CNRS Nantes University UFIP UFIP
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***  Lm_USP_3OGZ_open  ***

elNémo ID: 181218113417124560

Job options:

ID        	=	 181218113417124560
JOBID     	=	 Lm_USP_3OGZ_open
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 10
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER Lm_USP_3OGZ_open
ATOM      1  N   ASN A   3      -1.242  20.689  58.464  1.00115.87           N  
ANISOU    1  N   ASN A   3    15325  13759  14942  -3028   2036  -1306       N  
ATOM      2  CA  ASN A   3       0.002  20.136  58.993  1.00114.42           C  
ANISOU    2  CA  ASN A   3    15282  13604  14590  -3001   1972  -1234       C  
ATOM      3  C   ASN A   3       0.994  21.214  59.444  0.86108.13           C  
ANISOU    3  C   ASN A   3    14452  12870  13761  -2966   1969  -1252       C  
ATOM      4  O   ASN A   3       1.441  21.206  60.591  0.84109.52           O  
ANISOU    4  O   ASN A   3    14710  13088  13815  -3029   2005  -1256       O  
ATOM      5  CB  ASN A   3       0.644  19.181  57.978  1.00116.51           C  
ANISOU    5  CB  ASN A   3    15612  13836  14823  -2895   1844  -1141       C  
ATOM      6  CG  ASN A   3       1.977  18.627  58.452  0.83118.78           C  
ANISOU    6  CG  ASN A   3    16032  14149  14950  -2852   1769  -1063       C  
ATOM      7  ND2 ASN A   3       2.737  18.048  57.529  1.00118.16           N  
ANISOU    7  ND2 ASN A   3    15989  14050  14855  -2740   1657   -991       N  
ATOM      8  OD1 ASN A   3       2.317  18.713  59.632  0.88120.49           O  
ANISOU    8  OD1 ASN A   3    16316  14404  15060  -2918   1812  -1069       O  
ATOM      9  N   PRO A   4       1.344  22.148  58.544  1.00 97.79           N  
ANISOU    9  N   PRO A   4    13025  11571  12558  -2868   1926  -1262       N  
ATOM     10  CA  PRO A   4       2.275  23.213  58.927  1.00 89.15           C  
ANISOU   10  CA  PRO A   4    11894  10535  11446  -2837   1926  -1284       C  
ATOM     11  C   PRO A   4       1.588  24.272  59.783  1.00 83.23           C  
ANISOU   11  C   PRO A   4    11061   9805  10758  -2934   2056  -1390       C  
ATOM     12  O   PRO A   4       0.465  24.673  59.478  1.00 80.82           O  
ANISOU   12  O   PRO A   4    10652   9466  10590  -2967   2124  -1450       O  
ATOM     13  CB  PRO A   4       2.686  23.822  57.580  1.00 89.21           C  
ANISOU   13  CB  PRO A   4    11796  10533  11565  -2709   1846  -1260       C  
ATOM     14  CG  PRO A   4       2.196  22.862  56.530  1.00 91.72           C  
ANISOU   14  CG  PRO A   4    12130  10798  11922  -2665   1784  -1210       C  
ATOM     15  CD  PRO A   4       0.989  22.225  57.119  0.67 94.60           C  
ANISOU   15  CD  PRO A   4    12528  11130  12287  -2781   1867  -1246       C  
ATOM     16  N   SER A   5       2.259  24.718  60.840  1.00 80.90           N  
ANISOU   16  N   SER A   5    10809   9566  10364  -2980   2090  -1416       N  
ATOM     17  CA  SER A   5       1.714  25.747  61.720  1.00 79.46           C  
ANISOU   17  CA  SER A   5    10556   9406  10229  -3074   2218  -1525       C  
ATOM     18  C   SER A   5       1.665  27.097  61.017  1.00 79.43           C  
ANISOU   18  C   SER A   5    10390   9395  10395  -3010   2232  -1578       C  
ATOM     19  O   SER A   5       2.313  27.293  59.988  1.00 76.73           O  
ANISOU   19  O   SER A   5    10007   9047  10101  -2893   2136  -1523       O  
ATOM     20  CB  SER A   5       2.551  25.858  62.994  1.00 78.73           C  
ANISOU   20  CB  SER A   5    10558   9382   9973  -3137   2239  -1536       C  
ATOM     21  OG  SER A   5       3.879  26.250  62.697  1.00 75.76           O  
ANISOU   21  OG  SER A   5    10183   9045   9557  -3041   2144  -1492       O  
ATOM     22  N   ASN A   6       0.899  28.027  61.576  1.00 82.73           N  
ANISOU   22  N   ASN A   6    10717   9812  10905  -3087   2356  -1683       N  
ATOM     23  CA  ASN A   6       0.773  29.357  60.992  1.00 84.36           C  
ANISOU   23  CA  ASN A   6    10767  10002  11284  -3033   2381  -1738       C  
ATOM     24  C   ASN A   6       2.089  30.123  60.999  1.00 80.94           C  
ANISOU   24  C   ASN A   6    10328   9614  10812  -2969   2328  -1725       C  
ATOM     25  O   ASN A   6       2.423  30.802  60.029  1.00 76.93           O  
ANISOU   25  O   ASN A   6     9729   9089  10414  -2869   2275  -1704       O  
ATOM     26  CB  ASN A   6      -0.316  30.166  61.699  1.00 91.83           C  
ANISOU   26  CB  ASN A   6    11621  10934  12336  -3135   2534  -1860       C  
ATOM     27  CG  ASN A   6      -1.713  29.730  61.302  1.00 98.64           C  
ANISOU   27  CG  ASN A   6    12428  11742  13311  -3169   2580  -1880       C  
ATOM     28  ND2 ASN A   6      -2.665  29.885  62.216  1.00100.60           N  
ANISOU   28  ND2 ASN A   6    12655  11986  13583  -3289   2717  -1974       N  
ATOM     29  OD1 ASN A   6      -1.934  29.260  60.186  1.00102.27           O  
ANISOU   29  OD1 ASN A   6    12860  12164  13833  -3090   2496  -1814       O  
ATOM     30  N   SER A   7       2.836  30.007  62.092  1.00 80.47           N  
ANISOU   30  N   SER A   7    10368   9613  10594  -3028   2341  -1735       N  
ATOM     31  CA  SER A   7       4.114  30.698  62.213  1.00 80.39           C  
ANISOU   31  CA  SER A   7    10356   9653  10536  -2979   2292  -1728       C  
ATOM     32  C   SER A   7       5.118  30.164  61.195  1.00 76.86           C  
ANISOU   32  C   SER A   7     9943   9207  10051  -2850   2144  -1614       C  
ATOM     33  O   SER A   7       5.965  30.906  60.701  1.00 77.45           O  
ANISOU   33  O   SER A   7     9962   9298  10168  -2772   2095  -1603       O  
ATOM     34  CB  SER A   7       4.673  30.570  63.632  1.00 81.95           C  
ANISOU   34  CB  SER A   7    10661   9920  10557  -3077   2329  -1759       C  
ATOM     35  OG  SER A   7       4.997  29.225  63.934  1.00 84.70           O  
ANISOU   35  OG  SER A   7    11156  10286  10738  -3089   2261  -1673       O  
ATOM     36  N   ASN A   8       5.017  28.876  60.884  1.00 74.67           N  
ANISOU   36  N   ASN A   8     9760   8912   9699  -2830   2078  -1534       N  
ATOM     37  CA  ASN A   8       5.886  28.265  59.883  1.00 72.75           C  
ANISOU   37  CA  ASN A   8     9553   8665   9425  -2709   1943  -1430       C  
ATOM     38  C   ASN A   8       5.634  28.828  58.490  1.00 68.27           C  
ANISOU   38  C   ASN A   8     8862   8053   9025  -2611   1909  -1417       C  
ATOM     39  O   ASN A   8       6.571  29.203  57.784  1.00 65.36           O  
ANISOU   39  O   ASN A   8     8463   7699   8673  -2515   1833  -1375       O  
ATOM     40  CB  ASN A   8       5.719  26.745  59.880  1.00 74.97           C  
ANISOU   40  CB  ASN A   8     9961   8925   9600  -2718   1892  -1354       C  
ATOM     41  CG  ASN A   8       6.395  26.083  61.062  1.00 75.79           C  
ANISOU   41  CG  ASN A   8    10204   9079   9514  -2778   1880  -1328       C  
ATOM     42  ND2 ASN A   8       6.351  24.758  61.102  1.00 78.06           N  
ANISOU   42  ND2 ASN A   8    10610   9345   9706  -2782   1831  -1255       N  
ATOM     43  OD1 ASN A   8       6.947  26.754  61.932  1.00 74.88           O  
ANISOU   43  OD1 ASN A   8    10091   9020   9339  -2821   1913  -1372       O  
ATOM     44  N   LEU A   9       4.363  28.882  58.100  1.00 66.16           N  
ANISOU   44  N   LEU A   9     8524   7733   8880  -2639   1965  -1452       N  
ATOM     45  CA  LEU A   9       3.976  29.468  56.821  1.00 63.21           C  
ANISOU   45  CA  LEU A   9     8027   7318   8671  -2556   1937  -1442       C  
ATOM     46  C   LEU A   9       4.387  30.933  56.766  1.00 63.74           C  
ANISOU   46  C   LEU A   9     7985   7398   8837  -2528   1970  -1491       C  
ATOM     47  O   LEU A   9       4.807  31.436  55.726  1.00 60.88           O  
ANISOU   47  O   LEU A   9     7553   7024   8553  -2431   1908  -1452       O  
ATOM     48  CB  LEU A   9       2.467  29.343  56.607  1.00 60.74           C  
ANISOU   48  CB  LEU A   9     7650   6954   8476  -2607   2002  -1484       C  
ATOM     49  CG  LEU A   9       1.917  28.017  56.068  1.00 59.10           C  
ANISOU   49  CG  LEU A   9     7508   6713   8233  -2603   1950  -1426       C  
ATOM     50  CD1 LEU A   9       2.947  26.895  56.146  1.00 53.99           C  
ANISOU   50  CD1 LEU A   9     7009   6091   7415  -2568   1858  -1342       C  
ATOM     51  CD2 LEU A   9       0.646  27.647  56.803  1.00 59.62           C  
ANISOU   51  CD2 LEU A   9     7579   6756   8319  -2720   2052  -1488       C  
ATOM     52  N   GLN A  10       4.258  31.615  57.898  1.00 65.81           N  
ANISOU   52  N   GLN A  10     8232   7682   9091  -2618   2071  -1578       N  
ATOM     53  CA  GLN A  10       4.647  33.012  57.988  1.00 63.23           C  
ANISOU   53  CA  GLN A  10     7807   7363   8854  -2604   2114  -1636       C  
ATOM     54  C   GLN A  10       6.159  33.151  57.861  1.00 57.42           C  
ANISOU   54  C   GLN A  10     7114   6678   8027  -2536   2028  -1584       C  
ATOM     55  O   GLN A  10       6.653  34.046  57.179  1.00 54.24           O  
ANISOU   55  O   GLN A  10     6627   6266   7715  -2465   2003  -1577       O  
ATOM     56  CB  GLN A  10       4.166  33.618  59.307  1.00 69.33           C  
ANISOU   56  CB  GLN A  10     8566   8151   9625  -2726   2248  -1749       C  
ATOM     57  CG  GLN A  10       4.438  35.106  59.430  1.00 71.45           C  
ANISOU   57  CG  GLN A  10     8726   8416  10005  -2722   2307  -1823       C  
ATOM     58  CD  GLN A  10       3.728  35.913  58.360  1.00 74.84           C  
ANISOU   58  CD  GLN A  10     9011   8778  10648  -2656   2318  -1828       C  
ATOM     59  NE2 GLN A  10       2.583  35.413  57.901  1.00 75.55           N  
ANISOU   59  NE2 GLN A  10     9069   8822  10815  -2661   2330  -1818       N  
ATOM     60  OE1 GLN A  10       4.201  36.974  57.952  1.00 74.26           O  
ANISOU   60  OE1 GLN A  10     8854   8693  10671  -2603   2316  -1839       O  
ATOM     61  N   ALA A  11       6.889  32.253  58.517  1.00 56.36           N  
ANISOU   61  N   ALA A  11     7109   6592   7713  -2559   1982  -1546       N  
ATOM     62  CA  ALA A  11       8.346  32.266  58.479  1.00 56.18           C  
ANISOU   62  CA  ALA A  11     7131   6622   7593  -2498   1896  -1496       C  
ATOM     63  C   ALA A  11       8.854  32.016  57.064  1.00 57.43           C  
ANISOU   63  C   ALA A  11     7265   6759   7795  -2369   1788  -1405       C  
ATOM     64  O   ALA A  11       9.820  32.639  56.617  1.00 55.59           O  
ANISOU   64  O   ALA A  11     6992   6548   7582  -2300   1742  -1386       O  
ATOM     65  CB  ALA A  11       8.907  31.227  59.432  1.00 55.49           C  
ANISOU   65  CB  ALA A  11     7189   6586   7310  -2545   1862  -1463       C  
ATOM     66  N   LEU A  12       8.196  31.101  56.362  1.00 55.20           N  
ANISOU   66  N   LEU A  12     7010   6436   7528  -2341   1750  -1354       N  
ATOM     67  CA  LEU A  12       8.575  30.787  54.992  1.00 55.52           C  
ANISOU   67  CA  LEU A  12     7033   6457   7605  -2225   1652  -1273       C  
ATOM     68  C   LEU A  12       8.263  31.955  54.066  1.00 53.01           C  
ANISOU   68  C   LEU A  12     6576   6107   7460  -2174   1669  -1291       C  
ATOM     69  O   LEU A  12       9.080  32.319  53.223  1.00 53.50           O  
ANISOU   69  O   LEU A  12     6604   6179   7546  -2085   1605  -1245       O  
ATOM     70  CB  LEU A  12       7.876  29.515  54.509  1.00 52.36           C  
ANISOU   70  CB  LEU A  12     6696   6020   7178  -2219   1613  -1223       C  
ATOM     71  CG  LEU A  12       8.134  29.099  53.057  1.00 52.62           C  
ANISOU   71  CG  LEU A  12     6717   6031   7246  -2108   1516  -1146       C  
ATOM     72  CD1 LEU A  12       9.625  28.962  52.771  1.00 50.24           C  
ANISOU   72  CD1 LEU A  12     6459   5771   6858  -2025   1429  -1087       C  
ATOM     73  CD2 LEU A  12       7.401  27.803  52.739  1.00 53.75           C  
ANISOU   73  CD2 LEU A  12     6931   6137   7355  -2120   1487  -1110       C  
ATOM     74  N   ARG A  13       7.083  32.544  54.231  1.00 53.00           N  
ANISOU   74  N   ARG A  13     6493   6066   7579  -2231   1758  -1357       N  
ATOM     75  CA  ARG A  13       6.689  33.687  53.418  1.00 54.51           C  
ANISOU   75  CA  ARG A  13     6548   6218   7944  -2187   1779  -1374       C  
ATOM     76  C   ARG A  13       7.711  34.814  53.523  1.00 51.49           C  
ANISOU   76  C   ARG A  13     6117   5863   7585  -2158   1786  -1392       C  
ATOM     77  O   ARG A  13       8.101  35.407  52.518  1.00 50.57           O  
ANISOU   77  O   ARG A  13     5934   5732   7549  -2075   1741  -1351       O  
ATOM     78  CB  ARG A  13       5.315  34.202  53.832  1.00 54.71           C  
ANISOU   78  CB  ARG A  13     6493   6201   8095  -2263   1886  -1455       C  
ATOM     79  CG  ARG A  13       4.932  35.509  53.163  1.00 56.60           C  
ANISOU   79  CG  ARG A  13     6586   6396   8521  -2222   1918  -1479       C  
ATOM     80  CD  ARG A  13       3.609  36.020  53.703  1.00 60.10           C  
ANISOU   80  CD  ARG A  13     6948   6797   9090  -2301   2032  -1568       C  
ATOM     81  NE  ARG A  13       3.277  37.346  53.195  1.00 61.92           N  
ANISOU   81  NE  ARG A  13     7038   6981   9508  -2264   2069  -1595       N  
ATOM     82  CZ  ARG A  13       2.174  38.009  53.524  1.00 64.10           C  
ANISOU   82  CZ  ARG A  13     7216   7211   9929  -2315   2168  -1673       C  
ATOM     83  NH1 ARG A  13       1.298  37.464  54.358  1.00 64.38           N1+
ANISOU   83  NH1 ARG A  13     7278   7245   9938  -2408   2242  -1735       N1+
ATOM     84  NH2 ARG A  13       1.944  39.214  53.019  1.00 62.75           N  
ANISOU   84  NH2 ARG A  13     6919   6992   9932  -2272   2195  -1689       N  
ATOM     85  N   GLU A  14       8.143  35.108  54.744  1.00 51.91           N  
ANISOU   85  N   GLU A  14     6206   5955   7564  -2231   1843  -1454       N  
ATOM     86  CA  GLU A  14       9.127  36.160  54.955  1.00 58.46           C  
ANISOU   86  CA  GLU A  14     6992   6811   8408  -2216   1854  -1482       C  
ATOM     87  C   GLU A  14      10.465  35.755  54.350  1.00 54.08           C  
ANISOU   87  C   GLU A  14     6488   6299   7762  -2128   1743  -1397       C  
ATOM     88  O   GLU A  14      11.156  36.575  53.749  1.00 47.78           O  
ANISOU   88  O   GLU A  14     5625   5502   7027  -2068   1720  -1381       O  
ATOM     89  CB  GLU A  14       9.265  36.486  56.446  1.00 65.99           C  
ANISOU   89  CB  GLU A  14     7979   7805   9290  -2324   1938  -1572       C  
ATOM     90  CG  GLU A  14       7.950  36.913  57.094  1.00 73.20           C  
ANISOU   90  CG  GLU A  14     8839   8677  10295  -2416   2061  -1667       C  
ATOM     91  CD  GLU A  14       8.105  37.324  58.546  1.00 82.89           C  
ANISOU   91  CD  GLU A  14    10096   9946  11451  -2527   2151  -1765       C  
ATOM     92  OE1 GLU A  14       7.319  36.839  59.388  1.00 86.03           O  
ANISOU   92  OE1 GLU A  14    10541  10347  11799  -2619   2218  -1813       O  
ATOM     93  OE2 GLU A  14       9.004  38.141  58.843  1.00 87.27           O1-
ANISOU   93  OE2 GLU A  14    10628  10532  11998  -2526   2157  -1797       O1-
ATOM     94  N   GLU A  15      10.824  34.484  54.493  1.00 51.55           N  
ANISOU   94  N   GLU A  15     6281   6009   7297  -2119   1675  -1342       N  
ATOM     95  CA  GLU A  15      12.079  34.002  53.925  1.00 50.11           C  
ANISOU   95  CA  GLU A  15     6147   5864   7029  -2032   1571  -1263       C  
ATOM     96  C   GLU A  15      12.109  34.205  52.413  1.00 44.84           C  
ANISOU   96  C   GLU A  15     5415   5162   6460  -1930   1515  -1201       C  
ATOM     97  O   GLU A  15      13.099  34.678  51.849  1.00 41.68           O  
ANISOU   97  O   GLU A  15     4983   4784   6071  -1863   1471  -1170       O  
ATOM     98  CB  GLU A  15      12.290  32.524  54.250  1.00 48.26           C  
ANISOU   98  CB  GLU A  15     6044   5653   6641  -2036   1510  -1210       C  
ATOM     99  CG  GLU A  15      13.514  31.924  53.579  1.00 44.48           C  
ANISOU   99  CG  GLU A  15     5612   5204   6085  -1938   1401  -1128       C  
ATOM    100  CD  GLU A  15      13.718  30.467  53.929  1.00 51.58           C  
ANISOU  100  CD  GLU A  15     6640   6116   6841  -1939   1343  -1076       C  
ATOM    101  OE1 GLU A  15      12.745  29.820  54.366  1.00 52.16           O  
ANISOU  101  OE1 GLU A  15     6763   6161   6894  -2003   1379  -1089       O  
ATOM    102  OE2 GLU A  15      14.854  29.969  53.767  1.00 57.59           O1-
ANISOU  102  OE2 GLU A  15     7452   6913   7518  -1875   1263  -1021       O1-
ATOM    103  N   LEU A  16      11.012  33.841  51.760  1.00 44.43           N  
ANISOU  103  N   LEU A  16     5343   5060   6479  -1923   1517  -1185       N  
ATOM    104  CA  LEU A  16      10.940  33.897  50.308  1.00 43.36           C  
ANISOU  104  CA  LEU A  16     5157   4896   6423  -1832   1458  -1121       C  
ATOM    105  C   LEU A  16      10.966  35.329  49.762  1.00 47.50           C  
ANISOU  105  C   LEU A  16     5558   5398   7092  -1802   1490  -1138       C  
ATOM    106  O   LEU A  16      11.128  35.534  48.559  1.00 49.49           O  
ANISOU  106  O   LEU A  16     5767   5636   7402  -1723   1438  -1080       O  
ATOM    107  CB  LEU A  16       9.707  33.143  49.815  1.00 39.82           C  
ANISOU  107  CB  LEU A  16     4715   4403   6010  -1841   1451  -1105       C  
ATOM    108  CG  LEU A  16       9.778  31.630  50.056  1.00 41.71           C  
ANISOU  108  CG  LEU A  16     5082   4656   6111  -1851   1402  -1069       C  
ATOM    109  CD1 LEU A  16       8.493  30.945  49.616  1.00 39.98           C  
ANISOU  109  CD1 LEU A  16     4863   4390   5936  -1872   1405  -1064       C  
ATOM    110  CD2 LEU A  16      10.989  31.015  49.353  1.00 40.53           C  
ANISOU  110  CD2 LEU A  16     4992   4537   5872  -1760   1304   -994       C  
ATOM    111  N   CYS A  17      10.815  36.310  50.648  1.00 44.98           N  
ANISOU  111  N   CYS A  17     5186   5075   6830  -1867   1578  -1217       N  
ATOM    112  CA  CYS A  17      10.849  37.723  50.255  1.00 42.74           C  
ANISOU  112  CA  CYS A  17     4787   4761   6691  -1846   1618  -1239       C  
ATOM    113  C   CYS A  17      12.221  38.380  50.390  1.00 42.75           C  
ANISOU  113  C   CYS A  17     4781   4804   6657  -1821   1604  -1239       C  
ATOM    114  O   CYS A  17      12.390  39.550  50.031  1.00 45.34           O  
ANISOU  114  O   CYS A  17     5020   5107   7101  -1801   1635  -1251       O  
ATOM    115  CB  CYS A  17       9.830  38.537  51.056  1.00 40.84           C  
ANISOU  115  CB  CYS A  17     4476   4480   6560  -1929   1731  -1333       C  
ATOM    116  SG  CYS A  17       8.110  38.129  50.687  1.00 54.50           S  
ANISOU  116  SG  CYS A  17     6166   6150   8391  -1950   1758  -1338       S  
ATOM    117  N   THR A  18      13.191  37.639  50.912  1.00 39.91           N  
ANISOU  117  N   THR A  18     4514   4505   6144  -1823   1559  -1224       N  
ATOM    118  CA  THR A  18      14.530  38.178  51.141  1.00 40.09           C  
ANISOU  118  CA  THR A  18     4533   4577   6124  -1806   1542  -1228       C  
ATOM    119  C   THR A  18      15.352  38.253  49.851  1.00 39.53           C  
ANISOU  119  C   THR A  18     4438   4512   6071  -1703   1466  -1146       C  
ATOM    120  O   THR A  18      15.113  37.493  48.909  1.00 38.88           O  
ANISOU  120  O   THR A  18     4381   4415   5975  -1643   1404  -1078       O  
ATOM    121  CB  THR A  18      15.292  37.343  52.194  1.00 43.84           C  
ANISOU  121  CB  THR A  18     5111   5120   6427  -1845   1514  -1239       C  
ATOM    122  CG2 THR A  18      14.529  37.324  53.520  1.00 40.72           C  
ANISOU  122  CG2 THR A  18     4744   4726   6002  -1956   1595  -1322       C  
ATOM    123  OG1 THR A  18      15.435  35.999  51.724  1.00 45.34           O  
ANISOU  123  OG1 THR A  18     5387   5321   6517  -1793   1429  -1162       O  
ATOM    124  N   PRO A  19      16.320  39.182  49.799  1.00 41.38           N  
ANISOU  124  N   PRO A  19     4621   4766   6335  -1686   1473  -1157       N  
ATOM    125  CA  PRO A  19      17.190  39.317  48.628  1.00 40.42           C  
ANISOU  125  CA  PRO A  19     4476   4655   6227  -1594   1410  -1084       C  
ATOM    126  C   PRO A  19      17.828  37.983  48.260  1.00 44.01           C  
ANISOU  126  C   PRO A  19     5022   5153   6546  -1537   1317  -1017       C  
ATOM    127  O   PRO A  19      18.292  37.268  49.149  1.00 44.84           O  
ANISOU  127  O   PRO A  19     5202   5305   6531  -1566   1297  -1033       O  
ATOM    128  CB  PRO A  19      18.257  40.302  49.106  1.00 39.06           C  
ANISOU  128  CB  PRO A  19     4260   4515   6065  -1613   1438  -1125       C  
ATOM    129  CG  PRO A  19      17.539  41.153  50.103  1.00 41.42           C  
ANISOU  129  CG  PRO A  19     4514   4784   6439  -1704   1536  -1220       C  
ATOM    130  CD  PRO A  19      16.588  40.223  50.808  1.00 42.97           C  
ANISOU  130  CD  PRO A  19     4779   4978   6571  -1757   1550  -1244       C  
ATOM    131  N   GLY A  20      17.843  37.652  46.971  1.00 41.39           N  
ANISOU  131  N   GLY A  20     4685   4806   6234  -1458   1262   -943       N  
ATOM    132  CA  GLY A  20      18.386  36.383  46.524  1.00 39.78           C  
ANISOU  132  CA  GLY A  20     4564   4634   5915  -1400   1179   -883       C  
ATOM    133  C   GLY A  20      17.302  35.337  46.314  1.00 42.85           C  
ANISOU  133  C   GLY A  20     5011   4991   6281  -1406   1160   -862       C  
ATOM    134  O   GLY A  20      17.522  34.310  45.658  1.00 42.46           O  
ANISOU  134  O   GLY A  20     5021   4949   6162  -1351   1093   -808       O  
ATOM    135  N   LEU A  21      16.131  35.592  46.885  1.00 37.93           N  
ANISOU  135  N   LEU A  21     4366   4328   5717  -1475   1221   -911       N  
ATOM    136  CA  LEU A  21      14.975  34.726  46.682  1.00 38.56           C  
ANISOU  136  CA  LEU A  21     4483   4372   5795  -1490   1212   -900       C  
ATOM    137  C   LEU A  21      13.856  35.535  46.024  1.00 41.83           C  
ANISOU  137  C   LEU A  21     4804   4730   6359  -1494   1250   -906       C  
ATOM    138  O   LEU A  21      13.284  35.121  45.016  1.00 44.33           O  
ANISOU  138  O   LEU A  21     5116   5022   6704  -1454   1209   -859       O  
ATOM    139  CB  LEU A  21      14.512  34.107  48.005  1.00 39.86           C  
ANISOU  139  CB  LEU A  21     4716   4543   5887  -1575   1249   -951       C  
ATOM    140  CG  LEU A  21      15.470  33.138  48.713  1.00 40.80           C  
ANISOU  140  CG  LEU A  21     4939   4712   5851  -1574   1203   -936       C  
ATOM    141  CD1 LEU A  21      14.848  32.656  50.016  1.00 44.53           C  
ANISOU  141  CD1 LEU A  21     5473   5186   6261  -1668   1250   -985       C  
ATOM    142  CD2 LEU A  21      15.850  31.950  47.826  1.00 38.08           C  
ANISOU  142  CD2 LEU A  21     4663   4370   5434  -1497   1116   -862       C  
ATOM    143  N   ASP A  22      13.546  36.687  46.608  1.00 41.58           N  
ANISOU  143  N   ASP A  22     4696   4678   6424  -1544   1328   -965       N  
ATOM    144  CA  ASP A  22      12.750  37.702  45.924  1.00 43.73           C  
ANISOU  144  CA  ASP A  22     4863   4897   6855  -1532   1361   -964       C  
ATOM    145  C   ASP A  22      11.443  37.205  45.306  1.00 42.34           C  
ANISOU  145  C   ASP A  22     4674   4678   6735  -1530   1346   -942       C  
ATOM    146  O   ASP A  22      11.169  37.474  44.141  1.00 39.16           O  
ANISOU  146  O   ASP A  22     4221   4253   6404  -1473   1308   -887       O  
ATOM    147  CB  ASP A  22      13.611  38.352  44.841  1.00 41.59           C  
ANISOU  147  CB  ASP A  22     4547   4634   6622  -1454   1320   -904       C  
ATOM    148  CG  ASP A  22      14.797  39.099  45.421  1.00 45.17           C  
ANISOU  148  CG  ASP A  22     4986   5120   7056  -1463   1347   -934       C  
ATOM    149  OD1 ASP A  22      14.557  40.080  46.156  1.00 41.68           O  
ANISOU  149  OD1 ASP A  22     4485   4654   6696  -1518   1425  -1000       O  
ATOM    150  OD2 ASP A  22      15.959  38.709  45.154  1.00 38.52           O1-
ANISOU  150  OD2 ASP A  22     4188   4327   6121  -1417   1294   -896       O1-
ATOM    151  N   GLN A  23      10.629  36.501  46.085  1.00 42.45           N  
ANISOU  151  N   GLN A  23     4730   4684   6714  -1594   1376   -985       N  
ATOM    152  CA  GLN A  23       9.359  35.989  45.575  1.00 40.34           C  
ANISOU  152  CA  GLN A  23     4449   4379   6500  -1601   1364   -972       C  
ATOM    153  C   GLN A  23       8.181  36.844  46.057  1.00 43.73           C  
ANISOU  153  C   GLN A  23     4784   4759   7073  -1660   1452  -1037       C  
ATOM    154  O   GLN A  23       7.069  36.347  46.235  1.00 39.82           O  
ANISOU  154  O   GLN A  23     4286   4238   6605  -1703   1472  -1061       O  
ATOM    155  CB  GLN A  23       9.173  34.526  45.978  1.00 43.51           C  
ANISOU  155  CB  GLN A  23     4961   4798   6773  -1631   1335   -969       C  
ATOM    156  CG  GLN A  23      10.343  33.625  45.568  1.00 44.04           C  
ANISOU  156  CG  GLN A  23     5123   4909   6702  -1570   1252   -909       C  
ATOM    157  CD  GLN A  23      10.438  33.422  44.064  1.00 41.59           C  
ANISOU  157  CD  GLN A  23     4798   4595   6410  -1486   1174   -836       C  
ATOM    158  NE2 GLN A  23      11.654  33.222  43.566  1.00 37.72           N  
ANISOU  158  NE2 GLN A  23     4346   4141   5843  -1421   1119   -789       N  
ATOM    159  OE1 GLN A  23       9.428  33.439  43.360  1.00 42.76           O  
ANISOU  159  OE1 GLN A  23     4899   4710   6639  -1482   1164   -822       O  
ATOM    160  N   GLY A  24       8.439  38.136  46.257  1.00 48.71           N  
ANISOU  160  N   GLY A  24     5334   5373   7802  -1662   1506  -1068       N  
ATOM    161  CA  GLY A  24       7.422  39.064  46.724  1.00 50.09           C  
ANISOU  161  CA  GLY A  24     5411   5495   8127  -1713   1596  -1136       C  
ATOM    162  C   GLY A  24       6.171  39.071  45.863  1.00 52.58           C  
ANISOU  162  C   GLY A  24     5654   5762   8563  -1690   1577  -1107       C  
ATOM    163  O   GLY A  24       5.059  39.203  46.376  1.00 50.77           O  
ANISOU  163  O   GLY A  24     5374   5496   8419  -1747   1642  -1166       O  
ATOM    164  N   HIS A  25       6.353  38.917  44.553  1.00 56.90           N  
ANISOU  164  N   HIS A  25     6193   6311   9115  -1610   1488  -1018       N  
ATOM    165  CA  HIS A  25       5.239  38.935  43.608  1.00 59.35           C  
ANISOU  165  CA  HIS A  25     6433   6583   9533  -1582   1454   -980       C  
ATOM    166  C   HIS A  25       4.172  37.891  43.925  1.00 62.60           C  
ANISOU  166  C   HIS A  25     6876   6991   9917  -1635   1458  -1010       C  
ATOM    167  O   HIS A  25       3.060  37.962  43.406  1.00 65.96           O  
ANISOU  167  O   HIS A  25     7229   7382  10449  -1633   1448  -1002       O  
ATOM    168  CB  HIS A  25       5.738  38.758  42.167  1.00 57.89           C  
ANISOU  168  CB  HIS A  25     6260   6417   9318  -1494   1349   -877       C  
ATOM    169  CG  HIS A  25       6.207  37.371  41.850  1.00 59.17           C  
ANISOU  169  CG  HIS A  25     6538   6628   9315  -1477   1275   -839       C  
ATOM    170  CD2 HIS A  25       5.567  36.322  41.274  1.00 59.64           C  
ANISOU  170  CD2 HIS A  25     6636   6694   9331  -1472   1215   -811       C  
ATOM    171  ND1 HIS A  25       7.486  36.935  42.119  1.00 52.34           N  
ANISOU  171  ND1 HIS A  25     5764   5811   8313  -1462   1255   -829       N  
ATOM    172  CE1 HIS A  25       7.613  35.678  41.733  1.00 53.63           C  
ANISOU  172  CE1 HIS A  25     6017   6002   8359  -1445   1189   -796       C  
ATOM    173  NE2 HIS A  25       6.463  35.284  41.215  1.00 55.66           N  
ANISOU  173  NE2 HIS A  25     6247   6235   8668  -1454   1166   -786       N  
ATOM    174  N   LEU A  26       4.509  36.927  44.777  1.00 61.50           N  
ANISOU  174  N   LEU A  26     6843   6887   9638  -1685   1470  -1043       N  
ATOM    175  CA  LEU A  26       3.571  35.866  45.129  1.00 58.66           C  
ANISOU  175  CA  LEU A  26     6526   6523   9240  -1741   1478  -1070       C  
ATOM    176  C   LEU A  26       2.567  36.308  46.187  1.00 61.22           C  
ANISOU  176  C   LEU A  26     6789   6813   9657  -1828   1588  -1163       C  
ATOM    177  O   LEU A  26       1.504  35.701  46.335  1.00 60.71           O  
ANISOU  177  O   LEU A  26     6719   6731   9616  -1875   1605  -1189       O  
ATOM    178  CB  LEU A  26       4.313  34.616  45.612  1.00 54.34           C  
ANISOU  178  CB  LEU A  26     6122   6020   8505  -1760   1446  -1060       C  
ATOM    179  CG  LEU A  26       5.179  33.890  44.583  1.00 52.85           C  
ANISOU  179  CG  LEU A  26     6004   5862   8213  -1681   1339   -975       C  
ATOM    180  CD1 LEU A  26       5.765  32.620  45.188  1.00 47.40           C  
ANISOU  180  CD1 LEU A  26     5451   5205   7355  -1705   1318   -973       C  
ATOM    181  CD2 LEU A  26       4.371  33.569  43.334  1.00 50.71           C  
ANISOU  181  CD2 LEU A  26     5693   5572   8001  -1641   1273   -926       C  
ATOM    182  N   PHE A  27       2.900  37.360  46.925  1.00 58.05           N  
ANISOU  182  N   PHE A  27     6343   6403   9312  -1852   1666  -1218       N  
ATOM    183  CA  PHE A  27       2.039  37.807  48.015  1.00 63.31           C  
ANISOU  183  CA  PHE A  27     6956   7039  10059  -1939   1783  -1318       C  
ATOM    184  C   PHE A  27       1.555  39.236  47.781  1.00 68.28           C  
ANISOU  184  C   PHE A  27     7442   7613  10888  -1918   1835  -1345       C  
ATOM    185  O   PHE A  27       1.205  39.954  48.720  1.00 70.92           O  
ANISOU  185  O   PHE A  27     7725   7923  11299  -1979   1943  -1434       O  
ATOM    186  CB  PHE A  27       2.776  37.675  49.351  1.00 60.76           C  
ANISOU  186  CB  PHE A  27     6719   6754   9611  -2008   1845  -1380       C  
ATOM    187  CG  PHE A  27       3.651  36.454  49.432  1.00 58.66           C  
ANISOU  187  CG  PHE A  27     6595   6543   9148  -2000   1773  -1330       C  
ATOM    188  CD1 PHE A  27       5.017  36.548  49.213  1.00 56.76           C  
ANISOU  188  CD1 PHE A  27     6406   6343   8819  -1945   1716  -1284       C  
ATOM    189  CD2 PHE A  27       3.104  35.207  49.694  1.00 59.20           C  
ANISOU  189  CD2 PHE A  27     6743   6621   9129  -2045   1762  -1328       C  
ATOM    190  CE1 PHE A  27       5.824  35.424  49.274  1.00 58.40           C  
ANISOU  190  CE1 PHE A  27     6737   6596   8856  -1931   1649  -1237       C  
ATOM    191  CE2 PHE A  27       3.904  34.075  49.757  1.00 57.76           C  
ANISOU  191  CE2 PHE A  27     6691   6480   8775  -2033   1695  -1279       C  
ATOM    192  CZ  PHE A  27       5.266  34.184  49.547  1.00 58.15           C  
ANISOU  192  CZ  PHE A  27     6787   6568   8740  -1973   1637  -1234       C  
ATOM    193  N   GLU A  28       1.533  39.632  46.513  1.00 68.76           N  
ANISOU  193  N   GLU A  28     7439   7653  11032  -1832   1760  -1266       N  
ATOM    194  CA  GLU A  28       1.107  40.969  46.125  1.00 73.78           C  
ANISOU  194  CA  GLU A  28     7940   8230  11863  -1799   1794  -1271       C  
ATOM    195  C   GLU A  28      -0.331  41.219  46.549  0.82 74.74           C  
ANISOU  195  C   GLU A  28     7965   8302  12132  -1851   1872  -1342       C  
ATOM    196  O   GLU A  28      -1.250  40.552  46.079  0.98 74.40           O  
ANISOU  196  O   GLU A  28     7903   8253  12112  -1851   1832  -1320       O  
ATOM    197  CB  GLU A  28       1.244  41.148  44.612  0.79 77.26           C  
ANISOU  197  CB  GLU A  28     8344   8664  12348  -1700   1685  -1159       C  
ATOM    198  CG  GLU A  28       0.603  42.413  44.068  0.85 81.97           C  
ANISOU  198  CG  GLU A  28     8796   9192  13156  -1659   1705  -1147       C  
ATOM    199  CD  GLU A  28       0.690  42.502  42.556  0.48 85.29           C  
ANISOU  199  CD  GLU A  28     9190   9612  13605  -1567   1590  -1029       C  
ATOM    200  OE1 GLU A  28      -0.054  43.312  41.963  0.72 85.94           O  
ANISOU  200  OE1 GLU A  28     9156   9640  13857  -1531   1585  -1002       O  
ATOM    201  OE2 GLU A  28       1.503  41.762  41.960  0.89 86.28           O1-
ANISOU  201  OE2 GLU A  28     9409   9791  13581  -1531   1506   -963       O1-
ATOM    202  N   GLY A  29      -0.519  42.180  47.445  1.00 75.50           N  
ANISOU  202  N   GLY A  29     7996   8361  12330  -1897   1985  -1432       N  
ATOM    203  CA  GLY A  29      -1.848  42.541  47.900  1.00 79.86           C  
ANISOU  203  CA  GLY A  29     8444   8861  13039  -1947   2074  -1510       C  
ATOM    204  C   GLY A  29      -2.405  41.586  48.937  1.00 80.37           C  
ANISOU  204  C   GLY A  29     8572   8953  13010  -2047   2138  -1588       C  
ATOM    205  O   GLY A  29      -3.620  41.478  49.103  1.00 83.21           O  
ANISOU  205  O   GLY A  29     8860   9282  13473  -2086   2186  -1635       O  
ATOM    206  N   TRP A  30      -1.516  40.886  49.634  1.00 76.55           N  
ANISOU  206  N   TRP A  30     8223   8529  12334  -2089   2138  -1599       N  
ATOM    207  CA  TRP A  30      -1.930  39.998  50.713  1.00 72.01           C  
ANISOU  207  CA  TRP A  30     7723   7982  11654  -2191   2204  -1669       C  
ATOM    208  C   TRP A  30      -1.972  40.748  52.039  1.00 73.98           C  
ANISOU  208  C   TRP A  30     7951   8222  11936  -2276   2344  -1790       C  
ATOM    209  O   TRP A  30      -1.297  41.764  52.207  1.00 67.43           O  
ANISOU  209  O   TRP A  30     7090   7381  11151  -2256   2375  -1812       O  
ATOM    210  CB  TRP A  30      -0.980  38.806  50.841  1.00 67.18           C  
ANISOU  210  CB  TRP A  30     7273   7438  10815  -2196   2131  -1617       C  
ATOM    211  CG  TRP A  30      -1.097  37.785  49.749  1.00 64.58           C  
ANISOU  211  CG  TRP A  30     6985   7122  10430  -2139   2011  -1520       C  
ATOM    212  CD1 TRP A  30      -1.493  37.999  48.460  1.00 65.18           C  
ANISOU  212  CD1 TRP A  30     6981   7170  10614  -2058   1932  -1450       C  
ATOM    213  CD2 TRP A  30      -0.821  36.383  49.856  1.00 57.93           C  
ANISOU  213  CD2 TRP A  30     6277   6322   9411  -2161   1956  -1484       C  
ATOM    214  CE2 TRP A  30      -1.066  35.810  48.592  1.00 57.81           C  
ANISOU  214  CE2 TRP A  30     6255   6303   9408  -2093   1849  -1400       C  
ATOM    215  CE3 TRP A  30      -0.385  35.557  50.898  1.00 57.11           C  
ANISOU  215  CE3 TRP A  30     6299   6259   9140  -2232   1987  -1513       C  
ATOM    216  NE1 TRP A  30      -1.476  36.818  47.758  1.00 61.94           N  
ANISOU  216  NE1 TRP A  30     6647   6787  10100  -2033   1834  -1380       N  
ATOM    217  CZ2 TRP A  30      -0.892  34.449  48.341  1.00 54.36           C  
ANISOU  217  CZ2 TRP A  30     5932   5894   8827  -2094   1777  -1351       C  
ATOM    218  CZ3 TRP A  30      -0.216  34.204  50.649  1.00 56.26           C  
ANISOU  218  CZ3 TRP A  30     6305   6177   8895  -2229   1912  -1456       C  
ATOM    219  CH2 TRP A  30      -0.469  33.664  49.380  1.00 54.12           C  
ANISOU  219  CH2 TRP A  30     6023   5895   8645  -2161   1811  -1379       C  
ATOM    220  N   PRO A  31      -2.776  40.245  52.987  1.00 77.64           N  
ANISOU  220  N   PRO A  31     8434   8691  12376  -2375   2433  -1871       N  
ATOM    221  CA  PRO A  31      -2.796  40.760  54.359  1.00 80.12           C  
ANISOU  221  CA  PRO A  31     8752   9009  12681  -2473   2571  -1992       C  
ATOM    222  C   PRO A  31      -1.427  40.597  55.010  1.00 81.66           C  
ANISOU  222  C   PRO A  31     9074   9268  12687  -2493   2555  -1988       C  
ATOM    223  O   PRO A  31      -0.574  39.897  54.467  1.00 78.55           O  
ANISOU  223  O   PRO A  31     8770   8914  12161  -2439   2442  -1894       O  
ATOM    224  CB  PRO A  31      -3.817  39.856  55.051  1.00 79.92           C  
ANISOU  224  CB  PRO A  31     8757   8993  12615  -2569   2636  -2048       C  
ATOM    225  CG  PRO A  31      -4.704  39.381  53.952  1.00 80.03           C  
ANISOU  225  CG  PRO A  31     8708   8976  12723  -2515   2562  -1982       C  
ATOM    226  CD  PRO A  31      -3.804  39.214  52.767  1.00 78.20           C  
ANISOU  226  CD  PRO A  31     8512   8760  12441  -2403   2414  -1858       C  
ATOM    227  N   GLU A  32      -1.225  41.226  56.161  1.00 87.25           N  
ANISOU  227  N   GLU A  32     9785   9985  13382  -2572   2667  -2092       N  
ATOM    228  CA  GLU A  32       0.079  41.216  56.814  1.00 91.45           C  
ANISOU  228  CA  GLU A  32    10421  10578  13746  -2594   2653  -2096       C  
ATOM    229  C   GLU A  32       0.460  39.848  57.373  1.00 91.13           C  
ANISOU  229  C   GLU A  32    10538  10609  13479  -2645   2611  -2063       C  
ATOM    230  O   GLU A  32       1.575  39.374  57.156  1.00 91.75           O  
ANISOU  230  O   GLU A  32    10709  10736  13417  -2602   2514  -1988       O  
ATOM    231  CB  GLU A  32       0.138  42.263  57.928  1.00 96.55           C  
ANISOU  231  CB  GLU A  32    11029  11218  14438  -2674   2787  -2225       C  
ATOM    232  CG  GLU A  32       1.503  42.364  58.590  1.00 99.54           C  
ANISOU  232  CG  GLU A  32    11504  11664  14654  -2697   2770  -2233       C  
ATOM    233  CD  GLU A  32       1.495  43.260  59.813  0.41101.90           C  
ANISOU  233  CD  GLU A  32    11778  11965  14973  -2796   2909  -2373       C  
ATOM    234  OE1 GLU A  32       0.401  43.705  60.220  0.80102.29           O  
ANISOU  234  OE1 GLU A  32    11747  11967  15153  -2852   3026  -2467       O  
ATOM    235  OE2 GLU A  32       2.585  43.517  60.367  1.00102.21           O1-
ANISOU  235  OE2 GLU A  32    11878  12057  14899  -2819   2901  -2392       O1-
ATOM    236  N   THR A  33      -0.459  39.219  58.097  1.00 89.32           N  
ANISOU  236  N   THR A  33    10337  10382  13218  -2737   2685  -2118       N  
ATOM    237  CA  THR A  33      -0.160  37.947  58.745  1.00 87.62           C  
ANISOU  237  CA  THR A  33    10274  10227  12790  -2797   2658  -2091       C  
ATOM    238  C   THR A  33      -1.070  36.813  58.276  1.00 86.36           C  
ANISOU  238  C   THR A  33    10139  10050  12625  -2800   2622  -2042       C  
ATOM    239  O   THR A  33      -2.144  37.046  57.723  1.00 86.64           O  
ANISOU  239  O   THR A  33    10064  10030  12823  -2785   2648  -2058       O  
ATOM    240  CB  THR A  33      -0.220  38.063  60.279  0.52 90.48           C  
ANISOU  240  CB  THR A  33    10691  10627  13060  -2929   2782  -2201       C  
ATOM    241  CG2 THR A  33      -1.562  38.612  60.718  0.72 91.82           C  
ANISOU  241  CG2 THR A  33    10755  10748  13385  -3002   2923  -2313       C  
ATOM    242  OG1 THR A  33      -0.023  36.772  60.867  0.62 91.92           O  
ANISOU  242  OG1 THR A  33    11023  10863  13041  -2987   2752  -2163       O  
ATOM    243  N   VAL A  34      -0.622  35.584  58.512  1.00 84.13           N  
ANISOU  243  N   VAL A  34     9998   9811  12156  -2820   2560  -1982       N  
ATOM    244  CA  VAL A  34      -1.317  34.386  58.051  1.00 83.69           C  
ANISOU  244  CA  VAL A  34     9985   9741  12072  -2821   2513  -1926       C  
ATOM    245  C   VAL A  34      -2.788  34.342  58.458  1.00 88.02           C  
ANISOU  245  C   VAL A  34    10467  10253  12724  -2909   2625  -2007       C  
ATOM    246  O   VAL A  34      -3.650  33.954  57.668  1.00 86.05           O  
ANISOU  246  O   VAL A  34    10162   9965  12569  -2882   2595  -1978       O  
ATOM    247  CB  VAL A  34      -0.621  33.115  58.576  1.00 81.05           C  
ANISOU  247  CB  VAL A  34     9825   9457  11512  -2854   2458  -1868       C  
ATOM    248  CG1 VAL A  34      -1.540  31.908  58.448  1.00 83.85           C  
ANISOU  248  CG1 VAL A  34    10229   9791  11841  -2895   2452  -1842       C  
ATOM    249  CG2 VAL A  34       0.691  32.886  57.843  1.00 73.85           C  
ANISOU  249  CG2 VAL A  34     8971   8572  10516  -2746   2322  -1768       C  
ATOM    250  N   ASP A  35      -3.064  34.738  59.695  0.63 94.21           N  
ANISOU  250  N   ASP A  35    11256  11052  13488  -3017   2755  -2111       N  
ATOM    251  CA  ASP A  35      -4.413  34.667  60.245  0.93 98.46           C  
ANISOU  251  CA  ASP A  35    11739  11562  14108  -3115   2878  -2199       C  
ATOM    252  C   ASP A  35      -5.408  35.449  59.394  1.00 94.73           C  
ANISOU  252  C   ASP A  35    11089  11024  13881  -3062   2901  -2227       C  
ATOM    253  O   ASP A  35      -6.573  35.068  59.271  1.00 90.13           O  
ANISOU  253  O   ASP A  35    10452  10410  13384  -3101   2942  -2252       O  
ATOM    254  CB  ASP A  35      -4.426  35.197  61.679  1.00105.30           C  
ANISOU  254  CB  ASP A  35    12628  12459  14923  -3233   3021  -2316       C  
ATOM    255  CG  ASP A  35      -3.344  34.574  62.541  0.87109.40           C  
ANISOU  255  CG  ASP A  35    13317  13049  15200  -3280   2992  -2286       C  
ATOM    256  OD1 ASP A  35      -2.174  34.536  62.102  0.75108.26           O  
ANISOU  256  OD1 ASP A  35    13226  12932  14977  -3197   2878  -2206       O  
ATOM    257  OD2 ASP A  35      -3.665  34.120  63.660  0.88112.55           O1-
ANISOU  257  OD2 ASP A  35    13796  13480  15489  -3401   3082  -2341       O1-
ATOM    258  N   GLU A  36      -4.933  36.544  58.809  1.00 94.94           N  
ANISOU  258  N   GLU A  36    11024  11028  14021  -2975   2870  -2219       N  
ATOM    259  CA  GLU A  36      -5.775  37.427  58.012  1.00 94.32           C  
ANISOU  259  CA  GLU A  36    10772  10884  14181  -2917   2887  -2240       C  
ATOM    260  C   GLU A  36      -5.981  36.888  56.596  1.00 90.03           C  
ANISOU  260  C   GLU A  36    10200  10319  13687  -2816   2750  -2128       C  
ATOM    261  O   GLU A  36      -6.920  37.283  55.904  1.00 90.36           O  
ANISOU  261  O   GLU A  36    10109  10311  13913  -2780   2752  -2133       O  
ATOM    262  CB  GLU A  36      -5.152  38.824  57.954  1.00 98.13           C  
ANISOU  262  CB  GLU A  36    11175  11347  14763  -2865   2909  -2271       C  
ATOM    263  CG  GLU A  36      -4.719  39.370  59.308  1.00103.45           C  
ANISOU  263  CG  GLU A  36    11891  12050  15364  -2959   3028  -2378       C  
ATOM    264  CD  GLU A  36      -3.787  40.565  59.188  1.00109.44           C  
ANISOU  264  CD  GLU A  36    12605  12800  16176  -2902   3022  -2388       C  
ATOM    265  OE1 GLU A  36      -3.502  40.992  58.049  1.00111.93           O  
ANISOU  265  OE1 GLU A  36    12855  13082  16589  -2789   2929  -2309       O  
ATOM    266  OE2 GLU A  36      -3.334  41.076  60.234  1.00110.84           O1-
ANISOU  266  OE2 GLU A  36    12815  13004  16293  -2975   3110  -2475       O1-
ATOM    267  N   CYS A  37      -5.101  35.984  56.173  1.00 84.96           N  
ANISOU  267  N   CYS A  37     9682   9716  12881  -2772   2631  -2028       N  
ATOM    268  CA  CYS A  37      -5.142  35.446  54.815  1.00 79.55           C  
ANISOU  268  CA  CYS A  37     8986   9018  12221  -2677   2497  -1922       C  
ATOM    269  C   CYS A  37      -6.333  34.522  54.599  1.00 79.41           C  
ANISOU  269  C   CYS A  37     8955   8983  12235  -2721   2500  -1923       C  
ATOM    270  O   CYS A  37      -6.735  33.790  55.503  1.00 76.55           O  
ANISOU  270  O   CYS A  37     8665   8636  11784  -2823   2571  -1969       O  
ATOM    271  CB  CYS A  37      -3.842  34.705  54.489  1.00 78.22           C  
ANISOU  271  CB  CYS A  37     8958   8897  11866  -2623   2379  -1825       C  
ATOM    272  SG  CYS A  37      -2.358  35.748  54.509  1.00 82.33           S  
ANISOU  272  SG  CYS A  37     9487   9442  12355  -2556   2352  -1808       S  
ATOM    273  N   ASN A  38      -6.891  34.556  53.394  1.00 81.47           N  
ANISOU  273  N   ASN A  38     9124   9213  12620  -2647   2421  -1871       N  
ATOM    274  CA  ASN A  38      -8.033  33.717  53.063  1.00 86.05           C  
ANISOU  274  CA  ASN A  38     9677   9775  13243  -2683   2413  -1870       C  
ATOM    275  C   ASN A  38      -7.624  32.274  52.772  1.00 87.95           C  
ANISOU  275  C   ASN A  38    10066  10046  13306  -2684   2320  -1793       C  
ATOM    276  O   ASN A  38      -6.468  31.896  52.968  1.00 86.28           O  
ANISOU  276  O   ASN A  38     9982   9869  12933  -2664   2272  -1746       O  
ATOM    277  CB  ASN A  38      -8.808  34.306  51.880  1.00 88.44           C  
ANISOU  277  CB  ASN A  38     9822  10038  13745  -2605   2358  -1843       C  
ATOM    278  CG  ASN A  38      -8.001  34.310  50.594  1.00 88.46           C  
ANISOU  278  CG  ASN A  38     9841  10050  13720  -2484   2208  -1730       C  
ATOM    279  ND2 ASN A  38      -8.338  35.223  49.689  1.00 85.89           N  
ANISOU  279  ND2 ASN A  38     9379   9692  13563  -2405   2168  -1704       N  
ATOM    280  OD1 ASN A  38      -7.091  33.501  50.413  1.00 89.24           O  
ANISOU  280  OD1 ASN A  38    10074  10185  13649  -2462   2131  -1665       O  
ATOM    281  N   GLU A  39      -8.579  31.478  52.300  1.00 90.35           N  
ANISOU  281  N   GLU A  39    10349  10334  13647  -2707   2293  -1783       N  
ATOM    282  CA  GLU A  39      -8.344  30.069  52.003  1.00 93.80           C  
ANISOU  282  CA  GLU A  39    10918  10787  13933  -2715   2213  -1718       C  
ATOM    283  C   GLU A  39      -7.353  29.867  50.860  1.00 87.32           C  
ANISOU  283  C   GLU A  39    10146   9982  13048  -2599   2066  -1613       C  
ATOM    284  O   GLU A  39      -6.438  29.051  50.958  1.00 84.12           O  
ANISOU  284  O   GLU A  39     9884   9602  12475  -2588   2013  -1561       O  
ATOM    285  CB  GLU A  39      -9.664  29.369  51.666  1.00103.26           C  
ANISOU  285  CB  GLU A  39    12063  11960  15210  -2766   2219  -1738       C  
ATOM    286  CG  GLU A  39     -10.570  29.111  52.861  1.00113.06           C  
ANISOU  286  CG  GLU A  39    13302  13192  16461  -2899   2360  -1833       C  
ATOM    287  CD  GLU A  39     -10.095  27.949  53.717  1.00118.61           C  
ANISOU  287  CD  GLU A  39    14188  13917  16960  -2977   2382  -1821       C  
ATOM    288  OE1 GLU A  39     -10.882  26.998  53.919  1.00118.88           O  
ANISOU  288  OE1 GLU A  39    14257  13938  16973  -3058   2411  -1838       O  
ATOM    289  OE2 GLU A  39      -8.938  27.989  54.189  1.00119.63           O1-
ANISOU  289  OE2 GLU A  39    14426  14075  16954  -2959   2369  -1793       O1-
ATOM    290  N   ARG A  40      -7.550  30.602  49.771  1.00 83.72           N  
ANISOU  290  N   ARG A  40     9572   9512  12728  -2512   2002  -1581       N  
ATOM    291  CA  ARG A  40      -6.713  30.447  48.589  1.00 81.64           C  
ANISOU  291  CA  ARG A  40     9342   9263  12413  -2404   1867  -1483       C  
ATOM    292  C   ARG A  40      -5.259  30.786  48.910  1.00 76.61           C  
ANISOU  292  C   ARG A  40     8791   8655  11661  -2360   1852  -1453       C  
ATOM    293  O   ARG A  40      -4.336  30.085  48.490  1.00 72.74           O  
ANISOU  293  O   ARG A  40     8411   8191  11038  -2313   1766  -1385       O  
ATOM    294  CB  ARG A  40      -7.225  31.333  47.450  1.00 84.26           C  
ANISOU  294  CB  ARG A  40     9521   9574  12918  -2325   1812  -1456       C  
ATOM    295  CG  ARG A  40      -6.564  31.059  46.108  1.00 87.16           C  
ANISOU  295  CG  ARG A  40     9921   9960  13236  -2224   1670  -1355       C  
ATOM    296  CD  ARG A  40      -6.639  32.270  45.188  1.00 89.23           C  
ANISOU  296  CD  ARG A  40    10049  10208  13647  -2137   1627  -1320       C  
ATOM    297  NE  ARG A  40      -6.055  33.455  45.811  1.00 90.38           N  
ANISOU  297  NE  ARG A  40    10156  10345  13841  -2123   1698  -1350       N  
ATOM    298  CZ  ARG A  40      -4.750  33.687  45.902  0.21 84.70           C  
ANISOU  298  CZ  ARG A  40     9514   9649  13018  -2080   1677  -1316       C  
ATOM    299  NH1 ARG A  40      -3.883  32.814  45.411  0.63 84.18           N1+
ANISOU  299  NH1 ARG A  40     9567   9617  12799  -2042   1589  -1250       N1+
ATOM    300  NH2 ARG A  40      -4.312  34.792  46.489  0.65 80.04           N  
ANISOU  300  NH2 ARG A  40     8881   9049  12484  -2077   1747  -1353       N  
ATOM    301  N   GLN A  41      -5.067  31.864  49.665  1.00 74.40           N  
ANISOU  301  N   GLN A  41     8458   8373  11439  -2378   1940  -1509       N  
ATOM    302  CA  GLN A  41      -3.734  32.316  50.044  1.00 71.60           C  
ANISOU  302  CA  GLN A  41     8168   8047  10990  -2345   1935  -1493       C  
ATOM    303  C   GLN A  41      -3.067  31.331  50.998  1.00 68.97           C  
ANISOU  303  C   GLN A  41     7995   7748  10462  -2404   1950  -1495       C  
ATOM    304  O   GLN A  41      -1.880  31.033  50.865  1.00 65.77           O  
ANISOU  304  O   GLN A  41     7684   7374   9931  -2355   1883  -1438       O  
ATOM    305  CB  GLN A  41      -3.809  33.700  50.686  1.00 70.58           C  
ANISOU  305  CB  GLN A  41     7937   7901  10978  -2363   2035  -1566       C  
ATOM    306  CG  GLN A  41      -4.369  34.772  49.770  1.00 72.30           C  
ANISOU  306  CG  GLN A  41     7996   8078  11395  -2295   2018  -1556       C  
ATOM    307  CD  GLN A  41      -4.707  36.045  50.513  1.00 74.25           C  
ANISOU  307  CD  GLN A  41     8136   8295  11779  -2330   2137  -1646       C  
ATOM    308  NE2 GLN A  41      -4.869  37.137  49.774  1.00 75.09           N  
ANISOU  308  NE2 GLN A  41     8116   8364  12050  -2258   2120  -1628       N  
ATOM    309  OE1 GLN A  41      -4.819  36.050  51.740  1.00 73.77           O  
ANISOU  309  OE1 GLN A  41     8109   8242  11677  -2421   2245  -1730       O  
ATOM    310  N   ILE A  42      -3.833  30.827  51.958  1.00 65.61           N  
ANISOU  310  N   ILE A  42     7599   7316  10012  -2511   2039  -1558       N  
ATOM    311  CA  ILE A  42      -3.303  29.856  52.904  1.00 65.22           C  
ANISOU  311  CA  ILE A  42     7705   7296   9779  -2576   2056  -1556       C  
ATOM    312  C   ILE A  42      -2.882  28.587  52.167  1.00 63.53           C  
ANISOU  312  C   ILE A  42     7600   7087   9451  -2529   1942  -1467       C  
ATOM    313  O   ILE A  42      -1.917  27.924  52.549  1.00 64.87           O  
ANISOU  313  O   ILE A  42     7900   7284   9463  -2525   1905  -1426       O  
ATOM    314  CB  ILE A  42      -4.330  29.508  54.004  1.00 70.88           C  
ANISOU  314  CB  ILE A  42     8433   8003  10498  -2706   2177  -1637       C  
ATOM    315  CG1 ILE A  42      -3.614  29.122  55.296  1.00 71.44           C  
ANISOU  315  CG1 ILE A  42     8638   8111  10395  -2779   2227  -1655       C  
ATOM    316  CG2 ILE A  42      -5.272  28.407  53.547  1.00 74.85           C  
ANISOU  316  CG2 ILE A  42     8952   8478  11008  -2737   2151  -1618       C  
ATOM    317  CD1 ILE A  42      -2.825  30.267  55.893  1.00 69.65           C  
ANISOU  317  CD1 ILE A  42     8384   7912  10168  -2770   2271  -1696       C  
ATOM    318  N   ALA A  43      -3.607  28.262  51.102  1.00 58.50           N  
ANISOU  318  N   ALA A  43     6905   6423   8898  -2494   1884  -1438       N  
ATOM    319  CA  ALA A  43      -3.324  27.074  50.313  1.00 57.25           C  
ANISOU  319  CA  ALA A  43     6840   6265   8649  -2452   1779  -1363       C  
ATOM    320  C   ALA A  43      -2.037  27.232  49.515  1.00 56.40           C  
ANISOU  320  C   ALA A  43     6766   6181   8481  -2339   1676  -1288       C  
ATOM    321  O   ALA A  43      -1.290  26.273  49.327  1.00 57.32           O  
ANISOU  321  O   ALA A  43     7002   6309   8467  -2310   1607  -1232       O  
ATOM    322  CB  ALA A  43      -4.489  26.768  49.384  1.00 62.71           C  
ANISOU  322  CB  ALA A  43     7449   6925   9452  -2451   1747  -1362       C  
ATOM    323  N   LEU A  44      -1.778  28.443  49.040  1.00 56.48           N  
ANISOU  323  N   LEU A  44     6671   6197   8592  -2276   1668  -1286       N  
ATOM    324  CA  LEU A  44      -0.578  28.693  48.252  1.00 58.28           C  
ANISOU  324  CA  LEU A  44     6920   6448   8773  -2171   1578  -1217       C  
ATOM    325  C   LEU A  44       0.680  28.586  49.111  1.00 57.58           C  
ANISOU  325  C   LEU A  44     6937   6395   8544  -2174   1586  -1210       C  
ATOM    326  O   LEU A  44       1.683  28.008  48.689  1.00 54.76           O  
ANISOU  326  O   LEU A  44     6666   6060   8081  -2112   1506  -1148       O  
ATOM    327  CB  LEU A  44      -0.646  30.058  47.561  1.00 57.16           C  
ANISOU  327  CB  LEU A  44     6639   6299   8780  -2109   1573  -1216       C  
ATOM    328  CG  LEU A  44       0.561  30.372  46.672  1.00 53.21           C  
ANISOU  328  CG  LEU A  44     6154   5824   8240  -2003   1484  -1144       C  
ATOM    329  CD1 LEU A  44       0.128  31.013  45.362  1.00 55.85           C  
ANISOU  329  CD1 LEU A  44     6375   6142   8702  -1933   1427  -1104       C  
ATOM    330  CD2 LEU A  44       1.570  31.245  47.407  1.00 48.39           C  
ANISOU  330  CD2 LEU A  44     5547   5236   7602  -1997   1528  -1164       C  
ATOM    331  N   LEU A  45       0.617  29.147  50.315  1.00 57.92           N  
ANISOU  331  N   LEU A  45     6971   6447   8589  -2246   1685  -1277       N  
ATOM    332  CA  LEU A  45       1.734  29.090  51.253  1.00 56.95           C  
ANISOU  332  CA  LEU A  45     6943   6363   8332  -2261   1697  -1277       C  
ATOM    333  C   LEU A  45       2.013  27.663  51.699  1.00 54.47           C  
ANISOU  333  C   LEU A  45     6780   6058   7859  -2294   1666  -1243       C  
ATOM    334  O   LEU A  45       3.169  27.256  51.832  1.00 51.44           O  
ANISOU  334  O   LEU A  45     6489   5705   7353  -2254   1610  -1196       O  
ATOM    335  CB  LEU A  45       1.458  29.973  52.467  1.00 59.12           C  
ANISOU  335  CB  LEU A  45     7174   6644   8643  -2345   1816  -1366       C  
ATOM    336  CG  LEU A  45       2.088  31.360  52.401  1.00 63.36           C  
ANISOU  336  CG  LEU A  45     7624   7194   9257  -2301   1833  -1387       C  
ATOM    337  CD1 LEU A  45       1.581  32.241  53.531  1.00 69.70           C  
ANISOU  337  CD1 LEU A  45     8369   7993  10120  -2392   1962  -1489       C  
ATOM    338  CD2 LEU A  45       3.601  31.239  52.443  1.00 62.70           C  
ANISOU  338  CD2 LEU A  45     7623   7156   9044  -2246   1765  -1336       C  
ATOM    339  N   THR A  46       0.945  26.907  51.935  1.00 54.97           N  
ANISOU  339  N   THR A  46     6864   6091   7929  -2367   1704  -1265       N  
ATOM    340  CA  THR A  46       1.067  25.495  52.280  1.00 54.17           C  
ANISOU  340  CA  THR A  46     6906   5986   7692  -2401   1676  -1229       C  
ATOM    341  C   THR A  46       1.692  24.712  51.126  1.00 53.58           C  
ANISOU  341  C   THR A  46     6884   5905   7571  -2304   1555  -1146       C  
ATOM    342  O   THR A  46       2.533  23.837  51.340  1.00 52.84           O  
ANISOU  342  O   THR A  46     6912   5821   7344  -2284   1506  -1097       O  
ATOM    343  CB  THR A  46      -0.304  24.895  52.649  1.00 58.86           C  
ANISOU  343  CB  THR A  46     7498   6543   8322  -2501   1744  -1273       C  
ATOM    344  CG2 THR A  46      -0.164  23.436  53.060  1.00 56.39           C  
ANISOU  344  CG2 THR A  46     7338   6218   7868  -2542   1720  -1232       C  
ATOM    345  OG1 THR A  46      -0.870  25.646  53.732  1.00 59.83           O  
ANISOU  345  OG1 THR A  46     7570   6674   8490  -2594   1864  -1356       O  
ATOM    346  N   ASP A  47       1.283  25.036  49.903  1.00 55.70           N  
ANISOU  346  N   ASP A  47     7058   6156   7948  -2242   1509  -1131       N  
ATOM    347  CA  ASP A  47       1.867  24.428  48.710  1.00 50.66           C  
ANISOU  347  CA  ASP A  47     6457   5516   7274  -2148   1399  -1061       C  
ATOM    348  C   ASP A  47       3.379  24.664  48.696  1.00 48.76           C  
ANISOU  348  C   ASP A  47     6264   5314   6948  -2071   1348  -1017       C  
ATOM    349  O   ASP A  47       4.164  23.732  48.503  1.00 46.09           O  
ANISOU  349  O   ASP A  47     6030   4979   6501  -2029   1283   -965       O  
ATOM    350  CB  ASP A  47       1.222  25.012  47.449  1.00 47.60           C  
ANISOU  350  CB  ASP A  47     5947   5115   7022  -2097   1363  -1056       C  
ATOM    351  CG  ASP A  47       1.569  24.229  46.193  1.00 52.68           C  
ANISOU  351  CG  ASP A  47     6633   5755   7627  -2020   1257   -992       C  
ATOM    352  OD1 ASP A  47       1.892  23.028  46.300  1.00 56.20           O  
ANISOU  352  OD1 ASP A  47     7200   6191   7965  -2026   1224   -965       O  
ATOM    353  OD2 ASP A  47       1.511  24.816  45.091  1.00 56.43           O1-
ANISOU  353  OD2 ASP A  47     7024   6236   8182  -1954   1207   -970       O1-
ATOM    354  N   LEU A  48       3.780  25.916  48.916  1.00 50.39           N  
ANISOU  354  N   LEU A  48     6390   5546   7208  -2053   1380  -1040       N  
ATOM    355  CA  LEU A  48       5.193  26.273  48.968  1.00 47.46           C  
ANISOU  355  CA  LEU A  48     6049   5216   6768  -1988   1341  -1008       C  
ATOM    356  C   LEU A  48       5.898  25.515  50.082  1.00 48.79           C  
ANISOU  356  C   LEU A  48     6345   5406   6789  -2027   1347  -1000       C  
ATOM    357  O   LEU A  48       6.990  24.972  49.891  1.00 44.65           O  
ANISOU  357  O   LEU A  48     5896   4900   6168  -1964   1277   -946       O  
ATOM    358  CB  LEU A  48       5.358  27.773  49.197  1.00 43.09           C  
ANISOU  358  CB  LEU A  48     5387   4681   6306  -1985   1393  -1049       C  
ATOM    359  CG  LEU A  48       5.115  28.699  48.008  1.00 42.39           C  
ANISOU  359  CG  LEU A  48     5175   4579   6352  -1919   1367  -1035       C  
ATOM    360  CD1 LEU A  48       4.920  30.131  48.504  1.00 40.65           C  
ANISOU  360  CD1 LEU A  48     4846   4358   6240  -1947   1447  -1093       C  
ATOM    361  CD2 LEU A  48       6.284  28.626  47.033  1.00 39.94           C  
ANISOU  361  CD2 LEU A  48     4888   4294   5994  -1814   1275   -965       C  
ATOM    362  N   TYR A  49       5.258  25.477  51.245  1.00 48.90           N  
ANISOU  362  N   TYR A  49     6380   5415   6786  -2130   1431  -1052       N  
ATOM    363  CA  TYR A  49       5.843  24.843  52.416  1.00 51.27           C  
ANISOU  363  CA  TYR A  49     6799   5738   6943  -2179   1443  -1046       C  
ATOM    364  C   TYR A  49       6.035  23.338  52.241  1.00 49.44           C  
ANISOU  364  C   TYR A  49     6695   5483   6608  -2163   1379   -984       C  
ATOM    365  O   TYR A  49       7.104  22.810  52.537  1.00 46.41           O  
ANISOU  365  O   TYR A  49     6402   5122   6110  -2127   1326   -937       O  
ATOM    366  CB  TYR A  49       5.000  25.132  53.658  1.00 55.98           C  
ANISOU  366  CB  TYR A  49     7390   6335   7545  -2302   1555  -1119       C  
ATOM    367  CG  TYR A  49       5.635  24.637  54.932  1.00 62.04           C  
ANISOU  367  CG  TYR A  49     8276   7136   8161  -2359   1570  -1113       C  
ATOM    368  CD1 TYR A  49       6.497  25.449  55.666  1.00 62.48           C  
ANISOU  368  CD1 TYR A  49     8322   7244   8172  -2365   1589  -1136       C  
ATOM    369  CD2 TYR A  49       5.385  23.354  55.398  1.00 66.47           C  
ANISOU  369  CD2 TYR A  49     8960   7676   8620  -2409   1564  -1081       C  
ATOM    370  CE1 TYR A  49       7.085  24.995  56.832  1.00 65.39           C  
ANISOU  370  CE1 TYR A  49     8801   7651   8395  -2419   1595  -1127       C  
ATOM    371  CE2 TYR A  49       5.967  22.891  56.561  1.00 71.08           C  
ANISOU  371  CE2 TYR A  49     9657   8290   9060  -2460   1572  -1065       C  
ATOM    372  CZ  TYR A  49       6.815  23.713  57.274  1.00 71.59           C  
ANISOU  372  CZ  TYR A  49     9709   8414   9078  -2465   1584  -1088       C  
ATOM    373  OH  TYR A  49       7.391  23.242  58.431  1.00 75.50           O  
ANISOU  373  OH  TYR A  49    10317   8946   9423  -2518   1584  -1069       O  
ATOM    374  N   MET A  50       5.003  22.651  51.757  1.00 50.43           N  
ANISOU  374  N   MET A  50     6824   5561   6777  -2190   1382   -985       N  
ATOM    375  CA  MET A  50       5.063  21.202  51.607  1.00 49.20           C  
ANISOU  375  CA  MET A  50     6790   5372   6534  -2185   1331   -933       C  
ATOM    376  C   MET A  50       6.080  20.751  50.557  1.00 49.42           C  
ANISOU  376  C   MET A  50     6849   5400   6526  -2066   1225   -867       C  
ATOM    377  O   MET A  50       6.429  19.571  50.493  1.00 49.69           O  
ANISOU  377  O   MET A  50     6993   5409   6476  -2047   1176   -820       O  
ATOM    378  CB  MET A  50       3.678  20.635  51.273  1.00 54.27           C  
ANISOU  378  CB  MET A  50     7416   5962   7242  -2246   1362   -958       C  
ATOM    379  CG  MET A  50       2.636  20.858  52.360  1.00 56.67           C  
ANISOU  379  CG  MET A  50     7703   6260   7571  -2372   1473  -1024       C  
ATOM    380  SD  MET A  50       3.087  20.088  53.929  1.00 73.60           S  
ANISOU  380  SD  MET A  50    10001   8415   9548  -2455   1512  -1008       S  
ATOM    381  CE  MET A  50       2.849  18.356  53.525  1.00 68.37           C  
ANISOU  381  CE  MET A  50     9467   7689   8821  -2456   1457   -949       C  
ATOM    382  N   PHE A  51       6.564  21.682  49.739  1.00 44.70           N  
ANISOU  382  N   PHE A  51     6158   4831   5996  -1988   1193   -864       N  
ATOM    383  CA  PHE A  51       7.515  21.320  48.689  1.00 44.02           C  
ANISOU  383  CA  PHE A  51     6094   4750   5882  -1877   1100   -807       C  
ATOM    384  C   PHE A  51       8.754  20.644  49.279  1.00 43.98           C  
ANISOU  384  C   PHE A  51     6200   4763   5747  -1843   1057   -761       C  
ATOM    385  O   PHE A  51       9.436  19.876  48.601  1.00 49.15           O  
ANISOU  385  O   PHE A  51     6912   5406   6357  -1766    984   -712       O  
ATOM    386  CB  PHE A  51       7.910  22.546  47.854  1.00 42.25           C  
ANISOU  386  CB  PHE A  51     5752   4558   5743  -1806   1083   -810       C  
ATOM    387  CG  PHE A  51       8.566  22.200  46.540  1.00 42.88           C  
ANISOU  387  CG  PHE A  51     5838   4639   5817  -1702    997   -760       C  
ATOM    388  CD1 PHE A  51       9.840  22.657  46.238  1.00 43.09           C  
ANISOU  388  CD1 PHE A  51     5851   4706   5815  -1620    955   -731       C  
ATOM    389  CD2 PHE A  51       7.909  21.404  45.611  1.00 43.02           C  
ANISOU  389  CD2 PHE A  51     5873   4619   5855  -1691    961   -747       C  
ATOM    390  CE1 PHE A  51      10.443  22.334  45.026  1.00 40.89           C  
ANISOU  390  CE1 PHE A  51     5579   4430   5529  -1528    884   -689       C  
ATOM    391  CE2 PHE A  51       8.504  21.080  44.403  1.00 40.10           C  
ANISOU  391  CE2 PHE A  51     5511   4252   5473  -1600    887   -707       C  
ATOM    392  CZ  PHE A  51       9.771  21.546  44.109  1.00 39.13           C  
ANISOU  392  CZ  PHE A  51     5376   4170   5321  -1519    851   -678       C  
ATOM    393  N   SER A  52       9.025  20.916  50.552  1.00 44.14           N  
ANISOU  393  N   SER A  52     6251   4812   5709  -1901   1101   -779       N  
ATOM    394  CA  SER A  52      10.207  20.381  51.226  1.00 48.80           C  
ANISOU  394  CA  SER A  52     6939   5427   6177  -1873   1058   -734       C  
ATOM    395  C   SER A  52      10.212  18.857  51.376  1.00 48.76           C  
ANISOU  395  C   SER A  52     7067   5375   6084  -1877   1020   -685       C  
ATOM    396  O   SER A  52      11.273  18.250  51.523  1.00 51.49           O  
ANISOU  396  O   SER A  52     7489   5729   6344  -1819    959   -632       O  
ATOM    397  CB  SER A  52      10.394  21.043  52.595  1.00 53.14           C  
ANISOU  397  CB  SER A  52     7490   6023   6679  -1948   1117   -769       C  
ATOM    398  OG  SER A  52      10.810  22.391  52.451  1.00 60.59           O  
ANISOU  398  OG  SER A  52     8324   7012   7686  -1922   1134   -803       O  
ATOM    399  N  AASN A  53       9.031  18.249  51.341  0.38 47.56           N  
ANISOU  399  N  AASN A  53     6941   5170   5960  -1944   1057   -702       N  
ATOM    400  N  BASN A  53       9.035  18.242  51.345  0.62 46.77           N  
ANISOU  400  N  BASN A  53     6842   5071   5859  -1944   1057   -702       N  
ATOM    401  CA AASN A  53       8.921  16.796  51.436  0.38 50.63           C  
ANISOU  401  CA AASN A  53     7456   5503   6278  -1955   1028   -658       C  
ATOM    402  CA BASN A  53       8.959  16.788  51.446  0.62 50.71           C  
ANISOU  402  CA BASN A  53     7467   5513   6285  -1953   1026   -657       C  
ATOM    403  C  AASN A  53       9.084  16.138  50.072  0.38 51.35           C  
ANISOU  403  C  AASN A  53     7552   5555   6401  -1866    958   -629       C  
ATOM    404  C  BASN A  53       9.178  16.125  50.088  0.62 51.57           C  
ANISOU  404  C  BASN A  53     7584   5586   6424  -1861    954   -625       C  
ATOM    405  O  AASN A  53       8.946  14.923  49.935  0.38 52.17           O  
ANISOU  405  O  AASN A  53     7754   5604   6466  -1867    931   -597       O  
ATOM    406  O  BASN A  53       9.177  14.901  49.973  0.62 52.08           O  
ANISOU  406  O  BASN A  53     7750   5597   6442  -1854    922   -589       O  
ATOM    407  CB AASN A  53       7.577  16.398  52.044  0.38 52.00           C  
ANISOU  407  CB AASN A  53     7657   5636   6464  -2076   1104   -693       C  
ATOM    408  CB BASN A  53       7.624  16.343  52.057  0.62 51.96           C  
ANISOU  408  CB BASN A  53     7658   5630   6454  -2074   1101   -689       C  
ATOM    409  CG AASN A  53       7.379  16.961  53.434  0.38 50.38           C  
ANISOU  409  CG AASN A  53     7457   5468   6217  -2174   1182   -726       C  
ATOM    410  CG BASN A  53       6.443  16.571  51.127  0.62 54.56           C  
ANISOU  410  CG BASN A  53     7897   5930   6904  -2094   1127   -734       C  
ATOM    411  ND2AASN A  53       6.175  17.449  53.708  0.38 44.75           N  
ANISOU  411  ND2AASN A  53     6680   4748   5576  -2266   1268   -790       N  
ATOM    412  OD1AASN A  53       8.299  16.965  54.251  0.38 54.42           O  
ANISOU  412  OD1AASN A  53     8028   6017   6633  -2167   1164   -697       O  
ATOM    413  ND2BASN A  53       5.236  16.342  51.637  0.62 55.16           N  
ANISOU  413  ND2BASN A  53     7978   5976   7006  -2202   1200   -773       N  
ATOM    414  OD1BASN A  53       6.612  16.937  49.962  0.62 56.03           O  
ANISOU  414  OD1BASN A  53     8009   6122   7157  -2014   1081   -733       O  
ATOM    415  N   MET A  54       9.386  16.955  49.070  1.00 49.54           N  
ANISOU  415  N   MET A  54     7223   5358   6244  -1793    931   -640       N  
ATOM    416  CA  MET A  54       9.463  16.504  47.689  1.00 53.34           C  
ANISOU  416  CA  MET A  54     7694   5813   6761  -1715    871   -622       C  
ATOM    417  C   MET A  54      10.833  16.819  47.095  1.00 47.80           C  
ANISOU  417  C   MET A  54     6972   5151   6038  -1600    808   -588       C  
ATOM    418  O   MET A  54      11.322  16.117  46.210  1.00 45.35           O  
ANISOU  418  O   MET A  54     6699   4818   5712  -1525    750   -559       O  
ATOM    419  CB  MET A  54       8.421  17.275  46.884  1.00 59.25           C  
ANISOU  419  CB  MET A  54     8325   6563   7624  -1737    899   -667       C  
ATOM    420  CG  MET A  54       7.565  16.452  45.971  1.00 63.49           C  
ANISOU  420  CG  MET A  54     8878   7048   8196  -1745    878   -672       C  
ATOM    421  SD  MET A  54       6.985  17.480  44.610  1.00 64.96           S  
ANISOU  421  SD  MET A  54     8917   7260   8503  -1709    864   -698       S  
ATOM    422  CE  MET A  54       8.431  17.432  43.551  1.00 48.25           C  
ANISOU  422  CE  MET A  54     6815   5173   6347  -1575    781   -651       C  
ATOM    423  N   TYR A  55      11.434  17.900  47.577  1.00 43.04           N  
ANISOU  423  N   TYR A  55     6308   4607   5439  -1592    825   -599       N  
ATOM    424  CA  TYR A  55      12.668  18.424  47.010  1.00 40.07           C  
ANISOU  424  CA  TYR A  55     5889   4277   5059  -1492    777   -576       C  
ATOM    425  C   TYR A  55      13.636  18.791  48.132  1.00 40.23           C  
ANISOU  425  C   TYR A  55     5930   4345   5012  -1495    779   -565       C  
ATOM    426  O   TYR A  55      13.243  19.417  49.110  1.00 40.44           O  
ANISOU  426  O   TYR A  55     5934   4394   5040  -1574    837   -598       O  
ATOM    427  CB  TYR A  55      12.361  19.653  46.150  1.00 39.52           C  
ANISOU  427  CB  TYR A  55     5689   4236   5092  -1473    794   -605       C  
ATOM    428  CG  TYR A  55      13.515  20.079  45.281  1.00 39.04           C  
ANISOU  428  CG  TYR A  55     5586   4213   5035  -1370    743   -580       C  
ATOM    429  CD1 TYR A  55      13.710  19.511  44.026  1.00 38.88           C  
ANISOU  429  CD1 TYR A  55     5578   4175   5020  -1297    691   -556       C  
ATOM    430  CD2 TYR A  55      14.418  21.040  45.716  1.00 38.84           C  
ANISOU  430  CD2 TYR A  55     5509   4243   5006  -1348    751   -582       C  
ATOM    431  CE1 TYR A  55      14.769  19.891  43.231  1.00 38.81           C  
ANISOU  431  CE1 TYR A  55     5531   4203   5012  -1206    652   -535       C  
ATOM    432  CE2 TYR A  55      15.480  21.423  44.930  1.00 38.46           C  
ANISOU  432  CE2 TYR A  55     5420   4230   4963  -1257    709   -560       C  
ATOM    433  CZ  TYR A  55      15.650  20.845  43.690  1.00 38.62           C  
ANISOU  433  CZ  TYR A  55     5454   4232   4987  -1187    662   -535       C  
ATOM    434  OH  TYR A  55      16.708  21.226  42.906  1.00 45.40           O  
ANISOU  434  OH  TYR A  55     6273   5129   5849  -1101    628   -515       O  
ATOM    435  N   PRO A  56      14.906  18.387  48.004  1.00 40.21           N  
ANISOU  435  N   PRO A  56     5967   4360   4950  -1411    717   -522       N  
ATOM    436  CA  PRO A  56      15.864  18.648  49.084  1.00 40.47           C  
ANISOU  436  CA  PRO A  56     6022   4442   4912  -1413    709   -508       C  
ATOM    437  C   PRO A  56      16.013  20.149  49.332  1.00 40.13           C  
ANISOU  437  C   PRO A  56     5868   4460   4919  -1435    750   -551       C  
ATOM    438  O   PRO A  56      16.453  20.880  48.440  1.00 41.24           O  
ANISOU  438  O   PRO A  56     5924   4626   5119  -1372    736   -557       O  
ATOM    439  CB  PRO A  56      17.179  18.080  48.535  1.00 40.41           C  
ANISOU  439  CB  PRO A  56     6045   4443   4865  -1299    631   -459       C  
ATOM    440  CG  PRO A  56      16.777  17.122  47.456  1.00 42.16           C  
ANISOU  440  CG  PRO A  56     6307   4601   5109  -1257    604   -444       C  
ATOM    441  CD  PRO A  56      15.525  17.696  46.861  1.00 41.89           C  
ANISOU  441  CD  PRO A  56     6202   4552   5161  -1310    653   -488       C  
ATOM    442  N   GLY A  57      15.646  20.598  50.528  1.00 41.20           N  
ANISOU  442  N   GLY A  57     6007   4617   5029  -1527    804   -583       N  
ATOM    443  CA  GLY A  57      15.795  21.992  50.899  1.00 42.91           C  
ANISOU  443  CA  GLY A  57     6126   4887   5290  -1556    850   -630       C  
ATOM    444  C   GLY A  57      14.561  22.805  50.564  1.00 44.11           C  
ANISOU  444  C   GLY A  57     6191   5017   5551  -1612    921   -685       C  
ATOM    445  O   GLY A  57      14.533  24.019  50.762  1.00 46.65           O  
ANISOU  445  O   GLY A  57     6424   5371   5932  -1637    967   -729       O  
ATOM    446  N   GLY A  58      13.536  22.133  50.051  1.00 40.57           N  
ANISOU  446  N   GLY A  58     5767   4513   5136  -1631    929   -682       N  
ATOM    447  CA  GLY A  58      12.288  22.796  49.733  1.00 40.01           C  
ANISOU  447  CA  GLY A  58     5613   4418   5172  -1684    991   -731       C  
ATOM    448  C   GLY A  58      12.414  23.860  48.658  1.00 39.42           C  
ANISOU  448  C   GLY A  58     5420   4357   5201  -1623    984   -739       C  
ATOM    449  O   GLY A  58      13.361  23.854  47.871  1.00 39.04           O  
ANISOU  449  O   GLY A  58     5363   4328   5142  -1533    925   -702       O  
ATOM    450  N   VAL A  59      11.455  24.783  48.644  1.00 39.42           N  
ANISOU  450  N   VAL A  59     5328   4347   5304  -1674   1048   -788       N  
ATOM    451  CA  VAL A  59      11.336  25.778  47.590  1.00 38.98           C  
ANISOU  451  CA  VAL A  59     5158   4292   5359  -1625   1045   -792       C  
ATOM    452  C   VAL A  59      12.460  26.819  47.632  1.00 41.60           C  
ANISOU  452  C   VAL A  59     5433   4672   5700  -1581   1041   -792       C  
ATOM    453  O   VAL A  59      12.870  27.335  46.591  1.00 40.39           O  
ANISOU  453  O   VAL A  59     5220   4527   5599  -1509   1008   -767       O  
ATOM    454  CB  VAL A  59       9.961  26.486  47.640  1.00 41.58           C  
ANISOU  454  CB  VAL A  59     5400   4593   5806  -1693   1116   -843       C  
ATOM    455  CG1 VAL A  59       9.795  27.263  48.955  1.00 39.57           C  
ANISOU  455  CG1 VAL A  59     5120   4355   5560  -1776   1200   -905       C  
ATOM    456  CG2 VAL A  59       9.805  27.420  46.451  1.00 44.42           C  
ANISOU  456  CG2 VAL A  59     5649   4948   6282  -1635   1101   -833       C  
ATOM    457  N   ALA A  60      12.958  27.127  48.827  1.00 38.98           N  
ANISOU  457  N   ALA A  60     5123   4373   5314  -1627   1075   -821       N  
ATOM    458  CA  ALA A  60      14.076  28.058  48.949  1.00 40.44           C  
ANISOU  458  CA  ALA A  60     5258   4606   5501  -1592   1070   -825       C  
ATOM    459  C   ALA A  60      15.326  27.495  48.274  1.00 38.48           C  
ANISOU  459  C   ALA A  60     5050   4383   5186  -1495    985   -765       C  
ATOM    460  O   ALA A  60      15.985  28.183  47.497  1.00 39.51           O  
ANISOU  460  O   ALA A  60     5115   4533   5363  -1431    964   -749       O  
ATOM    461  CB  ALA A  60      14.354  28.396  50.417  1.00 39.27           C  
ANISOU  461  CB  ALA A  60     5133   4493   5294  -1669   1118   -871       C  
ATOM    462  N   GLN A  61      15.650  26.240  48.558  1.00 39.32           N  
ANISOU  462  N   GLN A  61     5264   4487   5189  -1482    938   -729       N  
ATOM    463  CA  GLN A  61      16.795  25.620  47.897  1.00 40.47           C  
ANISOU  463  CA  GLN A  61     5448   4650   5279  -1386    860   -675       C  
ATOM    464  C   GLN A  61      16.532  25.424  46.406  1.00 39.44           C  
ANISOU  464  C   GLN A  61     5289   4490   5206  -1319    827   -646       C  
ATOM    465  O   GLN A  61      17.458  25.461  45.597  1.00 38.65           O  
ANISOU  465  O   GLN A  61     5171   4412   5101  -1236    782   -614       O  
ATOM    466  CB  GLN A  61      17.165  24.285  48.536  1.00 38.88           C  
ANISOU  466  CB  GLN A  61     5368   4442   4962  -1385    817   -641       C  
ATOM    467  CG  GLN A  61      18.514  23.762  48.065  1.00 38.78           C  
ANISOU  467  CG  GLN A  61     5386   4455   4895  -1285    741   -592       C  
ATOM    468  CD  GLN A  61      19.650  24.656  48.510  1.00 43.36           C  
ANISOU  468  CD  GLN A  61     5912   5100   5464  -1267    737   -602       C  
ATOM    469  NE2 GLN A  61      20.575  24.948  47.597  1.00 38.46           N  
ANISOU  469  NE2 GLN A  61     5241   4504   4868  -1181    700   -581       N  
ATOM    470  OE1 GLN A  61      19.687  25.094  49.660  1.00 41.06           O  
ANISOU  470  OE1 GLN A  61     5621   4839   5140  -1335    769   -633       O  
ATOM    471  N   TYR A  62      15.270  25.216  46.045  1.00 38.08           N  
ANISOU  471  N   TYR A  62     5110   4272   5086  -1357    851   -658       N  
ATOM    472  CA  TYR A  62      14.914  25.076  44.638  1.00 37.77           C  
ANISOU  472  CA  TYR A  62     5041   4209   5099  -1303    819   -635       C  
ATOM    473  C   TYR A  62      15.206  26.387  43.892  1.00 37.40           C  
ANISOU  473  C   TYR A  62     4883   4188   5139  -1265    830   -636       C  
ATOM    474  O   TYR A  62      15.706  26.383  42.770  1.00 37.12           O  
ANISOU  474  O   TYR A  62     4831   4163   5112  -1192    787   -602       O  
ATOM    475  CB  TYR A  62      13.442  24.676  44.489  1.00 37.96           C  
ANISOU  475  CB  TYR A  62     5070   4184   5168  -1362    844   -653       C  
ATOM    476  CG  TYR A  62      13.044  24.363  43.067  1.00 40.36           C  
ANISOU  476  CG  TYR A  62     5358   4467   5511  -1313    802   -628       C  
ATOM    477  CD1 TYR A  62      13.253  23.092  42.526  1.00 37.82           C  
ANISOU  477  CD1 TYR A  62     5124   4125   5122  -1273    748   -598       C  
ATOM    478  CD2 TYR A  62      12.456  25.333  42.264  1.00 37.57           C  
ANISOU  478  CD2 TYR A  62     4901   4113   5259  -1307    815   -634       C  
ATOM    479  CE1 TYR A  62      12.894  22.804  41.219  1.00 37.70           C  
ANISOU  479  CE1 TYR A  62     5096   4096   5135  -1233    710   -582       C  
ATOM    480  CE2 TYR A  62      12.099  25.060  40.962  1.00 37.46           C  
ANISOU  480  CE2 TYR A  62     4874   4088   5271  -1265    771   -609       C  
ATOM    481  CZ  TYR A  62      12.315  23.790  40.442  1.00 37.53           C  
ANISOU  481  CZ  TYR A  62     4972   4081   5205  -1231    719   -586       C  
ATOM    482  OH  TYR A  62      11.957  23.518  39.145  1.00 37.49           O  
ANISOU  482  OH  TYR A  62     4955   4069   5218  -1196    676   -567       O  
ATOM    483  N   ILE A  63      14.909  27.512  44.529  1.00 37.47           N  
ANISOU  483  N   ILE A  63     4819   4205   5211  -1318    890   -676       N  
ATOM    484  CA  ILE A  63      15.182  28.806  43.909  1.00 37.21           C  
ANISOU  484  CA  ILE A  63     4681   4188   5267  -1287    905   -676       C  
ATOM    485  C   ILE A  63      16.685  29.029  43.752  1.00 37.01           C  
ANISOU  485  C   ILE A  63     4656   4212   5195  -1222    872   -652       C  
ATOM    486  O   ILE A  63      17.144  29.476  42.701  1.00 36.74           O  
ANISOU  486  O   ILE A  63     4574   4190   5197  -1160    849   -622       O  
ATOM    487  CB  ILE A  63      14.520  29.961  44.687  1.00 39.73           C  
ANISOU  487  CB  ILE A  63     4923   4498   5673  -1361    984   -731       C  
ATOM    488  CG1 ILE A  63      12.999  29.884  44.528  1.00 37.94           C  
ANISOU  488  CG1 ILE A  63     4671   4224   5522  -1410   1014   -751       C  
ATOM    489  CG2 ILE A  63      15.049  31.320  44.203  1.00 37.21           C  
ANISOU  489  CG2 ILE A  63     4505   4196   5439  -1327   1001   -730       C  
ATOM    490  CD1 ILE A  63      12.237  30.542  45.653  1.00 37.99           C  
ANISOU  490  CD1 ILE A  63     4637   4215   5582  -1501   1098   -817       C  
ATOM    491  N   ARG A  64      17.449  28.684  44.786  1.00 37.21           N  
ANISOU  491  N   ARG A  64     4735   4267   5137  -1237    868   -663       N  
ATOM    492  CA  ARG A  64      18.900  28.850  44.739  1.00 39.18           C  
ANISOU  492  CA  ARG A  64     4981   4566   5341  -1179    834   -643       C  
ATOM    493  C   ARG A  64      19.528  28.000  43.651  1.00 37.23           C  
ANISOU  493  C   ARG A  64     4773   4321   5052  -1089    769   -592       C  
ATOM    494  O   ARG A  64      20.413  28.457  42.938  1.00 36.73           O  
ANISOU  494  O   ARG A  64     4665   4287   5003  -1029    751   -572       O  
ATOM    495  CB  ARG A  64      19.544  28.517  46.081  1.00 39.29           C  
ANISOU  495  CB  ARG A  64     5050   4612   5266  -1213    832   -661       C  
ATOM    496  CG  ARG A  64      19.194  29.485  47.173  1.00 44.52           C  
ANISOU  496  CG  ARG A  64     5668   5286   5961  -1300    899   -719       C  
ATOM    497  CD  ARG A  64      19.923  29.160  48.458  1.00 50.50           C  
ANISOU  497  CD  ARG A  64     6484   6088   6618  -1333    888   -732       C  
ATOM    498  NE  ARG A  64      19.209  29.730  49.594  1.00 58.44           N  
ANISOU  498  NE  ARG A  64     7478   7092   7635  -1436    959   -793       N  
ATOM    499  CZ  ARG A  64      18.465  29.026  50.441  1.00 55.92           C  
ANISOU  499  CZ  ARG A  64     7232   6754   7259  -1503    978   -807       C  
ATOM    500  NH1 ARG A  64      17.843  29.639  51.437  1.00 57.10           N1+
ANISOU  500  NH1 ARG A  64     7365   6908   7425  -1598   1051   -869       N1+
ATOM    501  NH2 ARG A  64      18.354  27.712  50.302  1.00 54.93           N  
ANISOU  501  NH2 ARG A  64     7201   6607   7063  -1478    929   -760       N  
ATOM    502  N   ASN A  65      19.080  26.755  43.534  1.00 38.82           N  
ANISOU  502  N   ASN A  65     5060   4491   5201  -1084    738   -574       N  
ATOM    503  CA  ASN A  65      19.608  25.881  42.497  1.00 36.93           C  
ANISOU  503  CA  ASN A  65     4863   4248   4923  -1003    680   -533       C  
ATOM    504  C   ASN A  65      19.286  26.460  41.133  1.00 36.63           C  
ANISOU  504  C   ASN A  65     4757   4204   4956   -968    680   -519       C  
ATOM    505  O   ASN A  65      20.104  26.411  40.219  1.00 36.49           O  
ANISOU  505  O   ASN A  65     4730   4209   4926   -896    649   -492       O  
ATOM    506  CB  ASN A  65      19.057  24.460  42.639  1.00 37.19           C  
ANISOU  506  CB  ASN A  65     4998   4236   4895  -1013    654   -522       C  
ATOM    507  CG  ASN A  65      19.511  23.787  43.922  1.00 39.81           C  
