 59.20           N  
ANISOU 3121  N   PHE A 463     6872   8859   6763  -2775   1401  -2087       N  
ATOM   3122  CA  PHE A 463       0.128 -12.449 -19.605  1.00 58.83           C  
ANISOU 3122  CA  PHE A 463     6843   8809   6700  -2619   1221  -1959       C  
ATOM   3123  C   PHE A 463      -1.300 -12.956 -19.651  1.00 59.21           C  
ANISOU 3123  C   PHE A 463     6957   8835   6704  -2683   1173  -1953       C  
ATOM   3124  O   PHE A 463      -1.572 -14.117 -19.308  1.00 58.01           O  
ANISOU 3124  O   PHE A 463     6766   8721   6556  -2564   1064  -1921       O  
ATOM   3125  CB  PHE A 463       0.442 -12.006 -18.190  1.00 58.10           C  
ANISOU 3125  CB  PHE A 463     6923   8618   6535  -2567   1157  -1792       C  
ATOM   3126  CG  PHE A 463       1.897 -11.997 -17.886  1.00 59.47           C  
ANISOU 3126  CG  PHE A 463     7046   8803   6746  -2450   1139  -1770       C  
ATOM   3127  CD1 PHE A 463       2.569 -13.191 -17.650  1.00 59.95           C  
ANISOU 3127  CD1 PHE A 463     6976   8935   6865  -2267   1012  -1729       C  
ATOM   3128  CD2 PHE A 463       2.611 -10.804 -17.858  1.00 61.33           C  
ANISOU 3128  CD2 PHE A 463     7393   8964   6945  -2540   1245  -1794       C  
ATOM   3129  CE1 PHE A 463       3.928 -13.190 -17.391  1.00 61.38           C  
ANISOU 3129  CE1 PHE A 463     7135   9098   7088  -2162    974  -1702       C  
ATOM   3130  CE2 PHE A 463       3.973 -10.790 -17.574  1.00 62.21           C  
ANISOU 3130  CE2 PHE A 463     7491   9052   7094  -2428   1227  -1784       C  
ATOM   3131  CZ  PHE A 463       4.630 -11.987 -17.350  1.00 62.78           C  
ANISOU 3131  CZ  PHE A 463     7426   9181   7246  -2231   1083  -1734       C  
ATOM   3132  N   LYS A 464      -2.212 -12.077 -20.041  1.00 60.15           N  
ANISOU 3132  N   LYS A 464     7210   8878   6768  -2886   1257  -1986       N  
ATOM   3133  CA  LYS A 464      -3.579 -12.472 -20.314  1.00 60.11           C  
ANISOU 3133  CA  LYS A 464     7284   8824   6731  -2973   1223  -2009       C  
ATOM   3134  C   LYS A 464      -3.954 -11.770 -21.584  1.00 62.32           C  
ANISOU 3134  C   LYS A 464     7552   9129   6997  -3217   1349  -2135       C  
ATOM   3135  O   LYS A 464      -3.705 -10.580 -21.743  1.00 61.46           O  
ANISOU 3135  O   LYS A 464     7527   8985   6838  -3370   1465  -2143       O  
ATOM   3136  CB  LYS A 464      -4.498 -12.032 -19.187  1.00 59.20           C  
ANISOU 3136  CB  LYS A 464     7403   8531   6558  -2979   1158  -1867       C  
ATOM   3137  CG  LYS A 464      -5.939 -12.499 -19.287  1.00 60.03           C  
ANISOU 3137  CG  LYS A 464     7624   8534   6651  -3022   1113  -1887       C  
ATOM   3138  CD  LYS A 464      -6.790 -11.820 -18.210  1.00 60.31           C  
ANISOU 3138  CD  LYS A 464     7879   8363   6675  -3023   1043  -1734       C  
ATOM   3139  CE  LYS A 464      -8.213 -12.367 -18.125  1.00 60.95           C  
ANISOU 3139  CE  LYS A 464     8086   8296   6778  -3004    993  -1754       C  
ATOM   3140  NZ  LYS A 464      -9.063 -11.633 -17.135  1.00 60.76           N1+
ANISOU 3140  NZ  LYS A 464     8254   8042   6790  -2990    903  -1595       N1+
ATOM   3141  N   GLY A 465      -4.558 -12.520 -22.489  1.00 64.70           N  