ANISOU  507  CG  ASN A  65     5407   4574   5145  -1037    644   -521       C  
ATOM    508  ND2 ASN A  65      18.847  22.691  44.286  1.00 37.89           N  
ANISOU  508  ND2 ASN A  65     5253   4285   4858  -1070    636   -516       N  
ATOM    509  OD1 ASN A  65      20.458  24.241  44.575  1.00 37.67           O  
ANISOU  509  OD1 ASN A  65     5116   4348   4847  -1028    641   -524       O  
ATOM    510  N   GLY A  66      18.093  27.033  41.019  1.00 36.59           N  
ANISOU  510  N   GLY A  66     4705   4171   5027  -1021    716   -537       N  
ATOM    511  CA  GLY A  66      17.669  27.696  39.802  1.00 36.39           C  
ANISOU  511  CA  GLY A  66     4611   4141   5076   -997    715   -519       C  
ATOM    512  C   GLY A  66      18.628  28.801  39.400  1.00 37.39           C  
ANISOU  512  C   GLY A  66     4662   4306   5238   -956    725   -506       C  
ATOM    513  O   GLY A  66      19.020  28.883  38.237  1.00 36.09           O  
ANISOU  513  O   GLY A  66     4479   4156   5077   -898    698   -472       O  
ATOM    514  N   HIS A  67      19.005  29.649  40.356  1.00 36.26           N  
ANISOU  514  N   HIS A  67     4477   4181   5119   -991    766   -535       N  
ATOM    515  CA  HIS A  67      19.957  30.724  40.082  1.00 36.15           C  
ANISOU  515  CA  HIS A  67     4391   4202   5142   -960    780   -527       C  
ATOM    516  C   HIS A  67      21.269  30.120  39.598  1.00 36.10           C  
ANISOU  516  C   HIS A  67     4421   4235   5060   -885    734   -498       C  
ATOM    517  O   HIS A  67      21.838  30.559  38.597  1.00 35.99           O  
ANISOU  517  O   HIS A  67     4366   4241   5066   -834    725   -470       O  
ATOM    518  CB  HIS A  67      20.199  31.591  41.332  1.00 36.30           C  
ANISOU  518  CB  HIS A  67     4369   4235   5186  -1017    830   -573       C  
ATOM    519  CG  HIS A  67      19.079  32.539  41.642  1.00 36.39           C  
ANISOU  519  CG  HIS A  67     4316   4210   5300  -1082    888   -605       C  
ATOM    520  CD2 HIS A  67      18.388  33.392  40.847  1.00 36.34           C  
ANISOU  520  CD2 HIS A  67     4237   4174   5397  -1080    909   -592       C  
ATOM    521  ND1 HIS A  67      18.549  32.682  42.907  1.00 36.64           N  
ANISOU  521  ND1 HIS A  67     4354   4230   5336  -1159    934   -658       N  
ATOM    522  CE1 HIS A  67      17.578  33.580  42.878  1.00 36.73           C  
ANISOU  522  CE1 HIS A  67     4295   4205   5456  -1200    985   -681       C  
ATOM    523  NE2 HIS A  67      17.457  34.023  41.640  1.00 38.18           N  
ANISOU  523  NE2 HIS A  67     4428   4375   5704  -1151    968   -639       N  
ATOM    524  N   GLU A  68      21.739  29.098  40.305  1.00 36.25           N  
ANISOU  524  N   GLU A  68     4516   4264   4993   -878    706   -504       N  
ATOM    525  CA  GLU A  68      22.998  28.456  39.943  1.00 36.29           C  
ANISOU  525  CA  GLU A  68     4555   4304   4932   -803    662   -480       C  
ATOM    526  C   GLU A  68      22.947  27.840  38.544  1.00 36.20           C  
ANISOU  526  C   GLU A  68     4566   4281   4907   -742    629   -447       C  
ATOM    527  O   GLU A  68      23.881  27.995  37.754  1.00 36.17           O  
ANISOU  527  O   GLU A  68     4538   4309   4896   -681    617   -427       O  
ATOM    528  CB  GLU A  68      23.385  27.388  40.967  1.00 36.57           C  
ANISOU  528  CB  GLU A  68     4674   4342   4881   -806    632   -486       C  
ATOM    529  CG  GLU A  68      24.707  26.723  40.633  1.00 41.80           C  
ANISOU  529  CG  GLU A  68     5361   5035   5484   -723    586   -463       C  
ATOM    530  CD  GLU A  68      25.191  25.781  41.716  1.00 47.13           C  
ANISOU  530  CD  GLU A  68     6111   5715   6082   -722    553   -462       C  
ATOM    531  OE1 GLU A  68      24.366  25.338  42.547  1.00 48.56           O  
ANISOU  531  OE1 GLU A  68     6347   5864   6238   -782    559   -472       O  
ATOM    532  OE2 GLU A  68      26.404  25.493  41.739  1.00 45.07           O1-
ANISOU  532  OE2 GLU A  68     5850   5489   5784   -662    519   -449       O1-
ATOM    533  N   LEU A  69      21.858  27.139  38.243  1.00 36.21           N  
ANISOU  533  N   LEU A  69     4616   4238   4904   -762    618   -444       N  
ATOM    534  CA  LEU A  69      21.720  26.464  36.954  1.00 36.20           C  
ANISOU  534  CA  LEU A  69     4646   4226   4883   -713    585   -420       C  
ATOM    535  C   LEU A  69      21.465  27.442  35.808  1.00 43.09           C  
ANISOU  535  C   LEU A  69     5443   5110   5817   -702    598   -399       C  
ATOM    536  O   LEU A  69      21.986  27.266  34.708  1.00 46.94           O  
ANISOU  536  O   LEU A  69     5934   5619   6283   -646    577   -376       O  
ATOM    537  CB  LEU A  69      20.617  25.404  37.014  1.00 36.33           C  
ANISOU  537  CB  LEU A  69     4736   4193   4876   -745    568   -427       C  
ATOM    538  CG  LEU A  69      20.952  24.273  37.986  1.00 38.76           C  
ANISOU  538  CG  LEU A  69     5132   4484   5113   -746    549   -436       C  
ATOM    539  CD1 LEU A  69      19.825  23.254  38.075  1.00 39.96           C  
ANISOU  539  CD1 LEU A  69     5357   4581   5247   -786    539   -444       C  
ATOM    540  CD2 LEU A  69      22.258  23.606  37.564  1.00 36.71           C  
ANISOU  540  CD2 LEU A  69     4906   4247   4794   -662    514   -418       C  
ATOM    541  N   LEU A  70      20.665  28.471  36.068  1.00 37.85           N  
ANISOU  541  N   LEU A  70     4715   4433   5234   -756    633   -407       N  
ATOM    542  CA  LEU A  70      20.373  29.470  35.052  1.00 39.21           C  
ANISOU  542  CA  LEU A  70     4814   4611   5473   -748    644   -380       C  
ATOM    543  C   LEU A  70      21.665  30.154  34.626  1.00 46.02           C  
ANISOU  543  C   LEU A  70     5633   5519   6335   -700    653   -361       C  
ATOM    544  O   LEU A  70      21.894  30.385  33.437  1.00 52.53           O  
ANISOU  544  O   LEU A  70     6437   6361   7160   -661    641   -327       O  
ATOM    545  CB  LEU A  70      19.326  30.473  35.550  1.00 35.91           C  
ANISOU  545  CB  LEU A  70     4329   4163   5153   -812    684   -395       C  
ATOM    546  CG  LEU A  70      17.897  29.911  35.543  1.00 36.02           C  
ANISOU  546  CG  LEU A  70     4368   4134   5185   -855    674   -405       C  
ATOM    547  CD1 LEU A  70      16.955  30.730  36.407  1.00 36.76           C  
ANISOU  547  CD1 LEU A  70     4403   4196   5368   -924    722   -436       C  
ATOM    548  CD2 LEU A  70      17.368  29.810  34.124  1.00 36.10           C  
ANISOU  548  CD2 LEU A  70     4370   4142   5205   -827    637   -367       C  
ATOM    549  N   ALA A  71      22.520  30.457  35.596  1.00 42.27           N  
ANISOU  549  N   ALA A  71     5143   5066   5853   -706    674   -384       N  
ATOM    550  CA  ALA A  71      23.845  30.965  35.283  1.00 41.63           C  
ANISOU  550  CA  ALA A  71     5023   5030   5764   -661    681   -372       C  
ATOM    551  C   ALA A  71      24.654  29.902  34.525  1.00 46.39           C  
ANISOU  551  C   ALA A  71     5683   5658   6285   -591    642   -355       C  
ATOM    552  O   ALA A  71      25.221  30.170  33.470  1.00 45.66           O  
ANISOU  552  O   ALA A  71     5566   5593   6191   -548    641   -329       O  
ATOM    553  CB  ALA A  71      24.566  31.404  36.555  1.00 37.19           C  
ANISOU  553  CB  ALA A  71     4435   4489   5204   -687    705   -406       C  
ATOM    554  N   ARG A  72      24.689  28.685  35.053  1.00 50.61           N  
ANISOU  554  N   ARG A  72     6295   6180   6754   -580    611   -371       N  
ATOM    555  CA  ARG A  72      25.440  27.614  34.407  1.00 49.35           C  
ANISOU  555  CA  ARG A  72     6191   6034   6525   -512    577   -362       C  
ATOM    556  C   ARG A  72      25.040  27.438  32.940  1.00 50.90           C  
ANISOU  556  C   ARG A  72     6397   6227   6715   -485    566   -337       C  
ATOM    557  O   ARG A  72      25.902  27.363  32.063  1.00 45.91           O  
ANISOU  557  O   ARG A  72     5758   5628   6056   -430    563   -324       O  
ATOM    558  CB  ARG A  72      25.264  26.296  35.167  1.00 51.88           C  
ANISOU  558  CB  ARG A  72     6602   6325   6787   -511    545   -377       C  
ATOM    559  CG  ARG A  72      25.922  25.096  34.499  1.00 56.89           C  
ANISOU  559  CG  ARG A  72     7298   6958   7357   -440    511   -371       C  
ATOM    560  CD  ARG A  72      25.829  23.865  35.389  1.00 61.72           C  
ANISOU  560  CD  ARG A  72     7997   7534   7919   -440    482   -382       C  
ATOM    561  NE  ARG A  72      26.461  24.103  36.683  1.00 67.78           N  
ANISOU  561  NE  ARG A  72     8751   8322   8681   -454    482   -390       N  
ATOM    562  CZ  ARG A  72      26.204  23.403  37.783  1.00 71.96           C  
ANISOU  562  CZ  ARG A  72     9341   8823   9175   -482    465   -395       C  
ATOM    563  NH1 ARG A  72      25.317  22.416  37.750  1.00 71.27           N1+
ANISOU  563  NH1 ARG A  72     9334   8682   9065   -500    450   -395       N1+
ATOM    564  NH2 ARG A  72      26.829  23.695  38.917  1.00 71.25           N  
ANISOU  564  NH2 ARG A  72     9236   8762   9074   -496    462   -401       N  
ATOM    565  N   GLU A  73      23.736  27.376  32.673  1.00 50.72           N  
ANISOU  565  N   GLU A  73     6388   6167   6714   -527    560   -333       N  
ATOM    566  CA  GLU A  73      23.259  27.140  31.309  1.00 54.99           C  
ANISOU  566  CA  GLU A  73     6944   6708   7241   -509    541   -311       C  
ATOM    567  C   GLU A  73      23.439  28.356  30.388  1.00 55.95           C  
ANISOU  567  C   GLU A  73     6990   6861   7407   -502    561   -277       C  
ATOM    568  O   GLU A  73      23.325  28.237  29.166  1.00 56.73           O  
ANISOU  568  O   GLU A  73     7099   6975   7481   -479    545   -253       O  
ATOM    569  CB  GLU A  73      21.806  26.636  31.298  1.00 56.39           C  
ANISOU  569  CB  GLU A  73     7157   6839   7428   -556    521   -318       C  
ATOM    570  CG  GLU A  73      20.752  27.724  31.210  1.00 62.31           C  
ANISOU  570  CG  GLU A  73     7838   7576   8261   -608    538   -303       C  
ATOM    571  CD  GLU A  73      20.520  28.202  29.789  1.00 61.80           C  
ANISOU  571  CD  GLU A  73     7742   7532   8206   -590    523   -264       C  
ATOM    572  OE1 GLU A  73      20.667  27.388  28.854  1.00 62.03           O  
ANISOU  572  OE1 GLU A  73     7824   7575   8170   -557    493   -259       O  
ATOM    573  OE2 GLU A  73      20.195  29.393  29.611  1.00 58.53           O1-
ANISOU  573  OE2 GLU A  73     7253   7120   7865   -610    543   -237       O1-
ATOM    574  N   SER A  74      23.732  29.517  30.968  1.00 49.11           N  
ANISOU  574  N   SER A  74     6052   6005   6603   -523    597   -273       N  
ATOM    575  CA  SER A  74      24.031  30.693  30.159  1.00 53.66           C  
ANISOU  575  CA  SER A  74     6558   6607   7225   -516    620   -237       C  
ATOM    576  C   SER A  74      25.462  30.611  29.619  1.00 58.19           C  
ANISOU  576  C   SER A  74     7129   7231   7751   -458    629   -231       C  
ATOM    577  O   SER A  74      25.859  31.403  28.765  1.00 59.03           O  
ANISOU  577  O   SER A  74     7190   7363   7875   -445    648   -197       O  
ATOM    578  CB  SER A  74      23.836  31.985  30.962  1.00 55.92           C  
ANISOU  578  CB  SER A  74     6765   6878   7602   -562    661   -240       C  
ATOM    579  OG  SER A  74      24.957  32.260  31.788  1.00 54.67           O  
ANISOU  579  OG  SER A  74     6584   6746   7443   -554    686   -265       O  
ATOM    580  N   GLU A  75      26.227  29.644  30.122  1.00 59.94           N  
ANISOU  580  N   GLU A  75     7397   7463   7915   -425    615   -261       N  
ATOM    581  CA  GLU A  75      27.614  29.449  29.698  1.00 62.69           C  
ANISOU  581  CA  GLU A  75     7740   7857   8222   -366    623   -263       C  
ATOM    582  C   GLU A  75      27.726  28.331  28.655  1.00 66.85           C  
ANISOU  582  C   GLU A  75     8334   8391   8675   -319    598   -262       C  
ATOM    583  O   GLU A  75      26.753  27.631  28.374  1.00 65.21           O  
ANISOU  583  O   GLU A  75     8183   8151   8444   -333    569   -264       O  
ATOM    584  CB  GLU A  75      28.498  29.114  30.905  1.00 62.13           C  
ANISOU  584  CB  GLU A  75     7670   7796   8139   -352    621   -295       C  
ATOM    585  CG  GLU A  75      28.326  30.038  32.110  1.00 64.10           C  
ANISOU  585  CG  GLU A  75     7868   8038   8450   -407    644   -309       C  
ATOM    586  CD  GLU A  75      29.029  31.379  31.943  1.00 63.32           C  
ANISOU  586  CD  GLU A  75     7680   7973   8407   -415    686   -298       C  
ATOM    587  OE1 GLU A  75      28.772  32.291  32.763  1.00 58.19           O  
ANISOU  587  OE1 GLU A  75     6981   7311   7818   -467    712   -310       O  
ATOM    588  OE2 GLU A  75      29.844  31.516  31.003  1.00 60.95           O1-
ANISOU  588  OE2 GLU A  75     7358   7708   8091   -373    698   -280       O1-
ATOM    589  N   GLU A  76      28.919  28.164  28.089  1.00 71.38           N  
ANISOU  589  N   GLU A  76     8900   9006   9214   -264    611   -265       N  
ATOM    590  CA  GLU A  76      29.168  27.105  27.111  1.00 73.15           C  
ANISOU  590  CA  GLU A  76     9186   9239   9368   -216    595   -274       C  
ATOM    591  C   GLU A  76      29.550  25.797  27.794  1.00 63.60           C  
ANISOU  591  C   GLU A  76     8039   8006   8120   -179    569   -311       C  
ATOM    592  O   GLU A  76      30.543  25.736  28.518  1.00 64.39           O  
ANISOU  592  O   GLU A  76     8115   8122   8226   -148    574   -326       O  
ATOM    593  CB  GLU A  76      30.285  27.511  26.146  1.00 83.00           C  
ANISOU  593  CB  GLU A  76    10395  10543  10599   -175    629   -263       C  
ATOM    594  CG  GLU A  76      29.940  28.661  25.214  1.00 95.75           C  
ANISOU  594  CG  GLU A  76    11963  12180  12236   -207    653   -218       C  
ATOM    595  CD  GLU A  76      31.101  29.045  24.307  1.00105.79           C  
ANISOU  595  CD  GLU A  76    13200  13509  13486   -171    694   -208       C  
ATOM    596  OE1 GLU A  76      32.229  28.553  24.536  1.00108.62           O  
ANISOU  596  OE1 GLU A  76    13553  13890  13826   -123    707   -240       O  
ATOM    597  OE2 GLU A  76      30.885  29.839  23.365  1.00108.06           O1-
ANISOU  597  OE2 GLU A  76    13463  13818  13777   -191    713   -166       O1-
ATOM    598  N   VAL A  77      28.766  24.748  27.571  1.00101.14           N  
ANISOU  598  N   VAL A  77    14430   6027  17969  -1481  -2813   -552       N  
ATOM    599  CA  VAL A  77      29.154  23.434  28.060  1.00 94.40           C  
ANISOU  599  CA  VAL A  77    13196   5721  16952  -1485  -2452   -634       C  
ATOM    600  C   VAL A  77      30.404  22.999  27.316  1.00 93.88           C  
ANISOU  600  C   VAL A  77    13153   5793  16726  -1916  -2166   -334       C  
ATOM    601  O   VAL A  77      30.420  22.956  26.085  0.84 98.04           O  
ANISOU  601  O   VAL A  77    13914   6221  17115  -2092  -2144    -31       O  
ATOM    602  CB  VAL A  77      28.055  22.367  27.852  1.00 84.04           C  
ANISOU  602  CB  VAL A  77    11732   4721  15478  -1173  -2377   -681       C  
ATOM    603  CG1 VAL A  77      28.608  20.978  28.143  1.00 73.20           C  
ANISOU  603  CG1 VAL A  77    10017   3876  13921  -1249  -2001   -689       C  
ATOM    604  CG2 VAL A  77      26.851  22.655  28.732  0.86 80.65           C  
ANISOU  604  CG2 VAL A  77    11198   4253  15191   -745  -2615  -1033       C  
ATOM    605  N   ASP A  78      31.457  22.691  28.061  1.00 87.02           N  
ANISOU  605  N   ASP A  78    12033   5158  15872  -2097  -1950   -425       N  
ATOM    606  CA  ASP A  78      32.662  22.149  27.456  0.70 86.30           C  
ANISOU  606  CA  ASP A  78    11890   5265  15635  -2481  -1648   -192       C  
ATOM    607  C   ASP A  78      33.435  21.330  28.476  1.00 82.14           C  
ANISOU  607  C   ASP A  78    10956   5145  15107  -2509  -1393   -371       C  
ATOM    608  O   ASP A  78      33.432  21.638  29.667  1.00 81.24           O  
ANISOU  608  O   ASP A  78    10684   5040  15142  -2380  -1485   -636       O  
ATOM    609  CB  ASP A  78      33.541  23.266  26.889  0.69 92.26           C  
ANISOU  609  CB  ASP A  78    12949   5651  16453  -2874  -1744     15       C  
ATOM    610  CG  ASP A  78      34.473  23.854  27.925  0.51 95.02           C  
ANISOU  610  CG  ASP A  78    13179   5954  16971  -3026  -1749   -153       C  
ATOM    611  OD1 ASP A  78      34.013  24.691  28.729  0.57 99.83           O  
ANISOU  611  OD1 ASP A  78    13844   6310  17778  -2836  -2011   -371       O  
ATOM    612  OD2 ASP A  78      35.666  23.481  27.932  0.86 92.80           O1-
ANISOU  612  OD2 ASP A  78    12739   5893  16627  -3336  -1492    -78       O1-
ATOM    613  N   PHE A  79      34.081  20.274  28.000  1.00 78.29           N  
ANISOU  613  N   PHE A  79    10297   4994  14455  -2677  -1081   -232       N  
ATOM    614  CA  PHE A  79      34.915  19.446  28.852  1.00 73.94           C  
ANISOU  614  CA  PHE A  79     9366   4821  13906  -2732   -842   -364       C  
ATOM    615  C   PHE A  79      36.368  19.697  28.489  1.00 75.87           C  
ANISOU  615  C   PHE A  79     9617   5057  14155  -3167   -673   -207       C  
ATOM    616  O   PHE A  79      36.663  20.193  27.403  1.00 79.72           O  
ANISOU  616  O   PHE A  79    10377   5338  14575  -3429   -676     32       O  
ATOM    617  CB  PHE A  79      34.586  17.967  28.647  1.00 69.19           C  
ANISOU  617  CB  PHE A  79     8526   4627  13136  -2578   -614   -352       C  
ATOM    618  CG  PHE A  79      33.126  17.636  28.786  1.00 67.06           C  
ANISOU  618  CG  PHE A  79     8269   4393  12818  -2185   -755   -469       C  
ATOM    619  CD1 PHE A  79      32.651  16.998  29.922  1.00 67.49           C  
ANISOU  619  CD1 PHE A  79     8037   4716  12892  -1917   -755   -724       C  
ATOM    620  CD2 PHE A  79      32.232  17.940  27.773  1.00 68.55           C  
ANISOU  620  CD2 PHE A  79     8751   4365  12932  -2099   -889   -320       C  
ATOM    621  CE1 PHE A  79      31.305  16.674  30.049  1.00 66.34           C  
ANISOU  621  CE1 PHE A  79     7886   4633  12686  -1573   -874   -842       C  
ATOM    622  CE2 PHE A  79      30.883  17.619  27.895  1.00 69.84           C  
ANISOU  622  CE2 PHE A  79     8907   4580  13050  -1736  -1017   -436       C  
ATOM    623  CZ  PHE A  79      30.422  16.985  29.035  1.00 66.73           C  
ANISOU  623  CZ  PHE A  79     8215   4468  12672  -1475  -1002   -705       C  
ATOM    624  N   ALA A  80      37.277  19.359  29.397  1.00 76.20           N  
ANISOU  624  N   ALA A  80     9354   5333  14265  -3258   -533   -341       N  
ATOM    625  CA  ALA A  80      38.702  19.508  29.131  1.00 83.39           C  
ANISOU  625  CA  ALA A  80    10212   6289  15182  -3666   -354   -221       C  
ATOM    626  C   ALA A  80      39.207  18.349  28.276  1.00 84.77           C  
ANISOU  626  C   ALA A  80    10231   6786  15192  -3799    -39    -69       C  
ATOM    627  O   ALA A  80      40.265  18.439  27.650  1.00 89.56           O  
ANISOU  627  O   ALA A  80    10847   7426  15757  -4159    130     74       O  
ATOM    628  CB  ALA A  80      39.483  19.589  30.434  1.00 83.78           C  
ANISOU  628  CB  ALA A  80     9986   6471  15377  -3709   -337   -426       C  
ATOM    629  N   ALA A  81      38.440  17.264  28.253  1.00 77.10           N  
ANISOU  629  N   ALA A  81     9113   6055  14125  -3514     39   -115       N  
ATOM    630  CA  ALA A  81      38.825  16.072  27.509  1.00 78.94           C  
ANISOU  630  CA  ALA A  81     9177   6601  14215  -3595    331     -7       C  
ATOM    631  C   ALA A  81      37.618  15.200  27.169  1.00 76.61           C  
ANISOU  631  C   ALA A  81     8888   6430  13790  -3277    333     -5       C  
ATOM    632  O   ALA A  81      36.682  15.069  27.961  1.00 69.77           O  
ANISOU  632  O   ALA A  81     7964   5583  12962  -2950    178   -168       O  
ATOM    633  CB  ALA A  81      39.858  15.268  28.291  1.00 78.20           C  
ANISOU  633  CB  ALA A  81     8680   6840  14194  -3658    530   -128       C  
ATOM    634  N   LEU A  82      37.653  14.605  25.982  1.00 76.52           N  
ANISOU  634  N   LEU A  82     8941   6519  13616  -3392    516    170       N  
ATOM    635  CA  LEU A  82      36.567  13.766  25.509  1.00 77.35           C  
ANISOU  635  CA  LEU A  82     9069   6743  13577  -3134    538    197       C  
ATOM    636  C   LEU A  82      37.113  12.722  24.536  1.00 75.00           C  
ANISOU  636  C   LEU A  82     8657   6708  13132  -3302    849    318       C  
ATOM    637  O   LEU A  82      37.732  13.067  23.527  1.00 72.65           O  
ANISOU  637  O   LEU A  82     8513   6337  12755  -3628    960    489       O  
ATOM    638  CB  LEU A  82      35.498  14.632  24.838  1.00 79.60           C  
ANISOU  638  CB  LEU A  82     9743   6697  13805  -3054    295    312       C  
ATOM    639  CG  LEU A  82      34.110  14.009  24.676  1.00 77.01           C  
ANISOU  639  CG  LEU A  82     9449   6444  13368  -2705    218    282       C  
ATOM    640  CD1 LEU A  82      33.070  15.085  24.391  1.00 80.20           C  
ANISOU  640  CD1 LEU A  82    10199   6478  13795  -2577    -99    330       C  
ATOM    641  CD2 LEU A  82      34.125  12.965  23.582  1.00 74.02           C  
ANISOU  641  CD2 LEU A  82     9044   6291  12788  -2787    467    431       C  
ATOM    642  N   GLU A  83      36.892  11.447  24.846  1.00 72.06           N  
ANISOU  642  N   GLU A  83     8014   6643  12721  -3093    987    221       N  
ATOM    643  CA  GLU A  83      37.398  10.364  24.006  1.00 71.03           C  
ANISOU  643  CA  GLU A  83     7741   6773  12475  -3219   1284    295       C  
ATOM    644  C   GLU A  83      36.612   9.066  24.192  1.00 66.29           C  
ANISOU  644  C   GLU A  83     6967   6422  11799  -2910   1346    215       C  
ATOM    645  O   GLU A  83      35.567   9.045  24.843  1.00 65.72           O  
ANISOU  645  O   GLU A  83     6920   6320  11729  -2612   1156    124       O  
ATOM    646  CB  GLU A  83      38.884  10.123  24.284  1.00 74.81           C  
ANISOU  646  CB  GLU A  83     7941   7418  13066  -3467   1486    242       C  
ATOM    647  CG  GLU A  83      39.168   9.499  25.643  1.00 76.22           C  
ANISOU  647  CG  GLU A  83     7771   7790  13399  -3274   1470     45       C  
ATOM    648  CD  GLU A  83      40.651   9.436  25.957  1.00 77.37           C  
ANISOU  648  CD  GLU A  83     7654   8064  13679  -3524   1627     -6       C  
ATOM    649  OE1 GLU A  83      41.045   8.622  26.819  1.00 77.79           O  
ANISOU  649  OE1 GLU A  83     7382   8336  13840  -3403   1675   -138       O  
ATOM    650  OE2 GLU A  83      41.423  10.202  25.344  1.00 76.35           O1-
ANISOU  650  OE2 GLU A  83     7645   7819  13545  -3851   1694     89       O1-
ATOM    651  N   MET A  84      37.121   7.984  23.609  1.00 61.98           N  
ANISOU  651  N   MET A  84     6241   6125  11184  -2992   1612    239       N  
ATOM    652  CA  MET A  84      36.449   6.689  23.667  1.00 60.61           C  
ANISOU  652  CA  MET A  84     5915   6183  10930  -2734   1687    179       C  
ATOM    653  C   MET A  84      36.455   6.123  25.083  1.00 58.46           C  
ANISOU  653  C   MET A  84     5353   6064  10794  -2506   1607     -4       C  
ATOM    654  O   MET A  84      37.459   6.221  25.789  1.00 63.84           O  
ANISOU  654  O   MET A  84     5827   6797  11634  -2614   1637    -83       O  
ATOM    655  CB  MET A  84      37.133   5.700  22.715  1.00 60.38           C  
ANISOU  655  CB  MET A  84     5749   6370  10823  -2899   1996    228       C  
ATOM    656  CG  MET A  84      36.404   4.374  22.539  1.00 63.18           C  
ANISOU  656  CG  MET A  84     5999   6935  11072  -2663   2082    193       C  
ATOM    657  SD  MET A  84      34.844   4.568  21.653  1.00 82.60           S  
ANISOU  657  SD  MET A  84     8817   9271  13297  -2524   1962    324       S  
ATOM    658  CE  MET A  84      35.312   5.841  20.480  1.00 86.37           C  
ANISOU  658  CE  MET A  84     9615   9504  13698  -2901   1979    519       C  
ATOM    659  N   PRO A  85      35.326   5.542  25.510  1.00 55.32           N  
ANISOU  659  N   PRO A  85     4944   5750  10325  -2205   1497    -69       N  
ATOM    660  CA  PRO A  85      35.308   4.773  26.757  1.00 53.41           C  
ANISOU  660  CA  PRO A  85     4419   5705  10170  -2014   1445   -227       C  
ATOM    661  C   PRO A  85      36.225   3.561  26.639  1.00 58.14           C  
ANISOU  661  C   PRO A  85     4731   6542  10816  -2084   1675   -242       C  
ATOM    662  O   PRO A  85      36.159   2.840  25.640  1.00 60.11           O  
ANISOU  662  O   PRO A  85     5004   6879  10957  -2114   1853   -166       O  
ATOM    663  CB  PRO A  85      33.854   4.301  26.857  1.00 49.57           C  
ANISOU  663  CB  PRO A  85     4019   5278   9538  -1727   1327   -258       C  
ATOM    664  CG  PRO A  85      33.081   5.286  26.055  1.00 52.67           C  
ANISOU  664  CG  PRO A  85     4751   5427   9833  -1735   1217   -157       C  
ATOM    665  CD  PRO A  85      33.982   5.671  24.921  1.00 53.97           C  
ANISOU  665  CD  PRO A  85     5033   5487   9988  -2041   1386     -2       C  
ATOM    666  N   PRO A  86      37.068   3.332  27.654  1.00 61.33           N  
ANISOU  666  N   PRO A  86     4958   7625  10720  -1499    -59   -123       N  
ATOM    667  CA  PRO A  86      37.985   2.188  27.669  1.00 62.39           C  
ANISOU  667  CA  PRO A  86     4895   7852  10960  -1407   -123   -152       C  
ATOM    668  C   PRO A  86      37.266   0.837  27.659  1.00 58.15           C  
ANISOU  668  C   PRO A  86     4481   7366  10249  -1232   -184   -104       C  
ATOM    669  O   PRO A  86      37.791  -0.123  27.099  1.00 54.89           O  
ANISOU  669  O   PRO A  86     3954   7007   9894  -1138   -136    -95       O  
ATOM    670  CB  PRO A  86      38.746   2.367  28.989  1.00 67.87           C  
ANISOU  670  CB  PRO A  86     5443   8572  11771  -1458   -366   -256       C  
ATOM    671  CG  PRO A  86      38.609   3.822  29.319  1.00 68.97           C  
ANISOU  671  CG  PRO A  86     5634   8626  11948  -1621   -354   -291       C  
ATOM    672  CD  PRO A  86      37.250   4.204  28.827  1.00 63.62           C  
ANISOU  672  CD  PRO A  86     5229   7880  11065  -1607   -230   -207       C  
ATOM    673  N   LEU A  87      36.083   0.768  28.263  1.00 48.82           N  
ANISOU  673  N   LEU A  87     3525   6163   8863  -1194   -283    -78       N  
ATOM    674  CA  LEU A  87      35.395  -0.503  28.441  1.00 47.41           C  
ANISOU  674  CA  LEU A  87     3462   6025   8527  -1044   -367    -38       C  
ATOM    675  C   LEU A  87      34.175  -0.617  27.534  1.00 49.37           C  
ANISOU  675  C   LEU A  87     3921   6241   8598   -996   -208     44       C  
ATOM    676  O   LEU A  87      33.047  -0.363  27.950  1.00 52.36           O  
ANISOU  676  O   LEU A  87     4497   6589   8809   -996   -251     66       O  
ATOM    677  CB  LEU A  87      34.985  -0.677  29.906  1.00 47.04           C  
ANISOU  677  CB  LEU A  87     3505   5993   8376  -1027   -614    -72       C  
ATOM    678  CG  LEU A  87      36.143  -0.613  30.910  1.00 53.02           C  
ANISOU  678  CG  LEU A  87     4068   6790   9288  -1063   -809   -159       C  
ATOM    679  CD1 LEU A  87      35.636  -0.588  32.346  1.00 53.38           C  
ANISOU  679  CD1 LEU A  87     4236   6845   9199  -1059  -1039   -190       C  
ATOM    680  CD2 LEU A  87      37.114  -1.772  30.697  1.00 53.73           C  
ANISOU  680  CD2 LEU A  87     3970   6943   9503   -956   -853   -168       C  
ATOM    681  N   ILE A  88      34.413  -0.993  26.285  1.00 45.66           N  
ANISOU  681  N   ILE A  88     3402   5781   8165   -951    -23     82       N  
ATOM    682  CA  ILE A  88      33.340  -1.182  25.327  1.00 44.11           C  
ANISOU  682  CA  ILE A  88     3390   5563   7805   -894    124    153       C  
ATOM    683  C   ILE A  88      33.405  -2.607  24.795  1.00 45.09           C  
ANISOU  683  C   ILE A  88     3491   5737   7904   -752    140    170       C  
ATOM    684  O   ILE A  88      34.472  -3.087  24.417  1.00 45.31           O  
ANISOU  684  O   ILE A  88     3333   5804   8079   -721    180    142       O  
ATOM    685  CB  ILE A  88      33.443  -0.168  24.180  1.00 46.17           C  
ANISOU  685  CB  ILE A  88     3656   5780   8108   -978    356    189       C  
ATOM    686  CG1 ILE A  88      33.153   1.238  24.710  1.00 53.99           C  
ANISOU  686  CG1 ILE A  88     4715   6698   9102  -1110    336    179       C  
ATOM    687  CG2 ILE A  88      32.476  -0.505  23.068  1.00 45.92           C  
ANISOU  687  CG2 ILE A  88     3793   5740   7914   -899    505    259       C  
ATOM    688  CD1 ILE A  88      33.252   2.312  23.661  1.00 60.67           C  
ANISOU  688  CD1 ILE A  88     5580   7482   9990  -1201    555    224       C  
ATOM    689  N   PHE A  89      32.266  -3.284  24.782  1.00 42.14           N  
ANISOU  689  N   PHE A  89     3302   5360   7351   -667    107    208       N  
ATOM    690  CA  PHE A  89      32.222  -4.690  24.409  1.00 46.79           C  
ANISOU  690  CA  PHE A  89     3890   5982   7908   -532     96    218       C  
ATOM    691  C   PHE A  89      31.171  -4.944  23.340  1.00 45.24           C  
ANISOU  691  C   PHE A  89     3862   5770   7558   -476    239    268       C  
ATOM    692  O   PHE A  89      30.054  -4.440  23.427  1.00 48.04           O  
ANISOU  692  O   PHE A  89     4389   6092   7770   -505    243    299       O  
ATOM    693  CB  PHE A  89      31.963  -5.548  25.649  1.00 44.16           C  
ANISOU  693  CB  PHE A  89     3599   5660   7522   -471   -131    207       C  
ATOM    694  CG  PHE A  89      32.897  -5.239  26.782  1.00 48.09           C  
ANISOU  694  CG  PHE A  89     3952   6176   8144   -524   -296    156       C  
ATOM    695  CD1 PHE A  89      34.146  -5.847  26.856  1.00 50.63           C  
ANISOU  695  CD1 PHE A  89     4065   6536   8637   -474   -351    115       C  
ATOM    696  CD2 PHE A  89      32.550  -4.309  27.750  1.00 43.86           C  
ANISOU  696  CD2 PHE A  89     3482   5621   7562   -619   -396    140       C  
ATOM    697  CE1 PHE A  89      35.016  -5.550  27.889  1.00 46.77           C  
ANISOU  697  CE1 PHE A  89     3436   6069   8266   -519   -517     61       C  
ATOM    698  CE2 PHE A  89      33.417  -4.007  28.785  1.00 47.83           C  
ANISOU  698  CE2 PHE A  89     3855   6144   8174   -668   -557     83       C  
ATOM    699  CZ  PHE A  89      34.652  -4.627  28.855  1.00 46.96           C  
ANISOU  699  CZ  PHE A  89     3535   6075   8232   -619   -622     44       C  
ATOM    700  N   GLU A  90      31.547  -5.712  22.323  1.00 41.18           N  
ANISOU  700  N   GLU A  90     3292   5280   7076   -392    354    268       N  
ATOM    701  CA  GLU A  90      30.642  -6.056  21.234  1.00 44.23           C  
ANISOU  701  CA  GLU A  90     3827   5660   7320   -329    483    304       C  
ATOM    702  C   GLU A  90      29.861  -7.315  21.577  1.00 46.01           C  
ANISOU  702  C   GLU A  90     4160   5884   7440   -224    363    306       C  
ATOM    703  O   GLU A  90      30.451  -8.359  21.857  1.00 46.58           O  
ANISOU  703  O   GLU A  90     4139   5971   7588   -145    279    278       O  
ATOM    704  CB  GLU A  90      31.429  -6.293  19.943  1.00 51.33           C  
ANISOU  704  CB  GLU A  90     4620   6589   8293   -287    672    295       C  
ATOM    705  CG  GLU A  90      31.926  -5.028  19.263  1.00 64.65           C  
ANISOU  705  CG  GLU A  90     6254   8269  10041   -393    849    315       C  
ATOM    706  CD  GLU A  90      30.843  -4.340  18.450  1.00 75.46           C  
ANISOU  706  CD  GLU A  90     7822   9606  11242   -413    972    374       C  
ATOM    707  OE1 GLU A  90      29.745  -4.922  18.303  1.00 79.89           O  
ANISOU  707  OE1 GLU A  90     8545  10163  11648   -337    930    388       O  
ATOM    708  OE2 GLU A  90      31.089  -3.218  17.954  1.00 78.87           O1-
ANISOU  708  OE2 GLU A  90     8249  10014  11703   -505   1109    405       O1-
ATOM    709  N   ALA A  91      28.537  -7.222  21.554  1.00 41.14           N  
ANISOU  709  N   ALA A  91     3733   5243   6656   -222    355    338       N  
ATOM    710  CA  ALA A  91      27.704  -8.404  21.739  1.00 36.36           C  
ANISOU  710  CA  ALA A  91     3236   4630   5949   -134    267    342       C  
ATOM    711  C   ALA A  91      27.651  -9.182  20.434  1.00 36.47           C  
ANISOU  711  C   ALA A  91     3268   4655   5936    -40    395    333       C  
ATOM    712  O   ALA A  91      27.665  -8.590  19.362  1.00 36.69           O  
ANISOU  712  O   ALA A  91     3309   4693   5939    -54    558    342       O  
ATOM    713  CB  ALA A  91      26.297  -8.010  22.173  1.00 34.88           C  
ANISOU  713  CB  ALA A  91     3230   4421   5603   -171    218    370       C  
ATOM    714  N   PRO A  92      27.595 -10.518  20.516  1.00 36.45           N  
ANISOU  714  N   PRO A  92     3272   4644   5933     57    320    315       N  
ATOM    715  CA  PRO A  92      27.423 -11.299  19.289  1.00 36.54           C  
ANISOU  715  CA  PRO A  92     3320   4660   5904    150    432    294       C  
ATOM    716  C   PRO A  92      26.004 -11.125  18.747  1.00 35.21           C  
ANISOU  716  C   PRO A  92     3339   4480   5559    146    478    315       C  
ATOM    717  O   PRO A  92      25.094 -10.808  19.511  1.00 34.16           O  
ANISOU  717  O   PRO A  92     3306   4328   5344     95    387    341       O  
ATOM    718  CB  PRO A  92      27.648 -12.741  19.758  1.00 37.95           C  
ANISOU  718  CB  PRO A  92     3471   4814   6135    245    307    269       C  
ATOM    719  CG  PRO A  92      27.282 -12.721  21.217  1.00 38.74           C  
ANISOU  719  CG  PRO A  92     3612   4890   6217    196    125    300       C  
ATOM    720  CD  PRO A  92      27.695 -11.364  21.717  1.00 36.49           C  
ANISOU  720  CD  PRO A  92     3261   4629   5973     87    131    313       C  
ATOM    721  N   SER A  93      25.825 -11.328  17.447  1.00 35.38           N  
ANISOU  721  N   SER A  93     3404   4517   5522    203    615    299       N  
ATOM    722  CA  SER A  93      24.525 -11.180  16.806  1.00 35.68           C  
ANISOU  722  CA  SER A  93     3610   4551   5396    211    656    311       C  
ATOM    723  C   SER A  93      23.420 -11.962  17.513  1.00 38.85           C  
ANISOU  723  C   SER A  93     4119   4920   5723    227    514    309       C  
ATOM    724  O   SER A  93      23.650 -13.053  18.037  1.00 39.25           O  
ANISOU  724  O   SER A  93     4137   4944   5831    274    416    289       O  
ATOM    725  CB  SER A  93      24.599 -11.634  15.348  1.00 35.26           C  
ANISOU  725  CB  SER A  93     3582   4522   5293    295    797    278       C  
ATOM    726  OG  SER A  93      23.314 -11.588  14.756  1.00 37.09           O  
ANISOU  726  OG  SER A  93     3974   4753   5366    312    813    281       O  
ATOM    727  N   LEU A  94      22.216 -11.401  17.503  1.00 32.18           N  
ANISOU  727  N   LEU A  94     3402   4073   4753    188    508    330       N  
ATOM    728  CA  LEU A  94      21.058 -12.060  18.092  1.00 31.21           C  
ANISOU  728  CA  LEU A  94     3381   3924   4553    192    395    327       C  
ATOM    729  C   LEU A  94      20.500 -13.151  17.195  1.00 31.20           C  
ANISOU  729  C   LEU A  94     3446   3914   4494    276    416    284       C  
ATOM    730  O   LEU A  94      19.633 -13.905  17.613  1.00 30.63           O  
ANISOU  730  O   LEU A  94     3445   3813   4380    282    327    274       O  
ATOM    731  CB  LEU A  94      19.950 -11.038  18.386  1.00 30.23           C  
ANISOU  731  CB  LEU A  94     3354   3807   4323    125    385    354       C  
ATOM    732  CG  LEU A  94      19.317 -10.314  17.189  1.00 34.10           C  
ANISOU  732  CG  LEU A  94     3927   4320   4710    141    499    355       C  
ATOM    733  CD1 LEU A  94      18.194 -11.137  16.566  1.00 31.84           C  
ANISOU  733  CD1 LEU A  94     3741   4035   4322    200    483    320       C  
ATOM    734  CD2 LEU A  94      18.783  -8.941  17.618  1.00 31.86           C  
ANISOU  734  CD2 LEU A  94     3690   4036   4379     66    501    391       C  
ATOM    735  N   HIS A  95      20.974 -13.232  15.957  1.00 31.93           N  
ANISOU  735  N   HIS A  95     3520   4030   4582    337    537    255       N  
ATOM    736  CA  HIS A  95      20.389 -14.192  15.025  1.00 32.01           C  
ANISOU  736  CA  HIS A  95     3605   4035   4524    418    559    201       C  
ATOM    737  C   HIS A  95      21.376 -15.256  14.548  1.00 35.66           C  
ANISOU  737  C   HIS A  95     3988   4484   5077    506    589    150       C  
ATOM    738  O   HIS A  95      21.136 -15.934  13.549  1.00 43.32           O  
ANISOU  738  O   HIS A  95     5009   5457   5995    582    640     93       O  
ATOM    739  CB  HIS A  95      19.721 -13.488  13.840  1.00 31.89           C  
ANISOU  739  CB  HIS A  95     3683   4059   4374    432    665    196       C  
ATOM    740  CG  HIS A  95      20.677 -12.772  12.945  1.00 39.58           C  
ANISOU  740  CG  HIS A  95     4605   5074   5361    446    818    209       C  
ATOM    741  CD2 HIS A  95      20.994 -11.458  12.849  1.00 43.57           C  
ANISOU  741  CD2 HIS A  95     5096   5600   5859    386    901    264       C  
ATOM    742  ND1 HIS A  95      21.441 -13.422  12.001  1.00 46.34           N  
ANISOU  742  ND1 HIS A  95     5418   5948   6240    527    912    161       N  
ATOM    743  CE1 HIS A  95      22.191 -12.541  11.363  1.00 49.49           C  
ANISOU  743  CE1 HIS A  95     5776   6386   6643    513   1054    190       C  
ATOM    744  NE2 HIS A  95      21.937 -11.342  11.857  1.00 49.49           N  
ANISOU  744  NE2 HIS A  95     5794   6383   6628    424   1048    256       N  
ATOM    745  N   ARG A  96      22.473 -15.412  15.281  1.00 34.75           N  
ANISOU  745  N   ARG A  96     3749   4357   5099    501    551    162       N  
ATOM    746  CA  ARG A  96      23.427 -16.482  15.010  1.00 35.57           C  
ANISOU  746  CA  ARG A  96     3765   4441   5310    593    558    111       C  
ATOM    747  C   ARG A  96      23.640 -17.308  16.277  1.00 38.71           C  
ANISOU  747  C   ARG A  96     4125   4779   5805    596    396    126       C  
ATOM    748  O   ARG A  96      24.149 -16.808  17.278  1.00 34.96           O  
ANISOU  748  O   ARG A  96     3576   4308   5399    539    330    171       O  
ATOM    749  CB  ARG A  96      24.755 -15.911  14.507  1.00 38.26           C  
ANISOU  749  CB  ARG A  96     3966   4832   5740    604    685    105       C  
ATOM    750  CG  ARG A  96      24.649 -15.164  13.187  1.00 46.36           C  
ANISOU  750  CG  ARG A  96     5037   5914   6665    609    861     99       C  
ATOM    751  CD  ARG A  96      26.006 -14.629  12.724  1.00 57.20           C  
ANISOU  751  CD  ARG A  96     6262   7335   8138    609   1001     96       C  
ATOM    752  NE  ARG A  96      25.887 -13.861  11.486  1.00 66.75           N  
ANISOU  752  NE  ARG A  96     7532   8595   9236    606   1177    106       N  
ATOM    753  CZ  ARG A  96      25.970 -12.535  11.411  1.00 76.93           C  
ANISOU  753  CZ  ARG A  96     8822   9908  10500    516   1259    170       C  
ATOM    754  NH1 ARG A  96      25.841 -11.927  10.238  1.00 80.21           N1+
ANISOU  754  NH1 ARG A  96     9310  10362  10802    524   1419    185       N1+
ATOM    755  NH2 ARG A  96      26.191 -11.815  12.504  1.00 78.32           N  
ANISOU  755  NH2 ARG A  96     8935  10064  10761    421   1181    217       N  
ATOM    756  N   ARG A  97      23.235 -18.573  16.233  1.00 41.18           N  
ANISOU  756  N   ARG A  97     4497   5030   6118    661    329     90       N  
ATOM    757  CA  ARG A  97      23.343 -19.443  17.400  1.00 37.73           C  
ANISOU  757  CA  ARG A  97     4052   4524   5761    668    174    114       C  
ATOM    758  C   ARG A  97      24.760 -20.009  17.551  1.00 41.07           C  
ANISOU  758  C   ARG A  97     4330   4931   6342    750    155     91       C  
ATOM    759  O   ARG A  97      24.990 -21.203  17.331  1.00 40.61           O  
ANISOU  759  O   ARG A  97     4273   4811   6345    844    121     46       O  
ATOM    760  CB  ARG A  97      22.322 -20.577  17.295  1.00 38.06           C  
ANISOU  760  CB  ARG A  97     4220   4491   5749    698    112     88       C  
ATOM    761  CG  ARG A  97      21.912 -21.186  18.617  1.00 36.19           C  
ANISOU  761  CG  ARG A  97     4035   4184   5534    660    -44    144       C  
ATOM    762  CD  ARG A  97      20.988 -22.362  18.395  1.00 35.81           C  
ANISOU  762  CD  ARG A  97     4101   4053   5454    686    -87    112       C  
ATOM    763  NE  ARG A  97      20.507 -22.927  19.649  1.00 37.61           N  
ANISOU  763  NE  ARG A  97     4393   4209   5688    637   -221    176       N  
ATOM    764  CZ  ARG A  97      19.751 -24.018  19.732  1.00 41.11           C  
ANISOU  764  CZ  ARG A  97     4934   4560   6125    642   -278    167       C  
ATOM    765  NH1 ARG A  97      19.396 -24.672  18.629  1.00 42.50           N1+
ANISOU  765  NH1 ARG A  97     5151   4705   6292    698   -223     83       N1+
ATOM    766  NH2 ARG A  97      19.359 -24.462  20.919  1.00 34.60           N  
ANISOU  766  NH2 ARG A  97     4171   3673   5302    589   -388    239       N  
ATOM    767  N   THR A  98      25.702 -19.148  17.936  1.00 37.06           N  
ANISOU  767  N   THR A  98     3695   4475   5910    713    171    116       N  
ATOM    768  CA  THR A  98      27.090 -19.552  18.143  1.00 38.84           C  
ANISOU  768  CA  THR A  98     3758   4700   6300    785    147     92       C  
ATOM    769  C   THR A  98      27.315 -20.048  19.570  1.00 38.74           C  
ANISOU  769  C   THR A  98     3728   4633   6356    783    -45    139       C  
ATOM    770  O   THR A  98      26.491 -19.821  20.458  1.00 37.72           O  
ANISOU  770  O   THR A  98     3702   4486   6145    704   -139    198       O  
ATOM    771  CB  THR A  98      28.072 -18.388  17.886  1.00 39.95           C  
ANISOU  771  CB  THR A  98     3749   4924   6506    741    254     91       C  
ATOM    772  CG2 THR A  98      27.962 -17.890  16.451  1.00 40.64           C  
ANISOU  772  CG2 THR A  98     3854   5065   6520    747    455     54       C  
ATOM    773  OG1 THR A  98      27.785 -17.312  18.787  1.00 41.28           O  
ANISOU  773  OG1 THR A  98     3933   5116   6637    621    197    154       O  
ATOM    774  N   ALA A  99      28.438 -20.717  19.789  1.00 40.18           N  
ANISOU  774  N   ALA A  99     3783   4795   6687    874   -101    113       N  
ATOM    775  CA  ALA A  99      28.780 -21.180  21.128  1.00 43.26           C  
ANISOU  775  CA  ALA A  99     4152   5138   7145    886   -291    161       C  
ATOM    776  C   ALA A  99      28.812 -19.997  22.094  1.00 43.79           C  
ANISOU  776  C   ALA A  99     4192   5261   7184    767   -349    217       C  
ATOM    777  O   ALA A  99      28.340 -20.092  23.233  1.00 39.65           O  
ANISOU  777  O   ALA A  99     3753   4705   6607    723   -491    278       O  
ATOM    778  CB  ALA A  99      30.120 -21.919  21.120  1.00 42.51           C  
ANISOU  778  CB  ALA A  99     3895   5027   7230   1011   -335    116       C  
ATOM    779  N   GLU A 100      29.351 -18.875  21.622  1.00 41.14           N  
ANISOU  779  N   GLU A 100     3746   5007   6879    713   -232    195       N  
ATOM    780  CA  GLU A 100      29.436 -17.668  22.430  1.00 39.81           C  
ANISOU  780  CA  GLU A 100     3544   4887   6695    597   -273    233       C  
ATOM    781  C   GLU A 100      28.052 -17.122  22.775  1.00 38.12           C  
ANISOU  781  C   GLU A 100     3511   4666   6308    498   -281    282       C  
ATOM    782  O   GLU A 100      27.779 -16.793  23.930  1.00 37.95           O  
ANISOU  782  O   GLU A 100     3533   4642   6245    434   -404    327       O  
ATOM    783  CB  GLU A 100      30.268 -16.598  21.717  1.00 44.96           C  
ANISOU  783  CB  GLU A 100     4046   5613   7423    554   -125    197       C  
ATOM    784  CG  GLU A 100      30.382 -15.296  22.489  1.00 54.64           C  
ANISOU  784  CG  GLU A 100     5236   6879   8645    428   -161    226       C  
ATOM    785  CD  GLU A 100      31.052 -14.188  21.686  1.00 62.73           C  
ANISOU  785  CD  GLU A 100     6138   7963   9735    368      8    200       C  
ATOM    786  OE1 GLU A 100      31.408 -14.431  20.509  1.00 66.23           O  
ANISOU  786  OE1 GLU A 100     6528   8424  10211    425    163    163       O  
ATOM    787  OE2 GLU A 100      31.223 -13.074  22.234  1.00 56.31           O1-
ANISOU  787  OE2 GLU A 100     5285   7174   8936    261    -10    215       O1-
ATOM    788  N   ARG A 101      27.180 -17.026  21.777  1.00 37.22           N  
ANISOU  788  N   ARG A 101     3497   4552   6091    490   -153    269       N  
ATOM    789  CA  ARG A 101      25.838 -16.508  22.003  1.00 35.72           C  
ANISOU  789  CA  ARG A 101     3466   4361   5746    406   -152    307       C  
ATOM    790  C   ARG A 101      25.076 -17.405  22.978  1.00 37.36           C  
ANISOU  790  C   ARG A 101     3792   4508   5897    410   -299    346       C  
ATOM    791  O   ARG A 101      24.370 -16.922  23.864  1.00 34.54           O  
ANISOU  791  O   ARG A 101     3516   4156   5453    329   -365    389       O  
ATOM    792  CB  ARG A 101      25.082 -16.388  20.678  1.00 35.07           C  
ANISOU  792  CB  ARG A 101     3464   4290   5571    417     -1    278       C  
ATOM    793  CG  ARG A 101      23.690 -15.812  20.809  1.00 33.67           C  
ANISOU  793  CG  ARG A 101     3434   4117   5243    340      5    307       C  
ATOM    794  CD  ARG A 101      23.697 -14.292  21.047  1.00 33.24           C  
ANISOU  794  CD  ARG A 101     3358   4110   5160    242     48    332       C  
ATOM    795  NE  ARG A 101      22.368 -13.829  21.430  1.00 32.20           N  
ANISOU  795  NE  ARG A 101     3361   3977   4896    177     23    358       N  
ATOM    796  CZ  ARG A 101      21.980 -12.556  21.481  1.00 35.23           C  
ANISOU  796  CZ  ARG A 101     3773   4390   5224    101     69    375       C  
ATOM    797  NH1 ARG A 101      20.742 -12.263  21.857  1.00 30.43           N1+
ANISOU  797  NH1 ARG A 101     3281   3779   4502     56     39    390       N1+
ATOM    798  NH2 ARG A 101      22.816 -11.578  21.159  1.00 32.00           N  
ANISOU  798  NH2 ARG A 101     3274   4006   4877     69    147    373       N  
ATOM    799  N   THR A 102      25.231 -18.716  22.810  1.00 38.11           N  
ANISOU  799  N   THR A 102     3898   4541   6042    505   -343    331       N  
ATOM    800  CA  THR A 102      24.579 -19.691  23.675  1.00 39.24           C  
ANISOU  800  CA  THR A 102     4156   4610   6143    513   -474    375       C  
ATOM    801  C   THR A 102      25.074 -19.564  25.113  1.00 39.74           C  
ANISOU  801  C   THR A 102     4192   4673   6235    485   -628    431       C  
ATOM    802  O   THR A 102      24.286 -19.607  26.053  1.00 36.99           O  
ANISOU  802  O   THR A 102     3958   4306   5791    425   -711    486       O  
ATOM    803  CB  THR A 102      24.832 -21.127  23.171  1.00 39.67           C  
ANISOU  803  CB  THR A 102     4218   4584   6272    630   -492    344       C  
ATOM    804  CG2 THR A 102      24.295 -22.146  24.165  1.00 36.94           C  
ANISOU  804  CG2 THR A 102     3988   4147   5900    635   -634    403       C  
ATOM    805  OG1 THR A 102      24.190 -21.300  21.901  1.00 36.28           O  
ANISOU  805  OG1 THR A 102     3842   4152   5789    651   -362    288       O  
ATOM    806  N   ALA A 103      26.383 -19.405  25.273  1.00 37.54           N  
ANISOU  806  N   ALA A 103     3758   4422   6084    530   -666    411       N  
ATOM    807  CA  ALA A 103      26.979 -19.238  26.595  1.00 44.03           C  
ANISOU  807  CA  ALA A 103     4538   5254   6939    513   -825    452       C  
ATOM    808  C   ALA A 103      26.521 -17.949  27.291  1.00 37.39           C  
ANISOU  808  C   ALA A 103     3732   4474   6000    386   -832    476       C  
ATOM    809  O   ALA A 103      26.214 -17.956  28.482  1.00 37.39           O  
ANISOU  809  O   ALA A 103     3809   4467   5931    346   -959    527       O  
ATOM    810  CB  ALA A 103      28.506 -19.296  26.503  1.00 39.83           C  
ANISOU  810  CB  ALA A 103     3807   4745   6580    590   -858    411       C  
ATOM    811  N   LEU A 104      26.464 -16.849  26.547  1.00 36.76           N  
ANISOU  811  N   LEU A 104     3605   4450   5911    326   -695    440       N  
ATOM    812  CA  LEU A 104      25.989 -15.582  27.112  1.00 36.03           C  
ANISOU  812  CA  LEU A 104     3552   4405   5733    210   -691    454       C  
ATOM    813  C   LEU A 104      24.485 -15.608  27.444  1.00 34.67           C  
ANISOU  813  C   LEU A 104     3564   4215   5395    154   -689    491       C  
ATOM    814  O   LEU A 104      24.072 -15.138  28.508  1.00 34.41           O  
ANISOU  814  O   LEU A 104     3595   4198   5282     86   -770    521       O  
ATOM    815  CB  LEU A 104      26.327 -14.402  26.186  1.00 35.80           C  
ANISOU  815  CB  LEU A 104     3433   4425   5744    163   -540    412       C  
ATOM    816  CG  LEU A 104      27.810 -14.066  25.957  1.00 38.83           C  
ANISOU  816  CG  LEU A 104     3616   4842   6295    184   -524    372       C  
ATOM    817  CD1 LEU A 104      27.963 -12.918  24.954  1.00 36.98           C  
ANISOU  817  CD1 LEU A 104     3325   4646   6081    125   -348    344       C  
ATOM    818  CD2 LEU A 104      28.537 -13.730  27.263  1.00 38.07           C  
ANISOU  818  CD2 LEU A 104     3444   4766   6255    150   -688    376       C  
ATOM    819  N   GLU A 105      23.664 -16.160  26.551  1.00 35.78           N  
ANISOU  819  N   GLU A 105     3785   4326   5486    183   -598    484       N  
ATOM    820  CA  GLU A 105      22.231 -16.261  26.841  1.00 36.70           C  
ANISOU  820  CA  GLU A 105     4057   4425   5460    130   -597    512       C  
ATOM    821  C   GLU A 105      21.975 -17.136  28.068  1.00 39.85           C  
ANISOU  821  C   GLU A 105     4541   4781   5820    131   -740    570       C  
ATOM    822  O   GLU A 105      21.112 -16.818  28.888  1.00 41.73           O  
ANISOU  822  O   GLU A 105     4877   5032   5946     58   -773    603       O  
ATOM    823  CB  GLU A 105      21.435 -16.778  25.637  1.00 34.07           C  
ANISOU  823  CB  GLU A 105     3785   4068   5092    165   -487    484       C  
ATOM    824  CG  GLU A 105      21.304 -15.766  24.502  1.00 34.77           C  
ANISOU  824  CG  GLU A 105     3843   4206   5163    147   -342    443       C  
ATOM    825  CD  GLU A 105      20.331 -16.207  23.411  1.00 38.02           C  
ANISOU  825  CD  GLU A 105     4336   4602   5508    175   -253    413       C  
ATOM    826  OE1 GLU A 105      19.664 -17.261  23.568  1.00 32.94           O  
ANISOU  826  OE1 GLU A 105     3772   3906   4836    194   -301    420       O  
ATOM    827  OE2 GLU A 105      20.233 -15.491  22.392  1.00 37.22           O1-
ANISOU  827  OE2 GLU A 105     4222   4537   5382    176   -136    383       O1-
ATOM    828  N   ASN A 106      22.730 -18.228  28.185  1.00 37.38           N  
ANISOU  828  N   ASN A 106     4192   4415   5598    216   -820    583       N  
ATOM    829  CA  ASN A 106      22.615 -19.154  29.312  1.00 39.29           C  
ANISOU  829  CA  ASN A 106     4519   4601   5810    230   -961    649       C  
ATOM    830  C   ASN A 106      22.938 -18.477  30.633  1.00 36.84           C  
ANISOU  830  C   ASN A 106     4206   4337   5453    177  -1075    684       C  
ATOM    831  O   ASN A 106      22.121 -18.465  31.554  1.00 35.19           O  
ANISOU  831  O   ASN A 106     4120   4129   5123    114  -1123    734       O  
ATOM    832  CB  ASN A 106      23.564 -20.344  29.136  1.00 41.91           C  
ANISOU  832  CB  ASN A 106     4793   4864   6269    349  -1032    651       C  
ATOM    833  CG  ASN A 106      22.866 -21.579  28.590  1.00 50.87           C  
ANISOU  833  CG  ASN A 106     6026   5906   7398    393  -1002    658       C  
ATOM    834  ND2 ASN A 106      21.635 -21.806  29.029  1.00 50.51           N  
ANISOU  834  ND2 ASN A 106     6126   5832   7233    320  -1001    702       N  
ATOM    835  OD1 ASN A 106      23.433 -22.324  27.785  1.00 55.68           O  
ANISOU  835  OD1 ASN A 106     6576   6466   8113    490   -979    617       O  
ATOM    836  N   ALA A 107      24.150 -17.933  30.712  1.00 36.25           N  
ANISOU  836  N   ALA A 107     3988   4303   5480    202  -1117    652       N  
ATOM    837  CA  ALA A 107      24.592 -17.177  31.877  1.00 36.91           C  
ANISOU  837  CA  ALA A 107     4049   4439   5535    152  -1230    665       C  
ATOM    838  C   ALA A 107      23.646 -16.019  32.190  1.00 36.30           C  
ANISOU  838  C   ALA A 107     4049   4416   5329     38  -1169    657       C  
ATOM    839  O   ALA A 107      23.255 -15.820  33.340  1.00 37.82           O  
ANISOU  839  O   ALA A 107     4331   4627   5413    -12  -1257    692       O  
ATOM    840  CB  ALA A 107      26.015 -16.662  31.667  1.00 38.29           C  
ANISOU  840  CB  ALA A 107     4032   4654   5862    186  -1257    611       C  
ATOM    841  N   GLY A 108      23.270 -15.263  31.161  1.00 37.05           N  
ANISOU  841  N   GLY A 108     4114   4534   5430      4  -1017    610       N  
ATOM    842  CA  GLY A 108      22.424 -14.094  31.345  1.00 33.65           C  
ANISOU  842  CA  GLY A 108     3743   4148   4895    -92   -954    594       C  
ATOM    843  C   GLY A 108      21.042 -14.458  31.855  1.00 33.19           C  
ANISOU  843  C   GLY A 108     3848   4076   4687   -132   -952    635       C  
ATOM    844  O   GLY A 108      20.489 -13.779  32.715  1.00 36.98           O  
ANISOU  844  O   GLY A 108     4396   4592   5063   -202   -978    640       O  
ATOM    845  N   THR A 109      20.485 -15.541  31.330  1.00 34.29           N  
ANISOU  845  N   THR A 109     4047   4164   4820    -90   -917    658       N  
ATOM    846  CA  THR A 109      19.144 -15.976  31.714  1.00 36.40           C  
ANISOU  846  CA  THR A 109     4455   4413   4962   -135   -900    694       C  
ATOM    847  C   THR A 109      19.108 -16.426  33.176  1.00 36.40           C  
ANISOU  847  C   THR A 109     4541   4406   4882   -157  -1030    760       C  
ATOM    848  O   THR A 109      18.154 -16.138  33.902  1.00 36.12           O  
ANISOU  848  O   THR A 109     4607   4398   4721   -227  -1022    780       O  
ATOM    849  CB  THR A 109      18.634 -17.080  30.764  1.00 41.87           C  
ANISOU  849  CB  THR A 109     5182   5043   5685    -87   -838    696       C  
ATOM    850  CG2 THR A 109      17.266 -17.590  31.194  1.00 41.59           C  
ANISOU  850  CG2 THR A 109     5280   4986   5537   -143   -823    732       C  
ATOM    851  OG1 THR A 109      18.541 -16.540  29.438  1.00 47.22           O  
ANISOU  851  OG1 THR A 109     5799   5742   6402    -72   -714    634       O  
ATOM    852  N   ALA A 110      20.160 -17.115  33.606  1.00 34.95           N  
ANISOU  852  N   ALA A 110     4319   4190   4771    -92  -1149    792       N  
ATOM    853  CA  ALA A 110      20.294 -17.511  35.003  1.00 38.73           C  
ANISOU  853  CA  ALA A 110     4881   4664   5172   -100  -1289    860       C  
ATOM    854  C   ALA A 110      20.373 -16.281  35.897  1.00 38.60           C  
ANISOU  854  C   ALA A 110     4862   4730   5074   -168  -1330    836       C  
ATOM    855  O   ALA A 110      19.814 -16.271  36.991  1.00 39.64           O  
ANISOU  855  O   ALA A 110     5110   4882   5069   -217  -1382    879       O  
ATOM    856  CB  ALA A 110      21.527 -18.386  35.202  1.00 38.90           C  
ANISOU  856  CB  ALA A 110     4842   4636   5301     -1  -1420    891       C  
ATOM    857  N   MET A 111      21.072 -15.252  35.424  1.00 35.41           N  
ANISOU  857  N   MET A 111     4329   4370   4754   -173  -1302    764       N  
ATOM    858  CA  MET A 111      21.220 -14.012  36.174  1.00 37.49           C  
ANISOU  858  CA  MET A 111     4579   4702   4962   -238  -1340    725       C  
ATOM    859  C   MET A 111      19.895 -13.268  36.291  1.00 35.73           C  
ANISOU  859  C   MET A 111     4455   4512   4607   -321  -1237    707       C  
ATOM    860  O   MET A 111      19.704 -12.482  37.216  1.00 37.18           O  
ANISOU  860  O   MET A 111     4684   4745   4696   -377  -1279    688       O  
ATOM    861  CB  MET A 111      22.282 -13.106  35.534  1.00 35.27           C  
ANISOU  861  CB  MET A 111     4131   4445   4823   -232  -1320    652       C  
ATOM    862  CG  MET A 111      23.696 -13.654  35.648  1.00 37.31           C  
ANISOU  862  CG  MET A 111     4270   4691   5216   -156  -1441    655       C  
ATOM    863  SD  MET A 111      24.904 -12.640  34.783  1.00 42.68           S  
ANISOU  863  SD  MET A 111     4737   5399   6079   -161  -1387    569       S  
ATOM    864  CE  MET A 111      25.001 -11.215  35.862  1.00 41.81           C  
ANISOU  864  CE  MET A 111     4631   5349   5904   -261  -1461    519       C  
ATOM    865  N   LEU A 112      18.983 -13.510  35.353  1.00 32.97           N  
ANISOU  865  N   LEU A 112     4136   4139   4253   -324  -1106    705       N  
ATOM    866  CA  LEU A 112      17.672 -12.869  35.397  1.00 34.28           C  
ANISOU  866  CA  LEU A 112     4384   4336   4305   -392  -1009    684       C  
ATOM    867  C   LEU A 112      16.887 -13.277  36.647  1.00 37.75           C  
ANISOU  867  C   LEU A 112     4960   4792   4593   -435  -1059    736       C  
ATOM    868  O   LEU A 112      15.975 -12.564  37.068  1.00 35.40           O  
ANISOU  868  O   LEU A 112     4723   4540   4188   -496  -1006    710       O  
ATOM    869  CB  LEU A 112      16.861 -13.184  34.131  1.00 34.74           C  
ANISOU  869  CB  LEU A 112     4442   4366   4391   -377   -877    671       C  
ATOM    870  CG  LEU A 112      17.285 -12.457  32.853  1.00 35.58           C  
ANISOU  870  CG  LEU A 112     4444   4475   4602   -352   -787    614       C  
ATOM    871  CD1 LEU A 112      16.641 -13.099  31.632  1.00 34.84           C  
ANISOU  871  CD1 LEU A 112     4359   4347   4533   -317   -688    609       C  
ATOM    872  CD2 LEU A 112      16.952 -10.967  32.929  1.00 34.03           C  
ANISOU  872  CD2 LEU A 112     4241   4323   4364   -409   -735    562       C  
ATOM    873  N   CYS A 113      17.240 -14.420  37.235  1.00 33.44           N  
ANISOU  873  N   CYS A 113     4463   4206   4035   -401  -1156    810       N  
ATOM    874  CA  CYS A 113      16.577 -14.890  38.452  1.00 34.12           C  
ANISOU  874  CA  CYS A 113     4690   4304   3970   -442  -1203    875       C  
ATOM    875  C   CYS A 113      16.852 -13.972  39.638  1.00 36.91           C  
ANISOU  875  C   CYS A 113     5073   4729   4221   -481  -1284    852       C  
ATOM    876  O   CYS A 113      16.100 -13.971  40.614  1.00 40.47           O  
ANISOU  876  O   CYS A 113     5644   5215   4519   -532  -1286    882       O  
ATOM    877  CB  CYS A 113      17.024 -16.315  38.807  1.00 38.62           C  
ANISOU  877  CB  CYS A 113     5314   4802   4558   -388  -1301    968       C  
ATOM    878  SG  CYS A 113      16.554 -17.561  37.591  1.00 45.86           S  
ANISOU  878  SG  CYS A 113     6229   5621   5574   -350  -1214    995       S  
ATOM    879  N   LYS A 114      17.931 -13.199  39.556  1.00 35.06           N  
ANISOU  879  N   LYS A 114     4731   4518   4074   -459  -1350    795       N  
ATOM    880  CA  LYS A 114      18.322 -12.331  40.661  1.00 35.89           C  
ANISOU  880  CA  LYS A 114     4855   4686   4097   -492  -1447    760       C  
ATOM    881  C   LYS A 114      18.379 -10.872  40.215  1.00 37.37           C  
ANISOU  881  C   LYS A 114     4957   4909   4335   -532  -1380    656       C  
ATOM    882  O   LYS A 114      19.208 -10.096  40.679  1.00 36.14           O  
ANISOU  882  O   LYS A 114     4744   4783   4205   -543  -1468    603       O  
ATOM    883  CB  LYS A 114      19.666 -12.777  41.248  1.00 37.35           C  
ANISOU  883  CB  LYS A 114     4994   4863   4334   -434  -1627    787       C  
ATOM    884  CG  LYS A 114      19.662 -14.212  41.792  1.00 40.17           C  
ANISOU  884  CG  LYS A 114     5454   5174   4636   -386  -1711    900       C  
ATOM    885  CD  LYS A 114      20.953 -14.524  42.547  1.00 49.12           C  
ANISOU  885  CD  LYS A 114     6553   6311   5800   -322  -1911    923       C  
ATOM    886  CE  LYS A 114      20.966 -15.959  43.068  1.00 56.96           C  
ANISOU  886  CE  LYS A 114     7659   7243   6740   -265  -2000   1044       C  
ATOM    887  NZ  LYS A 114      22.232 -16.274  43.790  1.00 63.30           N1+
ANISOU  887  NZ  LYS A 114     8427   8050   7574   -188  -2210   1067       N1+
ATOM    888  N   THR A 115      17.476 -10.510  39.313  1.00 37.79           N  
ANISOU  888  N   THR A 115     5005   4953   4402   -555  -1227    627       N  
ATOM    889  CA  THR A 115      17.437  -9.162  38.771  1.00 36.50           C  
ANISOU  889  CA  THR A 115     4774   4806   4289   -587  -1151    541       C  
ATOM    890  C   THR A 115      16.194  -8.403  39.217  1.00 33.48           C  
ANISOU  890  C   THR A 115     4484   4464   3772   -644  -1073    502       C  
ATOM    891  O   THR A 115      15.082  -8.942  39.224  1.00 34.77           O  
ANISOU  891  O   THR A 115     4729   4633   3851   -654  -1000    536       O  
ATOM    892  CB  THR A 115      17.507  -9.191  37.232  1.00 35.82           C  
ANISOU  892  CB  THR A 115     4595   4676   4338   -554  -1040    530       C  
ATOM    893  CG2 THR A 115      17.405  -7.775  36.648  1.00 33.08           C  
ANISOU  893  CG2 THR A 115     4197   4336   4036   -588   -954    454       C  
ATOM    894  OG1 THR A 115      18.752  -9.778  36.840  1.00 35.68           O  
ANISOU  894  OG1 THR A 115     4476   4627   4454   -500  -1107    551       O  
ATOM    895  N   VAL A 116      16.397  -7.154  39.615  1.00 35.25           N  
ANISOU  895  N   VAL A 116     4693   4716   3986   -680  -1090    425       N  
ATOM    896  CA  VAL A 116      15.295  -6.235  39.845  1.00 35.51           C  
ANISOU  896  CA  VAL A 116     4790   4779   3922   -723  -1003    368       C  
ATOM    897  C   VAL A 116      15.050  -5.473  38.546  1.00 33.49           C  
ANISOU  897  C   VAL A 116     4464   4488   3774   -715   -884    326       C  
ATOM    898  O   VAL A 116      16.002  -5.055  37.886  1.00 34.15           O  
ANISOU  898  O   VAL A 116     4449   4536   3990   -705   -894    307       O  
ATOM    899  CB  VAL A 116      15.637  -5.247  40.969  1.00 35.78           C  
ANISOU  899  CB  VAL A 116     4854   4853   3887   -762  -1088    297       C  
ATOM    900  CG1 VAL A 116      14.521  -4.232  41.159  1.00 36.27           C  
ANISOU  900  CG1 VAL A 116     4977   4940   3863   -796   -993    225       C  
ATOM    901  CG2 VAL A 116      15.902  -5.998  42.259  1.00 35.99           C  
ANISOU  901  CG2 VAL A 116     4963   4921   3789   -763  -1214    344       C  
ATOM    902  N   PHE A 117      13.784  -5.294  38.174  1.00 30.74           N  
ANISOU  902  N   PHE A 117     4163   4148   3368   -719   -771    313       N  
ATOM    903  CA  PHE A 117      13.451  -4.602  36.929  1.00 29.83           C  
ANISOU  903  CA  PHE A 117     3998   3999   3337   -702   -663    280       C  
ATOM    904  C   PHE A 117      12.760  -3.276  37.202  1.00 31.37           C  
ANISOU  904  C   PHE A 117     4229   4207   3483   -728   -615    201       C  
ATOM    905  O   PHE A 117      11.880  -3.190  38.063  1.00 30.04           O  
ANISOU  905  O   PHE A 117     4138   4085   3191   -749   -606    177       O  
ATOM    906  CB  PHE A 117      12.547  -5.458  36.040  1.00 28.97           C  
ANISOU  906  CB  PHE A 117     3900   3882   3225   -670   -575    322       C  
ATOM    907  CG  PHE A 117      13.142  -6.789  35.670  1.00 32.76           C  
ANISOU  907  CG  PHE A 117     4350   4336   3760   -637   -613    393       C  
ATOM    908  CD1 PHE A 117      12.893  -7.914  36.444  1.00 32.43           C  
ANISOU  908  CD1 PHE A 117     4371   4308   3642   -645   -663    449       C  
ATOM    909  CD2 PHE A 117      13.942  -6.918  34.547  1.00 35.24           C  
ANISOU  909  CD2 PHE A 117     4579   4608   4201   -597   -594    404       C  
ATOM    910  CE1 PHE A 117      13.443  -9.151  36.106  1.00 38.53           C  
ANISOU  910  CE1 PHE A 117     5123   5042   4474   -609   -702    513       C  
ATOM    911  CE2 PHE A 117      14.495  -8.145  34.203  1.00 36.09           C  
ANISOU  911  CE2 PHE A 117     4659   4689   4366   -558   -628    458       C  
ATOM    912  CZ  PHE A 117      14.243  -9.264  34.982  1.00 35.10           C  
ANISOU  912  CZ  PHE A 117     4598   4567   4173   -561   -687    512       C  
ATOM    913  N   VAL A 118      13.150  -2.250  36.454  1.00 29.62           N  
ANISOU  913  N   VAL A 118     3955   3940   3359   -725   -577    162       N  
ATOM    914  CA  VAL A 118      12.559  -0.928  36.617  1.00 29.69           C  
ANISOU  914  CA  VAL A 118     3999   3941   3342   -741   -533     85       C  
ATOM    915  C   VAL A 118      12.075  -0.393  35.278  1.00 28.92           C  
ANISOU  915  C   VAL A 118     3879   3798   3312   -705   -426     83       C  
ATOM    916  O   VAL A 118      12.854  -0.271  34.336  1.00 32.99           O  
ANISOU  916  O   VAL A 118     4331   4264   3938   -693   -405    109       O  
ATOM    917  CB  VAL A 118      13.564   0.074  37.238  1.00 30.63           C  
ANISOU  917  CB  VAL A 118     4095   4036   3509   -785   -610     26       C  
ATOM    918  CG1 VAL A 118      12.914   1.445  37.411  1.00 30.81           C  
ANISOU  918  CG1 VAL A 118     4163   4035   3509   -798   -564    -60       C  
ATOM    919  CG2 VAL A 118      14.072  -0.447  38.564  1.00 31.55           C  
ANISOU  919  CG2 VAL A 118     4238   4203   3548   -813   -732     25       C  
ATOM    920  N   LEU A 119      10.786  -0.077  35.207  1.00 28.55           N  
ANISOU  920  N   LEU A 119     3883   3770   3194   -684   -358     52       N  
ATOM    921  CA  LEU A 119      10.162   0.436  33.990  1.00 28.25           C  
ANISOU  921  CA  LEU A 119     3838   3696   3201   -638   -267     48       C  
ATOM    922  C   LEU A 119       9.848   1.926  34.128  1.00 28.32           C  
ANISOU  922  C   LEU A 119     3879   3665   3217   -639   -242    -25       C  
ATOM    923  O   LEU A 119       9.123   2.344  35.032  1.00 28.68           O  
ANISOU  923  O   LEU A 119     3974   3745   3180   -649   -247    -86       O  
ATOM    924  CB  LEU A 119       8.876  -0.340  33.684  1.00 27.33           C  
ANISOU  924  CB  LEU A 119     3744   3627   3015   -602   -213     63       C  
ATOM    925  CG  LEU A 119       7.974   0.128  32.535  1.00 27.69           C  
ANISOU  925  CG  LEU A 119     3790   3652   3079   -543   -133     50       C  
ATOM    926  CD1 LEU A 119       8.734   0.187  31.204  1.00 26.99           C  
ANISOU  926  CD1 LEU A 119     3663   3506   3087   -512   -105     97       C  
ATOM    927  CD2 LEU A 119       6.743  -0.795  32.416  1.00 27.46           C  
ANISOU  927  CD2 LEU A 119     3768   3682   2985   -521    -98     54       C  
ATOM    928  N   VAL A 120      10.408   2.717  33.224  1.00 29.44           N  
ANISOU  928  N   VAL A 120     3996   3732   3458   -630   -209    -17       N  
ATOM    929  CA  VAL A 120      10.194   4.158  33.203  1.00 30.63           C  
ANISOU  929  CA  VAL A 120     4182   3820   3636   -628   -183    -76       C  
ATOM    930  C   VAL A 120       9.007   4.471  32.300  1.00 28.96           C  
ANISOU  930  C   VAL A 120     4003   3598   3404   -555   -105    -77       C  
ATOM    931  O   VAL A 120       9.098   4.336  31.083  1.00 27.95           O  
ANISOU  931  O   VAL A 120     3858   3438   3323   -517    -56    -21       O  
ATOM    932  CB  VAL A 120      11.444   4.881  32.677  1.00 38.62           C  
ANISOU  932  CB  VAL A 120     5154   4744   4774   -664   -184    -59       C  
ATOM    933  CG1 VAL A 120      11.166   6.369  32.493  1.00 43.69           C  
ANISOU  933  CG1 VAL A 120     5844   5300   5455   -659   -147   -109       C  
ATOM    934  CG2 VAL A 120      12.611   4.663  33.633  1.00 41.66           C  
ANISOU  934  CG2 VAL A 120     5495   5144   5189   -735   -277    -75       C  
ATOM    935  N   ALA A 121       7.891   4.873  32.901  1.00 31.55           N  
ANISOU  935  N   ALA A 121     4375   3956   3655   -531    -94   -143       N  
ATOM    936  CA  ALA A 121       6.636   5.043  32.170  1.00 29.43           C  
ANISOU  936  CA  ALA A 121     4126   3696   3360   -454    -34   -153       C  
ATOM    937  C   ALA A 121       5.840   6.264  32.640  1.00 30.97           C  
ANISOU  937  C   ALA A 121     4370   3863   3535   -423    -19   -243       C  
ATOM    938  O   ALA A 121       4.736   6.135  33.193  1.00 30.08           O  
ANISOU  938  O   ALA A 121     4267   3818   3345   -397     -4   -298       O  
ATOM    939  CB  ALA A 121       5.793   3.793  32.307  1.00 27.61           C  
ANISOU  939  CB  ALA A 121     3876   3563   3052   -441    -25   -138       C  
ATOM    940  N   GLY A 122       6.394   7.450  32.416  1.00 29.36           N  
ANISOU  940  N   GLY A 122     4194   3557   3405   -428    -18   -259       N  
ATOM    941  CA  GLY A 122       5.738   8.671  32.855  1.00 30.11           C  
ANISOU  941  CA  GLY A 122     4342   3605   3495   -395    -10   -349       C  
ATOM    942  C   GLY A 122       5.119   9.471  31.726  1.00 30.21           C  
ANISOU  942  C   GLY A 122     4385   3540   3551   -307     38   -334       C  
ATOM    943  O   GLY A 122       4.652  10.584  31.950  1.00 31.95           O  
ANISOU  943  O   GLY A 122     4654   3697   3787   -269     45   -403       O  
ATOM    944  N   GLY A 123       5.080   8.901  30.522  1.00 30.06           N  
ANISOU  944  N   GLY A 123     4346   3527   3547   -266     67   -249       N  
ATOM    945  CA  GLY A 123       4.644   9.647  29.353  1.00 34.53           C  
ANISOU  945  CA  GLY A 123     4955   4016   4150   -181    104   -218       C  
ATOM    946  C   GLY A 123       3.394   9.158  28.640  1.00 31.21           C  
ANISOU  946  C   GLY A 123     4522   3662   3675    -82    122   -214       C  
ATOM    947  O   GLY A 123       3.189   7.963  28.469  1.00 28.63           O  
ANISOU  947  O   GLY A 123     4145   3428   3305    -88    120   -186       O  
ATOM    948  N   LEU A 124       2.553  10.101  28.227  1.00 33.66           N  
ANISOU  948  N   LEU A 124     4877   3920   3993     11    133   -245       N  
ATOM    949  CA  LEU A 124       1.464   9.823  27.299  1.00 32.79           C  
ANISOU  949  CA  LEU A 124     4758   3852   3848    118    139   -234       C  
ATOM    950  C   LEU A 124       2.060   9.808  25.895  1.00 34.82           C  
ANISOU  950  C   LEU A 124     5051   4049   4129    146    159   -126       C  
ATOM    951  O   LEU A 124       3.194  10.244  25.707  1.00 33.98           O  
ANISOU  951  O   LEU A 124     4979   3855   4077     88    177    -71       O  
ATOM    952  CB  LEU A 124       0.387  10.904  27.390  1.00 30.62           C  
ANISOU  952  CB  LEU A 124     4519   3538   3578    219    135   -310       C  
ATOM    953  CG  LEU A 124      -0.281  11.073  28.753  1.00 34.06           C  
ANISOU  953  CG  LEU A 124     4926   4032   3986    205    130   -429       C  
ATOM    954  CD1 LEU A 124      -1.241  12.268  28.721  1.00 32.01           C  
ANISOU  954  CD1 LEU A 124     4704   3711   3748    319    127   -505       C  
ATOM    955  CD2 LEU A 124      -1.005   9.786  29.157  1.00 30.35           C  
ANISOU  955  CD2 LEU A 124     4368   3715   3447    185    134   -457       C  
ATOM    956  N   GLY A 125       1.307   9.315  24.914  1.00 32.82           N  
ANISOU  956  N   GLY A 125     4788   3845   3836    232    156   -101       N  
ATOM    957  CA  GLY A 125       1.823   9.190  23.560  1.00 32.09           C  
ANISOU  957  CA  GLY A 125     4735   3713   3743    264    177     -1       C  
ATOM    958  C   GLY A 125       1.339  10.278  22.619  1.00 33.98           C  
ANISOU  958  C   GLY A 125     5062   3863   3984    377    179     28       C  
ATOM    959  O   GLY A 125       1.243  10.058  21.411  1.00 38.31           O  
ANISOU  959  O   GLY A 125     5646   4414   4496    443    184     93       O  
ATOM    960  N   GLU A 126       1.050  11.457  23.168  1.00 33.85           N  
ANISOU  960  N   GLU A 126     5091   3763   4006    403    171    -21       N  
ATOM    961  CA  GLU A 126       0.433  12.536  22.396  1.00 37.39           C  
ANISOU  961  CA  GLU A 126     5628   4120   4459    526    161     -2       C  
ATOM    962  C   GLU A 126       1.250  12.933  21.168  1.00 35.12           C  
ANISOU  962  C   GLU A 126     5434   3732   4178    536    200    125       C  
ATOM    963  O   GLU A 126       0.696  13.145  20.096  1.00 35.82           O  
ANISOU  963  O   GLU A 126     5583   3805   4221    650    187    172       O  
ATOM    964  CB  GLU A 126       0.131  13.750  23.289  1.00 39.02           C  
ANISOU  964  CB  GLU A 126     5871   4236   4720    542    150    -81       C  
ATOM    965  CG  GLU A 126      -0.986  13.472  24.305  1.00 50.73           C  
ANISOU  965  CG  GLU A 126     7271   5824   6179    572    118   -211       C  
ATOM    966  CD  GLU A 126      -1.111  14.532  25.393  1.00 63.35           C  
ANISOU  966  CD  GLU A 126     8897   7347   7826    564    115   -306       C  
ATOM    967  OE1 GLU A 126      -0.070  15.042  25.865  1.00 64.08           O  
ANISOU  967  OE1 GLU A 126     9030   7347   7969    469    134   -292       O  
ATOM    968  OE2 GLU A 126      -2.258  14.847  25.784  1.00 68.43           O1-
ANISOU  968  OE2 GLU A 126     9514   8027   8460    655     94   -402       O1-
ATOM    969  N   ARG A 127       2.565  13.017  21.323  1.00 36.05           N  
ANISOU  969  N   ARG A 127     5561   3788   4347    418    249    179       N  
ATOM    970  CA  ARG A 127       3.432  13.333  20.195  1.00 44.11           C  
ANISOU  970  CA  ARG A 127     6661   4723   5377    410    308    302       C  
ATOM    971  C   ARG A 127       3.279  12.307  19.061  1.00 43.49           C  
ANISOU  971  C   ARG A 127     6573   4741   5211    465    315    361       C  
ATOM    972  O   ARG A 127       3.364  12.659  17.885  1.00 46.93           O  
ANISOU  972  O   ARG A 127     7100   5124   5608    529    345    452       O  
ATOM    973  CB  ARG A 127       4.887  13.432  20.656  1.00 52.46           C  
ANISOU  973  CB  ARG A 127     7694   5722   6517    260    360    333       C  
ATOM    974  CG  ARG A 127       5.831  14.004  19.608  1.00 67.54           C  
ANISOU  974  CG  ARG A 127     9687   7519   8455    236    439    457       C  
ATOM    975  CD  ARG A 127       6.439  12.904  18.759  1.00 74.56           C  
ANISOU  975  CD  ARG A 127    10536   8496   9296    215    486    527       C  
ATOM    976  NE  ARG A 127       7.610  12.318  19.400  1.00 77.32           N  
ANISOU  976  NE  ARG A 127    10786   8878   9713     79    511    516       N  
ATOM    977  CZ  ARG A 127       8.863  12.592  19.057  1.00 81.26           C  
ANISOU  977  CZ  ARG A 127    11286   9308  10282    -11    590    588       C  
ATOM    978  NH1 ARG A 127       9.868  12.013  19.700  1.00 86.58           N1+
ANISOU  978  NH1 ARG A 127    11853  10022  11023   -124    596    565       N1+
ATOM    979  NH2 ARG A 127       9.111  13.439  18.068  1.00 80.97           N  
ANISOU  979  NH2 ARG A 127    11355   9162  10248     13    663    685       N  
ATOM    980  N   LEU A 128       3.036  11.047  19.424  1.00 35.20           N  
ANISOU  980  N   LEU A 128     5419   3829   4125    439    287    309       N  
ATOM    981  CA  LEU A 128       2.841   9.965  18.456  1.00 37.16           C  
ANISOU  981  CA  LEU A 128     5649   4174   4296    486    284    342       C  
ATOM    982  C   LEU A 128       1.487  10.044  17.774  1.00 38.77           C  
ANISOU  982  C   LEU A 128     5884   4418   4427    632    225    316       C  
ATOM    983  O   LEU A 128       1.310   9.516  16.680  1.00 41.64           O  
ANISOU  983  O   LEU A 128     6275   4828   4717    698    220    358       O  
ATOM    984  CB  LEU A 128       2.928   8.600  19.159  1.00 45.44           C  
ANISOU  984  CB  LEU A 128     6578   5344   5341    411    264    285       C  
ATOM    985  CG  LEU A 128       4.280   8.091  19.650  1.00 49.82           C  
ANISOU  985  CG  LEU A 128     7082   5897   5952    281    307    313       C  
ATOM    986  CD1 LEU A 128       4.102   7.059  20.747  1.00 48.59           C  
ANISOU  986  CD1 LEU A 128     6824   5837   5799    218    266    240       C  
ATOM    987  CD2 LEU A 128       5.041   7.496  18.491  1.00 50.95           C  
ANISOU  987  CD2 LEU A 128     7241   6050   6067    284    359    395       C  
ATOM    988  N   GLY A 129       0.530  10.691  18.436  1.00 41.16           N  
ANISOU  988  N   GLY A 129     6180   4709   4751    686    176    239       N  
ATOM    989  CA  GLY A 129      -0.852  10.698  17.992  1.00 37.09           C  
ANISOU  989  CA  GLY A 129     5660   4249   4183    824    107    189       C  
ATOM    990  C   GLY A 129      -1.726   9.778  18.834  1.00 35.37           C  
ANISOU  990  C   GLY A 129     5312   4164   3964    806     64     75       C  
ATOM    991  O   GLY A 129      -2.816   9.386  18.421  1.00 36.14           O  
ANISOU  991  O   GLY A 129     5369   4342   4019    898      8     26       O  
ATOM    992  N   TYR A 130      -1.250   9.439  20.028  1.00 34.73           N  
ANISOU  992  N   TYR A 130     5164   4104   3927    685     91     33       N  
ATOM    993  CA  TYR A 130      -1.943   8.495  20.899  1.00 30.42           C  
ANISOU  993  CA  TYR A 130     4503   3681   3375    645     68    -59       C  
ATOM    994  C   TYR A 130      -2.192   9.131  22.270  1.00 30.68           C  
ANISOU  994  C   TYR A 130     4509   3697   3450    607     74   -141       C  
ATOM    995  O   TYR A 130      -1.252   9.487  22.973  1.00 32.77           O  
ANISOU  995  O   TYR A 130     4797   3900   3752    515    105   -126       O  
ATOM    996  CB  TYR A 130      -1.099   7.220  21.036  1.00 30.27           C  
ANISOU  996  CB  TYR A 130     4433   3721   3348    532     93    -26       C  
ATOM    997  CG  TYR A 130      -1.730   6.134  21.869  1.00 29.01           C  
ANISOU  997  CG  TYR A 130     4168   3677   3178    480     77   -102       C  
ATOM    998  CD1 TYR A 130      -1.198   5.782  23.106  1.00 30.58           C  
ANISOU  998  CD1 TYR A 130     4327   3892   3399    364     98   -123       C  
ATOM    999  CD2 TYR A 130      -2.863   5.466  21.426  1.00 31.16           C  
ANISOU  999  CD2 TYR A 130     4381   4039   3418    543     38   -151       C  
ATOM   1000  CE1 TYR A 130      -1.777   4.786  23.877  1.00 27.57           C  
ANISOU 1000  CE1 TYR A 130     3863   3612   3002    312     91   -179       C  
ATOM   1001  CE2 TYR A 130      -3.454   4.471  22.192  1.00 29.35           C  
ANISOU 1001  CE2 TYR A 130     4056   3909   3188    482     33   -216       C  
ATOM   1002  CZ  TYR A 130      -2.900   4.128  23.413  1.00 29.66           C  
ANISOU 1002  CZ  TYR A 130     4069   3958   3243    366     65   -223       C  
ATOM   1003  OH  TYR A 130      -3.479   3.136  24.177  1.00 30.10           O  
ANISOU 1003  OH  TYR A 130     4042   4105   3289    302     69   -275       O  
ATOM   1004  N   SER A 131      -3.454   9.277  22.659  1.00 30.63           N  
ANISOU 1004  N   SER A 131     4449   3749   3439    677     44   -236       N  
ATOM   1005  CA  SER A 131      -3.759  10.085  23.837  1.00 32.22           C  
ANISOU 1005  CA  SER A 131     4642   3925   3675    667     54   -320       C  
ATOM   1006  C   SER A 131      -3.622   9.384  25.203  1.00 30.60           C  
ANISOU 1006  C   SER A 131     4363   3801   3462    545     81   -380       C  
ATOM   1007  O   SER A 131      -3.741  10.029  26.232  1.00 32.00           O  
ANISOU 1007  O   SER A 131     4544   3959   3656    527     95   -450       O  
ATOM   1008  CB  SER A 131      -5.132  10.761  23.701  1.00 40.12           C  
ANISOU 1008  CB  SER A 131     5623   4939   4682    808     18   -402       C  
ATOM   1009  OG  SER A 131      -6.156   9.800  23.510  1.00 50.74           O  
ANISOU 1009  OG  SER A 131     6862   6418   5999    840     -7   -453       O  
ATOM   1010  N  ASER A 132      -3.333   8.086  25.190  0.50 29.68           N  
ANISOU 1010  N  ASER A 132     4192   3767   3317    467     88   -348       N  
ATOM   1011  N  BSER A 132      -3.388   8.074  25.226  0.50 29.69           N  
ANISOU 1011  N  BSER A 132     4190   3774   3318    467     88   -353       N  
ATOM   1012  CA ASER A 132      -3.199   7.323  26.427  0.50 29.24           C  
ANISOU 1012  CA ASER A 132     4079   3788   3242    354    110   -387       C  
ATOM   1013  CA BSER A 132      -3.224   7.393  26.516  0.50 29.29           C  
ANISOU 1013  CA BSER A 132     4085   3793   3249    354    111   -394       C  
ATOM   1014  C  ASER A 132      -1.742   7.075  26.809  0.50 29.00           C  
ANISOU 1014  C  ASER A 132     4085   3712   3223    241    122   -320       C  
ATOM   1015  C  BSER A 132      -1.759   7.098  26.831  0.50 29.00           C  
ANISOU 1015  C  BSER A 132     4085   3711   3223    242    122   -322       C  