ANISOU 3141  N   GLY A 465     7761   9497   7322  -3284   1329  -2233       N  
ATOM   3142  CA  GLY A 465      -5.041 -11.954 -23.737  1.00 65.36           C  
ANISOU 3142  CA  GLY A 465     7819   9622   7393  -3550   1443  -2349       C  
ATOM   3143  C   GLY A 465      -5.774 -13.020 -24.497  1.00 64.62           C  
ANISOU 3143  C   GLY A 465     7650   9586   7318  -3603   1361  -2424       C  
ATOM   3144  O   GLY A 465      -5.835 -14.148 -24.048  1.00 63.11           O  
ANISOU 3144  O   GLY A 465     7440   9401   7136  -3432   1231  -2396       O  
ATOM   3145  N   PRO A 466      -6.323 -12.673 -25.659  1.00 67.27           N  
ANISOU 3145  N   PRO A 466     7950   9969   7640  -3867   1439  -2522       N  
ATOM   3146  CA  PRO A 466      -6.971 -13.660 -26.505  1.00 68.24           C  
ANISOU 3146  CA  PRO A 466     7995  10160   7774  -3965   1349  -2597       C  
ATOM   3147  C   PRO A 466      -6.034 -14.828 -26.849  1.00 67.20           C  
ANISOU 3147  C   PRO A 466     7559  10209   7761  -3783   1244  -2632       C  
ATOM   3148  O   PRO A 466      -4.900 -14.600 -27.290  1.00 65.08           O  
ANISOU 3148  O   PRO A 466     7020  10083   7625  -3711   1308  -2669       O  
ATOM   3149  CB  PRO A 466      -7.328 -12.854 -27.761  1.00 71.63           C  
ANISOU 3149  CB  PRO A 466     8360  10660   8194  -4298   1487  -2693       C  
ATOM   3150  CG  PRO A 466      -6.390 -11.685 -27.756  1.00 71.92           C  
ANISOU 3150  CG  PRO A 466     8314  10749   8265  -4307   1678  -2708       C  
ATOM   3151  CD  PRO A 466      -6.278 -11.352 -26.307  1.00 70.08           C  
ANISOU 3151  CD  PRO A 466     8325  10341   7960  -4121   1628  -2575       C  
ATOM   3152  N   GLY A 467      -6.507 -16.060 -26.618  1.00 66.64           N  
ANISOU 3152  N   GLY A 467     7557  10121   7642  -3711   1081  -2617       N  
ATOM   3153  CA  GLY A 467      -5.727 -17.276 -26.882  1.00 66.81           C  
ANISOU 3153  CA  GLY A 467     7351  10296   7735  -3574    931  -2623       C  
ATOM   3154  C   GLY A 467      -4.298 -17.205 -26.362  1.00 65.98           C  
ANISOU 3154  C   GLY A 467     7072  10256   7741  -3323    931  -2562       C  
ATOM   3155  O   GLY A 467      -3.362 -17.570 -27.068  1.00 67.12           O  
ANISOU 3155  O   GLY A 467     6923  10550   8031  -3266    869  -2587       O  
ATOM   3156  N   ILE A 468      -4.151 -16.700 -25.134  1.00 63.03           N  
ANISOU 3156  N   ILE A 468     6879   9757   7310  -3182    987  -2477       N  
ATOM   3157  CA  ILE A 468      -2.899 -16.636 -24.413  1.00 59.62           C  
ANISOU 3157  CA  ILE A 468     6364   9344   6942  -2958    974  -2402       C  
ATOM   3158  C   ILE A 468      -3.045 -17.518 -23.198  1.00 57.38           C  
ANISOU 3158  C   ILE A 468     6244   9000   6558  -2799    863  -2301       C  
ATOM   3159  O   ILE A 468      -3.966 -17.340 -22.401  1.00 54.05           O  
ANISOU 3159  O   ILE A 468     6052   8448   6037  -2812    897  -2263       O  
ATOM   3160  CB  ILE A 468      -2.640 -15.238 -23.852  1.00 59.34           C  
ANISOU 3160  CB  ILE A 468     6441   9210   6895  -2965   1132  -2368       C  
ATOM   3161  CG1 ILE A 468      -2.374 -14.239 -24.968  1.00 59.45           C  
ANISOU 3161  CG1 ILE A 468     6308   9289   6991  -3131   1302  -2483       C  
ATOM   3162  CG2 ILE A 468      -1.486 -15.279 -22.836  1.00 59.18           C  
ANISOU 3162  CG2 ILE A 468     6414   9171   6901  -2741   1090  -2268       C  
ATOM   3163  CD1 ILE A 468      -0.998 -14.356 -25.581  1.00 60.19           C  
ANISOU 3163  CD1 ILE A 468     6092   9507   7269  -2998   1320  -2542       C  
ATOM   3164  N   GLY A 469      -2.085 -18.411 -23.023  1.00 58.12           N  
ANISOU 3164  N   GLY A 469     6212   9182   6687  -2647    734  -2254       N  
ATOM   3165  CA  GLY A 469      -2.144 -19.412 -21.975  1.00 57.13           C  
ANISOU 3165  CA  GLY A 469     6218   9038   6451  -2528    637  -2169       C  
ATOM   3166  C   GLY A 469      -2.110 -18.895 -20.546  1.00 55.16           C  
ANISOU 3166  C   GLY A 469     6126   8682   6149  -2414    707  -2063       C  
ATOM   3167  O   GLY A 469      -1.858 -17.713 -20.278  1.00 52.08           O  
ANISOU 3167  O   GLY A 469     5760   8223   5805  -2416    801  -2031       O  
ATOM   3168  N   PRO A 470      -2.346 -19.808 -19.612  1.00 55.22           N  
ANISOU 3168  N   PRO A 470     6241   8685   6055  -2330    658  -2005       N  
ATOM   3169  CA  PRO A 470      -2.519 -19.450 -18.227  1.00 54.66           C  
ANISOU 3169  CA  PRO A 470     6293   8526   5949  -2233    719  -1903       C  
ATOM   3170  C   PRO A 470      -1.273 -18.809 -17.609  1.00 54.40           C  
ANISOU 3170  C   PRO A 470     6199   8500   5971  -2142    704  -1787       C  
ATOM   3171  O   PRO A 470      -1.380 -18.055 -16.623  1.00 53.57           O  
ANISOU 3171  O   PRO A 470     6179   8310   5866  -2109    754  -1693       O  
ATOM   3172  CB  PRO A 470      -2.853 -20.799 -17.542  1.00 54.59           C  
ANISOU 3172  CB  PRO A 470     6360   8559   5823  -2173    685  -1893       C  
ATOM   3173  CG  PRO A 470      -2.858 -21.840 -18.600  1.00 55.53           C  
ANISOU 3173  CG  PRO A 470     6435   8776   5885  -2263    583  -1986       C  
ATOM   3174  CD  PRO A 470      -2.189 -21.259 -19.800  1.00 56.44           C  
ANISOU 3174  CD  PRO A 470     6375   8942   6127  -2324    528  -2018       C  
ATOM   3175  N   TRP A 471      -0.100 -19.103 -18.165  1.00 55.79           N  
ANISOU 3175  N   TRP A 471     6236   8762   6200  -2104    617  -1786       N  
ATOM   3176  CA  TRP A 471       1.157 -18.567 -17.625  1.00 55.56           C  
ANISOU 3176  CA  TRP A 471     6176   8713   6219  -2018    594  -1690       C  
ATOM   3177  C   TRP A 471       1.731 -17.536 -18.574  1.00 57.46           C  
ANISOU 3177  C   TRP A 471     6320   8930   6583  -2055    663  -1773       C  
ATOM   3178  O   TRP A 471       2.917 -17.259 -18.564  1.00 57.26           O  
ANISOU 3178  O   TRP A 471     6237   8891   6629  -1978    636  -1746       O  
ATOM   3179  CB  TRP A 471       2.151 -19.708 -17.384  1.00 55.03           C  
ANISOU 3179  CB  TRP A 471     6056   8727   6127  -1926    436  -1613       C  
ATOM   3180  CG  TRP A 471       1.549 -20.740 -16.518  1.00 54.43           C  
ANISOU 3180  CG  TRP A 471     6080   8694   5905  -1923    412  -1558       C  
ATOM   3181  CD1 TRP A 471       1.003 -21.941 -16.905  1.00 55.63           C  