ATOM   1016  O  ASER A 132      -0.817   7.559  26.146  0.50 28.71           O  
ANISOU 1016  O  ASER A 132     4110   3581   3217    242    124   -249       O  
ATOM   1017  O  BSER A 132      -0.849   7.568  26.138  0.50 28.72           O  
ANISOU 1017  O  BSER A 132     4111   3583   3218    245    124   -250       O  
ATOM   1018  CB ASER A 132      -3.943   5.991  26.307  0.50 29.40           C  
ANISOU 1018  CB ASER A 132     4009   3929   3231    337    106   -405       C  
ATOM   1019  CB BSER A 132      -4.060   6.103  26.595  0.50 29.71           C  
ANISOU 1019  CB BSER A 132     4043   3975   3270    333    111   -424       C  
ATOM   1020  OG ASER A 132      -5.313   6.211  26.025  0.50 29.45           O  
ANISOU 1020  OG ASER A 132     3962   3988   3239    437     91   -480       O  
ATOM   1021  OG BSER A 132      -4.205   5.656  27.944  0.50 28.91           O  
ANISOU 1021  OG BSER A 132     3899   3942   3143    242    141   -476       O  
ATOM   1022  N   ILE A 133      -1.542   6.322  27.886  1.00 28.37           N  
ANISOU 1022  N   ILE A 133     3965   3698   3116    143    132   -342       N  
ATOM   1023  CA  ILE A 133      -0.199   6.006  28.354  1.00 27.98           C  
ANISOU 1023  CA  ILE A 133     3937   3617   3077     40    129   -287       C  
ATOM   1024  C   ILE A 133       0.558   5.122  27.363  1.00 27.31           C  
ANISOU 1024  C   ILE A 133     3846   3526   3006     24    124   -194       C  
ATOM   1025  O   ILE A 133      -0.008   4.187  26.788  1.00 26.95           O  
ANISOU 1025  O   ILE A 133     3760   3543   2939     48    121   -183       O  
ATOM   1026  CB  ILE A 133      -0.238   5.336  29.742  1.00 27.93           C  
ANISOU 1026  CB  ILE A 133     3898   3689   3023    -49    131   -327       C  
ATOM   1027  CG1 ILE A 133      -0.812   3.913  29.659  1.00 27.45           C  
ANISOU 1027  CG1 ILE A 133     3776   3727   2927    -73    138   -312       C  
ATOM   1028  CG2 ILE A 133      -1.063   6.178  30.705  1.00 28.71           C  
ANISOU 1028  CG2 ILE A 133     4004   3808   3098    -26    147   -431       C  
ATOM   1029  CD1 ILE A 133      -0.987   3.262  31.036  1.00 27.60           C  
ANISOU 1029  CD1 ILE A 133     3776   3824   2888   -159    150   -344       C  
ATOM   1030  N   LYS A 134       1.839   5.422  27.159  1.00 27.26           N  
ANISOU 1030  N   LYS A 134     3874   3443   3041    -19    126   -133       N  
ATOM   1031  CA  LYS A 134       2.605   4.708  26.149  1.00 28.30           C  
ANISOU 1031  CA  LYS A 134     4000   3563   3190    -24    133    -50       C  
ATOM   1032  C   LYS A 134       2.668   3.196  26.403  1.00 26.19           C  
ANISOU 1032  C   LYS A 134     3677   3377   2896    -75    120    -35       C  
ATOM   1033  O   LYS A 134       2.653   2.420  25.454  1.00 25.85           O  
ANISOU 1033  O   LYS A 134     3620   3354   2849    -45    124      3       O  
ATOM   1034  CB  LYS A 134       4.000   5.314  25.960  1.00 28.87           C  
ANISOU 1034  CB  LYS A 134     4105   3543   3323    -69    147      7       C  
ATOM   1035  CG  LYS A 134       3.966   6.691  25.277  1.00 31.83           C  
ANISOU 1035  CG  LYS A 134     4547   3816   3729    -10    171     21       C  
ATOM   1036  CD  LYS A 134       5.356   7.296  25.051  1.00 37.53           C  
ANISOU 1036  CD  LYS A 134     5295   4442   4523    -69    198     79       C  
ATOM   1037  CE  LYS A 134       6.132   6.522  23.991  1.00 44.00           C  
ANISOU 1037  CE  LYS A 134     6097   5271   5351    -73    231    163       C  
ATOM   1038  NZ  LYS A 134       7.474   7.110  23.707  1.00 46.37           N1+
ANISOU 1038  NZ  LYS A 134     6408   5483   5729   -133    272    221       N1+
ATOM   1039  N   VAL A 135       2.703   2.771  27.664  1.00 26.15           N  
ANISOU 1039  N   VAL A 135     3649   3417   2871   -147    103    -66       N  
ATOM   1040  CA  VAL A 135       2.761   1.330  27.937  1.00 25.72           C  
ANISOU 1040  CA  VAL A 135     3553   3425   2793   -196     90    -43       C  
ATOM   1041  C   VAL A 135       1.459   0.591  27.595  1.00 26.73           C  
ANISOU 1041  C   VAL A 135     3646   3624   2886   -159     98    -75       C  
ATOM   1042  O   VAL A 135       1.413  -0.644  27.640  1.00 25.68           O  
ANISOU 1042  O   VAL A 135     3484   3531   2742   -196     90    -54       O  
ATOM   1043  CB  VAL A 135       3.207   0.994  29.391  1.00 29.26           C  
ANISOU 1043  CB  VAL A 135     3999   3902   3216   -285     66    -53       C  
ATOM   1044  CG1 VAL A 135       4.584   1.593  29.687  1.00 27.63           C  
ANISOU 1044  CG1 VAL A 135     3811   3630   3056   -327     43    -26       C  
ATOM   1045  CG2 VAL A 135       2.162   1.456  30.422  1.00 26.32           C  
ANISOU 1045  CG2 VAL A 135     3634   3580   2789   -290     78   -132       C  
ATOM   1046  N   SER A 136       0.401   1.333  27.268  1.00 25.92           N  
ANISOU 1046  N   SER A 136     3544   3532   2773    -87    109   -129       N  
ATOM   1047  CA  SER A 136      -0.854   0.704  26.850  1.00 25.96           C  
ANISOU 1047  CA  SER A 136     3500   3605   2758    -48    111   -169       C  
ATOM   1048  C   SER A 136      -0.883   0.510  25.336  1.00 25.80           C  
ANISOU 1048  C   SER A 136     3486   3566   2751     28     97   -138       C  
ATOM   1049  O   SER A 136      -1.842  -0.028  24.793  1.00 25.90           O  
ANISOU 1049  O   SER A 136     3458   3630   2752     67     85   -172       O  
ATOM   1050  CB  SER A 136      -2.073   1.513  27.299  1.00 26.56           C  
ANISOU 1050  CB  SER A 136     3556   3718   2819     -1    123   -255       C  
ATOM   1051  OG  SER A 136      -2.182   2.728  26.582  1.00 29.45           O  
ANISOU 1051  OG  SER A 136     3961   4025   3205     93    116   -264       O  
ATOM   1052  N   LEU A 137       0.161   0.974  24.657  1.00 25.69           N  
ANISOU 1052  N   LEU A 137     3524   3480   2758     47    101    -77       N  
ATOM   1053  CA  LEU A 137       0.297   0.713  23.228  1.00 29.94           C  
ANISOU 1053  CA  LEU A 137     4081   4002   3291    113     97    -38       C  
ATOM   1054  C   LEU A 137       0.528  -0.780  23.033  1.00 29.26           C  
ANISOU 1054  C   LEU A 137     3957   3954   3204     70     87    -21       C  
ATOM   1055  O   LEU A 137       1.193  -1.411  23.852  1.00 24.93           O  
ANISOU 1055  O   LEU A 137     3392   3407   2673    -13     89      1       O  
ATOM   1056  CB  LEU A 137       1.478   1.486  22.643  1.00 25.74           C  
ANISOU 1056  CB  LEU A 137     3611   3386   2783    125    122     30       C  
ATOM   1057  CG  LEU A 137       1.265   2.976  22.342  1.00 26.34           C  
ANISOU 1057  CG  LEU A 137     3747   3398   2863    192    132     30       C  
ATOM   1058  CD1 LEU A 137       2.589   3.602  21.967  1.00 26.52           C  
ANISOU 1058  CD1 LEU A 137     3821   3332   2921    167    169    104       C  
ATOM   1059  CD2 LEU A 137       0.252   3.154  21.225  1.00 26.72           C  
ANISOU 1059  CD2 LEU A 137     3816   3466   2871    307    110     15       C  
ATOM   1060  N   PRO A 138      -0.035  -1.352  21.958  1.00 25.27           N  
ANISOU 1060  N   PRO A 138     3443   3479   2680    129     70    -34       N  
ATOM   1061  CA  PRO A 138       0.271  -2.759  21.674  1.00 24.98           C  
ANISOU 1061  CA  PRO A 138     3380   3461   2649     93     61    -21       C  
ATOM   1062  C   PRO A 138       1.660  -2.900  21.059  1.00 26.47           C  
ANISOU 1062  C   PRO A 138     3607   3598   2854     92     84     49       C  
ATOM   1063  O   PRO A 138       2.071  -2.058  20.257  1.00 25.04           O  
ANISOU 1063  O   PRO A 138     3475   3379   2662    149    106     82       O  
ATOM   1064  CB  PRO A 138      -0.816  -3.169  20.671  1.00 25.28           C  
ANISOU 1064  CB  PRO A 138     3399   3546   2660    165     28    -72       C  
ATOM   1065  CG  PRO A 138      -1.203  -1.871  19.978  1.00 27.61           C  
ANISOU 1065  CG  PRO A 138     3739   3825   2927    265     23    -76       C  
ATOM   1066  CD  PRO A 138      -0.991  -0.764  20.999  1.00 25.74           C  
ANISOU 1066  CD  PRO A 138     3518   3554   2710    236     48    -68       C  
ATOM   1067  N   VAL A 139       2.378  -3.948  21.451  1.00 24.96           N  
ANISOU 1067  N   VAL A 139     3392   3401   2692     28     83     73       N  
ATOM   1068  CA  VAL A 139       3.664  -4.264  20.852  1.00 24.48           C  
ANISOU 1068  CA  VAL A 139     3346   3300   2655     30    106    127       C  
ATOM   1069  C   VAL A 139       3.439  -4.666  19.390  1.00 25.22           C  
ANISOU 1069  C   VAL A 139     3463   3406   2715    111    110    117       C  
ATOM   1070  O   VAL A 139       4.243  -4.345  18.519  1.00 24.91           O  
ANISOU 1070  O   VAL A 139     3459   3338   2669    151    148    158       O  
ATOM   1071  CB  VAL A 139       4.379  -5.392  21.624  1.00 24.27           C  
ANISOU 1071  CB  VAL A 139     3284   3266   2670    -43     90    147       C  
ATOM   1072  CG1 VAL A 139       5.701  -5.755  20.944  1.00 29.56           C  
ANISOU 1072  CG1 VAL A 139     3956   3899   3376    -28    116    193       C  
ATOM   1073  CG2 VAL A 139       4.622  -4.968  23.079  1.00 24.74           C  
ANISOU 1073  CG2 VAL A 139     3333   3321   2746   -118     78    157       C  
ATOM   1074  N   GLU A 140       2.329  -5.356  19.140  1.00 24.77           N  
ANISOU 1074  N   GLU A 140     3386   3393   2633    131     72     59       N  
ATOM   1075  CA  GLU A 140       1.915  -5.744  17.794  1.00 25.12           C  
ANISOU 1075  CA  GLU A 140     3452   3458   2633    210     57     30       C  
ATOM   1076  C   GLU A 140       0.407  -5.943  17.849  1.00 25.32           C  
ANISOU 1076  C   GLU A 140     3442   3539   2641    226      6    -46       C  
ATOM   1077  O   GLU A 140      -0.143  -6.136  18.932  1.00 26.41           O  
ANISOU 1077  O   GLU A 140     3531   3695   2809    159     -5    -71       O  
ATOM   1078  CB  GLU A 140       2.639  -7.017  17.309  1.00 25.12           C  
ANISOU 1078  CB  GLU A 140     3447   3445   2652    201     62     35       C  
ATOM   1079  CG  GLU A 140       2.959  -8.038  18.404  1.00 26.62           C  
ANISOU 1079  CG  GLU A 140     3590   3618   2905    109     48     40       C  
ATOM   1080  CD  GLU A 140       1.754  -8.859  18.847  1.00 26.46           C  
ANISOU 1080  CD  GLU A 140     3530   3629   2893     69      3    -21       C  
ATOM   1081  OE1 GLU A 140       0.787  -8.956  18.072  1.00 25.24           O  
ANISOU 1081  OE1 GLU A 140     3372   3512   2706    119    -26    -81       O  
ATOM   1082  OE2 GLU A 140       1.778  -9.414  19.975  1.00 30.24           O1-
ANISOU 1082  OE2 GLU A 140     3981   4098   3411    -14     -4     -8       O1-
ATOM   1083  N   THR A 141      -0.264  -5.864  16.706  1.00 25.80           N  
ANISOU 1083  N   THR A 141     3524   3629   2651    314    -25    -85       N  
ATOM   1084  CA  THR A 141      -1.728  -5.879  16.693  1.00 26.18           C  
ANISOU 1084  CA  THR A 141     3524   3734   2688    340    -80   -165       C  
ATOM   1085  C   THR A 141      -2.304  -7.265  16.383  1.00 29.57           C  
ANISOU 1085  C   THR A 141     3907   4195   3135    316   -124   -233       C  
ATOM   1086  O   THR A 141      -3.521  -7.440  16.316  1.00 26.85           O  
ANISOU 1086  O   THR A 141     3507   3902   2795    328   -173   -310       O  
ATOM   1087  CB  THR A 141      -2.314  -4.852  15.697  1.00 26.78           C  
ANISOU 1087  CB  THR A 141     3647   3830   2700    461   -110   -178       C  
ATOM   1088  CG2 THR A 141      -1.956  -3.406  16.105  1.00 26.72           C  
ANISOU 1088  CG2 THR A 141     3684   3780   2688    481    -71   -119       C  
ATOM   1089  OG1 THR A 141      -1.820  -5.114  14.381  1.00 27.13           O  
ANISOU 1089  OG1 THR A 141     3758   3868   2684    532   -113   -160       O  
ATOM   1090  N   ALA A 142      -1.426  -8.239  16.172  1.00 27.99           N  
ANISOU 1090  N   ALA A 142     3723   3959   2952    283   -107   -210       N  
ATOM   1091  CA  ALA A 142      -1.855  -9.622  15.998  1.00 26.78           C  
ANISOU 1091  CA  ALA A 142     3532   3814   2831    245   -145   -272       C  
ATOM   1092  C   ALA A 142      -2.480 -10.145  17.293  1.00 26.37           C  
ANISOU 1092  C   ALA A 142     3408   3768   2844    136   -146   -291       C  
ATOM   1093  O   ALA A 142      -3.556 -10.733  17.270  1.00 28.46           O  
ANISOU 1093  O   ALA A 142     3615   4068   3132    111   -185   -366       O  
ATOM   1094  CB  ALA A 142      -0.670 -10.506  15.574  1.00 26.40           C  
ANISOU 1094  CB  ALA A 142     3523   3714   2795    240   -122   -240       C  
ATOM   1095  N   THR A 143      -1.795  -9.929  18.414  1.00 25.86           N  
ANISOU 1095  N   THR A 143     3348   3672   2805     68   -101   -223       N  
ATOM   1096  CA  THR A 143      -2.312 -10.298  19.736  1.00 25.83           C  
ANISOU 1096  CA  THR A 143     3294   3678   2843    -36    -89   -226       C  
ATOM   1097  C   THR A 143      -2.765  -9.062  20.526  1.00 25.94           C  
ANISOU 1097  C   THR A 143     3291   3728   2836    -36    -66   -223       C  
ATOM   1098  O   THR A 143      -3.506  -9.183  21.507  1.00 25.93           O  
ANISOU 1098  O   THR A 143     3241   3757   2852   -106    -51   -246       O  
ATOM   1099  CB  THR A 143      -1.239 -11.011  20.592  1.00 25.82           C  
ANISOU 1099  CB  THR A 143     3316   3618   2877   -114    -65   -154       C  
ATOM   1100  CG2 THR A 143      -0.528 -12.093  19.782  1.00 25.62           C  
ANISOU 1100  CG2 THR A 143     3317   3542   2876    -95    -83   -151       C  
ATOM   1101  OG1 THR A 143      -0.282 -10.045  21.063  1.00 27.63           O  
ANISOU 1101  OG1 THR A 143     3580   3828   3089   -104    -35    -88       O  
ATOM   1102  N   ASN A 144      -2.314  -7.881  20.100  1.00 25.55           N  
ANISOU 1102  N   ASN A 144     3287   3671   2751     40    -56   -195       N  
ATOM   1103  CA  ASN A 144      -2.576  -6.632  20.828  1.00 25.51           C  
ANISOU 1103  CA  ASN A 144     3280   3681   2732     48    -34   -191       C  
ATOM   1104  C   ASN A 144      -1.998  -6.579  22.244  1.00 28.53           C  
ANISOU 1104  C   ASN A 144     3666   4044   3130    -45      2   -146       C  
ATOM   1105  O   ASN A 144      -2.407  -5.739  23.046  1.00 28.62           O  
ANISOU 1105  O   ASN A 144     3666   4077   3130    -55     20   -162       O  
ATOM   1106  CB  ASN A 144      -4.077  -6.313  20.881  1.00 28.38           C  
ANISOU 1106  CB  ASN A 144     3579   4112   3094     74    -55   -274       C  
ATOM   1107  CG  ASN A 144      -4.631  -5.911  19.531  1.00 30.40           C  
ANISOU 1107  CG  ASN A 144     3843   4389   3319    191   -103   -316       C  
ATOM   1108  ND2 ASN A 144      -5.731  -6.535  19.131  1.00 27.06           N  
ANISOU 1108  ND2 ASN A 144     3352   4020   2911    201   -147   -397       N  
ATOM   1109  OD1 ASN A 144      -4.069  -5.059  18.851  1.00 28.28           O  
ANISOU 1109  OD1 ASN A 144     3644   4089   3014    271   -102   -275       O  
ATOM   1110  N   THR A 145      -1.055  -7.470  22.553  1.00 24.93           N  
ANISOU 1110  N   THR A 145     3228   3549   2697   -104      6    -94       N  
ATOM   1111  CA  THR A 145      -0.371  -7.445  23.841  1.00 24.75           C  
ANISOU 1111  CA  THR A 145     3219   3506   2679   -182     25    -45       C  
ATOM   1112  C   THR A 145       0.248  -6.063  24.098  1.00 27.48           C  
ANISOU 1112  C   THR A 145     3599   3833   3011   -153     42    -20       C  
ATOM   1113  O   THR A 145       1.028  -5.565  23.284  1.00 24.46           O  
ANISOU 1113  O   THR A 145     3247   3412   2633    -99     46     10       O  
ATOM   1114  CB  THR A 145       0.748  -8.496  23.896  1.00 24.58           C  
ANISOU 1114  CB  THR A 145     3217   3433   2689   -220     14     13       C  
ATOM   1115  CG2 THR A 145       1.408  -8.512  25.272  1.00 24.55           C  
ANISOU 1115  CG2 THR A 145     3229   3415   2684   -296     16     63       C  
ATOM   1116  OG1 THR A 145       0.195  -9.785  23.610  1.00 24.83           O  
ANISOU 1116  OG1 THR A 145     3226   3466   2743   -246     -3    -12       O  
ATOM   1117  N   THR A 146      -0.114  -5.444  25.220  1.00 24.74           N  
ANISOU 1117  N   THR A 146     3246   3509   2644   -193     56    -37       N  
ATOM   1118  CA  THR A 146       0.425  -4.128  25.562  1.00 24.72           C  
ANISOU 1118  CA  THR A 146     3277   3480   2635   -174     67    -26       C  
ATOM   1119  C   THR A 146       1.889  -4.230  25.963  1.00 24.51           C  
ANISOU 1119  C   THR A 146     3279   3404   2631   -218     60     39       C  
ATOM   1120  O   THR A 146       2.349  -5.293  26.408  1.00 24.45           O  
ANISOU 1120  O   THR A 146     3264   3393   2633   -273     44     72       O  
ATOM   1121  CB  THR A 146      -0.348  -3.479  26.736  1.00 25.07           C  
ANISOU 1121  CB  THR A 146     3310   3565   2649   -205     85    -74       C  
ATOM   1122  CG2 THR A 146      -1.818  -3.249  26.360  1.00 25.43           C  
ANISOU 1122  CG2 THR A 146     3311   3665   2685   -154     93   -149       C  
ATOM   1123  OG1 THR A 146      -0.265  -4.330  27.895  1.00 25.17           O  
ANISOU 1123  OG1 THR A 146     3317   3602   2644   -298     88    -58       O  
ATOM   1124  N   TYR A 147       2.620  -3.129  25.808  1.00 24.53           N  
ANISOU 1124  N   TYR A 147     3310   3364   2648   -193     69     57       N  
ATOM   1125  CA  TYR A 147       3.989  -3.057  26.295  1.00 24.51           C  
ANISOU 1125  CA  TYR A 147     3317   3319   2677   -239     58    105       C  
ATOM   1126  C   TYR A 147       4.034  -3.414  27.792  1.00 24.67           C  
ANISOU 1126  C   TYR A 147     3336   3366   2673   -318     33    101       C  
ATOM   1127  O   TYR A 147       4.912  -4.150  28.230  1.00 24.68           O  
ANISOU 1127  O   TYR A 147     3332   3354   2691   -361      4    144       O  
ATOM   1128  CB  TYR A 147       4.626  -1.677  26.012  1.00 24.70           C  
ANISOU 1128  CB  TYR A 147     3368   3289   2727   -214     76    114       C  
ATOM   1129  CG  TYR A 147       5.191  -1.557  24.600  1.00 26.30           C  
ANISOU 1129  CG  TYR A 147     3581   3452   2958   -157    104    153       C  
ATOM   1130  CD1 TYR A 147       6.475  -2.014  24.304  1.00 26.49           C  
ANISOU 1130  CD1 TYR A 147     3588   3446   3030   -178    110    204       C  
ATOM   1131  CD2 TYR A 147       4.429  -1.034  23.563  1.00 24.78           C  
ANISOU 1131  CD2 TYR A 147     3418   3259   2740    -77    125    139       C  
ATOM   1132  CE1 TYR A 147       6.991  -1.935  23.023  1.00 24.77           C  
ANISOU 1132  CE1 TYR A 147     3381   3201   2829   -128    151    238       C  
ATOM   1133  CE2 TYR A 147       4.941  -0.941  22.270  1.00 24.90           C  
ANISOU 1133  CE2 TYR A 147     3457   3244   2762    -24    157    180       C  
ATOM   1134  CZ  TYR A 147       6.226  -1.394  22.010  1.00 24.90           C  
ANISOU 1134  CZ  TYR A 147     3439   3217   2804    -53    177    229       C  
ATOM   1135  OH  TYR A 147       6.745  -1.316  20.734  1.00 25.15           O  
ANISOU 1135  OH  TYR A 147     3496   3225   2834     -2    223    269       O  
ATOM   1136  N   LEU A 148       3.072  -2.922  28.562  1.00 24.92           N  
ANISOU 1136  N   LEU A 148     3373   3438   2659   -331     44     50       N  
ATOM   1137  CA  LEU A 148       3.048  -3.207  29.998  1.00 25.24           C  
ANISOU 1137  CA  LEU A 148     3425   3511   2654   -404     30     45       C  
ATOM   1138  C   LEU A 148       2.987  -4.719  30.281  1.00 25.23           C  
ANISOU 1138  C   LEU A 148     3414   3531   2640   -451     16     85       C  
ATOM   1139  O   LEU A 148       3.792  -5.248  31.039  1.00 25.40           O  
ANISOU 1139  O   LEU A 148     3455   3542   2655   -500    -20    130       O  
ATOM   1140  CB  LEU A 148       1.873  -2.506  30.680  1.00 25.63           C  
ANISOU 1140  CB  LEU A 148     3478   3611   2651   -403     61    -26       C  
ATOM   1141  CG  LEU A 148       1.793  -2.733  32.197  1.00 26.14           C  
ANISOU 1141  CG  LEU A 148     3565   3719   2647   -477     57    -35       C  
ATOM   1142  CD1 LEU A 148       3.019  -2.122  32.873  1.00 26.34           C  
ANISOU 1142  CD1 LEU A 148     3628   3707   2673   -505     13    -19       C  
ATOM   1143  CD2 LEU A 148       0.507  -2.150  32.788  1.00 27.74           C  
ANISOU 1143  CD2 LEU A 148     3760   3983   2797   -471    106   -115       C  
ATOM   1144  N   ALA A 149       2.032  -5.406  29.666  1.00 25.14           N  
ANISOU 1144  N   ALA A 149     3376   3544   2632   -436     38     68       N  
ATOM   1145  CA  ALA A 149       1.891  -6.858  29.862  1.00 27.94           C  
ANISOU 1145  CA  ALA A 149     3726   3904   2987   -484     29    103       C  
ATOM   1146  C   ALA A 149       3.112  -7.619  29.344  1.00 26.56           C  
ANISOU 1146  C   ALA A 149     3558   3669   2864   -474    -10    165       C  
ATOM   1147  O   ALA A 149       3.574  -8.573  29.960  1.00 25.64           O  
ANISOU 1147  O   ALA A 149     3460   3536   2747   -520    -39    214       O  
ATOM   1148  CB  ALA A 149       0.625  -7.370  29.193  1.00 25.31           C  
ANISOU 1148  CB  ALA A 149     3352   3602   2661   -470     57     59       C  
ATOM   1149  N   TYR A 150       3.619  -7.184  28.199  1.00 26.18           N  
ANISOU 1149  N   TYR A 150     3497   3591   2861   -408     -8    163       N  
ATOM   1150  CA  TYR A 150       4.804  -7.764  27.587  1.00 24.54           C  
ANISOU 1150  CA  TYR A 150     3284   3332   2707   -387    -32    210       C  
ATOM   1151  C   TYR A 150       6.008  -7.765  28.536  1.00 27.72           C  
ANISOU 1151  C   TYR A 150     3697   3711   3123   -426    -73    256       C  
ATOM   1152  O   TYR A 150       6.638  -8.801  28.730  1.00 26.39           O  
ANISOU 1152  O   TYR A 150     3528   3516   2981   -441   -109    299       O  
ATOM   1153  CB  TYR A 150       5.135  -7.002  26.316  1.00 24.30           C  
ANISOU 1153  CB  TYR A 150     3246   3282   2705   -314     -5    198       C  
ATOM   1154  CG  TYR A 150       6.357  -7.490  25.574  1.00 28.44           C  
ANISOU 1154  CG  TYR A 150     3757   3763   3286   -285    -10    238       C  
ATOM   1155  CD1 TYR A 150       6.299  -8.604  24.744  1.00 32.36           C  
ANISOU 1155  CD1 TYR A 150     4247   4247   3803   -255    -11    237       C  
ATOM   1156  CD2 TYR A 150       7.563  -6.813  25.682  1.00 29.94           C  
ANISOU 1156  CD2 TYR A 150     3936   3924   3514   -288    -10    267       C  
ATOM   1157  CE1 TYR A 150       7.432  -9.040  24.050  1.00 33.10           C  
ANISOU 1157  CE1 TYR A 150     4324   4304   3948   -220     -7    264       C  
ATOM   1158  CE2 TYR A 150       8.685  -7.226  24.987  1.00 28.11           C  
ANISOU 1158  CE2 TYR A 150     3679   3660   3342   -260     -4    297       C  
ATOM   1159  CZ  TYR A 150       8.618  -8.335  24.179  1.00 32.02           C  
ANISOU 1159  CZ  TYR A 150     4169   4147   3850   -222      1    295       C  
ATOM   1160  OH  TYR A 150       9.752  -8.727  23.505  1.00 35.73           O  
ANISOU 1160  OH  TYR A 150     4609   4589   4380   -188     15    317       O  
ATOM   1161  N   TYR A 151       6.324  -6.617  29.132  1.00 24.88           N  
ANISOU 1161  N   TYR A 151     3346   3358   2747   -440    -76    243       N  
ATOM   1162  CA  TYR A 151       7.438  -6.558  30.076  1.00 25.24           C  
ANISOU 1162  CA  TYR A 151     3396   3389   2804   -478   -129    276       C  
ATOM   1163  C   TYR A 151       7.170  -7.374  31.349  1.00 26.52           C  
ANISOU 1163  C   TYR A 151     3593   3577   2906   -536   -168    300       C  
ATOM   1164  O   TYR A 151       8.049  -8.100  31.828  1.00 28.12           O  
ANISOU 1164  O   TYR A 151     3800   3758   3126   -552   -225    349       O  
ATOM   1165  CB  TYR A 151       7.745  -5.114  30.475  1.00 26.10           C  
ANISOU 1165  CB  TYR A 151     3511   3497   2910   -486   -128    243       C  
ATOM   1166  CG  TYR A 151       8.191  -4.208  29.346  1.00 25.20           C  
ANISOU 1166  CG  TYR A 151     3375   3345   2857   -440    -89    235       C  
ATOM   1167  CD1 TYR A 151       9.151  -4.613  28.422  1.00 25.18           C  
ANISOU 1167  CD1 TYR A 151     3335   3306   2925   -411    -83    272       C  
ATOM   1168  CD2 TYR A 151       7.653  -2.939  29.215  1.00 25.22           C  
ANISOU 1168  CD2 TYR A 151     3397   3343   2844   -424    -54    191       C  
ATOM   1169  CE1 TYR A 151       9.558  -3.766  27.393  1.00 25.12           C  
ANISOU 1169  CE1 TYR A 151     3316   3265   2964   -375    -33    273       C  
ATOM   1170  CE2 TYR A 151       8.042  -2.093  28.194  1.00 29.98           C  
ANISOU 1170  CE2 TYR A 151     3994   3900   3496   -385    -15    196       C  
ATOM   1171  CZ  TYR A 151       8.991  -2.505  27.290  1.00 29.82           C  
ANISOU 1171  CZ  TYR A 151     3943   3850   3538   -365      0    240       C  
ATOM   1172  OH  TYR A 151       9.358  -1.636  26.289  1.00 33.33           O  
ANISOU 1172  OH  TYR A 151     4391   4251   4022   -331     52    252       O  
ATOM   1173  N   LEU A 152       5.966  -7.242  31.903  1.00 25.77           N  
ANISOU 1173  N   LEU A 152     3525   3530   2739   -565   -134    267       N  
ATOM   1174  CA  LEU A 152       5.634  -7.891  33.177  1.00 27.13           C  
ANISOU 1174  CA  LEU A 152     3742   3732   2835   -627   -153    293       C  
ATOM   1175  C   LEU A 152       5.568  -9.417  33.078  1.00 26.52           C  
ANISOU 1175  C   LEU A 152     3675   3628   2773   -645   -167    351       C  
ATOM   1176  O   LEU A 152       6.041 -10.125  33.967  1.00 27.09           O  
ANISOU 1176  O   LEU A 152     3789   3689   2815   -681   -216    408       O  
ATOM   1177  CB  LEU A 152       4.323  -7.338  33.763  1.00 26.58           C  
ANISOU 1177  CB  LEU A 152     3687   3725   2686   -655    -94    237       C  
ATOM   1178  CG  LEU A 152       4.413  -5.944  34.404  1.00 29.08           C  
ANISOU 1178  CG  LEU A 152     4020   4066   2962   -653    -94    182       C  
ATOM   1179  CD1 LEU A 152       3.037  -5.354  34.679  1.00 26.99           C  
ANISOU 1179  CD1 LEU A 152     3754   3861   2641   -657    -24    111       C  
ATOM   1180  CD2 LEU A 152       5.237  -5.995  35.690  1.00 35.10           C  
ANISOU 1180  CD2 LEU A 152     4832   4837   3665   -699   -158    212       C  
ATOM   1181  N   ARG A 153       4.974  -9.925  32.008  1.00 26.14           N  
ANISOU 1181  N   ARG A 153     3596   3565   2772   -618   -130    335       N  
ATOM   1182  CA  ARG A 153       4.902 -11.366  31.842  1.00 26.38           C  
ANISOU 1182  CA  ARG A 153     3638   3555   2830   -635   -143    380       C  
ATOM   1183  C   ARG A 153       6.286 -11.962  31.608  1.00 27.04           C  
ANISOU 1183  C   ARG A 153     3720   3577   2979   -601   -208    433       C  
ATOM   1184  O   ARG A 153       6.615 -13.017  32.149  1.00 27.66           O  
ANISOU 1184  O   ARG A 153     3835   3617   3059   -626   -251    493       O  
ATOM   1185  CB  ARG A 153       3.904 -11.747  30.745  1.00 30.13           C  
ANISOU 1185  CB  ARG A 153     4078   4031   3341   -616    -96    334       C  
ATOM   1186  CG  ARG A 153       2.481 -11.463  31.182  1.00 33.09           C  
ANISOU 1186  CG  ARG A 153     4445   4469   3659   -661    -38    287       C  
ATOM   1187  CD  ARG A 153       1.496 -12.442  30.610  1.00 42.95           C  
ANISOU 1187  CD  ARG A 153     5669   5709   4940   -684    -11    266       C  
ATOM   1188  NE  ARG A 153       0.162 -12.192  31.148  1.00 50.20           N  
ANISOU 1188  NE  ARG A 153     6566   6695   5811   -735     49    221       N  
ATOM   1189  CZ  ARG A 153      -0.756 -11.445  30.543  1.00 53.42           C  
ANISOU 1189  CZ  ARG A 153     6917   7155   6226   -699     83    140       C  
ATOM   1190  NH1 ARG A 153      -0.487 -10.888  29.366  1.00 45.87           N1+
ANISOU 1190  NH1 ARG A 153     5935   6187   5308   -611     61    105       N1+
ATOM   1191  NH2 ARG A 153      -1.945 -11.265  31.109  1.00 54.10           N  
ANISOU 1191  NH2 ARG A 153     6973   7307   6277   -746    140     95       N  
ATOM   1192  N   TRP A 154       7.112 -11.265  30.838  1.00 26.05           N  
ANISOU 1192  N   TRP A 154     3552   3438   2907   -544   -214    414       N  
ATOM   1193  CA  TRP A 154       8.487 -11.710  30.635  1.00 26.24           C  
ANISOU 1193  CA  TRP A 154     3555   3412   3002   -509   -269    454       C  
ATOM   1194  C   TRP A 154       9.264 -11.704  31.953  1.00 30.05           C  
ANISOU 1194  C   TRP A 154     4066   3898   3454   -542   -343    500       C  
ATOM   1195  O   TRP A 154       9.952 -12.680  32.288  1.00 27.41           O  
ANISOU 1195  O   TRP A 154     3745   3522   3148   -535   -406    554       O  
ATOM   1196  CB  TRP A 154       9.184 -10.843  29.587  1.00 26.62           C  
ANISOU 1196  CB  TRP A 154     3549   3456   3111   -452   -242    423       C  
ATOM   1197  CG  TRP A 154      10.644 -11.161  29.416  1.00 26.16           C  
ANISOU 1197  CG  TRP A 154     3448   3357   3133   -418   -289    455       C  
ATOM   1198  CD1 TRP A 154      11.181 -12.192  28.705  1.00 28.17           C  
ANISOU 1198  CD1 TRP A 154     3681   3567   3457   -371   -298    472       C  
ATOM   1199  CD2 TRP A 154      11.745 -10.434  29.966  1.00 27.19           C  
ANISOU 1199  CD2 TRP A 154     3547   3492   3293   -426   -332    464       C  
ATOM   1200  CE2 TRP A 154      12.924 -11.083  29.547  1.00 29.39           C  
ANISOU 1200  CE2 TRP A 154     3772   3732   3662   -381   -365    488       C  
ATOM   1201  CE3 TRP A 154      11.846  -9.301  30.775  1.00 29.62           C  
ANISOU 1201  CE3 TRP A 154     3861   3831   3563   -466   -349    445       C  
ATOM   1202  NE1 TRP A 154      12.556 -12.153  28.782  1.00 29.21           N  
ANISOU 1202  NE1 TRP A 154     3760   3679   3660   -345   -341    492       N  
ATOM   1203  CZ2 TRP A 154      14.189 -10.628  29.903  1.00 28.35           C  
ANISOU 1203  CZ2 TRP A 154     3583   3598   3592   -379   -414    495       C  
ATOM   1204  CZ3 TRP A 154      13.105  -8.854  31.127  1.00 40.92           C  
ANISOU 1204  CZ3 TRP A 154     5243   5253   5051   -468   -403    451       C  
ATOM   1205  CH2 TRP A 154      14.259  -9.516  30.690  1.00 37.15           C  
ANISOU 1205  CH2 TRP A 154     4702   4743   4670   -427   -436    476       C  
ATOM   1206  N   ALA A 155       9.135 -10.621  32.713  1.00 26.93           N  
ANISOU 1206  N   ALA A 155     3685   3550   2998   -574   -343    474       N  
ATOM   1207  CA  ALA A 155       9.792 -10.538  34.019  1.00 31.06           C  
ANISOU 1207  CA  ALA A 155     4242   4086   3473   -606   -422    506       C  
ATOM   1208  C   ALA A 155       9.338 -11.641  34.983  1.00 31.29           C  
ANISOU 1208  C   ALA A 155     4349   4114   3428   -649   -450    566       C  
ATOM   1209  O   ALA A 155      10.163 -12.236  35.679  1.00 30.62           O  
ANISOU 1209  O   ALA A 155     4290   4005   3338   -647   -537    623       O  
ATOM   1210  CB  ALA A 155       9.596  -9.158  34.650  1.00 30.12           C  
ANISOU 1210  CB  ALA A 155     4133   4017   3294   -634   -411    452       C  
ATOM   1211  N   GLN A 156       8.037 -11.910  35.042  1.00 28.72           N  
ANISOU 1211  N   GLN A 156     4056   3811   3044   -688   -379    556       N  
ATOM   1212  CA  GLN A 156       7.551 -12.962  35.936  1.00 33.11           C  
ANISOU 1212  CA  GLN A 156     4690   4360   3531   -741   -388    621       C  
ATOM   1213  C   GLN A 156       7.991 -14.345  35.460  1.00 32.67           C  
ANISOU 1213  C   GLN A 156     4640   4220   3552   -716   -427    683       C  
ATOM   1214  O   GLN A 156       8.218 -15.249  36.264  1.00 30.16           O  
ANISOU 1214  O   GLN A 156     4393   3870   3199   -739   -478    761       O  
ATOM   1215  CB  GLN A 156       6.032 -12.892  36.130  1.00 29.56           C  
ANISOU 1215  CB  GLN A 156     4261   3960   3012   -798   -291    589       C  
ATOM   1216  CG  GLN A 156       5.601 -11.749  37.051  1.00 31.75           C  
ANISOU 1216  CG  GLN A 156     4562   4318   3184   -830   -264    543       C  
ATOM   1217  CD  GLN A 156       4.119 -11.760  37.344  1.00 30.93           C  
ANISOU 1217  CD  GLN A 156     4470   4269   3013   -886   -163    512       C  
ATOM   1218  NE2 GLN A 156       3.763 -11.899  38.623  1.00 31.60           N  
ANISOU 1218  NE2 GLN A 156     4630   4398   2977   -947   -148    543       N  
ATOM   1219  OE1 GLN A 156       3.299 -11.648  36.436  1.00 31.71           O  
ANISOU 1219  OE1 GLN A 156     4508   4375   3166   -873   -100    458       O  
ATOM   1220  N   ARG A 157       8.137 -14.494  34.150  1.00 31.06           N  
ANISOU 1220  N   ARG A 157     4370   3980   3450   -664   -403    649       N  
ATOM   1221  CA  ARG A 157       8.611 -15.744  33.580  1.00 28.87           C  
ANISOU 1221  CA  ARG A 157     4092   3619   3258   -628   -438    689       C  
ATOM   1222  C   ARG A 157      10.069 -15.989  33.968  1.00 33.29           C  
ANISOU 1222  C   ARG A 157     4647   4141   3859   -580   -540    739       C  
ATOM   1223  O   ARG A 157      10.412 -17.061  34.464  1.00 31.01           O  
ANISOU 1223  O   ARG A 157     4412   3794   3578   -578   -602    810       O  
ATOM   1224  CB  ARG A 157       8.445 -15.735  32.057  1.00 28.44           C  
ANISOU 1224  CB  ARG A 157     3971   3547   3290   -576   -386    627       C  
ATOM   1225  CG  ARG A 157       9.042 -16.952  31.352  1.00 33.08           C  
ANISOU 1225  CG  ARG A 157     4550   4045   3972   -524   -420    650       C  
ATOM   1226  CD  ARG A 157       8.553 -18.254  31.969  1.00 39.49           C  
ANISOU 1226  CD  ARG A 157     5440   4795   4771   -573   -440    713       C  
ATOM   1227  NE  ARG A 157       7.111 -18.445  31.832  1.00 43.97           N  
ANISOU 1227  NE  ARG A 157     6024   5379   5303   -640   -366    683       N  
ATOM   1228  CZ  ARG A 157       6.377 -19.184  32.662  1.00 57.98           C  
ANISOU 1228  CZ  ARG A 157     7868   7130   7031   -719   -354    735       C  
ATOM   1229  NH1 ARG A 157       5.066 -19.306  32.475  1.00 55.92           N1+
ANISOU 1229  NH1 ARG A 157     7602   6892   6754   -783   -279    696       N1+
ATOM   1230  NH2 ARG A 157       6.953 -19.795  33.691  1.00 61.53           N  
ANISOU 1230  NH2 ARG A 157     8394   7535   7451   -736   -417    829       N  
ATOM   1231  N   VAL A 158      10.923 -14.989  33.773  1.00 29.11           N  
ANISOU 1231  N   VAL A 158     4054   3645   3362   -544   -562    702       N  
ATOM   1232  CA  VAL A 158      12.355 -15.161  34.019  1.00 31.97           C  
ANISOU 1232  CA  VAL A 158     4382   3978   3785   -494   -660    733       C  
ATOM   1233  C   VAL A 158      12.758 -14.980  35.488  1.00 36.59           C  
ANISOU 1233  C   VAL A 158     5024   4594   4286   -526   -752    778       C  
ATOM   1234  O   VAL A 158      13.818 -15.451  35.910  1.00 35.20           O  
ANISOU 1234  O   VAL A 158     4841   4387   4148   -486   -856    821       O  
ATOM   1235  CB  VAL A 158      13.206 -14.239  33.122  1.00 29.20           C  
ANISOU 1235  CB  VAL A 158     3927   3645   3525   -446   -641    675       C  
ATOM   1236  CG1 VAL A 158      12.833 -14.443  31.660  1.00 28.49           C  
ANISOU 1236  CG1 VAL A 158     3795   3531   3499   -408   -553    634       C  
ATOM   1237  CG2 VAL A 158      13.062 -12.762  33.541  1.00 28.89           C  
ANISOU 1237  CG2 VAL A 158     3876   3673   3429   -487   -620    627       C  
ATOM   1238  N   GLY A 159      11.909 -14.314  36.265  1.00 31.23           N  
ANISOU 1238  N   GLY A 159     4402   3976   3488   -591   -717    763       N  
ATOM   1239  CA  GLY A 159      12.210 -14.050  37.662  1.00 31.47           C  
ANISOU 1239  CA  GLY A 159     4497   4046   3415   -622   -798    794       C  
ATOM   1240  C   GLY A 159      11.228 -14.677  38.629  1.00 32.92           C  
ANISOU 1240  C   GLY A 159     4800   4241   3466   -685   -777    853       C  
ATOM   1241  O   GLY A 159      11.386 -14.564  39.849  1.00 33.06           O  
ANISOU 1241  O   GLY A 159     4895   4296   3372   -712   -840    887       O  
ATOM   1242  N   GLY A 160      10.225 -15.364  38.090  1.00 33.59           N  
ANISOU 1242  N   GLY A 160     4904   4296   3564   -710   -688    864       N  
ATOM   1243  CA  GLY A 160       9.193 -15.969  38.917  1.00 38.25           C  
ANISOU 1243  CA  GLY A 160     5597   4895   4041   -783   -643    918       C  
ATOM   1244  C   GLY A 160       8.106 -14.965  39.260  1.00 38.85           C  
ANISOU 1244  C   GLY A 160     5678   5063   4020   -842   -545    852       C  
ATOM   1245  O   GLY A 160       8.282 -13.756  39.084  1.00 33.61           O  
ANISOU 1245  O   GLY A 160     4958   4452   3362   -823   -538    773       O  
ATOM   1246  N   LYS A 161       6.980 -15.463  39.753  1.00 34.69           N  
ANISOU 1246  N   LYS A 161     5218   4552   3412   -914   -467    883       N  
ATOM   1247  CA  LYS A 161       5.837 -14.611  40.061  1.00 40.28           C  
ANISOU 1247  CA  LYS A 161     5921   5349   4036   -966   -362    815       C  
ATOM   1248  C   LYS A 161       6.189 -13.468  41.009  1.00 36.84           C  
ANISOU 1248  C   LYS A 161     5513   4991   3492   -966   -397    775       C  
ATOM   1249  O   LYS A 161       5.623 -12.383  40.913  1.00 33.35           O  
ANISOU 1249  O   LYS A 161     5029   4614   3029   -970   -334    684       O  
ATOM   1250  CB  LYS A 161       4.705 -15.442  40.663  1.00 45.22           C  
ANISOU 1250  CB  LYS A 161     6619   5981   4583  -1054   -277    868       C  
ATOM   1251  CG  LYS A 161       3.443 -14.648  40.954  1.00 53.32           C  
ANISOU 1251  CG  LYS A 161     7625   7104   5531  -1107   -156    791       C  
ATOM   1252  CD  LYS A 161       2.389 -15.513  41.635  1.00 61.31           C  
ANISOU 1252  CD  LYS A 161     8705   8125   6466  -1204    -63    851       C  
ATOM   1253  CE  LYS A 161       1.059 -14.779  41.734  1.00 69.87           C  
ANISOU 1253  CE  LYS A 161     9737   9307   7505  -1250     70    760       C  
ATOM   1254  NZ  LYS A 161       0.597 -14.285  40.398  1.00 73.91           N1+
ANISOU 1254  NZ  LYS A 161    10117   9819   8148  -1204    103    657       N1+
ATOM   1255  N   GLU A 162       7.125 -13.721  41.919  1.00 35.46           N  
ANISOU 1255  N   GLU A 162     5412   4808   3254   -956   -506    840       N  
ATOM   1256  CA  GLU A 162       7.472 -12.767  42.971  1.00 40.59           C  
ANISOU 1256  CA  GLU A 162     6107   5532   3783   -962   -554    805       C  
ATOM   1257  C   GLU A 162       8.561 -11.781  42.556  1.00 36.64           C  
ANISOU 1257  C   GLU A 162     5523   5029   3369   -902   -639    735       C  
ATOM   1258  O   GLU A 162       9.146 -11.099  43.402  1.00 34.46           O  
ANISOU 1258  O   GLU A 162     5280   4797   3018   -899   -716    708       O  
ATOM   1259  CB  GLU A 162       7.938 -13.520  44.220  1.00 42.30           C  
ANISOU 1259  CB  GLU A 162     6452   5747   3873   -980   -643    909       C  
ATOM   1260  CG  GLU A 162       6.998 -14.630  44.657  1.00 60.63           C  
ANISOU 1260  CG  GLU A 162     8869   8051   6115  -1047   -563   1002       C  
ATOM   1261  CD  GLU A 162       5.734 -14.109  45.312  1.00 75.60           C  
ANISOU 1261  CD  GLU A 162    10807  10042   7876  -1121   -429    957       C  
ATOM   1262  OE1 GLU A 162       5.794 -13.042  45.961  1.00 81.15           O  
ANISOU 1262  OE1 GLU A 162    11525  10827   8482  -1118   -438    884       O  
ATOM   1263  OE2 GLU A 162       4.681 -14.772  45.178  1.00 81.04           O1-
ANISOU 1263  OE2 GLU A 162    11509  10722   8562  -1182   -313    989       O1-
ATOM   1264  N   VAL A 163       8.844 -11.716  41.263  1.00 33.43           N  
ANISOU 1264  N   VAL A 163     5012   4572   3119   -857   -624    704       N  
ATOM   1265  CA  VAL A 163       9.904 -10.846  40.755  1.00 32.21           C  
ANISOU 1265  CA  VAL A 163     4770   4404   3062   -807   -688    647       C  
ATOM   1266  C   VAL A 163       9.742  -9.395  41.239  1.00 32.23           C  
ANISOU 1266  C   VAL A 163     4771   4472   3004   -825   -673    552       C  
ATOM   1267  O   VAL A 163       8.644  -8.839  41.204  1.00 32.40           O  
ANISOU 1267  O   VAL A 163     4801   4535   2976   -851   -569    496       O  
ATOM   1268  CB  VAL A 163       9.967 -10.901  39.206  1.00 31.02           C  
ANISOU 1268  CB  VAL A 163     4516   4201   3069   -763   -635    622       C  
ATOM   1269  CG1 VAL A 163       8.655 -10.421  38.597  1.00 33.82           C  
ANISOU 1269  CG1 VAL A 163     4851   4584   3416   -782   -505    562       C  
ATOM   1270  CG2 VAL A 163      11.161 -10.082  38.669  1.00 30.72           C  
ANISOU 1270  CG2 VAL A 163     4388   4145   3140   -718   -692    577       C  
ATOM   1271  N   PRO A 164      10.837  -8.784  41.720  1.00 32.78           N  
ANISOU 1271  N   PRO A 164     4826   4547   3080   -811   -780    526       N  
ATOM   1272  CA  PRO A 164      10.794  -7.368  42.116  1.00 34.92           C  
ANISOU 1272  CA  PRO A 164     5092   4863   3313   -827   -775    425       C  
ATOM   1273  C   PRO A 164      10.662  -6.484  40.886  1.00 34.37           C  
ANISOU 1273  C   PRO A 164     4926   4761   3371   -804   -698    357       C  
ATOM   1274  O   PRO A 164      11.494  -6.570  39.984  1.00 33.27           O  
ANISOU 1274  O   PRO A 164     4704   4568   3368   -770   -724    370       O  
ATOM   1275  CB  PRO A 164      12.166  -7.130  42.763  1.00 34.89           C  
ANISOU 1275  CB  PRO A 164     5078   4857   3321   -816   -927    421       C  
ATOM   1276  CG  PRO A 164      12.749  -8.503  42.994  1.00 38.46           C  
ANISOU 1276  CG  PRO A 164     5559   5282   3774   -793  -1013    530       C  
ATOM   1277  CD  PRO A 164      12.163  -9.383  41.940  1.00 35.07           C  
ANISOU 1277  CD  PRO A 164     5101   4803   3422   -778   -918    582       C  
ATOM   1278  N   PHE A 165       9.644  -5.634  40.850  1.00 31.92           N  
ANISOU 1278  N   PHE A 165     4629   4481   3016   -818   -603    285       N  
ATOM   1279  CA  PHE A 165       9.411  -4.818  39.668  1.00 35.27           C  
ANISOU 1279  CA  PHE A 165     4980   4872   3551   -790   -530    231       C  
ATOM   1280  C   PHE A 165       8.963  -3.430  40.096  1.00 35.43           C  
ANISOU 1280  C   PHE A 165     5019   4917   3524   -801   -498    130       C  
ATOM   1281  O   PHE A 165       8.116  -3.279  40.982  1.00 35.47           O  
ANISOU 1281  O   PHE A 165     5092   4982   3404   -825   -463     96       O  
ATOM   1282  CB  PHE A 165       8.350  -5.474  38.782  1.00 29.63           C  
ANISOU 1282  CB  PHE A 165     4249   4153   2858   -774   -428    257       C  
ATOM   1283  CG  PHE A 165       8.397  -5.048  37.336  1.00 28.68           C  
ANISOU 1283  CG  PHE A 165     4051   3983   2863   -728   -378    236       C  
ATOM   1284  CD1 PHE A 165       7.944  -3.795  36.950  1.00 28.40           C  
ANISOU 1284  CD1 PHE A 165     3999   3945   2846   -711   -324    160       C  
ATOM   1285  CD2 PHE A 165       8.868  -5.916  36.358  1.00 28.19           C  
ANISOU 1285  CD2 PHE A 165     3942   3875   2893   -698   -384    293       C  
ATOM   1286  CE1 PHE A 165       7.973  -3.410  35.608  1.00 30.37           C  
ANISOU 1286  CE1 PHE A 165     4194   4149   3197   -666   -277    152       C  
ATOM   1287  CE2 PHE A 165       8.900  -5.539  35.019  1.00 27.45           C  
ANISOU 1287  CE2 PHE A 165     3790   3744   2896   -653   -332    276       C  
ATOM   1288  CZ  PHE A 165       8.455  -4.277  34.645  1.00 27.20           C  
ANISOU 1288  CZ  PHE A 165     3750   3712   2874   -639   -280    210       C  
ATOM   1289  N   VAL A 166       9.548  -2.418  39.474  1.00 30.42           N  
ANISOU 1289  N   VAL A 166     4331   4234   2994   -784   -505     81       N  
ATOM   1290  CA  VAL A 166       9.189  -1.040  39.766  1.00 30.71           C  
ANISOU 1290  CA  VAL A 166     4386   4272   3011   -788   -478    -19       C  
ATOM   1291  C   VAL A 166       8.676  -0.371  38.507  1.00 29.87           C  
ANISOU 1291  C   VAL A 166     4233   4117   2998   -748   -389    -44       C  
ATOM   1292  O   VAL A 166       9.250  -0.519  37.432  1.00 29.28           O  
ANISOU 1292  O   VAL A 166     4100   3990   3037   -725   -383     -2       O  
ATOM   1293  CB  VAL A 166      10.396  -0.247  40.308  1.00 31.51           C  
ANISOU 1293  CB  VAL A 166     4477   4346   3149   -814   -579    -64       C  
ATOM   1294  CG1 VAL A 166      10.096   1.259  40.335  1.00 31.76           C  
ANISOU 1294  CG1 VAL A 166     4521   4348   3199   -814   -545   -170       C  
ATOM   1295  CG2 VAL A 166      10.778  -0.751  41.690  1.00 32.58           C  
ANISOU 1295  CG2 VAL A 166     4676   4541   3163   -847   -678    -55       C  
ATOM   1296  N   ILE A 167       7.581   0.358  38.635  1.00 29.91           N  
ANISOU 1296  N   ILE A 167     4269   4144   2953   -733   -319   -113       N  
ATOM   1297  CA  ILE A 167       7.132   1.202  37.542  1.00 29.36           C  
ANISOU 1297  CA  ILE A 167     4168   4022   2967   -686   -251   -146       C  
ATOM   1298  C   ILE A 167       7.139   2.644  38.014  1.00 31.20           C  
ANISOU 1298  C   ILE A 167     4432   4224   3200   -687   -257   -243       C  
ATOM   1299  O   ILE A 167       6.496   2.980  39.007  1.00 30.69           O  
ANISOU 1299  O   ILE A 167     4417   4210   3035   -698   -248   -311       O  
ATOM   1300  CB  ILE A 167       5.721   0.819  37.066  1.00 28.88           C  
ANISOU 1300  CB  ILE A 167     4101   4002   2869   -648   -163   -148       C  
ATOM   1301  CG1 ILE A 167       5.689  -0.660  36.662  1.00 32.95           C  
ANISOU 1301  CG1 ILE A 167     4593   4541   3386   -655   -161    -60       C  
ATOM   1302  CG2 ILE A 167       5.275   1.730  35.906  1.00 28.45           C  
ANISOU 1302  CG2 ILE A 167     4021   3892   2895   -586   -108   -179       C  
ATOM   1303  CD1 ILE A 167       4.316  -1.161  36.249  1.00 30.07           C  
ANISOU 1303  CD1 ILE A 167     4214   4221   2992   -632    -82    -66       C  
ATOM   1304  N   MET A 168       7.894   3.492  37.327  1.00 30.01           N  
ANISOU 1304  N   MET A 168     4254   3987   3163   -681   -269   -250       N  
ATOM   1305  CA  MET A 168       7.817   4.913  37.606  1.00 30.87           C  
ANISOU 1305  CA  MET A 168     4394   4042   3291   -678   -265   -343       C  
ATOM   1306  C   MET A 168       6.722   5.543  36.750  1.00 30.93           C  
ANISOU 1306  C   MET A 168     4408   4020   3323   -608   -178   -368       C  
ATOM   1307  O   MET A 168       6.735   5.430  35.524  1.00 31.86           O  
ANISOU 1307  O   MET A 168     4494   4095   3516   -571   -140   -309       O  
ATOM   1308  CB  MET A 168       9.141   5.615  37.327  1.00 31.07           C  
ANISOU 1308  CB  MET A 168     4392   3978   3436   -714   -316   -342       C  
ATOM   1309  CG  MET A 168       9.128   7.076  37.779  1.00 34.72           C  
ANISOU 1309  CG  MET A 168     4898   4375   3921   -724   -325   -446       C  
ATOM   1310  SD  MET A 168      10.620   7.957  37.285  1.00 45.16           S  
ANISOU 1310  SD  MET A 168     6176   5574   5408   -778   -366   -442       S  
ATOM   1311  CE  MET A 168      10.304   8.121  35.536  1.00 38.09           C  
ANISOU 1311  CE  MET A 168     5259   4605   4608   -718   -261   -359       C  
ATOM   1312  N   THR A 169       5.782   6.206  37.411  1.00 30.88           N  
ANISOU 1312  N   THR A 169     4445   4038   3249   -585   -150   -460       N  
ATOM   1313  CA  THR A 169       4.694   6.895  36.741  1.00 30.78           C  
ANISOU 1313  CA  THR A 169     4438   3999   3258   -508    -80   -499       C  
ATOM   1314  C   THR A 169       4.781   8.398  36.981  1.00 37.00           C  
ANISOU 1314  C   THR A 169     5271   4698   4090   -493    -87   -590       C  
ATOM   1315  O   THR A 169       5.692   8.884  37.668  1.00 33.77           O  
ANISOU 1315  O   THR A 169     4885   4250   3695   -551   -146   -628       O  
ATOM   1316  CB  THR A 169       3.334   6.402  37.262  1.00 30.85           C  
ANISOU 1316  CB  THR A 169     4446   4113   3160   -480    -27   -540       C  
ATOM   1317  CG2 THR A 169       3.130   4.933  36.907  1.00 30.05           C  
ANISOU 1317  CG2 THR A 169     4303   4083   3031   -495    -13   -450       C  
ATOM   1318  OG1 THR A 169       3.294   6.541  38.688  1.00 31.74           O  
ANISOU 1318  OG1 THR A 169     4605   4285   3172   -523    -48   -614       O  
ATOM   1319  N   SER A 170       3.831   9.130  36.407  1.00 37.17           N  
ANISOU 1319  N   SER A 170     5303   4681   4137   -412    -34   -630       N  
ATOM   1320  CA  SER A 170       3.726  10.568  36.629  1.00 35.50           C  
ANISOU 1320  CA  SER A 170     5143   4376   3968   -383    -34   -723       C  
ATOM   1321  C   SER A 170       2.266  10.921  36.858  1.00 34.80           C  
ANISOU 1321  C   SER A 170     5064   4335   3824   -299     20   -810       C  
ATOM   1322  O   SER A 170       1.400  10.054  36.770  1.00 33.84           O  
ANISOU 1322  O   SER A 170     4899   4316   3642   -272     59   -791       O  
ATOM   1323  CB  SER A 170       4.237  11.322  35.409  1.00 32.65           C  
ANISOU 1323  CB  SER A 170     4792   3879   3735   -356    -27   -668       C  
ATOM   1324  OG  SER A 170       3.453  10.998  34.275  1.00 31.97           O  
ANISOU 1324  OG  SER A 170     4683   3805   3660   -274     21   -608       O  
ATOM   1325  N   ASP A 171       1.985  12.191  37.127  1.00 34.12           N  
ANISOU 1325  N   ASP A 171     5026   4168   3768   -256     24   -909       N  
ATOM   1326  CA  ASP A 171       0.600  12.633  37.248  1.00 38.34           C  
ANISOU 1326  CA  ASP A 171     5560   4737   4270   -159     77   -999       C  
ATOM   1327  C   ASP A 171      -0.204  12.282  35.991  1.00 37.66           C  
ANISOU 1327  C   ASP A 171     5426   4662   4222    -72    114   -931       C  
ATOM   1328  O   ASP A 171      -1.391  11.969  36.075  1.00 34.75           O  
ANISOU 1328  O   ASP A 171     5012   4385   3805    -12    158   -975       O  
ATOM   1329  CB  ASP A 171       0.524  14.136  37.520  1.00 41.84           C  
ANISOU 1329  CB  ASP A 171     6069   5061   4768   -112     68  -1108       C  
ATOM   1330  CG  ASP A 171       1.050  14.508  38.894  1.00 45.25           C  
ANISOU 1330  CG  ASP A 171     6549   5503   5142   -184     32  -1211       C  
ATOM   1331  OD1 ASP A 171       0.857  13.723  39.844  1.00 50.74           O  
ANISOU 1331  OD1 ASP A 171     7231   6333   5716   -228     39  -1237       O  
ATOM   1332  OD2 ASP A 171       1.657  15.588  39.026  1.00 45.42           O1-
ANISOU 1332  OD2 ASP A 171     6628   5394   5236   -197     -5  -1265       O1-
ATOM   1333  N   ASP A 172       0.446  12.333  34.831  1.00 35.49           N  
ANISOU 1333  N   ASP A 172     5156   4297   4031    -67     97   -828       N  
ATOM   1334  CA  ASP A 172      -0.208  12.010  33.564  1.00 33.42           C  
ANISOU 1334  CA  ASP A 172     4860   4041   3797     17    120   -760       C  
ATOM   1335  C   ASP A 172      -0.588  10.535  33.440  1.00 34.86           C  
ANISOU 1335  C   ASP A 172     4968   4360   3916     -9    135   -707       C  
ATOM   1336  O   ASP A 172      -1.625  10.210  32.872  1.00 34.89           O  
ANISOU 1336  O   ASP A 172     4928   4420   3910     66    159   -711       O  
ATOM   1337  CB  ASP A 172       0.702  12.346  32.385  1.00 34.97           C  
ANISOU 1337  CB  ASP A 172     5090   4116   4081     17    105   -654       C  
ATOM   1338  CG  ASP A 172       0.605  13.801  31.956  1.00 45.99           C  
ANISOU 1338  CG  ASP A 172     6559   5362   5554     89    105   -683       C  
ATOM   1339  OD1 ASP A 172       1.323  14.169  31.001  1.00 45.39           O  
ANISOU 1339  OD1 ASP A 172     6521   5178   5546     87    105   -593       O  
ATOM   1340  OD2 ASP A 172      -0.187  14.564  32.553  1.00 46.55           O1-
ANISOU 1340  OD2 ASP A 172     6650   5420   5616    151    110   -792       O1-
ATOM   1341  N   THR A 173       0.263   9.645  33.942  1.00 31.84           N  
ANISOU 1341  N   THR A 173     4573   4025   3498   -112    116   -658       N  
ATOM   1342  CA  THR A 173       0.081   8.215  33.684  1.00 31.42           C  
ANISOU 1342  CA  THR A 173     4462   4072   3403   -141    125   -590       C  
ATOM   1343  C   THR A 173      -0.342   7.343  34.875  1.00 30.55           C  
ANISOU 1343  C   THR A 173     4328   4087   3194   -202    142   -626       C  
ATOM   1344  O   THR A 173      -0.737   6.199  34.679  1.00 30.02           O  
ANISOU 1344  O   THR A 173     4213   4098   3096   -220    159   -581       O  
ATOM   1345  CB  THR A 173       1.361   7.579  33.105  1.00 29.99           C  
ANISOU 1345  CB  THR A 173     4279   3853   3263   -202     93   -479       C  
ATOM   1346  CG2 THR A 173       1.849   8.334  31.856  1.00 29.64           C  
ANISOU 1346  CG2 THR A 173     4262   3691   3309   -153     93   -425       C  
ATOM   1347  OG1 THR A 173       2.383   7.576  34.108  1.00 29.97           O  
ANISOU 1347  OG1 THR A 173     4299   3843   3244   -293     55   -487       O  
ATOM   1348  N   HIS A 174      -0.246   7.864  36.095  1.00 31.36           N  
ANISOU 1348  N   HIS A 174     4469   4203   3243   -237    138   -706       N  
ATOM   1349  CA  HIS A 174      -0.370   7.022  37.290  1.00 31.61           C  
ANISOU 1349  CA  HIS A 174     4500   4344   3165   -310    149   -721       C  
ATOM   1350  C   HIS A 174      -1.701   6.285  37.413  1.00 31.67           C  
ANISOU 1350  C   HIS A 174     4452   4465   3116   -291    218   -744       C  
ATOM   1351  O   HIS A 174      -1.735   5.048  37.472  1.00 31.22           O  
ANISOU 1351  O   HIS A 174     4367   4475   3020   -345    227   -676       O  
ATOM   1352  CB  HIS A 174      -0.116   7.833  38.563  1.00 32.68           C  
ANISOU 1352  CB  HIS A 174     4698   4477   3240   -339    133   -819       C  
ATOM   1353  CG  HIS A 174      -0.102   7.002  39.804  1.00 33.08           C  
ANISOU 1353  CG  HIS A 174     4769   4637   3162   -416    138   -822       C  
ATOM   1354  CD2 HIS A 174      -0.982   6.913  40.831  1.00 33.95           C  
ANISOU 1354  CD2 HIS A 174     4891   4849   3160   -422    197   -899       C  
ATOM   1355  ND1 HIS A 174       0.909   6.109  40.087  1.00 33.16           N  
ANISOU 1355  ND1 HIS A 174     4795   4661   3145   -495     80   -734       N  
ATOM   1356  CE1 HIS A 174       0.657   5.513  41.240  1.00 33.34           C  
ANISOU 1356  CE1 HIS A 174     4849   4784   3037   -546     96   -749       C  
ATOM   1357  NE2 HIS A 174      -0.485   5.985  41.712  1.00 34.11           N  
ANISOU 1357  NE2 HIS A 174     4945   4938   3076   -507    173   -848       N  
ATOM   1358  N   ASP A 175      -2.795   7.038  37.471  1.00 32.36           N  
ANISOU 1358  N   ASP A 175     4519   4571   3205   -215    267   -843       N  
ATOM   1359  CA  ASP A 175      -4.118   6.427  37.566  1.00 32.61           C  
ANISOU 1359  CA  ASP A 175     4478   4714   3200   -195    338   -878       C  
ATOM   1360  C   ASP A 175      -4.390   5.456  36.414  1.00 32.42           C  
ANISOU 1360  C   ASP A 175     4386   4703   3228   -185    335   -793       C  
ATOM   1361  O   ASP A 175      -4.866   4.336  36.622  1.00 31.59           O  
ANISOU 1361  O   ASP A 175     4235   4686   3083   -239    371   -763       O  
ATOM   1362  CB  ASP A 175      -5.207   7.500  37.628  1.00 33.57           C  
ANISOU 1362  CB  ASP A 175     4573   4840   3341    -94    383  -1004       C  
ATOM   1363  CG  ASP A 175      -5.140   8.322  38.910  1.00 48.52           C  
ANISOU 1363  CG  ASP A 175     6529   6744   5164   -106    402  -1110       C  
ATOM   1364  OD1 ASP A 175      -5.499   9.524  38.889  1.00 45.99           O  
ANISOU 1364  OD1 ASP A 175     6224   6365   4884    -20    406  -1207       O  
ATOM   1365  OD2 ASP A 175      -4.717   7.760  39.943  1.00 43.66           O1-
ANISOU 1365  OD2 ASP A 175     5952   6189   4446   -200    409  -1098       O1-
ATOM   1366  N   ARG A 176      -4.077   5.882  35.197  1.00 33.43           N  
ANISOU 1366  N   ARG A 176     4516   4741   3446   -119    292   -753       N  
ATOM   1367  CA  ARG A 176      -4.335   5.049  34.032  1.00 30.38           C  
ANISOU 1367  CA  ARG A 176     4074   4365   3105    -97    282   -684       C  
ATOM   1368  C   ARG A 176      -3.516   3.760  34.102  1.00 32.03           C  
ANISOU 1368  C   ARG A 176     4290   4592   3289   -196    262   -583       C  
ATOM   1369  O   ARG A 176      -3.971   2.707  33.660  1.00 29.79           O  
ANISOU 1369  O   ARG A 176     3953   4359   3009   -213    274   -548       O  
ATOM   1370  CB  ARG A 176      -4.044   5.819  32.741  1.00 32.07           C  
ANISOU 1370  CB  ARG A 176     4310   4476   3400     -7    240   -654       C  
ATOM   1371  CG  ARG A 176      -5.039   6.948  32.456  1.00 40.50           C  
ANISOU 1371  CG  ARG A 176     5363   5523   4501    113    251   -744       C  
ATOM   1372  CD  ARG A 176      -4.315   8.196  31.970  1.00 52.11           C  
ANISOU 1372  CD  ARG A 176     6916   6856   6028    167    215   -729       C  
ATOM   1373  NE  ARG A 176      -4.624   8.546  30.587  1.00 60.68           N  
ANISOU 1373  NE  ARG A 176     8003   7886   7168    272    188   -692       N  
ATOM   1374  CZ  ARG A 176      -5.518   9.462  30.232  1.00 65.45           C  
ANISOU 1374  CZ  ARG A 176     8603   8462   7804    393    183   -757       C  
ATOM   1375  NH1 ARG A 176      -6.200  10.118  31.160  1.00 73.91           N1+
ANISOU 1375  NH1 ARG A 176     9660   9557   8866    423    211   -869       N1+
ATOM   1376  NH2 ARG A 176      -5.730   9.725  28.950  1.00 63.54           N  
ANISOU 1376  NH2 ARG A 176     8374   8168   7598    490    149   -711       N  
ATOM   1377  N   THR A 177      -2.314   3.838  34.663  1.00 29.51           N  
ANISOU 1377  N   THR A 177     4034   4228   2951   -258    226   -543       N  
ATOM   1378  CA  THR A 177      -1.475   2.645  34.819  1.00 28.96           C  
ANISOU 1378  CA  THR A 177     3973   4171   2861   -342    198   -451       C  
ATOM   1379  C   THR A 177      -2.084   1.647  35.805  1.00 29.36           C  
ANISOU 1379  C   THR A 177     4008   4321   2825   -413    240   -454       C  
ATOM   1380  O   THR A 177      -2.124   0.437  35.536  1.00 28.97           O  
ANISOU 1380  O   THR A 177     3932   4297   2777   -454    241   -388       O  
ATOM   1381  CB  THR A 177      -0.046   3.011  35.287  1.00 28.96           C  
ANISOU 1381  CB  THR A 177     4033   4105   2864   -389    141   -418       C  
ATOM   1382  CG2 THR A 177       0.821   1.797  35.376  1.00 28.49           C  
ANISOU 1382  CG2 THR A 177     3976   4054   2795   -458    104   -324       C  
ATOM   1383  OG1 THR A 177       0.540   3.925  34.358  1.00 28.72           O  
ANISOU 1383  OG1 THR A 177     4016   3976   2920   -337    116   -407       O  
ATOM   1384  N   LEU A 178      -2.551   2.145  36.946  1.00 30.25           N  
ANISOU 1384  N   LEU A 178     4144   4488   2863   -429    277   -531       N  
ATOM   1385  CA  LEU A 178      -3.188   1.274  37.927  1.00 31.20           C  
ANISOU 1385  CA  LEU A 178     4259   4708   2890   -499    334   -533       C  
ATOM   1386  C   LEU A 178      -4.457   0.647  37.325  1.00 30.85           C  
ANISOU 1386  C   LEU A 178     4123   4722   2878   -481    396   -548       C  
ATOM   1387  O   LEU A 178      -4.727  -0.532  37.520  1.00 33.41           O  
ANISOU 1387  O   LEU A 178     4427   5091   3174   -550    425   -496       O  
ATOM   1388  CB  LEU A 178      -3.489   2.028  39.230  1.00 32.32           C  
ANISOU 1388  CB  LEU A 178     4446   4901   2934   -511    373   -624       C  
ATOM   1389  CG  LEU A 178      -2.312   2.660  39.997  1.00 34.03           C  
ANISOU 1389  CG  LEU A 178     4752   5071   3106   -536    306   -631       C  
ATOM   1390  CD1 LEU A 178      -2.777   3.342  41.279  1.00 34.47           C  
ANISOU 1390  CD1 LEU A 178     4853   5191   3052   -543    352   -736       C  
ATOM   1391  CD2 LEU A 178      -1.233   1.638  40.320  1.00 31.94           C  
ANISOU 1391  CD2 LEU A 178     4532   4797   2805   -615    242   -520       C  
ATOM   1392  N   GLN A 179      -5.219   1.446  36.582  1.00 30.92           N  
ANISOU 1392  N   GLN A 179     4075   4721   2951   -388    411   -620       N  
ATOM   1393  CA  GLN A 179      -6.365   0.952  35.823  1.00 31.81           C  
ANISOU 1393  CA  GLN A 179     4089   4882   3115   -357    447   -643       C  
ATOM   1394  C   GLN A 179      -5.974  -0.200  34.886  1.00 32.70           C  
ANISOU 1394  C   GLN A 179     4183   4963   3277   -386    405   -547       C  
ATOM   1395  O   GLN A 179      -6.610  -1.254  34.887  1.00 30.23           O  
ANISOU 1395  O   GLN A 179     3817   4706   2964   -440    442   -532       O  
ATOM   1396  CB  GLN A 179      -6.998   2.095  35.012  1.00 36.57           C  
ANISOU 1396  CB  GLN A 179     4650   5458   3788   -231    436   -723       C  
ATOM   1397  CG  GLN A 179      -8.105   1.657  34.047  1.00 44.83           C  
ANISOU 1397  CG  GLN A 179     5589   6548   4898   -180    446   -751       C  
ATOM   1398  CD  GLN A 179      -8.735   2.816  33.257  1.00 49.46           C  
ANISOU 1398  CD  GLN A 179     6141   7105   5547    -41    422   -826       C  
ATOM   1399  NE2 GLN A 179      -8.372   4.048  33.610  1.00 43.83           N  
ANISOU 1399  NE2 GLN A 179     5493   6334   4828     13    412   -866       N  
ATOM   1400  OE1 GLN A 179      -9.538   2.595  32.339  1.00 44.77           O  
ANISOU 1400  OE1 GLN A 179     5465   6537   5009     20    405   -850       O  
ATOM   1401  N   LEU A 180      -4.938   0.011  34.079  1.00 29.23           N  
ANISOU 1401  N   LEU A 180     3788   4434   2884   -352    335   -487       N  
ATOM   1402  CA  LEU A 180      -4.495  -1.019  33.132  1.00 28.46           C  
ANISOU 1402  CA  LEU A 180     3678   4303   2832   -368    296   -406       C  
ATOM   1403  C   LEU A 180      -4.054  -2.326  33.815  1.00 28.43           C  
ANISOU 1403  C   LEU A 180     3698   4317   2786   -476    301   -331       C  
ATOM   1404  O   LEU A 180      -4.414  -3.417  33.371  1.00 30.11           O  
ANISOU 1404  O   LEU A 180     3872   4544   3026   -507    306   -301       O  
ATOM   1405  CB  LEU A 180      -3.387  -0.488  32.212  1.00 27.75           C  
ANISOU 1405  CB  LEU A 180     3634   4117   2792   -314    234   -356       C  
ATOM   1406  CG  LEU A 180      -3.029  -1.385  31.023  1.00 27.07           C  
ANISOU 1406  CG  LEU A 180     3531   3998   2755   -303    200   -291       C  
ATOM   1407  CD1 LEU A 180      -4.266  -1.680  30.167  1.00 30.48           C  
ANISOU 1407  CD1 LEU A 180     3888   4475   3218   -250    211   -339       C  
ATOM   1408  CD2 LEU A 180      -1.907  -0.792  30.167  1.00 27.47           C  
ANISOU 1408  CD2 LEU A 180     3628   3961   2848   -254    158   -242       C  
ATOM   1409  N   LEU A 181      -3.285  -2.219  34.894  1.00 28.66           N  
ANISOU 1409  N   LEU A 181     3796   4341   2751   -531    292   -304       N  
ATOM   1410  CA  LEU A 181      -2.881  -3.404  35.662  1.00 28.84           C  
ANISOU 1410  CA  LEU A 181     3857   4379   2722   -626    290   -228       C  
ATOM   1411  C   LEU A 181      -4.091  -4.235  36.081  1.00 29.53           C  
ANISOU 1411  C   LEU A 181     3899   4543   2778   -685    368   -245       C  
ATOM   1412  O   LEU A 181      -4.095  -5.463  35.938  1.00 29.49           O  
ANISOU 1412  O   LEU A 181     3889   4529   2787   -742    368   -180       O  
ATOM   1413  CB  LEU A 181      -2.077  -2.986  36.898  1.00 29.30           C  
ANISOU 1413  CB  LEU A 181     3997   4439   2696   -666    268   -218       C  
ATOM   1414  CG  LEU A 181      -0.690  -2.402  36.587  1.00 32.23           C  
ANISOU 1414  CG  LEU A 181     4408   4729   3108   -635    184   -187       C  
ATOM   1415  CD1 LEU A 181      -0.145  -1.573  37.737  1.00 31.35           C  
ANISOU 1415  CD1 LEU A 181     4361   4626   2923   -655    161   -223       C  
ATOM   1416  CD2 LEU A 181       0.284  -3.519  36.219  1.00 29.17           C  
ANISOU 1416  CD2 LEU A 181     4033   4294   2757   -666    127    -84       C  
ATOM   1417  N  AARG A 182      -5.114  -3.560  36.600  0.51 30.29           N  
ANISOU 1417  N  AARG A 182     3959   4711   2838   -672    438   -335       N  
ATOM   1418  N  BARG A 182      -5.104  -3.548  36.602  0.49 30.28           N  
ANISOU 1418  N  BARG A 182     3960   4710   2837   -671    437   -335       N  
ATOM   1419  CA AARG A 182      -6.343  -4.212  37.042  0.51 31.63           C  
ANISOU 1419  CA AARG A 182     4070   4964   2984   -731    529   -365       C  
ATOM   1420  CA BARG A 182      -6.354  -4.158  37.033  0.49 31.65           C  
ANISOU 1420  CA BARG A 182     4071   4966   2987   -727    529   -368       C  
ATOM   1421  C  AARG A 182      -7.094  -4.812  35.853  0.51 33.28           C  
ANISOU 1421  C  AARG A 182     4180   5171   3294   -709    529   -379       C  
ATOM   1422  C  BARG A 182      -7.053  -4.810  35.845  0.49 33.19           C  
ANISOU 1422  C  BARG A 182     4171   5156   3282   -709    526   -376       C  
ATOM   1423  O  AARG A 182      -7.520  -5.966  35.892  0.51 33.17           O  
ANISOU 1423  O  AARG A 182     4138   5174   3293   -787    562   -342       O  
ATOM   1424  O  BARG A 182      -7.403  -5.989  35.878  0.49 33.34           O  
ANISOU 1424  O  BARG A 182     4166   5187   3313   -787    555   -334       O  
ATOM   1425  CB AARG A 182      -7.242  -3.213  37.790  0.51 33.10           C  
ANISOU 1425  CB AARG A 182     4227   5230   3119   -705    607   -475       C  
ATOM   1426  CB BARG A 182      -7.269  -3.080  37.631  0.49 32.04           C  
ANISOU 1426  CB BARG A 182     4084   5091   2998   -688    601   -484       C  
ATOM   1427  CG AARG A 182      -8.511  -3.820  38.379  0.51 39.62           C  
ANISOU 1427  CG AARG A 182     4984   6155   3915   -774    721   -511       C  
ATOM   1428  CG BARG A 182      -8.489  -3.614  38.355  0.49 38.77           C  
ANISOU 1428  CG BARG A 182     4876   6045   3808   -759    716   -523       C  
ATOM   1429  CD AARG A 182      -9.390  -2.779  39.100  0.51 40.26           C  
ANISOU 1429  CD AARG A 182     5028   6320   3949   -736    805   -633       C  
ATOM   1430  CD BARG A 182      -9.776  -2.869  37.986  0.49 41.27           C  
ANISOU 1430  CD BARG A 182     5073   6426   4182   -684    772   -650       C  
ATOM   1431  NE AARG A 182      -8.660  -2.015  40.111  0.51 38.47           N  
ANISOU 1431  NE AARG A 182     4911   6090   3616   -732    794   -644       N  
ATOM   1432  NE BARG A 182      -9.624  -1.417  37.888  0.49 37.97           N  
ANISOU 1432  NE BARG A 182     4672   5985   3770   -573    740   -731       N  
ATOM   1433  CZ AARG A 182      -8.772  -2.187  41.427  0.51 38.83           C  
ANISOU 1433  CZ AARG A 182     5016   6205   3532   -806    869   -644       C  
ATOM   1434  CZ BARG A 182     -10.204  -0.677  36.943  0.49 39.75           C  
ANISOU 1434  CZ BARG A 182     4818   6199   4085   -461    713   -805       C  
ATOM   1435  NH1AARG A 182      -8.058  -1.430  42.254  0.51 36.00           N1+
ANISOU 1435  NH1AARG A 182     4760   5839   3081   -793    840   -665       N1+
ATOM   1436  NH2AARG A 182      -9.589  -3.109  41.922  0.51 36.66           N  
ANISOU 1436  NH2AARG A 182     4705   6006   3218   -897    973   -623       N  
ATOM   1437  NH1BARG A 182     -10.023   0.636  36.914  0.49 33.65           N1+
ANISOU 1437  NH1BARG A 182     4078   5390   3318   -364    684   -870       N1+
ATOM   1438  NH2BARG A 182     -10.966  -1.256  36.019  0.49 36.34           N  
ANISOU 1438  NH2BARG A 182     4281   5787   3738   -447    709   -817       N  
ATOM   1439  N   GLU A 183      -7.256  -4.020  34.798  1.00 32.63           N  
ANISOU 1439  N   GLU A 183     4051   5064   3283   -604    488   -433       N  
ATOM   1440  CA  GLU A 183      -7.963  -4.475  33.605  1.00 36.12           C  
ANISOU 1440  CA  GLU A 183     4403   5508   3813   -567    470   -458       C  
ATOM   1441  C   GLU A 183      -7.320  -5.699  32.964  1.00 35.33           C  
ANISOU 1441  C   GLU A 183     4326   5347   3750   -611    421   -370       C  
ATOM   1442  O   GLU A 183      -8.021  -6.597  32.494  1.00 32.62           O  
ANISOU 1442  O   GLU A 183     3916   5023   3456   -646    433   -381       O  
ATOM   1443  CB  GLU A 183      -8.090  -3.334  32.588  1.00 31.29           C  
ANISOU 1443  CB  GLU A 183     3765   4871   3252   -434    421   -517       C  
ATOM   1444  CG  GLU A 183      -9.044  -2.249  33.057  1.00 39.50           C  
ANISOU 1444  CG  GLU A 183     4754   5973   4280   -377    472   -625       C  
ATOM   1445  CD  GLU A 183      -8.989  -1.002  32.199  1.00 44.29           C  
ANISOU 1445  CD  GLU A 183     5367   6532   4928   -241    417   -667       C  
ATOM   1446  OE1 GLU A 183      -8.116  -0.940  31.302  1.00 38.84           O  
ANISOU 1446  OE1 GLU A 183     4732   5763   4264   -201    348   -605       O  
ATOM   1447  OE2 GLU A 183      -9.823  -0.091  32.424  1.00 39.21           O1-
ANISOU 1447  OE2 GLU A 183     4676   5930   4291   -173    447   -762       O1-
ATOM   1448  N   LEU A 184      -5.993  -5.744  32.955  1.00 34.59           N  
ANISOU 1448  N   LEU A 184     4322   5180   3639   -611    365   -290       N  
ATOM   1449  CA  LEU A 184      -5.291  -6.864  32.329  1.00 33.46           C  
ANISOU 1449  CA  LEU A 184     4203   4974   3536   -639    316   -212       C  
ATOM   1450  C   LEU A 184      -5.158  -8.041  33.287  1.00 35.20           C  
ANISOU 1450  C   LEU A 184     4462   5194   3717   -755    345   -142       C  
ATOM   1451  O   LEU A 184      -4.587  -9.083  32.938  1.00 35.62           O  
ANISOU 1451  O   LEU A 184     4542   5187   3803   -785    308    -74       O  
ATOM   1452  CB  LEU A 184      -3.918  -6.424  31.806  1.00 31.89           C  
ANISOU 1452  CB  LEU A 184     4068   4698   3351   -582    247   -160       C  
ATOM   1453  CG  LEU A 184      -3.892  -5.361  30.702  1.00 37.24           C  
ANISOU 1453  CG  LEU A 184     4728   5354   4069   -469    216   -204       C  
ATOM   1454  CD1 LEU A 184      -2.456  -4.941  30.395  1.00 37.18           C  
ANISOU 1454  CD1 LEU A 184     4785   5271   4071   -438    168   -144       C  
ATOM   1455  CD2 LEU A 184      -4.594  -5.840  29.429  1.00 37.61           C  
ANISOU 1455  CD2 LEU A 184     4712   5406   4173   -422    199   -236       C  
ATOM   1456  N   GLN A 185      -5.698  -7.872  34.494  1.00 32.83           N  
ANISOU 1456  N   GLN A 185     4172   4959   3345   -815    415   -160       N  
ATOM   1457  CA  GLN A 185      -5.656  -8.908  35.519  1.00 34.56           C  
ANISOU 1457  CA  GLN A 185     4442   5182   3506   -927    453    -87       C  
ATOM   1458  C   GLN A 185      -4.231  -9.365  35.811  1.00 37.70           C  
ANISOU 1458  C   GLN A 185     4942   5504   3877   -941    379     17       C  
ATOM   1459  O   GLN A 185      -3.997 -10.526  36.134  1.00 40.62           O  
ANISOU 1459  O   GLN A 185     5356   5837   4240  -1012    375     98       O  
ATOM   1460  CB  GLN A 185      -6.513 -10.102  35.091  1.00 37.55           C  
ANISOU 1460  CB  GLN A 185     4758   5560   3949   -992    489    -83       C  
ATOM   1461  CG  GLN A 185      -7.950  -9.721  34.778  1.00 41.70           C  
ANISOU 1461  CG  GLN A 185     5161   6167   4516   -981    555   -193       C  
ATOM   1462  CD  GLN A 185      -8.696 -10.815  34.041  1.00 50.74           C  
ANISOU 1462  CD  GLN A 185     6227   7298   5752  -1029    564   -206       C  
ATOM   1463  NE2 GLN A 185      -9.555 -11.532  34.755  1.00 52.08           N  
ANISOU 1463  NE2 GLN A 185     6363   7510   5914  -1143    655   -203       N  
ATOM   1464  OE1 GLN A 185      -8.500 -11.014  32.840  1.00 57.82           O  
ANISOU 1464  OE1 GLN A 185     7097   8147   6726   -969    491   -221       O  
ATOM   1465  N   LEU A 186      -3.284  -8.445  35.684  1.00 37.01           N  
ANISOU 1465  N   LEU A 186     4889   5389   3782   -871    319     13       N  
ATOM   1466  CA  LEU A 186      -1.894  -8.722  36.023  1.00 37.89           C  
ANISOU 1466  CA  LEU A 186     5082   5440   3873   -877    243     98       C  
ATOM   1467  C   LEU A 186      -1.728  -8.792  37.542  1.00 41.00           C  
ANISOU 1467  C   LEU A 186     5558   5873   4148   -945    260    136       C  
ATOM   1468  O   LEU A 186      -2.134  -7.880  38.263  1.00 39.90           O  
ANISOU 1468  O   LEU A 186     5428   5798   3936   -944    302     75       O  
ATOM   1469  CB  LEU A 186      -0.984  -7.651  35.417  1.00 38.73           C  
ANISOU 1469  CB  LEU A 186     5186   5509   4019   -792    182     73       C  
ATOM   1470  CG  LEU A 186      -0.817  -7.754  33.897  1.00 39.48           C  
ANISOU 1470  CG  LEU A 186     5230   5554   4219   -724    152     66       C  
ATOM   1471  CD1 LEU A 186      -0.323  -6.454  33.269  1.00 38.04           C  
ANISOU 1471  CD1 LEU A 186     5037   5349   4067   -641    127     25       C  
ATOM   1472  CD2 LEU A 186       0.110  -8.916  33.556  1.00 45.59           C  
ANISOU 1472  CD2 LEU A 186     6029   6258   5036   -739     98    150       C  
ATOM   1473  N   GLU A 187      -1.139  -9.883  38.021  1.00 37.60           N  
ANISOU 1473  N   GLU A 187     5193   5401   3691   -999    226    235       N  
ATOM   1474  CA  GLU A 187      -0.963 -10.094  39.451  1.00 42.59           C  
ANISOU 1474  CA  GLU A 187     5920   6067   4194  -1063    234    287       C  
ATOM   1475  C   GLU A 187       0.516 -10.178  39.789  1.00 40.71           C  
ANISOU 1475  C   GLU A 187     5754   5775   3939  -1040    119    356       C  
ATOM   1476  O   GLU A 187       1.152 -11.216  39.603  1.00 39.67           O  
ANISOU 1476  O   GLU A 187     5651   5575   3846  -1049     63    443       O  
ATOM   1477  CB  GLU A 187      -1.671 -11.374  39.892  1.00 50.96           C  
ANISOU 1477  CB  GLU A 187     7009   7128   5225  -1156    298    355       C  
ATOM   1478  CG  GLU A 187      -2.643 -11.170  41.043  1.00 68.55           C  
ANISOU 1478  CG  GLU A 187     9266   9452   7329  -1227    406    332       C  
ATOM   1479  CD  GLU A 187      -3.912 -10.457  40.615  1.00 79.07           C  
ANISOU 1479  CD  GLU A 187    10487  10856   8698  -1213    503    213       C  
ATOM   1480  OE1 GLU A 187      -4.462  -9.672  41.420  1.00 83.36           O  
ANISOU 1480  OE1 GLU A 187    11037  11487   9150  -1221    573    149       O  
ATOM   1481  OE2 GLU A 187      -4.365 -10.691  39.474  1.00 80.14           O1-
ANISOU 1481  OE2 GLU A 187    10529  10964   8957  -1188    506    178       O1-
ATOM   1482  N   VAL A 188       1.058  -9.073  40.285  1.00 35.65           N  
ANISOU 1482  N   VAL A 188     5135   5163   3246  -1007     81    310       N  
ATOM   1483  CA  VAL A 188       2.489  -8.943  40.491  1.00 33.34           C  
ANISOU 1483  CA  VAL A 188     4884   4826   2960   -977    -36    351       C  
ATOM   1484  C   VAL A 188       2.765  -8.548  41.930  1.00 37.75           C  
ANISOU 1484  C   VAL A 188     5533   5439   3370  -1009    -63    352       C  
ATOM   1485  O   VAL A 188       2.819  -7.359  42.251  1.00 39.76           O  
ANISOU 1485  O   VAL A 188     5786   5732   3590   -987    -66    268       O  
ATOM   1486  CB  VAL A 188       3.073  -7.876  39.560  1.00 30.29           C  
ANISOU 1486  CB  VAL A 188     4427   4407   2673   -904    -74    284       C  
ATOM   1487  CG1 VAL A 188       4.582  -7.955  39.563  1.00 30.20           C  
ANISOU 1487  CG1 VAL A 188     4430   4340   2704   -878   -191    333       C  
ATOM   1488  CG2 VAL A 188       2.530  -8.057  38.144  1.00 31.65           C  
ANISOU 1488  CG2 VAL A 188     4515   4547   2963   -866    -28    262       C  
ATOM   1489  N   PRO A 189       2.948  -9.551  42.799  1.00 38.33           N  
ANISOU 1489  N   PRO A 189     5697   5512   3354  -1059    -88    448       N  
ATOM   1490  CA  PRO A 189       3.051  -9.390  44.256  1.00 37.98           C  
ANISOU 1490  CA  PRO A 189     5762   5531   3136  -1097   -104    464       C  
ATOM   1491  C   PRO A 189       4.085  -8.351  44.685  1.00 40.47           C  
ANISOU 1491  C   PRO A 189     6094   5856   3425  -1056   -210    409       C  
ATOM   1492  O   PRO A 189       3.843  -7.599  45.628  1.00 38.57           O  
ANISOU 1492  O   PRO A 189     5909   5688   3059  -1071   -192    347       O  
ATOM   1493  CB  PRO A 189       3.494 -10.776  44.729  1.00 41.93           C  
ANISOU 1493  CB  PRO A 189     6349   5987   3594  -1132   -158    602       C  
ATOM   1494  CG  PRO A 189       2.997 -11.713  43.678  1.00 46.68           C  
ANISOU 1494  CG  PRO A 189     6889   6525   4324  -1142   -105    642       C  
ATOM   1495  CD  PRO A 189       3.082 -10.958  42.381  1.00 40.43           C  
ANISOU 1495  CD  PRO A 189     5972   5708   3680  -1078   -105    552       C  
ATOM   1496  N   ASN A 190       5.229  -8.318  44.009  1.00 38.10           N  
ANISOU 1496  N   ASN A 190     5744   5486   3244  -1006   -317    425       N  
ATOM   1497  CA  ASN A 190       6.318  -7.438  44.420  1.00 35.91           C  
ANISOU 1497  CA  ASN A 190     5474   5210   2959   -978   -428    378       C  
ATOM   1498  C   ASN A 190       6.514  -6.261  43.467  1.00 33.42           C  
ANISOU 1498  C   ASN A 190     5059   4866   2773   -934   -418    281       C  
ATOM   1499  O   ASN A 190       7.631  -5.797  43.249  1.00 33.12           O  
ANISOU 1499  O   ASN A 190     4984   4789   2812   -906   -514    264       O  
ATOM   1500  CB  ASN A 190       7.612  -8.234  44.599  1.00 34.72           C  
ANISOU 1500  CB  ASN A 190     5347   5010   2836   -959   -570    470       C  
ATOM   1501  CG  ASN A 190       7.599  -9.073  45.862  1.00 46.05           C  
ANISOU 1501  CG  ASN A 190     6912   6479   4105   -997   -610    557       C  
ATOM   1502  ND2 ASN A 190       8.022 -10.331  45.748  1.00 42.89           N  
ANISOU 1502  ND2 ASN A 190     6539   6021   3737   -990   -663    673       N  
ATOM   1503  OD1 ASN A 190       7.204  -8.596  46.931  1.00 45.36           O  
ANISOU 1503  OD1 ASN A 190     6908   6468   3858  -1028   -591    521       O  
ATOM   1504  N   LEU A 191       5.405  -5.792  42.912  1.00 32.68           N  
ANISOU 1504  N   LEU A 191     4922   4791   2704   -929   -301    218       N  
ATOM   1505  CA  LEU A 191       5.395  -4.615  42.061  1.00 35.43           C  
ANISOU 1505  CA  LEU A 191     5195   5111   3155   -885   -278    129       C  
ATOM   1506  C   LEU A 191       5.281  -3.371  42.931  1.00 37.42           C  
ANISOU 1506  C   LEU A 191     5488   5407   3323   -890   -280     26       C  
ATOM   1507  O   LEU A 191       4.541  -3.351  43.905  1.00 35.28           O  
ANISOU 1507  O   LEU A 191     5281   5209   2914   -920   -230     -1       O  
ATOM   1508  CB  LEU A 191       4.215  -4.678  41.085  1.00 40.03           C  
ANISOU 1508  CB  LEU A 191     5716   5695   3798   -867   -164    105       C  
ATOM   1509  CG  LEU A 191       3.924  -3.428  40.246  1.00 40.28           C  
ANISOU 1509  CG  LEU A 191     5686   5704   3915   -814   -126     14       C  
ATOM   1510  CD1 LEU A 191       5.077  -3.129  39.304  1.00 40.56           C  
ANISOU 1510  CD1 LEU A 191     5674   5658   4080   -777   -193     33       C  
ATOM   1511  CD2 LEU A 191       2.622  -3.587  39.472  1.00 36.50           C  
ANISOU 1511  CD2 LEU A 191     5155   5245   3469   -794    -24    -11       C  
ATOM   1512  N   HIS A 192       6.034  -2.340  42.577  1.00 37.67           N  
ANISOU 1512  N   HIS A 192     5483   5391   3439   -862   -333    -33       N  
ATOM   1513  CA  HIS A 192       5.933  -1.054  43.237  1.00 37.00           C  
ANISOU 1513  CA  HIS A 192     5430   5326   3301   -860   -335   -145       C  
ATOM   1514  C   HIS A 192       5.747   0.021  42.184  1.00 34.99           C  
ANISOU 1514  C   HIS A 192     5109   5010   3175   -815   -291   -212       C  
ATOM   1515  O   HIS A 192       6.582   0.185  41.301  1.00 37.62           O  
ANISOU 1515  O   HIS A 192     5386   5270   3638   -797   -333   -186       O  
ATOM   1516  CB  HIS A 192       7.185  -0.788  44.074  1.00 39.58           C  
ANISOU 1516  CB  HIS A 192     5797   5647   3596   -882   -468   -156       C  
ATOM   1517  CG  HIS A 192       7.397  -1.798  45.157  1.00 44.29           C  
ANISOU 1517  CG  HIS A 192     6475   6303   4052   -917   -525    -85       C  
ATOM   1518  CD2 HIS A 192       8.074  -2.971  45.164  1.00 44.56           C  
ANISOU 1518  CD2 HIS A 192     6514   6322   4093   -924   -598     28       C  
ATOM   1519  ND1 HIS A 192       6.842  -1.669  46.411  1.00 46.62           N  
ANISOU 1519  ND1 HIS A 192     6868   6681   4165   -944   -507   -126       N  
ATOM   1520  CE1 HIS A 192       7.182  -2.711  47.150  1.00 46.76           C  
ANISOU 1520  CE1 HIS A 192     6956   6732   4078   -969   -567    -33       C  
ATOM   1521  NE2 HIS A 192       7.931  -3.514  46.417  1.00 43.72           N  
ANISOU 1521  NE2 HIS A 192     6516   6284   3810   -955   -628     61       N  
ATOM   1522  N   VAL A 193       4.627   0.728  42.261  1.00 33.87           N  
ANISOU 1522  N   VAL A 193     4973   4898   2996   -793   -201   -296       N  
ATOM   1523  CA  VAL A 193       4.361   1.816  41.342  1.00 34.13           C  
ANISOU 1523  CA  VAL A 193     4959   4869   3138   -741   -162   -361       C  
ATOM   1524  C   VAL A 193       4.677   3.113  42.066  1.00 38.55           C  