ANISOU 3181  CD1 TRP A 471     6250   8923   5964  -1971    353  -1616       C  
ATOM   3182  CD2 TRP A 471       1.336 -20.638 -15.104  1.00 53.36           C  
ANISOU 3182  CD2 TRP A 471     6045   8530   5698  -1884    471  -1449       C  
ATOM   3183  CE2 TRP A 471       0.683 -21.826 -14.692  1.00 53.75           C  
ANISOU 3183  CE2 TRP A 471     6153   8647   5621  -1894    478  -1463       C  
ATOM   3184  CE3 TRP A 471       1.634 -19.657 -14.138  1.00 50.67           C  
ANISOU 3184  CE3 TRP A 471     5746   8118   5387  -1857    517  -1340       C  
ATOM   3185  NE1 TRP A 471       0.493 -22.603 -15.806  1.00 54.54           N  
ANISOU 3185  NE1 TRP A 471     6230   8803   5691  -1957    404  -1568       N  
ATOM   3186  CZ2 TRP A 471       0.338 -22.055 -13.360  1.00 53.52           C  
ANISOU 3186  CZ2 TRP A 471     6185   8625   5525  -1854    556  -1382       C  
ATOM   3187  CZ3 TRP A 471       1.291 -19.889 -12.817  1.00 49.30           C  
ANISOU 3187  CZ3 TRP A 471     5623   7956   5154  -1827    552  -1234       C  
ATOM   3188  CH2 TRP A 471       0.651 -21.069 -12.439  1.00 50.84           C  
ANISOU 3188  CH2 TRP A 471     5838   8227   5253  -1814    586  -1261       C  
ATOM   3189  N   GLY A 472       0.863 -16.966 -19.396  1.00 62.90           N  
ANISOU 3189  N   GLY A 472     7002   9605   7291  -2183    767  -1883       N  
ATOM   3190  CA  GLY A 472       1.245 -15.904 -20.312  1.00 65.53           C  
ANISOU 3190  CA  GLY A 472     7248   9928   7723  -2258    890  -1985       C  
ATOM   3191  C   GLY A 472       1.879 -16.397 -21.591  1.00 67.80           C  
ANISOU 3191  C   GLY A 472     7278  10322   8159  -2229    848  -2088       C  
ATOM   3192  O   GLY A 472       1.978 -17.600 -21.851  1.00 67.23           O  
ANISOU 3192  O   GLY A 472     7108  10330   8105  -2173    685  -2069       O  
ATOM   3193  N   GLU A 473       2.325 -15.437 -22.385  1.00 69.33           N  
ANISOU 3193  N   GLU A 473     7360  10516   8465  -2276    995  -2196       N  
ATOM   3194  CA  GLU A 473       2.758 -15.727 -23.722  1.00 71.83           C  
ANISOU 3194  CA  GLU A 473     7383  10941   8968  -2266    990  -2312       C  
ATOM   3195  C   GLU A 473       4.101 -16.415 -23.750  1.00 71.72           C  
ANISOU 3195  C   GLU A 473     7204  10940   9107  -2050    835  -2268       C  
ATOM   3196  O   GLU A 473       4.952 -16.202 -22.882  1.00 68.19           O  
ANISOU 3196  O   GLU A 473     6870  10398   8641  -1925    815  -2190       O  
ATOM   3197  CB  GLU A 473       2.810 -14.451 -24.550  1.00 75.64           C  
ANISOU 3197  CB  GLU A 473     7784  11428   9530  -2389   1243  -2461       C  
ATOM   3198  CG  GLU A 473       4.016 -13.561 -24.281  1.00 78.10           C  
ANISOU 3198  CG  GLU A 473     8107  11654   9913  -2281   1376  -2496       C  
ATOM   3199  CD  GLU A 473       3.984 -12.301 -25.118  1.00 81.04           C  
ANISOU 3199  CD  GLU A 473     8423  12041  10327  -2440   1670  -2668       C  
ATOM   3200  OE1 GLU A 473       3.448 -12.360 -26.252  1.00 83.99           O  
ANISOU 3200  OE1 GLU A 473     8589  12536  10787  -2567   1743  -2777       O  
ATOM   3201  OE2 GLU A 473       4.521 -11.266 -24.671  1.00 82.40           O1-