ANISOU 1524  C   VAL A 193     5563   5409   3674   -742   -199   -469       C  
ATOM   1525  O   VAL A 193       4.010   3.472  43.040  1.00 38.05           O  
ANISOU 1525  O   VAL A 193     5553   5410   3496   -747   -165   -548       O  
ATOM   1526  CB  VAL A 193       2.905   1.810  40.845  1.00 33.61           C  
ANISOU 1526  CB  VAL A 193     4861   4840   3070   -700    -49   -391       C  
ATOM   1527  CG1 VAL A 193       2.704   2.892  39.792  1.00 31.42           C  
ANISOU 1527  CG1 VAL A 193     4542   4487   2908   -634    -25   -441       C  
ATOM   1528  CG2 VAL A 193       2.544   0.434  40.272  1.00 32.04           C  
ANISOU 1528  CG2 VAL A 193     4624   4666   2883   -713    -18   -293       C  
ATOM   1529  N   LEU A 194       5.722   3.789  41.604  1.00 32.73           N  
ANISOU 1529  N   LEU A 194     4804   4583   3048   -741   -265   -476       N  
ATOM   1530  CA  LEU A 194       6.205   5.009  42.248  1.00 34.99           C  
ANISOU 1530  CA  LEU A 194     5129   4831   3335   -753   -316   -579       C  
ATOM   1531  C   LEU A 194       5.943   6.203  41.343  1.00 33.88           C  
ANISOU 1531  C   LEU A 194     4965   4595   3314   -705   -270   -634       C  
ATOM   1532  O   LEU A 194       6.399   6.239  40.192  1.00 32.67           O  
ANISOU 1532  O   LEU A 194     4760   4367   3288   -689   -266   -573       O  
ATOM   1533  CB  LEU A 194       7.699   4.896  42.528  1.00 35.23           C  
ANISOU 1533  CB  LEU A 194     5150   4827   3409   -803   -438   -549       C  
ATOM   1534  CG  LEU A 194       8.151   3.595  43.193  1.00 37.86           C  
ANISOU 1534  CG  LEU A 194     5500   5233   3650   -838   -503   -466       C  
ATOM   1535  CD1 LEU A 194       9.666   3.598  43.391  1.00 39.31           C  
ANISOU 1535  CD1 LEU A 194     5657   5379   3901   -875   -634   -449       C  
ATOM   1536  CD2 LEU A 194       7.432   3.418  44.518  1.00 35.87           C  
ANISOU 1536  CD2 LEU A 194     5339   5082   3208   -854   -491   -513       C  
ATOM   1537  N   LYS A 195       5.202   7.175  41.859  1.00 34.21           N  
ANISOU 1537  N   LYS A 195     5049   4638   3310   -677   -232   -749       N  
ATOM   1538  CA  LYS A 195       4.784   8.298  41.041  1.00 34.96           C  
ANISOU 1538  CA  LYS A 195     5135   4640   3510   -618   -185   -801       C  
ATOM   1539  C   LYS A 195       5.715   9.485  41.261  1.00 38.27           C  
ANISOU 1539  C   LYS A 195     5582   4953   4005   -645   -252   -872       C  
ATOM   1540  O   LYS A 195       5.910   9.936  42.396  1.00 36.07           O  
ANISOU 1540  O   LYS A 195     5356   4696   3651   -676   -299   -967       O  
ATOM   1541  CB  LYS A 195       3.341   8.692  41.362  1.00 35.28           C  
ANISOU 1541  CB  LYS A 195     5195   4733   3477   -556    -99   -890       C  
ATOM   1542  CG  LYS A 195       2.812   9.829  40.481  1.00 35.07           C  
ANISOU 1542  CG  LYS A 195     5161   4606   3558   -477    -55   -940       C  
ATOM   1543  CD  LYS A 195       1.452  10.332  40.957  1.00 38.24           C  
ANISOU 1543  CD  LYS A 195     5577   5060   3893   -409     19  -1052       C  
ATOM   1544  CE  LYS A 195       1.585  11.210  42.194  1.00 46.71           C  
ANISOU 1544  CE  LYS A 195     6722   6130   4898   -426     -7  -1187       C  
ATOM   1545  NZ  LYS A 195       2.389  12.436  41.908  1.00 48.78           N1+
ANISOU 1545  NZ  LYS A 195     7018   6238   5277   -426    -64  -1232       N1+
ATOM   1546  N   GLN A 196       6.291   9.995  40.182  1.00 36.72           N  
ANISOU 1546  N   GLN A 196     4500   3936   5517  -1766   -653  -1024       N  
ATOM   1547  CA  GLN A 196       7.145  11.176  40.309  1.00 41.56           C  
ANISOU 1547  CA  GLN A 196     5115   4564   6112  -1694   -588   -986       C  
ATOM   1548  C   GLN A 196       6.335  12.429  40.661  1.00 44.14           C  
ANISOU 1548  C   GLN A 196     5348   4955   6468  -1699   -510  -1023       C  
ATOM   1549  O   GLN A 196       5.164  12.552  40.298  1.00 42.82           O  
ANISOU 1549  O   GLN A 196     5106   4831   6334  -1695   -521  -1087       O  
ATOM   1550  CB  GLN A 196       8.016  11.380  39.062  1.00 47.59           C  
ANISOU 1550  CB  GLN A 196     5915   5311   6854  -1538   -625   -967       C  
ATOM   1551  CG  GLN A 196       7.275  11.446  37.750  1.00 53.88           C  
ANISOU 1551  CG  GLN A 196     6673   6139   7660  -1433   -675  -1013       C  
ATOM   1552  CD  GLN A 196       8.198  11.355  36.539  1.00 51.58           C  
ANISOU 1552  CD  GLN A 196     6433   5838   7329  -1298   -719   -992       C  
ATOM   1553  NE2 GLN A 196       9.460  11.731  36.713  1.00 53.13           N  
ANISOU 1553  NE2 GLN A 196     6676   6015   7496  -1271   -680   -940       N  
ATOM   1554  OE1 GLN A 196       7.770  10.963  35.458  1.00 50.23           O  
ANISOU 1554  OE1 GLN A 196     6252   5684   7149  -1219   -786  -1030       O  
ATOM   1555  N   GLY A 197       6.959  13.342  41.397  1.00 43.81           N  
ANISOU 1555  N   GLY A 197     5304   4920   6420  -1707   -436   -992       N  
ATOM   1556  CA  GLY A 197       6.318  14.596  41.750  1.00 41.62           C  
ANISOU 1556  CA  GLY A 197     4939   4695   6178  -1701   -367  -1032       C  
ATOM   1557  C   GLY A 197       6.808  15.715  40.852  1.00 37.35           C  
ANISOU 1557  C   GLY A 197     4399   4143   5648  -1554   -355  -1011       C  
ATOM   1558  O   GLY A 197       7.998  15.811  40.568  1.00 40.04           O  
ANISOU 1558  O   GLY A 197     4806   4446   5963  -1499   -351   -954       O  
ATOM   1559  N   GLN A 198       5.890  16.556  40.396  1.00 38.22           N  
ANISOU 1559  N   GLN A 198     4438   4287   5799  -1491   -352  -1060       N  
ATOM   1560  CA  GLN A 198       6.253  17.678  39.547  1.00 38.99           C  
ANISOU 1560  CA  GLN A 198     4544   4364   5905  -1356   -343  -1032       C  
ATOM   1561  C   GLN A 198       6.862  18.798  40.382  1.00 40.53           C  
ANISOU 1561  C   GLN A 198     4727   4547   6126  -1374   -261  -1012       C  
ATOM   1562  O   GLN A 198       6.587  18.920  41.575  1.00 42.00           O  
ANISOU 1562  O   GLN A 198     4862   4762   6332  -1475   -213  -1049       O  
ATOM   1563  CB  GLN A 198       5.041  18.169  38.755  1.00 40.76           C  
ANISOU 1563  CB  GLN A 198     4705   4619   6163  -1272   -386  -1093       C  
ATOM   1564  CG  GLN A 198       4.506  17.132  37.763  1.00 41.65           C  
ANISOU 1564  CG  GLN A 198     4830   4745   6251  -1233   -474  -1119       C  
ATOM   1565  CD  GLN A 198       3.376  17.671  36.903  1.00 49.29           C  
ANISOU 1565  CD  GLN A 198     5737   5744   7247  -1129   -527  -1183       C  
ATOM   1566  NE2 GLN A 198       3.689  18.645  36.061  1.00 45.87           N  
ANISOU 1566  NE2 GLN A 198     5339   5286   6802   -998   -535  -1138       N  
ATOM   1567  OE1 GLN A 198       2.235  17.209  36.990  1.00 54.56           O  
ANISOU 1567  OE1 GLN A 198     6329   6457   7945  -1169   -562  -1272       O  
ATOM   1568  N   VAL A 199       7.699  19.610  39.753  1.00 36.41           N  
ANISOU 1568  N   VAL A 199     4249   3984   5601  -1279   -241   -956       N  
ATOM   1569  CA  VAL A 199       8.386  20.680  40.463  1.00 40.19           C  
ANISOU 1569  CA  VAL A 199     4718   4440   6112  -1292   -165   -937       C  
ATOM   1570  C   VAL A 199       7.911  22.049  39.996  1.00 40.32           C  
ANISOU 1570  C   VAL A 199     4700   4436   6183  -1200   -155   -948       C  
ATOM   1571  O   VAL A 199       7.295  22.179  38.938  1.00 39.13           O  
ANISOU 1571  O   VAL A 199     4557   4284   6029  -1107   -210   -948       O  
ATOM   1572  CB  VAL A 199       9.905  20.567  40.291  1.00 38.09           C  
ANISOU 1572  CB  VAL A 199     4531   4133   5809  -1277   -139   -866       C  
ATOM   1573  CG1 VAL A 199      10.414  19.298  40.985  1.00 33.90           C  
ANISOU 1573  CG1 VAL A 199     4033   3613   5235  -1369   -156   -864       C  
ATOM   1574  CG2 VAL A 199      10.264  20.559  38.810  1.00 37.14           C  
ANISOU 1574  CG2 VAL A 199     4471   3991   5650  -1165   -176   -814       C  
ATOM   1575  N   PHE A 200       8.191  23.066  40.802  1.00 42.73           N  
ANISOU 1575  N   PHE A 200     4970   4724   6540  -1224    -91   -960       N  
ATOM   1576  CA  PHE A 200       7.800  24.431  40.482  1.00 38.06           C  
ANISOU 1576  CA  PHE A 200     4350   4096   6014  -1141    -84   -971       C  
ATOM   1577  C   PHE A 200       8.527  24.936  39.239  1.00 41.02           C  
ANISOU 1577  C   PHE A 200     4814   4406   6366  -1036    -92   -878       C  
ATOM   1578  O   PHE A 200       9.506  24.338  38.790  1.00 36.06           O  
ANISOU 1578  O   PHE A 200     4256   3769   5676  -1038    -83   -814       O  
ATOM   1579  CB  PHE A 200       8.087  25.352  41.670  1.00 38.95           C  
ANISOU 1579  CB  PHE A 200     4407   4200   6192  -1195    -13  -1009       C  
ATOM   1580  CG  PHE A 200       7.251  25.050  42.889  1.00 37.42           C  
ANISOU 1580  CG  PHE A 200     4117   4084   6016  -1295      1  -1109       C  
ATOM   1581  CD1 PHE A 200       5.899  24.788  42.769  1.00 39.03           C  
ANISOU 1581  CD1 PHE A 200     4253   4344   6235  -1292    -47  -1187       C  
ATOM   1582  CD2 PHE A 200       7.827  25.029  44.152  1.00 39.06           C  
ANISOU 1582  CD2 PHE A 200     4301   4318   6223  -1394     64  -1130       C  
ATOM   1583  CE1 PHE A 200       5.128  24.513  43.886  1.00 40.08           C  
ANISOU 1583  CE1 PHE A 200     4292   4559   6378  -1397    -22  -1282       C  
ATOM   1584  CE2 PHE A 200       7.071  24.763  45.271  1.00 37.76           C  
ANISOU 1584  CE2 PHE A 200     4052   4235   6060  -1493     84  -1217       C  
ATOM   1585  CZ  PHE A 200       5.714  24.498  45.138  1.00 43.28           C  
ANISOU 1585  CZ  PHE A 200     4680   4992   6771  -1500     46  -1293       C  
ATOM   1586  N   CYS A 201       8.054  26.053  38.698  1.00 42.25           N  
ANISOU 1586  N   CYS A 201     4965   4516   6570   -946   -110   -873       N  
ATOM   1587  CA  CYS A 201       8.586  26.578  37.450  1.00 38.00           C  
ANISOU 1587  CA  CYS A 201     4520   3919   6001   -847   -121   -777       C  
ATOM   1588  C   CYS A 201       9.039  28.020  37.604  1.00 37.31           C  
ANISOU 1588  C   CYS A 201     4446   3746   5984   -822    -70   -743       C  
ATOM   1589  O   CYS A 201       8.551  28.750  38.470  1.00 37.54           O  
ANISOU 1589  O   CYS A 201     4400   3762   6101   -842    -57   -813       O  
ATOM   1590  CB  CYS A 201       7.537  26.493  36.342  1.00 37.64           C  
ANISOU 1590  CB  CYS A 201     4487   3886   5930   -741   -214   -785       C  
ATOM   1591  SG  CYS A 201       6.930  24.822  36.000  1.00 43.34           S  
ANISOU 1591  SG  CYS A 201     5191   4698   6578   -761   -283   -833       S  
ATOM   1592  N   PHE A 202       9.973  28.424  36.751  1.00 37.49           N  
ANISOU 1592  N   PHE A 202     4562   3714   5970   -781    -41   -639       N  
ATOM   1593  CA  PHE A 202      10.469  29.795  36.748  1.00 38.04           C  
ANISOU 1593  CA  PHE A 202     4661   3686   6106   -760      7   -591       C  
ATOM   1594  C   PHE A 202       9.905  30.570  35.560  1.00 46.94           C  
ANISOU 1594  C   PHE A 202     5858   4750   7227   -641    -54   -527       C  
ATOM   1595  O   PHE A 202      10.032  30.145  34.407  1.00 39.41           O  
ANISOU 1595  O   PHE A 202     4984   3813   6177   -584    -85   -456       O  
ATOM   1596  CB  PHE A 202      11.997  29.807  36.702  1.00 37.65           C  
ANISOU 1596  CB  PHE A 202     4667   3613   6026   -816     96   -519       C  
ATOM   1597  CG  PHE A 202      12.647  29.075  37.844  1.00 36.67           C  
ANISOU 1597  CG  PHE A 202     4486   3544   5904   -921    146   -577       C  
ATOM   1598  CD1 PHE A 202      12.293  29.351  39.155  1.00 37.11           C  
ANISOU 1598  CD1 PHE A 202     4450   3610   6039   -980    164   -667       C  
ATOM   1599  CD2 PHE A 202      13.598  28.097  37.602  1.00 38.21           C  
ANISOU 1599  CD2 PHE A 202     4719   3784   6017   -956    168   -548       C  
ATOM   1600  CE1 PHE A 202      12.888  28.680  40.203  1.00 35.67           C  
ANISOU 1600  CE1 PHE A 202     4227   3479   5846  -1073    203   -714       C  
ATOM   1601  CE2 PHE A 202      14.193  27.418  38.647  1.00 36.48           C  
ANISOU 1601  CE2 PHE A 202     4456   3607   5797  -1042    198   -601       C  
ATOM   1602  CZ  PHE A 202      13.839  27.714  39.949  1.00 36.81           C  
ANISOU 1602  CZ  PHE A 202     4419   3657   5911  -1101    216   -677       C  
ATOM   1603  N   ALA A 203       9.284  31.712  35.850  1.00 40.00           N  
ANISOU 1603  N   ALA A 203     4951   3800   6449   -598    -76   -558       N  
ATOM   1604  CA  ALA A 203       8.693  32.554  34.820  1.00 45.04           C  
ANISOU 1604  CA  ALA A 203     5659   4362   7092   -477   -148   -501       C  
ATOM   1605  C   ALA A 203       9.761  33.320  34.056  1.00 48.99           C  
ANISOU 1605  C   ALA A 203     6283   4766   7565   -466    -92   -359       C  
ATOM   1606  O   ALA A 203       9.544  33.728  32.914  1.00 48.39           O  
ANISOU 1606  O   ALA A 203     6306   4641   7438   -373   -144   -270       O  
ATOM   1607  CB  ALA A 203       7.703  33.532  35.444  1.00 46.27           C  
ANISOU 1607  CB  ALA A 203     5739   4465   7375   -432   -199   -593       C  
ATOM   1608  N   ASP A 204      10.909  33.529  34.693  1.00 41.21           N  
ANISOU 1608  N   ASP A 204     5290   3755   6611   -564     14   -340       N  
ATOM   1609  CA  ASP A 204      11.947  34.359  34.106  1.00 41.88           C  
ANISOU 1609  CA  ASP A 204     5478   3746   6690   -576     83   -217       C  
ATOM   1610  C   ASP A 204      13.362  33.958  34.521  1.00 41.06           C  
ANISOU 1610  C   ASP A 204     5366   3674   6561   -689    199   -202       C  
ATOM   1611  O   ASP A 204      13.565  33.048  35.327  1.00 39.94           O  
ANISOU 1611  O   ASP A 204     5144   3621   6410   -753    220   -284       O  
ATOM   1612  CB  ASP A 204      11.696  35.849  34.415  1.00 42.93           C  
ANISOU 1612  CB  ASP A 204     5617   3737   6956   -548     76   -211       C  
ATOM   1613  CG  ASP A 204      11.831  36.182  35.900  1.00 42.33           C  
ANISOU 1613  CG  ASP A 204     5421   3655   7008   -626    124   -328       C  
ATOM   1614  OD1 ASP A 204      12.434  35.385  36.653  1.00 41.18           O  
ANISOU 1614  OD1 ASP A 204     5209   3597   6840   -717    186   -382       O  
ATOM   1615  OD2 ASP A 204      11.345  37.254  36.312  1.00 43.11           O1-
ANISOU 1615  OD2 ASP A 204     5492   3658   7230   -592     94   -368       O1-
ATOM   1616  N   SER A 205      14.332  34.665  33.956  1.00 41.76           N  
ANISOU 1616  N   SER A 205     5540   3687   6640   -711    273    -97       N  
ATOM   1617  CA  SER A 205      15.747  34.390  34.153  1.00 41.26           C  
ANISOU 1617  CA  SER A 205     5475   3652   6550   -810    384    -79       C  
ATOM   1618  C   SER A 205      16.243  34.719  35.562  1.00 42.12           C  
ANISOU 1618  C   SER A 205     5483   3741   6779   -897    446   -173       C  
ATOM   1619  O   SER A 205      17.398  34.443  35.898  1.00 40.16           O  
ANISOU 1619  O   SER A 205     5214   3525   6521   -978    531   -185       O  
ATOM   1620  CB  SER A 205      16.549  35.187  33.125  1.00 42.46           C  
ANISOU 1620  CB  SER A 205     5744   3724   6664   -816    450     58       C  
ATOM   1621  OG  SER A 205      15.993  36.489  32.975  1.00 43.68           O  
ANISOU 1621  OG  SER A 205     5950   3739   6907   -768    418    110       O  
ATOM   1622  N   ALA A 206      15.384  35.322  36.377  1.00 40.75           N  
ANISOU 1622  N   ALA A 206     5243   3521   6717   -876    402   -248       N  
ATOM   1623  CA  ALA A 206      15.753  35.651  37.750  1.00 40.25           C  
ANISOU 1623  CA  ALA A 206     5079   3451   6764   -951    452   -349       C  
ATOM   1624  C   ALA A 206      15.096  34.669  38.716  1.00 42.58           C  
ANISOU 1624  C   ALA A 206     5271   3861   7045   -969    408   -469       C  
ATOM   1625  O   ALA A 206      15.081  34.887  39.927  1.00 38.84           O  
ANISOU 1625  O   ALA A 206     4704   3400   6652  -1018    429   -568       O  
ATOM   1626  CB  ALA A 206      15.370  37.096  38.089  1.00 41.26           C  
ANISOU 1626  CB  ALA A 206     5195   3446   7037   -927    444   -363       C  
ATOM   1627  N   ALA A 207      14.549  33.587  38.164  1.00 38.77           N  
ANISOU 1627  N   ALA A 207     4809   3465   6457   -933    348   -459       N  
ATOM   1628  CA  ALA A 207      13.975  32.514  38.963  1.00 37.86           C  
ANISOU 1628  CA  ALA A 207     4614   3459   6313   -964    310   -556       C  
ATOM   1629  C   ALA A 207      12.758  32.940  39.790  1.00 38.08           C  
ANISOU 1629  C   ALA A 207     4550   3492   6428   -947    260   -659       C  
ATOM   1630  O   ALA A 207      12.538  32.428  40.885  1.00 37.47           O  
ANISOU 1630  O   ALA A 207     4387   3490   6360  -1009    266   -753       O  
ATOM   1631  CB  ALA A 207      15.048  31.891  39.863  1.00 36.97           C  
ANISOU 1631  CB  ALA A 207     4460   3402   6184  -1060    376   -597       C  
ATOM   1632  N   HIS A 208      11.974  33.884  39.279  1.00 39.07           N  
ANISOU 1632  N   HIS A 208     4694   3539   6612   -863    209   -645       N  
ATOM   1633  CA  HIS A 208      10.702  34.203  39.917  1.00 39.41           C  
ANISOU 1633  CA  HIS A 208     4643   3600   6730   -832    147   -757       C  
ATOM   1634  C   HIS A 208       9.730  33.069  39.602  1.00 44.43           C  
ANISOU 1634  C   HIS A 208     5257   4340   7282   -808     76   -792       C  
ATOM   1635  O   HIS A 208       9.637  32.626  38.451  1.00 45.36           O  
ANISOU 1635  O   HIS A 208     5457   4460   7319   -748     33   -714       O  
ATOM   1636  CB  HIS A 208      10.144  35.543  39.425  1.00 40.69           C  
ANISOU 1636  CB  HIS A 208     4834   3641   6987   -736     97   -740       C  
ATOM   1637  CG  HIS A 208      11.009  36.721  39.753  1.00 47.70           C  
ANISOU 1637  CG  HIS A 208     5738   4410   7975   -763    162   -713       C  
ATOM   1638  CD2 HIS A 208      11.766  37.518  38.963  1.00 41.92           C  
ANISOU 1638  CD2 HIS A 208     5115   3555   7258   -744    193   -591       C  
ATOM   1639  ND1 HIS A 208      11.145  37.213  41.035  1.00 47.44           N  
ANISOU 1639  ND1 HIS A 208     5602   4379   8045   -822    204   -822       N  
ATOM   1640  CE1 HIS A 208      11.962  38.251  41.021  1.00 41.62           C  
ANISOU 1640  CE1 HIS A 208     4903   3519   7390   -835    255   -775       C  
ATOM   1641  NE2 HIS A 208      12.351  38.458  39.777  1.00 42.19           N  
ANISOU 1641  NE2 HIS A 208     5106   3511   7412   -794    253   -632       N  
ATOM   1642  N   LEU A 209       9.017  32.584  40.617  1.00 41.93           N  
ANISOU 1642  N   LEU A 209     4832   4116   6985   -859     66   -912       N  
ATOM   1643  CA  LEU A 209       8.158  31.412  40.431  1.00 40.90           C  
ANISOU 1643  CA  LEU A 209     4674   4086   6779   -862     10   -952       C  
ATOM   1644  C   LEU A 209       6.930  31.723  39.582  1.00 42.02           C  
ANISOU 1644  C   LEU A 209     4813   4213   6939   -748    -89   -975       C  
ATOM   1645  O   LEU A 209       6.352  32.808  39.682  1.00 41.48           O  
ANISOU 1645  O   LEU A 209     4709   4087   6966   -685   -122  -1024       O  
ATOM   1646  CB  LEU A 209       7.751  30.811  41.778  1.00 42.17           C  
ANISOU 1646  CB  LEU A 209     4724   4351   6949   -965     36  -1068       C  
ATOM   1647  CG  LEU A 209       8.896  30.144  42.543  1.00 40.82           C  
ANISOU 1647  CG  LEU A 209     4567   4214   6728  -1074    111  -1043       C  
ATOM   1648  CD1 LEU A 209       8.479  29.817  43.968  1.00 42.81           C  
ANISOU 1648  CD1 LEU A 209     4714   4559   6992  -1174    140  -1155       C  
ATOM   1649  CD2 LEU A 209       9.377  28.888  41.817  1.00 38.70           C  
ANISOU 1649  CD2 LEU A 209     4380   3975   6348  -1085     95   -964       C  
ATOM   1650  N   ALA A 210       6.539  30.765  38.746  1.00 42.83           N  
ANISOU 1650  N   ALA A 210     4952   4367   6953   -716   -143   -948       N  
ATOM   1651  CA  ALA A 210       5.438  30.960  37.809  1.00 48.46           C  
ANISOU 1651  CA  ALA A 210     5672   5073   7668   -596   -245   -967       C  
ATOM   1652  C   ALA A 210       4.101  30.519  38.401  1.00 49.87           C  
ANISOU 1652  C   ALA A 210     5721   5347   7880   -613   -294  -1118       C  
ATOM   1653  O   ALA A 210       4.046  29.600  39.219  1.00 45.42           O  
ANISOU 1653  O   ALA A 210     5093   4874   7289   -724   -254  -1175       O  
ATOM   1654  CB  ALA A 210       5.714  30.213  36.507  1.00 46.93           C  
ANISOU 1654  CB  ALA A 210     5584   4888   7360   -543   -283   -867       C  
ATOM   1655  N   LEU A 211       3.029  31.183  37.983  1.00 51.47           N  
ANISOU 1655  N   LEU A 211     5887   5530   8140   -504   -382  -1183       N  
ATOM   1656  CA  LEU A 211       1.677  30.793  38.373  1.00 56.61           C  
ANISOU 1656  CA  LEU A 211     6408   6279   8823   -507   -436  -1338       C  
ATOM   1657  C   LEU A 211       0.895  30.320  37.153  1.00 57.52           C  
ANISOU 1657  C   LEU A 211     6552   6416   8885   -399   -541  -1338       C  
ATOM   1658  O   LEU A 211       1.158  30.761  36.031  1.00 59.01           O  
ANISOU 1658  O   LEU A 211     6855   6526   9042   -285   -594  -1235       O  
ATOM   1659  CB  LEU A 211       0.944  31.965  39.020  1.00 57.58           C  
ANISOU 1659  CB  LEU A 211     6428   6378   9071   -462   -461  -1460       C  
ATOM   1660  CG  LEU A 211       1.611  32.609  40.233  1.00 57.92           C  
ANISOU 1660  CG  LEU A 211     6428   6398   9180   -551   -368  -1484       C  
ATOM   1661  CD1 LEU A 211       0.841  33.847  40.656  1.00 56.09           C  
ANISOU 1661  CD1 LEU A 211     6103   6130   9080   -476   -415  -1608       C  
ATOM   1662  CD2 LEU A 211       1.705  31.613  41.375  1.00 58.62           C  
ANISOU 1662  CD2 LEU A 211     6435   6610   9227   -712   -285  -1546       C  
ATOM   1663  N   ASP A 212      -0.067  29.428  37.369  1.00 56.99           N  
ANISOU 1663  N   ASP A 212     6387   6460   8809   -439   -572  -1454       N  
ATOM   1664  CA  ASP A 212      -0.901  28.950  36.273  1.00 64.10           C  
ANISOU 1664  CA  ASP A 212     7295   7392   9669   -337   -678  -1480       C  
ATOM   1665  C   ASP A 212      -2.090  29.873  36.025  1.00 69.64           C  
ANISOU 1665  C   ASP A 212     7922   8081  10457   -205   -781  -1597       C  
ATOM   1666  O   ASP A 212      -2.174  30.967  36.585  1.00 69.13           O  
ANISOU 1666  O   ASP A 212     7819   7965  10484   -179   -775  -1640       O  
ATOM   1667  CB  ASP A 212      -1.366  27.504  36.501  1.00 63.77           C  
ANISOU 1667  CB  ASP A 212     7185   7465   9578   -440   -670  -1550       C  
ATOM   1668  CG  ASP A 212      -2.323  27.364  37.678  1.00 61.92           C  
ANISOU 1668  CG  ASP A 212     6785   7328   9415   -539   -642  -1721       C  
ATOM   1669  OD1 ASP A 212      -3.016  28.345  38.023  1.00 60.79           O  
ANISOU 1669  OD1 ASP A 212     6554   7181   9361   -482   -671  -1826       O  
ATOM   1670  OD2 ASP A 212      -2.390  26.257  38.253  1.00 60.76           O1-
ANISOU 1670  OD2 ASP A 212     6594   7261   9232   -677   -593  -1753       O1-
ATOM   1671  N   GLU A 213      -3.005  29.409  35.181  1.00 75.07           N  
ANISOU 1671  N   GLU A 213     8587   8817  11118   -117   -883  -1658       N  
ATOM   1672  CA  GLU A 213      -4.169  30.182  34.763  1.00 78.52           C  
ANISOU 1672  CA  GLU A 213     8960   9247  11627     32  -1006  -1774       C  
ATOM   1673  C   GLU A 213      -5.127  30.501  35.909  1.00 75.71           C  
ANISOU 1673  C   GLU A 213     8418   8964  11383    -20   -994  -1974       C  
ATOM   1674  O   GLU A 213      -5.995  31.362  35.773  1.00 75.99           O  
ANISOU 1674  O   GLU A 213     8389   8982  11503    103  -1089  -2085       O  
ATOM   1675  CB  GLU A 213      -4.913  29.423  33.660  1.00 83.07           C  
ANISOU 1675  CB  GLU A 213     9541   9881  12142    124  -1113  -1810       C  
ATOM   1676  CG  GLU A 213      -4.837  27.907  33.819  1.00 87.10           C  
ANISOU 1676  CG  GLU A 213    10017  10492  12583    -11  -1058  -1824       C  
ATOM   1677  CD  GLU A 213      -5.697  27.155  32.819  1.00 93.50           C  
ANISOU 1677  CD  GLU A 213    10804  11368  13352     75  -1168  -1894       C  
ATOM   1678  OE1 GLU A 213      -6.329  27.805  31.958  1.00 96.63           O  
ANISOU 1678  OE1 GLU A 213    11216  11736  13761    248  -1290  -1926       O  
ATOM   1679  OE2 GLU A 213      -5.745  25.909  32.899  1.00 94.18           O1-
ANISOU 1679  OE2 GLU A 213    10857  11530  13395    -29  -1138  -1920       O1-
ATOM   1680  N   THR A 214      -4.966  29.813  37.035  1.00 73.72           N  
ANISOU 1680  N   THR A 214     8083   8798  11129   -200   -882  -2022       N  
ATOM   1681  CA  THR A 214      -5.903  29.941  38.149  1.00 73.46           C  
ANISOU 1681  CA  THR A 214     7864   8867  11182   -274   -857  -2221       C  
ATOM   1682  C   THR A 214      -5.280  30.587  39.383  1.00 71.57           C  
ANISOU 1682  C   THR A 214     7594   8610  10992   -371   -752  -2221       C  
ATOM   1683  O   THR A 214      -5.909  30.654  40.440  1.00 70.86           O  
ANISOU 1683  O   THR A 214     7350   8616  10956   -457   -709  -2378       O  
ATOM   1684  CB  THR A 214      -6.488  28.573  38.554  1.00 75.03           C  
ANISOU 1684  CB  THR A 214     7964   9207  11337   -418   -816  -2312       C  
ATOM   1685  CG2 THR A 214      -7.078  27.864  37.341  1.00 73.12           C  
ANISOU 1685  CG2 THR A 214     7746   8987  11050   -327   -919  -2321       C  
ATOM   1686  OG1 THR A 214      -5.458  27.759  39.128  1.00 74.14           O  
ANISOU 1686  OG1 THR A 214     7921   9100  11148   -579   -700  -2192       O  
ATOM   1687  N   GLY A 215      -4.045  31.059  39.249  1.00 68.74           N  
ANISOU 1687  N   GLY A 215     7373   8134  10610   -361   -709  -2053       N  
ATOM   1688  CA  GLY A 215      -3.366  31.718  40.350  1.00 65.52           C  
ANISOU 1688  CA  GLY A 215     6943   7699  10251   -442   -615  -2050       C  
ATOM   1689  C   GLY A 215      -2.655  30.760  41.288  1.00 65.29           C  
ANISOU 1689  C   GLY A 215     6911   7745  10151   -632   -490  -2010       C  
ATOM   1690  O   GLY A 215      -2.284  31.130  42.402  1.00 68.21           O  
ANISOU 1690  O   GLY A 215     7228   8134  10555   -720   -409  -2047       O  
ATOM   1691  N   LYS A 216      -2.467  29.523  40.838  1.00 61.71           N  
ANISOU 1691  N   LYS A 216     6517   7331   9600   -689   -482  -1937       N  
ATOM   1692  CA  LYS A 216      -1.751  28.520  41.620  1.00 59.16           C  
ANISOU 1692  CA  LYS A 216     6214   7061   9202   -859   -381  -1882       C  
ATOM   1693  C   LYS A 216      -0.347  28.313  41.064  1.00 51.21           C  
ANISOU 1693  C   LYS A 216     5373   5959   8126   -850   -353  -1693       C  
ATOM   1694  O   LYS A 216      -0.097  28.548  39.881  1.00 49.70           O  
ANISOU 1694  O   LYS A 216     5280   5688   7914   -729   -414  -1602       O  
ATOM   1695  CB  LYS A 216      -2.516  27.191  41.624  1.00 65.55           C  
ANISOU 1695  CB  LYS A 216     6967   7981   9959   -947   -390  -1946       C  
ATOM   1696  CG  LYS A 216      -3.859  27.252  42.339  1.00 74.43           C  
ANISOU 1696  CG  LYS A 216     7912   9226  11143   -996   -392  -2146       C  
ATOM   1697  CD  LYS A 216      -4.737  26.053  41.999  1.00 78.92           C  
ANISOU 1697  CD  LYS A 216     8430   9883  11674  -1050   -425  -2211       C  
ATOM   1698  CE  LYS A 216      -4.050  24.741  42.332  1.00 82.36           C  
ANISOU 1698  CE  LYS A 216     8942  10337  12015  -1204   -358  -2108       C  
ATOM   1699  NZ  LYS A 216      -4.891  23.574  41.937  1.00 88.76           N1+
ANISOU 1699  NZ  LYS A 216     9710  11217  12800  -1257   -395  -2169       N1+
ATOM   1700  N   LEU A 217       0.569  27.870  41.920  1.00 42.92           N  
ANISOU 1700  N   LEU A 217     4350   4924   7035   -977   -261  -1639       N  
ATOM   1701  CA  LEU A 217       1.946  27.641  41.496  1.00 46.48           C  
ANISOU 1701  CA  LEU A 217     4941   5297   7424   -978   -228  -1479       C  
ATOM   1702  C   LEU A 217       2.020  26.602  40.383  1.00 48.11           C  
ANISOU 1702  C   LEU A 217     5231   5502   7547   -945   -281  -1404       C  
ATOM   1703  O   LEU A 217       1.480  25.503  40.501  1.00 47.47           O  
ANISOU 1703  O   LEU A 217     5113   5496   7426  -1015   -295  -1449       O  
ATOM   1704  CB  LEU A 217       2.810  27.224  42.681  1.00 42.74           C  
ANISOU 1704  CB  LEU A 217     4468   4853   6918  -1121   -133  -1458       C  
ATOM   1705  CG  LEU A 217       3.138  28.375  43.630  1.00 45.66           C  
ANISOU 1705  CG  LEU A 217     4785   5200   7363  -1136    -76  -1502       C  
ATOM   1706  CD1 LEU A 217       3.483  27.845  45.012  1.00 45.28           C  
ANISOU 1706  CD1 LEU A 217     4692   5232   7281  -1288      5  -1537       C  
ATOM   1707  CD2 LEU A 217       4.273  29.235  43.063  1.00 49.10           C  
ANISOU 1707  CD2 LEU A 217     5322   5512   7821  -1058    -63  -1388       C  
ATOM   1708  N   LEU A 218       2.689  26.970  39.298  1.00 51.01           N  
ANISOU 1708  N   LEU A 218     5710   5784   7887   -840   -310  -1292       N  
ATOM   1709  CA  LEU A 218       2.810  26.108  38.133  1.00 50.26           C  
ANISOU 1709  CA  LEU A 218     5696   5689   7710   -788   -365  -1223       C  
ATOM   1710  C   LEU A 218       3.717  24.914  38.433  1.00 46.23           C  
ANISOU 1710  C   LEU A 218     5237   5203   7125   -896   -317  -1164       C  
ATOM   1711  O   LEU A 218       4.661  25.029  39.208  1.00 39.04           O  
ANISOU 1711  O   LEU A 218     4347   4272   6214   -972   -242  -1124       O  
ATOM   1712  CB  LEU A 218       3.362  26.913  36.957  1.00 49.12           C  
ANISOU 1712  CB  LEU A 218     5661   5454   7547   -656   -396  -1115       C  
ATOM   1713  CG  LEU A 218       3.286  26.265  35.579  1.00 50.82           C  
ANISOU 1713  CG  LEU A 218     5954   5678   7678   -567   -469  -1060       C  
ATOM   1714  CD1 LEU A 218       1.841  25.936  35.233  1.00 50.73           C  
ANISOU 1714  CD1 LEU A 218     5861   5729   7685   -511   -564  -1174       C  
ATOM   1715  CD2 LEU A 218       3.897  27.191  34.544  1.00 48.96           C  
ANISOU 1715  CD2 LEU A 218     5832   5355   7415   -452   -483   -942       C  
ATOM   1716  N   ARG A 219       3.421  23.771  37.819  1.00 47.67           N  
ANISOU 1716  N   ARG A 219     5438   5425   7249   -897   -369  -1166       N  
ATOM   1717  CA  ARG A 219       4.206  22.555  38.022  1.00 45.43           C  
ANISOU 1717  CA  ARG A 219     5206   5155   6899   -988   -346  -1118       C  
ATOM   1718  C   ARG A 219       4.565  21.898  36.699  1.00 40.28           C  
ANISOU 1718  C   ARG A 219     4640   4490   6175   -905   -406  -1055       C  
ATOM   1719  O   ARG A 219       3.735  21.801  35.797  1.00 38.05           O  
ANISOU 1719  O   ARG A 219     4344   4227   5885   -818   -482  -1090       O  
ATOM   1720  CB  ARG A 219       3.426  21.549  38.868  1.00 48.93           C  
ANISOU 1720  CB  ARG A 219     5572   5669   7349  -1112   -346  -1205       C  
ATOM   1721  CG  ARG A 219       3.120  22.011  40.276  1.00 50.20           C  
ANISOU 1721  CG  ARG A 219     5647   5866   7561  -1216   -278  -1272       C  
ATOM   1722  CD  ARG A 219       4.017  21.331  41.286  1.00 44.23           C  
ANISOU 1722  CD  ARG A 219     4928   5113   6764  -1346   -217  -1228       C  
ATOM   1723  NE  ARG A 219       3.580  21.607  42.648  1.00 44.60           N  
ANISOU 1723  NE  ARG A 219     4887   5217   6843  -1457   -155  -1303       N  
ATOM   1724  CZ  ARG A 219       4.099  21.039  43.730  1.00 48.73           C  
ANISOU 1724  CZ  ARG A 219     5426   5761   7328  -1585   -104  -1285       C  
ATOM   1725  NH1 ARG A 219       5.082  20.152  43.612  1.00 47.48           N1+
ANISOU 1725  NH1 ARG A 219     5369   5563   7110  -1612   -114  -1198       N1+
ATOM   1726  NH2 ARG A 219       3.632  21.355  44.931  1.00 47.45           N  
ANISOU 1726  NH2 ARG A 219     5180   5665   7186  -1681    -47  -1359       N  
ATOM   1727  N   LYS A 220       5.803  21.434  36.591  1.00 40.53           N  
ANISOU 1727  N   LYS A 220     4752   4494   6152   -929   -374   -973       N  
ATOM   1728  CA  LYS A 220       6.231  20.674  35.423  1.00 39.86           C  
ANISOU 1728  CA  LYS A 220     4742   4412   5993   -864   -426   -926       C  
ATOM   1729  C   LYS A 220       7.106  19.491  35.835  1.00 36.71           C  
ANISOU 1729  C   LYS A 220     4380   4016   5554   -952   -413   -906       C  
ATOM   1730  O   LYS A 220       7.605  19.452  36.956  1.00 39.35           O  
ANISOU 1730  O   LYS A 220     4703   4340   5908  -1051   -355   -903       O  
ATOM   1731  CB  LYS A 220       6.961  21.581  34.431  1.00 39.88           C  
ANISOU 1731  CB  LYS A 220     4821   4372   5959   -754   -413   -838       C  
ATOM   1732  CG  LYS A 220       6.029  22.465  33.636  1.00 42.35           C  
ANISOU 1732  CG  LYS A 220     5126   4678   6288   -637   -467   -849       C  
ATOM   1733  CD  LYS A 220       6.753  23.177  32.513  1.00 50.58           C  
ANISOU 1733  CD  LYS A 220     6266   5680   7271   -534   -462   -746       C  
ATOM   1734  CE  LYS A 220       5.796  24.080  31.740  1.00 57.69           C  
ANISOU 1734  CE  LYS A 220     7171   6563   8184   -409   -530   -750       C  
ATOM   1735  NZ  LYS A 220       6.486  24.822  30.647  1.00 60.58           N1+
ANISOU 1735  NZ  LYS A 220     7649   6886   8482   -317   -522   -634       N1+
ATOM   1736  N   PRO A 221       7.277  18.512  34.935  1.00 37.52           N  
ANISOU 1736  N   PRO A 221     4525   4133   5598   -911   -475   -899       N  
ATOM   1737  CA  PRO A 221       8.085  17.323  35.246  1.00 41.06           C  
ANISOU 1737  CA  PRO A 221     5012   4574   6014   -980   -482   -888       C  
ATOM   1738  C   PRO A 221       9.551  17.646  35.534  1.00 39.72           C  
ANISOU 1738  C   PRO A 221     4896   4373   5822   -994   -416   -823       C  
ATOM   1739  O   PRO A 221      10.137  18.506  34.882  1.00 37.45           O  
ANISOU 1739  O   PRO A 221     4643   4074   5513   -919   -382   -771       O  
ATOM   1740  CB  PRO A 221       7.975  16.481  33.974  1.00 36.93           C  
ANISOU 1740  CB  PRO A 221     4521   4073   5437   -897   -567   -900       C  
ATOM   1741  CG  PRO A 221       6.676  16.917  33.343  1.00 41.57           C  
ANISOU 1741  CG  PRO A 221     5060   4692   6044   -824   -615   -947       C  
ATOM   1742  CD  PRO A 221       6.568  18.383  33.649  1.00 39.53           C  
ANISOU 1742  CD  PRO A 221     4784   4414   5822   -798   -555   -919       C  
ATOM   1743  N   HIS A 222      10.123  16.938  36.504  1.00 38.98           N  
ANISOU 1743  N   HIS A 222     4813   4266   5733  -1091   -402   -828       N  
ATOM   1744  CA  HIS A 222      11.511  17.112  36.912  1.00 35.34           C  
ANISOU 1744  CA  HIS A 222     4391   3779   5256  -1111   -348   -786       C  
ATOM   1745  C   HIS A 222      12.459  16.194  36.127  1.00 39.32           C  
ANISOU 1745  C   HIS A 222     4954   4284   5703  -1064   -394   -776       C  
ATOM   1746  O   HIS A 222      13.674  16.248  36.301  1.00 44.08           O  
ANISOU 1746  O   HIS A 222     5586   4875   6290  -1068   -358   -754       O  
ATOM   1747  CB  HIS A 222      11.637  16.831  38.413  1.00 38.08           C  
ANISOU 1747  CB  HIS A 222     4720   4115   5632  -1232   -319   -803       C  
ATOM   1748  CG  HIS A 222      13.005  17.088  38.969  1.00 44.13           C  
ANISOU 1748  CG  HIS A 222     5516   4860   6392  -1252   -267   -776       C  
ATOM   1749  CD2 HIS A 222      13.743  18.222  39.035  1.00 40.91           C  
ANISOU 1749  CD2 HIS A 222     5103   4441   6002  -1226   -190   -750       C  
ATOM   1750  ND1 HIS A 222      13.770  16.099  39.549  1.00 46.31           N  
ANISOU 1750  ND1 HIS A 222     5830   5120   6644  -1303   -297   -780       N  
ATOM   1751  CE1 HIS A 222      14.921  16.611  39.948  1.00 45.17           C  
ANISOU 1751  CE1 HIS A 222     5696   4965   6502  -1303   -244   -766       C  
ATOM   1752  NE2 HIS A 222      14.930  17.898  39.647  1.00 43.92           N  
ANISOU 1752  NE2 HIS A 222     5508   4808   6370  -1262   -173   -748       N  
ATOM   1753  N   GLY A 223      11.897  15.343  35.271  1.00 41.20           N  
ANISOU 1753  N   GLY A 223     5199   4541   5915  -1020   -476   -803       N  
ATOM   1754  CA  GLY A 223      12.697  14.442  34.462  1.00 39.87           C  
ANISOU 1754  CA  GLY A 223     5075   4380   5694   -967   -530   -811       C  
ATOM   1755  C   GLY A 223      12.804  13.052  35.067  1.00 39.59           C  
ANISOU 1755  C   GLY A 223     5056   4315   5670  -1036   -599   -848       C  
ATOM   1756  O   GLY A 223      12.494  12.846  36.245  1.00 36.38           O  
ANISOU 1756  O   GLY A 223     4640   3882   5301  -1138   -589   -851       O  
ATOM   1757  N   HIS A 224      13.265  12.098  34.266  1.00 34.81           N  
ANISOU 1757  N   HIS A 224     4822   3739   4664   -892   -239   -411       N  
ATOM   1758  CA  HIS A 224      13.313  10.705  34.699  1.00 34.93           C  
ANISOU 1758  CA  HIS A 224     4788   3893   4589   -884   -286   -380       C  
ATOM   1759  C   HIS A 224      14.420  10.406  35.706  1.00 34.75           C  
ANISOU 1759  C   HIS A 224     4704   3910   4589   -967   -397   -423       C  
ATOM   1760  O   HIS A 224      14.473   9.317  36.264  1.00 38.40           O  
ANISOU 1760  O   HIS A 224     5141   4480   4969   -960   -454   -405       O  
ATOM   1761  CB  HIS A 224      13.360   9.767  33.490  1.00 37.40           C  
ANISOU 1761  CB  HIS A 224     5055   4238   4917   -842   -218   -261       C  
ATOM   1762  CG  HIS A 224      12.141   9.862  32.626  1.00 45.47           C  
ANISOU 1762  CG  HIS A 224     6138   5251   5886   -748   -133   -227       C  
ATOM   1763  CD2 HIS A 224      10.919  10.397  32.870  1.00 47.48           C  
ANISOU 1763  CD2 HIS A 224     6469   5503   6069   -687   -115   -284       C  
ATOM   1764  ND1 HIS A 224      12.100   9.387  31.332  1.00 43.74           N  
ANISOU 1764  ND1 HIS A 224     5902   5030   5688   -702    -60   -130       N  
ATOM   1765  CE1 HIS A 224      10.903   9.619  30.819  1.00 49.44           C  
ANISOU 1765  CE1 HIS A 224     6687   5747   6350   -618    -10   -128       C  
ATOM   1766  NE2 HIS A 224      10.168  10.232  31.732  1.00 50.53           N  
ANISOU 1766  NE2 HIS A 224     6877   5885   6438   -606    -42   -220       N  
ATOM   1767  N   GLY A 225      15.284  11.383  35.962  1.00 35.96           N  
ANISOU 1767  N   GLY A 225     4838   3972   4854  -1044   -434   -481       N  
ATOM   1768  CA  GLY A 225      16.240  11.269  37.051  1.00 36.92           C  
ANISOU 1768  CA  GLY A 225     4908   4130   4991  -1119   -560   -548       C  
ATOM   1769  C   GLY A 225      15.539  11.007  38.378  1.00 39.50           C  
ANISOU 1769  C   GLY A 225     5307   4552   5151  -1096   -638   -630       C  
ATOM   1770  O   GLY A 225      16.139  10.484  39.321  1.00 37.59           O  
ANISOU 1770  O   GLY A 225     5035   4384   4864  -1131   -751   -662       O  
ATOM   1771  N   ASP A 226      14.265  11.378  38.447  1.00 36.70           N  
ANISOU 1771  N   ASP A 226     5045   4196   4701  -1032   -578   -665       N  
ATOM   1772  CA  ASP A 226      13.431  11.121  39.615  1.00 38.83           C  
ANISOU 1772  CA  ASP A 226     5388   4564   4800  -1002   -620   -738       C  
ATOM   1773  C   ASP A 226      13.403   9.640  40.007  1.00 37.24           C  
ANISOU 1773  C   ASP A 226     5164   4499   4486   -986   -659   -669       C  
ATOM   1774  O   ASP A 226      13.171   9.309  41.169  1.00 38.15           O  
ANISOU 1774  O   ASP A 226     5327   4702   4467   -991   -725   -722       O  
ATOM   1775  CB  ASP A 226      11.990  11.555  39.338  1.00 38.19           C  
ANISOU 1775  CB  ASP A 226     5387   4472   4653   -921   -522   -762       C  
ATOM   1776  CG  ASP A 226      11.794  13.049  39.435  1.00 42.48           C  
ANISOU 1776  CG  ASP A 226     5988   4893   5259   -925   -508   -866       C  
ATOM   1777  OD1 ASP A 226      12.646  13.723  40.054  1.00 38.61           O  
ANISOU 1777  OD1 ASP A 226     5494   4346   4829   -998   -587   -946       O  
ATOM   1778  OD2 ASP A 226      10.775  13.540  38.897  1.00 42.10           O1-
ANISOU 1778  OD2 ASP A 226     5989   4803   5205   -852   -423   -871       O1-
ATOM   1779  N   VAL A 227      13.603   8.752  39.037  1.00 35.11           N  
ANISOU 1779  N   VAL A 227     4831   4244   4264   -963   -614   -552       N  
ATOM   1780  CA  VAL A 227      13.510   7.322  39.314  1.00 34.48           C  
ANISOU 1780  CA  VAL A 227     4737   4276   4087   -942   -643   -480       C  
ATOM   1781  C   VAL A 227      14.427   6.923  40.480  1.00 35.46           C  
ANISOU 1781  C   VAL A 227     4846   4457   4170   -993   -782   -511       C  
ATOM   1782  O   VAL A 227      14.047   6.132  41.348  1.00 35.53           O  
ANISOU 1782  O   VAL A 227     4904   4562   4035   -980   -827   -504       O  
ATOM   1783  CB  VAL A 227      13.777   6.460  38.048  1.00 33.41           C  
ANISOU 1783  CB  VAL A 227     4530   4133   4032   -914   -583   -359       C  
ATOM   1784  CG1 VAL A 227      15.261   6.422  37.716  1.00 33.91           C  
ANISOU 1784  CG1 VAL A 227     4493   4154   4238   -964   -636   -331       C  
ATOM   1785  CG2 VAL A 227      13.232   5.042  38.241  1.00 37.02           C  
ANISOU 1785  CG2 VAL A 227     5000   4691   4376   -876   -584   -292       C  
ATOM   1786  N   HIS A 228      15.621   7.507  40.526  1.00 36.38           N  
ANISOU 1786  N   HIS A 228     4897   4513   4410  -1052   -854   -548       N  
ATOM   1787  CA  HIS A 228      16.598   7.113  41.536  1.00 37.43           C  
ANISOU 1787  CA  HIS A 228     5000   4701   4521  -1095  -1003   -577       C  
ATOM   1788  C   HIS A 228      16.226   7.573  42.941  1.00 41.24           C  
ANISOU 1788  C   HIS A 228     5580   5232   4858  -1110  -1084   -689       C  
ATOM   1789  O   HIS A 228      16.439   6.840  43.911  1.00 41.20           O  
ANISOU 1789  O   HIS A 228     5603   5318   4734  -1110  -1187   -687       O  
ATOM   1790  CB  HIS A 228      18.006   7.578  41.147  1.00 38.23           C  
ANISOU 1790  CB  HIS A 228     4983   4730   4813  -1158  -1058   -590       C  
ATOM   1791  CG  HIS A 228      18.417   7.128  39.782  1.00 37.34           C  
ANISOU 1791  CG  HIS A 228     4776   4579   4835  -1142   -969   -484       C  
ATOM   1792  CD2 HIS A 228      18.766   7.828  38.678  1.00 37.26           C  
ANISOU 1792  CD2 HIS A 228     4709   4469   4980  -1167   -876   -463       C  
ATOM   1793  ND1 HIS A 228      18.469   5.798  39.425  1.00 36.51           N  
ANISOU 1793  ND1 HIS A 228     4635   4538   4700  -1094   -963   -382       N  
ATOM   1794  CE1 HIS A 228      18.840   5.698  38.161  1.00 35.94           C  
ANISOU 1794  CE1 HIS A 228     4484   4415   4757  -1085   -871   -312       C  
ATOM   1795  NE2 HIS A 228      19.030   6.916  37.686  1.00 40.60           N  
ANISOU 1795  NE2 HIS A 228     5062   4908   5456  -1131   -814   -355       N  
ATOM   1796  N   SER A 229      15.666   8.774  43.051  1.00 40.94           N  
ANISOU 1796  N   SER A 229     5602   5132   4822  -1118  -1037   -787       N  
ATOM   1797  CA  SER A 229      15.272   9.297  44.357  1.00 44.47           C  
ANISOU 1797  CA  SER A 229     6147   5622   5127  -1128  -1102   -911       C  
ATOM   1798  C   SER A 229      13.977   8.638  44.824  1.00 40.07           C  
ANISOU 1798  C   SER A 229     5685   5167   4373  -1068  -1037   -889       C  
ATOM   1799  O   SER A 229      13.787   8.402  46.016  1.00 40.37           O  
ANISOU 1799  O   SER A 229     5799   5294   4247  -1071  -1104   -940       O  
ATOM   1800  CB  SER A 229      15.142  10.827  44.338  1.00 44.75           C  
ANISOU 1800  CB  SER A 229     6215   5545   5242  -1154  -1077  -1035       C  
ATOM   1801  OG  SER A 229      14.226  11.264  43.350  1.00 46.99           O  
ANISOU 1801  OG  SER A 229     6519   5761   5576  -1105   -931  -1004       O  
ATOM   1802  N   LEU A 230      13.090   8.334  43.881  1.00 38.16           N  
ANISOU 1802  N   LEU A 230     5437   4914   4147  -1017   -905   -813       N  
ATOM   1803  CA  LEU A 230      11.889   7.558  44.192  1.00 37.58           C  
ANISOU 1803  CA  LEU A 230     5429   4940   3911   -968   -833   -777       C  
ATOM   1804  C   LEU A 230      12.267   6.207  44.791  1.00 39.57           C  
ANISOU 1804  C   LEU A 230     5685   5291   4060   -978   -909   -693       C  
ATOM   1805  O   LEU A 230      11.707   5.772  45.802  1.00 43.20           O  
ANISOU 1805  O   LEU A 230     6228   5845   4342   -973   -921   -709       O  
ATOM   1806  CB  LEU A 230      11.048   7.341  42.932  1.00 36.16           C  
ANISOU 1806  CB  LEU A 230     5217   4729   3793   -915   -698   -701       C  
ATOM   1807  CG  LEU A 230      10.260   8.556  42.455  1.00 36.15           C  
ANISOU 1807  CG  LEU A 230     5242   4650   3844   -880   -609   -778       C  
ATOM   1808  CD1 LEU A 230       9.584   8.280  41.119  1.00 34.84           C  
ANISOU 1808  CD1 LEU A 230     5037   4455   3746   -824   -498   -693       C  
ATOM   1809  CD2 LEU A 230       9.250   8.957  43.512  1.00 36.94           C  
ANISOU 1809  CD2 LEU A 230     5431   4814   3792   -858   -585   -886       C  
ATOM   1810  N   ILE A 231      13.221   5.539  44.157  1.00 37.17           N  
ANISOU 1810  N   ILE A 231     5294   4962   3868   -989   -955   -601       N  
ATOM   1811  CA  ILE A 231      13.691   4.254  44.652  1.00 38.99           C  
ANISOU 1811  CA  ILE A 231     5524   5267   4023   -990  -1039   -515       C  
ATOM   1812  C   ILE A 231      14.364   4.389  46.022  1.00 40.73           C  
ANISOU 1812  C   ILE A 231     5794   5540   4142  -1023  -1191   -584       C  
ATOM   1813  O   ILE A 231      14.047   3.648  46.955  1.00 40.10           O  
ANISOU 1813  O   ILE A 231     5798   5551   3889  -1015  -1230   -557       O  
ATOM   1814  CB  ILE A 231      14.620   3.565  43.632  1.00 37.54           C  
ANISOU 1814  CB  ILE A 231     5226   5039   3998   -984  -1057   -414       C  
ATOM   1815  CG1 ILE A 231      13.785   3.028  42.458  1.00 36.20           C  
ANISOU 1815  CG1 ILE A 231     5037   4852   3865   -940   -917   -330       C  
ATOM   1816  CG2 ILE A 231      15.396   2.432  44.286  1.00 37.22           C  
ANISOU 1816  CG2 ILE A 231     5180   5059   3905   -984  -1183   -348       C  
ATOM   1817  CD1 ILE A 231      14.603   2.597  41.263  1.00 34.42           C  
ANISOU 1817  CD1 ILE A 231     4702   4570   3804   -929   -904   -251       C  
ATOM   1818  N   TYR A 232      15.272   5.352  46.146  1.00 39.84           N  
ANISOU 1818  N   TYR A 232     5635   5370   4133  -1064  -1275   -674       N  
ATOM   1819  CA  TYR A 232      15.981   5.573  47.404  1.00 41.53           C  
ANISOU 1819  CA  TYR A 232     5888   5630   4261  -1097  -1436   -757       C  
ATOM   1820  C   TYR A 232      15.044   5.799  48.590  1.00 43.73           C  
ANISOU 1820  C   TYR A 232     6312   5990   4315  -1087  -1428   -835       C  
ATOM   1821  O   TYR A 232      15.340   5.377  49.714  1.00 45.49           O  
ANISOU 1821  O   TYR A 232     6604   6295   4385  -1092  -1546   -848       O  
ATOM   1822  CB  TYR A 232      16.955   6.753  47.285  1.00 42.43           C  
ANISOU 1822  CB  TYR A 232     5927   5657   4540  -1151  -1510   -864       C  
ATOM   1823  CG  TYR A 232      17.586   7.136  48.607  1.00 50.55           C  
ANISOU 1823  CG  TYR A 232     7000   6731   5476  -1186  -1680   -978       C  
ATOM   1824  CD1 TYR A 232      18.632   6.391  49.143  1.00 50.67           C  
ANISOU 1824  CD1 TYR A 232     6972   6801   5479  -1193  -1846   -943       C  
ATOM   1825  CD2 TYR A 232      17.132   8.238  49.322  1.00 48.68           C  
ANISOU 1825  CD2 TYR A 232     6852   6482   5162  -1206  -1683  -1126       C  
ATOM   1826  CE1 TYR A 232      19.209   6.735  50.353  1.00 52.43           C  
ANISOU 1826  CE1 TYR A 232     7240   7073   5608  -1219  -2017  -1051       C  
ATOM   1827  CE2 TYR A 232      17.706   8.592  50.533  1.00 51.95           C  
ANISOU 1827  CE2 TYR A 232     7314   6942   5482  -1236  -1846  -1240       C  
ATOM   1828  CZ  TYR A 232      18.741   7.835  51.042  1.00 53.64           C  
ANISOU 1828  CZ  TYR A 232     7486   7217   5679  -1244  -2016  -1201       C  
ATOM   1829  OH  TYR A 232      19.313   8.181  52.243  1.00 59.74           O  
ANISOU 1829  OH  TYR A 232     8308   8040   6350  -1269  -2192  -1319       O  
ATOM   1830  N   ASN A 233      13.924   6.470  48.343  1.00 42.22           N  
ANISOU 1830  N   ASN A 233     6167   5775   4097  -1069  -1289   -888       N  
ATOM   1831  CA  ASN A 233      12.981   6.811  49.411  1.00 46.86           C  
ANISOU 1831  CA  ASN A 233     6884   6438   4483  -1057  -1258   -980       C  
ATOM   1832  C   ASN A 233      11.862   5.790  49.599  1.00 48.54           C  
ANISOU 1832  C   ASN A 233     7164   6746   4535  -1023  -1153   -890       C  
ATOM   1833  O   ASN A 233      11.047   5.914  50.516  1.00 50.22           O  
ANISOU 1833  O   ASN A 233     7481   7036   4563  -1014  -1112   -952       O  
ATOM   1834  CB  ASN A 233      12.376   8.197  49.174  1.00 42.89           C  
ANISOU 1834  CB  ASN A 233     6396   5859   4041  -1051  -1174  -1111       C  
ATOM   1835  CG  ASN A 233      13.383   9.308  49.356  1.00 45.49           C  
ANISOU 1835  CG  ASN A 233     6694   6102   4487  -1099  -1286  -1230       C  
ATOM   1836  ND2 ASN A 233      13.891   9.454  50.575  1.00 45.68           N  
ANISOU 1836  ND2 ASN A 233     6781   6185   4390  -1127  -1423  -1320       N  
ATOM   1837  OD1 ASN A 233      13.702  10.030  48.416  1.00 50.90           O  
ANISOU 1837  OD1 ASN A 233     7304   6668   5367  -1114  -1252  -1241       O  
ATOM   1838  N   ALA A 234      11.823   4.780  48.740  1.00 42.71           N  
ANISOU 1838  N   ALA A 234     6363   5998   3866  -1006  -1104   -749       N  
ATOM   1839  CA  ALA A 234      10.759   3.785  48.809  1.00 44.36           C  
ANISOU 1839  CA  ALA A 234     6623   6282   3950   -984   -997   -661       C  
ATOM   1840  C   ALA A 234      10.993   2.790  49.947  1.00 44.94           C  
ANISOU 1840  C   ALA A 234     6787   6452   3835   -997  -1085   -599       C  
ATOM   1841  O   ALA A 234      12.136   2.437  50.251  1.00 42.23           O  
ANISOU 1841  O   ALA A 234     6428   6106   3511  -1009  -1236   -566       O  
ATOM   1842  CB  ALA A 234      10.613   3.062  47.474  1.00 39.30           C  
ANISOU 1842  CB  ALA A 234     5891   5592   3451   -962   -918   -541       C  
ATOM   1843  N   THR A 235       9.906   2.352  50.577  1.00 51.43           N  
ANISOU 1843  N   THR A 235     7703   7360   4476   -994   -990   -583       N  
ATOM   1844  CA  THR A 235       9.983   1.384  51.672  1.00 56.27           C  
ANISOU 1844  CA  THR A 235     8426   8065   4889  -1007  -1051   -511       C  
ATOM   1845  C   THR A 235       9.029   0.216  51.458  1.00 62.05           C  
ANISOU 1845  C   THR A 235     9183   8835   5558  -1008   -925   -384       C  
ATOM   1846  O   THR A 235       8.136   0.271  50.614  1.00 60.13           O  
ANISOU 1846  O   THR A 235     8881   8567   5398   -997   -783   -381       O  
ATOM   1847  CB  THR A 235       9.650   2.025  53.035  1.00 56.41           C  
ANISOU 1847  CB  THR A 235     8572   8170   4691  -1019  -1069   -628       C  
ATOM   1848  CG2 THR A 235      10.691   3.073  53.415  1.00 54.61           C  
ANISOU 1848  CG2 THR A 235     8332   7907   4509  -1026  -1223   -757       C  
ATOM   1849  OG1 THR A 235       8.353   2.632  52.972  1.00 59.51           O  
ANISOU 1849  OG1 THR A 235     8981   8588   5043  -1009   -897   -710       O  
ATOM   1850  N   VAL A 236       9.222  -0.841  52.239  1.00 69.52           N  
ANISOU 1850  N   VAL A 236    10220   9837   6355  -1021   -983   -281       N  
ATOM   1851  CA  VAL A 236       8.365  -2.014  52.169  1.00 75.73           C  
ANISOU 1851  CA  VAL A 236    11046  10654   7072  -1034   -870   -155       C  
ATOM   1852  C   VAL A 236       7.315  -1.980  53.273  1.00 79.51           C  
ANISOU 1852  C   VAL A 236    11653  11241   7315  -1060   -765   -188       C  
ATOM   1853  O   VAL A 236       7.053  -2.989  53.928  1.00 85.95           O  
ANISOU 1853  O   VAL A 236    12569  12108   7978  -1085   -747    -79       O  
ATOM   1854  CB  VAL A 236       9.184  -3.309  52.281  1.00 82.22           C  
ANISOU 1854  CB  VAL A 236    11898  11457   7887  -1032   -986     -1       C  
ATOM   1855  CG1 VAL A 236      10.091  -3.463  51.070  1.00 85.74           C  
ANISOU 1855  CG1 VAL A 236    12202  11799   8575  -1004  -1056     36       C  
ATOM   1856  CG2 VAL A 236       9.999  -3.312  53.564  1.00 83.82           C  
ANISOU 1856  CG2 VAL A 236    12214  11715   7917  -1032  -1150     -8       C  
TER    1857      VAL A 236 
ATOM   1858  N   ALA A 251       9.191  -0.655  57.572  1.00 89.75           N  
ANISOU 1858  N   ALA A 251    13358  12772   7969  -1063  -1194   -413       N  
ATOM   1859  CA  ALA A 251      10.096   0.434  57.918  1.00 90.02           C  
ANISOU 1859  CA  ALA A 251    13378  12793   8031  -1051  -1352   -564       C  
ATOM   1860  C   ALA A 251      11.424   0.302  57.178  1.00 86.24           C  
ANISOU 1860  C   ALA A 251    12773  12219   7776  -1038  -1522   -523       C  
ATOM   1861  O   ALA A 251      12.322   1.127  57.343  1.00 88.00           O  
ANISOU 1861  O   ALA A 251    12957  12416   8064  -1036  -1668   -637       O  
ATOM   1862  CB  ALA A 251      10.328   0.477  59.429  1.00 90.70           C  
ANISOU 1862  CB  ALA A 251    13640  12989   7832  -1052  -1459   -607       C  
ATOM   1863  N   GLN A 252      11.538  -0.738  56.358  1.00 80.02           N  
ANISOU 1863  N   GLN A 252    11916  11376   7110  -1030  -1499   -367       N  
ATOM   1864  CA  GLN A 252      12.780  -1.028  55.651  1.00 74.89           C  
ANISOU 1864  CA  GLN A 252    11144  10644   6667  -1012  -1646   -315       C  
ATOM   1865  C   GLN A 252      12.824  -0.350  54.281  1.00 62.12           C  
ANISOU 1865  C   GLN A 252     9356   8925   5322  -1013  -1570   -368       C  
ATOM   1866  O   GLN A 252      11.819  -0.304  53.574  1.00 58.91           O  
ANISOU 1866  O   GLN A 252     8917   8497   4969  -1016  -1391   -357       O  
ATOM   1867  CB  GLN A 252      12.943  -2.542  55.491  1.00 81.95           C  
ANISOU 1867  CB  GLN A 252    12061  11527   7551   -995  -1669   -122       C  
ATOM   1868  CG  GLN A 252      14.305  -2.983  54.983  1.00 86.71           C  
ANISOU 1868  CG  GLN A 252    12554  12062   8330   -964  -1842    -64       C  
ATOM   1869  CD  GLN A 252      14.408  -4.488  54.832  1.00 89.31           C  
ANISOU 1869  CD  GLN A 252    12915  12369   8650   -939  -1860    123       C  
ATOM   1870  NE2 GLN A 252      15.627  -5.011  54.916  1.00 90.83           N  
ANISOU 1870  NE2 GLN A 252    13068  12535   8906   -899  -2051    177       N  
ATOM   1871  OE1 GLN A 252      13.403  -5.174  54.646  1.00 89.33           O  
ANISOU 1871  OE1 GLN A 252    12972  12374   8595   -954  -1705    213       O  
ATOM   1872  N   PRO A 253      13.993   0.195  53.907  1.00 54.14           N  
ANISOU 1872  N   PRO A 253     8236   7852   4483  -1011  -1706   -426       N  
ATOM   1873  CA  PRO A 253      14.152   0.715  52.546  1.00 47.61           C  
ANISOU 1873  CA  PRO A 253     7250   6922   3916  -1013  -1636   -449       C  
ATOM   1874  C   PRO A 253      13.916  -0.397  51.535  1.00 48.00           C  
ANISOU 1874  C   PRO A 253     7238   6931   4068   -992  -1548   -297       C  
ATOM   1875  O   PRO A 253      14.279  -1.544  51.790  1.00 51.50           O  
ANISOU 1875  O   PRO A 253     7715   7394   4459   -974  -1621   -177       O  
ATOM   1876  CB  PRO A 253      15.615   1.152  52.503  1.00 49.61           C  
ANISOU 1876  CB  PRO A 253     7406   7131   4312  -1020  -1819   -504       C  
ATOM   1877  CG  PRO A 253      15.953   1.465  53.944  1.00 51.58           C  
ANISOU 1877  CG  PRO A 253     7772   7463   4364  -1029  -1968   -589       C  
ATOM   1878  CD  PRO A 253      15.172   0.463  54.752  1.00 55.42           C  
ANISOU 1878  CD  PRO A 253     8414   8040   4603  -1011  -1926   -488       C  
ATOM   1879  N   LEU A 254      13.314  -0.057  50.402  1.00 46.24           N  
ANISOU 1879  N   LEU A 254     6934   6648   3987   -990  -1401   -305       N  
ATOM   1880  CA  LEU A 254      13.045  -1.035  49.356  1.00 46.79           C  
ANISOU 1880  CA  LEU A 254     6942   6676   4160   -969  -1314   -179       C  
ATOM   1881  C   LEU A 254      14.317  -1.768  48.931  1.00 43.16           C  
ANISOU 1881  C   LEU A 254     6395   6171   3833   -949  -1442    -97       C  
ATOM   1882  O   LEU A 254      14.314  -2.990  48.792  1.00 45.51           O  
ANISOU 1882  O   LEU A 254     6708   6468   4116   -928  -1446     27       O  
ATOM   1883  CB  LEU A 254      12.397  -0.349  48.152  1.00 47.91           C  
ANISOU 1883  CB  LEU A 254     6998   6756   4449   -964  -1165   -222       C  
ATOM   1884  CG  LEU A 254      11.881  -1.255  47.039  1.00 49.89           C  
ANISOU 1884  CG  LEU A 254     7196   6972   4789   -943  -1056   -114       C  
ATOM   1885  CD1 LEU A 254      11.079  -2.409  47.617  1.00 52.60           C  
ANISOU 1885  CD1 LEU A 254     7636   7377   4972   -948  -1008    -21       C  
ATOM   1886  CD2 LEU A 254      11.051  -0.447  46.046  1.00 45.99           C  
ANISOU 1886  CD2 LEU A 254     6647   6436   4393   -932   -913   -172       C  
ATOM   1887  N   VAL A 255      15.403  -1.021  48.734  1.00 41.04           N  
ANISOU 1887  N   VAL A 255     6032   5860   3700   -956  -1545   -169       N  
ATOM   1888  CA  VAL A 255      16.659  -1.607  48.260  1.00 43.33           C  
ANISOU 1888  CA  VAL A 255     6212   6108   4142   -934  -1659   -108       C  
ATOM   1889  C   VAL A 255      17.272  -2.582  49.268  1.00 46.40           C  
ANISOU 1889  C   VAL A 255     6670   6551   4410   -910  -1822    -37       C  
ATOM   1890  O   VAL A 255      17.866  -3.595  48.886  1.00 43.92           O  
ANISOU 1890  O   VAL A 255     6303   6210   4173   -872  -1877     64       O  
ATOM   1891  CB  VAL A 255      17.695  -0.529  47.874  1.00 45.23           C  
ANISOU 1891  CB  VAL A 255     6326   6297   4562   -959  -1728   -210       C  
ATOM   1892  CG1 VAL A 255      17.149   0.356  46.751  1.00 42.47           C  
ANISOU 1892  CG1 VAL A 255     5914   5878   4344   -975  -1566   -257       C  
ATOM   1893  CG2 VAL A 255      18.084   0.308  49.094  1.00 45.20           C  
ANISOU 1893  CG2 VAL A 255     6380   6338   4455   -991  -1861   -330       C  
ATOM   1894  N   ASN A 256      17.122  -2.279  50.553  1.00 48.50           N  
ANISOU 1894  N   ASN A 256     7057   6890   4480   -925  -1901    -91       N  
ATOM   1895  CA  ASN A 256      17.611  -3.167  51.601  1.00 50.44           C  
ANISOU 1895  CA  ASN A 256     7396   7192   4576   -898  -2058    -19       C  
ATOM   1896  C   ASN A 256      16.934  -4.525  51.502  1.00 52.16           C  
ANISOU 1896  C   ASN A 256     7695   7410   4712   -872  -1980    138       C  
ATOM   1897  O   ASN A 256      17.572  -5.566  51.658  1.00 56.67           O  
ANISOU 1897  O   ASN A 256     8274   7971   5285   -831  -2092    244       O  
ATOM   1898  CB  ASN A 256      17.369  -2.556  52.984  1.00 48.33           C  
ANISOU 1898  CB  ASN A 256     7271   7012   4081   -920  -2128   -108       C  
ATOM   1899  CG  ASN A 256      18.160  -1.280  53.205  1.00 53.11           C  
ANISOU 1899  CG  ASN A 256     7803   7611   4767   -948  -2238   -269       C  
ATOM   1900  ND2 ASN A 256      18.544  -0.629  52.120  1.00 53.52           N  
ANISOU 1900  ND2 ASN A 256     7697   7580   5057   -966  -2188   -321       N  
ATOM   1901  OD1 ASN A 256      18.434  -0.891  54.342  1.00 63.83           O  
ANISOU 1901  OD1 ASN A 256     9249   9033   5970   -955  -2368   -347       O  
ATOM   1902  N   ASP A 257      15.631  -4.502  51.238  1.00 52.21           N  
ANISOU 1902  N   ASP A 257     7758   7425   4656   -898  -1790    149       N  
ATOM   1903  CA  ASP A 257      14.858  -5.722  51.045  1.00 50.90           C  
ANISOU 1903  CA  ASP A 257     7658   7251   4432   -890  -1691    287       C  
ATOM   1904  C   ASP A 257      15.391  -6.514  49.851  1.00 49.68           C  
ANISOU 1904  C   ASP A 257     7380   7009   4488   -852  -1690    371       C  
ATOM   1905  O   ASP A 257      15.575  -7.726  49.937  1.00 47.18           O  
ANISOU 1905  O   ASP A 257     7106   6670   4150   -823  -1736    495       O  
ATOM   1906  CB  ASP A 257      13.380  -5.382  50.846  1.00 52.24           C  
ANISOU 1906  CB  ASP A 257     7872   7444   4534   -928  -1482    256       C  
ATOM   1907  CG  ASP A 257      12.504  -6.612  50.763  1.00 64.59           C  
ANISOU 1907  CG  ASP A 257     9508   9005   6029   -935  -1376    388       C  
ATOM   1908  OD1 ASP A 257      12.865  -7.648  51.359  1.00 72.59           O  
ANISOU 1908  OD1 ASP A 257    10607  10020   6952   -921  -1466    502       O  
ATOM   1909  OD2 ASP A 257      11.447  -6.544  50.103  1.00 68.58           O1-
ANISOU 1909  OD2 ASP A 257     9985   9500   6572   -957  -1205    378       O1-
ATOM   1910  N   TRP A 258      15.644  -5.827  48.741  1.00 45.25           N  
ANISOU 1910  N   TRP A 258     6674   6394   4125   -852  -1636    304       N  
ATOM   1911  CA  TRP A 258      16.196  -6.481  47.558  1.00 42.67           C  
ANISOU 1911  CA  TRP A 258     6225   5991   3998   -814  -1627    367       C  
ATOM   1912  C   TRP A 258      17.526  -7.156  47.884  1.00 42.01           C  
ANISOU 1912  C   TRP A 258     6104   5893   3965   -766  -1817    420       C  
ATOM   1913  O   TRP A 258      17.734  -8.333  47.582  1.00 41.83           O  
ANISOU 1913  O   TRP A 258     6080   5830   3984   -724  -1839    528       O  
ATOM   1914  CB  TRP A 258      16.389  -5.472  46.423  1.00 38.93           C  
ANISOU 1914  CB  TRP A 258     5611   5470   3712   -823  -1551    278       C  
ATOM   1915  CG  TRP A 258      15.099  -4.912  45.874  1.00 38.76           C  
ANISOU 1915  CG  TRP A 258     5607   5447   3671   -850  -1367    238       C  
ATOM   1916  CD1 TRP A 258      13.851  -5.458  45.987  1.00 37.33           C  
ANISOU 1916  CD1 TRP A 258     5517   5291   3374   -862  -1250    286       C  
ATOM   1917  CD2 TRP A 258      14.936  -3.693  45.131  1.00 36.90           C  
ANISOU 1917  CD2 TRP A 258     5296   5181   3542   -867  -1283    140       C  
ATOM   1918  CE2 TRP A 258      13.565  -3.566  44.830  1.00 39.83           C  
ANISOU 1918  CE2 TRP A 258     5716   5564   3852   -876  -1127    132       C  
ATOM   1919  CE3 TRP A 258      15.816  -2.698  44.697  1.00 36.94           C  
ANISOU 1919  CE3 TRP A 258     5198   5145   3693   -877  -1324     61       C  
ATOM   1920  NE1 TRP A 258      12.924  -4.657  45.357  1.00 37.52           N  
ANISOU 1920  NE1 TRP A 258     5516   5309   3429   -877  -1107    218       N  
ATOM   1921  CZ2 TRP A 258      13.056  -2.485  44.109  1.00 37.00           C  
ANISOU 1921  CZ2 TRP A 258     5312   5178   3568   -882  -1022     51       C  
ATOM   1922  CZ3 TRP A 258      15.310  -1.626  43.985  1.00 36.90           C  
ANISOU 1922  CZ3 TRP A 258     5158   5105   3758   -892  -1210    -12       C  
ATOM   1923  CH2 TRP A 258      13.942  -1.528  43.698  1.00 37.42           C  
ANISOU 1923  CH2 TRP A 258     5281   5183   3756   -889  -1066    -15       C  
ATOM   1924  N   LEU A 259      18.429  -6.405  48.503  1.00 43.00           N  
ANISOU 1924  N   LEU A 259     6195   6049   4094   -771  -1960    336       N  
ATOM   1925  CA  LEU A 259      19.744  -6.939  48.826  1.00 49.93           C  
ANISOU 1925  CA  LEU A 259     7016   6921   5032   -722  -2155    369       C  
ATOM   1926  C   LEU A 259      19.625  -8.157  49.732  1.00 50.63           C  
ANISOU 1926  C   LEU A 259     7252   7033   4951   -683  -2244    492       C  
ATOM   1927  O   LEU A 259      20.305  -9.158  49.525  1.00 53.17           O  
ANISOU 1927  O   LEU A 259     7537   7313   5350   -621  -2333    581       O  
ATOM   1928  CB  LEU A 259      20.625  -5.870  49.473  1.00 52.40           C  
ANISOU 1928  CB  LEU A 259     7278   7274   5358   -744  -2301    245       C  
ATOM   1929  CG  LEU A 259      21.215  -4.831  48.518  1.00 53.79           C  
ANISOU 1929  CG  LEU A 259     7274   7404   5758   -774  -2260    140       C  
ATOM   1930  CD1 LEU A 259      22.034  -3.806  49.287  1.00 55.29           C  
ANISOU 1930  CD1 LEU A 259     7426   7630   5951   -807  -2412     13       C  
ATOM   1931  CD2 LEU A 259      22.066  -5.506  47.453  1.00 50.84           C  
ANISOU 1931  CD2 LEU A 259     6744   6970   5603   -726  -2267    198       C  
ATOM   1932  N   ALA A 260      18.747  -8.070  50.725  1.00 51.68           N  
ANISOU 1932  N   ALA A 260     7555   7229   4853   -717  -2213    500       N  
ATOM   1933  CA  ALA A 260      18.594  -9.146  51.699  1.00 56.88           C  
ANISOU 1933  CA  ALA A 260     8379   7912   5321   -690  -2291    623       C  
ATOM   1934  C   ALA A 260      18.021 -10.415  51.071  1.00 54.36           C  
ANISOU 1934  C   ALA A 260     8092   7525   5039   -672  -2185    762       C  
ATOM   1935  O   ALA A 260      18.288 -11.516  51.537  1.00 52.52           O  
ANISOU 1935  O   ALA A 260     7948   7270   4740   -628  -2278    885       O  
ATOM   1936  CB  ALA A 260      17.735  -8.688  52.877  1.00 56.15           C  
ANISOU 1936  CB  ALA A 260     8460   7909   4964   -739  -2256    591       C  
ATOM   1937  N   ALA A 261      17.240 -10.260  50.007  1.00 52.74           N  
ANISOU 1937  N   ALA A 261     7819   7281   4941   -703  -1997    743       N  
ATOM   1938  CA  ALA A 261      16.663 -11.414  49.333  1.00 50.08           C  
ANISOU 1938  CA  ALA A 261     7502   6874   4652   -692  -1893    857       C  
ATOM   1939  C   ALA A 261      17.631 -12.014  48.315  1.00 48.93           C  
ANISOU 1939  C   ALA A 261     7214   6643   4732   -624  -1953    888       C  
ATOM   1940  O   ALA A 261      17.271 -12.914  47.559  1.00 49.71           O  
ANISOU 1940  O   ALA A 261     7304   6673   4910   -608  -1870    962       O  
ATOM   1941  CB  ALA A 261      15.334 -11.046  48.672  1.00 45.30           C  
ANISOU 1941  CB  ALA A 261     6891   6271   4050   -751  -1672    820       C  
ATOM   1942  N   GLY A 262      18.859 -11.511  48.292  1.00 48.49           N  
ANISOU 1942  N   GLY A 262     7043   6596   4786   -586  -2094    823       N  
ATOM   1943  CA  GLY A 262      19.879 -12.045  47.405  1.00 47.51           C  
ANISOU 1943  CA  GLY A 262     6773   6403   4876   -516  -2157    842       C  
ATOM   1944  C   GLY A 262      19.867 -11.524  45.975  1.00 44.89           C  
ANISOU 1944  C   GLY A 262     6281   6032   4743   -527  -2020    772       C  
ATOM   1945  O   GLY A 262      20.503 -12.111  45.097  1.00 45.60           O  
ANISOU 1945  O   GLY A 262     6262   6063   5003   -470  -2028    797       O  
ATOM   1946  N   TYR A 263      19.158 -10.430  45.720  1.00 43.06           N  
ANISOU 1946  N   TYR A 263     6038   5833   4490   -592  -1894    684       N  
ATOM   1947  CA  TYR A 263      19.175  -9.853  44.372  1.00 41.58           C  
ANISOU 1947  CA  TYR A 263     5710   5609   4480   -599  -1769    622       C  
ATOM   1948  C   TYR A 263      20.520  -9.201  44.085  1.00 42.08           C  
ANISOU 1948  C   TYR A 263     5613   5668   4707   -581  -1866    549       C  
ATOM   1949  O   TYR A 263      21.159  -8.657  44.983  1.00 42.36           O  
ANISOU 1949  O   TYR A 263     5647   5748   4700   -593  -2002    498       O  
ATOM   1950  CB  TYR A 263      17.976  -8.924  44.130  1.00 39.18           C  
ANISOU 1950  CB  TYR A 263     5446   5329   4111   -664  -1607    558       C  
ATOM   1951  CG  TYR A 263      16.723  -9.745  43.931  1.00 37.75           C  
ANISOU 1951  CG  TYR A 263     5364   5134   3847   -674  -1483    632       C  
ATOM   1952  CD1 TYR A 263      16.331 -10.161  42.660  1.00 36.58           C  
ANISOU 1952  CD1 TYR A 263     5155   4931   3814   -657  -1363    652       C  
ATOM   1953  CD2 TYR A 263      15.982 -10.179  45.019  1.00 41.06           C  
ANISOU 1953  CD2 TYR A 263     5937   5593   4072   -702  -1490    684       C  
ATOM   1954  CE1 TYR A 263      15.206 -10.956  42.483  1.00 35.44           C  
ANISOU 1954  CE1 TYR A 263     5091   4771   3605   -671  -1260    712       C  
ATOM   1955  CE2 TYR A 263      14.860 -10.972  44.853  1.00 37.54           C  
ANISOU 1955  CE2 TYR A 263     5571   5131   3562   -723  -1374    753       C  
ATOM   1956  CZ  TYR A 263      14.476 -11.357  43.590  1.00 36.26           C  
ANISOU 1956  CZ  TYR A 263     5337   4911   3528   -709  -1264    763       C  
ATOM   1957  OH  TYR A 263      13.356 -12.152  43.451  1.00 37.87           O  
ANISOU 1957  OH  TYR A 263     5614   5098   3677   -736  -1157    822       O  
ATOM   1958  N   GLU A 264      20.969  -9.294  42.842  1.00 38.76           N  
ANISOU 1958  N   GLU A 264     5057   5198   4473   -553  -1798    541       N  
ATOM   1959  CA  GLU A 264      22.341  -8.921  42.521  1.00 43.92           C  
ANISOU 1959  CA  GLU A 264     5544   5844   5301   -530  -1886    488       C  
ATOM   1960  C   GLU A 264      22.450  -7.937  41.362  1.00 39.83           C  
ANISOU 1960  C   GLU A 264     4902   5303   4930   -566  -1752    415       C  
ATOM   1961  O   GLU A 264      23.487  -7.302  41.177  1.00 40.21           O  
ANISOU 1961  O   GLU A 264     4812   5351   5115   -577  -1803    352       O  
ATOM   1962  CB  GLU A 264      23.172 -10.178  42.245  1.00 48.68           C  
ANISOU 1962  CB  GLU A 264     6084   6409   6006   -441  -1971    560       C  
ATOM   1963  CG  GLU A 264      23.234 -11.110  43.444  1.00 58.49           C  
ANISOU 1963  CG  GLU A 264     7450   7665   7110   -399  -2128    640       C  
ATOM   1964  CD  GLU A 264      24.201 -12.260  43.261  1.00 64.80           C  
ANISOU 1964  CD  GLU A 264     8178   8420   8024   -299  -2240    702       C  
ATOM   1965  OE1 GLU A 264      24.724 -12.752  44.283  1.00 66.62           O  
ANISOU 1965  OE1 GLU A 264     8461   8668   8184   -255  -2420    743       O  
ATOM   1966  OE2 GLU A 264      24.432 -12.677  42.104  1.00 63.32           O1-
ANISOU 1966  OE2 GLU A 264     7888   8181   7991   -259  -2151    707       O1-
ATOM   1967  N   SER A 265      21.378  -7.811  40.588  1.00 37.30           N  
ANISOU 1967  N   SER A 265     4630   4961   4583   -585  -1582    424       N  
ATOM   1968  CA  SER A 265      21.357  -6.864  39.479  1.00 36.94           C  
ANISOU 1968  CA  SER A 265     4494   4889   4652   -615  -1448    367       C  
ATOM   1969  C   SER A 265      20.092  -6.023  39.471  1.00 36.86           C  
ANISOU 1969  C   SER A 265     4582   4888   4534   -667  -1331    331       C  
ATOM   1970  O   SER A 265      19.065  -6.418  40.027  1.00 34.83           O  
ANISOU 1970  O   SER A 265     4453   4656   4126   -672  -1311    363       O  
ATOM   1971  CB  SER A 265      21.481  -7.594  38.139  1.00 38.01           C  
ANISOU 1971  CB  SER A 265     4556   4978   4908   -561  -1348    410       C  
ATOM   1972  OG  SER A 265      22.707  -8.296  38.055  1.00 46.97           O  
ANISOU 1972  OG  SER A 265     5581   6102   6165   -505  -1446    430       O  
ATOM   1973  N   ILE A 266      20.179  -4.863  38.826  1.00 34.71           N  
ANISOU 1973  N   ILE A 266     4247   4596   4347   -705  -1249    266       N  
ATOM   1974  CA  ILE A 266      19.013  -4.035  38.574  1.00 33.79           C  
ANISOU 1974  CA  ILE A 266     4206   4475   4159   -738  -1126    231       C  
ATOM   1975  C   ILE A 266      19.123  -3.447  37.175  1.00 33.03           C  
ANISOU 1975  C   ILE A 266     4027   4328   4195   -736   -997    218       C  
ATOM   1976  O   ILE A 266      20.190  -2.987  36.767  1.00 33.76           O  
ANISOU 1976  O   ILE A 266     4005   4394   4426   -751  -1012    193       O  
ATOM   1977  CB  ILE A 266      18.834  -2.937  39.648  1.00 34.49           C  
ANISOU 1977  CB  ILE A 266     4353   4591   4162   -795  -1181    150       C  
ATOM   1978  CG1 ILE A 266      17.582  -2.103  39.360  1.00 33.61           C  
ANISOU 1978  CG1 ILE A 266     4317   4471   3984   -815  -1052    110       C  
ATOM   1979  CG2 ILE A 266      20.090  -2.056  39.752  1.00 35.52           C  
ANISOU 1979  CG2 ILE A 266     4372   4700   4422   -833  -1260     82       C  
ATOM   1980  CD1 ILE A 266      17.140  -1.242  40.522  1.00 34.31           C  
ANISOU 1980  CD1 ILE A 266     4492   4593   3950   -858  -1096     32       C  
ATOM   1981  N  AVAL A 267      18.010  -3.473  36.447  0.52 31.90           N  
ANISOU 1981  N  AVAL A 267     3942   4174   4005   -719   -871    236       N  
ATOM   1982  N  BVAL A 267      18.024  -3.501  36.428  0.48 31.90           N  
ANISOU 1982  N  BVAL A 267     3940   4173   4007   -718   -871    238       N  
ATOM   1983  CA AVAL A 267      17.966  -3.026  35.065  0.52 31.20           C  
ANISOU 1983  CA AVAL A 267     3800   4040   4012   -706   -745    237       C  
ATOM   1984  CA BVAL A 267      18.001  -2.999  35.063  0.48 31.22           C  
ANISOU 1984  CA BVAL A 267     3801   4043   4019   -707   -746    236       C  
ATOM   1985  C  AVAL A 267      16.854  -1.997  34.880  0.52 30.60           C  
ANISOU 1985  C  AVAL A 267     3799   3954   3873   -725   -653    196       C  
ATOM   1986  C  BVAL A 267      16.864  -2.002  34.872  0.48 30.60           C  
ANISOU 1986  C  BVAL A 267     3799   3954   3874   -725   -653    196       C  
ATOM   1987  O  AVAL A 267      15.748  -2.176  35.388  0.52 30.23           O  
ANISOU 1987  O  AVAL A 267     3845   3940   3701   -722   -642    192       O  
ATOM   1988  O  BVAL A 267      15.756  -2.204  35.372  0.48 30.22           O  
ANISOU 1988  O  BVAL A 267     3843   3939   3701   -721   -642    194       O  
ATOM   1989  CB AVAL A 267      17.688  -4.206  34.113  0.52 31.24           C  
ANISOU 1989  CB AVAL A 267     3798   4039   4032   -644   -683    301       C  
ATOM   1990  CB BVAL A 267      17.854  -4.139  34.027  0.48 30.72           C  
ANISOU 1990  CB BVAL A 267     3716   3968   3986   -645   -682    299       C  
ATOM   1991  CG1AVAL A 267      17.514  -3.714  32.689  0.52 29.80           C  
ANISOU 1991  CG1AVAL A 267     3585   3821   3918   -625   -550    301       C  
ATOM   1992  CG2AVAL A 267      18.802  -5.246  34.201  0.52 31.38           C  
ANISOU 1992  CG2AVAL A 267     3739   4057   4128   -611   -769    340       C  
ATOM   1993  CG1BVAL A 267      19.041  -5.090  34.103  0.48 32.62           C  
ANISOU 1993  CG1BVAL A 267     3871   4209   4313   -614   -768    333       C  
ATOM   1994  CG2BVAL A 267      16.547  -4.897  34.235  0.48 29.83           C  
ANISOU 1994  CG2BVAL A 267     3710   3881   3744   -625   -656    329       C  
ATOM   1995  N   PHE A 268      17.153  -0.927  34.147  1.00 30.63           N  
ANISOU 1995  N   PHE A 268     3762   3909   3967   -745   -586    166       N  
ATOM   1996  CA  PHE A 268      16.170   0.111  33.856  1.00 30.20           C  
ANISOU 1996  CA  PHE A 268     3774   3829   3870   -751   -501    130       C  
ATOM   1997  C   PHE A 268      15.821   0.072  32.376  1.00 31.20           C  
ANISOU 1997  C   PHE A 268     3891   3923   4039   -705   -379    171       C  
ATOM   1998  O   PHE A 268      16.711   0.069  31.521  1.00 33.73           O  
ANISOU 1998  O   PHE A 268     4135   4212   4469   -701   -341    198       O  
ATOM   1999  CB  PHE A 268      16.734   1.495  34.204  1.00 31.04           C  
ANISOU 1999  CB  PHE A 268     3863   3889   4041   -810   -521     64       C  
ATOM   2000  CG  PHE A 268      16.987   1.697  35.672  1.00 34.45           C  
ANISOU 2000  CG  PHE A 268     4318   4354   4416   -854   -644      5       C  
ATOM   2001  CD1 PHE A 268      18.070   1.093  36.295  1.00 32.71           C  
ANISOU 2001  CD1 PHE A 268     4031   4163   4233   -871   -760     13       C  
ATOM   2002  CD2 PHE A 268      16.141   2.495  36.430  1.00 32.08           C  
ANISOU 2002  CD2 PHE A 268     4109   4061   4020   -871   -648    -62       C  
ATOM   2003  CE1 PHE A 268      18.303   1.283  37.647  1.00 33.66           C  
ANISOU 2003  CE1 PHE A 268     4183   4320   4286   -906   -884    -43       C  
ATOM   2004  CE2 PHE A 268      16.373   2.690  37.783  1.00 33.02           C  
ANISOU 2004  CE2 PHE A 268     4260   4216   4071   -909   -760   -123       C  
ATOM   2005  CZ  PHE A 268      17.456   2.079  38.390  1.00 33.81           C  
ANISOU 2005  CZ  PHE A 268     4302   4348   4199   -927   -882   -111       C  
ATOM   2006  N   ILE A 269      14.526   0.050  32.073  1.00 29.17           N  
ANISOU 2006  N   ILE A 269     3709   3680   3694   -668   -318    171       N  
ATOM   2007  CA  ILE A 269      14.073  -0.063  30.691  1.00 28.02           C  
ANISOU 2007  CA  ILE A 269     3567   3514   3567   -615   -217    207       C  
ATOM   2008  C   ILE A 269      13.107   1.061  30.333  1.00 30.94           C  
ANISOU 2008  C   ILE A 269     4001   3853   3902   -599   -151    174       C  
ATOM   2009  O   ILE A 269      12.392   1.573  31.195  1.00 28.81           O  
ANISOU 2009  O   ILE A 269     3784   3598   3564   -614   -176    123       O  
ATOM   2010  CB  ILE A 269      13.389  -1.425  30.425  1.00 30.56           C  
ANISOU 2010  CB  ILE A 269     3906   3881   3826   -568   -211    243       C  
ATOM   2011  CG1 ILE A 269      12.106  -1.555  31.244  1.00 30.54           C  
ANISOU 2011  CG1 ILE A 269     3976   3924   3705   -570   -227    214       C  
ATOM   2012  CG2 ILE A 269      14.338  -2.574  30.747  1.00 35.18           C  
ANISOU 2012  CG2 ILE A 269     4434   4482   4450   -571   -280    279       C  
ATOM   2013  CD1 ILE A 269      11.297  -2.803  30.913  1.00 33.88           C  
ANISOU 2013  CD1 ILE A 269     4416   4381   4075   -535   -209    245       C  
ATOM   2014  N   GLN A 270      13.082   1.429  29.056  1.00 28.25           N  
ANISOU 2014  N   GLN A 270     3660   3471   3603   -563    -66    204       N  
ATOM   2015  CA  GLN A 270      12.178   2.472  28.570  1.00 29.07           C  
ANISOU 2015  CA  GLN A 270     3830   3538   3679   -531     -7    183       C  
ATOM   2016  C   GLN A 270      10.811   1.890  28.204  1.00 26.86           C  
ANISOU 2016  C   GLN A 270     3594   3307   3306   -465     16    182       C  
ATOM   2017  O   GLN A 270      10.653   0.672  28.152  1.00 26.42           O  
ANISOU 2017  O   GLN A 270     3517   3303   3219   -450      0    203       O  
ATOM   2018  CB  GLN A 270      12.794   3.193  27.379  1.00 27.94           C  
ANISOU 2018  CB  GLN A 270     3679   3323   3615   -523     72    224       C  
ATOM   2019  CG  GLN A 270      14.153   3.822  27.703  1.00 32.67           C  
ANISOU 2019  CG  GLN A 270     4219   3869   4325   -600     59    221       C  
ATOM   2020  CD  GLN A 270      14.063   4.809  28.857  1.00 39.72           C  
ANISOU 2020  CD  GLN A 270     5140   4731   5219   -654      1    151       C  
ATOM   2021  NE2 GLN A 270      15.041   4.766  29.757  1.00 38.02           N  
ANISOU 2021  NE2 GLN A 270     4864   4521   5059   -723    -74    122       N  
ATOM   2022  OE1 GLN A 270      13.118   5.590  28.941  1.00 43.86           O  
ANISOU 2022  OE1 GLN A 270     5740   5228   5696   -628     18    117       O  
ATOM   2023  N   ASP A 271       9.837   2.757  27.938  1.00 26.86           N  
ANISOU 2023  N   ASP A 271     3651   3286   3270   -426     51    153       N  
ATOM   2024  CA  ASP A 271       8.447   2.315  27.828  1.00 26.82           C  
ANISOU 2024  CA  ASP A 271     3674   3335   3181   -370     59    130       C  
ATOM   2025  C   ASP A 271       8.054   1.551  26.552  1.00 29.03           C  
ANISOU 2025  C   ASP A 271     3950   3636   3445   -305     97    171       C  
ATOM   2026  O   ASP A 271       7.188   0.688  26.608  1.00 26.37           O  
ANISOU 2026  O   ASP A 271     3607   3358   3053   -283     85    156       O  
ATOM   2027  CB  ASP A 271       7.463   3.466  28.110  1.00 29.73           C  
ANISOU 2027  CB  ASP A 271     4095   3683   3517   -341     70     72       C  
ATOM   2028  CG  ASP A 271       7.752   4.716  27.286  1.00 36.84           C  
ANISOU 2028  CG  ASP A 271     5034   4489   4473   -313    114     89       C  
ATOM   2029  OD1 ASP A 271       8.523   4.647  26.306  1.00 33.47           O  
ANISOU 2029  OD1 ASP A 271     4598   4025   4094   -308    151    152       O  
ATOM   2030  OD2 ASP A 271       7.186   5.774  27.623  1.00 38.87           O1-
ANISOU 2030  OD2 ASP A 271     5337   4708   4725   -295    115     40       O1-
ATOM   2031  N   THR A 272       8.671   1.848  25.411  1.00 26.06           N  
ANISOU 2031  N   THR A 272     3577   3212   3112   -278    145    218       N  
ATOM   2032  CA  THR A 272       8.205   1.225  24.166  1.00 25.76           C  
ANISOU 2032  CA  THR A 272     3550   3197   3041   -206    179    245       C  
ATOM   2033  C   THR A 272       9.307   0.604  23.299  1.00 30.66           C  
ANISOU 2033  C   THR A 272     4138   3806   3706   -206    215    300       C  
ATOM   2034  O   THR A 272       9.281   0.714  22.069  1.00 32.59           O  
ANISOU 2034  O   THR A 272     4411   4036   3935   -149    268    331       O  
ATOM   2035  CB  THR A 272       7.382   2.211  23.308  1.00 31.39           C  
ANISOU 2035  CB  THR A 272     4327   3878   3721   -132    215    242       C  
ATOM   2036  CG2 THR A 272       6.202   2.776  24.107  1.00 27.06           C  
ANISOU 2036  CG2 THR A 272     3801   3347   3134   -117    183    177       C  
ATOM   2037  OG1 THR A 272       8.227   3.282  22.869  1.00 32.64           O  
ANISOU 2037  OG1 THR A 272     4515   3954   3934   -145    262    283       O  
ATOM   2038  N   ASN A 273      10.270  -0.052  23.940  1.00 27.62           N  
ANISOU 2038  N   ASN A 273     3693   3430   3371   -262    185    309       N  
ATOM   2039  CA  ASN A 273      11.322  -0.742  23.211  1.00 29.96           C  
ANISOU 2039  CA  ASN A 273     3944   3723   3719   -257    218    350       C  
ATOM   2040  C   ASN A 273      11.333  -2.229  23.550  1.00 27.03           C  
ANISOU 2040  C   ASN A 273     3534   3399   3339   -256    168    345       C  
ATOM   2041  O   ASN A 273      11.953  -2.648  24.525  1.00 25.75           O  
ANISOU 2041  O   ASN A 273     3327   3242   3213   -306    112    343       O  
ATOM   2042  CB  ASN A 273      12.688  -0.109  23.493  1.00 30.36           C  
ANISOU 2042  CB  ASN A 273     3943   3727   3864   -319    232    371       C  
ATOM   2043  CG  ASN A 273      13.816  -0.788  22.733  1.00 32.54           C  
ANISOU 2043  CG  ASN A 273     4156   4005   4203   -310    276    407       C  
ATOM   2044  ND2 ASN A 273      15.056  -0.474  23.108  1.00 28.82           N  
ANISOU 2044  ND2 ASN A 273     3612   3507   3830   -370    276    416       N  
ATOM   2045  OD1 ASN A 273      13.579  -1.578  21.814  1.00 30.79           O  
ANISOU 2045  OD1 ASN A 273     3945   3808   3945   -250    310    419       O  
ATOM   2046  N   ALA A 274      10.649  -3.025  22.735  1.00 25.37           N  
ANISOU 2046  N   ALA A 274     3343   3215   3080   -198    183    341       N  
ATOM   2047  CA  ALA A 274      10.491  -4.445  23.025  1.00 25.05           C  
ANISOU 2047  CA  ALA A 274     3280   3206   3033   -197    136    333       C  
ATOM   2048  C   ALA A 274      11.830  -5.177  22.957  1.00 27.83           C  
ANISOU 2048  C   ALA A 274     3570   3543   3462   -205    133    360       C  
ATOM   2049  O   ALA A 274      11.968  -6.279  23.484  1.00 27.81           O  
ANISOU 2049  O   ALA A 274     3545   3549   3473   -215     80    361       O  
ATOM   2050  CB  ALA A 274       9.472  -5.074  22.074  1.00 24.80           C  
ANISOU 2050  CB  ALA A 274     3281   3200   2941   -134    152    311       C  
ATOM   2051  N   GLY A 275      12.819  -4.545  22.325  1.00 28.26           N  
ANISOU 2051  N   GLY A 275     3597   3572   3571   -201    192    384       N  
ATOM   2052  CA  GLY A 275      14.124  -5.159  22.123  1.00 26.34           C  
ANISOU 2052  CA  GLY A 275     3278   3318   3411   -200    203    403       C  
ATOM   2053  C   GLY A 275      14.870  -5.465  23.414  1.00 30.14           C  
ANISOU 2053  C   GLY A 275     3700   3797   3954   -254    119    404       C  
ATOM   2054  O   GLY A 275      15.774  -6.315  23.448  1.00 30.00           O  
ANISOU 2054  O   GLY A 275     3618   3778   4003   -242     96    413       O  
ATOM   2055  N   ALA A 276      14.483  -4.787  24.488  1.00 29.49           N  
ANISOU 2055  N   ALA A 276     3643   3716   3846   -308     67    392       N  
ATOM   2056  CA  ALA A 276      15.171  -4.942  25.765  1.00 30.89           C  
ANISOU 2056  CA  ALA A 276     3776   3896   4065   -359    -23    390       C  
ATOM   2057  C   ALA A 276      15.206  -6.391  26.264  1.00 28.87           C  
ANISOU 2057  C   ALA A 276     3511   3654   3803   -341    -96    403       C  
ATOM   2058  O   ALA A 276      16.185  -6.808  26.881  1.00 27.40           O  
ANISOU 2058  O   ALA A 276     3267   3465   3680   -354   -161    414       O  
ATOM   2059  CB  ALA A 276      14.560  -4.025  26.822  1.00 30.05           C  
ANISOU 2059  CB  ALA A 276     3717   3794   3905   -412    -64    365       C  
ATOM   2060  N   THR A 277      14.144  -7.155  26.010  1.00 29.51           N  
ANISOU 2060  N   THR A 277     3649   3747   3815   -312    -90    400       N  
ATOM   2061  CA  THR A 277      14.080  -8.520  26.517  1.00 28.79           C  
ANISOU 2061  CA  THR A 277     3565   3655   3719   -303   -156    416       C  
ATOM   2062  C   THR A 277      15.095  -9.409  25.813  1.00 33.21           C  
ANISOU 2062  C   THR A 277     4063   4191   4364   -250   -149    430       C  
ATOM   2063  O   THR A 277      15.386 -10.513  26.272  1.00 31.62           O  
ANISOU 2063  O   THR A 277     3855   3973   4187   -237   -215    448       O  
ATOM   2064  CB  THR A 277      12.663  -9.134  26.387  1.00 31.66           C  
ANISOU 2064  CB  THR A 277     3999   4032   4001   -295   -145    405       C  
ATOM   2065  CG2 THR A 277      11.647  -8.297  27.136  1.00 30.91           C  
ANISOU 2065  CG2 THR A 277     3954   3967   3825   -342   -146    385       C  
ATOM   2066  OG1 THR A 277      12.291  -9.197  25.009  1.00 28.76           O  
ANISOU 2066  OG1 THR A 277     3636   3661   3629   -241    -71    385       O  
ATOM   2067  N   ILE A 278      15.630  -8.923  24.696  1.00 32.62           N  
ANISOU 2067  N   ILE A 278     3948   4113   4335   -218    -66    421       N  
ATOM   2068  CA  ILE A 278      16.686  -9.632  23.989  1.00 33.72           C  
ANISOU 2068  CA  ILE A 278     4016   4237   4561   -165    -43    424       C  
ATOM   2069  C   ILE A 278      18.077  -9.167  24.411  1.00 35.00           C  
ANISOU 2069  C   ILE A 278     4077   4396   4826   -189    -65    432       C  
ATOM   2070  O   ILE A 278      18.998  -9.979  24.513  1.00 37.21           O  
ANISOU 2070  O   ILE A 278     4286   4665   5187   -155   -105    436       O  
ATOM   2071  CB  ILE A 278      16.559  -9.479  22.468  1.00 38.24           C  
ANISOU 2071  CB  ILE A 278     4597   4813   5120   -112     70    408       C  
ATOM   2072  CG1 ILE A 278      15.162  -9.886  22.008  1.00 42.79           C  
ANISOU 2072  CG1 ILE A 278     5264   5396   5597    -87     80    389       C  
ATOM   2073  CG2 ILE A 278      17.597 -10.345  21.775  1.00 43.89           C  
ANISOU 2073  CG2 ILE A 278     5241   5517   5918    -51     99    402       C  
ATOM   2074  CD1 ILE A 278      14.923 -11.390  22.069  1.00 44.27           C  
ANISOU 2074  CD1 ILE A 278     5466   5563   5792    -53     28    379       C  
ATOM   2075  N   THR A 279      18.240  -7.870  24.661  1.00 28.33           N  
ANISOU 2075  N   THR A 279     3220   3557   3987   -245    -43    429       N  
ATOM   2076  CA  THR A 279      19.569  -7.347  24.994  1.00 29.31           C  
ANISOU 2076  CA  THR A 279     3237   3678   4223   -278    -59    428       C  
ATOM   2077  C   THR A 279      19.963  -7.600  26.448  1.00 30.82           C  
ANISOU 2077  C   THR A 279     3403   3875   4433   -313   -200    428       C  
ATOM   2078  O   THR A 279      21.132  -7.847  26.738  1.00 30.49           O  
ANISOU 2078  O   THR A 279     3257   3834   4494   -308   -250    425       O  
ATOM   2079  CB  THR A 279      19.713  -5.829  24.699  1.00 32.72           C  
ANISOU 2079  CB  THR A 279     3661   4099   4670   -334     17    422       C  
ATOM   2080  CG2 THR A 279      19.366  -5.515  23.238  1.00 32.89           C  
ANISOU 2080  CG2 THR A 279     3720   4114   4660   -295    156    432       C  
ATOM   2081  OG1 THR A 279      18.875  -5.077  25.586  1.00 30.02           O  
ANISOU 2081  OG1 THR A 279     3397   3756   4253   -386    -33    411       O  
ATOM   2082  N   ILE A 280      18.985  -7.544  27.349  1.00 29.07           N  
ANISOU 2082  N   ILE A 280     3275   3662   4109   -344   -262    430       N  
ATOM   2083  CA  ILE A 280      19.254  -7.608  28.785  1.00 29.53           C  
ANISOU 2083  CA  ILE A 280     3334   3732   4155   -382   -392    431       C  
ATOM   2084  C   ILE A 280      20.053  -8.851  29.243  1.00 30.24           C  
ANISOU 2084  C   ILE A 280     3374   3817   4301   -338   -492    455       C  
ATOM   2085  O   ILE A 280      21.047  -8.715  29.958  1.00 31.14           O  
ANISOU 2085  O   ILE A 280     3413   3939   4481   -353   -582    448       O  
ATOM   2086  CB  ILE A 280      17.953  -7.437  29.606  1.00 29.42           C  
ANISOU 2086  CB  ILE A 280     3439   3734   4004   -418   -421    430       C  
ATOM   2087  CG1 ILE A 280      17.487  -5.976  29.552  1.00 31.07           C  
ANISOU 2087  CG1 ILE A 280     3678   3946   4183   -466   -362    396       C  
ATOM   2088  CG2 ILE A 280      18.159  -7.850  31.063  1.00 29.49           C  
ANISOU 2088  CG2 ILE A 280     3471   3760   3974   -443   -555    443       C  
ATOM   2089  CD1 ILE A 280      16.088  -5.763  30.121  1.00 28.25           C  
ANISOU 2089  CD1 ILE A 280     3429   3609   3696   -488   -362    384       C  
ATOM   2090  N   PRO A 281      19.633 -10.061  28.828  1.00 32.25           N  
ANISOU 2090  N   PRO A 281     3667   4052   4533   -280   -483    478       N  
ATOM   2091  CA  PRO A 281      20.401 -11.243  29.251  1.00 32.81           C  
ANISOU 2091  CA  PRO A 281     3698   4105   4665   -229   -582    503       C  
ATOM   2092  C   PRO A 281      21.860 -11.149  28.809  1.00 32.04           C  
ANISOU 2092  C   PRO A 281     3450   4006   4715   -195   -581    483       C  
ATOM   2093  O   PRO A 281      22.759 -11.499  29.576  1.00 36.02           O  
ANISOU 2093  O   PRO A 281     3891   4513   5283   -179   -696    490       O  
ATOM   2094  CB  PRO A 281      19.711 -12.405  28.518  1.00 35.15           C  
ANISOU 2094  CB  PRO A 281     4054   4367   4935   -172   -538    518       C  
ATOM   2095  CG  PRO A 281      18.353 -11.917  28.193  1.00 36.52           C  
ANISOU 2095  CG  PRO A 281     4321   4554   5000   -210   -458    508       C  
ATOM   2096  CD  PRO A 281      18.439 -10.417  28.041  1.00 29.42           C  
ANISOU 2096  CD  PRO A 281     3393   3686   4099   -259   -399    480       C  
ATOM   2097  N   ILE A 282      22.097 -10.687  27.584  1.00 31.58           N  
ANISOU 2097  N   ILE A 282     3336   3951   4712   -182   -451    458       N  
ATOM   2098  CA  ILE A 282      23.467 -10.544  27.097  1.00 32.59           C  
ANISOU 2098  CA  ILE A 282     3312   4086   4986   -158   -424    436       C  
ATOM   2099  C   ILE A 282      24.250  -9.523  27.937  1.00 36.48           C  
ANISOU 2099  C   ILE A 282     3722   4600   5538   -229   -491    417       C  
ATOM   2100  O   ILE A 282      25.400  -9.770  28.312  1.00 35.44           O  
ANISOU 2100  O   ILE A 282     3467   4477   5521   -209   -569    403       O  
ATOM   2101  CB  ILE A 282      23.520 -10.160  25.601  1.00 32.41           C  
ANISOU 2101  CB  ILE A 282     3257   4065   4990   -140   -253    418       C  
ATOM   2102  CG1 ILE A 282      22.687 -11.131  24.753  1.00 32.21           C  
ANISOU 2102  CG1 ILE A 282     3320   4022   4897    -71   -196    423       C  
ATOM   2103  CG2 ILE A 282      24.959 -10.117  25.115  1.00 33.64           C  
ANISOU 2103  CG2 ILE A 282     3247   4233   5303   -115   -213    395       C  
ATOM   2104  CD1 ILE A 282      23.193 -12.586  24.784  1.00 32.41           C  
ANISOU 2104  CD1 ILE A 282     3308   4020   4985     17   -262    423       C  
ATOM   2105  N   SER A 283      23.626  -8.385  28.241  1.00 33.73           N  
ANISOU 2105  N   SER A 283     3438   4259   5119   -308   -466    409       N  
ATOM   2106  CA  SER A 283      24.278  -7.344  29.035  1.00 33.50           C  
ANISOU 2106  CA  SER A 283     3344   4242   5141   -383   -529    379       C  
ATOM   2107  C   SER A 283      24.647  -7.865  30.416  1.00 34.20           C  
ANISOU 2107  C   SER A 283     3428   4348   5221   -379   -713    381       C  
ATOM   2108  O   SER A 283      25.736  -7.586  30.925  1.00 36.01           O  
ANISOU 2108  O   SER A 283     3539   4592   5553   -399   -797    353       O  
ATOM   2109  CB  SER A 283      23.374  -6.112  29.181  1.00 32.77           C  
ANISOU 2109  CB  SER A 283     3348   4143   4958   -459   -478    367       C  
ATOM   2110  OG  SER A 283      23.086  -5.535  27.922  1.00 32.30           O  
ANISOU 2110  OG  SER A 283     3300   4066   4907   -461   -318    371       O  
ATOM   2111  N   LEU A 284      23.735  -8.615  31.028  1.00 33.62           N  
ANISOU 2111  N   LEU A 284     3483   4272   5021   -355   -776    416       N  
ATOM   2112  CA  LEU A 284      24.000  -9.193  32.343  1.00 37.70           C  
ANISOU 2112  CA  LEU A 284     4021   4801   5501   -344   -949    433       C  
ATOM   2113  C   LEU A 284      25.198 -10.132  32.279  1.00 37.78           C  
ANISOU 2113  C   LEU A 284     3910   4805   5640   -267  -1028    440       C  
ATOM   2114  O   LEU A 284      26.096 -10.072  33.119  1.00 38.82           O  
ANISOU 2114  O   LEU A 284     3966   4957   5828   -268  -1164    425       O  
ATOM   2115  CB  LEU A 284      22.770  -9.933  32.873  1.00 36.42           C  
ANISOU 2115  CB  LEU A 284     4024   4632   5182   -334   -975    480       C  
ATOM   2116  CG  LEU A 284      21.614  -9.048  33.348  1.00 36.48           C  
ANISOU 2116  CG  LEU A 284     4150   4660   5053   -407   -937    467       C  
ATOM   2117  CD1 LEU A 284      20.343  -9.869  33.542  1.00 33.06           C  
ANISOU 2117  CD1 LEU A 284     3856   4217   4487   -395   -919    512       C  
ATOM   2118  CD2 LEU A 284      21.993  -8.330  34.634  1.00 40.96           C  
ANISOU 2118  CD2 LEU A 284     4720   5259   5583   -461  -1059    438       C  
ATOM   2119  N   ALA A 285      25.212 -10.995  31.270  1.00 35.39           N  
ANISOU 2119  N   ALA A 285     3587   4475   5387   -195   -948    457       N  
ATOM   2120  CA  ALA A 285      26.289 -11.962  31.124  1.00 36.44           C  
ANISOU 2120  CA  ALA A 285     3605   4594   5646   -106  -1012    460       C  
ATOM   2121  C   ALA A 285      27.624 -11.236  30.967  1.00 38.50           C  
ANISOU 2121  C   ALA A 285     3676   4886   6068   -124  -1017    406       C  
ATOM   2122  O   ALA A 285      28.624 -11.594  31.594  1.00 40.03           O  
ANISOU 2122  O   ALA A 285     3766   5092   6353    -85  -1152    395       O  
ATOM   2123  CB  ALA A 285      26.027 -12.859  29.940  1.00 35.98           C  
ANISOU 2123  CB  ALA A 285     3559   4500   5612    -31   -901    470       C  
ATOM   2124  N   LEU A 286      27.628 -10.193  30.144  1.00 38.23           N  
ANISOU 2124  N   LEU A 286     3594   4862   6069   -185   -870    374       N  
ATOM   2125  CA  LEU A 286      28.848  -9.437  29.897  1.00 38.35           C  
ANISOU 2125  CA  LEU A 286     3425   4901   6245   -221   -846    324       C  
ATOM   2126  C   LEU A 286      29.258  -8.556  31.077  1.00 40.32           C  
ANISOU 2126  C   LEU A 286     3638   5175   6506   -302   -979    291       C  
ATOM   2127  O   LEU A 286      30.445  -8.328  31.291  1.00 40.58           O  
ANISOU 2127  O   LEU A 286     3502   5231   6687   -310  -1042    248       O  
ATOM   2128  CB  LEU A 286      28.726  -8.621  28.609  1.00 37.85           C  
ANISOU 2128  CB  LEU A 286     3337   4833   6212   -264   -638    311       C  
ATOM   2129  CG  LEU A 286      28.801  -9.465  27.334  1.00 37.73           C  
ANISOU 2129  CG  LEU A 286     3296   4808   6233   -175   -509    320       C  
ATOM   2130  CD1 LEU A 286      28.376  -8.668  26.106  1.00 37.07           C  
ANISOU 2130  CD1 LEU A 286     3247   4719   6121   -215   -306    322       C  
ATOM   2131  CD2 LEU A 286      30.214 -10.040  27.166  1.00 39.35           C  
ANISOU 2131  CD2 LEU A 286     3302   5031   6617   -111   -539    287       C  
ATOM   2132  N   SER A 287      28.284  -8.066  31.843  1.00 38.29           N  
ANISOU 2132  N   SER A 287     3533   4916   6099   -359  -1023    303       N  
ATOM   2133  CA  SER A 287      28.591  -7.291  33.042  1.00 39.07           C  
ANISOU 2133  CA  SER A 287     3620   5039   6187   -430  -1161    264       C  
ATOM   2134  C   SER A 287      29.318  -8.167  34.051  1.00 40.34           C  
ANISOU 2134  C   SER A 287     3734   5223   6372   -366  -1366    269       C  
ATOM   2135  O   SER A 287      30.222  -7.702  34.749  1.00 41.69           O  
ANISOU 2135  O   SER A 287     3795   5422   6624   -398  -1489    219       O  
ATOM   2136  CB  SER A 287      27.322  -6.708  33.673  1.00 39.60           C  
ANISOU 2136  CB  SER A 287     3872   5102   6071   -489  -1162    273       C  
ATOM   2137  OG  SER A 287      26.926  -5.504  33.029  1.00 37.66           O  
ANISOU 2137  OG  SER A 287     3641   4836   5831   -566  -1019    246       O  
ATOM   2138  N   ALA A 288      28.921  -9.435  34.124  1.00 40.04           N  
ANISOU 2138  N   ALA A 288     3780   5167   6265   -275  -1407    330       N  
ATOM   2139  CA  ALA A 288      29.571 -10.387  35.021  1.00 46.52           C  
ANISOU 2139  CA  ALA A 288     4575   5998   7103   -197  -1601    351       C  
ATOM   2140  C   ALA A 288      30.960 -10.775  34.514  1.00 44.87           C  
ANISOU 2140  C   ALA A 288     4148   5796   7104   -129  -1627    316       C  
ATOM   2141  O   ALA A 288      31.914 -10.842  35.283  1.00 50.14           O  
ANISOU 2141  O   ALA A 288     4710   6493   7849   -106  -1795    288       O  
ATOM   2142  CB  ALA A 288      28.704 -11.628  35.211  1.00 44.63           C  
ANISOU 2142  CB  ALA A 288     4501   5723   6735   -125  -1626    432       C  
ATOM   2143  N   GLU A 289      31.070 -11.021  33.214  1.00 44.18           N  
ANISOU 2143  N   GLU A 289     3991   5687   7107    -95  -1460    313       N  
ATOM   2144  CA  GLU A 289      32.335 -11.440  32.626  1.00 45.06           C  
ANISOU 2144  CA  GLU A 289     3893   5809   7419    -24  -1455    276       C  
ATOM   2145  C   GLU A 289      33.387 -10.343  32.725  1.00 49.23           C  
ANISOU 2145  C   GLU A 289     4227   6381   8096   -103  -1468    200       C  
ATOM   2146  O   GLU A 289      34.573 -10.623  32.885  1.00 52.67           O  
ANISOU 2146  O   GLU A 289     4477   6843   8692    -53  -1562    159       O  
ATOM   2147  CB  GLU A 289      32.139 -11.849  31.165  1.00 49.24           C  
ANISOU 2147  CB  GLU A 289     4406   6313   7991     22  -1251    282       C  
ATOM   2148  CG  GLU A 289      33.437 -12.166  30.436  1.00 57.57           C  
ANISOU 2148  CG  GLU A 289     5233   7385   9255     90  -1208    233       C  
ATOM   2149  CD  GLU A 289      33.217 -12.589  28.993  1.00 63.46           C  
ANISOU 2149  CD  GLU A 289     5979   8110  10022    140  -1003    235       C  
ATOM   2150  OE1 GLU A 289      32.105 -13.064  28.667  1.00 58.75           O  
ANISOU 2150  OE1 GLU A 289     5562   7475   9284    161   -944    280       O  
ATOM   2151  OE2 GLU A 289      34.161 -12.447  28.185  1.00 68.69           O1-
ANISOU 2151  OE2 GLU A 289     6458   8798  10841    158   -898    186       O1-
ATOM   2152  N   HIS A 290      32.949  -9.091  32.635  1.00 48.91           N  
ANISOU 2152  N   HIS A 290     4227   6344   8012   -226  -1375    178       N  
ATOM   2153  CA  HIS A 290      33.875  -7.969  32.613  1.00 48.45           C  
ANISOU 2153  CA  HIS A 290     3992   6312   8102   -320  -1360    105       C  
ATOM   2154  C   HIS A 290      33.757  -7.110  33.866  1.00 48.71           C  
ANISOU 2154  C   HIS A 290     4078   6362   8067   -409  -1512     70       C  
ATOM   2155  O   HIS A 290      34.290  -5.996  33.923  1.00 47.88           O  
ANISOU 2155  O   HIS A 290     3867   6266   8061   -513  -1495      7       O  
ATOM   2156  CB  HIS A 290      33.655  -7.134  31.353  1.00 48.41           C  
ANISOU 2156  CB  HIS A 290     3969   6287   8137   -393  -1114    100       C  
ATOM   2157  CG  HIS A 290      33.870  -7.898  30.084  1.00 48.25           C  
ANISOU 2157  CG  HIS A 290     3888   6261   8185   -308   -959    121       C  
ATOM   2158  CD2 HIS A 290      32.999  -8.325  29.139  1.00 48.19           C  
ANISOU 2158  CD2 HIS A 290     4007   6226   8077   -264   -808    168       C  
ATOM   2159  ND1 HIS A 290      35.117  -8.318  29.672  1.00 50.04           N  
ANISOU 2159  ND1 HIS A 290     3894   6515   8604   -254   -951     81       N  
ATOM   2160  CE1 HIS A 290      35.006  -8.967  28.527  1.00 51.04           C  
ANISOU 2160  CE1 HIS A 290     4022   6631   8740   -180   -794    102       C  
ATOM   2161  NE2 HIS A 290      33.730  -8.986  28.182  1.00 50.58           N  
ANISOU 2161  NE2 HIS A 290     4177   6539   8504   -185   -711    155       N  
ATOM   2162  N   SER A 291      33.057  -7.636  34.868  1.00 45.23           N  
ANISOU 2162  N   SER A 291     3806   5923   7456   -371  -1655    110       N  
ATOM   2163  CA  SER A 291      32.941  -6.972  36.162  1.00 46.23           C  
ANISOU 2163  CA  SER A 291     3998   6073   7492   -438  -1818     75       C  
ATOM   2164  C   SER A 291      32.569  -5.499  36.003  1.00 48.95           C  
ANISOU 2164  C   SER A 291     4368   6402   7827   -574  -1709     26       C  
ATOM   2165  O   SER A 291      33.308  -4.619  36.448  1.00 53.10           O  
ANISOU 2165  O   SER A 291     4779   6944   8453   -653  -1783    -52       O  
ATOM   2166  CB  SER A 291      34.259  -7.092  36.936  1.00 52.27           C  
ANISOU 2166  CB  SER A 291     4586   6883   8392   -413  -2025     17       C  
ATOM   2167  OG  SER A 291      34.709  -8.439  36.960  1.00 56.70           O  
ANISOU 2167  OG  SER A 291     5103   7448   8991   -275  -2119     61       O  
ATOM   2168  N   LEU A 292      31.430  -5.239  35.363  1.00 43.48           N  
ANISOU 2168  N   LEU A 292     3824   5674   7023   -599  -1540     68       N  
ATOM   2169  CA  LEU A 292      30.950  -3.876  35.159  1.00 44.41           C  
ANISOU 2169  CA  LEU A 292     3990   5763   7121   -713  -1430     31       C  
ATOM   2170  C   LEU A 292      29.940  -3.488  36.237  1.00 48.31           C  
ANISOU 2170  C   LEU A 292     4675   6262   7418   -748  -1515     24       C  
ATOM   2171  O   LEU A 292      28.995  -4.229  36.510  1.00 49.76           O  
ANISOU 2171  O   LEU A 292     5016   6452   7438   -691  -1527     84       O  
ATOM   2172  CB  LEU A 292      30.303  -3.730  33.779  1.00 41.55           C  
ANISOU 2172  CB  LEU A 292     3674   5360   6753   -714  -1195     76       C  
ATOM   2173  CG  LEU A 292      31.170  -4.039  32.559  1.00 42.07           C  
ANISOU 2173  CG  LEU A 292     3571   5421   6991   -682  -1067     83       C  
ATOM   2174  CD1 LEU A 292      30.355  -3.919  31.281  1.00 42.85           C  
ANISOU 2174  CD1 LEU A 292     3760   5486   7037   -675   -849    132       C  
ATOM   2175  CD2 LEU A 292      32.378  -3.121  32.515  1.00 46.80           C  
ANISOU 2175  CD2 LEU A 292     3972   6022   7786   -771  -1066     13       C  
ATOM   2176  N   ASP A 293      30.142  -2.327  36.849  1.00 45.32           N  
ANISOU 2176  N   ASP A 293     4282   5880   7058   -845  -1569    -52       N  
ATOM   2177  CA  ASP A 293      29.209  -1.839  37.857  1.00 45.53           C  
ANISOU 2177  CA  ASP A 293     4485   5913   6900   -881  -1638    -75       C  
ATOM   2178  C   ASP A 293      28.031  -1.157  37.178  1.00 41.12           C  
ANISOU 2178  C   ASP A 293     4056   5307   6260   -918  -1452    -55       C  
ATOM   2179  O   ASP A 293      26.897  -1.237  37.646  1.00 40.18           O  
ANISOU 2179  O   ASP A 293     4109   5197   5961   -904  -1449    -34       O  
ATOM   2180  CB  ASP A 293      29.913  -0.882  38.815  1.00 46.46           C  
ANISOU 2180  CB  ASP A 293     4538   6044   7071   -964  -1782   -179       C  
ATOM   2181  CG  ASP A 293      31.058  -1.543  39.547  1.00 49.96           C  
ANISOU 2181  CG  ASP A 293     4852   6541   7588   -920  -1989   -204       C  
ATOM   2182  OD1 ASP A 293      30.781  -2.292  40.503  1.00 51.87           O  
ANISOU 2182  OD1 ASP A 293     5200   6828   7680   -856  -2136   -175       O  
ATOM   2183  OD2 ASP A 293      32.229  -1.325  39.159  1.00 47.36           O1-
ANISOU 2183  OD2 ASP A 293     4317   6211   7467   -947  -2002   -249       O1-
ATOM   2184  N   MET A 294      28.322  -0.477  36.074  1.00 41.00           N  
ANISOU 2184  N   MET A 294     3954   5243   6381   -964  -1297    -62       N  
ATOM   2185  CA  MET A 294      27.289   0.067  35.207  1.00 42.03           C  
ANISOU 2185  CA  MET A 294     4195   5325   6452   -979  -1114    -29       C  
ATOM   2186  C   MET A 294      27.584  -0.284  33.756  1.00 40.56           C  
ANISOU 2186  C   MET A 294     3925   5116   6371   -946   -949     26       C  
ATOM   2187  O   MET A 294      28.722  -0.179  33.294  1.00 43.77           O  
ANISOU 2187  O   MET A 294     4163   5518   6951   -970   -927      8       O  
ATOM   2188  CB  MET A 294      27.172   1.579  35.367  1.00 40.48           C  
ANISOU 2188  CB  MET A 294     4023   5074   6285  -1083  -1079    -98       C  
ATOM   2189  CG  MET A 294      26.044   2.181  34.545  1.00 38.71           C  
ANISOU 2189  CG  MET A 294     3925   4794   5988  -1087   -907    -64       C  
ATOM   2190  SD  MET A 294      25.896   3.948  34.837  1.00 40.76           S  
ANISOU 2190  SD  MET A 294     4228   4973   6285  -1200   -882   -147       S  
ATOM   2191  CE  MET A 294      24.488   4.341  33.804  1.00 41.42           C  
ANISOU 2191  CE  MET A 294     4467   5003   6268  -1164   -693    -87       C  
ATOM   2192  N   ASN A 295      26.543  -0.693  33.042  1.00 37.72           N  
ANISOU 2192  N   ASN A 295     3683   4747   5904   -890   -833     88       N  
ATOM   2193  CA  ASN A 295      26.672  -1.173  31.679  1.00 37.27           C  
ANISOU 2193  CA  ASN A 295     3576   4677   5908   -842   -682    141       C  
ATOM   2194  C   ASN A 295      25.606  -0.525  30.801  1.00 36.12           C  
ANISOU 2194  C   ASN A 295     3552   4487   5684   -851   -522    171       C  
ATOM   2195  O   ASN A 295      24.423  -0.866  30.905  1.00 34.93           O  
ANISOU 2195  O   ASN A 295     3543   4346   5384   -807   -516    197       O  
ATOM   2196  CB  ASN A 295      26.518  -2.701  31.674  1.00 36.85           C  
ANISOU 2196  CB  ASN A 295     3539   4663   5798   -736   -732    190       C  
ATOM   2197  CG  ASN A 295      26.810  -3.324  30.320  1.00 38.91           C  
ANISOU 2197  CG  ASN A 295     3734   4919   6131   -675   -595    230       C  
ATOM   2198  ND2 ASN A 295      26.863  -4.655  30.286  1.00 38.27           N  
ANISOU 2198  ND2 ASN A 295     3647   4861   6033   -583   -642    261       N  
ATOM   2199  OD1 ASN A 295      26.985  -2.624  29.318  1.00 40.86           O  
ANISOU 2199  OD1 ASN A 295     3944   5137   6444   -710   -446    233       O  
ATOM   2200  N   PHE A 296      26.019   0.423  29.961  1.00 36.60           N  
ANISOU 2200  N   PHE A 296     3558   4500   5847   -908   -395    168       N  
ATOM   2201  CA  PHE A 296      25.123   1.082  29.007  1.00 35.75           C  
ANISOU 2201  CA  PHE A 296     3562   4344   5676   -909   -241    204       C  
ATOM   2202  C   PHE A 296      24.809   0.169  27.823  1.00 34.97           C  
ANISOU 2202  C   PHE A 296     3482   4265   5538   -820   -128    265       C  
ATOM   2203  O   PHE A 296      25.716  -0.348  27.175  1.00 35.61           O  
ANISOU 2203  O   PHE A 296     3444   4363   5721   -798    -77    279       O  
ATOM   2204  CB  PHE A 296      25.772   2.348  28.444  1.00 38.69           C  
ANISOU 2204  CB  PHE A 296     3873   4650   6178  -1001   -136    193       C  
ATOM   2205  CG  PHE A 296      25.853   3.500  29.412  1.00 41.64           C  
ANISOU 2205  CG  PHE A 296     4262   4979   6582  -1096   -218    127       C  
ATOM   2206  CD1 PHE A 296      26.879   3.576  30.345  1.00 40.69           C  
ANISOU 2206  CD1 PHE A 296     4015   4877   6569  -1155   -350     62       C  
ATOM   2207  CD2 PHE A 296      24.935   4.540  29.345  1.00 41.01           C  
ANISOU 2207  CD2 PHE A 296     4318   4833   6432  -1124   -164    123       C  
ATOM   2208  CE1 PHE A 296      26.972   4.654  31.217  1.00 42.41           C  
ANISOU 2208  CE1 PHE A 296     4248   5050   6817  -1245   -429    -12       C  
ATOM   2209  CE2 PHE A 296      25.020   5.619  30.214  1.00 43.08           C  
ANISOU 2209  CE2 PHE A 296     4597   5043   6727  -1210   -236     52       C  
ATOM   2210  CZ  PHE A 296      26.040   5.676  31.151  1.00 44.03           C  
ANISOU 2210  CZ  PHE A 296     4595   5184   6949  -1274   -368    -18       C  
ATOM   2211  N   THR A 297      23.530  -0.011  27.516  1.00 33.70           N  
ANISOU 2211  N   THR A 297     3467   4104   5234   -768    -88    294       N  
ATOM   2212  CA  THR A 297      23.157  -0.733  26.303  1.00 33.05           C  
ANISOU 2212  CA  THR A 297     3415   4035   5108   -688     23    343       C  
ATOM   2213  C   THR A 297      23.301   0.210  25.113  1.00 37.45           C  
ANISOU 2213  C   THR A 297     3978   4544   5706   -715    186    371       C  
ATOM   2214  O   THR A 297      22.675   1.277  25.077  1.00 33.26           O  
ANISOU 2214  O   THR A 297     3540   3965   5134   -753    224    373       O  
ATOM   2215  CB  THR A 297      21.707  -1.262  26.375  1.00 32.14           C  
ANISOU 2215  CB  THR A 297     3445   3938   4829   -627      3    357       C  
ATOM   2216  CG2 THR A 297      21.402  -2.186  25.200  1.00 31.18           C  
ANISOU 2216  CG2 THR A 297     3344   3834   4668   -541     91    394       C  
ATOM   2217  OG1 THR A 297      21.520  -1.983  27.597  1.00 31.51           O  
ANISOU 2217  OG1 THR A 297     3378   3893   4701   -619   -142    337       O  
ATOM   2218  N   CYS A 298      24.124  -0.176  24.141  1.00 34.06           N  
ANISOU 2218  N   CYS A 298     3457   4126   5357   -693    286    395       N  
ATOM   2219  CA  CYS A 298      24.406   0.704  23.020  1.00 34.70           C  
ANISOU 2219  CA  CYS A 298     3541   4164   5480   -726    451    431       C  
ATOM   2220  C   CYS A 298      24.133   0.072  21.667  1.00 38.48           C  
ANISOU 2220  C   CYS A 298     4062   4667   5892   -640    578    476       C  
ATOM   2221  O   CYS A 298      23.974  -1.149  21.552  1.00 33.87           O  
ANISOU 2221  O   CYS A 298     3470   4132   5265   -558    541    469       O  
ATOM   2222  CB  CYS A 298      25.859   1.180  23.064  1.00 36.29           C  
ANISOU 2222  CB  CYS A 298     3574   4351   5863   -810    485    414       C  
ATOM   2223  SG  CYS A 298      26.300   2.077  24.562  1.00 38.28           S  
ANISOU 2223  SG  CYS A 298     3769   4569   6207   -923    338    350       S  
ATOM   2224  N   ILE A 299      24.075   0.933  20.652  1.00 34.85           N  
ANISOU 2224  N   ILE A 299     3655   4165   5420   -660    725    520       N  
ATOM   2225  CA  ILE A 299      24.074   0.522  19.257  1.00 37.18           C  
ANISOU 2225  CA  ILE A 299     3979   4482   5664   -592    869    563       C  
ATOM   2226  C   ILE A 299      25.053   1.414  18.496  1.00 39.37           C  
ANISOU 2226  C   ILE A 299     4193   4723   6044   -664   1028    600       C  
ATOM   2227  O   ILE A 299      25.328   2.542  18.916  1.00 40.13           O  
ANISOU 2227  O   ILE A 299     4278   4754   6215   -764   1033    604       O  
ATOM   2228  CB  ILE A 299      22.681   0.675  18.615  1.00 36.67           C  
ANISOU 2228  CB  ILE A 299     4098   4407   5428   -524    898    595       C  
ATOM   2229  CG1 ILE A 299      22.250   2.144  18.620  1.00 37.15           C  
ANISOU 2229  CG1 ILE A 299     4254   4388   5472   -586    935    627       C  
ATOM   2230  CG2 ILE A 299      21.649  -0.202  19.325  1.00 32.79           C  
ANISOU 2230  CG2 ILE A 299     3666   3952   4839   -462    756    558       C  
ATOM   2231  CD1 ILE A 299      20.888   2.379  18.005  1.00 37.62           C  
ANISOU 2231  CD1 ILE A 299     4486   4436   5371   -512    953    656       C  
ATOM   2232  N   PRO A 300      25.580   0.921  17.366  1.00 38.51           N  
ANISOU 2232  N   PRO A 300     4274   4117   6241  -1279   1662    727       N  
ATOM   2233  CA  PRO A 300      26.424   1.787  16.540  1.00 42.66           C  
ANISOU 2233  CA  PRO A 300     4969   4457   6781  -1592   1721    877       C  
ATOM   2234  C   PRO A 300      25.572   2.918  15.995  1.00 50.10           C  
ANISOU 2234  C   PRO A 300     6240   5145   7652  -1581   1469   1021       C  
ATOM   2235  O   PRO A 300      24.462   2.675  15.521  1.00 48.60           O  
ANISOU 2235  O   PRO A 300     6176   4991   7299  -1443   1385   1074       O  
ATOM   2236  CB  PRO A 300      26.857   0.878  15.385  1.00 41.44           C  
ANISOU 2236  CB  PRO A 300     4806   4479   6462  -1806   2024    960       C  
ATOM   2237  CG  PRO A 300      26.542  -0.513  15.829  1.00 39.32           C  
ANISOU 2237  CG  PRO A 300     4303   4476   6163  -1603   2139    822       C  
ATOM   2238  CD  PRO A 300      25.380  -0.405  16.763  1.00 36.94           C  
ANISOU 2238  CD  PRO A 300     3996   4163   5876  -1277   1878    733       C  
ATOM   2239  N   ARG A 301      26.072   4.143  16.068  1.00 55.65           N  
ANISOU 2239  N   ARG A 301     7080   5585   8481  -1723   1333   1083       N  
ATOM   2240  CA  ARG A 301      25.301   5.277  15.591  1.00 64.68           C  
ANISOU 2240  CA  ARG A 301     8543   6445   9589  -1708   1055   1222       C  
ATOM   2241  C   ARG A 301      25.994   5.952  14.423  1.00 70.22           C  
ANISOU 2241  C   ARG A 301     9492   6982  10208  -2095   1117   1451       C  
ATOM   2242  O   ARG A 301      27.219   6.023  14.382  1.00 71.74           O  
ANISOU 2242  O   ARG A 301     9599   7196  10465  -2361   1300   1457       O  
ATOM   2243  CB  ARG A 301      25.076   6.283  16.720  1.00 65.52           C  
ANISOU 2243  CB  ARG A 301     8645   6332   9918  -1515    767   1097       C  
ATOM   2244  CG  ARG A 301      26.347   6.736  17.402  1.00 69.21           C  
ANISOU 2244  CG  ARG A 301     8984   6731  10584  -1682    831   1027       C  
ATOM   2245  CD  ARG A 301      26.055   7.788  18.457  1.00 73.14           C  
ANISOU 2245  CD  ARG A 301     9503   6996  11290  -1499    535    900       C  
ATOM   2246  NE  ARG A 301      25.376   8.952  17.897  1.00 76.43           N  
ANISOU 2246  NE  ARG A 301    10254   7080  11708  -1494    249   1035       N  
ATOM   2247  CZ  ARG A 301      26.003   9.976  17.328  1.00 85.99           C  
ANISOU 2247  CZ  ARG A 301    11701   8010  12962  -1773    175   1204       C  
ATOM   2248  NH1 ARG A 301      27.327   9.972  17.239  1.00 88.56           N1+
ANISOU 2248  NH1 ARG A 301    11951   8377  13322  -2086    387   1247       N1+
ATOM   2249  NH2 ARG A 301      25.309  11.000  16.844  1.00 86.45           N  
ANISOU 2249  NH2 ARG A 301    12070   7747  13031  -1746   -121   1331       N  
ATOM   2250  N   VAL A 302      25.204   6.423  13.463  1.00 77.90           N  
ANISOU 2250  N   VAL A 302    10766   7806  11027  -2139    963   1640       N  
ATOM   2251  CA  VAL A 302      25.714   7.302  12.417  1.00 90.96           C  
ANISOU 2251  CA  VAL A 302    12712   9247  12601  -2511    936   1881       C  
ATOM   2252  C   VAL A 302      25.669   8.738  12.928  1.00 93.95           C  
ANISOU 2252  C   VAL A 302    13271   9248  13178  -2477    600   1909       C  
ATOM   2253  O   VAL A 302      24.805   9.085  13.734  1.00 90.55           O  
ANISOU 2253  O   VAL A 302    12823   8701  12880  -2134    340   1785       O  
ATOM   2254  CB  VAL A 302      24.904   7.184  11.109  1.00 94.71           C  
ANISOU 2254  CB  VAL A 302    13452   9721  12811  -2605    899   2097       C  
ATOM   2255  CG1 VAL A 302      25.327   5.947  10.330  1.00 93.70           C  
ANISOU 2255  CG1 VAL A 302    13196   9933  12472  -2795   1279   2108       C  
ATOM   2256  CG2 VAL A 302      23.410   7.165  11.402  1.00 95.19           C  
ANISOU 2256  CG2 VAL A 302    13566   9737  12864  -2209    630   2049       C  
ATOM   2257  N   PRO A 303      26.608   9.577  12.466  1.00102.34           N  
ANISOU 2257  N   PRO A 303    14502  10123  14261  -2844    607   2059       N  
ATOM   2258  CA  PRO A 303      26.765  10.958  12.944  1.00105.44           C  
ANISOU 2258  CA  PRO A 303    15068  10140  14855  -2865    308   2088       C  
ATOM   2259  C   PRO A 303      25.509  11.822  12.795  1.00107.23           C  
ANISOU 2259  C   PRO A 303    15580  10050  15112  -2643   -102   2177       C  
ATOM   2260  O   PRO A 303      25.568  13.023  13.049  1.00110.40           O  
ANISOU 2260  O   PRO A 303    16170  10097  15678  -2670   -381   2221       O  
ATOM   2261  CB  PRO A 303      27.889  11.503  12.059  1.00107.77           C  
ANISOU 2261  CB  PRO A 303    15544  10343  15062  -3375    429   2298       C  
ATOM   2262  CG  PRO A 303      28.665  10.295  11.656  1.00104.61           C  
ANISOU 2262  CG  PRO A 303    14898  10335  14512  -3565    858   2250       C  
ATOM   2263  CD  PRO A 303      27.646   9.213  11.486  1.00103.27           C  
ANISOU 2263  CD  PRO A 303    14632  10398  14208  -3280    923   2190       C  
ATOM   2264  N   LYS A 304      24.394  11.218  12.401  1.00107.73           N  
ANISOU 2264  N   LYS A 304    15666  10235  15031  -2423   -146   2193       N  
ATOM   2265  CA  LYS A 304      23.148  11.949  12.200  0.69109.69           C  
ANISOU 2265  CA  LYS A 304    16160  10210  15305  -2195   -534   2269       C  
ATOM   2266  C   LYS A 304      22.004  11.319  12.993  1.00105.62           C  
ANISOU 2266  C   LYS A 304    15428   9866  14836  -1719   -611   2031       C  
ATOM   2267  O   LYS A 304      21.084  10.748  12.409  0.67105.16           O  
ANISOU 2267  O   LYS A 304    15414   9942  14602  -1599   -623   2089       O  
ATOM   2268  CB  LYS A 304      22.799  11.965  10.710  0.78113.30           C  
ANISOU 2268  CB  LYS A 304    16922  10626  15500  -2444   -558   2575       C  
ATOM   2269  CG  LYS A 304      21.581  12.797  10.346  0.94115.95           C  
ANISOU 2269  CG  LYS A 304    17548  10644  15862  -2253   -988   2700       C  
ATOM   2270  CD  LYS A 304      21.859  14.281  10.481  0.90119.14           C  
ANISOU 2270  CD  LYS A 304    18214  10581  16474  -2354  -1324   2800       C  
ATOM   2271  CE  LYS A 304      20.690  15.103   9.965  0.99122.57           C  
ANISOU 2271  CE  LYS A 304    18960  10678  16934  -2194  -1767   2954       C  
ATOM   2272  NZ  LYS A 304      20.374  14.781   8.545  1.00123.83           N1+
ANISOU 2272  NZ  LYS A 304    19356  10909  16785  -2447  -1732   3256       N1+
ATOM   2273  N   GLU A 305      22.056  11.420  14.319  1.00101.05           N  
ANISOU 2273  N   GLU A 305    14615   9300  14480  -1468   -663   1762       N  
ATOM   2274  CA  GLU A 305      21.044  10.779  15.158  1.00 95.68           C  
ANISOU 2274  CA  GLU A 305    13699   8826  13827  -1050   -711   1513       C  
ATOM   2275  C   GLU A 305      20.735  11.520  16.454  1.00 94.98           C  
ANISOU 2275  C   GLU A 305    13504   8576  14010   -760   -961   1258       C  
ATOM   2276  O   GLU A 305      21.631  12.087  17.083  1.00 94.84           O  
ANISOU 2276  O   GLU A 305    13440   8428  14168   -874   -956   1190       O  
ATOM   2277  CB  GLU A 305      21.458   9.347  15.503  1.00 88.60           C  
ANISOU 2277  CB  GLU A 305    12482   8363  12821  -1050   -341   1386       C  
ATOM   2278  CG  GLU A 305      21.498   8.400  14.325  1.00 84.61           C  
ANISOU 2278  CG  GLU A 305    12028   8080  12040  -1249    -89   1567       C  
ATOM   2279  CD  GLU A 305      21.742   6.975  14.761  1.00 76.05           C  
ANISOU 2279  CD  GLU A 305    10622   7397  10878  -1184    228   1411       C  
ATOM   2280  OE1 GLU A 305      20.950   6.462  15.580  1.00 73.87           O  
ANISOU 2280  OE1 GLU A 305    10158   7282  10625   -864    168   1213       O  
ATOM   2281  OE2 GLU A 305      22.735   6.377  14.297  1.00 71.25           O1-
ANISOU 2281  OE2 GLU A 305     9942   6939  10189  -1458    528   1478       O1-
ATOM   2282  N   PRO A 306      19.455  11.497  16.860  1.00 94.06           N  
ANISOU 2282  N   PRO A 306    13333   8486  13920   -389  -1172   1099       N  
ATOM   2283  CA  PRO A 306      18.973  12.051  18.129  1.00 93.67           C  
ANISOU 2283  CA  PRO A 306    13136   8353  14102    -72  -1394    801       C  
ATOM   2284  C   PRO A 306      19.143  11.091  19.310  1.00 85.69           C  
ANISOU 2284  C   PRO A 306    11746   7718  13096     65  -1177    527       C  
ATOM   2285  O   PRO A 306      18.251  10.990  20.154  1.00 83.46           O  
ANISOU 2285  O   PRO A 306    11294   7549  12867    382  -1303    273       O  
ATOM   2286  CB  PRO A 306      17.487  12.293  17.854  1.00 95.40           C  
ANISOU 2286  CB  PRO A 306    13455   8494  14300    237  -1682    766       C  
ATOM   2287  CG  PRO A 306      17.128  11.244  16.868  1.00 93.45           C  
ANISOU 2287  CG  PRO A 306    13236   8509  13764    158  -1490    942       C  
ATOM   2288  CD  PRO A 306      18.344  11.056  15.997  1.00 93.55           C  
ANISOU 2288  CD  PRO A 306    13379   8509  13658   -272  -1238   1211       C  
ATOM   2289  N   ILE A 307      20.269  10.388  19.363  1.00 81.14           N  
ANISOU 2289  N   ILE A 307    11033   7337  12461   -179   -861    574       N  
ATOM   2290  CA  ILE A 307      20.632   9.632  20.558  1.00 72.73           C  
ANISOU 2290  CA  ILE A 307     9625   6567  11441    -91   -691    334       C  
ATOM   2291  C   ILE A 307      22.021  10.040  21.031  1.00 66.16           C  
ANISOU 2291  C   ILE A 307     8735   5640  10765   -330   -587    330       C  
ATOM   2292  O   ILE A 307      22.889  10.384  20.223  1.00 67.42           O  
ANISOU 2292  O   ILE A 307     9063   5644  10909   -635   -500    548       O  
ATOM   2293  CB  ILE A 307      20.582   8.095  20.353  1.00 61.33           C  
ANISOU 2293  CB  ILE A 307     7994   5530   9780   -101   -399    347       C  
ATOM   2294  CG1 ILE A 307      21.402   7.680  19.130  1.00 60.57           C  
ANISOU 2294  CG1 ILE A 307     8024   5451   9539   -431   -156    616       C  
ATOM   2295  CG2 ILE A 307      19.140   7.610  20.244  1.00 63.92           C  
ANISOU 2295  CG2 ILE A 307     8306   6015   9965    179   -506    274       C  
ATOM   2296  CD1 ILE A 307      21.364   6.185  18.870  1.00 64.05           C  
ANISOU 2296  CD1 ILE A 307     8292   6262   9782   -441    125    620       C  
ATOM   2297  N   GLY A 308      22.216  10.001  22.344  1.00 57.99           N  
ANISOU 2297  N   GLY A 308     7454   4712   9866   -206   -598     79       N  
ATOM   2298  CA  GLY A 308      23.472  10.402  22.945  1.00 54.74           C  
ANISOU 2298  CA  GLY A 308     6958   4225   9614   -406   -521     43       C  
ATOM   2299  C   GLY A 308      24.607   9.428  22.701  1.00 52.57           C  
ANISOU 2299  C   GLY A 308     6531   4188   9256   -658   -184    143       C  
ATOM   2300  O   GLY A 308      24.392   8.246  22.389  1.00 46.53           O  
ANISOU 2300  O   GLY A 308     5649   3708   8323   -626      5    171       O  
ATOM   2301  N   LEU A 309      25.826   9.937  22.851  1.00 50.18           N  
ANISOU 2301  N   LEU A 309     6223   3763   9079   -907   -115    185       N  
ATOM   2302  CA  LEU A 309      27.028   9.141  22.684  1.00 49.59           C  
ANISOU 2302  CA  LEU A 309     5981   3893   8968  -1153    191    253       C  
ATOM   2303  C   LEU A 309      27.567   8.739  24.046  1.00 48.32           C  
ANISOU 2303  C   LEU A 309     5501   3922   8935  -1085    246     36       C  
ATOM   2304  O   LEU A 309      27.537   9.531  24.991  1.00 51.12           O  
ANISOU 2304  O   LEU A 309     5828   4145   9449  -1000     63   -117       O  
ATOM   2305  CB  LEU A 309      28.104   9.945  21.948  1.00 53.35           C  
ANISOU 2305  CB  LEU A 309     6641   4139   9491  -1509    244    441       C  
ATOM   2306  CG  LEU A 309      27.834  10.552  20.570  1.00 58.90           C  
ANISOU 2306  CG  LEU A 309     7697   4607  10076  -1678    174    695       C  
ATOM   2307  CD1 LEU A 309      26.733  11.604  20.618  1.00 63.50           C  
ANISOU 2307  CD1 LEU A 309     8523   4878  10725  -1471   -186    684       C  
ATOM   2308  CD2 LEU A 309      29.122  11.159  20.029  1.00 56.95           C  
ANISOU 2308  CD2 LEU A 309     7558   4218   9864  -2082    282    851       C  
ATOM   2309  N   LEU A 310      28.064   7.513  24.148  1.00 45.92           N  
ANISOU 2309  N   LEU A 310     4959   3922   8566  -1126    489     20       N  
ATOM   2310  CA  LEU A 310      28.768   7.091  25.345  1.00 45.39           C  
ANISOU 2310  CA  LEU A 310     4593   4032   8620  -1117    551   -145       C  
ATOM   2311  C   LEU A 310      30.218   7.539  25.227  1.00 46.07           C  
ANISOU 2311  C   LEU A 310     4652   4022   8832  -1422    672    -72       C  
ATOM   2312  O   LEU A 310      30.966   7.030  24.392  1.00 48.55           O  
ANISOU 2312  O   LEU A 310     4946   4415   9086  -1631    898     60       O  
ATOM   2313  CB  LEU A 310      28.711   5.576  25.509  1.00 46.64           C  
ANISOU 2313  CB  LEU A 310     4511   4534   8674  -1032    734   -186       C  
ATOM   2314  CG  LEU A 310      29.216   5.098  26.870  1.00 46.23           C  
ANISOU 2314  CG  LEU A 310     4155   4672   8737   -982    739   -362       C  
ATOM   2315  CD1 LEU A 310      28.337   5.666  27.980  1.00 44.77           C  
ANISOU 2315  CD1 LEU A 310     3952   4461   8596   -763    488   -557       C  
ATOM   2316  CD2 LEU A 310      29.258   3.588  26.931  1.00 46.68           C  
ANISOU 2316  CD2 LEU A 310     3998   5035   8703   -928    910   -371       C  
ATOM   2317  N   CYS A 311      30.613   8.486  26.067  1.00 47.45           N  
ANISOU 2317  N   CYS A 311     4814   4038   9177  -1456    526   -173       N  
ATOM   2318  CA  CYS A 311      31.936   9.091  25.970  1.00 49.51           C  
ANISOU 2318  CA  CYS A 311     5075   4178   9558  -1757    608   -106       C  
ATOM   2319  C   CYS A 311      32.701   8.973  27.282  1.00 56.96           C  
ANISOU 2319  C   CYS A 311     5734   5249  10658  -1764    614   -278       C  
ATOM   2320  O   CYS A 311      32.105   8.924  28.356  1.00 53.16           O  
ANISOU 2320  O   CYS A 311     5138   4841  10218  -1547    468   -459       O  
ATOM   2321  CB  CYS A 311      31.810  10.577  25.612  1.00 57.16           C  
ANISOU 2321  CB  CYS A 311     6359   4767  10593  -1856    402    -30       C  
ATOM   2322  SG  CYS A 311      30.996  10.959  24.043  1.00 63.70           S  
ANISOU 2322  SG  CYS A 311     7568   5382  11251  -1898    341    208       S  
ATOM   2323  N   ARG A 312      34.028   8.935  27.190  1.00 58.59           N  
ANISOU 2323  N   ARG A 312     5822   5494  10945  -2029    780   -227       N  
ATOM   2324  CA  ARG A 312      34.874   9.154  28.357  1.00 56.95           C  
ANISOU 2324  CA  ARG A 312     5396   5336  10907  -2092    750   -364       C  
ATOM   2325  C   ARG A 312      35.109  10.656  28.451  1.00 58.70           C  
ANISOU 2325  C   ARG A 312     5833   5231  11240  -2231    580   -356       C  
ATOM   2326  O   ARG A 312      35.564  11.279  27.493  1.00 58.50           O  
ANISOU 2326  O   ARG A 312     6013   5020  11194  -2469    627   -194       O  
ATOM   2327  CB  ARG A 312      36.208   8.426  28.213  1.00 54.68           C  
ANISOU 2327  CB  ARG A 312     4864   5243  10669  -2308   1000   -324       C  
ATOM   2328  CG  ARG A 312      36.944   8.226  29.525  1.00 57.05           C  
ANISOU 2328  CG  ARG A 312     4866   5687  11123  -2310    975   -476       C  
ATOM   2329  CD  ARG A 312      38.408   7.893  29.287  1.00 63.62           C  
ANISOU 2329  CD  ARG A 312     5496   6632  12044  -2573   1190   -430       C  
ATOM   2330  NE  ARG A 312      38.992   7.149  30.399  1.00 67.94           N  
ANISOU 2330  NE  ARG A 312     5700   7406  12706  -2518   1202   -555       N  
ATOM   2331  CZ  ARG A 312      40.299   7.021  30.607  1.00 68.01           C  
ANISOU 2331  CZ  ARG A 312     5484   7508  12847  -2718   1319   -568       C  
ATOM   2332  NH1 ARG A 312      41.163   7.603  29.787  1.00 63.53           N1+
ANISOU 2332  NH1 ARG A 312     4995   6840  12304  -2999   1451   -475       N1+
ATOM   2333  NH2 ARG A 312      40.743   6.320  31.642  1.00 68.74           N  
ANISOU 2333  NH2 ARG A 312     5274   7800  13045  -2649   1296   -673       N  
ATOM   2334  N   THR A 313      34.791  11.244  29.598  1.00 58.11           N  
ANISOU 2334  N   THR A 313     5718   5087  11275  -2096    376   -535       N  
ATOM   2335  CA  THR A 313      34.799  12.695  29.715  1.00 59.39           C  
ANISOU 2335  CA  THR A 313     6111   4906  11548  -2179    175   -551       C  
ATOM   2336  C   THR A 313      35.585  13.175  30.930  1.00 63.81           C  
ANISOU 2336  C   THR A 313     6497   5472  12275  -2266    114   -711       C  
ATOM   2337  O   THR A 313      35.771  12.442  31.903  1.00 62.47           O  
ANISOU 2337  O   THR A 313     6037   5569  12131  -2180    157   -850       O  
ATOM   2338  CB  THR A 313      33.361  13.267  29.769  1.00 60.87           C  
ANISOU 2338  CB  THR A 313     6508   4907  11713  -1901    -78   -632       C  
ATOM   2339  CG2 THR A 313      32.486  12.624  28.693  1.00 60.21           C  
ANISOU 2339  CG2 THR A 313     6553   4875  11450  -1781    -21   -493       C  
ATOM   2340  OG1 THR A 313      32.788  13.008  31.056  1.00 62.24           O  
ANISOU 2340  OG1 THR A 313     6477   5246  11927  -1657   -186   -883       O  
ATOM   2341  N   LYS A 314      36.049  14.415  30.852  1.00 67.81           N  
ANISOU 2341  N   LYS A 314     7195   5679  12891  -2454      3   -681       N  
ATOM   2342  CA  LYS A 314      36.799  15.036  31.928  1.00 73.61           C  
ANISOU 2342  CA  LYS A 314     7808   6378  13785  -2565    -70   -825       C  
ATOM   2343  C   LYS A 314      36.426  16.509  31.923  1.00 73.68           C  
ANISOU 2343  C   LYS A 314     8121   5978  13895  -2580   -322   -856       C  
ATOM   2344  O   LYS A 314      36.889  17.262  31.071  1.00 71.82           O  
ANISOU 2344  O   LYS A 314     8129   5487  13672  -2820   -330   -681       O  
ATOM   2345  CB  LYS A 314      38.300  14.855  31.685  1.00 81.71           C  
ANISOU 2345  CB  LYS A 314     8693   7505  14848  -2903    142   -714       C  
ATOM   2346  CG  LYS A 314      39.187  15.173  32.875  1.00 88.88           C  
ANISOU 2346  CG  LYS A 314     9389   8477  15905  -3019    111   -864       C  
ATOM   2347  CD  LYS A 314      40.543  14.479  32.758  1.00 92.98           C  
ANISOU 2347  CD  LYS A 314     9647   9237  16444  -3265    356   -789       C  
ATOM   2348  CE  LYS A 314      41.379  15.047  31.622  1.00 98.60           C  
ANISOU 2348  CE  LYS A 314    10536   9789  17139  -3605    474   -594       C  
ATOM   2349  NZ  LYS A 314      42.717  14.388  31.531  1.00 99.10           N1+
ANISOU 2349  NZ  LYS A 314    10312  10106  17235  -3840    717   -557       N1+
ATOM   2350  N   LYS A 315      35.569  16.913  32.858  1.00 75.07           N  
ANISOU 2350  N   LYS A 315     8288   6094  14141  -2330   -534  -1083       N  
ATOM   2351  CA  LYS A 315      35.037  18.276  32.869  1.00 79.69           C  
ANISOU 2351  CA  LYS A 315     9162   6274  14843  -2281   -803  -1147       C  
ATOM   2352  C   LYS A 315      36.131  19.343  32.877  1.00 81.38           C  
ANISOU 2352  C   LYS A 315     9503   6230  15190  -2606   -843  -1086       C  
ATOM   2353  O   LYS A 315      36.192  20.183  31.980  1.00 81.64           O  
ANISOU 2353  O   LYS A 315     9851   5927  15241  -2758   -934   -913       O  
ATOM   2354  CB  LYS A 315      34.092  18.489  34.054  1.00 80.70           C  
ANISOU 2354  CB  LYS A 315     9186   6433  15042  -1978   -998  -1461       C  
ATOM   2355  CG  LYS A 315      33.148  19.665  33.866  1.00 83.89           C  
ANISOU 2355  CG  LYS A 315     9889   6436  15550  -1814  -1289  -1540       C  
ATOM   2356  CD  LYS A 315      32.313  19.476  32.604  1.00 87.52           C  
ANISOU 2356  CD  LYS A 315    10578   6781  15896  -1701  -1317  -1342       C  
ATOM   2357  CE  LYS A 315      31.393  20.658  32.340  1.00 91.18           C  
ANISOU 2357  CE  LYS A 315    11347   6814  16482  -1536  -1632  -1399       C  
ATOM   2358  NZ  LYS A 315      30.632  20.493  31.065  1.00 89.09           N1+
ANISOU 2358  NZ  LYS A 315    11316   6432  16102  -1452  -1672  -1178       N1+
ATOM   2359  N   ASN A 316      36.985  19.309  33.896  1.00 83.38           N  
ANISOU 2359  N   ASN A 316     9515   6640  15527  -2725   -784  -1222       N  
ATOM   2360  CA  ASN A 316      38.100  20.245  33.999  1.00 89.70           C  
ANISOU 2360  CA  ASN A 316    10396   7240  16446  -3051   -804  -1179       C  
ATOM   2361  C   ASN A 316      39.449  19.536  33.921  1.00 91.68           C  
ANISOU 2361  C   ASN A 316    10402   7773  16658  -3336   -533  -1066       C  
ATOM   2362  O   ASN A 316      39.550  18.343  34.206  1.00 85.07           O  
ANISOU 2362  O   ASN A 316     9272   7302  15749  -3242   -366  -1096       O  
ATOM   2363  CB  ASN A 316      37.999  21.060  35.290  1.00 90.62           C  
ANISOU 2363  CB  ASN A 316    10465   7246  16722  -2976  -1003  -1456       C  
ATOM   2364  CG  ASN A 316      36.714  21.862  35.372  1.00 89.59           C  
ANISOU 2364  CG  ASN A 316    10567   6811  16663  -2697  -1284  -1602       C  
ATOM   2365  ND2 ASN A 316      36.569  22.837  34.481  1.00 88.16           N  
ANISOU 2365  ND2 ASN A 316    10749   6213  16535  -2788  -1434  -1451       N  
ATOM   2366  OD1 ASN A 316      35.861  21.609  36.225  1.00 86.84           O  
ANISOU 2366  OD1 ASN A 316    10070   6603  16323  -2409  -1371  -1851       O  
ATOM   2367  N   SER A 317      40.485  20.277  33.541  0.45 98.97           N  
ANISOU 2367  N   SER A 317    11443   8524  17636  -3686   -500   -942       N  
ATOM   2368  CA  SER A 317      41.803  19.692  33.311  1.00103.68           C  
ANISOU 2368  CA  SER A 317    11821   9372  18201  -3981   -240   -830       C  
ATOM   2369  C   SER A 317      42.304  18.821  34.468  0.89102.60           C  
ANISOU 2369  C   SER A 317    11265   9609  18108  -3911   -138   -999       C  
ATOM   2370  O   SER A 317      43.020  17.842  34.250  1.00100.79           O  
ANISOU 2370  O   SER A 317    10786   9676  17831  -4004     88   -928       O  
ATOM   2371  CB  SER A 317      42.820  20.785  32.977  1.00113.35           C  
ANISOU 2371  CB  SER A 317    13224  10350  19493  -4376   -258   -723       C  
ATOM   2372  OG  SER A 317      42.456  21.459  31.784  1.00118.54           O  
ANISOU 2372  OG  SER A 317    14267  10689  20083  -4488   -336   -521       O  
ATOM   2373  N   GLY A 318      41.918  19.170  35.692  1.00102.08           N  
ANISOU 2373  N   GLY A 318    11121   9528  18135  -3751   -313  -1228       N  
ATOM   2374  CA  GLY A 318      42.321  18.406  36.861  1.00100.48           C  
ANISOU 2374  CA  GLY A 318    10545   9669  17965  -3695   -256  -1386       C  
ATOM   2375  C   GLY A 318      41.443  17.201  37.169  1.00 99.16           C  
ANISOU 2375  C   GLY A 318    10192   9788  17697  -3378   -224  -1458       C  
ATOM   2376  O   GLY A 318      41.886  16.250  37.815  1.00 97.61           O  
ANISOU 2376  O   GLY A 318     9677   9918  17494  -3363   -126  -1506       O  
ATOM   2377  N   ASP A 319      40.198  17.237  36.705  1.00 96.29           N  
ANISOU 2377  N   ASP A 319    10030   9299  17256  -3132   -319  -1459       N  
ATOM   2378  CA  ASP A 319      39.222  16.193  37.023  1.00 93.01           C  
ANISOU 2378  CA  ASP A 319     9468   9136  16733  -2827   -315  -1544       C  
ATOM   2379  C   ASP A 319      39.628  14.797  36.553  1.00 86.63           C  
ANISOU 2379  C   ASP A 319     8445   8641  15830  -2839    -84  -1403       C  
ATOM   2380  O   ASP A 319      40.372  14.650  35.586  1.00 88.50           O  
ANISOU 2380  O   ASP A 319     8719   8854  16053  -3036     82  -1214       O  
ATOM   2381  CB  ASP A 319      37.852  16.548  36.440  1.00 95.00           C  
ANISOU 2381  CB  ASP A 319     9994   9180  16922  -2583   -453  -1552       C  
ATOM   2382  CG  ASP A 319      37.241  17.766  37.095  0.81102.19           C  
ANISOU 2382  CG  ASP A 319    11066   9819  17942  -2485   -708  -1757       C  
ATOM   2383  OD1 ASP A 319      37.518  17.998  38.291  0.96106.01           O  
ANISOU 2383  OD1 ASP A 319    11380  10395  18504  -2507   -778  -1961       O  
ATOM   2384  OD2 ASP A 319      36.485  18.491  36.417  0.99104.95           O1-
ANISOU 2384  OD2 ASP A 319    11710   9861  18305  -2388   -846  -1720       O1-
ATOM   2385  N   PRO A 320      39.140  13.764  37.253  1.00 80.25           N  
ANISOU 2385  N   PRO A 320     7407   8129  14954  -2637    -78  -1505       N  
ATOM   2386  CA  PRO A 320      39.303  12.376  36.814  1.00 77.67           C  
ANISOU 2386  CA  PRO A 320     6897   8077  14538  -2592    108  -1389       C  
ATOM   2387  C   PRO A 320      38.381  12.081  35.638  1.00 76.16           C  
ANISOU 2387  C   PRO A 320     6917   7807  14215  -2446    156  -1265       C  
ATOM   2388  O   PRO A 320      37.559  12.923  35.274  1.00 75.54           O  
ANISOU 2388  O   PRO A 320     7110   7476  14117  -2357     22  -1278       O  
ATOM   2389  CB  PRO A 320      38.854  11.572  38.036  1.00 73.17           C  
ANISOU 2389  CB  PRO A 320     6078   7796  13930  -2415     31  -1553       C  
ATOM   2390  CG  PRO A 320      37.893  12.472  38.738  1.00 72.82           C  
ANISOU 2390  CG  PRO A 320     6168   7614  13886  -2273   -186  -1752       C  
ATOM   2391  CD  PRO A 320      38.431  13.858  38.541  1.00 78.89           C  
ANISOU 2391  CD  PRO A 320     7134   8057  14785  -2459   -254  -1748       C  
ATOM   2392  N   TRP A 321      38.515  10.899  35.050  1.00 73.90           N  
ANISOU 2392  N   TRP A 321     6505   7728  13846  -2420    335  -1150       N  
ATOM   2393  CA  TRP A 321      37.644  10.508  33.952  1.00 69.71           C  
ANISOU 2393  CA  TRP A 321     6155   7157  13173  -2288    392  -1034       C  
ATOM   2394  C   TRP A 321      36.281  10.076  34.461  1.00 64.93           C  
ANISOU 2394  C   TRP A 321     5550   6659  12463  -1982    262  -1158       C  
ATOM   2395  O   TRP A 321      36.168   9.435  35.506  1.00 65.86           O  
ANISOU 2395  O   TRP A 321     5438   7011  12575  -1883    219  -1287       O  
ATOM   2396  CB  TRP A 321      38.269   9.377  33.132  1.00 68.38           C  
ANISOU 2396  CB  TRP A 321     5849   7179  12955  -2372    638   -888       C  
ATOM   2397  CG  TRP A 321      39.463   9.800  32.354  1.00 68.21           C  
ANISOU 2397  CG  TRP A 321     5858   7059  12999  -2678    791   -761       C  
ATOM   2398  CD1 TRP A 321      40.769   9.582  32.678  1.00 71.54           C  
ANISOU 2398  CD1 TRP A 321     6035   7607  13539  -2878    907   -770       C  
ATOM   2399  CD2 TRP A 321      39.469  10.527  31.120  1.00 67.58           C  
ANISOU 2399  CD2 TRP A 321     6070   6746  12862  -2838    840   -606       C  
ATOM   2400  CE2 TRP A 321      40.818  10.712  30.752  1.00 72.70           C  
ANISOU 2400  CE2 TRP A 321     6630   7409  13585  -3152   1001   -535       C  
ATOM   2401  CE3 TRP A 321      38.466  11.040  30.291  1.00 63.63           C  
ANISOU 2401  CE3 TRP A 321     5895   6031  12249  -2758    753   -518       C  
ATOM   2402  NE1 TRP A 321      41.590  10.127  31.720  1.00 74.65           N  
ANISOU 2402  NE1 TRP A 321     6538   7877  13947  -3159   1040   -645       N  
ATOM   2403  CZ2 TRP A 321      41.190  11.389  29.588  1.00 74.29           C  
ANISOU 2403  CZ2 TRP A 321     7065   7429  13734  -3409   1085   -377       C  
ATOM   2404  CZ3 TRP A 321      38.836  11.706  29.135  1.00 70.61           C  
ANISOU 2404  CZ3 TRP A 321     7021   6718  13090  -3004    819   -345       C  
ATOM   2405  CH2 TRP A 321      40.188  11.876  28.795  1.00 73.93           C  
ANISOU 2405  CH2 TRP A 321     7354   7168  13568  -3338    988   -275       C  
ATOM   2406  N   LEU A 322      35.245  10.446  33.719  1.00 63.93           N  
ANISOU 2406  N   LEU A 322     5681   6364  12246  -1846    190  -1116       N  
ATOM   2407  CA  LEU A 322      33.906   9.925  33.950  1.00 61.98           C  
ANISOU 2407  CA  LEU A 322     5439   6240  11873  -1561     99  -1211       C  
ATOM   2408  C   LEU A 322      33.373   9.360  32.642  1.00 58.69           C  
ANISOU 2408  C   LEU A 322     5171   5817  11313  -1502    213  -1036       C  
ATOM   2409  O   LEU A 322      33.575   9.944  31.579  1.00 67.08           O  
ANISOU 2409  O   LEU A 322     6459   6655  12375  -1631    251   -879       O  
ATOM   2410  CB  LEU A 322      32.976  11.025  34.466  1.00 65.66           C  
ANISOU 2410  CB  LEU A 322     6062   6506  12378  -1409   -145  -1385       C  
ATOM   2411  CG  LEU A 322      32.981  11.300  35.971  1.00 64.57           C  
ANISOU 2411  CG  LEU A 322     5741   6476  12318  -1367   -280  -1635       C  
ATOM   2412  CD1 LEU A 322      32.198  12.565  36.289  1.00 60.67           C  
ANISOU 2412  CD1 LEU A 322     5431   5723  11899  -1246   -511  -1810       C  
ATOM   2413  CD2 LEU A 322      32.413  10.109  36.731  1.00 60.10           C  
ANISOU 2413  CD2 LEU A 322     4936   6276  11624  -1210   -263  -1743       C  
ATOM   2414  N   VAL A 323      32.711   8.213  32.717  1.00 51.14           N  
ANISOU 2414  N   VAL A 323     4093   5113  10224  -1330    264  -1056       N  
ATOM   2415  CA  VAL A 323      32.055   7.641  31.549  1.00 48.71           C  
ANISOU 2415  CA  VAL A 323     3924   4819   9764  -1251    358   -913       C  
ATOM   2416  C   VAL A 323      30.563   7.931  31.625  1.00 52.28           C  
ANISOU 2416  C   VAL A 323     4520   5224  10120   -994    175  -1012       C  
ATOM   2417  O   VAL A 323      29.873   7.438  32.519  1.00 55.05           O  
ANISOU 2417  O   VAL A 323     4723   5781  10414   -819     95  -1175       O  
ATOM   2418  CB  VAL A 323      32.278   6.118  31.451  1.00 44.05           C  
ANISOU 2418  CB  VAL A 323     3120   4532   9087  -1232    542   -861       C  
ATOM   2419  CG1 VAL A 323      31.429   5.533  30.339  1.00 42.53           C  
ANISOU 2419  CG1 VAL A 323     3075   4366   8720  -1128    618   -743       C  
ATOM   2420  CG2 VAL A 323      33.756   5.808  31.228  1.00 43.75           C  
ANISOU 2420  CG2 VAL A 323     2930   4536   9158  -1475    730   -769       C  
ATOM   2421  N   ALA A 324      30.068   8.728  30.684  1.00 51.31           N  
ANISOU 2421  N   ALA A 324     4682   4837   9977   -982    102   -915       N  
ATOM   2422  CA  ALA A 324      28.669   9.133  30.697  1.00 48.07           C  
ANISOU 2422  CA  ALA A 324     4413   4347   9504   -732    -94  -1015       C  
ATOM   2423  C   ALA A 324      28.092   9.298  29.294  1.00 47.07           C  
ANISOU 2423  C   ALA A 324     4561   4050   9274   -718    -91   -822       C  
ATOM   2424  O   ALA A 324      28.823   9.319  28.302  1.00 46.60           O  
ANISOU 2424  O   ALA A 324     4617   3891   9198   -935     49   -611       O  
ATOM   2425  CB  ALA A 324      28.507  10.424  31.484  1.00 54.13           C  
ANISOU 2425  CB  ALA A 324     5246   4888  10430   -683   -325  -1194       C  
ATOM   2426  N   ASN A 325      26.768   9.403  29.231  1.00 45.40           N  
ANISOU 2426  N   ASN A 325     4442   3825   8985   -470   -247   -903       N  
ATOM   2427  CA  ASN A 325      26.056   9.732  28.003  1.00 46.41           C  
ANISOU 2427  CA  ASN A 325     4847   3761   9027   -426   -310   -740       C  
ATOM   2428  C   ASN A 325      26.181  11.233  27.713  1.00 50.87           C  
ANISOU 2428  C   ASN A 325     5673   3908   9747   -498   -512   -697       C  
ATOM   2429  O   ASN A 325      25.950  12.061  28.594  1.00 57.76           O  
ANISOU 2429  O   ASN A 325     6529   4650  10768   -388   -709   -898       O  
ATOM   2430  CB  ASN A 325      24.580   9.324  28.134  1.00 45.08           C  
ANISOU 2430  CB  ASN A 325     4657   3738   8734   -124   -425   -865       C  
ATOM   2431  CG  ASN A 325      23.739   9.755  26.945  1.00 46.36           C  
ANISOU 2431  CG  ASN A 325     5104   3689   8821    -52   -536   -713       C  
ATOM   2432  ND2 ASN A 325      22.904  10.770  27.144  1.00 51.92           N  
ANISOU 2432  ND2 ASN A 325     5937   4164   9625    134   -810   -837       N  
ATOM   2433  OD1 ASN A 325      23.831   9.177  25.865  1.00 47.06           O  
ANISOU 2433  OD1 ASN A 325     5291   3822   8767   -161   -386   -495       O  
ATOM   2434  N   VAL A 326      26.569  11.574  26.487  1.00 51.27           N  
ANISOU 2434  N   VAL A 326     5967   3752   9760   -699   -465   -440       N  
ATOM   2435  CA  VAL A 326      26.698  12.973  26.069  1.00 54.62           C  
ANISOU 2435  CA  VAL A 326     6681   3756  10315   -802   -670   -353       C  
ATOM   2436  C   VAL A 326      25.910  13.213  24.789  1.00 57.75           C  
ANISOU 2436  C   VAL A 326     7375   3970  10599   -775   -771   -149       C  
ATOM   2437  O   VAL A 326      26.083  12.495  23.805  1.00 55.01           O  
ANISOU 2437  O   VAL A 326     7075   3750  10078   -915   -579     54       O  
ATOM   2438  CB  VAL A 326      28.159  13.351  25.795  1.00 56.18           C  
ANISOU 2438  CB  VAL A 326     6922   3842  10582  -1170   -533   -204       C  
ATOM   2439  CG1 VAL A 326      28.247  14.799  25.308  1.00 59.84           C  
ANISOU 2439  CG1 VAL A 326     7718   3855  11164  -1298   -763    -91       C  
ATOM   2440  CG2 VAL A 326      29.008  13.137  27.033  1.00 56.86           C  
ANISOU 2440  CG2 VAL A 326     6715   4104  10786  -1216   -441   -390       C  
ATOM   2441  N   GLU A 327      25.047  14.221  24.793  1.00 65.35           N  
ANISOU 2441  N   GLU A 327     8534   4633  11664   -597  -1080   -207       N  
ATOM   2442  CA  GLU A 327      24.236  14.508  23.615  1.00 72.10           C  
ANISOU 2442  CA  GLU A 327     9677   5293  12424   -557  -1221    -10       C  
ATOM   2443  C   GLU A 327      25.078  14.979  22.432  1.00 77.01           C  
ANISOU 2443  C   GLU A 327    10577   5685  12998   -928  -1167    313       C  
ATOM   2444  O   GLU A 327      26.127  15.605  22.601  1.00 77.51           O  
ANISOU 2444  O   GLU A 327    10686   5591  13175  -1177  -1144    356       O  
ATOM   2445  CB  GLU A 327      23.135  15.517  23.938  1.00 79.64           C  
ANISOU 2445  CB  GLU A 327    10765   5960  13535   -264  -1593   -165       C  
ATOM   2446  CG  GLU A 327      22.237  15.081  25.084  1.00 87.01           C  
ANISOU 2446  CG  GLU A 327    11417   7146  14497     88  -1646   -507       C  
ATOM   2447  CD  GLU A 327      21.697  13.674  24.902  1.00 95.03           C  
ANISOU 2447  CD  GLU A 327    12250   8582  15276    192  -1436   -503       C  
ATOM   2448  OE1 GLU A 327      21.487  13.258  23.742  1.00 98.42           O  
ANISOU 2448  OE1 GLU A 327    12834   9026  15536    109  -1362   -259       O  
ATOM   2449  OE2 GLU A 327      21.486  12.982  25.923  1.00 96.94           O1-
ANISOU 2449  OE2 GLU A 327    12198   9143  15493    340  -1349   -742       O1-
ATOM   2450  N   TYR A 328      24.606  14.651  21.235  1.00 82.36           N  
ANISOU 2450  N   TYR A 328    11436   6367  13489   -979  -1141    538       N  
ATOM   2451  CA  TYR A 328      25.272  15.003  19.987  1.00 90.20           C  
ANISOU 2451  CA  TYR A 328    12705   7185  14381  -1350  -1084    858       C  
ATOM   2452  C   TYR A 328      25.707  16.463  19.957  1.00 92.21           C  
ANISOU 2452  C   TYR A 328    13227   6990  14819  -1516  -1338    939       C  
ATOM   2453  O   TYR A 328      26.900  16.763  19.882  1.00 88.57           O  
ANISOU 2453  O   TYR A 328    12791   6475  14387  -1850  -1210   1031       O  
ATOM   2454  CB  TYR A 328      24.333  14.713  18.818  1.00 99.49           C  
ANISOU 2454  CB  TYR A 328    14085   8357  15361  -1302  -1143   1054       C  
ATOM   2455  CG  TYR A 328      22.875  14.865  19.192  1.00106.15           C  
ANISOU 2455  CG  TYR A 328    14928   9143  16262   -879  -1420    892       C  
ATOM   2456  CD1 TYR A 328      22.201  16.060  18.974  0.54110.51           C  
ANISOU 2456  CD1 TYR A 328    15756   9280  16953   -767  -1804    936       C  
ATOM   2457  CD2 TYR A 328      22.177  13.817  19.781  0.34102.69           C  
ANISOU 2457  CD2 TYR A 328    14207   9065  15747   -594  -1307    685       C  
ATOM   2458  CE1 TYR A 328      20.870  16.203  19.322  1.00111.91           C  
ANISOU 2458  CE1 TYR A 328    15906   9416  17199   -368  -2059    760       C  
ATOM   2459  CE2 TYR A 328      20.848  13.951  20.133  0.51103.72           C  
ANISOU 2459  CE2 TYR A 328    14315   9175  15921   -220  -1549    517       C  
ATOM   2460  CZ  TYR A 328      20.198  15.145  19.901  0.87108.78           C  
ANISOU 2460  CZ  TYR A 328    15211   9412  16708   -100  -1920    545       C  
ATOM   2461  OH  TYR A 328      18.874  15.284  20.248  0.36108.46           O  
ANISOU 2461  OH  TYR A 328    15123   9360  16725    283  -2163    352       O  
ATOM   2462  N   ASN A 329      24.732  17.366  20.011  1.00 94.47           N  
ANISOU 2462  N   ASN A 329    13709   6950  15233  -1283  -1705    898       N  
ATOM   2463  CA  ASN A 329      25.018  18.797  19.997  1.00 97.53           C  
ANISOU 2463  CA  ASN A 329    14375   6864  15817  -1406  -1997    966       C  
ATOM   2464  C   ASN A 329      26.214  19.134  20.881  1.00 96.69           C  
ANISOU 2464  C   ASN A 329    14126   6752  15860  -1590  -1886    843       C  
ATOM   2465  O   ASN A 329      27.208  19.684  20.413  1.00 99.41           O  
ANISOU 2465  O   ASN A 329    14644   6924  16203  -1967  -1847   1036       O  
ATOM   2466  CB  ASN A 329      23.784  19.601  20.415  0.69 97.12           C  
ANISOU 2466  CB  ASN A 329    14424   6520  15958  -1018  -2402    797       C  
ATOM   2467  CG  ASN A 329      23.058  18.986  21.596  0.39 96.92           C  
ANISOU 2467  CG  ASN A 329    14044   6787  15995   -615  -2370    427       C  
ATOM   2468  ND2 ASN A 329      23.459  19.367  22.801  0.79 96.96           N  
ANISOU 2468  ND2 ASN A 329    13871   6775  16194   -546  -2393    162       N  
ATOM   2469  OD1 ASN A 329      22.146  18.178  21.426  0.85 97.93           O  
ANISOU 2469  OD1 ASN A 329    14061   7163  15985   -388  -2324    380       O  
ATOM   2470  N   TRP A 330      26.123  18.765  22.166  1.00  0.00           N  
ATOM   2471  CA  TRP A 330      27.230  19.004  23.087  1.00  0.00           C  
ATOM   2472  C   TRP A 330      28.512  18.402  22.561  1.00  0.00           C  
ATOM   2473  O   TRP A 330      29.550  19.078  22.541  1.00  0.00           O  
ATOM   2474  CB  TRP A 330      26.886  18.381  24.469  1.00  0.00           C  
ATOM   2475  CG  TRP A 330      25.819  19.138  25.265  1.00  0.00           C  
ATOM   2476  CD1 TRP A 330      25.293  20.405  24.938  1.00  0.00           C  
ATOM   2477  CD2 TRP A 330      25.243  18.789  26.470  1.00  0.00           C  
ATOM   2478  CE2 TRP A 330      24.376  19.841  26.857  1.00  0.00           C  
ATOM   2479  CE3 TRP A 330      25.411  17.649  27.297  1.00  0.00           C  
ATOM   2480  NE1 TRP A 330      24.389  20.860  25.917  1.00  0.00           N  
ATOM   2481  CZ2 TRP A 330      23.661  19.754  28.071  1.00  0.00           C  
ATOM   2482  CZ3 TRP A 330      24.688  17.584  28.489  1.00  0.00           C  
ATOM   2483  CH2 TRP A 330      23.824  18.620  28.870  1.00  0.00           C  
ATOM   2484  N   PHE A 331      28.471  17.141  22.135  1.00 85.09           N  
ANISOU 2484  N   PHE A 331    11925   6119  14287  -1897  -1098    633       N  
ATOM   2485  CA  PHE A 331      29.659  16.451  21.635  1.00 85.11           C  
ANISOU 2485  CA  PHE A 331    11818   6363  14156  -2246   -752    775       C  
ATOM   2486  C   PHE A 331      30.361  17.228  20.524  1.00 89.58           C  
ANISOU 2486  C   PHE A 331    12705   6671  14661  -2663   -769   1067       C  
ATOM   2487  O   PHE A 331      31.558  17.511  20.613  1.00 88.78           O  
ANISOU 2487  O   PHE A 331    12565   6563  14603  -2979   -639   1105       O  
ATOM   2488  CB  PHE A 331      29.315  15.044  21.145  1.00 84.31           C  
ANISOU 2488  CB  PHE A 331    11549   6644  13841  -2163   -498    808       C  
ATOM   2489  CG  PHE A 331      30.474  14.327  20.511  1.00 85.77           C  
ANISOU 2489  CG  PHE A 331    11626   7068  13893  -2510   -147    942       C  
ATOM   2490  CD1 PHE A 331      31.431  13.703  21.293  1.00 83.52           C  
ANISOU 2490  CD1 PHE A 331    11009   7045  13679  -2569     81    795       C  
ATOM   2491  CD2 PHE A 331      30.611  14.284  19.134  1.00 89.51           C  
ANISOU 2491  CD2 PHE A 331    12325   7510  14176  -2783    -52   1204       C  
ATOM   2492  CE1 PHE A 331      32.502  13.047  20.712  1.00 84.63           C  
ANISOU 2492  CE1 PHE A 331    11028   7407  13721  -2872    399    890       C  
ATOM   2493  CE2 PHE A 331      31.679  13.628  18.548  1.00 89.23           C  
ANISOU 2493  CE2 PHE A 331    12170   7713  14022  -3106    282   1293       C  
ATOM   2494  CZ  PHE A 331      32.625  13.009  19.339  1.00 86.76           C  
ANISOU 2494  CZ  PHE A 331    11509   7655  13801  -3139    508   1127       C  
ATOM   2495  N   ALA A 332      29.615  17.563  19.476  1.00 90.58           N  
ANISOU 2495  N   ALA A 332    13145   6597  14675  -2679   -932   1276       N  
ATOM   2496  CA  ALA A 332      30.161  18.335  18.368  0.59 91.05           C  
ANISOU 2496  CA  ALA A 332    13547   6397  14649  -3091   -985   1576       C  
ATOM   2497  C   ALA A 332      30.799  19.624  18.871  0.84 95.37           C  
ANISOU 2497  C   ALA A 332    14244   6586  15407  -3256  -1192   1562       C  
ATOM   2498  O   ALA A 332      31.965  19.899  18.590  0.96 97.06           O  
ANISOU 2498  O   ALA A 332    14497   6794  15589  -3661  -1046   1679       O  
ATOM   2499  CB  ALA A 332      29.078  18.641  17.346  0.68 89.93           C  
ANISOU 2499  CB  ALA A 332    13737   6040  14395  -3021  -1222   1783       C  
ATOM   2500  N   GLU A 333      30.033  20.407  19.623  0.40 96.10           N  
ANISOU 2500  N   GLU A 333    14410   6388  15715  -2944  -1528   1403       N  
ATOM   2501  CA  GLU A 333      30.521  21.684  20.131  0.89100.43           C  
ANISOU 2501  CA  GLU A 333    15119   6557  16481  -3067  -1761   1370       C  
ATOM   2502  C   GLU A 333      31.806  21.545  20.947  1.00100.11           C  
ANISOU 2502  C   GLU A 333    14813   6708  16515  -3269  -1520   1235       C  
ATOM   2503  O   GLU A 333      32.671  22.421  20.902  1.00101.71           O  
ANISOU 2503  O   GLU A 333    15175   6680  16792  -3592  -1580   1327       O  
ATOM   2504  CB  GLU A 333      29.443  22.400  20.952  0.95100.81           C  
ANISOU 2504  CB  GLU A 333    15215   6319  16768  -2639  -2133   1144       C  
ATOM   2505  CG  GLU A 333      28.390  23.114  20.114  0.63103.55           C  
ANISOU 2505  CG  GLU A 333    15938   6281  17126  -2527  -2496   1318       C  
ATOM   2506  CD  GLU A 333      27.108  22.317  19.977  0.70101.84           C  
ANISOU 2506  CD  GLU A 333    15611   6264  16818  -2136  -2517   1236       C  
ATOM   2507  OE1 GLU A 333      26.851  21.778  18.878  0.82101.78           O  
ANISOU 2507  OE1 GLU A 333    15721   6369  16581  -2249  -2424   1477       O  
ATOM   2508  OE2 GLU A 333      26.354  22.230  20.970  0.76 98.41           O1-
ANISOU 2508  OE2 GLU A 333    14970   5889  16533  -1728  -2623    925       O1-
ATOM   2509  N   VAL A 334      31.932  20.449  21.689  1.00 95.66           N  
ANISOU 2509  N   VAL A 334    13851   6565  15931  -3090  -1261   1024       N  
ATOM   2510  CA  VAL A 334      33.109  20.241  22.531  0.62100.14           C  
ANISOU 2510  CA  VAL A 334    14134   7337  16579  -3250  -1046    883       C  
ATOM   2511  C   VAL A 334      34.327  19.828  21.712  0.91107.24           C  
ANISOU 2511  C   VAL A 334    15001   8431  17313  -3700   -730   1084       C  
ATOM   2512  O   VAL A 334      35.464  20.147  22.065  1.00110.61           O  
ANISOU 2512  O   VAL A 334    15342   8873  17812  -3975   -627   1062       O  
ATOM   2513  CB  VAL A 334      32.852  19.196  23.633  0.96 95.84           C  
ANISOU 2513  CB  VAL A 334    13173   7171  16069  -2920   -898    598       C  
ATOM   2514  CG1 VAL A 334      34.141  18.889  24.385  1.00 90.40           C  
ANISOU 2514  CG1 VAL A 334    12189   6715  15446  -3117   -666    490       C  
ATOM   2515  CG2 VAL A 334      31.776  19.689  24.588  1.00 97.88           C  
ANISOU 2515  CG2 VAL A 334    13427   7263  16499  -2515  -1196    352       C  
ATOM   2516  N   SER A 335      34.083  19.121  20.615  1.00110.79           N  
ANISOU 2516  N   SER A 335    15513   9041  17540  -3780   -574   1265       N  
ATOM   2517  CA  SER A 335      35.157  18.688  19.731  1.00118.05           C  
ANISOU 2517  CA  SER A 335    16399  10169  18284  -4208   -263   1440       C  
ATOM   2518  C   SER A 335      35.946  19.882  19.193  0.71127.59           C  
ANISOU 2518  C   SER A 335    17914  11067  19498  -4654   -369   1639       C  
ATOM   2519  O   SER A 335      37.167  19.951  19.342  0.98128.69           O  
ANISOU 2519  O   SER A 335    17921  11321  19655  -4972   -180   1628       O  
ATOM   2520  CB  SER A 335      34.595  17.859  18.574  1.00116.64           C  
ANISOU 2520  CB  SER A 335    16292  10168  17858  -4214   -124   1602       C  
ATOM   2521  OG  SER A 335      33.936  16.699  19.051  1.00111.82           O  
ANISOU 2521  OG  SER A 335    15395   9861  17229  -3835     -9   1424       O  
ATOM   2522  N   ARG A 336      35.239  20.819  18.571  1.00135.37           N  
ANISOU 2522  N   ARG A 336    19307  11656  20470  -4680   -685   1822       N  
ATOM   2523  CA  ARG A 336      35.861  22.005  17.995  1.00144.62           C  
ANISOU 2523  CA  ARG A 336    20827  12488  21634  -5111   -836   2044       C  
ATOM   2524  C   ARG A 336      36.642  22.781  19.046  1.00151.02           C  
ANISOU 2524  C   ARG A 336    21561  13148  22673  -5188   -917   1889       C  
ATOM   2525  O   ARG A 336      37.838  23.031  18.888  1.00153.20           O  
ANISOU 2525  O   ARG A 336    21816  13483  22910  -5609   -755   1960       O  
ATOM   2526  CB  ARG A 336      34.797  22.911  17.377  1.00146.95           C  
ANISOU 2526  CB  ARG A 336    21565  12333  21937  -5027  -1241   2231       C  
ATOM   2527  CG  ARG A 336      33.876  22.200  16.408  1.00145.63           C  
ANISOU 2527  CG  ARG A 336    21485  12293  21557  -4907  -1209   2374       C  
ATOM   2528  CD  ARG A 336      32.489  22.812  16.426  1.00146.89           C  
ANISOU 2528  CD  ARG A 336    21899  12082  21830  -4539  -1632   2388       C  
ATOM   2529  NE  ARG A 336      31.527  21.984  15.705  1.00146.07           N  
ANISOU 2529  NE  ARG A 336    21802  12158  21541  -4346  -1586   2467       N  
ATOM   2530  CZ  ARG A 336      30.208  22.113  15.805  1.00145.76           C  
ANISOU 2530  CZ  ARG A 336    21857  11946  21581  -3935  -1874   2414       C  
ATOM   2531  NH1 ARG A 336      29.689  23.037  16.602  1.00147.92           N1+
ANISOU 2531  NH1 ARG A 336    22217  11859  22126  -3660  -2228   2266       N1+
ATOM   2532  NH2 ARG A 336      29.408  21.315  15.111  1.00143.24           N  
ANISOU 2532  NH2 ARG A 336    21533  11822  21070  -3798  -1805   2495       N  
ATOM   2533  N   ALA A 337      35.954  23.160  20.118  1.00154.64           N  
ANISOU 2533  N   ALA A 337    21969  13425  23363  -4787  -1164   1665       N  
ATOM   2534  CA  ALA A 337      36.558  23.945  21.188  1.00160.02           C  
ANISOU 2534  CA  ALA A 337    22589  13939  24273  -4820  -1275   1494       C  
ATOM   2535  C   ALA A 337      37.842  23.303  21.704  1.00160.49           C  
ANISOU 2535  C   ALA A 337    22274  14386  24318  -5031   -917   1379       C  
ATOM   2536  O   ALA A 337      38.719  23.988  22.231  1.00163.72           O  
ANISOU 2536  O   ALA A 337    22673  14685  24846  -5258   -942   1330       O  
ATOM   2537  CB  ALA A 337      35.565  24.142  22.325  1.00159.69           C  
ANISOU 2537  CB  ALA A 337    22453  13768  24454  -4312  -1522   1211       C  
ATOM   2538  N   LEU A 338      37.947  21.987  21.552  1.00156.58           N  
ANISOU 2538  N   LEU A 338    21469  14338  23686  -4953   -596   1333       N  
ATOM   2539  CA  LEU A 338      39.138  21.262  21.981  1.00154.59           C  
ANISOU 2539  CA  LEU A 338    20838  14471  23428  -5128   -257   1224       C  
ATOM   2540  C   LEU A 338      39.569  20.228  20.945  1.00151.41           C  
ANISOU 2540  C   LEU A 338    20317  14422  22792  -5339     87   1357       C  
ATOM   2541  O   LEU A 338      40.751  19.900  20.836  1.00149.89           O  
ANISOU 2541  O   LEU A 338    19920  14475  22556  -5650    360   1355       O  
ATOM   2542  CB  LEU A 338      38.905  20.589  23.336  1.00152.60           C  
ANISOU 2542  CB  LEU A 338    20206  14448  23329  -4730   -222    918       C  
ATOM   2543  CG  LEU A 338      38.633  21.511  24.528  1.00154.64           C  
ANISOU 2543  CG  LEU A 338    20499  14434  23823  -4537   -511    724       C  
ATOM   2544  CD1 LEU A 338      37.157  21.880  24.624  1.00154.26           C  
ANISOU 2544  CD1 LEU A 338    20658  14123  23833  -4144   -823    671       C  
ATOM   2545  CD2 LEU A 338      39.120  20.876  25.821  1.00152.73           C  
ANISOU 2545  CD2 LEU A 338    19830  14502  23698  -4387   -371    459       C  
TER    2546      LEU A 338 
ATOM   2547  N   GLY A 351      30.486   2.933   8.898  1.00119.87           N  
ANISOU 2547  N   GLY A 351    15619  14264  15663  -3963   2868   1797       N  
ATOM   2548  CA  GLY A 351      30.058   4.293   8.629  0.56122.04           C  
ANISOU 2548  CA  GLY A 351    16251  14222  15897  -4073   2564   2016       C  
ATOM   2549  C   GLY A 351      29.487   4.958   9.864  0.45119.90           C  
ANISOU 2549  C   GLY A 351    15986  13715  15855  -3718   2228   1955       C  
ATOM   2550  O   GLY A 351      28.800   5.978   9.777  1.00122.84           O  