ANISOU 3201  OE2 GLU A 473     8759  12109  10438  -2458   1833  -2698       O1-
ATOM   3202  N   ASP A 474       4.258 -17.229 -24.793  1.00 75.86           N  
ANISOU 3202  N   ASP A 474     7463  11575   9787  -2026    704  -2309       N  
ATOM   3203  CA  ASP A 474       5.481 -17.964 -25.080  1.00 78.55           C  
ANISOU 3203  CA  ASP A 474     7601  11926  10319  -1829    509  -2262       C  
ATOM   3204  C   ASP A 474       5.902 -18.722 -23.837  1.00 74.99           C  
ANISOU 3204  C   ASP A 474     7370  11405   9719  -1724    320  -2089       C  
ATOM   3205  O   ASP A 474       7.087 -18.922 -23.589  1.00 75.33           O  
ANISOU 3205  O   ASP A 474     7376  11377   9868  -1555    206  -2023       O  
ATOM   3206  CB  ASP A 474       6.586 -17.008 -25.566  1.00 82.01           C  
ANISOU 3206  CB  ASP A 474     7865  12303  10993  -1700    675  -2374       C  
ATOM   3207  CG  ASP A 474       6.185 -16.228 -26.834  1.00 85.83           C  
ANISOU 3207  CG  ASP A 474     8103  12882  11625  -1826    909  -2562       C  
ATOM   3208  OD1 ASP A 474       5.558 -16.830 -27.749  1.00 84.43           O  
ANISOU 3208  OD1 ASP A 474     7723  12844  11514  -1933    816  -2589       O  
ATOM   3209  OD2 ASP A 474       6.513 -15.010 -26.906  1.00 86.97           O1-
ANISOU 3209  OD2 ASP A 474     8272  12966  11807  -1841   1189  -2686       O1-
ATOM   3210  N   ALA A 475       4.909 -19.137 -23.059  1.00 70.97           N  
ANISOU 3210  N   ALA A 475     7088  10909   8969  -1834    299  -2020       N  
ATOM   3211  CA  ALA A 475       5.168 -19.800 -21.809  1.00 68.24           C  
ANISOU 3211  CA  ALA A 475     6947  10521   8459  -1771    172  -1865       C  
ATOM   3212  C   ALA A 475       5.739 -21.178 -22.094  1.00 69.86           C  
ANISOU 3212  C   ALA A 475     7062  10788   8692  -1714   -114  -1778       C  
ATOM   3213  O   ALA A 475       5.390 -21.819 -23.084  1.00 71.00           O  
ANISOU 3213  O   ALA A 475     7053  11028   8897  -1782   -227  -1822       O  
ATOM   3214  CB  ALA A 475       3.896 -19.903 -20.994  1.00 66.24           C  
ANISOU 3214  CB  ALA A 475     6917  10270   7980  -1889    251  -1841       C  
ATOM   3215  N   ARG A 476       6.650 -21.604 -21.231  1.00 70.50           N  
ANISOU 3215  N   ARG A 476     7252  10812   8724  -1613   -247  -1639       N  
ATOM   3216  CA  ARG A 476       7.214 -22.934 -21.281  1.00 73.37           C  
ANISOU 3216  CA  ARG A 476     7604  11215   9058  -1588   -541  -1517       C  
ATOM   3217  C   ARG A 476       7.387 -23.448 -19.842  1.00 68.63           C  
ANISOU 3217  C   ARG A 476     7267  10591   8220  -1603   -587  -1366       C  
ATOM   3218  O   ARG A 476       7.653 -22.694 -18.908  1.00 66.85           O  
ANISOU 3218  O   ARG A 476     7160  10285   7954  -1563   -456  -1329       O  
ATOM   3219  CB  ARG A 476       8.548 -22.950 -22.102  1.00 80.35           C  
ANISOU 3219  CB  ARG A 476     8262  12036  10230  -1424   -717  -1499       C  
ATOM   3220  CG  ARG A 476       9.701 -22.083 -21.574  1.00 85.03           C  
ANISOU 3220  CG  ARG A 476     8899  12466  10942  -1262   -645  -1477       C  
ATOM   3221  CD  ARG A 476      11.097 -22.446 -22.116  1.00 91.78           C  
ANISOU 3221  CD  ARG A 476     9598  13217  12055  -1075   -887  -1417       C  
ATOM   3222  NE  ARG A 476      11.511 -23.870 -22.010  1.00 97.78           N  
ANISOU 3222  NE  ARG A 476    10411  13999  12742  -1092  -1254  -1231       N  
ATOM   3223  CZ  ARG A 476      12.232 -24.435 -21.019  1.00 97.60           C  
ANISOU 3223  CZ  ARG A 476    10621  13892  12568  -1085  -1429  -1051       C  
ATOM   3224  NH1 ARG A 476      12.653 -23.737 -19.957  1.00 94.96           N1+
ANISOU 3224  NH1 ARG A 476    10489  13447  12143  -1056  -1286  -1019       N1+
ATOM   3225  NH2 ARG A 476      12.534 -25.735 -21.086  1.00 95.78           N  
ANISOU 3225  NH2 ARG A 476    10439  13694  12259  -1140  -1769   -888       N  
ATOM   3226  N   ASN A 477       7.205 -24.743 -19.679  1.00 67.89           N  
ANISOU 3226  N   ASN A 477     7262  10577   7953  -1692   -771  -1280       N  
ATOM   3227  CA  ASN A 477       7.450 -25.398 -18.420  1.00 66.80           C  
ANISOU 3227  CA  ASN A 477     7346  10446   7589  -1731   -824  -1135       C  
ATOM   3228  C   ASN A 477       8.879 -25.139 -17.960  1.00 65.74           C  
ANISOU 3228  C   ASN A 477     7235  10193   7549  -1611   -944  -1007       C  
ATOM   3229  O   ASN A 477       9.830 -25.623 -18.581  1.00 68.28           O  
ANISOU 3229  O   ASN A 477     7473  10467   8002  -1543  -1197   -938       O  
ATOM   3230  CB  ASN A 477       7.222 -26.901 -18.587  1.00 69.60           C  
ANISOU 3230  CB  ASN A 477     7788  10905   7752  -1867  -1035  -1071       C  
ATOM   3231  CG  ASN A 477       7.509 -27.684 -17.325  1.00 70.41           C  
ANISOU 3231  CG  ASN A 477     8122  11036   7594  -1942  -1078   -925       C  
ATOM   3232  ND2 ASN A 477       7.213 -28.967 -17.360  1.00 72.08           N  
ANISOU 3232  ND2 ASN A 477     8461  11345   7582  -2099  -1215   -884       N  
ATOM   3233  OD1 ASN A 477       7.989 -27.144 -16.332  1.00 70.88           O  
ANISOU 3233  OD1 ASN A 477     8252  11036   7641  -1886   -985   -850       O  
ATOM   3234  N   PRO A 478       9.041 -24.392 -16.857  1.00 61.89           N  
ANISOU 3234  N   PRO A 478     6871   9644   7000  -1590   -787   -964       N  
ATOM   3235  CA  PRO A 478      10.388 -24.116 -16.373  1.00 60.95           C  
ANISOU 3235  CA  PRO A 478     6816   9392   6949  -1501   -901   -845       C  
ATOM   3236  C   PRO A 478      11.136 -25.316 -15.805  1.00 60.63           C  
ANISOU 3236  C   PRO A 478     6922   9361   6754  -1562  -1159   -651       C  
ATOM   3237  O   PRO A 478      12.326 -25.216 -15.596  1.00 61.93           O  
ANISOU 3237  O   PRO A 478     7144   9391   6997  -1487  -1308   -547       O  
ATOM   3238  CB  PRO A 478      10.176 -23.048 -15.298  1.00 59.21           C  
ANISOU 3238  CB  PRO A 478     6706   9126   6664  -1521   -674   -840       C  
ATOM   3239  CG  PRO A 478       8.753 -23.166 -14.905  1.00 58.36           C  
ANISOU 3239  CG  PRO A 478     6623   9146   6405  -1626   -496   -895       C  
ATOM   3240  CD  PRO A 478       8.021 -23.628 -16.125  1.00 59.61           C  
ANISOU 3240  CD  PRO A 478     6651   9380   6620  -1643   -516  -1026       C  
ATOM   3241  N   PHE A 479      10.479 -26.445 -15.590  1.00 61.39           N  