ANISOU 2550  O   GLY A 351    16647  13806  16222  -3681   1916   2105       O  
ATOM   2551  N   PHE A 352      29.773   4.375  11.023  0.51114.22           N  
ANISOU 2551  N   PHE A 352    14943  13112  15343  -3461   2286   1727       N  
ATOM   2552  CA  PHE A 352      29.287   4.911  12.286  0.79109.10           C  
ANISOU 2552  CA  PHE A 352    14255  12288  14909  -3132   1999   1628       C  
ATOM   2553  C   PHE A 352      30.394   5.666  13.007  0.51108.01           C  
ANISOU 2553  C   PHE A 352    14021  12027  14990  -3272   1981   1567       C  
ATOM   2554  O   PHE A 352      31.571   5.525  12.677  0.61109.40           O  
ANISOU 2554  O   PHE A 352    14081  12313  15171  -3575   2226   1558       O  
ATOM   2555  CB  PHE A 352      28.775   3.786  13.186  1.00102.57           C  
ANISOU 2555  CB  PHE A 352    13145  11677  14151  -2756   2039   1420       C  
ATOM   2556  CG  PHE A 352      27.882   2.803  12.488  0.90 98.67           C  
ANISOU 2556  CG  PHE A 352    12683  11369  13439  -2649   2130   1450       C  
ATOM   2557  CD1 PHE A 352      28.324   1.519  12.218  1.00 96.32           C  
ANISOU 2557  CD1 PHE A 352    12159  11360  13078  -2692   2440   1354       C  
ATOM   2558  CD2 PHE A 352      26.598   3.157  12.109  0.39 98.49           C  
ANISOU 2558  CD2 PHE A 352    12909  11228  13283  -2500   1897   1565       C  
ATOM   2559  CE1 PHE A 352      27.504   0.604  11.583  1.00 93.28           C  
ANISOU 2559  CE1 PHE A 352    11808  11142  12491  -2601   2524   1375       C  
ATOM   2560  CE2 PHE A 352      25.773   2.248  11.470  1.00 96.69           C  
ANISOU 2560  CE2 PHE A 352    12708  11182  12846  -2412   1980   1592       C  
ATOM   2561  CZ  PHE A 352      26.227   0.969  11.207  1.00 93.80           C  
ANISOU 2561  CZ  PHE A 352    12127  11103  12408  -2469   2298   1498       C  
ATOM   2562  N   SER A 353      30.009   6.467  13.996  0.69105.19           N  
ANISOU 2562  N   SER A 353    13703  11451  14814  -3053   1692   1510       N  
ATOM   2563  CA  SER A 353      30.974   7.140  14.850  0.70103.26           C  
ANISOU 2563  CA  SER A 353    13346  11096  14791  -3141   1655   1425       C  
ATOM   2564  C   SER A 353      31.822   6.083  15.541  1.00 99.58           C  
ANISOU 2564  C   SER A 353    12480  10919  14436  -3092   1913   1225       C  
ATOM   2565  O   SER A 353      31.435   4.917  15.601  1.00 96.64           O  
ANISOU 2565  O   SER A 353    11932  10784  14004  -2903   2041   1133       O  
ATOM   2566  CB  SER A 353      30.256   7.983  15.904  0.92102.98           C  
ANISOU 2566  CB  SER A 353    13378  10819  14931  -2848   1307   1346       C  
ATOM   2567  OG  SER A 353      29.193   8.725  15.333  0.91105.79           O  
ANISOU 2567  OG  SER A 353    14068  10931  15197  -2781   1040   1498       O  
ATOM   2568  N   PRO A 354      32.992   6.480  16.055  1.00 99.06           N  
ANISOU 2568  N   PRO A 354    12272  10832  14536  -3270   1979   1160       N  
ATOM   2569  CA  PRO A 354      33.752   5.552  16.894  1.00 92.48           C  
ANISOU 2569  CA  PRO A 354    11046  10242  13850  -3179   2162    960       C  
ATOM   2570  C   PRO A 354      33.010   5.354  18.211  1.00 82.50           C  
ANISOU 2570  C   PRO A 354     9649   8977  12719  -2783   1957    804       C  
ATOM   2571  O   PRO A 354      33.203   4.350  18.897  1.00 79.87           O  
ANISOU 2571  O   PRO A 354     9021   8864  12463  -2620   2061    652       O  
ATOM   2572  CB  PRO A 354      35.068   6.299  17.140  1.00 95.46           C  
ANISOU 2572  CB  PRO A 354    11355  10544  14372  -3471   2217    949       C  
ATOM   2573  CG  PRO A 354      35.139   7.339  16.067  1.00101.87           C  
ANISOU 2573  CG  PRO A 354    12515  11144  15045  -3801   2166   1166       C  
ATOM   2574  CD  PRO A 354      33.722   7.734  15.811  1.00103.17           C  
ANISOU 2574  CD  PRO A 354    12980  11117  15104  -3590   1902   1277       C  
ATOM   2575  N   PHE A 355      32.156   6.319  18.542  1.00 74.81           N  
ANISOU 2575  N   PHE A 355     8899   7756  11771  -2639   1658    838       N  
ATOM   2576  CA  PHE A 355      31.431   6.331  19.807  1.00 63.37           C  
ANISOU 2576  CA  PHE A 355     7342   6293  10441  -2293   1443    675       C  
ATOM   2577  C   PHE A 355      30.046   5.716  19.678  1.00 55.97           C  
ANISOU 2577  C   PHE A 355     6463   5443   9362  -2001   1357    661       C  
ATOM   2578  O   PHE A 355      29.251   6.130  18.834  1.00 52.85           O  
ANISOU 2578  O   PHE A 355     6340   4911   8831  -2002   1251    800       O  
ATOM   2579  CB  PHE A 355      31.301   7.764  20.320  1.00 59.83           C  
ANISOU 2579  CB  PHE A 355     7078   5527  10127  -2289   1161    676       C  
ATOM   2580  CG  PHE A 355      32.614   8.423  20.617  1.00 58.94           C  
ANISOU 2580  CG  PHE A 355     6903   5325  10165  -2561   1216    670       C  
ATOM   2581  CD1 PHE A 355      33.515   8.692  19.601  1.00 65.95           C  
ANISOU 2581  CD1 PHE A 355     7897   6178  10983  -2936   1385    828       C  
ATOM   2582  CD2 PHE A 355      32.940   8.793  21.911  1.00 60.77           C  
ANISOU 2582  CD2 PHE A 355     6971   5524  10597  -2460   1099    503       C  
ATOM   2583  CE1 PHE A 355      34.724   9.308  19.871  1.00 69.81           C  
ANISOU 2583  CE1 PHE A 355     8323   6600  11601  -3202   1438    818       C  
ATOM   2584  CE2 PHE A 355      34.147   9.413  22.190  1.00 63.97           C  
ANISOU 2584  CE2 PHE A 355     7318   5852  11137  -2718   1145    498       C  
ATOM   2585  CZ  PHE A 355      35.040   9.670  21.168  1.00 68.57           C  
ANISOU 2585  CZ  PHE A 355     8002   6400  11652  -3087   1315    656       C  
ATOM   2586  N   PRO A 356      29.747   4.727  20.527  1.00 53.74           N  
ANISOU 2586  N   PRO A 356     5923   5389   9105  -1761   1391    500       N  
ATOM   2587  CA  PRO A 356      28.438   4.068  20.495  1.00 52.01           C  
ANISOU 2587  CA  PRO A 356     5731   5287   8744  -1490   1316    468       C  
ATOM   2588  C   PRO A 356      27.330   4.995  20.992  1.00 46.75           C  
ANISOU 2588  C   PRO A 356     5224   4430   8108  -1265    997    418       C  
ATOM   2589  O   PRO A 356      27.603   5.937  21.734  1.00 46.80           O  
ANISOU 2589  O   PRO A 356     5239   4262   8283  -1261    836    343       O  
ATOM   2590  CB  PRO A 356      28.623   2.884  21.447  1.00 51.60           C  
ANISOU 2590  CB  PRO A 356     5350   5512   8744  -1340   1418    302       C  
ATOM   2591  CG  PRO A 356      29.714   3.316  22.376  1.00 51.30           C  
ANISOU 2591  CG  PRO A 356     5139   5432   8921  -1438   1411    208       C  
ATOM   2592  CD  PRO A 356      30.633   4.165  21.560  1.00 50.23           C  
ANISOU 2592  CD  PRO A 356     5154   5112   8820  -1749   1490    345       C  
ATOM   2593  N   GLY A 357      26.099   4.733  20.563  1.00 45.83           N  
ANISOU 2593  N   GLY A 357     4923   5338   7151   -997    941    556       N  
ATOM   2594  CA  GLY A 357      24.945   5.486  21.019  1.00 43.58           C  
ANISOU 2594  CA  GLY A 357     4799   4995   6765   -995    877    554       C  
ATOM   2595  C   GLY A 357      24.192   4.717  22.088  1.00 42.60           C  
ANISOU 2595  C   GLY A 357     4705   4928   6553   -936    701    497       C  
ATOM   2596  O   GLY A 357      23.982   3.504  21.970  1.00 36.97           O  
ANISOU 2596  O   GLY A 357     3978   4292   5775   -849    667    495       O  
ATOM   2597  N   SER A 358      23.784   5.423  23.138  1.00 38.17           N  
ANISOU 2597  N   SER A 358     4190   4324   5988   -985    595    450       N  
ATOM   2598  CA  SER A 358      23.103   4.796  24.267  1.00 37.72           C  
ANISOU 2598  CA  SER A 358     4165   4320   5845   -944    434    395       C  
ATOM   2599  C   SER A 358      21.594   4.733  24.041  1.00 40.02           C  
ANISOU 2599  C   SER A 358     4621   4615   5968   -859    435    414       C  
ATOM   2600  O   SER A 358      20.971   5.743  23.719  1.00 37.23           O  
ANISOU 2600  O   SER A 358     4374   4192   5580   -867    489    432       O  
ATOM   2601  CB  SER A 358      23.419   5.559  25.556  1.00 35.89           C  
ANISOU 2601  CB  SER A 358     3901   4053   5684  -1035    316    323       C  
ATOM   2602  OG  SER A 358      22.570   5.150  26.612  1.00 41.39           O  
ANISOU 2602  OG  SER A 358     4665   4793   6267   -996    181    278       O  
ATOM   2603  N   VAL A 359      21.008   3.551  24.214  1.00 32.89           N  
ANISOU 2603  N   VAL A 359     3736   3790   4969   -779    372    409       N  
ATOM   2604  CA  VAL A 359      19.569   3.389  24.024  1.00 33.59           C  
ANISOU 2604  CA  VAL A 359     3960   3893   4909   -701    368    418       C  
ATOM   2605  C   VAL A 359      18.805   3.562  25.334  1.00 31.24           C  
ANISOU 2605  C   VAL A 359     3716   3606   4549   -715    245    359       C  
ATOM   2606  O   VAL A 359      17.584   3.495  25.358  1.00 31.99           O  
ANISOU 2606  O   VAL A 359     3909   3716   4530   -660    232    354       O  
ATOM   2607  CB  VAL A 359      19.206   2.007  23.393  1.00 33.01           C  
ANISOU 2607  CB  VAL A 359     3890   3892   4760   -608    380    442       C  
ATOM   2608  CG1 VAL A 359      19.978   1.784  22.106  1.00 36.94           C  
ANISOU 2608  CG1 VAL A 359     4338   4389   5308   -587    506    490       C  
ATOM   2609  CG2 VAL A 359      19.452   0.880  24.385  1.00 32.78           C  
ANISOU 2609  CG2 VAL A 359     3794   3923   4737   -602    258    408       C  
ATOM   2610  N   ASN A 360      19.533   3.785  26.421  1.00 35.98           N  
ANISOU 2610  N   ASN A 360     4246   4203   5223   -787    154    311       N  
ATOM   2611  CA  ASN A 360      18.932   3.982  27.739  1.00 34.98           C  
ANISOU 2611  CA  ASN A 360     4168   4091   5031   -806     38    250       C  
ATOM   2612  C   ASN A 360      18.251   2.733  28.297  1.00 36.73           C  
ANISOU 2612  C   ASN A 360     4416   4398   5144   -748    -39    246       C  
ATOM   2613  O   ASN A 360      17.196   2.811  28.920  1.00 33.27           O  
ANISOU 2613  O   ASN A 360     4062   3978   4600   -729    -79    217       O  
ATOM   2614  CB  ASN A 360      17.982   5.193  27.763  1.00 36.16           C  
ANISOU 2614  CB  ASN A 360     4432   4177   5131   -810     70    227       C  
ATOM   2615  CG  ASN A 360      18.143   6.040  29.029  1.00 46.10           C  
ANISOU 2615  CG  ASN A 360     5696   5405   6414   -882    -21    148       C  
ATOM   2616  ND2 ASN A 360      17.362   7.115  29.140  1.00 43.88           N  
ANISOU 2616  ND2 ASN A 360     5511   5060   6100   -882      0    116       N  
ATOM   2617  OD1 ASN A 360      18.974   5.738  29.883  1.00 51.23           O  
ANISOU 2617  OD1 ASN A 360     6266   6086   7114   -932   -114    112       O  
ATOM   2618  N   THR A 361      18.862   1.579  28.050  1.00 34.83           N  
ANISOU 2618  N   THR A 361     4099   4202   4933   -718    -53    276       N  
ATOM   2619  CA  THR A 361      18.592   0.392  28.843  1.00 32.52           C  
ANISOU 2619  CA  THR A 361     3811   3975   4571   -687   -152    272       C  
ATOM   2620  C   THR A 361      19.822   0.267  29.729  1.00 32.51           C  
ANISOU 2620  C   THR A 361     3708   3985   4660   -737   -256    246       C  
ATOM   2621  O   THR A 361      20.919   0.029  29.233  1.00 32.56           O  
ANISOU 2621  O   THR A 361     3604   3986   4781   -742   -234    262       O  
ATOM   2622  CB  THR A 361      18.412  -0.872  27.965  1.00 29.99           C  
ANISOU 2622  CB  THR A 361     3482   3686   4226   -611   -108    320       C  
ATOM   2623  CG2 THR A 361      18.166  -2.112  28.830  1.00 29.31           C  
ANISOU 2623  CG2 THR A 361     3408   3651   4079   -585   -212    322       C  
ATOM   2624  OG1 THR A 361      17.286  -0.692  27.098  1.00 29.42           O  
ANISOU 2624  OG1 THR A 361     3500   3606   4074   -564    -21    336       O  
ATOM   2625  N   LEU A 362      19.651   0.468  31.032  1.00 31.46           N  
ANISOU 2625  N   LEU A 362     3609   3872   4474   -772   -367    201       N  
ATOM   2626  CA  LEU A 362      20.793   0.558  31.936  1.00 32.59           C  
ANISOU 2626  CA  LEU A 362     3662   4025   4697   -824   -482    164       C  
ATOM   2627  C   LEU A 362      20.875  -0.686  32.820  1.00 32.96           C  
ANISOU 2627  C   LEU A 362     3709   4134   4681   -787   -605    178       C  
ATOM   2628  O   LEU A 362      19.895  -1.073  33.447  1.00 33.37           O  
ANISOU 2628  O   LEU A 362     3866   4218   4597   -766   -639    182       O  
ATOM   2629  CB  LEU A 362      20.700   1.821  32.797  1.00 33.22           C  
ANISOU 2629  CB  LEU A 362     3780   4074   4767   -896   -530     92       C  
ATOM   2630  CG  LEU A 362      20.531   3.163  32.065  1.00 38.49           C  
ANISOU 2630  CG  LEU A 362     4471   4662   5492   -936   -418     77       C  
ATOM   2631  CD1 LEU A 362      20.469   4.317  33.056  1.00 39.90           C  
ANISOU 2631  CD1 LEU A 362     4690   4806   5665  -1004   -484     -6       C  
ATOM   2632  CD2 LEU A 362      21.649   3.391  31.052  1.00 36.97           C  
ANISOU 2632  CD2 LEU A 362     4159   4426   5460   -965   -336    107       C  
ATOM   2633  N   VAL A 363      22.047  -1.306  32.868  1.00 33.42           N  
ANISOU 2633  N   VAL A 363     3650   4207   4841   -778   -670    188       N  
ATOM   2634  CA  VAL A 363      22.234  -2.531  33.642  1.00 33.65           C  
ANISOU 2634  CA  VAL A 363     3679   4282   4822   -732   -793    212       C  
ATOM   2635  C   VAL A 363      23.263  -2.311  34.749  1.00 35.03           C  
ANISOU 2635  C   VAL A 363     3781   4479   5050   -772   -949    165       C  
ATOM   2636  O   VAL A 363      24.399  -1.898  34.484  1.00 38.49           O  
ANISOU 2636  O   VAL A 363     4082   4902   5639   -803   -959    136       O  
ATOM   2637  CB  VAL A 363      22.656  -3.687  32.718  1.00 35.59           C  
ANISOU 2637  CB  VAL A 363     3858   4529   5137   -660   -749    266       C  
ATOM   2638  CG1 VAL A 363      22.909  -4.960  33.513  1.00 36.07           C  
ANISOU 2638  CG1 VAL A 363     3923   4621   5161   -608   -883    297       C  
ATOM   2639  CG2 VAL A 363      21.597  -3.900  31.644  1.00 32.20           C  
ANISOU 2639  CG2 VAL A 363     3507   4082   4643   -621   -608    302       C  
ATOM   2640  N   PHE A 364      22.859  -2.554  35.995  1.00 35.27           N  
ANISOU 2640  N   PHE A 364     3901   4547   4952   -774  -1070    155       N  
ATOM   2641  CA  PHE A 364      23.735  -2.303  37.139  1.00 36.78           C  
ANISOU 2641  CA  PHE A 364     4044   4766   5166   -808  -1236    103       C  
ATOM   2642  C   PHE A 364      23.989  -3.546  37.980  1.00 38.21           C  
ANISOU 2642  C   PHE A 364     4246   4991   5279   -748  -1381    147       C  
ATOM   2643  O   PHE A 364      23.114  -4.403  38.134  1.00 36.54           O  
ANISOU 2643  O   PHE A 364     4149   4793   4941   -705  -1367    207       O  
ATOM   2644  CB  PHE A 364      23.132  -1.264  38.089  1.00 36.91           C  
ANISOU 2644  CB  PHE A 364     4162   4790   5073   -870  -1274     34       C  
ATOM   2645  CG  PHE A 364      22.962   0.108  37.497  1.00 40.08           C  
ANISOU 2645  CG  PHE A 364     4552   5135   5543   -934  -1162    -20       C  
ATOM   2646  CD1 PHE A 364      23.928   1.091  37.697  1.00 40.31           C  
ANISOU 2646  CD1 PHE A 364     4482   5135   5699  -1006  -1213    -95       C  
ATOM   2647  CD2 PHE A 364      21.812   0.431  36.789  1.00 35.45           C  
ANISOU 2647  CD2 PHE A 364     4057   4519   4894   -922  -1015      2       C  
ATOM   2648  CE1 PHE A 364      23.764   2.369  37.175  1.00 40.70           C  
ANISOU 2648  CE1 PHE A 364     4534   5116   5815  -1068  -1109   -139       C  
ATOM   2649  CE2 PHE A 364      21.638   1.699  36.266  1.00 36.00           C  
ANISOU 2649  CE2 PHE A 364     4130   4526   5022   -972   -920    -40       C  
ATOM   2650  CZ  PHE A 364      22.614   2.674  36.456  1.00 36.70           C  
ANISOU 2650  CZ  PHE A 364     4131   4575   5239  -1047   -963   -107       C  
ATOM   2651  N   LYS A 365      25.182  -3.609  38.558  1.00 38.71           N  
ANISOU 2651  N   LYS A 365     4202   5076   5430   -750  -1528    115       N  
ATOM   2652  CA  LYS A 365      25.428  -4.476  39.693  1.00 43.55           C  
ANISOU 2652  CA  LYS A 365     4862   5734   5953   -705  -1705    141       C  
ATOM   2653  C   LYS A 365      24.690  -3.829  40.854  1.00 41.37           C  
ANISOU 2653  C   LYS A 365     4729   5490   5499   -755  -1765     98       C  
ATOM   2654  O   LYS A 365      24.927  -2.663  41.169  1.00 45.23           O  
ANISOU 2654  O   LYS A 365     5191   5977   6017   -825  -1786      9       O  
ATOM   2655  CB  LYS A 365      26.925  -4.553  39.989  1.00 48.13           C  
ANISOU 2655  CB  LYS A 365     5274   6331   6682   -694  -1855    102       C  
ATOM   2656  CG  LYS A 365      27.305  -5.604  41.025  1.00 56.40           C  
ANISOU 2656  CG  LYS A 365     6358   7418   7651   -623  -2049    144       C  
ATOM   2657  CD  LYS A 365      28.817  -5.721  41.158  1.00 64.13           C  
ANISOU 2657  CD  LYS A 365     7146   8415   8805   -598  -2194    102       C  
ATOM   2658  CE  LYS A 365      29.217  -6.857  42.093  1.00 70.66           C  
ANISOU 2658  CE  LYS A 365     8012   9275   9562   -507  -2394    156       C  
ATOM   2659  NZ  LYS A 365      28.784  -6.624  43.499  1.00 71.78           N1+
ANISOU 2659  NZ  LYS A 365     8310   9463   9500   -532  -2535    142       N1+
ATOM   2660  N   LEU A 366      23.787  -4.572  41.483  1.00 39.50           N  
ANISOU 2660  N   LEU A 366     4647   5280   5082   -723  -1784    157       N  
ATOM   2661  CA  LEU A 366      22.896  -3.977  42.473  1.00 39.58           C  
ANISOU 2661  CA  LEU A 366     4806   5326   4907   -768  -1799    119       C  
ATOM   2662  C   LEU A 366      23.615  -3.341  43.666  1.00 43.21           C  
ANISOU 2662  C   LEU A 366     5259   5827   5332   -803  -1975     36       C  
ATOM   2663  O   LEU A 366      23.259  -2.241  44.089  1.00 48.69           O  
ANISOU 2663  O   LEU A 366     6001   6528   5973   -864  -1961    -51       O  
ATOM   2664  CB  LEU A 366      21.841  -4.981  42.944  1.00 39.12           C  
ANISOU 2664  CB  LEU A 366     4908   5292   4663   -731  -1780    205       C  
ATOM   2665  CG  LEU A 366      20.838  -4.444  43.972  1.00 39.74           C  
ANISOU 2665  CG  LEU A 366     5144   5417   4538   -774  -1775    168       C  
ATOM   2666  CD1 LEU A 366      20.172  -3.167  43.473  1.00 38.41           C  
ANISOU 2666  CD1 LEU A 366     4974   5226   4393   -828  -1638     85       C  
ATOM   2667  CD2 LEU A 366      19.794  -5.501  44.325  1.00 40.93           C  
ANISOU 2667  CD2 LEU A 366     5438   5589   4523   -747  -1730    263       C  
ATOM   2668  N   SER A 367      24.616  -4.024  44.212  1.00 44.65           N  
ANISOU 2668  N   SER A 367     5384   6036   5545   -760  -2148     56       N  
ATOM   2669  CA  SER A 367      25.313  -3.515  45.392  1.00 47.23           C  
ANISOU 2669  CA  SER A 367     5708   6411   5827   -785  -2339    -24       C  
ATOM   2670  C   SER A 367      25.972  -2.168  45.110  1.00 47.12           C  
ANISOU 2670  C   SER A 367     5563   6372   5970   -863  -2334   -147       C  
ATOM   2671  O   SER A 367      25.958  -1.274  45.953  1.00 48.28           O  
ANISOU 2671  O   SER A 367     5757   6542   6045   -918  -2411   -244       O  
ATOM   2672  CB  SER A 367      26.351  -4.522  45.894  1.00 47.24           C  
ANISOU 2672  CB  SER A 367     5649   6441   5858   -711  -2533     23       C  
ATOM   2673  OG  SER A 367      27.254  -4.874  44.863  1.00 49.25           O  
ANISOU 2673  OG  SER A 367     5716   6656   6340   -678  -2507     40       O  
ATOM   2674  N   SER A 368      26.548  -2.030  43.921  1.00 44.33           N  
ANISOU 2674  N   SER A 368     5049   5966   5830   -871  -2238   -145       N  
ATOM   2675  CA  SER A 368      27.177  -0.782  43.517  1.00 44.82           C  
ANISOU 2675  CA  SER A 368     4980   5988   6060   -955  -2207   -247       C  
ATOM   2676  C   SER A 368      26.130   0.306  43.360  1.00 44.94           C  
ANISOU 2676  C   SER A 368     5105   5965   6004  -1019  -2065   -294       C  
ATOM   2677  O   SER A 368      26.299   1.430  43.848  1.00 45.31           O  
ANISOU 2677  O   SER A 368     5151   5999   6068  -1093  -2110   -402       O  
ATOM   2678  CB  SER A 368      27.935  -0.968  42.202  1.00 46.55           C  
ANISOU 2678  CB  SER A 368     5017   6162   6508   -946  -2105   -216       C  
ATOM   2679  OG  SER A 368      28.955  -1.943  42.338  1.00 50.37           O  
ANISOU 2679  OG  SER A 368     5384   6680   7076   -878  -2238   -184       O  
ATOM   2680  N   TYR A 369      25.042  -0.035  42.676  1.00 42.16           N  
ANISOU 2680  N   TYR A 369     4846   5592   5580   -988  -1900   -219       N  
ATOM   2681  CA  TYR A 369      23.959   0.912  42.467  1.00 43.09           C  
ANISOU 2681  CA  TYR A 369     5068   5675   5629  -1030  -1762   -256       C  
ATOM   2682  C   TYR A 369      23.473   1.440  43.808  1.00 46.12           C  
ANISOU 2682  C   TYR A 369     5585   6102   5837  -1058  -1860   -335       C  
ATOM   2683  O   TYR A 369      23.299   2.647  43.984  1.00 42.39           O  
ANISOU 2683  O   TYR A 369     5135   5595   5378  -1119  -1837   -432       O  
ATOM   2684  CB  TYR A 369      22.804   0.264  41.699  1.00 42.43           C  
ANISOU 2684  CB  TYR A 369     5071   5582   5468   -979  -1602   -162       C  
ATOM   2685  CG  TYR A 369      21.599   1.163  41.563  1.00 43.04           C  
ANISOU 2685  CG  TYR A 369     5259   5632   5462  -1006  -1474   -200       C  
ATOM   2686  CD1 TYR A 369      21.537   2.127  40.565  1.00 39.42           C  
ANISOU 2686  CD1 TYR A 369     4753   5099   5127  -1041  -1346   -227       C  
ATOM   2687  CD2 TYR A 369      20.525   1.052  42.436  1.00 44.59           C  
ANISOU 2687  CD2 TYR A 369     5608   5878   5456   -994  -1480   -209       C  
ATOM   2688  CE1 TYR A 369      20.434   2.953  40.436  1.00 37.43           C  
ANISOU 2688  CE1 TYR A 369     4600   4816   4804  -1053  -1239   -263       C  
ATOM   2689  CE2 TYR A 369      19.420   1.872  42.316  1.00 39.63           C  
ANISOU 2689  CE2 TYR A 369     5069   5229   4761  -1010  -1364   -252       C  
ATOM   2690  CZ  TYR A 369      19.382   2.822  41.316  1.00 37.27           C  
ANISOU 2690  CZ  TYR A 369     4718   4850   4593  -1035  -1251   -280       C  
ATOM   2691  OH  TYR A 369      18.286   3.643  41.194  1.00 36.73           O  
ANISOU 2691  OH  TYR A 369     4738   4755   4464  -1038  -1146   -324       O  
ATOM   2692  N   VAL A 370      23.277   0.531  44.760  1.00 42.51           N  
ANISOU 2692  N   VAL A 370     5220   5717   5213  -1011  -1970   -292       N  
ATOM   2693  CA  VAL A 370      22.771   0.911  46.070  1.00 44.11           C  
ANISOU 2693  CA  VAL A 370     5566   5975   5219  -1029  -2056   -359       C  
ATOM   2694  C   VAL A 370      23.758   1.791  46.835  1.00 48.30           C  
ANISOU 2694  C   VAL A 370     6035   6513   5803  -1083  -2220   -486       C  
ATOM   2695  O   VAL A 370      23.363   2.760  47.487  1.00 48.31           O  
ANISOU 2695  O   VAL A 370     6118   6517   5721  -1129  -2233   -591       O  
ATOM   2696  CB  VAL A 370      22.394  -0.319  46.908  1.00 48.81           C  
ANISOU 2696  CB  VAL A 370     6283   6646   5618   -968  -2133   -270       C  
ATOM   2697  CG1 VAL A 370      22.140   0.082  48.358  1.00 50.22           C  
ANISOU 2697  CG1 VAL A 370     6597   6893   5592   -987  -2250   -346       C  
ATOM   2698  CG2 VAL A 370      21.170  -1.004  46.303  1.00 45.54           C  
ANISOU 2698  CG2 VAL A 370     5954   6223   5126   -934  -1960   -170       C  
ATOM   2699  N   ASP A 371      25.042   1.463  46.749  1.00 51.09           N  
ANISOU 2699  N   ASP A 371     6239   6869   6305  -1078  -2347   -484       N  
ATOM   2700  CA  ASP A 371      26.056   2.282  47.405  1.00 56.38           C  
ANISOU 2700  CA  ASP A 371     6825   7544   7053  -1135  -2511   -612       C  
ATOM   2701  C   ASP A 371      26.045   3.717  46.882  1.00 52.15           C  
ANISOU 2701  C   ASP A 371     6236   6923   6655  -1226  -2410   -717       C  
ATOM   2702  O   ASP A 371      26.101   4.676  47.658  1.00 49.16           O  
ANISOU 2702  O   ASP A 371     5899   6542   6236  -1284  -2491   -844       O  
ATOM   2703  CB  ASP A 371      27.442   1.660  47.245  1.00 64.88           C  
ANISOU 2703  CB  ASP A 371     7719   8635   8297  -1110  -2649   -591       C  
ATOM   2704  CG  ASP A 371      27.641   0.456  48.142  1.00 72.39           C  
ANISOU 2704  CG  ASP A 371     8737   9669   9100  -1024  -2820   -521       C  
ATOM   2705  OD1 ASP A 371      28.498  -0.396  47.821  1.00 76.73           O  
ANISOU 2705  OD1 ASP A 371     9161  10227   9767   -968  -2893   -460       O  
ATOM   2706  OD2 ASP A 371      26.936   0.364  49.171  1.00 71.13           O1-
ANISOU 2706  OD2 ASP A 371     8758   9564   8702  -1008  -2877   -526       O1-
ATOM   2707  N   ARG A 372      25.972   3.862  45.563  1.00 48.04           N  
ANISOU 2707  N   ARG A 372     5631   6328   6293  -1239  -2234   -664       N  
ATOM   2708  CA  ARG A 372      25.907   5.188  44.956  1.00 47.33           C  
ANISOU 2708  CA  ARG A 372     5505   6143   6334  -1321  -2120   -741       C  
ATOM   2709  C   ARG A 372      24.607   5.873  45.358  1.00 45.99           C  
ANISOU 2709  C   ARG A 372     5519   5960   5996  -1326  -2039   -788       C  
ATOM   2710  O   ARG A 372      24.577   7.075  45.619  1.00 47.75           O  
ANISOU 2710  O   ARG A 372     5763   6127   6253  -1394  -2042   -903       O  
ATOM   2711  CB  ARG A 372      26.013   5.097  43.430  1.00 50.28           C  
ANISOU 2711  CB  ARG A 372     5776   6447   6882  -1320  -1938   -655       C  
ATOM   2712  CG  ARG A 372      27.435   4.999  42.877  1.00 61.19           C  
ANISOU 2712  CG  ARG A 372     6941   7810   8499  -1353  -1981   -657       C  
ATOM   2713  CD  ARG A 372      28.462   4.681  43.955  1.00 66.67           C  
ANISOU 2713  CD  ARG A 372     7555   8574   9202  -1354  -2219   -722       C  
ATOM   2714  NE  ARG A 372      28.833   5.861  44.725  1.00 71.48           N  
ANISOU 2714  NE  ARG A 372     8157   9157   9845  -1447  -2325   -869       N  
ATOM   2715  CZ  ARG A 372      29.443   5.822  45.904  1.00 75.68           C  
ANISOU 2715  CZ  ARG A 372     8675   9754  10325  -1453  -2548   -955       C  
ATOM   2716  NH1 ARG A 372      29.746   4.658  46.462  1.00 79.13           N1+
ANISOU 2716  NH1 ARG A 372     9112  10285  10671  -1367  -2689   -897       N1+
ATOM   2717  NH2 ARG A 372      29.741   6.949  46.531  1.00 72.61           N  
ANISOU 2717  NH2 ARG A 372     8282   9333   9974  -1542  -2635  -1100       N  
ATOM   2718  N   LEU A 373      23.531   5.096  45.411  1.00 44.74           N  
ANISOU 2718  N   LEU A 373     5488   5851   5660  -1255  -1966   -702       N  
ATOM   2719  CA  LEU A 373      22.228   5.623  45.786  1.00 44.31           C  
ANISOU 2719  CA  LEU A 373     5598   5799   5441  -1249  -1879   -742       C  
ATOM   2720  C   LEU A 373      22.265   6.192  47.201  1.00 48.25           C  
ANISOU 2720  C   LEU A 373     6187   6345   5803  -1278  -2026   -870       C  
ATOM   2721  O   LEU A 373      21.779   7.295  47.450  1.00 48.38           O  
ANISOU 2721  O   LEU A 373     6270   6316   5796  -1315  -1986   -977       O  
ATOM   2722  CB  LEU A 373      21.175   4.520  45.700  1.00 44.67           C  
ANISOU 2722  CB  LEU A 373     5745   5904   5324  -1173  -1794   -626       C  
ATOM   2723  CG  LEU A 373      19.737   4.946  45.408  1.00 48.11           C  
ANISOU 2723  CG  LEU A 373     6295   6320   5665  -1156  -1627   -630       C  
ATOM   2724  CD1 LEU A 373      19.650   5.564  44.029  1.00 46.05           C  
ANISOU 2724  CD1 LEU A 373     5959   5957   5580  -1169  -1478   -610       C  
ATOM   2725  CD2 LEU A 373      18.802   3.755  45.518  1.00 45.92           C  
ANISOU 2725  CD2 LEU A 373     6107   6115   5225  -1093  -1571   -524       C  
ATOM   2726  N   ARG A 374      22.840   5.433  48.128  1.00 46.93           N  
ANISOU 2726  N   ARG A 374     6027   6265   5540  -1254  -2199   -860       N  
ATOM   2727  CA  ARG A 374      22.852   5.825  49.534  1.00 50.96           C  
ANISOU 2727  CA  ARG A 374     6641   6838   5882  -1269  -2349   -974       C  
ATOM   2728  C   ARG A 374      23.716   7.058  49.777  1.00 53.84           C  
ANISOU 2728  C   ARG A 374     6924   7144   6388  -1353  -2450  -1131       C  
ATOM   2729  O   ARG A 374      23.396   7.894  50.622  1.00 55.19           O  
ANISOU 2729  O   ARG A 374     7194   7321   6453  -1382  -2498  -1261       O  
ATOM   2730  CB  ARG A 374      23.319   4.664  50.415  1.00 52.87           C  
ANISOU 2730  CB  ARG A 374     6914   7186   5987  -1217  -2521   -912       C  
ATOM   2731  CG  ARG A 374      22.366   3.475  50.427  1.00 54.41           C  
ANISOU 2731  CG  ARG A 374     7227   7439   6009  -1144  -2433   -768       C  
ATOM   2732  CD  ARG A 374      22.907   2.333  51.278  1.00 58.33           C  
ANISOU 2732  CD  ARG A 374     7759   8022   6381  -1091  -2609   -696       C  
ATOM   2733  NE  ARG A 374      21.921   1.267  51.443  1.00 57.59           N  
ANISOU 2733  NE  ARG A 374     7803   7977   6101  -1035  -2524   -566       N  
ATOM   2734  CZ  ARG A 374      22.221   0.016  51.773  1.00 59.16           C  
ANISOU 2734  CZ  ARG A 374     8031   8221   6225   -976  -2618   -448       C  
ATOM   2735  NH1 ARG A 374      23.485  -0.337  51.965  1.00 60.10           N1+
ANISOU 2735  NH1 ARG A 374     8046   8349   6439   -954  -2807   -445       N1+
ATOM   2736  NH2 ARG A 374      21.260  -0.887  51.903  1.00 58.48           N  
ANISOU 2736  NH2 ARG A 374     8075   8166   5979   -940  -2524   -333       N  
ATOM   2737  N   GLU A 375      24.809   7.166  49.031  1.00 54.98           N  
ANISOU 2737  N   GLU A 375     6884   7230   6776  -1393  -2476  -1123       N  
ATOM   2738  CA  GLU A 375      25.715   8.302  49.154  1.00 57.19           C  
ANISOU 2738  CA  GLU A 375     7062   7443   7227  -1486  -2564  -1266       C  
ATOM   2739  C   GLU A 375      25.065   9.592  48.654  1.00 57.73           C  
ANISOU 2739  C   GLU A 375     7176   7394   7364  -1543  -2410  -1340       C  
ATOM   2740  O   GLU A 375      25.349  10.678  49.158  1.00 56.62           O  
ANISOU 2740  O   GLU A 375     7042   7202   7270  -1615  -2481  -1489       O  
ATOM   2741  CB  GLU A 375      27.009   8.029  48.381  1.00 62.61           C  
ANISOU 2741  CB  GLU A 375     7525   8096   8167  -1517  -2602  -1226       C  
ATOM   2742  CG  GLU A 375      27.781   9.276  47.970  1.00 75.04           C  
ANISOU 2742  CG  GLU A 375     8969   9560   9983  -1632  -2595  -1339       C  
ATOM   2743  CD  GLU A 375      28.553   9.901  49.117  1.00 90.38           C  
ANISOU 2743  CD  GLU A 375    10886  11527  11929  -1693  -2818  -1506       C  
ATOM   2744  OE1 GLU A 375      28.941  11.083  48.999  1.00 95.04           O  
ANISOU 2744  OE1 GLU A 375    11416  12017  12676  -1796  -2814  -1625       O  
ATOM   2745  OE2 GLU A 375      28.780   9.208  50.133  1.00 96.11           O1-
ANISOU 2745  OE2 GLU A 375    11653  12366  12498  -1640  -3002  -1519       O1-
ATOM   2746  N   SER A 376      24.182   9.469  47.669  1.00 54.21           N  
ANISOU 2746  N   SER A 376     6769   6903   6926  -1508  -2205  -1239       N  
ATOM   2747  CA  SER A 376      23.618  10.644  47.016  1.00 51.40           C  
ANISOU 2747  CA  SER A 376     6445   6423   6660  -1550  -2054  -1287       C  
ATOM   2748  C   SER A 376      22.160  10.891  47.385  1.00 49.97           C  
ANISOU 2748  C   SER A 376     6449   6259   6277  -1496  -1958  -1310       C  
ATOM   2749  O   SER A 376      21.589  11.908  47.007  1.00 50.57           O  
ANISOU 2749  O   SER A 376     6575   6237   6404  -1517  -1850  -1365       O  
ATOM   2750  CB  SER A 376      23.725  10.490  45.499  1.00 47.76           C  
ANISOU 2750  CB  SER A 376     5882   5886   6378  -1549  -1887  -1165       C  
ATOM   2751  OG  SER A 376      22.882   9.440  45.048  1.00 46.49           O  
ANISOU 2751  OG  SER A 376     5779   5788   6098  -1458  -1783  -1030       O  
ATOM   2752  N   HIS A 377      21.550   9.953  48.101  1.00 51.41           N  
ANISOU 2752  N   HIS A 377     6732   6564   6237  -1426  -1993  -1263       N  
ATOM   2753  CA  HIS A 377      20.123  10.034  48.395  1.00 49.76           C  
ANISOU 2753  CA  HIS A 377     6682   6387   5837  -1372  -1882  -1271       C  
ATOM   2754  C   HIS A 377      19.313   9.958  47.103  1.00 47.08           C  
ANISOU 2754  C   HIS A 377     6332   5986   5570  -1335  -1679  -1166       C  
ATOM   2755  O   HIS A 377      18.184  10.444  47.035  1.00 51.92           O  
ANISOU 2755  O   HIS A 377     7042   6578   6106  -1303  -1563  -1196       O  
ATOM   2756  CB  HIS A 377      19.788  11.328  49.150  1.00 56.84           C  
ANISOU 2756  CB  HIS A 377     7671   7239   6685  -1407  -1909  -1447       C  
ATOM   2757  CG  HIS A 377      20.367  11.401  50.530  1.00 63.45           C  
ANISOU 2757  CG  HIS A 377     8553   8154   7401  -1432  -2108  -1565       C  
ATOM   2758  CD2 HIS A 377      20.355  12.395  51.451  1.00 66.37           C  
ANISOU 2758  CD2 HIS A 377     9000   8507   7710  -1467  -2191  -1741       C  
ATOM   2759  ND1 HIS A 377      21.060  10.357  51.106  1.00 66.87           N  
ANISOU 2759  ND1 HIS A 377     8957   8694   7756  -1415  -2256  -1507       N  
ATOM   2760  CE1 HIS A 377      21.453  10.706  52.319  1.00 65.05           C  
ANISOU 2760  CE1 HIS A 377     8785   8516   7413  -1439  -2425  -1639       C  
ATOM   2761  NE2 HIS A 377      21.038  11.938  52.552  1.00 64.37           N  
ANISOU 2761  NE2 HIS A 377     8764   8359   7335  -1473  -2388  -1787       N  
ATOM   2762  N   GLY A 378      19.896   9.348  46.076  1.00 44.49           N  
ANISOU 2762  N   GLY A 378     5883   5632   5387  -1333  -1639  -1048       N  
ATOM   2763  CA  GLY A 378      19.238   9.223  44.787  1.00 43.70           C  
ANISOU 2763  CA  GLY A 378     5768   5478   5357  -1296  -1460   -947       C  
ATOM   2764  C   GLY A 378      19.179  10.514  43.986  1.00 47.43           C  
ANISOU 2764  C   GLY A 378     6223   5811   5988  -1335  -1361   -996       C  
ATOM   2765  O   GLY A 378      18.439  10.601  43.008  1.00 46.38           O  
ANISOU 2765  O   GLY A 378     6110   5631   5883  -1296  -1213   -929       O  
ATOM   2766  N   ILE A 379      19.962  11.510  44.399  1.00 40.79           N  
ANISOU 2766  N   ILE A 379     4942   4574   5981   -591   -583   -797       N  
ATOM   2767  CA  ILE A 379      20.016  12.810  43.724  1.00 38.37           C  
ANISOU 2767  CA  ILE A 379     4678   4267   5635   -628   -542   -801       C  
ATOM   2768  C   ILE A 379      21.088  12.793  42.638  1.00 37.82           C  
ANISOU 2768  C   ILE A 379     4655   4218   5499   -638   -505   -858       C  
ATOM   2769  O   ILE A 379      22.254  12.554  42.921  1.00 38.39           O  
ANISOU 2769  O   ILE A 379     4693   4344   5549   -630   -461   -912       O  
ATOM   2770  CB  ILE A 379      20.346  13.938  44.724  1.00 39.68           C  
ANISOU 2770  CB  ILE A 379     4793   4474   5811   -649   -478   -802       C  
ATOM   2771  CG1 ILE A 379      19.292  13.995  45.826  1.00 42.74           C  
ANISOU 2771  CG1 ILE A 379     5127   4850   6261   -641   -512   -751       C  
ATOM   2772  CG2 ILE A 379      20.428  15.308  44.020  1.00 37.27           C  
ANISOU 2772  CG2 ILE A 379     4540   4154   5467   -689   -430   -804       C  
ATOM   2773  CD1 ILE A 379      17.924  14.378  45.317  1.00 43.37           C  
ANISOU 2773  CD1 ILE A 379     5248   4870   6359   -648   -564   -699       C  
ATOM   2774  N   VAL A 380      20.699  13.006  41.387  1.00 36.24           N  
ANISOU 2774  N   VAL A 380     4526   3981   5261   -655   -526   -850       N  
ATOM   2775  CA  VAL A 380      21.696  13.082  40.330  1.00 41.58           C  
ANISOU 2775  CA  VAL A 380     5248   4684   5868   -673   -487   -905       C  
ATOM   2776  C   VAL A 380      21.870  14.541  39.928  1.00 42.44           C  
ANISOU 2776  C   VAL A 380     5397   4794   5934   -719   -428   -896       C  
ATOM   2777  O   VAL A 380      20.988  15.360  40.182  1.00 41.55           O  
ANISOU 2777  O   VAL A 380     5295   4645   5847   -728   -437   -840       O  
ATOM   2778  CB  VAL A 380      21.328  12.216  39.106  1.00 45.93           C  
ANISOU 2778  CB  VAL A 380     5854   5204   6394   -664   -544   -913       C  
ATOM   2779  CG1 VAL A 380      21.125  10.762  39.521  1.00 49.55           C  
ANISOU 2779  CG1 VAL A 380     6279   5647   6901   -621   -598   -922       C  
ATOM   2780  CG2 VAL A 380      20.094  12.757  38.411  1.00 43.57           C  
ANISOU 2780  CG2 VAL A 380     5608   4856   6089   -678   -588   -854       C  
ATOM   2781  N   PRO A 381      23.012  14.874  39.310  1.00 44.70           N  
ANISOU 2781  N   PRO A 381     5707   5123   6156   -749   -365   -952       N  
ATOM   2782  CA  PRO A 381      23.236  16.276  38.944  1.00 43.87           C  
ANISOU 2782  CA  PRO A 381     5647   5012   6009   -800   -301   -942       C  
ATOM   2783  C   PRO A 381      22.057  16.803  38.136  1.00 41.30           C  
ANISOU 2783  C   PRO A 381     5396   4621   5677   -804   -347   -872       C  
ATOM   2784  O   PRO A 381      21.494  16.068  37.323  1.00 42.68           O  
ANISOU 2784  O   PRO A 381     5603   4774   5838   -784   -411   -858       O  
ATOM   2785  CB  PRO A 381      24.495  16.213  38.077  1.00 48.46           C  
ANISOU 2785  CB  PRO A 381     6255   5647   6512   -831   -247  -1014       C  
ATOM   2786  CG  PRO A 381      25.203  14.973  38.533  1.00 49.97           C  
ANISOU 2786  CG  PRO A 381     6379   5888   6717   -790   -260  -1074       C  
ATOM   2787  CD  PRO A 381      24.109  13.998  38.866  1.00 42.75           C  
ANISOU 2787  CD  PRO A 381     5450   4925   5869   -738   -350  -1027       C  
ATOM   2788  N   GLU A 382      21.682  18.054  38.372  1.00 37.61           N  
ANISOU 2788  N   GLU A 382     4952   4121   5219   -827   -314   -829       N  
ATOM   2789  CA  GLU A 382      20.544  18.657  37.688  1.00 38.78           C  
ANISOU 2789  CA  GLU A 382     5168   4207   5361   -821   -357   -757       C  
ATOM   2790  C   GLU A 382      20.970  19.651  36.619  1.00 38.98           C  
ANISOU 2790  C   GLU A 382     5283   4218   5311   -865   -304   -749       C  
ATOM   2791  O   GLU A 382      22.142  20.008  36.520  1.00 39.95           O  
ANISOU 2791  O   GLU A 382     5411   4377   5390   -910   -225   -801       O  
ATOM   2792  CB  GLU A 382      19.645  19.369  38.695  1.00 37.56           C  
ANISOU 2792  CB  GLU A 382     4981   4015   5276   -806   -366   -707       C  
ATOM   2793  CG  GLU A 382      18.803  18.443  39.558  1.00 38.42           C  
ANISOU 2793  CG  GLU A 382     5017   4124   5455   -762   -437   -692       C  
ATOM   2794  CD  GLU A 382      18.194  19.185  40.730  1.00 43.57           C  
ANISOU 2794  CD  GLU A 382     5621   4760   6173   -756   -427   -662       C  
ATOM   2795  OE1 GLU A 382      16.978  19.055  40.963  1.00 49.54           O  
ANISOU 2795  OE1 GLU A 382     6362   5487   6972   -725   -493   -615       O  
ATOM   2796  OE2 GLU A 382      18.940  19.913  41.416  1.00 48.16           O1-
ANISOU 2796  OE2 GLU A 382     6175   5361   6761   -784   -351   -691       O1-
ATOM   2797  N   PHE A 383      19.998  20.098  35.829  1.00 38.90           N  
ANISOU 2797  N   PHE A 383     5340   4157   5281   -853   -349   -682       N  
ATOM   2798  CA  PHE A 383      20.222  21.127  34.822  1.00 39.60           C  
ANISOU 2798  CA  PHE A 383     5525   4221   5299   -889   -305   -654       C  
ATOM   2799  C   PHE A 383      18.912  21.861  34.526  1.00 39.89           C  
ANISOU 2799  C   PHE A 383     5615   4192   5350   -856   -356   -565       C  
ATOM   2800  O   PHE A 383      17.837  21.466  34.988  1.00 39.55           O  
ANISOU 2800  O   PHE A 383     5530   4133   5365   -807   -430   -534       O  
ATOM   2801  CB  PHE A 383      20.784  20.514  33.530  1.00 40.08           C  
ANISOU 2801  CB  PHE A 383     5633   4322   5273   -909   -312   -686       C  
ATOM   2802  CG  PHE A 383      19.771  19.721  32.737  1.00 40.23           C  
ANISOU 2802  CG  PHE A 383     5671   4335   5279   -867   -411   -654       C  
ATOM   2803  CD1 PHE A 383      19.010  20.330  31.748  1.00 40.85           C  
ANISOU 2803  CD1 PHE A 383     5830   4381   5309   -859   -444   -586       C  
ATOM   2804  CD2 PHE A 383      19.582  18.370  32.980  1.00 39.83           C  
ANISOU 2804  CD2 PHE A 383     5557   4312   5264   -835   -471   -692       C  
ATOM   2805  CE1 PHE A 383      18.079  19.607  31.022  1.00 43.71           C  
ANISOU 2805  CE1 PHE A 383     6202   4750   5654   -823   -534   -563       C  
ATOM   2806  CE2 PHE A 383      18.652  17.636  32.254  1.00 42.86           C  
ANISOU 2806  CE2 PHE A 383     5955   4693   5637   -804   -557   -671       C  
ATOM   2807  CZ  PHE A 383      17.897  18.255  31.276  1.00 45.09           C  
ANISOU 2807  CZ  PHE A 383     6310   4954   5867   -799   -590   -610       C  
ATOM   2808  N   ILE A 384      19.005  22.937  33.757  1.00 40.58           N  
ANISOU 2808  N   ILE A 384     5794   4242   5382   -882   -316   -524       N  
ATOM   2809  CA  ILE A 384      17.808  23.618  33.285  1.00 41.03           C  
ANISOU 2809  CA  ILE A 384     5912   4240   5438   -842   -368   -436       C  
ATOM   2810  C   ILE A 384      17.984  23.978  31.818  1.00 41.94           C  
ANISOU 2810  C   ILE A 384     6133   4352   5450   -863   -362   -402       C  
ATOM   2811  O   ILE A 384      19.093  24.274  31.373  1.00 42.27           O  
ANISOU 2811  O   ILE A 384     6217   4412   5431   -924   -284   -435       O  
ATOM   2812  CB  ILE A 384      17.497  24.873  34.131  1.00 41.06           C  
ANISOU 2812  CB  ILE A 384     5922   4178   5500   -839   -325   -398       C  
ATOM   2813  CG1 ILE A 384      16.068  25.354  33.880  1.00 41.40           C  
ANISOU 2813  CG1 ILE A 384     6001   4168   5563   -774   -399   -313       C  
ATOM   2814  CG2 ILE A 384      18.509  25.971  33.861  1.00 41.61           C  
ANISOU 2814  CG2 ILE A 384     6065   4221   5525   -904   -216   -405       C  
ATOM   2815  CD1 ILE A 384      15.595  26.356  34.900  1.00 41.31           C  
ANISOU 2815  CD1 ILE A 384     5970   4096   5630   -756   -373   -288       C  
ATOM   2816  N   ASN A 385      16.890  23.948  31.066  1.00 42.34           N  
ANISOU 2816  N   ASN A 385     6224   4386   5476   -815   -443   -337       N  
ATOM   2817  CA  ASN A 385      16.952  24.183  29.632  1.00 46.31           C  
ANISOU 2817  CA  ASN A 385     6824   4897   5875   -828   -450   -300       C  
ATOM   2818  C   ASN A 385      15.764  25.010  29.150  1.00 46.82           C  
ANISOU 2818  C   ASN A 385     6954   4908   5926   -773   -503   -200       C  
ATOM   2819  O   ASN A 385      14.841  24.476  28.537  1.00 50.62           O  
ANISOU 2819  O   ASN A 385     7433   5415   6384   -725   -594   -172       O  
ATOM   2820  CB  ASN A 385      17.001  22.843  28.897  1.00 53.16           C  
ANISOU 2820  CB  ASN A 385     7662   5839   6696   -826   -509   -348       C  
ATOM   2821  CG  ASN A 385      17.097  23.000  27.394  1.00 61.02           C  
ANISOU 2821  CG  ASN A 385     8748   6860   7576   -843   -517   -318       C  
ATOM   2822  ND2 ASN A 385      16.352  22.174  26.668  1.00 65.64           N  
ANISOU 2822  ND2 ASN A 385     9323   7488   8130   -808   -606   -314       N  
ATOM   2823  OD1 ASN A 385      17.828  23.852  26.889  1.00 63.70           O  
ANISOU 2823  OD1 ASN A 385     9166   7185   7852   -892   -443   -300       O  
ATOM   2824  N   PRO A 386      15.783  26.320  29.430  1.00 44.28           N  
ANISOU 2824  N   PRO A 386     6692   4512   5622   -777   -446   -149       N  
ATOM   2825  CA  PRO A 386      14.661  27.199  29.083  1.00 50.69           C  
ANISOU 2825  CA  PRO A 386     7566   5262   6430   -714   -494    -51       C  
ATOM   2826  C   PRO A 386      14.467  27.329  27.571  1.00 56.22           C  
ANISOU 2826  C   PRO A 386     8365   5980   7015   -706   -527      9       C  
ATOM   2827  O   PRO A 386      15.448  27.385  26.827  1.00 59.00           O  
ANISOU 2827  O   PRO A 386     8776   6355   7286   -770   -468     -8       O  
ATOM   2828  CB  PRO A 386      15.083  28.561  29.662  1.00 52.39           C  
ANISOU 2828  CB  PRO A 386     7834   5389   6681   -741   -400    -25       C  
ATOM   2829  CG  PRO A 386      16.179  28.265  30.637  1.00 48.96           C  
ANISOU 2829  CG  PRO A 386     7328   4981   6294   -807   -320   -118       C  
ATOM   2830  CD  PRO A 386      16.875  27.051  30.095  1.00 45.15           C  
ANISOU 2830  CD  PRO A 386     6811   4590   5754   -843   -332   -184       C  
ATOM   2831  N   LYS A 387      13.214  27.379  27.129  1.00 53.64           N  
ANISOU 2831  N   LYS A 387     8051   5650   6678   -627   -621     75       N  
ATOM   2832  CA  LYS A 387      12.904  27.697  25.740  1.00 58.26           C  
ANISOU 2832  CA  LYS A 387     8734   6248   7152   -607   -655    148       C  
ATOM   2833  C   LYS A 387      12.604  29.189  25.631  1.00 58.54           C  
ANISOU 2833  C   LYS A 387     8875   6186   7183   -576   -623    247       C  
ATOM   2834  O   LYS A 387      11.646  29.674  26.228  1.00 59.34           O  
ANISOU 2834  O   LYS A 387     8956   6237   7354   -504   -664    288       O  
ATOM   2835  CB  LYS A 387      11.707  26.878  25.246  1.00 57.69           C  
ANISOU 2835  CB  LYS A 387     8616   6243   7062   -537   -779    160       C  
ATOM   2836  CG  LYS A 387      11.932  25.374  25.267  0.43 61.36           C  
ANISOU 2836  CG  LYS A 387     8986   6796   7531   -566   -814     65       C  
ATOM   2837  CD  LYS A 387      13.114  24.990  24.392  0.43 67.75           C  
ANISOU 2837  CD  LYS A 387     9839   7655   8248   -643   -759     21       C  
ATOM   2838  CE  LYS A 387      13.377  23.495  24.436  0.43 70.51           C  
ANISOU 2838  CE  LYS A 387    10098   8083   8609   -667   -791    -79       C  
ATOM   2839  NZ  LYS A 387      14.510  23.121  23.545  0.43 74.43           N1+
ANISOU 2839  NZ  LYS A 387    10632   8634   9014   -737   -740   -128       N1+
ATOM   2840  N   TYR A 388      13.426  29.911  24.872  1.00 61.06           N  
ANISOU 2840  N   TYR A 388     9305   6475   7420   -631   -547    283       N  
ATOM   2841  CA  TYR A 388      13.308  31.369  24.776  1.00 64.80           C  
ANISOU 2841  CA  TYR A 388     9893   6839   7889   -614   -499    376       C  
ATOM   2842  C   TYR A 388      12.405  31.843  23.636  1.00 68.62           C  
ANISOU 2842  C   TYR A 388    10470   7315   8287   -539   -570    489       C  
ATOM   2843  O   TYR A 388      12.167  31.118  22.669  1.00 67.36           O  
ANISOU 2843  O   TYR A 388    10307   7245   8039   -527   -636    493       O  
ATOM   2844  CB  TYR A 388      14.692  32.012  24.636  1.00 65.77           C  
ANISOU 2844  CB  TYR A 388    10095   6924   7972   -721   -367    359       C  
ATOM   2845  CG  TYR A 388      15.594  31.775  25.826  1.00 66.06           C  
ANISOU 2845  CG  TYR A 388    10045   6960   8093   -790   -287    254       C  
ATOM   2846  CD1 TYR A 388      15.653  32.691  26.870  1.00 60.65           C  
ANISOU 2846  CD1 TYR A 388     9362   6182   7501   -794   -224    255       C  
ATOM   2847  CD2 TYR A 388      16.380  30.631  25.910  1.00 66.51           C  
ANISOU 2847  CD2 TYR A 388    10018   7115   8136   -847   -277    151       C  
ATOM   2848  CE1 TYR A 388      16.472  32.479  27.961  1.00 56.88           C  
ANISOU 2848  CE1 TYR A 388     8801   5719   7094   -856   -152    158       C  
ATOM   2849  CE2 TYR A 388      17.204  30.409  27.001  1.00 62.93           C  
ANISOU 2849  CE2 TYR A 388     9484   6672   7755   -902   -208     58       C  
ATOM   2850  CZ  TYR A 388      17.246  31.338  28.021  1.00 58.23           C  
ANISOU 2850  CZ  TYR A 388     8887   5992   7244   -907   -146     62       C  
ATOM   2851  OH  TYR A 388      18.062  31.121  29.107  1.00 55.11           O  
ANISOU 2851  OH  TYR A 388     8406   5618   6914   -961    -79    -32       O  
ATOM   2852  N   SER A 389      11.909  33.070  23.763  1.00 72.01           N  
ANISOU 2852  N   SER A 389    10981   7637   8742   -486   -557    579       N  
ATOM   2853  CA  SER A 389      11.082  33.687  22.733  1.00 76.23           C  
ANISOU 2853  CA  SER A 389    11616   8152   9196   -405   -619    698       C  
ATOM   2854  C   SER A 389      11.920  34.005  21.504  0.93 81.56           C  
ANISOU 2854  C   SER A 389    12415   8836   9736   -474   -562    745       C  
ATOM   2855  O   SER A 389      11.594  33.594  20.392  0.91 84.29           O  
ANISOU 2855  O   SER A 389    12789   9263   9976   -450   -627    783       O  
ATOM   2856  CB  SER A 389      10.442  34.975  23.257  1.00 77.51           C  
ANISOU 2856  CB  SER A 389    11840   8183   9429   -331   -607    780       C  
ATOM   2857  OG  SER A 389       9.660  34.735  24.413  1.00 77.88           O  
ANISOU 2857  OG  SER A 389    11769   8224   9598   -270   -656    734       O  
ATOM   2858  N   ASP A 390      13.001  34.745  21.716  0.92 85.92           N  
ANISOU 2858  N   ASP A 390    13041   9311  10293   -565   -437    738       N  
ATOM   2859  CA  ASP A 390      13.873  35.166  20.630  1.00 91.16           C  
ANISOU 2859  CA  ASP A 390    13829   9974  10831   -644   -367    782       C  
ATOM   2860  C   ASP A 390      15.250  34.543  20.779  0.99 92.00           C  
ANISOU 2860  C   ASP A 390    13891  10145  10921   -775   -278    666       C  
ATOM   2861  O   ASP A 390      15.433  33.590  21.533  0.95 89.53           O  
ANISOU 2861  O   ASP A 390    13446   9895  10676   -790   -292    558       O  
ATOM   2862  CB  ASP A 390      14.000  36.689  20.618  1.00 94.78           C  
ANISOU 2862  CB  ASP A 390    14435  10283  11295   -646   -287    882       C  
ATOM   2863  CG  ASP A 390      12.658  37.382  20.525  0.76 97.76           C  
ANISOU 2863  CG  ASP A 390    14860  10588  11695   -506   -372    996       C  
ATOM   2864  OD1 ASP A 390      11.770  36.868  19.814  0.23 97.96           O  
ANISOU 2864  OD1 ASP A 390    14864  10695  11659   -422   -487   1039       O  
ATOM   2865  OD2 ASP A 390      12.491  38.439  21.169  0.92100.22           O1-
ANISOU 2865  OD2 ASP A 390    15227  10766  12087   -479   -325   1039       O1-
ATOM   2866  N   GLU A 391      16.218  35.093  20.056  1.00 97.66           N  
ANISOU 2866  N   GLU A 391    14717  10844  11544   -868   -184    691       N  
ATOM   2867  CA  GLU A 391      17.593  34.628  20.142  1.00101.28           C  
ANISOU 2867  CA  GLU A 391    15141  11364  11977   -996    -89    581       C  
ATOM   2868  C   GLU A 391      18.437  35.591  20.972  1.00 98.92           C  
ANISOU 2868  C   GLU A 391    14882  10961  11743  -1075     43    557       C  
ATOM   2869  O   GLU A 391      19.650  35.420  21.088  1.00 99.54           O  
ANISOU 2869  O   GLU A 391    14942  11080  11800  -1188    137    469       O  
ATOM   2870  CB  GLU A 391      18.189  34.479  18.740  1.00107.43           C  
ANISOU 2870  CB  GLU A 391    16001  12219  12597  -1061    -69    605       C  
ATOM   2871  CG  GLU A 391      18.475  33.043  18.321  0.91112.00           C  
ANISOU 2871  CG  GLU A 391    16475  12952  13127  -1083   -121    504       C  
ATOM   2872  CD  GLU A 391      19.830  32.550  18.797  0.56114.81           C  
ANISOU 2872  CD  GLU A 391    16763  13361  13499  -1196    -26    370       C  
ATOM   2873  OE1 GLU A 391      20.298  33.013  19.858  0.37114.61           O  
ANISOU 2873  OE1 GLU A 391    16713  13267  13566  -1231     50    328       O  
ATOM   2874  OE2 GLU A 391      20.431  31.703  18.102  0.97116.91           O1-
ANISOU 2874  OE2 GLU A 391    16996  13742  13681  -1248    -28    302       O1-
ATOM   2875  N   THR A 392      17.794  36.597  21.557  1.00 96.55           N  
ANISOU 2875  N   THR A 392    14631  10531  11523  -1016     49    629       N  
ATOM   2876  CA  THR A 392      18.525  37.631  22.284  0.77 99.07           C  
ANISOU 2876  CA  THR A 392    15001  10739  11901  -1092    178    612       C  
ATOM   2877  C   THR A 392      17.853  38.096  23.574  0.76102.18           C  
ANISOU 2877  C   THR A 392    15340  11040  12444  -1023    167    606       C  
ATOM   2878  O   THR A 392      18.468  38.068  24.640  0.81102.21           O  
ANISOU 2878  O   THR A 392    15265  11039  12531  -1081    236    509       O  
ATOM   2879  CB  THR A 392      18.790  38.863  21.393  0.63 99.16           C  
ANISOU 2879  CB  THR A 392    15200  10649  11826  -1134    252    726       C  
ATOM   2880  CG2 THR A 392      19.252  40.046  22.236  0.79 98.82           C  
ANISOU 2880  CG2 THR A 392    15216  10465  11867  -1190    373    721       C  
ATOM   2881  OG1 THR A 392      19.801  38.548  20.427  0.29 98.53           O  
ANISOU 2881  OG1 THR A 392    15164  10655  11616  -1243    308    700       O  
ATOM   2882  N   ARG A 393      16.597  38.523  23.473  0.93105.20           N  
ANISOU 2882  N   ARG A 393    15760  11356  12854   -900     80    707       N  
ATOM   2883  CA  ARG A 393      15.907  39.180  24.588  0.32108.52           C  
ANISOU 2883  CA  ARG A 393    16151  11673  13408   -831     75    715       C  
ATOM   2884  C   ARG A 393      15.895  38.373  25.894  0.60107.23           C  
ANISOU 2884  C   ARG A 393    15813  11572  13358   -828     56    593       C  
ATOM   2885  O   ARG A 393      15.707  38.934  26.975  0.83108.40           O  
ANISOU 2885  O   ARG A 393    15927  11644  13618   -812     90    569       O  
ATOM   2886  CB  ARG A 393      14.483  39.577  24.182  0.58111.52           C  
ANISOU 2886  CB  ARG A 393    16582  12000  13790   -684    -35    836       C  
ATOM   2887  CG  ARG A 393      13.796  40.530  25.151  0.94113.45           C  
ANISOU 2887  CG  ARG A 393    16833  12114  14159   -612    -27    863       C  
ATOM   2888  CD  ARG A 393      12.581  41.187  24.511  1.00117.36           C  
ANISOU 2888  CD  ARG A 393    17421  12539  14632   -475   -114   1000       C  
ATOM   2889  NE  ARG A 393      12.950  42.045  23.387  1.00122.12           N  
ANISOU 2889  NE  ARG A 393    18206  13066  15128   -503    -61   1111       N  
ATOM   2890  CZ  ARG A 393      13.112  43.364  23.471  1.00124.78           C  
ANISOU 2890  CZ  ARG A 393    18677  13240  15493   -512     25   1179       C  
ATOM   2891  NH1 ARG A 393      12.932  43.985  24.628  1.00123.59           N1+
ANISOU 2891  NH1 ARG A 393    18493  12987  15477   -493     67   1141       N1+
ATOM   2892  NH2 ARG A 393      13.451  44.065  22.396  1.00126.49           N  
ANISOU 2892  NH2 ARG A 393    19063  13393  15604   -542     71   1285       N  
ATOM   2893  N   ARG A 394      16.094  37.063  25.789  1.00103.58           N  
ANISOU 2893  N   ARG A 394    15242  11248  12865   -844      4    518       N  
ATOM   2894  CA  ARG A 394      16.201  36.201  26.965  1.00 97.73           C  
ANISOU 2894  CA  ARG A 394    14340  10574  12218   -851    -10    404       C  
ATOM   2895  C   ARG A 394      14.901  36.089  27.762  0.71 89.41           C  
ANISOU 2895  C   ARG A 394    13205   9502  11267   -735   -106    420       C  
ATOM   2896  O   ARG A 394      14.926  35.896  28.980  0.78 86.64           O  
ANISOU 2896  O   ARG A 394    12747   9156  11017   -739    -91    346       O  
ATOM   2897  CB  ARG A 394      17.331  36.677  27.882  1.00101.02           C  
ANISOU 2897  CB  ARG A 394    14738  10956  12690   -955    122    320       C  
ATOM   2898  CG  ARG A 394      18.723  36.615  27.267  0.79103.73           C  
ANISOU 2898  CG  ARG A 394    15129  11345  12939  -1081    222    274       C  
ATOM   2899  CD  ARG A 394      19.159  35.186  26.969  1.00102.99           C  
ANISOU 2899  CD  ARG A 394    14937  11399  12794  -1104    176    194       C  
ATOM   2900  NE  ARG A 394      18.629  34.693  25.701  0.98103.32           N  
ANISOU 2900  NE  ARG A 394    15028  11491  12736  -1058     88    260       N  
ATOM   2901  CZ  ARG A 394      18.968  33.531  25.152  0.61101.01           C  
ANISOU 2901  CZ  ARG A 394    14680  11320  12380  -1078     48    204       C  
ATOM   2902  NH1 ARG A 394      19.841  32.737  25.758  0.35 99.97           N1+
ANISOU 2902  NH1 ARG A 394    14444  11267  12275  -1136     85     85       N1+
ATOM   2903  NH2 ARG A 394      18.437  33.163  23.995  0.94100.77           N  
ANISOU 2903  NH2 ARG A 394    14696  11334  12258  -1036    -30    265       N  
ATOM   2904  N   SER A 395      13.769  36.210  27.077  0.70 82.22           N  
ANISOU 2904  N   SER A 395    12339   8577  10324   -632   -205    515       N  
ATOM   2905  CA  SER A 395      12.473  35.987  27.707  1.00 74.73           C  
ANISOU 2905  CA  SER A 395    11305   7633   9458   -520   -308    526       C  
ATOM   2906  C   SER A 395      11.992  34.569  27.413  1.00 64.36           C  
ANISOU 2906  C   SER A 395     9888   6452   8114   -488   -415    487       C  
ATOM   2907  O   SER A 395      12.173  34.064  26.305  1.00 60.15           O  
ANISOU 2907  O   SER A 395     9395   5985   7474   -504   -445    507       O  
ATOM   2908  CB  SER A 395      11.449  37.010  27.215  1.00 78.45           C  
ANISOU 2908  CB  SER A 395    11877   8010   9920   -416   -354    647       C  
ATOM   2909  OG  SER A 395      11.857  38.327  27.544  1.00 86.85           O  
ANISOU 2909  OG  SER A 395    13039   8937  11024   -444   -252    681       O  
ATOM   2910  N   PHE A 396      11.383  33.929  28.406  1.00 59.58           N  
ANISOU 2910  N   PHE A 396     9151   5887   7601   -448   -471    430       N  
ATOM   2911  CA  PHE A 396      10.940  32.543  28.266  1.00 57.63           C  
ANISOU 2911  CA  PHE A 396     8800   5759   7338   -427   -565    383       C  
ATOM   2912  C   PHE A 396       9.684  32.412  27.393  1.00 56.91           C  
ANISOU 2912  C   PHE A 396     8730   5700   7194   -326   -684    458       C  
ATOM   2913  O   PHE A 396       8.698  33.116  27.607  1.00 51.90           O  
ANISOU 2913  O   PHE A 396     8109   5011   6600   -237   -728    518       O  
ATOM   2914  CB  PHE A 396      10.667  31.919  29.642  1.00 56.59           C  
ANISOU 2914  CB  PHE A 396     8524   5657   7320   -420   -583    302       C  
ATOM   2915  CG  PHE A 396      11.889  31.791  30.523  1.00 51.25           C  
ANISOU 2915  CG  PHE A 396     7803   4982   6689   -515   -481    215       C  
ATOM   2916  CD1 PHE A 396      13.144  32.170  30.068  1.00 49.05           C  
ANISOU 2916  CD1 PHE A 396     7602   4684   6350   -603   -380    202       C  
ATOM   2917  CD2 PHE A 396      11.774  31.279  31.810  1.00 45.81           C  
ANISOU 2917  CD2 PHE A 396     6988   4321   6098   -516   -486    143       C  
ATOM   2918  CE1 PHE A 396      14.259  32.044  30.884  1.00 47.13           C  
ANISOU 2918  CE1 PHE A 396     7308   4455   6145   -688   -288    115       C  
ATOM   2919  CE2 PHE A 396      12.883  31.153  32.630  1.00 45.12           C  
ANISOU 2919  CE2 PHE A 396     6853   4245   6046   -597   -396     63       C  
ATOM   2920  CZ  PHE A 396      14.127  31.533  32.167  1.00 45.48           C  
ANISOU 2920  CZ  PHE A 396     6972   4277   6032   -681   -298     47       C  
ATOM   2921  N   LYS A 397       9.720  31.509  26.415  1.00 58.44           N  
ANISOU 2921  N   LYS A 397     8920   5987   7296   -338   -736    450       N  
ATOM   2922  CA  LYS A 397       8.525  31.198  25.634  1.00 64.07           C  
ANISOU 2922  CA  LYS A 397     9630   6757   7957   -248   -854    503       C  
ATOM   2923  C   LYS A 397       7.473  30.596  26.555  1.00 59.31           C  
ANISOU 2923  C   LYS A 397     8896   6192   7448   -187   -935    461       C  
ATOM   2924  O   LYS A 397       6.282  30.884  26.437  1.00 57.66           O  
ANISOU 2924  O   LYS A 397     8678   5984   7245    -91  -1017    513       O  
ATOM   2925  CB  LYS A 397       8.839  30.231  24.488  1.00 71.28           C  
ANISOU 2925  CB  LYS A 397    10550   7776   8759   -286   -888    482       C  
ATOM   2926  CG  LYS A 397       9.055  30.916  23.146  1.00 82.74           C  
ANISOU 2926  CG  LYS A 397    12140   9216  10084   -284   -875    572       C  
ATOM   2927  CD  LYS A 397       8.864  29.964  21.967  1.00 88.42           C  
ANISOU 2927  CD  LYS A 397    12848  10055  10691   -285   -947    561       C  
ATOM   2928  CE  LYS A 397      10.012  28.974  21.841  1.00 91.86           C  
ANISOU 2928  CE  LYS A 397    13246  10557  11101   -391   -895    462       C  
ATOM   2929  NZ  LYS A 397       9.899  28.149  20.604  1.00 93.64           N1+
ANISOU 2929  NZ  LYS A 397    13473  10895  11211   -398   -955    451       N1+
ATOM   2930  N   LYS A 398       7.935  29.758  27.474  1.00 55.16           N  
ANISOU 2930  N   LYS A 398     8268   5699   6991   -245   -909    365       N  
ATOM   2931  CA  LYS A 398       7.092  29.195  28.517  1.00 55.44           C  
ANISOU 2931  CA  LYS A 398     8178   5763   7123   -206   -967    318       C  
ATOM   2932  C   LYS A 398       7.935  29.041  29.779  1.00 52.72           C  
ANISOU 2932  C   LYS A 398     7769   5393   6868   -275   -885    243       C  
ATOM   2933  O   LYS A 398       9.162  29.023  29.707  1.00 48.63           O  
ANISOU 2933  O   LYS A 398     7286   4866   6326   -355   -800    210       O  
ATOM   2934  CB  LYS A 398       6.507  27.848  28.074  1.00 60.72           C  
ANISOU 2934  CB  LYS A 398     8769   6542   7758   -196  -1061    277       C  
ATOM   2935  CG  LYS A 398       7.545  26.816  27.656  1.00 66.49           C  
ANISOU 2935  CG  LYS A 398     9492   7332   8441   -283  -1028    210       C  
ATOM   2936  CD  LYS A 398       6.922  25.689  26.833  1.00 75.04           C  
ANISOU 2936  CD  LYS A 398    10534   8514   9464   -267  -1121    187       C  
ATOM   2937  CE  LYS A 398       5.791  24.999  27.584  1.00 81.05           C  
ANISOU 2937  CE  LYS A 398    11179   9315  10301   -224  -1201    153       C  
ATOM   2938  NZ  LYS A 398       5.209  23.858  26.818  1.00 82.76           N1+
ANISOU 2938  NZ  LYS A 398    11353   9629  10463   -219  -1285    119       N1+
ATOM   2939  N   PRO A 399       7.283  28.955  30.945  1.00 54.57           N  
ANISOU 2939  N   PRO A 399     7907   5625   7204   -244   -910    213       N  
ATOM   2940  CA  PRO A 399       8.029  28.804  32.199  1.00 52.94           C  
ANISOU 2940  CA  PRO A 399     7631   5404   7079   -304   -837    143       C  
ATOM   2941  C   PRO A 399       8.963  27.596  32.171  1.00 48.23           C  
ANISOU 2941  C   PRO A 399     6990   4875   6459   -379   -814     68       C  
ATOM   2942  O   PRO A 399       8.603  26.548  31.637  1.00 45.67           O  
ANISOU 2942  O   PRO A 399     6632   4621   6098   -372   -884     50       O  
ATOM   2943  CB  PRO A 399       6.922  28.605  33.233  1.00 55.38           C  
ANISOU 2943  CB  PRO A 399     7833   5730   7480   -250   -898    125       C  
ATOM   2944  CG  PRO A 399       5.753  29.362  32.658  1.00 56.95           C  
ANISOU 2944  CG  PRO A 399     8077   5902   7658   -155   -966    202       C  
ATOM   2945  CD  PRO A 399       5.837  29.126  31.173  1.00 55.16           C  
ANISOU 2945  CD  PRO A 399     7934   5707   7316   -150  -1001    246       C  
ATOM   2946  N   ALA A 400      10.157  27.751  32.734  1.00 44.43           N  
ANISOU 2946  N   ALA A 400     6508   4375   5999   -450   -717     22       N  
ATOM   2947  CA  ALA A 400      11.136  26.671  32.750  1.00 43.53           C  
ANISOU 2947  CA  ALA A 400     6352   4323   5864   -516   -690    -51       C  
ATOM   2948  C   ALA A 400      11.183  26.010  34.117  1.00 42.64           C  
ANISOU 2948  C   ALA A 400     6120   4238   5842   -529   -685   -116       C  
ATOM   2949  O   ALA A 400      10.713  26.570  35.104  1.00 47.33           O  
ANISOU 2949  O   ALA A 400     6671   4799   6512   -505   -678   -110       O  
ATOM   2950  CB  ALA A 400      12.511  27.190  32.367  1.00 43.27           C  
ANISOU 2950  CB  ALA A 400     6394   4268   5779   -588   -586    -66       C  
ATOM   2951  N   ARG A 401      11.749  24.813  34.172  1.00 41.71           N  
ANISOU 2951  N   ARG A 401     5951   4182   5716   -565   -690   -177       N  
ATOM   2952  CA  ARG A 401      11.894  24.117  35.440  1.00 41.87           C  
ANISOU 2952  CA  ARG A 401     5863   4231   5813   -579   -684   -234       C  
ATOM   2953  C   ARG A 401      13.194  23.327  35.472  1.00 40.08           C  
ANISOU 2953  C   ARG A 401     5618   4048   5562   -637   -631   -303       C  
ATOM   2954  O   ARG A 401      13.794  23.057  34.432  1.00 40.45           O  
ANISOU 2954  O   ARG A 401     5722   4114   5532   -661   -621   -312       O  
ATOM   2955  CB  ARG A 401      10.692  23.204  35.714  1.00 40.20           C  
ANISOU 2955  CB  ARG A 401     5578   4055   5641   -535   -783   -233       C  
ATOM   2956  CG  ARG A 401      10.767  21.814  35.083  1.00 40.07           C  
ANISOU 2956  CG  ARG A 401     5545   4095   5587   -547   -834   -268       C  
ATOM   2957  CD  ARG A 401      10.629  21.855  33.569  1.00 40.86           C  
ANISOU 2957  CD  ARG A 401     5729   4203   5593   -537   -867   -237       C  
ATOM   2958  NE  ARG A 401      10.290  20.536  33.033  1.00 40.81           N  
ANISOU 2958  NE  ARG A 401     5693   4250   5564   -537   -935   -269       N  
ATOM   2959  CZ  ARG A 401      10.061  20.286  31.747  1.00 43.35           C  
ANISOU 2959  CZ  ARG A 401     6067   4598   5805   -529   -977   -256       C  
ATOM   2960  NH1 ARG A 401      10.136  21.270  30.860  1.00 43.51           N1+
ANISOU 2960  NH1 ARG A 401     6177   4599   5757   -519   -961   -203       N1+
ATOM   2961  NH2 ARG A 401       9.753  19.054  31.349  1.00 41.41           N  
ANISOU 2961  NH2 ARG A 401     5788   4400   5548   -534  -1035   -296       N  
ATOM   2962  N   ILE A 402      13.633  22.975  36.672  1.00 39.37           N  
ANISOU 2962  N   ILE A 402     5445   3979   5534   -655   -598   -351       N  
ATOM   2963  CA  ILE A 402      14.843  22.184  36.824  1.00 38.99           C  
ANISOU 2963  CA  ILE A 402     5367   3978   5469   -699   -553   -419       C  
ATOM   2964  C   ILE A 402      14.567  20.724  36.450  1.00 38.79           C  
ANISOU 2964  C   ILE A 402     5310   3996   5434   -683   -627   -442       C  
ATOM   2965  O   ILE A 402      13.514  20.181  36.774  1.00 39.82           O  
ANISOU 2965  O   ILE A 402     5394   4129   5608   -648   -700   -425       O  
ATOM   2966  CB  ILE A 402      15.407  22.291  38.253  1.00 38.38           C  
ANISOU 2966  CB  ILE A 402     5208   3916   5456   -718   -496   -462       C  
ATOM   2967  CG1 ILE A 402      15.683  23.764  38.604  1.00 38.65           C  
ANISOU 2967  CG1 ILE A 402     5277   3905   5503   -740   -417   -447       C  
ATOM   2968  CG2 ILE A 402      16.680  21.454  38.393  1.00 38.07           C  
ANISOU 2968  CG2 ILE A 402     5136   3934   5395   -753   -453   -532       C  
ATOM   2969  CD1 ILE A 402      16.106  23.987  40.042  1.00 38.12           C  
ANISOU 2969  CD1 ILE A 402     5124   3858   5500   -759   -362   -489       C  
ATOM   2970  N   GLU A 403      15.513  20.109  35.747  1.00 38.92           N  
ANISOU 2970  N   GLU A 403     5350   4045   5393   -712   -604   -486       N  
ATOM   2971  CA  GLU A 403      15.379  18.732  35.303  1.00 38.84           C  
ANISOU 2971  CA  GLU A 403     5318   4069   5371   -701   -665   -517       C  
ATOM   2972  C   GLU A 403      16.603  17.895  35.663  1.00 41.02           C  
ANISOU 2972  C   GLU A 403     5553   4385   5647   -726   -621   -591       C  
ATOM   2973  O   GLU A 403      17.656  18.431  36.023  1.00 38.43           O  
ANISOU 2973  O   GLU A 403     5223   4071   5309   -756   -541   -621       O  
ATOM   2974  CB  GLU A 403      15.188  18.671  33.785  1.00 39.54           C  
ANISOU 2974  CB  GLU A 403     5484   4164   5375   -702   -698   -501       C  
ATOM   2975  CG  GLU A 403      13.947  19.344  33.263  1.00 40.85           C  
ANISOU 2975  CG  GLU A 403     5691   4301   5528   -667   -754   -428       C  
ATOM   2976  CD  GLU A 403      13.752  19.077  31.788  1.00 50.33           C  
ANISOU 2976  CD  GLU A 403     6957   5525   6641   -666   -795   -418       C  
ATOM   2977  OE1 GLU A 403      14.050  19.975  30.975  1.00 47.14           O  
ANISOU 2977  OE1 GLU A 403     6633   5109   6168   -679   -762   -384       O  
ATOM   2978  OE2 GLU A 403      13.312  17.955  31.444  1.00 53.37           O1-
ANISOU 2978  OE2 GLU A 403     7313   5942   7025   -656   -859   -446       O1-
ATOM   2979  N   SER A 404      16.449  16.579  35.528  1.00 38.38           N  
ANISOU 2979  N   SER A 404     5188   4072   5324   -711   -674   -622       N  
ATOM   2980  CA  SER A 404      17.528  15.618  35.721  1.00 39.42           C  
ANISOU 2980  CA  SER A 404     5285   4239   5454   -720   -647   -692       C  
ATOM   2981  C   SER A 404      17.238  14.385  34.877  1.00 38.81           C  
ANISOU 2981  C   SER A 404     5220   4171   5357   -708   -710   -718       C  
ATOM   2982  O   SER A 404      16.080  14.078  34.594  1.00 39.53           O  
ANISOU 2982  O   SER A 404     5315   4243   5462   -690   -781   -685       O  
ATOM   2983  CB  SER A 404      17.643  15.211  37.190  1.00 43.28           C  
ANISOU 2983  CB  SER A 404     5690   4734   6020   -706   -638   -704       C  
ATOM   2984  OG  SER A 404      16.528  14.432  37.585  1.00 49.82           O  
ANISOU 2984  OG  SER A 404     6483   5542   6904   -678   -713   -678       O  
ATOM   2985  N   LEU A 405      18.290  13.676  34.484  1.00 38.60           N  
ANISOU 2985  N   LEU A 405     5193   4176   5297   -719   -683   -784       N  
ATOM   2986  CA  LEU A 405      18.158  12.528  33.601  1.00 38.94           C  
ANISOU 2986  CA  LEU A 405     5252   4228   5318   -711   -734   -822       C  
ATOM   2987  C   LEU A 405      18.561  11.250  34.323  1.00 38.66           C  
ANISOU 2987  C   LEU A 405     5159   4193   5338   -689   -745   -871       C  
ATOM   2988  O   LEU A 405      19.508  11.239  35.105  1.00 38.38           O  
ANISOU 2988  O   LEU A 405     5085   4178   5321   -685   -693   -901       O  
ATOM   2989  CB  LEU A 405      19.013  12.719  32.353  1.00 43.17           C  
ANISOU 2989  CB  LEU A 405     5843   4800   5760   -740   -698   -863       C  
ATOM   2990  CG  LEU A 405      18.734  14.017  31.597  1.00 47.82           C  
ANISOU 2990  CG  LEU A 405     6500   5386   6284   -764   -680   -809       C  
ATOM   2991  CD1 LEU A 405      19.713  14.197  30.445  1.00 49.98           C  
ANISOU 2991  CD1 LEU A 405     6826   5703   6461   -801   -634   -853       C  
ATOM   2992  CD2 LEU A 405      17.301  14.032  31.097  1.00 50.95           C  
ANISOU 2992  CD2 LEU A 405     6919   5758   6681   -743   -760   -751       C  
ATOM   2993  N   MET A 406      17.832  10.172  34.070  1.00 35.87           N  
ANISOU 2993  N   MET A 406     4573   3947   5110  -1124   -377   -284       N  
ATOM   2994  CA  MET A 406      18.107   8.921  34.762  1.00 35.51           C  
ANISOU 2994  CA  MET A 406     4476   4023   4994  -1110   -470   -277       C  
ATOM   2995  C   MET A 406      19.520   8.394  34.481  1.00 36.05           C  
ANISOU 2995  C   MET A 406     4404   4104   5191  -1159   -501   -239       C  
ATOM   2996  O   MET A 406      20.175   7.839  35.365  1.00 37.47           O  
ANISOU 2996  O   MET A 406     4524   4349   5365  -1183   -622   -272       O  
ATOM   2997  CB  MET A 406      17.060   7.871  34.398  1.00 38.12           C  
ANISOU 2997  CB  MET A 406     4855   4434   5193  -1016   -424   -211       C  
ATOM   2998  CG  MET A 406      16.986   7.569  32.919  1.00 43.30           C  
ANISOU 2998  CG  MET A 406     5492   5065   5897   -971   -304   -113       C  
ATOM   2999  SD  MET A 406      15.779   6.273  32.577  1.00 55.68           S  
ANISOU 2999  SD  MET A 406     7109   6730   7319   -869   -270    -54       S  
ATOM   3000  CE  MET A 406      16.475   4.929  33.514  1.00 31.92           C  
ANISOU 3000  CE  MET A 406     4031   3819   4277   -884   -388    -47       C  
ATOM   3001  N   GLN A 407      19.991   8.573  33.255  1.00 36.06           N  
ANISOU 3001  N   GLN A 407     4351   4046   5306  -1168   -391   -171       N  
ATOM   3002  CA  GLN A 407      21.319   8.090  32.888  1.00 42.05           C  
ANISOU 3002  CA  GLN A 407     4962   4818   6197  -1210   -398   -137       C  
ATOM   3003  C   GLN A 407      22.448   8.896  33.530  1.00 44.22           C  
ANISOU 3003  C   GLN A 407     5147   5042   6611  -1320   -477   -217       C  
ATOM   3004  O   GLN A 407      23.593   8.448  33.574  1.00 43.37           O  
ANISOU 3004  O   GLN A 407     4900   4967   6611  -1357   -525   -216       O  
ATOM   3005  CB  GLN A 407      21.491   8.061  31.364  1.00 48.43           C  
ANISOU 3005  CB  GLN A 407     5743   5583   7077  -1190   -242    -43       C  
ATOM   3006  CG  GLN A 407      21.403   9.419  30.685  1.00 51.87           C  
ANISOU 3006  CG  GLN A 407     6230   5890   7587  -1237   -134    -36       C  
ATOM   3007  CD  GLN A 407      19.979   9.808  30.300  1.00 52.20           C  
ANISOU 3007  CD  GLN A 407     6427   5900   7506  -1161    -69    -15       C  
ATOM   3008  NE2 GLN A 407      19.855  10.675  29.297  1.00 51.17           N  
ANISOU 3008  NE2 GLN A 407     6349   5667   7427  -1167     52     35       N  
ATOM   3009  OE1 GLN A 407      19.009   9.340  30.895  1.00 48.51           O  
ANISOU 3009  OE1 GLN A 407     6031   5500   6902  -1096   -126    -42       O  
ATOM   3010  N   ASP A 408      22.142  10.091  34.021  1.00 39.01           N  
ANISOU 3010  N   ASP A 408     4561   4302   5959  -1370   -494   -294       N  
ATOM   3011  CA  ASP A 408      23.189  10.897  34.633  1.00 45.43           C  
ANISOU 3011  CA  ASP A 408     5290   5060   6911  -1483   -574   -382       C  
ATOM   3012  C   ASP A 408      23.622  10.355  35.998  1.00 41.28           C  
ANISOU 3012  C   ASP A 408     4720   4630   6334  -1494   -761   -464       C  
ATOM   3013  O   ASP A 408      24.534  10.888  36.628  1.00 42.88           O  
ANISOU 3013  O   ASP A 408     4842   4807   6645  -1582   -859   -549       O  
ATOM   3014  CB  ASP A 408      22.807  12.383  34.682  1.00 47.27           C  
ANISOU 3014  CB  ASP A 408     5616   5158   7187  -1538   -534   -443       C  
ATOM   3015  CG  ASP A 408      23.075  13.092  33.358  1.00 52.17           C  
ANISOU 3015  CG  ASP A 408     6224   5658   7940  -1577   -370   -367       C  
ATOM   3016  OD1 ASP A 408      23.687  12.465  32.462  1.00 53.65           O  
ANISOU 3016  OD1 ASP A 408     6314   5875   8194  -1573   -291   -278       O  
ATOM   3017  OD2 ASP A 408      22.694  14.276  33.214  1.00 50.61           O1-
ANISOU 3017  OD2 ASP A 408     6117   5333   7779  -1610   -318   -394       O1-
ATOM   3018  N   ILE A 409      22.990   9.276  36.444  1.00 40.21           N  
ANISOU 3018  N   ILE A 409     4637   4604   6036  -1406   -814   -435       N  
ATOM   3019  CA  ILE A 409      23.479   8.598  37.637  1.00 41.53           C  
ANISOU 3019  CA  ILE A 409     4765   4868   6149  -1405   -989   -486       C  
ATOM   3020  C   ILE A 409      24.918   8.125  37.412  1.00 41.77           C  
ANISOU 3020  C   ILE A 409     4609   4919   6341  -1444  -1042   -471       C  
ATOM   3021  O   ILE A 409      25.658   7.897  38.364  1.00 42.88           O  
ANISOU 3021  O   ILE A 409     4682   5113   6496  -1470  -1203   -534       O  
ATOM   3022  CB  ILE A 409      22.588   7.410  38.055  1.00 44.15           C  
ANISOU 3022  CB  ILE A 409     5185   5307   6284  -1306  -1020   -435       C  
ATOM   3023  CG1 ILE A 409      23.000   6.924  39.445  1.00 47.35           C  
ANISOU 3023  CG1 ILE A 409     5585   5799   6607  -1310  -1210   -496       C  
ATOM   3024  CG2 ILE A 409      22.663   6.280  37.027  1.00 42.33           C  
ANISOU 3024  CG2 ILE A 409     4897   5111   6075  -1241   -937   -317       C  
ATOM   3025  CD1 ILE A 409      22.095   5.885  40.025  1.00 44.18           C  
ANISOU 3025  CD1 ILE A 409     5292   5492   6003  -1229  -1242   -451       C  
ATOM   3026  N   ALA A 410      25.315   8.003  36.148  1.00 41.46           N  
ANISOU 3026  N   ALA A 410     4487   4842   6424  -1445   -906   -391       N  
ATOM   3027  CA  ALA A 410      26.669   7.563  35.808  1.00 45.05           C  
ANISOU 3027  CA  ALA A 410     4752   5319   7048  -1478   -929   -376       C  
ATOM   3028  C   ALA A 410      27.738   8.507  36.354  1.00 46.74           C  
ANISOU 3028  C   ALA A 410     4851   5483   7423  -1597  -1018   -481       C  
ATOM   3029  O   ALA A 410      28.863   8.088  36.649  1.00 48.65           O  
ANISOU 3029  O   ALA A 410     4933   5773   7778  -1622  -1119   -510       O  
ATOM   3030  CB  ALA A 410      26.819   7.414  34.299  1.00 41.87           C  
ANISOU 3030  CB  ALA A 410     4295   4877   6735  -1462   -741   -278       C  
ATOM   3031  N   LEU A 411      27.387   9.782  36.484  1.00 47.83           N  
ANISOU 3031  N   LEU A 411     5069   5522   7581  -1670   -984   -542       N  
ATOM   3032  CA  LEU A 411      28.341  10.780  36.959  1.00 53.24           C  
ANISOU 3032  CA  LEU A 411     5655   6142   8432  -1796  -1060   -650       C  
ATOM   3033  C   LEU A 411      28.762  10.490  38.397  1.00 53.71           C  
ANISOU 3033  C   LEU A 411     5684   6286   8438  -1801  -1292   -756       C  
ATOM   3034  O   LEU A 411      29.769  11.005  38.874  1.00 57.72           O  
ANISOU 3034  O   LEU A 411     6067   6773   9091  -1896  -1396   -851       O  
ATOM   3035  CB  LEU A 411      27.762  12.195  36.832  1.00 54.38           C  
ANISOU 3035  CB  LEU A 411     5917   6148   8597  -1863   -978   -695       C  
ATOM   3036  CG  LEU A 411      27.310  12.599  35.425  1.00 54.35           C  
ANISOU 3036  CG  LEU A 411     5966   6049   8635  -1856   -757   -587       C  
ATOM   3037  CD1 LEU A 411      26.617  13.957  35.431  1.00 53.02           C  
ANISOU 3037  CD1 LEU A 411     5940   5741   8466  -1901   -699   -633       C  
ATOM   3038  CD2 LEU A 411      28.476  12.596  34.447  1.00 55.68           C  
ANISOU 3038  CD2 LEU A 411     5959   6186   9011  -1928   -654   -532       C  
ATOM   3039  N   LEU A 412      27.992   9.646  39.076  1.00 49.94           N  
ANISOU 3039  N   LEU A 412     5320   5905   7751  -1700  -1372   -737       N  
ATOM   3040  CA  LEU A 412      28.271   9.301  40.464  1.00 51.12           C  
ANISOU 3040  CA  LEU A 412     5473   6142   7808  -1689  -1591   -824       C  
ATOM   3041  C   LEU A 412      29.263   8.144  40.607  1.00 51.89           C  
ANISOU 3041  C   LEU A 412     5417   6338   7960  -1648  -1705   -789       C  
ATOM   3042  O   LEU A 412      29.626   7.778  41.721  1.00 52.76           O  
ANISOU 3042  O   LEU A 412     5518   6526   8003  -1632  -1901   -851       O  
ATOM   3043  CB  LEU A 412      26.968   8.963  41.195  1.00 51.74           C  
ANISOU 3043  CB  LEU A 412     5755   6278   7626  -1606  -1619   -818       C  
ATOM   3044  CG  LEU A 412      25.876  10.038  41.187  1.00 54.47           C  
ANISOU 3044  CG  LEU A 412     6260   6540   7897  -1624  -1521   -863       C  
ATOM   3045  CD1 LEU A 412      24.766   9.665  42.152  1.00 56.84           C  
ANISOU 3045  CD1 LEU A 412     6732   6918   7945  -1550  -1579   -882       C  
ATOM   3046  CD2 LEU A 412      26.447  11.406  41.540  1.00 56.16           C  
ANISOU 3046  CD2 LEU A 412     6439   6654   8246  -1741  -1571   -995       C  
ATOM   3047  N   PHE A 413      29.686   7.564  39.486  1.00 49.96           N  
ANISOU 3047  N   PHE A 413     5059   6091   7832  -1622  -1586   -693       N  
ATOM   3048  CA  PHE A 413      30.609   6.426  39.509  1.00 51.98           C  
ANISOU 3048  CA  PHE A 413     5164   6433   8153  -1568  -1679   -657       C  
ATOM   3049  C   PHE A 413      32.004   6.828  39.031  1.00 54.50           C  
ANISOU 3049  C   PHE A 413     5248   6722   8740  -1656  -1673   -700       C  
ATOM   3050  O   PHE A 413      32.263   6.852  37.828  1.00 57.47           O  
ANISOU 3050  O   PHE A 413     5539   7054   9243  -1671  -1497   -635       O  
ATOM   3051  CB  PHE A 413      30.106   5.295  38.604  1.00 46.52           C  
ANISOU 3051  CB  PHE A 413     4505   5774   7397  -1459  -1553   -522       C  
ATOM   3052  CG  PHE A 413      28.815   4.656  39.057  1.00 45.41           C  
ANISOU 3052  CG  PHE A 413     4568   5677   7009  -1368  -1564   -471       C  
ATOM   3053  CD1 PHE A 413      28.823   3.429  39.708  1.00 45.77           C  
ANISOU 3053  CD1 PHE A 413     4636   5812   6943  -1278  -1694   -432       C  
ATOM   3054  CD2 PHE A 413      27.593   5.267  38.805  1.00 43.78           C  
ANISOU 3054  CD2 PHE A 413     4526   5420   6688  -1372  -1440   -458       C  
ATOM   3055  CE1 PHE A 413      27.636   2.826  40.111  1.00 49.27           C  
ANISOU 3055  CE1 PHE A 413     5262   6292   7166  -1206  -1690   -379       C  
ATOM   3056  CE2 PHE A 413      26.401   4.669  39.207  1.00 46.53           C  
ANISOU 3056  CE2 PHE A 413     5044   5815   6821  -1295  -1440   -414       C  
ATOM   3057  CZ  PHE A 413      26.424   3.446  39.860  1.00 46.39           C  
ANISOU 3057  CZ  PHE A 413     5046   5884   6695  -1219  -1559   -374       C  
ATOM   3058  N   SER A 414      32.907   7.125  39.960  1.00 55.86           N  
ANISOU 3058  N   SER A 414     5309   6920   8995  -1714  -1864   -812       N  