ANISOU 3241  N   PHE A 479     7100   9600   6624  -1708  -1213   -610       N  
ATOM   3242  CA  PHE A 479      11.142 -27.610 -14.987  1.00 63.62           C  
ANISOU 3242  CA  PHE A 479     7561   9907   6704  -1818  -1441   -420       C  
ATOM   3243  C   PHE A 479      11.645 -28.651 -15.996  1.00 66.33           C  
ANISOU 3243  C   PHE A 479     7870  10245   7088  -1837  -1782   -353       C  
ATOM   3244  O   PHE A 479      11.828 -29.815 -15.640  1.00 66.85           O  
ANISOU 3244  O   PHE A 479     8108  10374   6917  -1997  -1967   -216       O  
ATOM   3245  CB  PHE A 479      10.191 -28.269 -13.979  1.00 63.81           C  
ANISOU 3245  CB  PHE A 479     7735  10096   6415  -1998  -1274   -407       C  
ATOM   3246  CG  PHE A 479       9.758 -27.350 -12.856  1.00 62.11           C  
ANISOU 3246  CG  PHE A 479     7538   9888   6173  -1983   -989   -427       C  
ATOM   3247  CD1 PHE A 479       8.667 -26.518 -13.005  1.00 61.54           C  
ANISOU 3247  CD1 PHE A 479     7362   9832   6189  -1930   -738   -587       C  
ATOM   3248  CD2 PHE A 479      10.444 -27.321 -11.651  1.00 62.58           C  
ANISOU 3248  CD2 PHE A 479     7722   9933   6124  -2042   -999   -267       C  
ATOM   3249  CE1 PHE A 479       8.275 -25.674 -11.972  1.00 60.59           C  
ANISOU 3249  CE1 PHE A 479     7254   9707   6062  -1921   -524   -578       C  
ATOM   3250  CE2 PHE A 479      10.051 -26.486 -10.614  1.00 61.83           C  
ANISOU 3250  CE2 PHE A 479     7619   9852   6021  -2043   -772   -262       C  
ATOM   3251  CZ  PHE A 479       8.969 -25.657 -10.777  1.00 59.77           C  
ANISOU 3251  CZ  PHE A 479     7246   9601   5863  -1974   -546   -413       C  
ATOM   3252  N   LEU A 480      11.863 -28.229 -17.244  1.00 68.55           N  
ANISOU 3252  N   LEU A 480     7923  10454   7668  -1690  -1870   -444       N  
ATOM   3253  CA  LEU A 480      12.371 -29.104 -18.312  1.00 71.39           C  
ANISOU 3253  CA  LEU A 480     8185  10794   8143  -1681  -2228   -371       C  
ATOM   3254  C   LEU A 480      13.629 -28.522 -18.965  1.00 73.45           C  
ANISOU 3254  C   LEU A 480     8274  10855   8778  -1443  -2397   -344       C  
ATOM   3255  O   LEU A 480      14.572 -29.223 -19.357  1.00 74.99           O  
ANISOU 3255  O   LEU A 480     8466  10952   9073  -1400  -2761   -190       O  
ATOM   3256  CB  LEU A 480      11.287 -29.287 -19.368  1.00 71.64           C  
ANISOU 3256  CB  LEU A 480     8045  10960   8214  -1744  -2183   -521       C  
ATOM   3257  CG  LEU A 480      10.019 -29.996 -18.893  1.00 71.47           C  
ANISOU 3257  CG  LEU A 480     8208  11109   7839  -1975  -2039   -570       C  
ATOM   3258  CD1 LEU A 480       8.897 -29.931 -19.923  1.00 71.58           C  
ANISOU 3258  CD1 LEU A 480     8068  11217   7912  -2033  -1953   -743       C  
ATOM   3259  CD2 LEU A 480      10.319 -31.448 -18.552  1.00 73.74           C  
ANISOU 3259  CD2 LEU A 480     8731  11454   7834  -2174  -2320   -394       C  
ATOM   3260  OXT LEU A 480      13.725 -27.303 -19.134  1.00 74.14           O1-
ANISOU 3260  OXT LEU A 480     8225  10861   9085  -1282  -2165   -484       O1-
TER



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