ATOM   3059  CA  SER A 414      34.266   7.498  39.579  1.00 56.60           C  
ANISOU 3059  CA  SER A 414     5157   6991   9356  -1806  -1868   -865       C  
ATOM   3060  C   SER A 414      35.003   6.300  38.990  1.00 58.51           C  
ANISOU 3060  C   SER A 414     5235   7307   9690  -1722  -1855   -790       C  
ATOM   3061  O   SER A 414      34.760   5.161  39.386  1.00 58.70           O  
ANISOU 3061  O   SER A 414     5312   7414   9577  -1599  -1952   -739       O  
ATOM   3062  CB  SER A 414      35.041   8.041  40.780  1.00 58.44           C  
ANISOU 3062  CB  SER A 414     5306   7245   9652  -1881  -2100  -1015       C  
ATOM   3063  OG  SER A 414      35.309   7.009  41.714  1.00 59.36           O  
ANISOU 3063  OG  SER A 414     5409   7480   9665  -1781  -2317  -1024       O  
ATOM   3064  N   GLU A 415      35.902   6.557  38.047  1.00 62.57           N  
ANISOU 3064  N   GLU A 415     5552   7786  10435  -1788  -1730   -785       N  
ATOM   3065  CA  GLU A 415      36.695   5.488  37.448  1.00 71.64           C  
ANISOU 3065  CA  GLU A 415     6524   9003  11694  -1711  -1708   -730       C  
ATOM   3066  C   GLU A 415      37.601   4.818  38.477  1.00 72.58           C  
ANISOU 3066  C   GLU A 415     6501   9218  11857  -1662  -1971   -802       C  
ATOM   3067  O   GLU A 415      38.030   3.677  38.293  1.00 73.03           O  
ANISOU 3067  O   GLU A 415     6465   9345  11937  -1551  -2010   -753       O  
ATOM   3068  CB  GLU A 415      37.530   6.013  36.276  1.00 81.09           C  
ANISOU 3068  CB  GLU A 415     7527  10146  13137  -1806  -1513   -722       C  
ATOM   3069  CG  GLU A 415      36.829   5.939  34.921  1.00 80.62           C  
ANISOU 3069  CG  GLU A 415     7567  10035  13029  -1777  -1241   -600       C  
ATOM   3070  CD  GLU A 415      37.797   6.065  33.756  1.00 80.85           C  
ANISOU 3070  CD  GLU A 415     7386  10048  13287  -1835  -1056   -576       C  
ATOM   3071  OE1 GLU A 415      38.996   6.326  34.004  1.00 84.44           O  
ANISOU 3071  OE1 GLU A 415     7608  10520  13954  -1915  -1129   -662       O  
ATOM   3072  OE2 GLU A 415      37.361   5.899  32.594  1.00 73.48           O1-
ANISOU 3072  OE2 GLU A 415     6515   9086  12316  -1801   -838   -476       O1-
ATOM   3073  N   ASP A 416      37.887   5.528  39.563  1.00 71.68           N  
ANISOU 3073  N   ASP A 416     6378   9104  11751  -1739  -2158   -922       N  
ATOM   3074  CA  ASP A 416      38.764   5.002  40.601  1.00 75.76           C  
ANISOU 3074  CA  ASP A 416     6766   9713  12305  -1696  -2430  -1001       C  
ATOM   3075  C   ASP A 416      38.124   3.870  41.399  1.00 71.87           C  
ANISOU 3075  C   ASP A 416     6444   9300  11563  -1542  -2582   -941       C  
ATOM   3076  O   ASP A 416      38.804   2.928  41.807  1.00 73.19           O  
ANISOU 3076  O   ASP A 416     6503   9548  11758  -1447  -2748   -939       O  
ATOM   3077  CB  ASP A 416      39.215   6.119  41.545  1.00 83.57           C  
ANISOU 3077  CB  ASP A 416     7711  10680  13362  -1825  -2593  -1156       C  
ATOM   3078  CG  ASP A 416      40.198   7.071  40.891  1.00 90.37           C  
ANISOU 3078  CG  ASP A 416     8340  11475  14521  -1981  -2492  -1229       C  
ATOM   3079  OD1 ASP A 416      40.143   8.285  41.184  1.00 93.34           O  
ANISOU 3079  OD1 ASP A 416     8748  11772  14946  -2117  -2494  -1324       O  
ATOM   3080  OD2 ASP A 416      41.027   6.603  40.081  1.00 91.70           O1-
ANISOU 3080  OD2 ASP A 416     8294  11668  14879  -1968  -2403  -1194       O1-
ATOM   3081  N   ASP A 417      36.816   3.959  41.617  1.00 63.42           N  
ANISOU 3081  N   ASP A 417     5637   8205  10254  -1517  -2524   -890       N  
ATOM   3082  CA  ASP A 417      36.138   3.004  42.484  1.00 60.92           C  
ANISOU 3082  CA  ASP A 417     5500   7957   9688  -1392  -2664   -837       C  
ATOM   3083  C   ASP A 417      35.169   2.089  41.739  1.00 55.35           C  
ANISOU 3083  C   ASP A 417     4935   7245   8850  -1290  -2497   -691       C  
ATOM   3084  O   ASP A 417      34.648   1.136  42.317  1.00 54.29           O  
ANISOU 3084  O   ASP A 417     4936   7162   8530  -1183  -2590   -627       O  
ATOM   3085  CB  ASP A 417      35.397   3.743  43.600  1.00 63.21           C  
ANISOU 3085  CB  ASP A 417     5986   8244   9785  -1439  -2770   -912       C  
ATOM   3086  CG  ASP A 417      36.295   4.697  44.360  1.00 70.31           C  
ANISOU 3086  CG  ASP A 417     6763   9144  10809  -1546  -2942  -1071       C  
ATOM   3087  OD1 ASP A 417      35.838   5.814  44.680  1.00 73.05           O  
ANISOU 3087  OD1 ASP A 417     7209   9434  11114  -1643  -2918  -1153       O  
ATOM   3088  OD2 ASP A 417      37.459   4.332  44.632  1.00 71.07           O1-
ANISOU 3088  OD2 ASP A 417     6658   9295  11050  -1531  -3105  -1120       O1-
ATOM   3089  N   TYR A 418      34.924   2.376  40.463  1.00 54.41           N  
ANISOU 3089  N   TYR A 418     4790   7061   8822  -1323  -2252   -637       N  
ATOM   3090  CA  TYR A 418      33.945   1.607  39.696  1.00 55.30           C  
ANISOU 3090  CA  TYR A 418     5039   7162   8809  -1235  -2089   -512       C  
ATOM   3091  C   TYR A 418      34.319   1.410  38.232  1.00 55.91           C  
ANISOU 3091  C   TYR A 418     4986   7206   9051  -1229  -1879   -452       C  
ATOM   3092  O   TYR A 418      35.124   2.152  37.673  1.00 58.94           O  
ANISOU 3092  O   TYR A 418     5202   7554   9637  -1321  -1802   -501       O  
ATOM   3093  CB  TYR A 418      32.562   2.256  39.781  1.00 52.94           C  
ANISOU 3093  CB  TYR A 418     4974   6816   8323  -1267  -1987   -496       C  
ATOM   3094  CG  TYR A 418      32.006   2.321  41.181  1.00 54.81           C  
ANISOU 3094  CG  TYR A 418     5372   7095   8357  -1257  -2164   -543       C  
ATOM   3095  CD1 TYR A 418      31.399   1.215  41.755  1.00 53.79           C  
ANISOU 3095  CD1 TYR A 418     5379   7026   8034  -1149  -2244   -470       C  
ATOM   3096  CD2 TYR A 418      32.088   3.490  41.929  1.00 57.23           C  
ANISOU 3096  CD2 TYR A 418     5701   7379   8665  -1356  -2245   -660       C  
ATOM   3097  CE1 TYR A 418      30.889   1.265  43.037  1.00 54.24           C  
ANISOU 3097  CE1 TYR A 418     5590   7127   7892  -1141  -2393   -507       C  
ATOM   3098  CE2 TYR A 418      31.581   3.551  43.215  1.00 58.90           C  
ANISOU 3098  CE2 TYR A 418     6066   7637   8678  -1342  -2402   -709       C  
ATOM   3099  CZ  TYR A 418      30.980   2.434  43.762  1.00 55.97           C  
ANISOU 3099  CZ  TYR A 418     5830   7333   8103  -1234  -2471   -629       C  
ATOM   3100  OH  TYR A 418      30.469   2.482  45.039  1.00 55.23           O  
ANISOU 3100  OH  TYR A 418     5897   7291   7797  -1221  -2613   -672       O  
ATOM   3101  N   ARG A 419      33.715   0.396  37.622  1.00 54.68           N  
ANISOU 3101  N   ARG A 419     4912   7060   8803  -1124  -1785   -348       N  
ATOM   3102  CA  ARG A 419      33.881   0.128  36.199  1.00 52.45           C  
ANISOU 3102  CA  ARG A 419     4545   6751   8632  -1103  -1575   -287       C  
ATOM   3103  C   ARG A 419      32.566   0.378  35.467  1.00 46.01           C  
ANISOU 3103  C   ARG A 419     3924   5884   7675  -1102  -1384   -218       C  
ATOM   3104  O   ARG A 419      31.558  -0.273  35.735  1.00 44.67           O  
ANISOU 3104  O   ARG A 419     3926   5729   7317  -1028  -1403   -162       O  
ATOM   3105  CB  ARG A 419      34.353  -1.311  35.977  1.00 49.32           C  
ANISOU 3105  CB  ARG A 419     4066   6406   8267   -971  -1623   -234       C  
ATOM   3106  CG  ARG A 419      35.808  -1.551  36.388  1.00 51.83           C  
ANISOU 3106  CG  ARG A 419     4144   6773   8777   -963  -1779   -302       C  
ATOM   3107  CD  ARG A 419      36.134  -3.039  36.449  1.00 54.73           C  
ANISOU 3107  CD  ARG A 419     4469   7185   9139   -811  -1874   -252       C  
ATOM   3108  NE  ARG A 419      35.888  -3.714  35.179  1.00 52.97           N  
ANISOU 3108  NE  ARG A 419     4246   6942   8938   -743  -1675   -178       N  
ATOM   3109  CZ  ARG A 419      36.766  -3.769  34.183  1.00 52.63           C  
ANISOU 3109  CZ  ARG A 419     4004   6902   9090   -741  -1549   -193       C  
ATOM   3110  NH1 ARG A 419      37.951  -3.179  34.308  1.00 52.24           N1+
ANISOU 3110  NH1 ARG A 419     3727   6875   9246   -811  -1596   -277       N1+
ATOM   3111  NH2 ARG A 419      36.460  -4.409  33.061  1.00 49.30           N  
ANISOU 3111  NH2 ARG A 419     3608   6465   8660   -671  -1372   -129       N  
ATOM   3112  N   VAL A 420      32.583   1.341  34.552  1.00 45.93           N  
ANISOU 3112  N   VAL A 420     3883   5811   7757  -1187  -1204   -221       N  
ATOM   3113  CA  VAL A 420      31.395   1.702  33.793  1.00 44.24           C  
ANISOU 3113  CA  VAL A 420     3842   5544   7423  -1186  -1026   -160       C  
ATOM   3114  C   VAL A 420      31.694   1.507  32.321  1.00 46.49           C  
ANISOU 3114  C   VAL A 420     4046   5810   7810  -1168   -821   -100       C  
ATOM   3115  O   VAL A 420      32.655   2.072  31.795  1.00 46.93           O  
ANISOU 3115  O   VAL A 420     3940   5842   8049  -1243   -744   -127       O  
ATOM   3116  CB  VAL A 420      30.995   3.170  34.034  1.00 44.41           C  
ANISOU 3116  CB  VAL A 420     3943   5494   7437  -1301   -992   -212       C  
ATOM   3117  CG1 VAL A 420      29.702   3.501  33.295  1.00 42.72           C  
ANISOU 3117  CG1 VAL A 420     3914   5228   7090  -1281   -827   -148       C  
ATOM   3118  CG2 VAL A 420      30.854   3.440  35.524  1.00 44.98           C  
ANISOU 3118  CG2 VAL A 420     4079   5591   7422  -1326  -1199   -292       C  
ATOM   3119  N   GLY A 421      30.882   0.696  31.654  1.00 44.60           N  
ANISOU 3119  N   GLY A 421     3915   5580   7450  -1072   -730    -23       N  
ATOM   3120  CA  GLY A 421      31.148   0.379  30.268  1.00 43.36           C  
ANISOU 3120  CA  GLY A 421     3693   5416   7366  -1039   -544     30       C  
ATOM   3121  C   GLY A 421      29.917   0.379  29.395  1.00 42.01           C  
ANISOU 3121  C   GLY A 421     3700   5214   7047   -998   -393     99       C  
ATOM   3122  O   GLY A 421      28.816   0.727  29.833  1.00 39.65           O  
ANISOU 3122  O   GLY A 421     3570   4894   6600  -1002   -421    105       O  
ATOM   3123  N   GLY A 422      30.113  -0.011  28.142  1.00 43.03           N  
ANISOU 3123  N   GLY A 422     3786   5345   7217   -954   -232    146       N  
ATOM   3124  CA  GLY A 422      29.022  -0.111  27.198  1.00 42.03           C  
ANISOU 3124  CA  GLY A 422     3816   5198   6955   -903    -94    209       C  
ATOM   3125  C   GLY A 422      29.050  -1.453  26.498  1.00 40.06           C  
ANISOU 3125  C   GLY A 422     3546   4993   6682   -786    -53    244       C  
ATOM   3126  O   GLY A 422      30.118  -2.040  26.291  1.00 40.39           O  
ANISOU 3126  O   GLY A 422     3425   5069   6854   -759    -54    227       O  
ATOM   3127  N   THR A 423      27.868  -1.950  26.155  1.00 37.30           N  
ANISOU 3127  N   THR A 423     3357   4644   6173   -716    -22    284       N  
ATOM   3128  CA  THR A 423      27.750  -3.152  25.346  1.00 38.76           C  
ANISOU 3128  CA  THR A 423     3547   4858   6324   -609     34    313       C  
ATOM   3129  C   THR A 423      27.049  -2.762  24.055  1.00 36.21           C  
ANISOU 3129  C   THR A 423     3326   4510   5921   -595    215    355       C  
ATOM   3130  O   THR A 423      25.955  -2.200  24.078  1.00 35.23           O  
ANISOU 3130  O   THR A 423     3350   4359   5675   -611    229    374       O  
ATOM   3131  CB  THR A 423      26.957  -4.237  26.079  1.00 37.96           C  
ANISOU 3131  CB  THR A 423     3545   4776   6103   -534   -101    321       C  
ATOM   3132  CG2 THR A 423      26.826  -5.498  25.221  1.00 35.52           C  
ANISOU 3132  CG2 THR A 423     3245   4483   5768   -425    -45    344       C  
ATOM   3133  OG1 THR A 423      27.619  -4.555  27.310  1.00 42.26           O  
ANISOU 3133  OG1 THR A 423     4008   5341   6707   -543   -277    290       O  
ATOM   3134  N   VAL A 424      27.691  -3.048  22.928  1.00 36.89           N  
ANISOU 3134  N   VAL A 424     3332   4610   6072   -561    353    368       N  
ATOM   3135  CA  VAL A 424      27.179  -2.616  21.636  1.00 36.59           C  
ANISOU 3135  CA  VAL A 424     3388   4555   5960   -549    531    411       C  
ATOM   3136  C   VAL A 424      26.412  -3.737  20.955  1.00 35.65           C  
ANISOU 3136  C   VAL A 424     3363   4462   5721   -434    554    425       C  
ATOM   3137  O   VAL A 424      26.964  -4.812  20.714  1.00 37.88           O  
ANISOU 3137  O   VAL A 424     3563   4777   6052   -362    547    406       O  
ATOM   3138  CB  VAL A 424      28.318  -2.156  20.710  1.00 38.55           C  
ANISOU 3138  CB  VAL A 424     3505   4805   6338   -589    694    419       C  
ATOM   3139  CG1 VAL A 424      27.750  -1.659  19.393  1.00 41.94           C  
ANISOU 3139  CG1 VAL A 424     4054   5213   6666   -576    876    473       C  
ATOM   3140  CG2 VAL A 424      29.160  -1.071  21.390  1.00 41.41           C  
ANISOU 3140  CG2 VAL A 424     3754   5135   6844   -715    669    396       C  
ATOM   3141  N   PHE A 425      25.141  -3.479  20.655  1.00 34.50           N  
ANISOU 3141  N   PHE A 425     3386   4299   5425   -416    575    451       N  
ATOM   3142  CA  PHE A 425      24.273  -4.453  19.993  1.00 35.77           C  
ANISOU 3142  CA  PHE A 425     3647   4480   5464   -316    591    457       C  
ATOM   3143  C   PHE A 425      23.962  -4.006  18.569  1.00 37.51           C  
ANISOU 3143  C   PHE A 425     3945   4697   5611   -291    760    490       C  
ATOM   3144  O   PHE A 425      24.245  -2.877  18.195  1.00 37.75           O  
ANISOU 3144  O   PHE A 425     3976   4699   5667   -354    858    520       O  
ATOM   3145  CB  PHE A 425      22.958  -4.620  20.765  1.00 32.87           C  
ANISOU 3145  CB  PHE A 425     3409   4104   4974   -307    473    454       C  
ATOM   3146  CG  PHE A 425      23.127  -5.212  22.128  1.00 32.21           C  
ANISOU 3146  CG  PHE A 425     3282   4029   4929   -320    308    430       C  
ATOM   3147  CD1 PHE A 425      22.943  -6.575  22.335  1.00 31.86           C  
ANISOU 3147  CD1 PHE A 425     3243   4000   4861   -248    231    421       C  
ATOM   3148  CD2 PHE A 425      23.476  -4.417  23.206  1.00 32.50           C  
ANISOU 3148  CD2 PHE A 425     3278   4052   5018   -402    226    418       C  
ATOM   3149  CE1 PHE A 425      23.095  -7.132  23.594  1.00 31.89           C  
ANISOU 3149  CE1 PHE A 425     3222   4007   4888   -256     78    411       C  
ATOM   3150  CE2 PHE A 425      23.638  -4.970  24.472  1.00 32.53           C  
ANISOU 3150  CE2 PHE A 425     3253   4069   5039   -408     68    399       C  
ATOM   3151  CZ  PHE A 425      23.445  -6.332  24.662  1.00 32.23           C  
ANISOU 3151  CZ  PHE A 425     3229   4048   4970   -333     -4    402       C  
ATOM   3152  N   GLU A 426      23.379  -4.901  17.783  1.00 33.31           N  
ANISOU 3152  N   GLU A 426     3483   4190   4984   -197    790    485       N  
ATOM   3153  CA  GLU A 426      22.913  -4.570  16.441  1.00 37.00           C  
ANISOU 3153  CA  GLU A 426     4051   4662   5347   -157    930    513       C  
ATOM   3154  C   GLU A 426      21.844  -3.479  16.528  1.00 32.73           C  
ANISOU 3154  C   GLU A 426     3644   4086   4706   -194    921    547       C  
ATOM   3155  O   GLU A 426      21.020  -3.495  17.441  1.00 31.76           O  
ANISOU 3155  O   GLU A 426     3572   3952   4543   -207    798    531       O  
ATOM   3156  CB  GLU A 426      22.332  -5.829  15.774  1.00 38.96           C  
ANISOU 3156  CB  GLU A 426     4357   4941   5503    -49    922    484       C  
ATOM   3157  CG  GLU A 426      23.367  -6.927  15.520  1.00 46.68           C  
ANISOU 3157  CG  GLU A 426     5213   5948   6576      6    945    446       C  
ATOM   3158  CD  GLU A 426      22.744  -8.316  15.336  1.00 47.36           C  
ANISOU 3158  CD  GLU A 426     5351   6045   6598    101    877    402       C  
ATOM   3159  OE1 GLU A 426      21.849  -8.681  16.126  1.00 39.86           O  
ANISOU 3159  OE1 GLU A 426     4464   5078   5603     97    747    395       O  
ATOM   3160  OE2 GLU A 426      23.158  -9.045  14.403  1.00 45.06           O1-
ANISOU 3160  OE2 GLU A 426     5037   5778   6306    178    959    372       O1-
ATOM   3161  N   ARG A 427      21.851  -2.540  15.584  1.00 33.35           N  
ANISOU 3161  N   ARG A 427     3784   4144   4744   -207   1055    594       N  
ATOM   3162  CA  ARG A 427      20.840  -1.475  15.564  1.00 35.36           C  
ANISOU 3162  CA  ARG A 427     4173   4357   4906   -227   1050    628       C  
ATOM   3163  C   ARG A 427      19.410  -2.028  15.505  1.00 32.86           C  
ANISOU 3163  C   ARG A 427     3974   4062   4448   -148    965    605       C  
ATOM   3164  O   ARG A 427      18.480  -1.443  16.067  1.00 30.99           O  
ANISOU 3164  O   ARG A 427     3812   3800   4161   -165    893    605       O  
ATOM   3165  CB  ARG A 427      21.083  -0.513  14.393  1.00 36.67           C  
ANISOU 3165  CB  ARG A 427     4402   4495   5037   -236   1214    693       C  
ATOM   3166  CG  ARG A 427      22.381   0.292  14.497  1.00 39.49           C  
ANISOU 3166  CG  ARG A 427     4649   4816   5542   -338   1308    721       C  
ATOM   3167  CD  ARG A 427      22.570   1.219  13.290  1.00 44.93           C  
ANISOU 3167  CD  ARG A 427     5418   5471   6184   -350   1485    798       C  
ATOM   3168  NE  ARG A 427      21.396   2.051  13.039  1.00 47.73           N  
ANISOU 3168  NE  ARG A 427     5947   5776   6412   -325   1468    841       N  
ATOM   3169  CZ  ARG A 427      21.184   3.240  13.598  1.00 57.13           C  
ANISOU 3169  CZ  ARG A 427     7180   6884   7642   -398   1443    866       C  
ATOM   3170  NH1 ARG A 427      22.065   3.745  14.451  1.00 56.99           N1+
ANISOU 3170  NH1 ARG A 427     7045   6824   7783   -510   1429    850       N1+
ATOM   3171  NH2 ARG A 427      20.086   3.924  13.306  1.00 61.22           N  
ANISOU 3171  NH2 ARG A 427     7858   7360   8045   -356   1426    901       N  
ATOM   3172  N   PHE A 428      19.234  -3.160  14.829  1.00 31.54           N  
ANISOU 3172  N   PHE A 428     3818   3943   4224    -64    975    579       N  
ATOM   3173  CA  PHE A 428      17.915  -3.792  14.740  1.00 31.47           C  
ANISOU 3173  CA  PHE A 428     3905   3957   4096      4    893    548       C  
ATOM   3174  C   PHE A 428      17.277  -4.102  16.103  1.00 32.14           C  
ANISOU 3174  C   PHE A 428     3976   4036   4200    -30    744    514       C  
ATOM   3175  O   PHE A 428      16.058  -4.138  16.219  1.00 31.16           O  
ANISOU 3175  O   PHE A 428     3935   3919   3987     -3    682    497       O  
ATOM   3176  CB  PHE A 428      17.968  -5.062  13.877  1.00 32.85           C  
ANISOU 3176  CB  PHE A 428     4078   4175   4227     91    919    511       C  
ATOM   3177  CG  PHE A 428      16.643  -5.768  13.758  1.00 33.99           C  
ANISOU 3177  CG  PHE A 428     4310   4341   4264    153    833    470       C  
ATOM   3178  CD1 PHE A 428      15.666  -5.294  12.900  1.00 36.43           C  
ANISOU 3178  CD1 PHE A 428     4738   4661   4442    203    858    480       C  
ATOM   3179  CD2 PHE A 428      16.375  -6.904  14.511  1.00 30.34           C  
ANISOU 3179  CD2 PHE A 428     3808   3884   3834    158    724    422       C  
ATOM   3180  CE1 PHE A 428      14.444  -5.938  12.791  1.00 37.20           C  
ANISOU 3180  CE1 PHE A 428     4899   4781   4452    255    773    433       C  
ATOM   3181  CE2 PHE A 428      15.159  -7.558  14.404  1.00 32.47           C  
ANISOU 3181  CE2 PHE A 428     4149   4169   4019    201    651    382       C  
ATOM   3182  CZ  PHE A 428      14.189  -7.075  13.546  1.00 34.71           C  
ANISOU 3182  CZ  PHE A 428     4535   4470   4181    248    674    381       C  
ATOM   3183  N   SER A 429      18.094  -4.319  17.130  1.00 32.60           N  
ANISOU 3183  N   SER A 429     3930   4086   4372    -86    687    503       N  
ATOM   3184  CA  SER A 429      17.580  -4.669  18.459  1.00 28.86           C  
ANISOU 3184  CA  SER A 429     3450   3611   3906   -118    550    477       C  
ATOM   3185  C   SER A 429      16.969  -3.463  19.175  1.00 28.61           C  
ANISOU 3185  C   SER A 429     3470   3551   3850   -177    516    486       C  
ATOM   3186  O   SER A 429      16.365  -3.597  20.246  1.00 30.79           O  
ANISOU 3186  O   SER A 429     3761   3832   4107   -203    416    463       O  
ATOM   3187  CB  SER A 429      18.696  -5.263  19.326  1.00 29.27           C  
ANISOU 3187  CB  SER A 429     3379   3664   4078   -152    490    465       C  
ATOM   3188  OG  SER A 429      19.705  -4.294  19.591  1.00 36.11           O  
ANISOU 3188  OG  SER A 429     4170   4509   5043   -221    527    481       O  
ATOM   3189  N   TYR A 430      17.150  -2.286  18.589  1.00 29.06           N  
ANISOU 3189  N   TYR A 430     3559   3576   3908   -197    605    519       N  
ATOM   3190  CA  TYR A 430      16.636  -1.047  19.157  1.00 28.95           C  
ANISOU 3190  CA  TYR A 430     3599   3521   3881   -246    584    525       C  
ATOM   3191  C   TYR A 430      15.350  -0.682  18.422  1.00 28.57           C  
ANISOU 3191  C   TYR A 430     3674   3472   3709   -181    606    533       C  
ATOM   3192  O   TYR A 430      15.393  -0.257  17.269  1.00 29.10           O  
ANISOU 3192  O   TYR A 430     3794   3525   3736   -143    702    572       O  
ATOM   3193  CB  TYR A 430      17.695   0.050  19.007  1.00 29.98           C  
ANISOU 3193  CB  TYR A 430     3687   3598   4107   -315    664    558       C  
ATOM   3194  CG  TYR A 430      17.266   1.433  19.449  1.00 33.06           C  
ANISOU 3194  CG  TYR A 430     4141   3925   4495   -364    657    565       C  
ATOM   3195  CD1 TYR A 430      16.804   1.670  20.743  1.00 29.64           C  
ANISOU 3195  CD1 TYR A 430     3710   3486   4064   -403    546    519       C  
ATOM   3196  CD2 TYR A 430      17.354   2.506  18.577  1.00 32.99           C  
ANISOU 3196  CD2 TYR A 430     4195   3858   4481   -371    764    616       C  
ATOM   3197  CE1 TYR A 430      16.427   2.948  21.137  1.00 35.70           C  
ANISOU 3197  CE1 TYR A 430     4539   4191   4836   -442    541    514       C  
ATOM   3198  CE2 TYR A 430      16.984   3.775  18.961  1.00 37.93           C  
ANISOU 3198  CE2 TYR A 430     4884   4410   5115   -411    756    621       C  
ATOM   3199  CZ  TYR A 430      16.525   3.994  20.236  1.00 37.98           C  
ANISOU 3199  CZ  TYR A 430     4888   4412   5132   -445    643    564       C  
ATOM   3200  OH  TYR A 430      16.152   5.267  20.600  1.00 39.36           O  
ANISOU 3200  OH  TYR A 430     5129   4508   5317   -478    637    559       O  
ATOM   3201  N   GLN A 431      14.206  -0.855  19.084  1.00 27.77           N  
ANISOU 3201  N   GLN A 431     3617   3390   3546   -166    517    496       N  
ATOM   3202  CA  GLN A 431      12.920  -0.768  18.399  1.00 28.59           C  
ANISOU 3202  CA  GLN A 431     3816   3509   3537    -92    518    490       C  
ATOM   3203  C   GLN A 431      11.902   0.160  19.081  1.00 28.47           C  
ANISOU 3203  C   GLN A 431     3857   3472   3487   -102    468    468       C  
ATOM   3204  O   GLN A 431      10.749  -0.214  19.263  1.00 30.46           O  
ANISOU 3204  O   GLN A 431     4140   3762   3673    -63    412    430       O  
ATOM   3205  CB  GLN A 431      12.327  -2.182  18.207  1.00 30.70           C  
ANISOU 3205  CB  GLN A 431     4075   3835   3753    -40    471    453       C  
ATOM   3206  CG  GLN A 431      13.273  -3.163  17.483  1.00 33.44           C  
ANISOU 3206  CG  GLN A 431     4372   4200   4132    -15    519    462       C  
ATOM   3207  CD  GLN A 431      12.696  -4.575  17.312  1.00 36.73           C  
ANISOU 3207  CD  GLN A 431     4788   4659   4509     34    467    419       C  
ATOM   3208  NE2 GLN A 431      13.471  -5.452  16.679  1.00 31.62           N  
ANISOU 3208  NE2 GLN A 431     4102   4023   3890     65    506    416       N  
ATOM   3209  OE1 GLN A 431      11.574  -4.868  17.735  1.00 33.39           O  
ANISOU 3209  OE1 GLN A 431     4394   4255   4036     41    398    385       O  
ATOM   3210  N   PRO A 432      12.317   1.387  19.430  1.00 28.80           N  
ANISOU 3210  N   PRO A 432     3911   3452   3581   -152    492    487       N  
ATOM   3211  CA  PRO A 432      11.384   2.275  20.128  1.00 28.18           C  
ANISOU 3211  CA  PRO A 432     3885   3348   3476   -156    445    456       C  
ATOM   3212  C   PRO A 432      10.240   2.732  19.226  1.00 29.52           C  
ANISOU 3212  C   PRO A 432     4149   3513   3554    -64    462    464       C  
ATOM   3213  O   PRO A 432      10.414   2.867  18.012  1.00 28.04           O  
ANISOU 3213  O   PRO A 432     4008   3312   3332    -15    530    514       O  
ATOM   3214  CB  PRO A 432      12.258   3.485  20.483  1.00 28.27           C  
ANISOU 3214  CB  PRO A 432     3890   3277   3574   -229    479    477       C  
ATOM   3215  CG  PRO A 432      13.284   3.525  19.387  1.00 28.98           C  
ANISOU 3215  CG  PRO A 432     3967   3341   3701   -232    580    542       C  
ATOM   3216  CD  PRO A 432      13.582   2.068  19.090  1.00 29.53           C  
ANISOU 3216  CD  PRO A 432     3975   3489   3758   -205    573    535       C  
ATOM   3217  N   VAL A 433       9.078   2.954  19.834  1.00 27.88           N  
ANISOU 3217  N   VAL A 433     3966   3322   3304    -40    399    413       N  
ATOM   3218  CA  VAL A 433       7.958   3.598  19.170  1.00 27.42           C  
ANISOU 3218  CA  VAL A 433     3991   3254   3175     49    398    411       C  
ATOM   3219  C   VAL A 433       7.863   5.000  19.767  1.00 28.86           C  
ANISOU 3219  C   VAL A 433     4215   3355   3397     26    397    404       C  
ATOM   3220  O   VAL A 433       7.406   5.174  20.892  1.00 31.61           O  
ANISOU 3220  O   VAL A 433     4540   3713   3758     -4    344    343       O  
ATOM   3221  CB  VAL A 433       6.639   2.822  19.399  1.00 27.97           C  
ANISOU 3221  CB  VAL A 433     4044   3404   3180     99    329    346       C  
ATOM   3222  CG1 VAL A 433       5.438   3.627  18.879  1.00 27.57           C  
ANISOU 3222  CG1 VAL A 433     4063   3342   3070    194    312    330       C  
ATOM   3223  CG2 VAL A 433       6.701   1.451  18.742  1.00 26.45           C  
ANISOU 3223  CG2 VAL A 433     3819   3277   2954    122    328    347       C  
ATOM   3224  N   LYS A 434       8.320   6.001  19.028  1.00 29.17           N  
ANISOU 3224  N   LYS A 434     4322   3309   3453     37    460    466       N  
ATOM   3225  CA  LYS A 434       8.434   7.329  19.606  1.00 40.46           C  
ANISOU 3225  CA  LYS A 434     5792   4641   4942      1    464    462       C  
ATOM   3226  C   LYS A 434       8.053   8.469  18.665  1.00 38.32           C  
ANISOU 3226  C   LYS A 434     5636   4280   4643     74    504    517       C  
ATOM   3227  O   LYS A 434       7.817   9.572  19.127  1.00 33.66           O  
ANISOU 3227  O   LYS A 434     5094   3605   4091     70    492    500       O  
ATOM   3228  CB  LYS A 434       9.836   7.547  20.194  1.00 47.15           C  
ANISOU 3228  CB  LYS A 434     6581   5440   5896   -119    495    476       C  
ATOM   3229  CG  LYS A 434      10.974   7.304  19.220  1.00 52.76           C  
ANISOU 3229  CG  LYS A 434     7276   6135   6637   -146    584    556       C  
ATOM   3230  CD  LYS A 434      12.338   7.472  19.885  1.00 57.81           C  
ANISOU 3230  CD  LYS A 434     7831   6737   7398   -267    604    557       C  
ATOM   3231  CE  LYS A 434      13.463   7.273  18.867  1.00 64.70           C  
ANISOU 3231  CE  LYS A 434     8678   7598   8309   -293    710    633       C  
ATOM   3232  NZ  LYS A 434      14.831   7.518  19.415  1.00 66.45           N1+
ANISOU 3232  NZ  LYS A 434     8803   7780   8665   -412    735    633       N1+
ATOM   3233  N   ASN A 435       7.974   8.203  17.361  1.00 34.46           N  
ANISOU 3233  N   ASN A 435     5202   3808   4083    146    548    581       N  
ATOM   3234  CA  ASN A 435       7.616   9.240  16.395  1.00 31.66           C  
ANISOU 3234  CA  ASN A 435     4974   3370   3686    225    584    648       C  
ATOM   3235  C   ASN A 435       6.237   9.030  15.789  1.00 32.31           C  
ANISOU 3235  C   ASN A 435     5107   3509   3659    363    520    624       C  
ATOM   3236  O   ASN A 435       5.768   7.901  15.667  1.00 30.81           O  
ANISOU 3236  O   ASN A 435     4861   3431   3414    395    478    579       O  
ATOM   3237  CB  ASN A 435       8.646   9.313  15.262  1.00 34.98           C  
ANISOU 3237  CB  ASN A 435     5440   3752   4097    206    694    754       C  
ATOM   3238  CG  ASN A 435      10.027   9.699  15.750  1.00 37.17           C  
ANISOU 3238  CG  ASN A 435     5664   3960   4498     71    765    782       C  
ATOM   3239  ND2 ASN A 435      11.047   9.012  15.247  1.00 32.97           N  
ANISOU 3239  ND2 ASN A 435     5078   3468   3981     23    840    822       N  
ATOM   3240  OD1 ASN A 435      10.174  10.595  16.579  1.00 40.48           O  
ANISOU 3240  OD1 ASN A 435     6085   4292   5003     10    748    759       O  
ATOM   3241  N   SER A 436       5.593  10.123  15.400  1.00 32.47           N  
ANISOU 3241  N   SER A 436     5234   3450   3655    445    508    652       N  
ATOM   3242  CA  SER A 436       4.345  10.031  14.667  1.00 32.69           C  
ANISOU 3242  CA  SER A 436     5315   3525   3579    588    444    638       C  
ATOM   3243  C   SER A 436       4.628   9.638  13.221  1.00 33.21           C  
ANISOU 3243  C   SER A 436     5455   3619   3546    646    493    722       C  
ATOM   3244  O   SER A 436       5.758   9.750  12.740  1.00 33.68           O  
ANISOU 3244  O   SER A 436     5546   3632   3620    583    592    806       O  
ATOM   3245  CB  SER A 436       3.613  11.366  14.696  1.00 34.24           C  
ANISOU 3245  CB  SER A 436     5607   3617   3784    669    411    644       C  
ATOM   3246  OG  SER A 436       4.329  12.327  13.937  1.00 41.38           O  
ANISOU 3246  OG  SER A 436     6636   4395   4693    666    490    761       O  
ATOM   3247  N   LEU A 437       3.591   9.185  12.528  1.00 35.53           N  
ANISOU 3247  N   LEU A 437     5772   3991   3737    767    423    695       N  
ATOM   3248  CA  LEU A 437       3.703   8.834  11.116  1.00 35.65           C  
ANISOU 3248  CA  LEU A 437     5872   4040   3633    842    454    763       C  
ATOM   3249  C   LEU A 437       4.300   9.992  10.321  1.00 35.70           C  
ANISOU 3249  C   LEU A 437     6028   3923   3615    860    539    893       C  
ATOM   3250  O   LEU A 437       5.211   9.800   9.513  1.00 40.14           O  
ANISOU 3250  O   LEU A 437     6637   4480   4134    831    638    975       O  
ATOM   3251  CB  LEU A 437       2.326   8.469  10.562  1.00 40.95           C  
ANISOU 3251  CB  LEU A 437     6560   4797   4205    983    341    705       C  
ATOM   3252  CG  LEU A 437       2.140   7.055  10.008  1.00 49.51           C  
ANISOU 3252  CG  LEU A 437     7586   6012   5213   1005    311    654       C  
ATOM   3253  CD1 LEU A 437       2.996   6.050  10.764  1.00 46.71           C  
ANISOU 3253  CD1 LEU A 437     7108   5700   4939    871    358    615       C  
ATOM   3254  CD2 LEU A 437       0.670   6.661  10.041  1.00 46.58           C  
ANISOU 3254  CD2 LEU A 437     7168   5728   4804   1103    179    551       C  
ATOM   3255  N   GLU A 438       3.784  11.195  10.559  1.00 36.13           N  
ANISOU 3255  N   GLU A 438     6157   3872   3698    909    507    912       N  
ATOM   3256  CA  GLU A 438       4.272  12.393   9.872  1.00 44.93           C  
ANISOU 3256  CA  GLU A 438     7427   4846   4799    925    584   1041       C  
ATOM   3257  C   GLU A 438       5.759  12.634  10.112  1.00 44.57           C  
ANISOU 3257  C   GLU A 438     7363   4723   4849    768    720   1107       C  
ATOM   3258  O   GLU A 438       6.513  12.883   9.173  1.00 44.58           O  
ANISOU 3258  O   GLU A 438     7458   4679   4802    754    827   1222       O  
ATOM   3259  CB  GLU A 438       3.468  13.634  10.286  1.00 49.40           C  
ANISOU 3259  CB  GLU A 438     8065   5298   5409    996    517   1033       C  
ATOM   3260  CG  GLU A 438       2.487  14.111   9.228  1.00 67.05           C  
ANISOU 3260  CG  GLU A 438    10440   7517   7518   1175    449   1083       C  
ATOM   3261  CD  GLU A 438       2.133  15.584   9.378  1.00 80.32           C  
ANISOU 3261  CD  GLU A 438    12240   9031   9249   1234    428   1130       C  
ATOM   3262  OE1 GLU A 438       1.838  16.234   8.350  1.00 85.35           O  
ANISOU 3262  OE1 GLU A 438    13040   9599   9789   1351    420   1232       O  
ATOM   3263  OE2 GLU A 438       2.150  16.090  10.522  1.00 81.63           O1-
ANISOU 3263  OE2 GLU A 438    12341   9128   9545   1167    418   1063       O1-
ATOM   3264  N   GLU A 439       6.175  12.571  11.373  1.00 40.25           N  
ANISOU 3264  N   GLU A 439     6693   4165   4435    650    715   1034       N  
ATOM   3265  CA  GLU A 439       7.584  12.720  11.715  1.00 42.19           C  
ANISOU 3265  CA  GLU A 439     6890   4350   4788    495    826   1076       C  
ATOM   3266  C   GLU A 439       8.428  11.638  11.042  1.00 39.14           C  
ANISOU 3266  C   GLU A 439     6453   4063   4357    456    907   1107       C  
ATOM   3267  O   GLU A 439       9.478  11.926  10.463  1.00 39.79           O  
ANISOU 3267  O   GLU A 439     6571   4090   4457    390   1033   1200       O  
ATOM   3268  CB  GLU A 439       7.778  12.678  13.235  1.00 43.26           C  
ANISOU 3268  CB  GLU A 439     6895   4483   5057    390    779    972       C  
ATOM   3269  CG  GLU A 439       7.249  13.908  13.955  1.00 46.94           C  
ANISOU 3269  CG  GLU A 439     7415   4826   5592    403    729    943       C  
ATOM   3270  CD  GLU A 439       7.140  13.708  15.458  1.00 50.03           C  
ANISOU 3270  CD  GLU A 439     7683   5251   6075    330    660    818       C  
ATOM   3271  OE1 GLU A 439       7.284  14.698  16.205  1.00 51.27           O  
ANISOU 3271  OE1 GLU A 439     7860   5293   6326    280    654    793       O  
ATOM   3272  OE2 GLU A 439       6.904  12.562  15.894  1.00 46.77           O1-
ANISOU 3272  OE2 GLU A 439     7161   4975   5636    323    611    743       O1-
ATOM   3273  N   ALA A 440       7.971  10.392  11.111  1.00 38.64           N  
ANISOU 3273  N   ALA A 440     6302   4140   4239    494    840   1026       N  
ATOM   3274  CA  ALA A 440       8.719   9.295  10.498  1.00 40.25           C  
ANISOU 3274  CA  ALA A 440     6453   4436   4402    469    908   1039       C  
ATOM   3275  C   ALA A 440       8.970   9.562   9.017  1.00 39.17           C  
ANISOU 3275  C   ALA A 440     6456   4282   4145    535   1002   1152       C  
ATOM   3276  O   ALA A 440      10.071   9.335   8.510  1.00 42.55           O  
ANISOU 3276  O   ALA A 440     6872   4713   4582    471   1127   1210       O  
ATOM   3277  CB  ALA A 440       7.993   7.966  10.691  1.00 41.15           C  
ANISOU 3277  CB  ALA A 440     6480   4690   4466    519    809    935       C  
ATOM   3278  N   ALA A 441       7.942  10.039   8.325  1.00 37.43           N  
ANISOU 3278  N   ALA A 441     6366   4048   3808    666    944   1180       N  
ATOM   3279  CA  ALA A 441       8.053  10.369   6.908  1.00 45.62           C  
ANISOU 3279  CA  ALA A 441     7563   5067   4706    745   1020   1294       C  
ATOM   3280  C   ALA A 441       9.202  11.345   6.659  1.00 52.57           C  
ANISOU 3280  C   ALA A 441     8511   5818   5646    648   1176   1419       C  
ATOM   3281  O   ALA A 441      10.051  11.117   5.797  1.00 52.58           O  
ANISOU 3281  O   ALA A 441     8548   5839   5591    622   1307   1494       O  
ATOM   3282  CB  ALA A 441       6.742  10.951   6.394  1.00 46.58           C  
ANISOU 3282  CB  ALA A 441     7816   5169   4713    902    912   1307       C  
ATOM   3283  N   GLY A 442       9.219  12.435   7.417  1.00 52.34           N  
ANISOU 3283  N   GLY A 442     8497   5657   5734    593   1167   1435       N  
ATOM   3284  CA  GLY A 442      10.293  13.406   7.319  1.00 50.92           C  
ANISOU 3284  CA  GLY A 442     8368   5340   5641    482   1309   1543       C  
ATOM   3285  C   GLY A 442      11.643  12.782   7.626  1.00 49.51           C  
ANISOU 3285  C   GLY A 442     8042   5203   5568    333   1419   1528       C  
ATOM   3286  O   GLY A 442      12.617  13.015   6.913  1.00 51.66           O  
ANISOU 3286  O   GLY A 442     8353   5438   5837    271   1574   1628       O  
ATOM   3287  N   LEU A 443      11.704  11.983   8.687  1.00 40.78           N  
ANISOU 3287  N   LEU A 443     6764   4175   4554    279   1341   1405       N  
ATOM   3288  CA  LEU A 443      12.957  11.357   9.095  1.00 44.67           C  
ANISOU 3288  CA  LEU A 443     7102   4710   5161    148   1422   1379       C  
ATOM   3289  C   LEU A 443      13.506  10.444   8.001  1.00 54.81           C  
ANISOU 3289  C   LEU A 443     8383   6096   6344    177   1524   1416       C  
ATOM   3290  O   LEU A 443      14.679  10.534   7.632  1.00 62.83           O  
ANISOU 3290  O   LEU A 443     9365   7091   7414     88   1672   1477       O  
ATOM   3291  CB  LEU A 443      12.780  10.590  10.414  1.00 45.28           C  
ANISOU 3291  CB  LEU A 443     7015   4860   5330    107   1299   1243       C  
ATOM   3292  CG  LEU A 443      12.727  11.468  11.669  1.00 47.57           C  
ANISOU 3292  CG  LEU A 443     7269   5049   5755     29   1236   1197       C  
ATOM   3293  CD1 LEU A 443      12.246  10.696  12.888  1.00 38.60           C  
ANISOU 3293  CD1 LEU A 443     6008   3998   4660     22   1101   1067       C  
ATOM   3294  CD2 LEU A 443      14.095  12.096  11.933  1.00 51.05           C  
ANISOU 3294  CD2 LEU A 443     7653   5396   6346   -124   1348   1242       C  
ATOM   3295  N   VAL A 444      12.653   9.573   7.475  1.00 54.62           N  
ANISOU 3295  N   VAL A 444     8391   6184   6178    302   1448   1372       N  
ATOM   3296  CA  VAL A 444      13.060   8.674   6.405  1.00 55.01           C  
ANISOU 3296  CA  VAL A 444     8452   6334   6116    347   1533   1392       C  
ATOM   3297  C   VAL A 444      13.607   9.470   5.218  1.00 52.96           C  
ANISOU 3297  C   VAL A 444     8341   6009   5774    351   1696   1535       C  
ATOM   3298  O   VAL A 444      14.627   9.106   4.638  1.00 56.67           O  
ANISOU 3298  O   VAL A 444     8776   6515   6241    302   1842   1573       O  
ATOM   3299  CB  VAL A 444      11.903   7.757   5.955  1.00 52.58           C  
ANISOU 3299  CB  VAL A 444     8181   6139   5656    490   1411   1320       C  
ATOM   3300  CG1 VAL A 444      12.310   6.938   4.734  1.00 54.87           C  
ANISOU 3300  CG1 VAL A 444     8511   6523   5814    546   1504   1341       C  
ATOM   3301  CG2 VAL A 444      11.475   6.842   7.104  1.00 46.34           C  
ANISOU 3301  CG2 VAL A 444     7237   5417   4952    470   1275   1185       C  
ATOM   3302  N   ALA A 445      12.938  10.565   4.875  1.00 55.56           N  
ANISOU 3302  N   ALA A 445     8834   6239   6037    409   1675   1616       N  
ATOM   3303  CA  ALA A 445      13.390  11.427   3.783  1.00 61.60           C  
ANISOU 3303  CA  ALA A 445     9765   6924   6717    412   1828   1770       C  
ATOM   3304  C   ALA A 445      14.821  11.925   3.990  1.00 69.52           C  
ANISOU 3304  C   ALA A 445    10695   7846   7875    242   2003   1834       C  
ATOM   3305  O   ALA A 445      15.511  12.267   3.030  1.00 74.08           O  
ANISOU 3305  O   ALA A 445    11362   8395   8389    217   2174   1951       O  
ATOM   3306  CB  ALA A 445      12.438  12.604   3.602  1.00 59.38           C  
ANISOU 3306  CB  ALA A 445     9664   6524   6374    496   1757   1843       C  
ATOM   3307  N   GLN A 446      15.261  11.965   5.244  1.00 73.32           N  
ANISOU 3307  N   GLN A 446    11011   8292   8554    124   1961   1756       N  
ATOM   3308  CA  GLN A 446      16.600  12.438   5.578  1.00 73.82           C  
ANISOU 3308  CA  GLN A 446    10979   8280   8791    -46   2103   1797       C  
ATOM   3309  C   GLN A 446      17.545  11.277   5.849  1.00 68.49           C  
ANISOU 3309  C   GLN A 446    10100   7727   8196   -112   2148   1714       C  
ATOM   3310  O   GLN A 446      18.662  11.477   6.328  1.00 68.60           O  
ANISOU 3310  O   GLN A 446     9983   7702   8379   -254   2235   1713       O  
ATOM   3311  CB  GLN A 446      16.552  13.338   6.809  1.00 79.25           C  
ANISOU 3311  CB  GLN A 446    11619   8840   9654   -139   2022   1761       C  
ATOM   3312  CG  GLN A 446      15.622  14.521   6.676  1.00 87.46           C  
ANISOU 3312  CG  GLN A 446    12847   9743  10641    -71   1966   1828       C  
ATOM   3313  CD  GLN A 446      15.392  15.218   7.999  1.00 92.66           C  
ANISOU 3313  CD  GLN A 446    13448  10298  11459   -138   1855   1754       C  
ATOM   3314  NE2 GLN A 446      15.592  14.491   9.095  1.00 88.72           N  
ANISOU 3314  NE2 GLN A 446    12763   9880  11066   -194   1767   1623       N  
ATOM   3315  OE1 GLN A 446      15.035  16.395   8.038  1.00 98.78           O  
ANISOU 3315  OE1 GLN A 446    14352  10921  12260   -134   1846   1813       O  
ATOM   3316  N   GLY A 447      17.090  10.064   5.556  1.00 63.86           N  
ANISOU 3316  N   GLY A 447     9485   7283   7497     -7   2081   1641       N  
ATOM   3317  CA  GLY A 447      17.899   8.880   5.769  1.00 62.24           C  
ANISOU 3317  CA  GLY A 447     9098   7191   7358    -46   2111   1559       C  
ATOM   3318  C   GLY A 447      18.006   8.477   7.227  1.00 65.04           C  
ANISOU 3318  C   GLY A 447     9274   7557   7881   -116   1978   1442       C  
ATOM   3319  O   GLY A 447      18.931   7.763   7.618  1.00 66.46           O  
ANISOU 3319  O   GLY A 447     9286   7794   8172   -183   2010   1387       O  
ATOM   3320  N   ASN A 448      17.061   8.934   8.041  1.00 62.22           N  
ANISOU 3320  N   ASN A 448     8955   7148   7539    -95   1828   1404       N  
ATOM   3321  CA  ASN A 448      17.035   8.559   9.451  1.00 61.75           C  
ANISOU 3321  CA  ASN A 448     8747   7104   7610   -151   1694   1294       C  
ATOM   3322  C   ASN A 448      15.946   7.529   9.741  1.00 55.35           C  
ANISOU 3322  C   ASN A 448     7927   6396   6709    -44   1540   1199       C  
ATOM   3323  O   ASN A 448      14.995   7.393   8.973  1.00 56.70           O  
ANISOU 3323  O   ASN A 448     8220   6600   6724     75   1508   1215       O  
ATOM   3324  CB  ASN A 448      16.859   9.796  10.337  1.00 63.86           C  
ANISOU 3324  CB  ASN A 448     9041   7240   7983   -224   1643   1300       C  
ATOM   3325  CG  ASN A 448      18.019  10.772  10.211  1.00 69.54           C  
ANISOU 3325  CG  ASN A 448     9744   7849   8829   -357   1789   1379       C  
ATOM   3326  ND2 ASN A 448      17.805  11.865   9.481  1.00 66.12           N  
ANISOU 3326  ND2 ASN A 448     9476   7306   8343   -345   1870   1488       N  
ATOM   3327  OD1 ASN A 448      19.094  10.543  10.764  1.00 73.56           O  
ANISOU 3327  OD1 ASN A 448    10094   8370   9485   -469   1825   1343       O  
ATOM   3328  N   GLY A 449      16.098   6.804  10.847  1.00 49.59           N  
ANISOU 3328  N   GLY A 449     7052   5714   6075    -88   1443   1103       N  
ATOM   3329  CA  GLY A 449      15.121   5.812  11.260  1.00 47.03           C  
ANISOU 3329  CA  GLY A 449     6706   5478   5687     -9   1302   1014       C  
ATOM   3330  C   GLY A 449      13.774   6.420  11.613  1.00 46.90           C  
ANISOU 3330  C   GLY A 449     6787   5426   5609     52   1190    995       C  
ATOM   3331  O   GLY A 449      13.704   7.485  12.227  1.00 47.82           O  
ANISOU 3331  O   GLY A 449     6928   5447   5793      1   1173   1009       O  
ATOM   3332  N   ALA A 450      12.701   5.735  11.228  1.00 40.19           N  
ANISOU 3332  N   ALA A 450     5984   4650   4636    162   1112    955       N  
ATOM   3333  CA  ALA A 450      11.351   6.233  11.455  1.00 41.66           C  
ANISOU 3333  CA  ALA A 450     6251   4819   4760    236   1006    929       C  
ATOM   3334  C   ALA A 450      10.940   6.129  12.926  1.00 36.21           C  
ANISOU 3334  C   ALA A 450     5469   4133   4158    185    893    841       C  
ATOM   3335  O   ALA A 450      10.346   7.055  13.478  1.00 37.53           O  
ANISOU 3335  O   ALA A 450     5679   4234   4346    188    844    831       O  
ATOM   3336  CB  ALA A 450      10.355   5.492  10.566  1.00 37.99           C  
ANISOU 3336  CB  ALA A 450     5848   4440   4145    365    954    904       C  
ATOM   3337  N   TYR A 451      11.255   4.995  13.541  1.00 33.59           N  
ANISOU 3337  N   TYR A 451     5017   3875   3870    145    854    777       N  
ATOM   3338  CA  TYR A 451      10.916   4.723  14.942  1.00 30.36           C  
ANISOU 3338  CA  TYR A 451     4525   3485   3527     96    752    697       C  
ATOM   3339  C   TYR A 451       9.478   5.112  15.293  1.00 29.98           C  
ANISOU 3339  C   TYR A 451     4531   3439   3421    162    659    651       C  
ATOM   3340  O   TYR A 451       9.227   5.755  16.308  1.00 31.69           O  
ANISOU 3340  O   TYR A 451     4734   3614   3692    121    613    616       O  
ATOM   3341  CB  TYR A 451      11.926   5.385  15.888  1.00 30.65           C  
ANISOU 3341  CB  TYR A 451     4497   3452   3697    -23    774    703       C  
ATOM   3342  CG  TYR A 451      13.341   4.886  15.661  1.00 33.57           C  
ANISOU 3342  CG  TYR A 451     4780   3834   4142    -90    854    732       C  
ATOM   3343  CD1 TYR A 451      13.641   3.530  15.766  1.00 33.17           C  
ANISOU 3343  CD1 TYR A 451     4641   3869   4095    -84    828    693       C  
ATOM   3344  CD2 TYR A 451      14.371   5.762  15.333  1.00 38.05           C  
ANISOU 3344  CD2 TYR A 451     5350   4323   4785   -158    958    796       C  
ATOM   3345  CE1 TYR A 451      14.923   3.064  15.547  1.00 35.82           C  
ANISOU 3345  CE1 TYR A 451     4887   4217   4505   -132    899    712       C  
ATOM   3346  CE2 TYR A 451      15.663   5.300  15.114  1.00 40.26           C  
ANISOU 3346  CE2 TYR A 451     5532   4621   5143   -218   1037    816       C  
ATOM   3347  CZ  TYR A 451      15.930   3.948  15.223  1.00 43.76           C  
ANISOU 3347  CZ  TYR A 451     5884   5157   5588   -198   1005    771       C  
ATOM   3348  OH  TYR A 451      17.203   3.469  15.013  1.00 48.27           O  
ANISOU 3348  OH  TYR A 451     6348   5749   6243   -245   1079    782       O  
ATOM   3349  N   CYS A 452       8.548   4.711  14.432  1.00 31.13           N  
ANISOU 3349  N   CYS A 452     4734   3638   3457    268    632    643       N  
ATOM   3350  CA  CYS A 452       7.124   4.971  14.619  1.00 31.15           C  
ANISOU 3350  CA  CYS A 452     4773   3658   3403    345    543    592       C  
ATOM   3351  C   CYS A 452       6.418   3.651  14.934  1.00 30.24           C  
ANISOU 3351  C   CYS A 452     4583   3648   3260    363    466    510       C  
ATOM   3352  O   CYS A 452       7.071   2.611  15.065  1.00 28.34           O  
ANISOU 3352  O   CYS A 452     4271   3450   3046    314    479    498       O  
ATOM   3353  CB  CYS A 452       6.533   5.601  13.353  1.00 30.66           C  
ANISOU 3353  CB  CYS A 452     4839   3573   3239    460    557    645       C  
ATOM   3354  SG  CYS A 452       6.661   4.546  11.871  1.00 32.43           S  
ANISOU 3354  SG  CYS A 452     5099   3879   3346    535    592    669       S  
ATOM   3355  N   ALA A 453       5.095   3.681  15.068  1.00 28.63           N  
ANISOU 3355  N   ALA A 453     4388   3480   3010    430    386    452       N  
ATOM   3356  CA  ALA A 453       4.358   2.471  15.437  1.00 27.88           C  
ANISOU 3356  CA  ALA A 453     4216   3477   2901    432    318    372       C  
ATOM   3357  C   ALA A 453       4.395   1.404  14.329  1.00 27.95           C  
ANISOU 3357  C   ALA A 453     4233   3546   2842    482    322    371       C  
ATOM   3358  O   ALA A 453       4.385   0.203  14.608  1.00 27.38           O  
ANISOU 3358  O   ALA A 453     4091   3528   2785    448    295    324       O  
ATOM   3359  CB  ALA A 453       2.917   2.818  15.804  1.00 27.89           C  
ANISOU 3359  CB  ALA A 453     4212   3507   2878    490    240    305       C  
ATOM   3360  N   ALA A 454       4.446   1.844  13.075  1.00 28.78           N  
ANISOU 3360  N   ALA A 454     4432   3635   2868    564    356    423       N  
ATOM   3361  CA  ALA A 454       4.494   0.914  11.946  1.00 29.04           C  
ANISOU 3361  CA  ALA A 454     4489   3725   2821    621    363    416       C  
ATOM   3362  C   ALA A 454       5.791   0.106  11.943  1.00 28.94           C  
ANISOU 3362  C   ALA A 454     4428   3714   2855    550    436    438       C  
ATOM   3363  O   ALA A 454       5.775  -1.106  11.731  1.00 28.53           O  
ANISOU 3363  O   ALA A 454     4333   3717   2792    554    414    389       O  
ATOM   3364  CB  ALA A 454       4.322   1.659  10.619  1.00 30.17           C  
ANISOU 3364  CB  ALA A 454     4761   3851   2853    726    388    476       C  
ATOM   3365  N   THR A 455       6.910   0.778  12.196  1.00 29.04           N  
ANISOU 3365  N   THR A 455     4442   3663   2931    485    520    506       N  
ATOM   3366  CA  THR A 455       8.197   0.109  12.124  1.00 29.61           C  
ANISOU 3366  CA  THR A 455     4459   3737   3056    427    594    528       C  
ATOM   3367  C   THR A 455       8.456  -0.674  13.395  1.00 28.13           C  
ANISOU 3367  C   THR A 455     4156   3563   2969    342    545    477       C  
ATOM   3368  O   THR A 455       9.149  -1.678  13.362  1.00 27.99           O  
ANISOU 3368  O   THR A 455     4080   3570   2985    319    563    463       O  
ATOM   3369  CB  THR A 455       9.363   1.088  11.830  1.00 30.88           C  
ANISOU 3369  CB  THR A 455     4652   3828   3254    385    710    618       C  
ATOM   3370  CG2 THR A 455       9.183   1.722  10.466  1.00 30.96           C  
ANISOU 3370  CG2 THR A 455     4791   3825   3146    472    770    681       C  
ATOM   3371  OG1 THR A 455       9.404   2.109  12.834  1.00 34.60           O  
ANISOU 3371  OG1 THR A 455     5108   4231   3806    319    695    633       O  
ATOM   3372  N   GLY A 456       7.873  -0.229  14.508  1.00 27.62           N  
ANISOU 3372  N   GLY A 456     4065   3482   2946    301    482    450       N  
ATOM   3373  CA  GLY A 456       7.977  -0.967  15.752  1.00 26.86           C  
ANISOU 3373  CA  GLY A 456     3877   3404   2923    226    429    405       C  
ATOM   3374  C   GLY A 456       7.275  -2.308  15.631  1.00 28.62           C  
ANISOU 3374  C   GLY A 456     4071   3692   3113    255    370    344       C  
ATOM   3375  O   GLY A 456       7.815  -3.350  16.015  1.00 26.87           O  
ANISOU 3375  O   GLY A 456     3788   3483   2938    214    359    329       O  
ATOM   3376  N   GLU A 457       6.072  -2.298  15.073  1.00 26.53           N  
ANISOU 3376  N   GLU A 457     3849   3461   2771    328    326    307       N  
ATOM   3377  CA  GLU A 457       5.336  -3.543  14.919  1.00 26.96           C  
ANISOU 3377  CA  GLU A 457     3873   3570   2800    348    268    240       C  
ATOM   3378  C   GLU A 457       5.992  -4.474  13.899  1.00 27.83           C  
ANISOU 3378  C   GLU A 457     3994   3695   2886    384    303    241       C  
ATOM   3379  O   GLU A 457       6.103  -5.675  14.135  1.00 26.35           O  
ANISOU 3379  O   GLU A 457     3758   3522   2733    358    276    203       O  
ATOM   3380  CB  GLU A 457       3.874  -3.286  14.543  1.00 26.47           C  
ANISOU 3380  CB  GLU A 457     3840   3548   2670    418    205    189       C  
ATOM   3381  CG  GLU A 457       3.108  -4.563  14.179  1.00 26.44           C  
ANISOU 3381  CG  GLU A 457     3806   3599   2643    440    145    114       C  
ATOM   3382  CD  GLU A 457       1.606  -4.359  14.187  1.00 26.61           C  
ANISOU 3382  CD  GLU A 457     3816   3664   2630    484     71     49       C  
ATOM   3383  OE1 GLU A 457       0.854  -5.355  14.066  1.00 26.64           O  
ANISOU 3383  OE1 GLU A 457     3779   3712   2633    484     16    -23       O  
ATOM   3384  OE2 GLU A 457       1.174  -3.195  14.318  1.00 26.81           O1-
ANISOU 3384  OE2 GLU A 457     3869   3678   2639    517     68     65       O1-
ATOM   3385  N   ALA A 458       6.420  -3.920  12.768  1.00 27.31           N  
ANISOU 3385  N   ALA A 458     3998   3620   2757    446    366    284       N  
ATOM   3386  CA  ALA A 458       7.041  -4.742  11.736  1.00 28.57           C  
ANISOU 3386  CA  ALA A 458     4175   3799   2879    488    411    278       C  
ATOM   3387  C   ALA A 458       8.345  -5.355  12.245  1.00 29.76           C  
ANISOU 3387  C   ALA A 458     4252   3925   3128    422    461    297       C  
ATOM   3388  O   ALA A 458       8.658  -6.507  11.944  1.00 27.71           O  
ANISOU 3388  O   ALA A 458     3965   3683   2880    436    458    258       O  
ATOM   3389  CB  ALA A 458       7.280  -3.925  10.459  1.00 28.75           C  
ANISOU 3389  CB  ALA A 458     4298   3820   2804    564    484    332       C  
ATOM   3390  N   ALA A 459       9.091  -4.585  13.034  1.00 27.48           N  
ANISOU 3390  N   ALA A 459     3929   3595   2916    353    497    351       N  
ATOM   3391  CA  ALA A 459      10.369  -5.048  13.571  1.00 31.38           C  
ANISOU 3391  CA  ALA A 459     4343   4067   3513    292    534    369       C  
ATOM   3392  C   ALA A 459      10.168  -6.158  14.598  1.00 29.83           C  
ANISOU 3392  C   ALA A 459     4077   3878   3379    248    448    322       C  
ATOM   3393  O   ALA A 459      10.990  -7.072  14.711  1.00 26.90           O  
ANISOU 3393  O   ALA A 459     3651   3502   3069    237    456    313       O  
ATOM   3394  CB  ALA A 459      11.162  -3.881  14.182  1.00 27.61           C  
ANISOU 3394  CB  ALA A 459     3842   3542   3104    225    581    430       C  
ATOM   3395  N   PHE A 460       9.074  -6.086  15.345  1.00 26.23           N  
ANISOU 3395  N   PHE A 460     3627   3432   2908    226    371    292       N  
ATOM   3396  CA  PHE A 460       8.787  -7.141  16.292  1.00 25.75           C  
ANISOU 3396  CA  PHE A 460     3516   3376   2893    181    298    256       C  
ATOM   3397  C   PHE A 460       8.554  -8.484  15.590  1.00 25.94           C  
ANISOU 3397  C   PHE A 460     3541   3415   2898    226    278    206       C  
ATOM   3398  O   PHE A 460       9.100  -9.500  16.005  1.00 25.92           O  
ANISOU 3398  O   PHE A 460     3496   3394   2960    202    258    198       O  
ATOM   3399  CB  PHE A 460       7.590  -6.802  17.180  1.00 25.28           C  
ANISOU 3399  CB  PHE A 460     3461   3332   2814    147    235    231       C  
ATOM   3400  CG  PHE A 460       7.322  -7.843  18.228  1.00 27.59           C  
ANISOU 3400  CG  PHE A 460     3709   3625   3148     88    173    207       C  
ATOM   3401  CD1 PHE A 460       7.984  -7.804  19.447  1.00 25.30           C  
ANISOU 3401  CD1 PHE A 460     3382   3314   2918     17    156    238       C  
ATOM   3402  CD2 PHE A 460       6.431  -8.878  17.985  1.00 27.51           C  
ANISOU 3402  CD2 PHE A 460     3700   3634   3118    102    131    154       C  
ATOM   3403  CE1 PHE A 460       7.745  -8.781  20.416  1.00 27.48           C  
ANISOU 3403  CE1 PHE A 460     3634   3587   3220    -35    101    229       C  
ATOM   3404  CE2 PHE A 460       6.195  -9.860  18.942  1.00 27.11           C  
ANISOU 3404  CE2 PHE A 460     3619   3573   3107     40     83    143       C  
ATOM   3405  CZ  PHE A 460       6.850  -9.807  20.160  1.00 27.13           C  
ANISOU 3405  CZ  PHE A 460     3596   3554   3157    -26     70    186       C  
ATOM   3406  N   TYR A 461       7.737  -8.487  14.540  1.00 26.21           N  
ANISOU 3406  N   TYR A 461     3630   3480   2848    295    275    168       N  
ATOM   3407  CA  TYR A 461       7.473  -9.716  13.786  1.00 26.53           C  
ANISOU 3407  CA  TYR A 461     3680   3534   2867    341    251    106       C  
ATOM   3408  C   TYR A 461       8.761 -10.248  13.163  1.00 27.32           C  
ANISOU 3408  C   TYR A 461     3769   3617   2995    371    318    118       C  
ATOM   3409  O   TYR A 461       9.010 -11.450  13.174  1.00 27.20           O  
ANISOU 3409  O   TYR A 461     3727   3583   3023    374    294     79       O  
ATOM   3410  CB  TYR A 461       6.443  -9.481  12.674  1.00 27.88           C  
ANISOU 3410  CB  TYR A 461     3916   3748   2930    418    233     61       C  
ATOM   3411  CG  TYR A 461       5.062  -9.072  13.149  1.00 27.57           C  
ANISOU 3411  CG  TYR A 461     3873   3734   2867    404    162     30       C  
ATOM   3412  CD1 TYR A 461       4.481  -9.663  14.267  1.00 26.14           C  
ANISOU 3412  CD1 TYR A 461     3636   3548   2750    329    106      2       C  
ATOM   3413  CD2 TYR A 461       4.341  -8.097  12.473  1.00 26.94           C  
ANISOU 3413  CD2 TYR A 461     3848   3685   2701    469    156     29       C  
ATOM   3414  CE1 TYR A 461       3.224  -9.298  14.693  1.00 26.00           C  
ANISOU 3414  CE1 TYR A 461     3603   3561   2715    316     54    -32       C  
ATOM   3415  CE2 TYR A 461       3.080  -7.719  12.892  1.00 27.32           C  
ANISOU 3415  CE2 TYR A 461     3881   3761   2738    466     91     -8       C  
ATOM   3416  CZ  TYR A 461       2.526  -8.319  14.001  1.00 29.27           C  
ANISOU 3416  CZ  TYR A 461     4058   4008   3053    387     45    -42       C  
ATOM   3417  OH  TYR A 461       1.280  -7.934  14.424  1.00 26.29           O  
ANISOU 3417  OH  TYR A 461     3653   3665   2669    383     -6    -84       O  
ATOM   3418  N   GLU A 462       9.572  -9.345  12.617  1.00 27.82           N  
ANISOU 3418  N   GLU A 462     3852   3682   3038    394    405    171       N  
ATOM   3419  CA  GLU A 462      10.817  -9.723  11.953  1.00 28.11           C  
ANISOU 3419  CA  GLU A 462     3869   3713   3099    426    488    182       C  
ATOM   3420  C   GLU A 462      11.808 -10.275  12.975  1.00 27.92           C  
ANISOU 3420  C   GLU A 462     3753   3652   3205    367    477    199       C  
ATOM   3421  O   GLU A 462      12.535 -11.223  12.702  1.00 28.37           O  
ANISOU 3421  O   GLU A 462     3774   3698   3309    396    495    172       O  
ATOM   3422  CB  GLU A 462      11.406  -8.521  11.209  1.00 28.70           C  
ANISOU 3422  CB  GLU A 462     3984   3795   3125    448    595    244       C  
ATOM   3423  CG  GLU A 462      12.836  -8.686  10.689  1.00 29.50           C  
ANISOU 3423  CG  GLU A 462     4045   3893   3271    461    705    267       C  
ATOM   3424  CD  GLU A 462      13.006  -9.818   9.683  1.00 33.91           C  
ANISOU 3424  CD  GLU A 462     4621   4477   3787    541    730    202       C  
ATOM   3425  OE1 GLU A 462      12.001 -10.351   9.159  1.00 33.64           O  
ANISOU 3425  OE1 GLU A 462     4650   4466   3667    592    669    141       O  
ATOM   3426  OE2 GLU A 462      14.170 -10.178   9.421  1.00 34.64           O1-
ANISOU 3426  OE2 GLU A 462     4658   4567   3936    552    810    204       O1-
ATOM   3427  N   LEU A 463      11.813  -9.684  14.164  1.00 27.36           N  
ANISOU 3427  N   LEU A 463     3645   3561   3189    292    439    238       N  
ATOM   3428  CA  LEU A 463      12.649 -10.174  15.245  1.00 27.24           C  
ANISOU 3428  CA  LEU A 463     3549   3515   3286    238    405    255       C  
ATOM   3429  C   LEU A 463      12.314 -11.640  15.582  1.00 28.41           C  
ANISOU 3429  C   LEU A 463     3686   3643   3464    245    328    208       C  
ATOM   3430  O   LEU A 463      13.212 -12.482  15.684  1.00 27.55           O  
ANISOU 3430  O   LEU A 463     3526   3509   3432    259    327    203       O  
ATOM   3431  CB  LEU A 463      12.514  -9.274  16.476  1.00 26.72           C  
ANISOU 3431  CB  LEU A 463     3465   3438   3249    158    365    295       C  
ATOM   3432  CG  LEU A 463      13.130  -9.831  17.767  1.00 33.28           C  
ANISOU 3432  CG  LEU A 463     4228   4243   4174    102    299    308       C  
ATOM   3433  CD1 LEU A 463      14.632  -9.988  17.617  1.00 28.07           C  
ANISOU 3433  CD1 LEU A 463     3490   3570   3606    111    344    327       C  
ATOM   3434  CD2 LEU A 463      12.804  -8.906  18.926  1.00 37.27           C  
ANISOU 3434  CD2 LEU A 463     4735   4747   4680     29    256    334       C  
ATOM   3435  N   GLN A 464      11.026 -11.954  15.722  1.00 27.09           N  
ANISOU 3435  N   GLN A 464     3563   3485   3244    236    266    173       N  
ATOM   3436  CA  GLN A 464      10.628 -13.344  15.966  1.00 29.68           C  
ANISOU 3436  CA  GLN A 464     3890   3784   3604    234    200    129       C  
ATOM   3437  C   GLN A 464      11.141 -14.259  14.859  1.00 29.29           C  
ANISOU 3437  C   GLN A 464     3847   3723   3560    312    234     80       C  
ATOM   3438  O   GLN A 464      11.642 -15.348  15.124  1.00 28.77           O  
ANISOU 3438  O   GLN A 464     3752   3610   3567    318    204     65       O  
ATOM   3439  CB  GLN A 464       9.111 -13.495  16.092  1.00 30.35           C  
ANISOU 3439  CB  GLN A 464     4015   3886   3632    212    143     89       C  
ATOM   3440  CG  GLN A 464       8.451 -12.450  16.969  1.00 28.58           C  
ANISOU 3440  CG  GLN A 464     3790   3686   3381    153    125    121       C  
ATOM   3441  CD  GLN A 464       9.167 -12.268  18.291  1.00 37.19           C  
ANISOU 3441  CD  GLN A 464     4840   4751   4537     85    106    179       C  
ATOM   3442  NE2 GLN A 464       9.329 -13.363  19.035  1.00 31.01           N  
ANISOU 3442  NE2 GLN A 464     4041   3931   3811     51     55    184       N  
ATOM   3443  OE1 GLN A 464       9.566 -11.154  18.644  1.00 37.48           O  
ANISOU 3443  OE1 GLN A 464     4867   4800   4572     65    133    218       O  
ATOM   3444  N   ARG A 465      11.017 -13.816  13.616  1.00 27.85           N  
ANISOU 3444  N   ARG A 465     3708   3580   3295    376    295     55       N  
ATOM   3445  CA  ARG A 465      11.467 -14.622  12.492  1.00 28.67           C  
ANISOU 3445  CA  ARG A 465     3826   3682   3383    456    336     -1       C  
ATOM   3446  C   ARG A 465      12.976 -14.864  12.499  1.00 31.65           C  
ANISOU 3446  C   ARG A 465     4138   4038   3847    477    399     22       C  
ATOM   3447  O   ARG A 465      13.430 -15.976  12.229  1.00 29.81           O  
ANISOU 3447  O   ARG A 465     3888   3773   3664    522    393    -26       O  
ATOM   3448  CB  ARG A 465      11.018 -13.992  11.169  1.00 29.07           C  
ANISOU 3448  CB  ARG A 465     3950   3789   3305    523    391    -26       C  
ATOM   3449  CG  ARG A 465       9.496 -13.945  11.021  1.00 28.76           C  
ANISOU 3449  CG  ARG A 465     3966   3775   3188    521    314    -71       C  
ATOM   3450  CD  ARG A 465       9.074 -13.530   9.610  1.00 30.90           C  
ANISOU 3450  CD  ARG A 465     4318   4100   3323    607    349   -106       C  
ATOM   3451  NE  ARG A 465       9.499 -12.171   9.266  1.00 31.33           N  
ANISOU 3451  NE  ARG A 465     4402   4183   3319    621    433    -29       N  
ATOM   3452  CZ  ARG A 465       8.708 -11.100   9.321  1.00 31.91           C  
ANISOU 3452  CZ  ARG A 465     4515   4280   3329    616    413      5       C  
ATOM   3453  NH1 ARG A 465       7.446 -11.222   9.712  1.00 28.79           N1+
ANISOU 3453  NH1 ARG A 465     4121   3895   2922    598    314    -38       N1+
ATOM   3454  NH2 ARG A 465       9.181  -9.904   8.976  1.00 30.30           N  
ANISOU 3454  NH2 ARG A 465     4346   4085   3080    628    494     80       N  
ATOM   3455  N   ARG A 466      13.758 -13.831  12.800  1.00 30.96           N  
ANISOU 3455  N   ARG A 466     4009   3967   3788    447    457     90       N  
ATOM   3456  CA  ARG A 466      15.209 -13.992  12.816  1.00 34.11           C  
ANISOU 3456  CA  ARG A 466     4326   4354   4282    463    519    108       C  
ATOM   3457  C   ARG A 466      15.641 -14.958  13.907  1.00 31.16           C  
ANISOU 3457  C   ARG A 466     3887   3925   4027    438    431    108       C  
ATOM   3458  O   ARG A 466      16.558 -15.752  13.718  1.00 30.86           O  
ANISOU 3458  O   ARG A 466     3794   3864   4067    487    449     83       O  
ATOM   3459  CB  ARG A 466      15.913 -12.650  13.008  1.00 37.07           C  
ANISOU 3459  CB  ARG A 466     4660   4749   4675    418    591    179       C  
ATOM   3460  CG  ARG A 466      15.737 -11.699  11.843  1.00 39.49           C  
ANISOU 3460  CG  ARG A 466     5034   5098   4871    450    696    194       C  
ATOM   3461  CD  ARG A 466      16.585 -10.456  12.033  1.00 40.03           C  
ANISOU 3461  CD  ARG A 466     5057   5171   4983    398    778    266       C  
ATOM   3462  NE  ARG A 466      16.321  -9.471  10.990  1.00 42.19           N  
ANISOU 3462  NE  ARG A 466     5414   5472   5143    422    875    297       N  
ATOM   3463  CZ  ARG A 466      17.014  -8.351  10.833  1.00 35.86           C  
ANISOU 3463  CZ  ARG A 466     4596   4668   4360    383    973    361       C  
ATOM   3464  NH1 ARG A 466      16.697  -7.505   9.860  1.00 31.92           N1+
ANISOU 3464  NH1 ARG A 466     4195   4187   3748    411   1057    397       N1+
ATOM   3465  NH2 ARG A 466      18.025  -8.077  11.649  1.00 34.17           N  
ANISOU 3465  NH2 ARG A 466     4271   4431   4280    316    984    389       N  
ATOM   3466  N   ARG A 467      14.976 -14.875  15.052  1.00 29.20           N  
ANISOU 3466  N   ARG A 467     3649   3656   3789    367    339    138       N  
ATOM   3467  CA  ARG A 467      15.288 -15.741  16.178  1.00 31.61           C  
ANISOU 3467  CA  ARG A 467     3913   3908   4189    339    247    153       C  
ATOM   3468  C   ARG A 467      14.939 -17.198  15.847  1.00 34.27           C  
ANISOU 3468  C   ARG A 467     4283   4195   4543    387    202     93       C  
ATOM   3469  O   ARG A 467      15.705 -18.115  16.130  1.00 33.64           O  
ANISOU 3469  O   ARG A 467     4161   4064   4556    419    170     87       O  
ATOM   3470  CB  ARG A 467      14.536 -15.254  17.424  1.00 28.18           C  
ANISOU 3470  CB  ARG A 467     3500   3473   3736    249    172    198       C  
ATOM   3471  CG  ARG A 467      14.981 -13.870  17.897  1.00 27.92           C  
ANISOU 3471  CG  ARG A 467     3431   3474   3704    199    203    250       C  
ATOM   3472  CD  ARG A 467      16.368 -13.902  18.536  1.00 28.47           C  
ANISOU 3472  CD  ARG A 467     3406   3527   3884    191    189    282       C  
ATOM   3473  NE  ARG A 467      16.315 -14.425  19.900  1.00 29.47           N  
ANISOU 3473  NE  ARG A 467     3527   3621   4050    146     77    311       N  
ATOM   3474  CZ  ARG A 467      17.384 -14.663  20.655  1.00 31.52           C  
ANISOU 3474  CZ  ARG A 467     3713   3861   4404    143     25    336       C  
ATOM   3475  NH1 ARG A 467      18.604 -14.439  20.182  1.00 30.69           N1+
ANISOU 3475  NH1 ARG A 467     3515   3767   4378    179     80    330       N1+
ATOM   3476  NH2 ARG A 467      17.231 -15.136  21.884  1.00 32.80           N  
ANISOU 3476  NH2 ARG A 467     3891   3994   4577    105    -81    368       N  
ATOM   3477  N   LEU A 468      13.783 -17.399  15.226  1.00 29.18           N  
ANISOU 3477  N   LEU A 468     3713   3561   3814    395    196     44       N  
ATOM   3478  CA  LEU A 468      13.343 -18.738  14.865  1.00 33.24           C  
ANISOU 3478  CA  LEU A 468     4264   4021   4343    430    151    -23       C  
ATOM   3479  C   LEU A 468      14.223 -19.343  13.770  1.00 35.64           C  
ANISOU 3479  C   LEU A 468     4552   4316   4672    531    214    -83       C  
ATOM   3480  O   LEU A 468      14.557 -20.533  13.815  1.00 35.42           O  
ANISOU 3480  O   LEU A 468     4518   4219   4721    569    176   -121       O  
ATOM   3481  CB  LEU A 468      11.863 -18.722  14.474  1.00 29.28           C  
ANISOU 3481  CB  LEU A 468     3834   3541   3750    408    123    -70       C  
ATOM   3482  CG  LEU A 468      10.969 -18.535  15.701  1.00 32.59           C  
ANISOU 3482  CG  LEU A 468     4262   3951   4172    309     52    -24       C  
ATOM   3483  CD1 LEU A 468       9.533 -18.214  15.314  1.00 37.77           C  
ANISOU 3483  CD1 LEU A 468     4963   4649   4738    287     36    -68       C  
ATOM   3484  CD2 LEU A 468      11.031 -19.781  16.595  1.00 32.40           C  
ANISOU 3484  CD2 LEU A 468     4236   3837   4237    275    -23    -12       C  
ATOM   3485  N   LYS A 469      14.636 -18.525  12.808  1.00 30.88           N  
ANISOU 3485  N   LYS A 469     3946   3781   4007    575    315    -90       N  
ATOM   3486  CA  LYS A 469      15.562 -19.018  11.789  1.00 32.03           C  
ANISOU 3486  CA  LYS A 469     4069   3930   4170    670    395   -146       C  
ATOM   3487  C   LYS A 469      16.895 -19.454  12.396  1.00 32.53           C  
ANISOU 3487  C   LYS A 469     4032   3953   4373    689    396   -121       C  
ATOM   3488  O   LYS A 469      17.510 -20.416  11.928  1.00 33.49           O  
ANISOU 3488  O   LYS A 469     4133   4039   4554    768    412   -182       O  
ATOM   3489  CB  LYS A 469      15.779 -17.992  10.669  1.00 32.26           C  
ANISOU 3489  CB  LYS A 469     4120   4043   4095    707    518   -145       C  
ATOM   3490  CG  LYS A 469      14.589 -17.862   9.716  1.00 32.20           C  
ANISOU 3490  CG  LYS A 469     4219   4074   3942    734    515   -198       C  
ATOM   3491  CD  LYS A 469      14.913 -16.969   8.500  1.00 33.58           C  
ANISOU 3491  CD  LYS A 469     4432   4326   4002    787    642   -192       C  
ATOM   3492  CE  LYS A 469      15.071 -15.510   8.907  1.00 36.27           C  
ANISOU 3492  CE  LYS A 469     4756   4701   4326    724    689    -90       C  
ATOM   3493  NZ  LYS A 469      15.340 -14.625   7.733  1.00 39.90           N1+
ANISOU 3493  NZ  LYS A 469     5268   5224   4670    770    817    -70       N1+
ATOM   3494  N   ALA A 470      17.334 -18.749  13.438  1.00 32.04           N  
ANISOU 3494  N   ALA A 470     3908   3897   4367    623    373    -39       N  
ATOM   3495  CA  ALA A 470      18.597 -19.057  14.101  1.00 33.33           C  
ANISOU 3495  CA  ALA A 470     3967   4031   4667    638    357    -12       C  
ATOM   3496  C   ALA A 470      18.637 -20.478  14.683  1.00 35.80           C  
ANISOU 3496  C   ALA A 470     4283   4250   5070    669    251    -36       C  
ATOM   3497  O   ALA A 470      19.705 -21.073  14.801  1.00 34.17           O  
ANISOU 3497  O   ALA A 470     3999   4011   4975    729    246    -48       O  
ATOM   3498  CB  ALA A 470      18.909 -18.019  15.185  1.00 36.95           C  
ANISOU 3498  CB  ALA A 470     4370   4512   5157    552    329     73       C  
ATOM   3499  N   ILE A 471      17.482 -21.027  15.041  1.00 34.67           N  
ANISOU 3499  N   ILE A 471     4228   4060   4885    629    168    -42       N  
ATOM   3500  CA  ILE A 471      17.449 -22.404  15.534  1.00 33.08           C  
ANISOU 3500  CA  ILE A 471     4048   3754   4767    653     74    -59       C  
ATOM   3501  C   ILE A 471      17.093 -23.423  14.449  1.00 33.81           C  
ANISOU 3501  C   ILE A 471     4197   3803   4845    728     92   -163       C  
ATOM   3502  O   ILE A 471      16.891 -24.602  14.746  1.00 36.58           O  
ANISOU 3502  O   ILE A 471     4586   4054   5261    743     16   -187       O  
ATOM   3503  CB  ILE A 471      16.489 -22.580  16.737  1.00 35.22           C  
ANISOU 3503  CB  ILE A 471     4378   3980   5023    555    -32      2       C  
ATOM   3504  CG1 ILE A 471      15.046 -22.326  16.304  1.00 36.62           C  
ANISOU 3504  CG1 ILE A 471     4638   4187   5088    503    -22    -31       C  
ATOM   3505  CG2 ILE A 471      16.901 -21.677  17.896  1.00 31.84           C  
ANISOU 3505  CG2 ILE A 471     3899   3588   4608    489    -63     95       C  
ATOM   3506  CD1 ILE A 471      14.019 -23.051  17.131  1.00 34.94           C  
ANISOU 3506  CD1 ILE A 471     4492   3905   4881    429   -112    -12       C  
ATOM   3507  N   GLY A 472      17.016 -22.978  13.198  1.00 33.96           N  
ANISOU 3507  N   GLY A 472     4233   3893   4779    774    192   -225       N  
ATOM   3508  CA  GLY A 472      16.808 -23.888  12.082  1.00 34.84           C  
ANISOU 3508  CA  GLY A 472     4396   3975   4868    856    216   -338       C  
ATOM   3509  C   GLY A 472      15.399 -23.956  11.511  1.00 34.74           C  
ANISOU 3509  C   GLY A 472     4484   3975   4743    825    192   -394       C  
ATOM   3510  O   GLY A 472      15.107 -24.806  10.674  1.00 35.25           O  
ANISOU 3510  O   GLY A 472     4598   4003   4790    884    188   -497       O  
ATOM   3511  N   LEU A 473      14.506 -23.083  11.961  1.00 33.36           N  
ANISOU 3511  N   LEU A 473     4333   3848   4494    736    169   -337       N  
ATOM   3512  CA  LEU A 473      13.180 -23.032  11.357  1.00 34.18           C  
ANISOU 3512  CA  LEU A 473     4516   3980   4492    713    146   -396       C  
ATOM   3513  C   LEU A 473      13.320 -22.517   9.920  1.00 35.65           C  
ANISOU 3513  C   LEU A 473     4731   4252   4563    795    242   -459       C  
ATOM   3514  O   LEU A 473      13.871 -21.443   9.697  1.00 40.74           O  
ANISOU 3514  O   LEU A 473     5347   4972   5159    805    327   -405       O  
ATOM   3515  CB  LEU A 473      12.257 -22.108  12.155  1.00 34.01           C  
ANISOU 3515  CB  LEU A 473     4501   4000   4421    610    109   -322       C  
ATOM   3516  CG  LEU A 473      10.768 -22.416  12.018  1.00 33.01           C  
ANISOU 3516  CG  LEU A 473     4434   3868   4240    563     43   -378       C  
ATOM   3517  CD1 LEU A 473      10.482 -23.786  12.627  1.00 34.16           C  
ANISOU 3517  CD1 LEU A 473     4594   3896   4489    527    -40   -403       C  
ATOM   3518  CD2 LEU A 473       9.917 -21.344  12.671  1.00 32.92           C  
ANISOU 3518  CD2 LEU A 473     4420   3917   4172    479     27   -313       C  
ATOM   3519  N   PRO A 474      12.821 -23.279   8.939  1.00 34.39           N  
ANISOU 3519  N   PRO A 474     4634   4079   4354    852    229   -574       N  
ATOM   3520  CA  PRO A 474      12.996 -22.875   7.543  1.00 38.88           C  
ANISOU 3520  CA  PRO A 474     5244   4731   4797    940    320   -636       C  
ATOM   3521  C   PRO A 474      11.905 -21.909   7.096  1.00 38.76           C  
ANISOU 3521  C   PRO A 474     5289   4802   4637    914    311   -629       C  
ATOM   3522  O   PRO A 474      10.884 -22.326   6.552  1.00 45.73           O  
ANISOU 3522  O   PRO A 474     6234   5687   5455    922    247   -716       O  
ATOM   3523  CB  PRO A 474      12.879 -24.198   6.782  1.00 37.49           C  
ANISOU 3523  CB  PRO A 474     5115   4495   4635   1013    289   -774       C  
ATOM   3524  CG  PRO A 474      12.234 -25.179   7.752  1.00 37.74           C  
ANISOU 3524  CG  PRO A 474     5146   4411   4783    939    166   -781       C  
ATOM   3525  CD  PRO A 474      11.996 -24.491   9.055  1.00 35.97           C  
ANISOU 3525  CD  PRO A 474     4877   4188   4602    832    129   -652       C  
ATOM   3526  N   LEU A 475      12.131 -20.626   7.334  1.00 33.85           N  
ANISOU 3526  N   LEU A 475     4645   4244   3971    883    369   -528       N  
ATOM   3527  CA  LEU A 475      11.184 -19.593   6.946  1.00 34.77           C  
ANISOU 3527  CA  LEU A 475     4817   4437   3955    868    363   -508       C  
ATOM   3528  C   LEU A 475      11.642 -18.936   5.653  1.00 40.79           C  
ANISOU 3528  C   LEU A 475     5634   5282   4584    955    474   -518       C  
ATOM   3529  O   LEU A 475      12.721 -18.349   5.590  1.00 40.76           O  
ANISOU 3529  O   LEU A 475     5593   5300   4594    968    584   -453       O  
ATOM   3530  CB  LEU A 475      11.068 -18.539   8.045  1.00 32.22           C  
ANISOU 3530  CB  LEU A 475     4450   4125   3667    779    354   -391       C  
ATOM   3531  CG  LEU A 475      10.435 -18.982   9.365  1.00 32.68           C  
ANISOU 3531  CG  LEU A 475     4471   4121   3825    684    249   -369       C  
ATOM   3532  CD1 LEU A 475      10.442 -17.840  10.399  1.00 30.39           C  
ANISOU 3532  CD1 LEU A 475     4142   3852   3554    606    254   -259       C  
ATOM   3533  CD2 LEU A 475       9.024 -19.480   9.126  1.00 35.12           C  
ANISOU 3533  CD2 LEU A 475     4827   4429   4089    668    157   -450       C  
ATOM   3534  N   PHE A 476      10.824 -19.049   4.615  1.00 36.84           N  
ANISOU 3534  N   PHE A 476     5221   4826   3951   1013    447   -601       N  
ATOM   3535  CA  PHE A 476      11.109 -18.364   3.364  1.00 35.75           C  
ANISOU 3535  CA  PHE A 476     5158   4771   3653   1096    547   -602       C  
ATOM   3536  C   PHE A 476      10.062 -17.300   3.155  1.00 35.33           C  
ANISOU 3536  C   PHE A 476     5169   4778   3479   1085    504   -561       C  
ATOM   3537  O   PHE A 476       8.866 -17.588   3.178  1.00 37.65           O  
ANISOU 3537  O   PHE A 476     5488   5072   3746   1073    385   -623       O  
ATOM   3538  CB  PHE A 476      11.102 -19.339   2.195  1.00 37.13           C  
ANISOU 3538  CB  PHE A 476     5399   4958   3749   1194    551   -738       C  
ATOM   3539  CG  PHE A 476      12.191 -20.366   2.270  1.00 45.02           C  
ANISOU 3539  CG  PHE A 476     6341   5900   4865   1226    603   -788       C  
ATOM   3540  CD1 PHE A 476      13.451 -20.096   1.758  1.00 45.73           C  
ANISOU 3540  CD1 PHE A 476     6410   6025   4939   1282    755   -760       C  
ATOM   3541  CD2 PHE A 476      11.958 -21.596   2.860  1.00 43.46           C  
ANISOU 3541  CD2 PHE A 476     6107   5608   4799   1201    503   -860       C  
ATOM   3542  CE1 PHE A 476      14.459 -21.044   1.826  1.00 49.11           C  
ANISOU 3542  CE1 PHE A 476     6774   6401   5483   1323    801   -814       C  
ATOM   3543  CE2 PHE A 476      12.962 -22.549   2.930  1.00 45.18           C  
ANISOU 3543  CE2 PHE A 476     6275   5762   5129   1243    543   -907       C  
ATOM   3544  CZ  PHE A 476      14.213 -22.271   2.415  1.00 45.29           C  
ANISOU 3544  CZ  PHE A 476     6259   5818   5129   1309    689   -887       C  
ATOM   3545  N   TYR A 477      10.512 -16.070   2.962  1.00 35.30           N  
ANISOU 3545  N   TYR A 477     5186   4818   3409   1088    601   -457       N  
ATOM   3546  CA  TYR A 477       9.585 -14.964   2.775  1.00 36.69           C  
ANISOU 3546  CA  TYR A 477     5427   5041   3473   1088    564   -407       C  
ATOM   3547  C   TYR A 477      10.245 -13.800   2.061  1.00 40.45           C  
ANISOU 3547  C   TYR A 477     5965   5564   3839   1127    699   -313       C  
ATOM   3548  O   TYR A 477      11.460 -13.610   2.144  1.00 38.53           O  
ANISOU 3548  O   TYR A 477     5677   5310   3653   1112    824   -255       O  
ATOM   3549  CB  TYR A 477       8.982 -14.509   4.113  1.00 33.62           C  
ANISOU 3549  CB  TYR A 477     4968   4613   3191    988    482   -346       C  
ATOM   3550  CG  TYR A 477       9.990 -14.125   5.178  1.00 35.53           C  
ANISOU 3550  CG  TYR A 477     5120   4810   3569    910    548   -250       C  
ATOM   3551  CD1 TYR A 477      10.412 -12.810   5.315  1.00 38.07           C  
ANISOU 3551  CD1 TYR A 477     5449   5146   3872    886    626   -140       C  
ATOM   3552  CD2 TYR A 477      10.501 -15.073   6.063  1.00 32.48           C  
ANISOU 3552  CD2 TYR A 477     4645   4363   3335    861    521   -270       C  
ATOM   3553  CE1 TYR A 477      11.320 -12.442   6.291  1.00 36.99           C  
ANISOU 3553  CE1 TYR A 477     5223   4968   3861    811    675    -63       C  
ATOM   3554  CE2 TYR A 477      11.417 -14.712   7.054  1.00 35.13           C  
ANISOU 3554  CE2 TYR A 477     4895   4662   3790    795    564   -186       C  
ATOM   3555  CZ  TYR A 477      11.821 -13.395   7.158  1.00 38.01           C  
ANISOU 3555  CZ  TYR A 477     5260   5048   4133    768    639    -88       C  
ATOM   3556  OH  TYR A 477      12.725 -13.009   8.126  1.00 35.98           O  
ANISOU 3556  OH  TYR A 477     4916   4758   3996    700    674    -16       O  
ATOM   3557  N   SER A 478       9.423 -13.035   1.354  1.00 39.59           N  
ANISOU 3557  N   SER A 478     5959   5507   3575   1177    670   -297       N  
ATOM   3558  CA  SER A 478       9.872 -11.875   0.606  1.00 41.11           C  
ANISOU 3558  CA  SER A 478     6239   5739   3642   1216    789   -199       C  
ATOM   3559  C   SER A 478      10.331 -10.774   1.550  1.00 41.76           C  
ANISOU 3559  C   SER A 478     6264   5779   3826   1128    844    -68       C  
ATOM   3560  O   SER A 478       9.842 -10.661   2.673  1.00 39.55           O  
ANISOU 3560  O   SER A 478     5910   5457   3658   1054    754    -55       O  
ATOM   3561  CB  SER A 478       8.727 -11.367  -0.278  1.00 46.95           C  
ANISOU 3561  CB  SER A 478     7107   6535   4196   1297    710   -216       C  
ATOM   3562  OG  SER A 478       9.066 -10.162  -0.936  1.00 50.81           O  
ANISOU 3562  OG  SER A 478     7696   7049   4559   1332    816   -103       O  
ATOM   3563  N   SER A 479      11.270  -9.956   1.093  1.00 42.40           N  
ANISOU 3563  N   SER A 479     6378   5868   3864   1132    996     26       N  
ATOM   3564  CA  SER A 479      11.673  -8.786   1.858  1.00 48.08           C  
ANISOU 3564  CA  SER A 479     7059   6543   4666   1049   1049    148       C  
ATOM   3565  C   SER A 479      10.918  -7.528   1.402  1.00 47.92           C  
ANISOU 3565  C   SER A 479     7163   6533   4513   1083   1035    227       C  
ATOM   3566  O   SER A 479      11.093  -6.451   1.967  1.00 45.80           O  
ANISOU 3566  O   SER A 479     6884   6220   4300   1022   1069    326       O  
ATOM   3567  CB  SER A 479      13.178  -8.572   1.746  1.00 49.24           C  
ANISOU 3567  CB  SER A 479     7153   6681   4876   1015   1225    210       C  
ATOM   3568  OG  SER A 479      13.553  -8.409   0.394  1.00 56.07           O  
ANISOU 3568  OG  SER A 479     8125   7598   5579   1094   1349    225       O  
ATOM   3569  N   GLN A 480      10.075  -7.671   0.384  1.00 46.83           N  
ANISOU 3569  N   GLN A 480     7143   6449   4201   1183    978    179       N  
ATOM   3570  CA  GLN A 480       9.286  -6.544  -0.112  1.00 45.31           C  
ANISOU 3570  CA  GLN A 480     7077   6266   3873   1235    946    249       C  
ATOM   3571  C   GLN A 480       8.233  -6.105   0.913  1.00 44.16           C  
ANISOU 3571  C   GLN A 480     6882   6085   3812   1194    802    248       C  
ATOM   3572  O   GLN A 480       7.684  -6.936   1.635  1.00 42.05           O  
ANISOU 3572  O   GLN A 480     6521   5816   3641   1161    690    156       O  
ATOM   3573  CB  GLN A 480       8.618  -6.906  -1.442  1.00 39.13           C  
ANISOU 3573  CB  GLN A 480     6429   5558   2880   1363    898    184       C  
ATOM   3574  CG  GLN A 480       9.594  -7.189  -2.569  1.00 40.65           C  
ANISOU 3574  CG  GLN A 480     6697   5796   2953   1417   1054    191       C  
ATOM   3575  CD  GLN A 480      10.261  -5.928  -3.103  1.00 45.88           C  
ANISOU 3575  CD  GLN A 480     7462   6444   3527   1418   1212    344       C  
ATOM   3576  NE2 GLN A 480      11.475  -6.075  -3.617  1.00 48.04           N  
ANISOU 3576  NE2 GLN A 480     7736   6734   3783   1408   1395    374       N  
ATOM   3577  OE1 GLN A 480       9.692  -4.837  -3.050  1.00 48.98           O  
ANISOU 3577  OE1 GLN A 480     7930   6807   3872   1426   1174    434       O  
ATOM   3578  N   PRO A 481       7.943  -4.795   0.971  1.00 41.21           N  
ANISOU 3578  N   PRO A 481     6575   5678   3402   1197    809    350       N  
ATOM   3579  CA  PRO A 481       6.912  -4.271   1.875  1.00 39.82           C  
ANISOU 3579  CA  PRO A 481     6361   5472   3295   1172    682    346       C  
ATOM   3580  C   PRO A 481       5.539  -4.763   1.445  1.00 42.04           C  
ANISOU 3580  C   PRO A 481     6675   5813   3484   1259    522    243       C  
ATOM   3581  O   PRO A 481       5.338  -5.023   0.263  1.00 41.09           O  
ANISOU 3581  O   PRO A 481     6658   5749   3204   1357    513    213       O  
ATOM   3582  CB  PRO A 481       6.984  -2.753   1.669  1.00 46.58           C  
ANISOU 3582  CB  PRO A 481     7319   6281   4098   1186    741    477       C  
ATOM   3583  CG  PRO A 481       8.189  -2.497   0.802  1.00 51.47           C  
ANISOU 3583  CG  PRO A 481     8013   6897   4645   1191    918    561       C  
ATOM   3584  CD  PRO A 481       8.466  -3.761   0.064  1.00 48.34           C  
ANISOU 3584  CD  PRO A 481     7613   6574   4181   1238    936    468       C  
ATOM   3585  N   GLU A 482       4.612  -4.890   2.387  1.00 38.87           N  
ANISOU 3585  N   GLU A 482     6185   5404   3181   1222    398    186       N  
ATOM   3586  CA  GLU A 482       3.275  -5.379   2.072  1.00 40.61           C  
ANISOU 3586  CA  GLU A 482     6408   5682   3340   1292    242     78       C  
ATOM   3587  C   GLU A 482       2.239  -4.265   2.118  1.00 36.31           C  
ANISOU 3587  C   GLU A 482     5910   5134   2752   1349    155    113       C  
ATOM   3588  O   GLU A 482       1.140  -4.407   1.593  1.00 36.60           O  
ANISOU 3588  O   GLU A 482     5973   5225   2706   1434     29     40       O  
ATOM   3589  CB  GLU A 482       2.878  -6.493   3.037  1.00 40.78           C  
ANISOU 3589  CB  GLU A 482     6286   5703   3504   1211    163    -27       C  
ATOM   3590  CG  GLU A 482       3.644  -7.784   2.809  1.00 43.73           C  
ANISOU 3590  CG  GLU A 482     6626   6084   3906   1186    210    -90       C  
ATOM   3591  CD  GLU A 482       3.329  -8.831   3.850  1.00 48.43           C  
ANISOU 3591  CD  GLU A 482     7090   6659   4652   1096    142   -173       C  
ATOM   3592  OE1 GLU A 482       3.571  -8.569   5.050  1.00 44.64           O  
ANISOU 3592  OE1 GLU A 482     6528   6131   4301   1003    163   -125       O  
ATOM   3593  OE2 GLU A 482       2.832  -9.911   3.469  1.00 51.09           O1-
ANISOU 3593  OE2 GLU A 482     7412   7024   4975   1118     66   -286       O1-
ATOM   3594  N   VAL A 483       2.586  -3.168   2.776  1.00 34.97           N  
ANISOU 3594  N   VAL A 483     5741   4898   2647   1302    217    216       N  
ATOM   3595  CA  VAL A 483       1.704  -2.017   2.838  1.00 36.26           C  
ANISOU 3595  CA  VAL A 483     5955   5042   2778   1363    146    256       C  
ATOM   3596  C   VAL A 483       2.581  -0.777   2.873  1.00 37.60           C  
ANISOU 3596  C   VAL A 483     6205   5130   2950   1339    272    402       C  
ATOM   3597  O   VAL A 483       3.715  -0.841   3.341  1.00 39.60           O  
ANISOU 3597  O   VAL A 483     6414   5340   3292   1241    391    449       O  
ATOM   3598  CB  VAL A 483       0.789  -2.081   4.082  1.00 34.22           C  
ANISOU 3598  CB  VAL A 483     5563   4780   2657   1307     46    186       C  
ATOM   3599  CG1 VAL A 483       1.612  -2.035   5.366  1.00 32.97           C  
ANISOU 3599  CG1 VAL A 483     5308   4559   2659   1170    130    222       C  
ATOM   3600  CG2 VAL A 483      -0.232  -0.972   4.047  1.00 34.78           C  
ANISOU 3600  CG2 VAL A 483     5681   4841   2692   1391    -39    206       C  
ATOM   3601  N   THR A 484       2.093   0.342   2.349  1.00 36.65           N  
ANISOU 3601  N   THR A 484     6204   4985   2737   1430    245    472       N  
ATOM   3602  CA  THR A 484       2.866   1.571   2.445  1.00 39.75           C  
ANISOU 3602  CA  THR A 484     6673   5281   3148   1398    362    611       C  
ATOM   3603  C   THR A 484       2.101   2.588   3.271  1.00 41.59           C  
ANISOU 3603  C   THR A 484     6888   5453   3462   1403    288    625       C  
ATOM   3604  O   THR A 484       0.878   2.659   3.196  1.00 52.16           O  
ANISOU 3604  O   THR A 484     8224   6830   4764   1493    150    562       O  
ATOM   3605  CB  THR A 484       3.233   2.146   1.066  1.00 49.82           C  
ANISOU 3605  CB  THR A 484     8136   6550   4241   1491    436    716       C  
ATOM   3606  CG2 THR A 484       3.805   1.051   0.179  1.00 46.15           C  
ANISOU 3606  CG2 THR A 484     7692   6166   3677   1507    493    675       C  
ATOM   3607  OG1 THR A 484       2.068   2.711   0.457  1.00 59.58           O  
ANISOU 3607  OG1 THR A 484     9475   7804   5358   1630    308    716       O  
ATOM   3608  N   VAL A 485       2.821   3.356   4.079  1.00 38.16           N  
ANISOU 3608  N   VAL A 485     6431   4925   3143   1307    377    698       N  
ATOM   3609  CA  VAL A 485       2.175   4.289   4.995  1.00 45.74           C  
ANISOU 3609  CA  VAL A 485     7362   5820   4195   1302    316    697       C  
ATOM   3610  C   VAL A 485       2.703   5.713   4.839  1.00 52.13           C  
ANISOU 3610  C   VAL A 485     8294   6508   5004   1302    402    832       C  
ATOM   3611  O   VAL A 485       3.655   5.959   4.092  1.00 45.80           O  
ANISOU 3611  O   VAL A 485     7589   5673   4142   1287    525    933       O  
ATOM   3612  CB  VAL A 485       2.330   3.834   6.462  1.00 44.07           C  
ANISOU 3612  CB  VAL A 485     6983   5606   4155   1173    310    624       C  
ATOM   3613  CG1 VAL A 485       1.841   2.395   6.625  1.00 42.43           C  
ANISOU 3613  CG1 VAL A 485     6662   5504   3955   1163    234    501       C  
ATOM   3614  CG2 VAL A 485       3.776   3.948   6.911  1.00 39.52           C  
ANISOU 3614  CG2 VAL A 485     6379   4968   3669   1045    449    692       C  
ATOM   3615  N   ALA A 486       2.064   6.647   5.538  1.00 54.85           N  
ANISOU 3615  N   ALA A 486     8636   6785   5419   1319    342    831       N  
ATOM   3616  CA  ALA A 486       2.502   8.039   5.563  1.00 53.08           C  
ANISOU 3616  CA  ALA A 486     8521   6424   5223   1310    413    948       C  
ATOM   3617  C   ALA A 486       2.498   8.666   4.174  1.00 58.22           C  
ANISOU 3617  C   ALA A 486     9367   7042   5710   1424    442   1064       C  
ATOM   3618  O   ALA A 486       3.501   9.228   3.738  1.00 63.82           O  
ANISOU 3618  O   ALA A 486    10172   7672   6403   1375    578   1185       O  
ATOM   3619  CB  ALA A 486       3.887   8.137   6.193  1.00 51.25           C  
ANISOU 3619  CB  ALA A 486     8235   6127   5111   1148    554    996       C  
ATOM   3620  N   LYS A 487       1.367   8.567   3.481  1.00 63.86           N  
ANISOU 3620  N   LYS A 487    10141   7819   6304   1576    313   1027       N  
ATOM   3621  CA  LYS A 487       1.246   9.097   2.123  1.00 72.94           C  
ANISOU 3621  CA  LYS A 487    11489   8951   7273   1704    317   1134       C  
ATOM   3622  C   LYS A 487       2.281   8.495   1.170  1.00 71.34           C  
ANISOU 3622  C   LYS A 487    11354   8794   6958   1670    449   1197       C  
ATOM   3623  O   LYS A 487       3.003   9.222   0.483  1.00 68.17           O  
ANISOU 3623  O   LYS A 487    11103   8315   6485   1668    569   1339       O  
ATOM   3624  CB  LYS A 487       1.369  10.624   2.123  1.00 80.80           C  
ANISOU 3624  CB  LYS A 487    12624   9786   8290   1728    358   1264       C  
ATOM   3625  CG  LYS A 487       0.231  11.362   2.815  1.00 86.18           C  
ANISOU 3625  CG  LYS A 487    13278  10417   9050   1807    220   1210       C  
ATOM   3626  CD  LYS A 487      -1.084  11.204   2.063  1.00 91.32           C  
ANISOU 3626  CD  LYS A 487    13978  11153   9568   1995     48   1158       C  
ATOM   3627  CE  LYS A 487      -1.976  12.425   2.250  1.00 92.95           C  
ANISOU 3627  CE  LYS A 487    14255  11257   9803   2115    -52   1182       C  
ATOM   3628  NZ  LYS A 487      -2.143  12.780   3.687  1.00 91.91           N1+
ANISOU 3628  NZ  LYS A 487    13982  11068   9871   2030    -59   1103       N1+
ATOM   3629  N   ASP A 488       2.345   7.167   1.130  1.00 69.60           N  
ANISOU 3629  N   ASP A 488    11024   8697   6725   1642    431   1090       N  
ATOM   3630  CA  ASP A 488       3.281   6.459   0.259  1.00 68.67           C  
ANISOU 3630  CA  ASP A 488    10951   8635   6504   1617    552   1123       C  
ATOM   3631  C   ASP A 488       4.740   6.853   0.505  1.00 60.47           C  
ANISOU 3631  C   ASP A 488     9910   7511   5553   1477    750   1226       C  
ATOM   3632  O   ASP A 488       5.573   6.759  -0.395  1.00 58.69           O  
ANISOU 3632  O   ASP A 488     9775   7298   5225   1473    883   1304       O  
ATOM   3633  CB  ASP A 488       2.923   6.668  -1.219  1.00 80.06           C  
ANISOU 3633  CB  ASP A 488    12593  10115   7712   1769    529   1188       C  
ATOM   3634  CG  ASP A 488       1.658   5.927  -1.630  1.00 88.02           C  
ANISOU 3634  CG  ASP A 488    13582  11242   8622   1899    338   1061       C  
ATOM   3635  OD1 ASP A 488       1.277   4.958  -0.940  1.00 87.21           O  
ANISOU 3635  OD1 ASP A 488    13307  11209   8620   1852    260    918       O  
ATOM   3636  OD2 ASP A 488       1.050   6.310  -2.655  1.00 92.18           O1-
ANISOU 3636  OD2 ASP A 488    14266  11789   8968   2046    264   1103       O1-
ATOM   3637  N   ALA A 489       5.047   7.284   1.724  1.00 53.51           N  
ANISOU 3637  N   ALA A 489     8919   6549   4862   1363    771   1220       N  
ATOM   3638  CA  ALA A 489       6.412   7.669   2.073  1.00 49.07           C  
ANISOU 3638  CA  ALA A 489     8330   5906   4409   1220    943   1301       C  
ATOM   3639  C   ALA A 489       7.322   6.449   2.198  1.00 46.81           C  
ANISOU 3639  C   ALA A 489     7912   5705   4171   1131   1022   1238       C  
ATOM   3640  O   ALA A 489       8.399   6.411   1.615  1.00 52.22           O  
ANISOU 3640  O   ALA A 489     8630   6385   4828   1083   1179   1310       O  
ATOM   3641  CB  ALA A 489       6.427   8.486   3.359  1.00 50.03           C  
ANISOU 3641  CB  ALA A 489     8375   5920   4715   1130    924   1299       C  
ATOM   3642  N   PHE A 490       6.890   5.454   2.967  1.00 38.93           N  
ANISOU 3642  N   PHE A 490     6762   4780   3249   1110    918   1104       N  
ATOM   3643  CA  PHE A 490       7.650   4.219   3.089  1.00 41.39           C  
ANISOU 3643  CA  PHE A 490     6952   5167   3606   1043    971   1036       C  
ATOM   3644  C   PHE A 490       6.740   3.015   3.297  1.00 39.41           C  
ANISOU 3644  C   PHE A 490     6616   5018   3341   1092    827    894       C  
ATOM   3645  O   PHE A 490       5.542   3.158   3.533  1.00 41.30           O  
ANISOU 3645  O   PHE A 490     6859   5271   3561   1158    688    841       O  
ATOM   3646  CB  PHE A 490       8.700   4.304   4.207  1.00 41.27           C  
ANISOU 3646  CB  PHE A 490     6801   5094   3785    890   1051   1042       C  
ATOM   3647  CG  PHE A 490       8.126   4.544   5.573  1.00 40.72           C  
ANISOU 3647  CG  PHE A 490     6633   4988   3852    838    941    981       C  
ATOM   3648  CD1 PHE A 490       7.870   5.832   6.014  1.00 42.82           C  
ANISOU 3648  CD1 PHE A 490     6954   5150   4166    825    930   1039       C  
ATOM   3649  CD2 PHE A 490       7.864   3.483   6.425  1.00 39.91           C  
ANISOU 3649  CD2 PHE A 490     6388   4950   3828    801    855    866       C  
ATOM   3650  CE1 PHE A 490       7.348   6.058   7.274  1.00 46.91           C  
ANISOU 3650  CE1 PHE A 490     7383   5640   4800    782    836    974       C  
ATOM   3651  CE2 PHE A 490       7.342   3.701   7.690  1.00 44.44           C  
ANISOU 3651  CE2 PHE A 490     6877   5496   4512    753    766    813       C  
ATOM   3652  CZ  PHE A 490       7.082   4.991   8.114  1.00 45.95           C  
ANISOU 3652  CZ  PHE A 490     7121   5594   4743    745    757    862       C  
ATOM   3653  N   GLY A 491       7.319   1.829   3.186  1.00 36.73           N  
ANISOU 3653  N   GLY A 491     6195   4745   3014   1060    865    831       N  
ATOM   3654  CA  GLY A 491       6.563   0.607   3.364  1.00 41.71           C  
ANISOU 3654  CA  GLY A 491     6744   5460   3642   1092    742    698       C  
ATOM   3655  C   GLY A 491       7.094  -0.243   4.500  1.00 41.70           C  
ANISOU 3655  C   GLY A 491     6576   5460   3808    979    743    632       C  
ATOM   3656  O   GLY A 491       8.229  -0.069   4.944  1.00 42.19           O  
ANISOU 3656  O   GLY A 491     6583   5478   3971    886    850    682       O  
ATOM   3657  N   VAL A 492       6.254  -1.145   4.990  1.00 38.50           N  
ANISOU 3657  N   VAL A 492     6090   5104   3435    985    618    522       N  
ATOM   3658  CA  VAL A 492       6.697  -2.183   5.904  1.00 36.78           C  
ANISOU 3658  CA  VAL A 492     5732   4895   3348    896    610    456       C  
ATOM   3659  C   VAL A 492       6.046  -3.485   5.488  1.00 38.29           C  
ANISOU 3659  C   VAL A 492     5901   5158   3488    947    523    343       C  
ATOM   3660  O   VAL A 492       5.040  -3.489   4.783  1.00 40.24           O  
ANISOU 3660  O   VAL A 492     6216   5450   3625   1039    440    302       O  
ATOM   3661  CB  VAL A 492       6.315  -1.887   7.372  1.00 35.29           C  
ANISOU 3661  CB  VAL A 492     5447   4668   3293    813    544    438       C  
ATOM   3662  CG1 VAL A 492       6.915  -0.559   7.836  1.00 37.99           C  
ANISOU 3662  CG1 VAL A 492     5812   4929   3694    759    618    536       C  
ATOM   3663  CG2 VAL A 492       4.795  -1.906   7.558  1.00 31.08           C  
ANISOU 3663  CG2 VAL A 492     4913   4170   2727    867    406    367       C  
ATOM   3664  N   ARG A 493       6.623  -4.597   5.912  1.00 37.21           N  
ANISOU 3664  N   ARG A 493     5670   5029   3437    890    537    291       N  
ATOM   3665  CA  ARG A 493       5.934  -5.866   5.767  1.00 39.26           C  
ANISOU 3665  CA  ARG A 493     5894   5338   3684    917    441    176       C  
ATOM   3666  C   ARG A 493       5.710  -6.451   7.148  1.00 34.10           C  
ANISOU 3666  C   ARG A 493     5117   4661   3178    822    377    132       C  
ATOM   3667  O   ARG A 493       6.399  -6.092   8.110  1.00 32.31           O  
ANISOU 3667  O   ARG A 493     4831   4389   3057    738    423    186       O  
ATOM   3668  CB  ARG A 493       6.707  -6.831   4.876  1.00 42.62           C  
ANISOU 3668  CB  ARG A 493     6339   5791   4063    953    506    139       C  
ATOM   3669  CG  ARG A 493       7.869  -7.521   5.549  1.00 38.52           C  
ANISOU 3669  CG  ARG A 493     5721   5238   3677    874    574    142       C  
ATOM   3670  CD  ARG A 493       8.402  -8.629   4.645  1.00 37.24           C  
ANISOU 3670  CD  ARG A 493     5574   5106   3469    928    616     76       C  
ATOM   3671  NE  ARG A 493       7.463  -9.743   4.531  1.00 39.44           N  
ANISOU 3671  NE  ARG A 493     5841   5410   3734    956    496    -42       N  
ATOM   3672  CZ  ARG A 493       6.815 -10.080   3.420  1.00 43.77           C  
ANISOU 3672  CZ  ARG A 493     6474   6010   4146   1049    451   -113       C  
ATOM   3673  NH1 ARG A 493       6.995  -9.390   2.304  1.00 41.09           N1+
ANISOU 3673  NH1 ARG A 493     6248   5708   3654   1130    518    -69       N1+
ATOM   3674  NH2 ARG A 493       5.986 -11.119   3.423  1.00 45.35           N  
ANISOU 3674  NH2 ARG A 493     6648   6223   4360   1057    337   -228       N  
ATOM   3675  N   LEU A 494       4.724  -7.329   7.249  1.00 30.28           N  
ANISOU 3675  N   LEU A 494     4598   4209   2697    831    270     35       N  
ATOM   3676  CA  LEU A 494       4.351  -7.886   8.535  1.00 31.68           C  
ANISOU 3676  CA  LEU A 494     4671   4368   2998    741    210     -3       C  
ATOM   3677  C   LEU A 494       4.517  -9.397   8.559  1.00 31.68           C  
ANISOU 3677  C   LEU A 494     4623   4367   3048    717    183    -80       C  
ATOM   3678  O   LEU A 494       4.925  -9.957   9.563  1.00 28.62           O  
ANISOU 3678  O   LEU A 494     4161   3942   2772    635    184    -75       O  
ATOM   3679  CB  LEU A 494       2.903  -7.527   8.862  1.00 30.53           C  
ANISOU 3679  CB  LEU A 494     4511   4251   2839    753    107    -48       C  
ATOM   3680  CG  LEU A 494       2.560  -6.037   8.941  1.00 33.82           C  
ANISOU 3680  CG  LEU A 494     4974   4660   3218    784    114     16       C  
ATOM   3681  CD1 LEU A 494       1.111  -5.869   9.354  1.00 33.79           C  
ANISOU 3681  CD1 LEU A 494     4929   4690   3221    796      9    -48       C  
ATOM   3682  CD2 LEU A 494       3.487  -5.317   9.921  1.00 31.73           C  
ANISOU 3682  CD2 LEU A 494     4682   4336   3040    702    191    102       C  
ATOM   3683  N   PHE A 495       4.197 -10.045   7.442  1.00 31.07           N  
ANISOU 3683  N   PHE A 495     4596   4326   2885    793    154   -152       N  
ATOM   3684  CA  PHE A 495       4.080 -11.499   7.400  1.00 30.19           C  
ANISOU 3684  CA  PHE A 495     4446   4207   2819    778    107   -247       C  
ATOM   3685  C   PHE A 495       5.391 -12.186   7.018  1.00 30.55           C  
ANISOU 3685  C   PHE A 495     4496   4225   2885    790    193   -240       C  
ATOM   3686  O   PHE A 495       6.226 -11.595   6.336  1.00 34.83           O  
ANISOU 3686  O   PHE A 495     5091   4779   3363    838    289   -185       O  
ATOM   3687  CB  PHE A 495       2.963 -11.898   6.429  1.00 31.01           C  
ANISOU 3687  CB  PHE A 495     4592   4363   2826    852     14   -350       C  
ATOM   3688  CG  PHE A 495       1.593 -11.449   6.868  1.00 30.78           C  
ANISOU 3688  CG  PHE A 495     4529   4364   2802    838    -84   -380       C  
ATOM   3689  CD1 PHE A 495       0.827 -12.237   7.717  1.00 30.38           C  
ANISOU 3689  CD1 PHE A 495     4390   4300   2855    757   -156   -444       C  
ATOM   3690  CD2 PHE A 495       1.076 -10.238   6.440  1.00 31.10           C  
ANISOU 3690  CD2 PHE A 495     4624   4443   2749    906    -98   -341       C  
ATOM   3691  CE1 PHE A 495      -0.432 -11.824   8.122  1.00 30.31           C  
ANISOU 3691  CE1 PHE A 495     4334   4326   2857    744   -235   -478       C  
ATOM   3692  CE2 PHE A 495      -0.186  -9.815   6.846  1.00 33.75           C  
ANISOU 3692  CE2 PHE A 495     4916   4809   3099    903   -189   -377       C  
ATOM   3693  CZ  PHE A 495      -0.943 -10.611   7.683  1.00 31.03           C  
ANISOU 3693  CZ  PHE A 495     4469   4461   2859    821   -254   -450       C  
ATOM   3694  N   PRO A 496       5.572 -13.445   7.452  1.00 30.42           N  
ANISOU 3694  N   PRO A 496     4424   4168   2964    748    163   -297       N  
ATOM   3695  CA  PRO A 496       4.612 -14.197   8.266  1.00 29.99           C  
ANISOU 3695  CA  PRO A 496     4312   4091   2990    680     63   -356       C  
ATOM   3696  C   PRO A 496       4.655 -13.773   9.729  1.00 31.56           C  
ANISOU 3696  C   PRO A 496     4444   4259   3290    581     62   -281       C  
ATOM   3697  O   PRO A 496       5.730 -13.515  10.269  1.00 29.60           O  
ANISOU 3697  O   PRO A 496     4172   3978   3097    551    128   -206       O  
ATOM   3698  CB  PRO A 496       5.105 -15.640   8.136  1.00 30.41           C  
ANISOU 3698  CB  PRO A 496     4350   4095   3109    677     56   -423       C  
ATOM   3699  CG  PRO A 496       6.576 -15.500   7.920  1.00 30.58           C  
ANISOU 3699  CG  PRO A 496     4377   4100   3143    707    164   -364       C  
ATOM   3700  CD  PRO A 496       6.729 -14.272   7.061  1.00 30.92           C  
ANISOU 3700  CD  PRO A 496     4485   4203   3059    773    230   -314       C  
ATOM   3701  N   ILE A 497       3.481 -13.719  10.350  1.00 28.64           N  
ANISOU 3701  N   ILE A 497     4041   3902   2941    532    -12   -309       N  
ATOM   3702  CA  ILE A 497       3.344 -13.315  11.735  1.00 28.78           C  
ANISOU 3702  CA  ILE A 497     4002   3899   3033    441    -16   -251       C  
ATOM   3703  C   ILE A 497       3.450 -14.539  12.642  1.00 27.89           C  
ANISOU 3703  C   ILE A 497     3839   3729   3028    358    -44   -266       C  
ATOM   3704  O   ILE A 497       2.687 -15.498  12.502  1.00 29.41           O  
ANISOU 3704  O   ILE A 497     4020   3911   3243    340   -103   -344       O  
ATOM   3705  CB  ILE A 497       1.994 -12.585  11.962  1.00 27.71           C  
ANISOU 3705  CB  ILE A 497     3852   3814   2864    435    -70   -275       C  
ATOM   3706  CG1 ILE A 497       2.012 -11.212  11.274  1.00 28.73           C  
ANISOU 3706  CG1 ILE A 497     4037   3982   2897    515    -40   -234       C  
ATOM   3707  CG2 ILE A 497       1.677 -12.464  13.452  1.00 27.04           C  
ANISOU 3707  CG2 ILE A 497     3705   3712   2859    333    -79   -241       C  
ATOM   3708  CD1 ILE A 497       0.672 -10.455  11.322  1.00 27.98           C  
ANISOU 3708  CD1 ILE A 497     3931   3937   2764    537   -101   -266       C  
ATOM   3709  N   ILE A 498       4.406 -14.510  13.559  1.00 27.20           N  
ANISOU 3709  N   ILE A 498     3728   3600   3009    308     -6   -190       N  
ATOM   3710  CA  ILE A 498       4.588 -15.616  14.499  1.00 27.14           C  
ANISOU 3710  CA  ILE A 498     3686   3529   3097    234    -35   -185       C  
ATOM   3711  C   ILE A 498       4.789 -15.067  15.900  1.00 29.52           C  
ANISOU 3711  C   ILE A 498     3955   3821   3439    155    -28   -105       C  
ATOM   3712  O   ILE A 498       5.796 -14.413  16.172  1.00 31.32           O  
ANISOU 3712  O   ILE A 498     4178   4044   3677    161     15    -40       O  
ATOM   3713  CB  ILE A 498       5.800 -16.487  14.120  1.00 27.56           C  
ANISOU 3713  CB  ILE A 498     3747   3528   3198    272     -9   -184       C  
ATOM   3714  CG1 ILE A 498       5.634 -17.027  12.693  1.00 28.33           C  
ANISOU 3714  CG1 ILE A 498     3885   3638   3242    357    -11   -274       C  
ATOM   3715  CG2 ILE A 498       5.957 -17.623  15.123  1.00 27.63           C  
ANISOU 3715  CG2 ILE A 498     3731   3460   3306    202    -50   -170       C  
ATOM   3716  CD1 ILE A 498       6.841 -17.749  12.162  1.00 28.89           C  
ANISOU 3716  CD1 ILE A 498     3963   3666   3347    413     30   -284       C  
ATOM   3717  N   VAL A 499       3.829 -15.324  16.786  1.00 27.15           N  
ANISOU 3717  N   VAL A 499     3633   3522   3162     78    -68   -115       N  
ATOM   3718  CA  VAL A 499       3.872 -14.753  18.127  1.00 25.88           C  
ANISOU 3718  CA  VAL A 499     3451   3364   3019      5    -62    -49       C  
ATOM   3719  C   VAL A 499       3.661 -15.829  19.186  1.00 28.07           C  
ANISOU 3719  C   VAL A 499     3717   3592   3357    -84    -94    -33       C  
ATOM   3720  O   VAL A 499       2.582 -16.410  19.282  1.00 27.75           O  
ANISOU 3720  O   VAL A 499     3665   3554   3326   -128   -120    -81       O  
ATOM   3721  CB  VAL A 499       2.825 -13.625  18.318  1.00 31.55           C  
ANISOU 3721  CB  VAL A 499     4158   4149   3682     -3    -60    -65       C  
ATOM   3722  CG1 VAL A 499       2.987 -12.996  19.705  1.00 31.04           C  
ANISOU 3722  CG1 VAL A 499     4079   4088   3628    -73    -47     -4       C  
ATOM   3723  CG2 VAL A 499       2.977 -12.558  17.227  1.00 25.61           C  
ANISOU 3723  CG2 VAL A 499     3433   3434   2863     89    -32    -72       C  
ATOM   3724  N   LEU A 500       4.705 -16.083  19.971  1.00 29.68           N  
ANISOU 3724  N   LEU A 500     3924   3750   3605   -108    -93     36       N  
ATOM   3725  CA  LEU A 500       4.673 -17.095  21.020  1.00 31.85           C  
ANISOU 3725  CA  LEU A 500     4205   3966   3929   -185   -125     72       C  
ATOM   3726  C   LEU A 500       4.592 -16.415  22.376  1.00 28.30           C  
ANISOU 3726  C   LEU A 500     3753   3545   3455   -254   -122    133       C  
ATOM   3727  O   LEU A 500       5.349 -15.480  22.638  1.00 27.00           O  
ANISOU 3727  O   LEU A 500     3581   3403   3273   -234   -107    171       O  
ATOM   3728  CB  LEU A 500       5.945 -17.940  20.961  1.00 27.71           C  
ANISOU 3728  CB  LEU A 500     3692   3368   3470   -150   -141    105       C  
ATOM   3729  CG  LEU A 500       6.364 -18.431  19.570  1.00 31.92           C  
ANISOU 3729  CG  LEU A 500     4229   3879   4020    -61   -131     44       C  
ATOM   3730  CD1 LEU A 500       7.685 -19.184  19.642  1.00 42.26           C  
ANISOU 3730  CD1 LEU A 500     5537   5118   5403    -21   -142     77       C  
ATOM   3731  CD2 LEU A 500       5.282 -19.314  18.960  1.00 27.47           C  
ANISOU 3731  CD2 LEU A 500     3681   3295   3463    -72   -155    -36       C  
ATOM   3732  N   ASP A 501       3.702 -16.881  23.250  1.00 27.15           N  
ANISOU 3732  N   ASP A 501     3613   3395   3307   -339   -132    141       N  
ATOM   3733  CA  ASP A 501       3.568 -16.238  24.559  1.00 29.67           C  
ANISOU 3733  CA  ASP A 501     3938   3750   3587   -403   -123    192       C  
ATOM   3734  C   ASP A 501       4.658 -16.711  25.536  1.00 28.65           C  
ANISOU 3734  C   ASP A 501     3840   3567   3481   -427   -156    277       C  
ATOM   3735  O   ASP A 501       5.483 -17.544  25.174  1.00 26.67           O  
ANISOU 3735  O   ASP A 501     3599   3248   3286   -390   -184    294       O  
ATOM   3736  CB  ASP A 501       2.123 -16.298  25.095  1.00 32.87           C  
ANISOU 3736  CB  ASP A 501     4330   4196   3965   -482   -102    162       C  
ATOM   3737  CG  ASP A 501       1.783 -17.601  25.826  1.00 37.60           C  
ANISOU 3737  CG  ASP A 501     4957   4734   4596   -569   -113    197       C  
ATOM   3738  OD1 ASP A 501       0.687 -17.636  26.431  1.00 36.21           O  
ANISOU 3738  OD1 ASP A 501     4767   4594   4399   -647    -83    183       O  
ATOM   3739  OD2 ASP A 501       2.577 -18.569  25.819  1.00 31.95           O1-
ANISOU 3739  OD2 ASP A 501     4275   3933   3929   -560   -147    238       O1-
ATOM   3740  N   THR A 502       4.703 -16.145  26.738  1.00 26.36           N  
ANISOU 3740  N   THR A 502     3564   3307   3143   -478   -157    324       N  
ATOM   3741  CA  THR A 502       5.821 -16.412  27.648  1.00 28.88           C  
ANISOU 3741  CA  THR A 502     3912   3587   3473   -487   -202    401       C  
ATOM   3742  C   THR A 502       5.767 -17.819  28.245  1.00 30.74           C  
ANISOU 3742  C   THR A 502     4198   3748   3736   -535   -236    454       C  
ATOM   3743  O   THR A 502       6.783 -18.363  28.674  1.00 32.12           O  
ANISOU 3743  O   THR A 502     4396   3866   3942   -515   -290    514       O  
ATOM   3744  CB  THR A 502       5.892 -15.384  28.798  1.00 31.00           C  
ANISOU 3744  CB  THR A 502     4193   3914   3673   -527   -202    429       C  
ATOM   3745  CG2 THR A 502       6.237 -13.993  28.257  1.00 30.01           C  
ANISOU 3745  CG2 THR A 502     4027   3837   3538   -476   -178    389       C  
ATOM   3746  OG1 THR A 502       4.627 -15.330  29.460  1.00 31.16           O  
ANISOU 3746  OG1 THR A 502     4231   3977   3632   -601   -165    416       O  
ATOM   3747  N   VAL A 503       4.581 -18.409  28.282  1.00 27.78           N  
ANISOU 3747  N   VAL A 503     3836   3366   3354   -597   -207    433       N  
ATOM   3748  CA  VAL A 503       4.467 -19.773  28.767  1.00 32.30           C  
ANISOU 3748  CA  VAL A 503     4462   3851   3960   -649   -232    486       C  
ATOM   3749  C   VAL A 503       5.044 -20.699  27.712  1.00 31.26           C  
ANISOU 3749  C   VAL A 503     4324   3632   3920   -582   -264    461       C  
ATOM   3750  O   VAL A 503       5.730 -21.662  28.027  1.00 32.71           O  
ANISOU 3750  O   VAL A 503     4553   3725   4151   -572   -311    519       O  
ATOM   3751  CB  VAL A 503       3.010 -20.162  29.059  1.00 36.43           C  
ANISOU 3751  CB  VAL A 503     4990   4388   4464   -748   -181    465       C  
ATOM   3752  CG1 VAL A 503       2.937 -21.622  29.496  1.00 35.00           C  
ANISOU 3752  CG1 VAL A 503     4874   4096   4328   -808   -202    527       C  
ATOM   3753  CG2 VAL A 503       2.419 -19.241  30.134  1.00 35.49           C  
ANISOU 3753  CG2 VAL A 503     4875   4362   4249   -810   -139    482       C  
ATOM   3754  N   CYS A 504       4.773 -20.387  26.452  1.00 28.75           N  
ANISOU 3754  N   CYS A 504     3957   3343   3623   -527   -239    372       N  
ATOM   3755  CA  CYS A 504       5.258 -21.204  25.349  1.00 30.30           C  
ANISOU 3755  CA  CYS A 504     4149   3468   3894   -456   -261    330       C  
ATOM   3756  C   CYS A 504       6.764 -21.055  25.179  1.00 30.64           C  
ANISOU 3756  C   CYS A 504     4182   3490   3971   -367   -290    361       C  
ATOM   3757  O   CYS A 504       7.498 -22.044  25.172  1.00 35.13           O  
ANISOU 3757  O   CYS A 504     4774   3968   4606   -334   -331    388       O  
ATOM   3758  CB  CYS A 504       4.556 -20.799  24.050  1.00 33.74           C  
ANISOU 3758  CB  CYS A 504     4542   3957   4321   -416   -228    225       C  
ATOM   3759  SG  CYS A 504       5.288 -21.540  22.580  1.00 34.60           S  
ANISOU 3759  SG  CYS A 504     4647   4003   4495   -309   -244    158       S  
ATOM   3760  N   ALA A 505       7.216 -19.807  25.056  1.00 28.82           N  
ANISOU 3760  N   ALA A 505     3911   3339   3699   -331   -267    356       N  
ATOM   3761  CA  ALA A 505       8.593 -19.508  24.674  1.00 30.39           C  
ANISOU 3761  CA  ALA A 505     4077   3534   3937   -248   -278    367       C  
ATOM   3762  C   ALA A 505       9.509 -19.229  25.866  1.00 30.82           C  
ANISOU 3762  C   ALA A 505     4132   3586   3990   -264   -324    447       C  
ATOM   3763  O   ALA A 505      10.720 -19.055  25.699  1.00 28.08           O  
ANISOU 3763  O   ALA A 505     3745   3233   3691   -202   -341    459       O  
ATOM   3764  CB  ALA A 505       8.621 -18.330  23.697  1.00 31.86           C  
ANISOU 3764  CB  ALA A 505     4220   3798   4090   -198   -221    313       C  
ATOM   3765  N   SER A 506       8.934 -19.190  27.064  1.00 30.05           N  
ANISOU 3765  N   SER A 506     4078   3501   3838   -345   -343    497       N  
ATOM   3766  CA  SER A 506       9.719 -18.972  28.276  1.00 30.89           C  
ANISOU 3766  CA  SER A 506     4200   3611   3927   -363   -399    571       C  
ATOM   3767  C   SER A 506      10.456 -17.633  28.178  1.00 34.58           C  
ANISOU 3767  C   SER A 506     4607   4147   4383   -332   -387    553       C  
ATOM   3768  O   SER A 506       9.827 -16.613  27.895  1.00 32.77           O  
ANISOU 3768  O   SER A 506     4362   3984   4104   -350   -332    510       O  
ATOM   3769  CB  SER A 506      10.687 -20.141  28.492  1.00 34.53           C  
ANISOU 3769  CB  SER A 506     4679   3976   4463   -318   -472    622       C  
ATOM   3770  OG  SER A 506      11.186 -20.156  29.812  1.00 37.34           O  
ANISOU 3770  OG  SER A 506     5074   4329   4786   -345   -542    701       O  
ATOM   3771  N   SER A 507      11.776 -17.632  28.382  1.00 31.69           N  
ANISOU 3771  N   SER A 507     4205   3762   4072   -285   -440    581       N  
ATOM   3772  CA  SER A 507      12.554 -16.387  28.343  1.00 32.17           C  
ANISOU 3772  CA  SER A 507     4203   3880   4138   -268   -430    565       C  
ATOM   3773  C   SER A 507      12.800 -15.862  26.928  1.00 28.63           C  
ANISOU 3773  C   SER A 507     3695   3451   3733   -211   -354    506       C  
ATOM   3774  O   SER A 507      13.236 -14.720  26.750  1.00 30.54           O  
ANISOU 3774  O   SER A 507     3891   3737   3975   -209   -324    489       O  
ATOM   3775  CB  SER A 507      13.912 -16.560  29.041  1.00 35.01           C  
ANISOU 3775  CB  SER A 507     4528   4219   4554   -239   -517    609       C  
ATOM   3776  OG  SER A 507      14.812 -17.322  28.245  1.00 31.97           O  
ANISOU 3776  OG  SER A 507     4091   3782   4273   -158   -526    599       O  
ATOM   3777  N   GLY A 508      12.539 -16.691  25.924  1.00 29.04           N  
ANISOU 3777  N   GLY A 508     3752   3464   3817   -166   -324    474       N  
ATOM   3778  CA  GLY A 508      12.825 -16.309  24.548  1.00 27.34           C  
ANISOU 3778  CA  GLY A 508     3492   3267   3628   -104   -251    421       C  
ATOM   3779  C   GLY A 508      14.268 -16.535  24.104  1.00 30.77           C  
ANISOU 3779  C   GLY A 508     3856   3679   4158    -33   -253    421       C  
ATOM   3780  O   GLY A 508      14.639 -16.205  22.977  1.00 28.72           O  
ANISOU 3780  O   GLY A 508     3558   3438   3917     19   -182    383       O  
ATOM   3781  N   SER A 509      15.093 -17.104  24.975  1.00 30.30           N  
ANISOU 3781  N   SER A 509     3777   3582   4154    -27   -334    465       N  
ATOM   3782  CA  SER A 509      16.434 -17.504  24.560  1.00 29.67           C  
ANISOU 3782  CA  SER A 509     3617   3476   4179     49   -343    458       C  
ATOM   3783  C   SER A 509      16.309 -18.476  23.383  1.00 29.60           C  
ANISOU 3783  C   SER A 509     3619   3423   4205    121   -299    408       C  
ATOM   3784  O   SER A 509      15.244 -19.052  23.159  1.00 29.35           O  
ANISOU 3784  O   SER A 509     3661   3364   4126    103   -294    391       O  
ATOM   3785  CB  SER A 509      17.177 -18.178  25.714  1.00 30.16           C  
ANISOU 3785  CB  SER A 509     3671   3495   4295     56   -458    513       C  
ATOM   3786  OG  SER A 509      16.692 -19.493  25.913  1.00 32.17           O  
ANISOU 3786  OG  SER A 509     3999   3671   4554     69   -507    532       O  
ATOM   3787  N   LEU A 510      17.385 -18.653  22.626  1.00 30.22           N  
ANISOU 3787  N   LEU A 510     3620   3496   4366    199   -264    378       N  
ATOM   3788  CA  LEU A 510      17.365 -19.596  21.507  1.00 30.65           C  
ANISOU 3788  CA  LEU A 510     3685   3509   4451    277   -222    320       C  
ATOM   3789  C   LEU A 510      17.105 -21.040  21.969  1.00 31.27           C  
ANISOU 3789  C   LEU A 510     3823   3489   4570    295   -308    332       C  
ATOM   3790  O   LEU A 510      16.372 -21.787  21.311  1.00 31.35           O  
ANISOU 3790  O   LEU A 510     3893   3457   4563    312   -290    286       O  
ATOM   3791  CB  LEU A 510      18.667 -19.516  20.698  1.00 31.40           C  
ANISOU 3791  CB  LEU A 510     3677   3621   4632    361   -161    284       C  
ATOM   3792  CG  LEU A 510      18.908 -18.146  20.041  1.00 31.02           C  
ANISOU 3792  CG  LEU A 510     3580   3658   4547    342    -54    273       C  
ATOM   3793  CD1 LEU A 510      20.226 -18.124  19.292  1.00 31.97           C  
ANISOU 3793  CD1 LEU A 510     3591   3797   4758    416     18    241       C  
ATOM   3794  CD2 LEU A 510      17.754 -17.765  19.099  1.00 30.30           C  
ANISOU 3794  CD2 LEU A 510     3572   3599   4342    330     22    237       C  
ATOM   3795  N   ASP A 511      17.707 -21.432  23.090  1.00 31.80           N  
ANISOU 3795  N   ASP A 511     3878   3516   4690    292   -406    393       N  
ATOM   3796  CA  ASP A 511      17.460 -22.769  23.648  1.00 32.50           C  
ANISOU 3796  CA  ASP A 511     4038   3497   4812    303   -493    424       C  
ATOM   3797  C   ASP A 511      15.979 -22.948  23.997  1.00 31.90           C  
ANISOU 3797  C   ASP A 511     4071   3405   4644    210   -495    442       C  
ATOM   3798  O   ASP A 511      15.393 -23.998  23.737  1.00 33.61           O  
ANISOU 3798  O   ASP A 511     4353   3539   4879    215   -507    423       O  
ATOM   3799  CB  ASP A 511      18.330 -23.027  24.881  1.00 37.36           C  
ANISOU 3799  CB  ASP A 511     4634   4081   5481    315   -607    500       C  
ATOM   3800  CG  ASP A 511      19.796 -23.284  24.529  1.00 39.68           C  
ANISOU 3800  CG  ASP A 511     4814   4362   5900    425   -624    474       C  
ATOM   3801  OD1 ASP A 511      20.645 -23.288  25.452  1.00 40.53           O  
ANISOU 3801  OD1 ASP A 511     4878   4465   6056    443   -720    525       O  
ATOM   3802  OD2 ASP A 511      20.099 -23.489  23.334  1.00 34.50           O1-
ANISOU 3802  OD2 ASP A 511     4111   3706   5292    496   -544    398       O1-
ATOM   3803  N   ASP A 512      15.375 -21.912  24.573  1.00 31.06           N  
ANISOU 3803  N   ASP A 512     3979   3375   4447    124   -480    471       N  
ATOM   3804  CA  ASP A 512      13.954 -21.949  24.904  1.00 30.54           C  
ANISOU 3804  CA  ASP A 512     3997   3312   4296     34   -468    480       C  
ATOM   3805  C   ASP A 512      13.088 -22.044  23.649  1.00 30.75           C  
ANISOU 3805  C   ASP A 512     4036   3348   4300     44   -393    396       C  
ATOM   3806  O   ASP A 512      12.061 -22.728  23.644  1.00 37.23           O  
ANISOU 3806  O   ASP A 512     4919   4125   5103     -2   -398    382       O  
ATOM   3807  CB  ASP A 512      13.560 -20.720  25.733  1.00 29.82           C  
ANISOU 3807  CB  ASP A 512     3906   3309   4114    -46   -461    515       C  
ATOM   3808  CG  ASP A 512      13.969 -20.845  27.194  1.00 36.78           C  
ANISOU 3808  CG  ASP A 512     4817   4173   4984    -82   -551    601       C  
ATOM   3809  OD1 ASP A 512      14.306 -21.968  27.624  1.00 42.53           O  
ANISOU 3809  OD1 ASP A 512     5584   4813   5761    -57   -621    646       O  
ATOM   3810  OD2 ASP A 512      13.950 -19.828  27.916  1.00 41.30           O1-
ANISOU 3810  OD2 ASP A 512     5380   4817   5494   -131   -556    623       O1-
ATOM   3811  N   LEU A 513      13.496 -21.360  22.583  1.00 29.82           N  
ANISOU 3811  N   LEU A 513     3860   3288   4180    101   -324    338       N  
ATOM   3812  CA  LEU A 513      12.774 -21.466  21.322  1.00 29.62           C  
ANISOU 3812  CA  LEU A 513     3852   3277   4124    127   -263    255       C  
ATOM   3813  C   LEU A 513      12.908 -22.878  20.750  1.00 31.98           C  
ANISOU 3813  C   LEU A 513     4178   3478   4496    185   -286    208       C  
ATOM   3814  O   LEU A 513      11.969 -23.404  20.152  1.00 30.58           O  
ANISOU 3814  O   LEU A 513     4045   3276   4298    173   -277    149       O  
ATOM   3815  CB  LEU A 513      13.270 -20.433  20.311  1.00 29.28           C  
ANISOU 3815  CB  LEU A 513     3755   3315   4054    180   -180    215       C  
ATOM   3816  CG  LEU A 513      13.007 -18.975  20.698  1.00 30.22           C  
ANISOU 3816  CG  LEU A 513     3858   3520   4102    124   -150    248       C  
ATOM   3817  CD1 LEU A 513      13.425 -18.037  19.578  1.00 28.75           C  
ANISOU 3817  CD1 LEU A 513     3637   3398   3889    176    -60    213       C  
ATOM   3818  CD2 LEU A 513      11.541 -18.783  21.036  1.00 30.30           C  
ANISOU 3818  CD2 LEU A 513     3925   3552   4034     49   -160    242       C  
ATOM   3819  N   ALA A 514      14.085 -23.475  20.925  1.00 31.30           N  
ANISOU 3819  N   ALA A 514     4058   3334   4501    253   -321    228       N  
ATOM   3820  CA  ALA A 514      14.339 -24.819  20.424  1.00 32.31           C  
ANISOU 3820  CA  ALA A 514     4209   3357   4710    322   -347    182       C  
ATOM   3821  C   ALA A 514      13.486 -25.863  21.157  1.00 33.22           C  
ANISOU 3821  C   ALA A 514     4412   3368   4842    255   -416    215       C  
ATOM   3822  O   ALA A 514      13.245 -26.953  20.640  1.00 33.48           O  
ANISOU 3822  O   ALA A 514     4488   3306   4927    285   -431    162       O  
ATOM   3823  CB  ALA A 514      15.827 -25.156  20.517  1.00 33.17           C  
ANISOU 3823  CB  ALA A 514     4251   3431   4922    417   -371    197       C  
ATOM   3824  N  AARG A 515      13.042 -25.523  22.363  0.50 33.34           N  
ANISOU 3824  N  AARG A 515     4458   3398   4813    162   -454    303       N  
ATOM   3825  N  BARG A 515      13.026 -25.521  22.356  0.50 33.34           N  
ANISOU 3825  N  BARG A 515     4458   3397   4811    161   -453    302       N  
ATOM   3826  CA AARG A 515      12.142 -26.394  23.106  0.50 36.39           C  
ANISOU 3826  CA AARG A 515     4931   3696   5200     79   -500    346       C  
ATOM   3827  CA BARG A 515      12.143 -26.410  23.103  0.50 36.42           C  
ANISOU 3827  CA BARG A 515     4935   3698   5205     79   -501    346       C  
ATOM   3828  C  AARG A 515      10.783 -26.442  22.424  0.50 34.15           C  
ANISOU 3828  C  AARG A 515     4676   3430   4871     19   -454    271       C  
ATOM   3829  C  BARG A 515      10.723 -26.387  22.549  0.50 33.89           C  
ANISOU 3829  C  BARG A 515     4644   3401   4831      8   -455    280       C  
ATOM   3830  O  AARG A 515      10.118 -27.479  22.415  0.50 33.37           O  
ANISOU 3830  O  AARG A 515     4635   3233   4812    -20   -477    255       O  
ATOM   3831  O  BARG A 515       9.955 -27.327  22.753  0.50 34.24           O  
ANISOU 3831  O  BARG A 515     4752   3356   4904    -51   -479    280       O  
ATOM   3832  CB AARG A 515      11.993 -25.924  24.556  0.50 38.79           C  
ANISOU 3832  CB AARG A 515     5261   4029   5447     -6   -538    455       C  
ATOM   3833  CB BARG A 515      12.158 -26.074  24.596  0.50 40.70           C  
ANISOU 3833  CB BARG A 515     5505   4255   5704      5   -549    461       C  
ATOM   3834  CG AARG A 515      13.306 -25.869  25.319  0.50 46.95           C  
ANISOU 3834  CG AARG A 515     6266   5050   6521     50   -605    528       C  
ATOM   3835  CG BARG A 515      13.468 -26.445  25.272  0.50 48.77           C  
ANISOU 3835  CG BARG A 515     6515   5224   6793     75   -627    530       C  
ATOM   3836  CD AARG A 515      13.098 -25.527  26.789  0.50 49.96           C  
ANISOU 3836  CD AARG A 515     6696   5455   6833    -34   -653    633       C  
ATOM   3837  CD BARG A 515      13.488 -26.069  26.746  0.50 52.15           C  
ANISOU 3837  CD BARG A 515     6980   5677   7159      6   -683    640       C  
ATOM   3838  NE AARG A 515      12.213 -26.478  27.459  0.50 50.50           N  
ANISOU 3838  NE AARG A 515     6869   5431   6886   -113   -678    689       N  
ATOM   3839  NE BARG A 515      14.656 -26.634  27.417  0.50 58.35           N  
ANISOU 3839  NE BARG A 515     7766   6394   8011     77   -781    707       N  
ATOM   3840  CZ AARG A 515      11.023 -26.164  27.962  0.50 51.51           C  
ANISOU 3840  CZ AARG A 515     7043   5602   6928   -227   -638    709       C  
ATOM   3841  CZ BARG A 515      15.789 -25.975  27.638  0.50 59.31           C  
ANISOU 3841  CZ BARG A 515     7805   6576   8155    137   -815    718       C  
ATOM   3842  NH1AARG A 515      10.288 -27.094  28.556  0.50 46.19           N1+
ANISOU 3842  NH1AARG A 515     6462   4837   6252   -303   -652    764       N1+
ATOM   3843  NH2AARG A 515      10.571 -24.915  27.879  0.50 53.18           N  
ANISOU 3843  NH2AARG A 515     7205   5942   7058   -266   -579    673       N  
ATOM   3844  NH1BARG A 515      16.796 -26.583  28.252  0.50 61.17           N1+
ANISOU 3844  NH1BARG A 515     8038   6745   8457    207   -918    775       N1+
ATOM   3845  NH2BARG A 515      15.915 -24.711  27.251  0.50 55.52           N  
ANISOU 3845  NH2BARG A 515     7242   6219   7634    126   -752    671       N  
ATOM   3846  N   VAL A 516      10.378 -25.321  21.835  1.00 31.48           N  
ANISOU 3846  N   VAL A 516     4294   3212   4455     13   -392    223       N  
ATOM   3847  CA  VAL A 516       9.078 -25.246  21.185  1.00 31.19           C  
ANISOU 3847  CA  VAL A 516     4271   3208   4370    -36   -359    148       C  
ATOM   3848  C   VAL A 516       9.122 -25.975  19.847  1.00 32.10           C  
ANISOU 3848  C   VAL A 516     4391   3278   4526     42   -349     38       C  
ATOM   3849  O   VAL A 516       8.136 -26.576  19.430  1.00 33.49           O  
ANISOU 3849  O   VAL A 516     4598   3417   4708      2   -357    -28       O  
ATOM   3850  CB  VAL A 516       8.592 -23.791  20.984  1.00 30.14           C  
ANISOU 3850  CB  VAL A 516     4099   3215   4139    -57   -306    133       C  
ATOM   3851  CG1 VAL A 516       7.190 -23.779  20.377  1.00 29.98           C  
ANISOU 3851  CG1 VAL A 516     4088   3227   4075   -102   -288     54       C  
ATOM   3852  CG2 VAL A 516       8.600 -23.039  22.302  1.00 31.89           C  
ANISOU 3852  CG2 VAL A 516     4318   3482   4318   -127   -315    229       C  
ATOM   3853  N   PHE A 517      10.276 -25.932  19.188  1.00 34.23           N  
ANISOU 3853  N   PHE A 517     4628   3552   4827    152   -330     12       N  
ATOM   3854  CA  PHE A 517      10.452 -26.588  17.894  1.00 35.02           C  
ANISOU 3854  CA  PHE A 517     4734   3616   4955    240   -312    -98       C  
ATOM   3855  C   PHE A 517      11.635 -27.561  17.912  1.00 40.75           C  
ANISOU 3855  C   PHE A 517     5458   4237   5790    327   -341    -95       C  
ATOM   3856  O   PHE A 517      12.722 -27.231  17.436  1.00 37.75           O  
ANISOU 3856  O   PHE A 517     5023   3894   5424    421   -303   -108       O  
ATOM   3857  CB  PHE A 517      10.667 -25.543  16.797  1.00 33.58           C  
ANISOU 3857  CB  PHE A 517     4512   3556   4691    306   -237   -155       C  
ATOM   3858  CG  PHE A 517       9.558 -24.541  16.684  1.00 35.43           C  
ANISOU 3858  CG  PHE A 517     4748   3892   4822    242   -214   -163       C  
ATOM   3859  CD1 PHE A 517       9.670 -23.292  17.285  1.00 35.06           C  
ANISOU 3859  CD1 PHE A 517     4668   3931   4720    206   -188    -88       C  
ATOM   3860  CD2 PHE A 517       8.409 -24.832  15.967  1.00 32.00           C  
ANISOU 3860  CD2 PHE A 517     4346   3465   4349    223   -225   -253       C  
ATOM   3861  CE1 PHE A 517       8.662 -22.353  17.173  1.00 29.62           C  
ANISOU 3861  CE1 PHE A 517     3981   3331   3943    160   -168    -99       C  
ATOM   3862  CE2 PHE A 517       7.393 -23.889  15.855  1.00 35.04           C  
ANISOU 3862  CE2 PHE A 517     4724   3947   4644    177   -211   -264       C  
ATOM   3863  CZ  PHE A 517       7.528 -22.646  16.465  1.00 29.82           C  
ANISOU 3863  CZ  PHE A 517     4032   3367   3932    149   -181   -185       C  
ATOM   3864  N   PRO A 518      11.419 -28.773  18.453  1.00 39.15           N  
ANISOU 3864  N   PRO A 518     5312   3895   5668    298   -407    -76       N  
ATOM   3865  CA  PRO A 518      12.482 -29.774  18.639  1.00 37.06           C  
ANISOU 3865  CA  PRO A 518     5053   3509   5517    382   -452    -61       C  
ATOM   3866  C   PRO A 518      13.020 -30.321  17.311  1.00 42.24           C  
ANISOU 3866  C   PRO A 518     5696   4138   6215    505   -419   -188       C  
ATOM   3867  O   PRO A 518      14.166 -30.768  17.245  1.00 41.83           O  
ANISOU 3867  O   PRO A 518     5613   4034   6246    608   -430   -190       O  
ATOM   3868  CB  PRO A 518      11.784 -30.911  19.403  1.00 37.65           C  
ANISOU 3868  CB  PRO A 518     5216   3438   5653    302   -522    -19       C  
ATOM   3869  CG  PRO A 518      10.461 -30.398  19.821  1.00 40.59           C  
ANISOU 3869  CG  PRO A 518     5611   3870   5943    165   -507      5       C  
ATOM   3870  CD  PRO A 518      10.104 -29.260  18.896  1.00 38.09           C  
ANISOU 3870  CD  PRO A 518     5238   3707   5526    180   -438    -70       C  
ATOM   3871  N   THR A 519      12.180 -30.307  16.280  1.00 38.18           N  
ANISOU 3871  N   THR A 519     5206   3659   5643    498   -384   -297       N  
ATOM   3872  CA  THR A 519      12.555 -30.765  14.949  1.00 37.26           C  
ANISOU 3872  CA  THR A 519     5088   3531   5537    610   -347   -430       C  
ATOM   3873  C   THR A 519      12.089 -29.736  13.912  1.00 37.50           C  
ANISOU 3873  C   THR A 519     5101   3714   5435    620   -273   -499       C  
ATOM   3874  O   THR A 519      11.133 -29.980  13.163  1.00 36.72           O  
ANISOU 3874  O   THR A 519     5046   3618   5287    601   -280   -596       O  
ATOM   3875  CB  THR A 519      11.936 -32.145  14.640  1.00 38.90           C  
ANISOU 3875  CB  THR A 519     5374   3589   5819    602   -403   -517       C  
ATOM   3876  CG2 THR A 519      12.541 -33.217  15.546  1.00 39.46           C  
ANISOU 3876  CG2 THR A 519     5474   3492   6026    617   -473   -449       C  
ATOM   3877  OG1 THR A 519      10.518 -32.095  14.856  1.00 38.02           O  
ANISOU 3877  OG1 THR A 519     5302   3482   5661    473   -429   -521       O  
ATOM   3878  N   PRO A 520      12.782 -28.585  13.868  1.00 37.03           N  
ANISOU 3878  N   PRO A 520     4977   3774   5318    651   -208   -448       N  
ATOM   3879  CA  PRO A 520      12.411 -27.359  13.142  1.00 43.24           C  
ANISOU 3879  CA  PRO A 520     5749   4708   5972    648   -137   -468       C  
ATOM   3880  C   PRO A 520      12.216 -27.602  11.650  1.00 40.79           C  
ANISOU 3880  C   PRO A 520     5474   4428   5596    731    -94   -606       C  
ATOM   3881  O   PRO A 520      11.361 -26.976  11.020  1.00 36.77           O  
ANISOU 3881  O   PRO A 520     4992   4005   4973    711    -77   -646       O  
ATOM   3882  CB  PRO A 520      13.628 -26.445  13.338  1.00 42.83           C  
ANISOU 3882  CB  PRO A 520     5620   4731   5923    692    -73   -395       C  
ATOM   3883  CG  PRO A 520      14.404 -27.030  14.454  1.00 40.38           C  
ANISOU 3883  CG  PRO A 520     5278   4329   5736    688   -132   -318       C  
ATOM   3884  CD  PRO A 520      14.120 -28.488  14.476  1.00 35.97           C  
ANISOU 3884  CD  PRO A 520     4778   3627   5262    704   -201   -372       C  
ATOM   3885  N   GLU A 521      13.021 -28.500  11.095  1.00 36.85           N  
ANISOU 3885  N   GLU A 521     4976   3861   5164    832    -80   -679       N  
ATOM   3886  CA  GLU A 521      12.991 -28.781   9.666  1.00 39.49           C  
ANISOU 3886  CA  GLU A 521     5348   4225   5430    925    -33   -818       C  
ATOM   3887  C   GLU A 521      11.664 -29.392   9.226  1.00 38.07           C  
ANISOU 3887  C   GLU A 521     5245   4006   5215    880   -102   -918       C  
ATOM   3888  O   GLU A 521      11.381 -29.472   8.036  1.00 44.48           O  
ANISOU 3888  O   GLU A 521     6099   4864   5939    943    -78  -1037       O  
ATOM   3889  CB  GLU A 521      14.152 -29.708   9.280  1.00 48.06           C  
ANISOU 3889  CB  GLU A 521     6414   5233   6612   1045     -7   -883       C  
ATOM   3890  CG  GLU A 521      14.061 -31.105   9.881  1.00 58.74           C  
ANISOU 3890  CG  GLU A 521     7800   6409   8109   1035   -104   -904       C  
ATOM   3891  CD  GLU A 521      14.483 -31.164  11.348  1.00 64.96           C  
ANISOU 3891  CD  GLU A 521     8548   7129   9007    977   -161   -761       C  
ATOM   3892  OE1 GLU A 521      14.235 -32.210  11.990  1.00 70.84           O  
ANISOU 3892  OE1 GLU A 521     9336   7724   9855    946   -247   -750       O  
ATOM   3893  OE2 GLU A 521      15.076 -30.183  11.854  1.00 54.12           O1-
ANISOU 3893  OE2 GLU A 521     7105   5844   7614    964   -121   -660       O1-
ATOM   3894  N   LYS A 522      10.851 -29.834  10.176  1.00 37.76           N  
ANISOU 3894  N   LYS A 522     5221   3883   5242    770   -188   -873       N  
ATOM   3895  CA  LYS A 522       9.541 -30.386   9.835  1.00 38.41           C  
ANISOU 3895  CA  LYS A 522     5359   3928   5307    709   -255   -967       C  
ATOM   3896  C   LYS A 522       8.407 -29.366   9.966  1.00 41.79           C  
ANISOU 3896  C   LYS A 522     5777   4470   5632    619   -264   -934       C  
ATOM   3897  O   LYS A 522       7.226 -29.710   9.851  1.00 43.26           O  
ANISOU 3897  O   LYS A 522     5987   4637   5813    550   -325   -999       O  
ATOM   3898  CB  LYS A 522       9.235 -31.613  10.695  1.00 41.90           C  
ANISOU 3898  CB  LYS A 522     5828   4197   5893    636   -336   -953       C  
ATOM   3899  CG  LYS A 522      10.270 -32.717  10.568  1.00 41.92           C  
ANISOU 3899  CG  LYS A 522     5848   4067   6011    732   -343   -994       C  
ATOM   3900  CD  LYS A 522       9.862 -33.937  11.357  1.00 51.80           C  
ANISOU 3900  CD  LYS A 522     7146   5133   7400    657   -427   -978       C  
ATOM   3901  CE  LYS A 522      10.955 -34.999  11.312  1.00 58.43           C  
ANISOU 3901  CE  LYS A 522     8005   5831   8366    765   -440  -1008       C  
ATOM   3902  NZ  LYS A 522      10.596 -36.186  12.131  1.00 61.50           N1+
ANISOU 3902  NZ  LYS A 522     8453   6022   8893    692   -524   -975       N1+
ATOM   3903  N   VAL A 523       8.764 -28.112  10.215  1.00 39.33           N  
ANISOU 3903  N   VAL A 523     5423   4272   5247    621   -205   -837       N  
ATOM   3904  CA  VAL A 523       7.761 -27.067  10.380  1.00 37.52           C  
ANISOU 3904  CA  VAL A 523     5183   4148   4925    549   -212   -801       C  
ATOM   3905  C   VAL A 523       7.841 -26.094   9.211  1.00 35.86           C  
ANISOU 3905  C   VAL A 523     4986   4070   4569    634   -150   -843       C  
ATOM   3906  O   VAL A 523       8.862 -25.431   9.007  1.00 39.01           O  
ANISOU 3906  O   VAL A 523     5366   4523   4935    698    -70   -791       O  
ATOM   3907  CB  VAL A 523       7.918 -26.350  11.732  1.00 37.25           C  
ANISOU 3907  CB  VAL A 523     5103   4129   4922    466   -204   -651       C  
ATOM   3908  CG1 VAL A 523       6.967 -25.162  11.833  1.00 36.85           C  
ANISOU 3908  CG1 VAL A 523     5038   4193   4771    411   -199   -621       C  
ATOM   3909  CG2 VAL A 523       7.665 -27.336  12.870  1.00 39.50           C  
ANISOU 3909  CG2 VAL A 523     5394   4285   5328    376   -268   -607       C  
ATOM   3910  N   HIS A 524       6.771 -26.035   8.426  1.00 35.22           N  
ANISOU 3910  N   HIS A 524     4939   4039   4404    635   -191   -939       N  
ATOM   3911  CA  HIS A 524       6.775 -25.248   7.198  1.00 37.09           C  
ANISOU 3911  CA  HIS A 524     5211   4394   4488    727   -145   -988       C  
ATOM   3912  C   HIS A 524       5.678 -24.194   7.203  1.00 39.78           C  
ANISOU 3912  C   HIS A 524     5547   4834   4733    685   -174   -965       C  
ATOM   3913  O   HIS A 524       4.508 -24.493   6.979  1.00 42.07           O  
ANISOU 3913  O   HIS A 524     5846   5130   5008    649   -256  -1048       O  
ATOM   3914  CB  HIS A 524       6.648 -26.161   5.980  1.00 39.10           C  
ANISOU 3914  CB  HIS A 524     5525   4626   4704    809   -171  -1148       C  
ATOM   3915  CG  HIS A 524       7.653 -27.270   5.965  1.00 48.13           C  
ANISOU 3915  CG  HIS A 524     6673   5661   5952    858   -148  -1187       C  
ATOM   3916  CD2 HIS A 524       7.557 -28.565   6.353  1.00 49.53           C  
ANISOU 3916  CD2 HIS A 524     6857   5699   6265    825   -212  -1243       C  
ATOM   3917  ND1 HIS A 524       8.949 -27.096   5.528  1.00 48.56           N  
ANISOU 3917  ND1 HIS A 524     6723   5739   5987    957    -48  -1169       N  
ATOM   3918  CE1 HIS A 524       9.605 -28.237   5.639  1.00 52.86           C  
ANISOU 3918  CE1 HIS A 524     7266   6168   6649    991    -56  -1218       C  
ATOM   3919  NE2 HIS A 524       8.783 -29.144   6.134  1.00 50.74           N  
ANISOU 3919  NE2 HIS A 524     7011   5794   6475    914   -157  -1260       N  
ATOM   3920  N   ILE A 525       6.080 -22.958   7.469  1.00 37.56           N  
ANISOU 3920  N   ILE A 525     5248   4627   4397    689   -109   -854       N  
ATOM   3921  CA  ILE A 525       5.153 -21.846   7.582  1.00 35.06           C  
ANISOU 3921  CA  ILE A 525     4925   4397   4000    657   -131   -816       C  
ATOM   3922  C   ILE A 525       5.268 -20.943   6.365  1.00 35.27           C  
ANISOU 3922  C   ILE A 525     5009   4525   3866    760    -83   -832       C  
ATOM   3923  O   ILE A 525       6.299 -20.310   6.136  1.00 33.47           O  
ANISOU 3923  O   ILE A 525     4793   4326   3600    809     15   -762       O  
ATOM   3924  CB  ILE A 525       5.417 -21.049   8.869  1.00 31.99           C  
ANISOU 3924  CB  ILE A 525     4481   4007   3667    579   -100   -679       C  
ATOM   3925  CG1 ILE A 525       5.280 -21.979  10.081  1.00 31.79           C  
ANISOU 3925  CG1 ILE A 525     4414   3881   3782    479   -148   -656       C  
ATOM   3926  CG2 ILE A 525       4.457 -19.863   8.975  1.00 31.39           C  
ANISOU 3926  CG2 ILE A 525     4400   4016   3511    556   -119   -647       C  
ATOM   3927  CD1 ILE A 525       5.737 -21.380  11.385  1.00 30.82           C  
ANISOU 3927  CD1 ILE A 525     4247   3748   3714    410   -121   -527       C  
ATOM   3928  N   ASP A 526       4.208 -20.906   5.568  1.00 36.79           N  
ANISOU 3928  N   ASP A 526     5240   4772   3966    792   -152   -924       N  
ATOM   3929  CA  ASP A 526       4.202 -20.088   4.364  1.00 37.16           C  
ANISOU 3929  CA  ASP A 526     5360   4916   3842    896   -121   -939       C  
ATOM   3930  C   ASP A 526       4.316 -18.603   4.705  1.00 33.86           C  
ANISOU 3930  C   ASP A 526     4939   4556   3371    890    -65   -808       C  
ATOM   3931  O   ASP A 526       3.856 -18.159   5.758  1.00 32.90           O  
ANISOU 3931  O   ASP A 526     4758   4423   3321    807    -92   -744       O  
ATOM   3932  CB  ASP A 526       2.940 -20.335   3.548  1.00 36.21           C  
ANISOU 3932  CB  ASP A 526     5275   4843   3638    929   -232  -1065       C  
ATOM   3933  CG  ASP A 526       2.848 -19.426   2.348  1.00 43.20           C  
ANISOU 3933  CG  ASP A 526     6250   5832   4331   1041   -214  -1069       C  
ATOM   3934  OD1 ASP A 526       2.051 -18.468   2.397  1.00 41.00           O  
ANISOU 3934  OD1 ASP A 526     5971   5615   3992   1043   -257  -1031       O  
ATOM   3935  OD2 ASP A 526       3.592 -19.658   1.368  1.00 49.27           O1-
ANISOU 3935  OD2 ASP A 526     7092   6620   5007   1132   -152  -1107       O1-
ATOM   3936  N   GLN A 527       4.921 -17.848   3.797  1.00 34.34           N  
ANISOU 3936  N   GLN A 527     5068   4675   3303    978     17   -772       N  
ATOM   3937  CA  GLN A 527       5.223 -16.441   4.030  1.00 34.44           C  
ANISOU 3937  CA  GLN A 527     5089   4726   3270    976     87   -643       C  
ATOM   3938  C   GLN A 527       3.993 -15.590   4.344  1.00 37.35           C  
ANISOU 3938  C   GLN A 527     5452   5135   3604    953      5   -623       C  
ATOM   3939  O   GLN A 527       4.125 -14.523   4.942  1.00 38.80           O  
ANISOU 3939  O   GLN A 527     5619   5322   3800    921     44   -518       O  
ATOM   3940  CB  GLN A 527       5.993 -15.845   2.846  1.00 34.64           C  
ANISOU 3940  CB  GLN A 527     5205   4806   3150   1076    192   -613       C  
ATOM   3941  CG  GLN A 527       5.174 -15.679   1.584  1.00 36.13           C  
ANISOU 3941  CG  GLN A 527     5496   5069   3162   1174    136   -688       C  
ATOM   3942  CD  GLN A 527       5.955 -15.009   0.469  1.00 38.80           C  
ANISOU 3942  CD  GLN A 527     5937   5462   3343   1267    255   -638       C  
ATOM   3943  NE2 GLN A 527       6.768 -14.025   0.826  1.00 38.81           N  
ANISOU 3943  NE2 GLN A 527     5929   5454   3363   1239    369   -504       N  
ATOM   3944  OE1 GLN A 527       5.823 -15.369  -0.700  1.00 41.18           O  
ANISOU 3944  OE1 GLN A 527     6329   5814   3505   1360    246   -721       O  
ATOM   3945  N   HIS A 528       2.806 -16.060   3.962  1.00 34.67           N  
ANISOU 3945  N   HIS A 528     5118   4823   3232    969   -112   -732       N  
ATOM   3946  CA  HIS A 528       1.579 -15.295   4.207  1.00 35.22           C  
ANISOU 3946  CA  HIS A 528     5168   4937   3275    959   -197   -729       C  
ATOM   3947  C   HIS A 528       0.839 -15.724   5.470  1.00 34.72           C  
ANISOU 3947  C   HIS A 528     4999   4834   3360    843   -261   -745       C  
ATOM   3948  O   HIS A 528      -0.251 -15.230   5.755  1.00 38.33           O  
ANISOU 3948  O   HIS A 528     5418   5329   3816    827   -332   -761       O  
ATOM   3949  CB  HIS A 528       0.632 -15.376   3.005  1.00 34.75           C  
ANISOU 3949  CB  HIS A 528     5172   4949   3083   1053   -294   -837       C  
ATOM   3950  CG  HIS A 528       1.221 -14.841   1.736  1.00 37.64           C  
ANISOU 3950  CG  HIS A 528     5661   5366   3273   1173   -233   -813       C  
ATOM   3951  CD2 HIS A 528       1.491 -13.573   1.344  1.00 36.93           C  
ANISOU 3951  CD2 HIS A 528     5646   5314   3071   1234   -172   -707       C  
ATOM   3952  ND1 HIS A 528       1.594 -15.656   0.688  1.00 36.86           N  
ANISOU 3952  ND1 HIS A 528     5631   5282   3091   1243   -226   -904       N  
ATOM   3953  CE1 HIS A 528       2.076 -14.913  -0.293  1.00 37.65           C  
ANISOU 3953  CE1 HIS A 528     5843   5435   3026   1342   -156   -852       C  
ATOM   3954  NE2 HIS A 528       2.026 -13.648   0.078  1.00 41.10           N  
ANISOU 3954  NE2 HIS A 528     6288   5882   3445   1336   -122   -728       N  
ATOM   3955  N   SER A 529       1.441 -16.628   6.232  1.00 32.69           N  
ANISOU 3955  N   SER A 529     4692   4500   3227    765   -231   -739       N  
ATOM   3956  CA  SER A 529       0.759 -17.260   7.358  1.00 32.93           C  
ANISOU 3956  CA  SER A 529     4635   4485   3391    652   -287   -760       C  
ATOM   3957  C   SER A 529       0.814 -16.481   8.664  1.00 33.63           C  
ANISOU 3957  C   SER A 529     4669   4562   3546    572   -250   -650       C  
ATOM   3958  O   SER A 529       1.610 -15.557   8.820  1.00 31.62           O  
ANISOU 3958  O   SER A 529     4437   4316   3262    593   -175   -552       O  
ATOM   3959  CB  SER A 529       1.314 -18.667   7.593  1.00 32.09           C  
ANISOU 3959  CB  SER A 529     4515   4290   3388    607   -284   -803       C  
ATOM   3960  OG  SER A 529       0.906 -19.543   6.559  1.00 34.99           O  
ANISOU 3960  OG  SER A 529     4917   4659   3717    658   -346   -936       O  
ATOM   3961  N   THR A 530      -0.051 -16.885   9.591  1.00 30.47           N  
ANISOU 3961  N   THR A 530     4198   4144   3237    476   -302   -674       N  
ATOM   3962  CA  THR A 530      -0.100 -16.352  10.945  1.00 29.56           C  
ANISOU 3962  CA  THR A 530     4029   4016   3188    389   -273   -586       C  
ATOM   3963  C   THR A 530      -0.111 -17.523  11.919  1.00 32.09           C  
ANISOU 3963  C   THR A 530     4303   4259   3629    279   -284   -591       C  
ATOM   3964  O   THR A 530      -0.987 -18.392  11.845  1.00 35.27           O  
ANISOU 3964  O   THR A 530     4676   4648   4078    236   -345   -678       O  
ATOM   3965  CB  THR A 530      -1.377 -15.513  11.172  1.00 29.52           C  
ANISOU 3965  CB  THR A 530     3981   4080   3157    381   -319   -608       C  
ATOM   3966  CG2 THR A 530      -1.433 -14.978  12.606  1.00 28.69           C  
ANISOU 3966  CG2 THR A 530     3824   3965   3113    291   -282   -528       C  
ATOM   3967  OG1 THR A 530      -1.400 -14.410  10.255  1.00 30.78           O  
ANISOU 3967  OG1 THR A 530     4194   4301   3200    490   -316   -596       O  
ATOM   3968  N   LEU A 531       0.871 -17.561  12.813  1.00 29.64           N  
ANISOU 3968  N   LEU A 531     3992   3896   3374    235   -230   -497       N  
ATOM   3969  CA  LEU A 531       0.934 -18.590  13.847  1.00 28.89           C  
ANISOU 3969  CA  LEU A 531     3869   3723   3387    134   -240   -478       C  
ATOM   3970  C   LEU A 531       0.975 -17.940  15.231  1.00 28.14           C  
ANISOU 3970  C   LEU A 531     3742   3632   3317     56   -209   -381       C  
ATOM   3971  O   LEU A 531       1.945 -17.277  15.592  1.00 30.21           O  
ANISOU 3971  O   LEU A 531     4018   3894   3567     74   -164   -299       O  
ATOM   3972  CB  LEU A 531       2.153 -19.497  13.653  1.00 29.16           C  
ANISOU 3972  CB  LEU A 531     3937   3675   3468    161   -219   -463       C  
ATOM   3973  CG  LEU A 531       2.345 -20.588  14.717  1.00 30.75           C  
ANISOU 3973  CG  LEU A 531     4126   3779   3779     70   -234   -428       C  
ATOM   3974  CD1 LEU A 531       1.140 -21.545  14.739  1.00 30.02           C  
ANISOU 3974  CD1 LEU A 531     4015   3653   3738     -2   -292   -511       C  
ATOM   3975  CD2 LEU A 531       3.645 -21.366  14.501  1.00 29.64           C  
ANISOU 3975  CD2 LEU A 531     4015   3558   3688    119   -216   -412       C  
ATOM   3976  N   ILE A 532      -0.097 -18.115  15.991  1.00 28.23           N  
ANISOU 3976  N   ILE A 532     3709   3654   3363    -32   -233   -398       N  
ATOM   3977  CA  ILE A 532      -0.161 -17.612  17.360  1.00 27.70           C  
ANISOU 3977  CA  ILE A 532     3617   3594   3312   -112   -204   -318       C  
ATOM   3978  C   ILE A 532      -0.165 -18.792  18.330  1.00 28.27           C  
ANISOU 3978  C   ILE A 532     3687   3587   3467   -216   -210   -289       C  
ATOM   3979  O   ILE A 532      -0.951 -19.728  18.174  1.00 32.78           O  
ANISOU 3979  O   ILE A 532     4240   4127   4086   -266   -241   -352       O  
ATOM   3980  CB  ILE A 532      -1.397 -16.705  17.569  1.00 31.54           C  
ANISOU 3980  CB  ILE A 532     4055   4168   3763   -128   -209   -353       C  
ATOM   3981  CG1 ILE A 532      -1.271 -15.467  16.677  1.00 41.40           C  
ANISOU 3981  CG1 ILE A 532     5324   5479   4927    -18   -203   -361       C  
ATOM   3982  CG2 ILE A 532      -1.528 -16.285  19.034  1.00 28.59           C  
ANISOU 3982  CG2 ILE A 532     3658   3802   3402   -215   -173   -283       C  
ATOM   3983  CD1 ILE A 532      -2.541 -14.686  16.526  1.00 50.03           C  
ANISOU 3983  CD1 ILE A 532     6370   6652   5985      1   -228   -418       C  
ATOM   3984  N   VAL A 533       0.738 -18.766  19.305  1.00 27.94           N  
ANISOU 3984  N   VAL A 533     3667   3505   3443   -248   -186   -192       N  
ATOM   3985  CA  VAL A 533       0.862 -19.882  20.240  1.00 34.15           C  
ANISOU 3985  CA  VAL A 533     4471   4207   4298   -336   -195   -145       C  
ATOM   3986  C   VAL A 533       0.795 -19.409  21.687  1.00 32.05           C  
ANISOU 3986  C   VAL A 533     4202   3960   4013   -416   -169    -60       C  
ATOM   3987  O   VAL A 533       1.549 -18.534  22.097  1.00 33.87           O  
ANISOU 3987  O   VAL A 533     4442   4221   4207   -386   -152     -2       O  
ATOM   3988  CB  VAL A 533       2.163 -20.676  20.020  1.00 36.60           C  
ANISOU 3988  CB  VAL A 533     4824   4426   4655   -288   -210   -111       C  
ATOM   3989  CG1 VAL A 533       2.139 -21.969  20.850  1.00 32.06           C  
ANISOU 3989  CG1 VAL A 533     4279   3746   4156   -372   -232    -70       C  
ATOM   3990  CG2 VAL A 533       2.348 -20.998  18.531  1.00 32.54           C  
ANISOU 3990  CG2 VAL A 533     4319   3905   4140   -193   -224   -201       C  
ATOM   3991  N   GLU A 534      -0.126 -19.990  22.446  1.00 32.22           N  
ANISOU 3991  N   GLU A 534     4213   3968   4062   -521   -163    -58       N  
ATOM   3992  CA  GLU A 534      -0.306 -19.647  23.850  1.00 33.84           C  
ANISOU 3992  CA  GLU A 534     4425   4196   4237   -604   -132     17       C  
ATOM   3993  C   GLU A 534      -0.189 -20.897  24.704  1.00 34.15           C  
ANISOU 3993  C   GLU A 534     4511   4138   4326   -693   -138     83       C  
ATOM   3994  O   GLU A 534      -0.758 -21.931  24.375  1.00 36.96           O  
ANISOU 3994  O   GLU A 534     4866   4433   4745   -739   -150     44       O  
ATOM   3995  CB  GLU A 534      -1.686 -19.022  24.073  1.00 38.63           C  
ANISOU 3995  CB  GLU A 534     4969   4894   4814   -654    -98    -38       C  
ATOM   3996  CG  GLU A 534      -1.967 -17.801  23.200  1.00 43.81           C  
ANISOU 3996  CG  GLU A 534     5582   5639   5423   -561    -99   -105       C  
ATOM   3997  CD  GLU A 534      -3.447 -17.426  23.154  1.00 52.54           C  
ANISOU 3997  CD  GLU A 534     6613   6827   6525   -595    -83   -186       C  
ATOM   3998  OE1 GLU A 534      -4.297 -18.267  23.521  1.00 52.62           O  
ANISOU 3998  OE1 GLU A 534     6591   6820   6582   -691    -72   -209       O  
ATOM   3999  OE2 GLU A 534      -3.761 -16.287  22.739  1.00 50.06           O1-
ANISOU 3999  OE2 GLU A 534     6268   6589   6165   -524    -82   -226       O1-
ATOM   4000  N   GLY A 535       0.543 -20.794  25.804  1.00 34.02           N  
ANISOU 4000  N   GLY A 535     4542   4104   4281   -717   -136    184       N  
ATOM   4001  CA  GLY A 535       0.629 -21.878  26.755  1.00 38.16           C  
ANISOU 4001  CA  GLY A 535     5127   4538   4833   -801   -142    265       C  
ATOM   4002  C   GLY A 535       1.706 -22.903  26.447  1.00 33.57           C  
ANISOU 4002  C   GLY A 535     4599   3837   4321   -751   -197    302       C  
ATOM   4003  O   GLY A 535       2.523 -22.747  25.536  1.00 29.89           O  
ANISOU 4003  O   GLY A 535     4118   3362   3877   -647   -225    266       O  
ATOM   4004  N   ARG A 536       1.679 -23.973  27.224  1.00 35.15           N  
ANISOU 4004  N   ARG A 536     4863   3940   4554   -825   -208    375       N  
ATOM   4005  CA  ARG A 536       2.697 -25.003  27.180  1.00 37.49           C  
ANISOU 4005  CA  ARG A 536     5219   4107   4917   -780   -265    426       C  
ATOM   4006  C   ARG A 536       2.503 -25.854  25.927  1.00 35.76           C  
ANISOU 4006  C   ARG A 536     4985   3813   4789   -745   -284    331       C  
ATOM   4007  O   ARG A 536       1.791 -26.858  25.944  1.00 36.58           O  
ANISOU 4007  O   ARG A 536     5114   3831   4953   -823   -281    319       O  
ATOM   4008  CB  ARG A 536       2.595 -25.847  28.455  1.00 44.54           C  
ANISOU 4008  CB  ARG A 536     6199   4916   5807   -877   -269    541       C  
ATOM   4009  CG  ARG A 536       3.836 -26.637  28.805  1.00 52.16           C  
ANISOU 4009  CG  ARG A 536     7238   5765   6815   -818   -341    628       C  
ATOM   4010  CD  ARG A 536       5.056 -25.737  28.923  1.00 51.49           C  
ANISOU 4010  CD  ARG A 536     7129   5745   6689   -716   -379    653       C  
ATOM   4011  NE  ARG A 536       5.993 -25.988  27.832  1.00 55.01           N  
ANISOU 4011  NE  ARG A 536     7541   6145   7214   -595   -418    596       N  
ATOM   4012  CZ  ARG A 536       6.826 -27.025  27.791  1.00 55.25           C  
ANISOU 4012  CZ  ARG A 536     7617   6050   7326   -540   -478    632       C  
ATOM   4013  NH1 ARG A 536       6.844 -27.909  28.784  1.00 54.58           N1+
ANISOU 4013  NH1 ARG A 536     7623   5864   7250   -593   -514    736       N1+
ATOM   4014  NH2 ARG A 536       7.640 -27.181  26.755  1.00 52.44           N  
ANISOU 4014  NH2 ARG A 536     7219   5668   7038   -426   -500    567       N  
ATOM   4015  N   VAL A 537       3.139 -25.436  24.837  1.00 33.10           N  
ANISOU 4015  N   VAL A 537     4608   3507   4460   -629   -300    261       N  
ATOM   4016  CA  VAL A 537       2.948 -26.070  23.538  1.00 34.33           C  
ANISOU 4016  CA  VAL A 537     4749   3616   4679   -581   -316    152       C  
ATOM   4017  C   VAL A 537       4.279 -26.476  22.916  1.00 36.77           C  
ANISOU 4017  C   VAL A 537     5076   3859   5036   -460   -353    147       C  
ATOM   4018  O   VAL A 537       5.271 -25.752  23.024  1.00 38.53           O  
ANISOU 4018  O   VAL A 537     5282   4131   5226   -388   -352    187       O  
ATOM   4019  CB  VAL A 537       2.233 -25.123  22.547  1.00 31.81           C  
ANISOU 4019  CB  VAL A 537     4359   3419   4307   -548   -288     44       C  
ATOM   4020  CG1 VAL A 537       2.165 -25.758  21.152  1.00 35.13           C  
ANISOU 4020  CG1 VAL A 537     4774   3798   4777   -482   -314    -73       C  
ATOM   4021  CG2 VAL A 537       0.839 -24.769  23.047  1.00 33.10           C  
ANISOU 4021  CG2 VAL A 537     4486   3651   4440   -658   -253     28       C  
ATOM   4022  N   ILE A 538       4.293 -27.635  22.264  1.00 34.30           N  
ANISOU 4022  N   ILE A 538     4792   3432   4807   -440   -382     91       N  
ATOM   4023  CA  ILE A 538       5.467 -28.099  21.536  1.00 33.25           C  
ANISOU 4023  CA  ILE A 538     4671   3237   4728   -317   -410     62       C  
ATOM   4024  C   ILE A 538       5.029 -28.433  20.117  1.00 37.02           C  
ANISOU 4024  C   ILE A 538     5131   3710   5223   -269   -408    -82       C  
ATOM   4025  O   ILE A 538       4.092 -29.206  19.922  1.00 36.83           O  
ANISOU 4025  O   ILE A 538     5125   3623   5244   -339   -423   -140       O  
ATOM   4026  CB  ILE A 538       6.073 -29.369  22.195  1.00 39.07           C  
ANISOU 4026  CB  ILE A 538     5478   3808   5558   -322   -460    134       C  
ATOM   4027  CG1 ILE A 538       6.561 -29.060  23.614  1.00 34.29           C  
ANISOU 4027  CG1 ILE A 538     4899   3209   4920   -359   -475    279       C  
ATOM   4028  CG2 ILE A 538       7.197 -29.951  21.330  1.00 34.91           C  
ANISOU 4028  CG2 ILE A 538     4954   3211   5102   -186   -487     80       C  
ATOM   4029  CD1 ILE A 538       7.078 -30.274  24.362  1.00 36.92           C  
ANISOU 4029  CD1 ILE A 538     5315   3379   5333   -365   -533    368       C  
ATOM   4030  N   ILE A 539       5.690 -27.843  19.125  1.00 35.35           N  
ANISOU 4030  N   ILE A 539     4887   3570   4974   -154   -388   -142       N  
ATOM   4031  CA  ILE A 539       5.334 -28.093  17.733  1.00 34.05           C  
ANISOU 4031  CA  ILE A 539     4717   3417   4803    -95   -388   -281       C  
ATOM   4032  C   ILE A 539       6.437 -28.877  17.031  1.00 35.82           C  
ANISOU 4032  C   ILE A 539     4965   3555   5089     20   -400   -326       C  
ATOM   4033  O   ILE A 539       7.499 -28.330  16.720  1.00 33.97           O  
ANISOU 4033  O   ILE A 539     4705   3372   4830    117   -369   -310       O  
ATOM   4034  CB  ILE A 539       5.049 -26.782  16.971  1.00 32.50           C  
ANISOU 4034  CB  ILE A 539     4476   3378   4495    -50   -348   -328       C  
ATOM   4035  CG1 ILE A 539       3.952 -25.988  17.687  1.00 34.63           C  
ANISOU 4035  CG1 ILE A 539     4715   3731   4711   -153   -337   -291       C  
ATOM   4036  CG2 ILE A 539       4.642 -27.075  15.529  1.00 33.06           C  
ANISOU 4036  CG2 ILE A 539     4554   3464   4542     14   -357   -472       C  
ATOM   4037  CD1 ILE A 539       3.897 -24.535  17.303  1.00 35.18           C  
ANISOU 4037  CD1 ILE A 539     4747   3943   4676   -108   -298   -292       C  
ATOM   4038  N   GLU A 540       6.183 -30.163  16.806  1.00 35.37           N  
ANISOU 4038  N   GLU A 540     4954   3364   5122      6   -441   -386       N  
ATOM   4039  CA  GLU A 540       7.153 -31.057  16.179  1.00 38.54           C  
ANISOU 4039  CA  GLU A 540     5383   3664   5596    116   -457   -441       C  
ATOM   4040  C   GLU A 540       7.101 -30.976  14.657  1.00 40.33           C  
ANISOU 4040  C   GLU A 540     5603   3948   5771    211   -436   -592       C  
ATOM   4041  O   GLU A 540       8.134 -30.974  13.987  1.00 41.30           O  
ANISOU 4041  O   GLU A 540     5718   4081   5892    334   -407   -628       O  
ATOM   4042  CB  GLU A 540       6.912 -32.508  16.619  1.00 43.48           C  
ANISOU 4042  CB  GLU A 540     6073   4101   6345     62   -514   -441       C  
ATOM   4043  CG  GLU A 540       7.163 -32.766  18.100  1.00 44.77           C  
ANISOU 4043  CG  GLU A 540     6267   4186   6559    -10   -538   -283       C  
ATOM   4044  CD  GLU A 540       6.948 -34.222  18.488  1.00 53.12           C  
ANISOU 4044  CD  GLU A 540     7403   5041   7740    -60   -592   -274       C  
ATOM   4045  OE1 GLU A 540       7.211 -34.571  19.659  1.00 54.20           O  
ANISOU 4045  OE1 GLU A 540     7583   5094   7915   -108   -618   -140       O  
ATOM   4046  OE2 GLU A 540       6.518 -35.016  17.624  1.00 56.06           O1-
ANISOU 4046  OE2 GLU A 540     7801   5333   8167    -52   -610   -399       O1-
ATOM   4047  N   SER A 541       5.891 -30.914  14.116  1.00 38.81           N  
ANISOU 4047  N   SER A 541     5412   3798   5536    154   -451   -682       N  
ATOM   4048  CA  SER A 541       5.705 -30.916  12.669  1.00 39.26           C  
ANISOU 4048  CA  SER A 541     5477   3908   5532    239   -447   -833       C  
ATOM   4049  C   SER A 541       4.393 -30.239  12.292  1.00 40.19           C  
ANISOU 4049  C   SER A 541     5570   4138   5562    178   -460   -890       C  
ATOM   4050  O   SER A 541       3.354 -30.498  12.898  1.00 42.08           O  
ANISOU 4050  O   SER A 541     5798   4347   5844     55   -495   -881       O  
ATOM   4051  CB  SER A 541       5.749 -32.348  12.126  1.00 43.90           C  
ANISOU 4051  CB  SER A 541     6118   4344   6218    268   -494   -946       C  
ATOM   4052  OG  SER A 541       4.881 -33.197  12.855  1.00 39.56           O  
ANISOU 4052  OG  SER A 541     5591   3673   5768    137   -547   -933       O  
ATOM   4053  N   LEU A 542       4.454 -29.372  11.286  1.00 38.84           N  
ANISOU 4053  N   LEU A 542     5389   4098   5269    265   -430   -947       N  
ATOM   4054  CA  LEU A 542       3.317 -28.546  10.908  1.00 39.58           C  
ANISOU 4054  CA  LEU A 542     5457   4315   5268    232   -445   -990       C  
ATOM   4055  C   LEU A 542       3.498 -27.978   9.506  1.00 41.38           C  
ANISOU 4055  C   LEU A 542     5707   4650   5365    357   -426  -1081       C  
ATOM   4056  O   LEU A 542       4.578 -27.498   9.154  1.00 42.85           O  
ANISOU 4056  O   LEU A 542     5905   4876   5498    453   -359  -1042       O  
ATOM   4057  CB  LEU A 542       3.148 -27.400  11.912  1.00 35.46           C  
ANISOU 4057  CB  LEU A 542     4888   3877   4709    169   -411   -855       C  
ATOM   4058  CG  LEU A 542       2.295 -26.189  11.521  1.00 37.98           C  
ANISOU 4058  CG  LEU A 542     5176   4344   4912    173   -408   -873       C  
ATOM   4059  CD1 LEU A 542       0.814 -26.546  11.479  1.00 37.66           C  
ANISOU 4059  CD1 LEU A 542     5106   4307   4897     85   -475   -962       C  
ATOM   4060  CD2 LEU A 542       2.533 -25.055  12.503  1.00 32.75           C  
ANISOU 4060  CD2 LEU A 542     4479   3746   4220    138   -360   -735       C  
ATOM   4061  N   GLU A 543       2.436 -28.054   8.711  1.00 36.77           N  
ANISOU 4061  N   GLU A 543     5129   4112   4729    354   -484  -1204       N  
ATOM   4062  CA  GLU A 543       2.359 -27.368   7.428  1.00 38.31           C  
ANISOU 4062  CA  GLU A 543     5354   4428   4774    464   -478  -1283       C  
ATOM   4063  C   GLU A 543       1.282 -26.304   7.558  1.00 36.53           C  
ANISOU 4063  C   GLU A 543     5086   4320   4473    421   -504  -1260       C  
ATOM   4064  O   GLU A 543       0.105 -26.636   7.728  1.00 39.07           O  
ANISOU 4064  O   GLU A 543     5372   4633   4840    339   -578  -1325       O  
ATOM   4065  CB  GLU A 543       1.950 -28.350   6.325  1.00 47.00           C  
ANISOU 4065  CB  GLU A 543     6500   5490   5867    509   -545  -1462       C  
ATOM   4066  CG  GLU A 543       2.830 -29.582   6.213  1.00 58.80           C  
ANISOU 4066  CG  GLU A 543     8036   6846   7458    545   -534  -1511       C  
ATOM   4067  CD  GLU A 543       4.127 -29.313   5.478  1.00 68.58           C  
ANISOU 4067  CD  GLU A 543     9317   8125   8617    686   -448  -1506       C  
ATOM   4068  OE1 GLU A 543       4.159 -28.379   4.651  1.00 71.80           O  
ANISOU 4068  OE1 GLU A 543     9746   8665   8869    766   -413  -1516       O  
ATOM   4069  OE2 GLU A 543       5.115 -30.039   5.729  1.00 76.63           O1-
ANISOU 4069  OE2 GLU A 543    10346   9041   9729    718   -413  -1490       O1-
ATOM   4070  N   LEU A 544       1.667 -25.032   7.479  1.00 35.45           N  
ANISOU 4070  N   LEU A 544     4950   4287   4232    476   -444  -1171       N  
ATOM   4071  CA  LEU A 544       0.710 -23.943   7.695  1.00 34.81           C  
ANISOU 4071  CA  LEU A 544     4830   4309   4088    445   -467  -1138       C  
ATOM   4072  C   LEU A 544       0.610 -22.988   6.505  1.00 38.86           C  
ANISOU 4072  C   LEU A 544     5390   4943   4434    563   -464  -1173       C  
ATOM   4073  O   LEU A 544       1.576 -22.310   6.153  1.00 36.29           O  
ANISOU 4073  O   LEU A 544     5105   4654   4029    641   -383  -1104       O  
ATOM   4074  CB  LEU A 544       1.061 -23.156   8.964  1.00 35.41           C  
ANISOU 4074  CB  LEU A 544     4862   4388   4203    380   -407   -982       C  
ATOM   4075  CG  LEU A 544       0.225 -21.907   9.273  1.00 34.68           C  
ANISOU 4075  CG  LEU A 544     4731   4398   4049    359   -414   -937       C  
ATOM   4076  CD1 LEU A 544      -1.250 -22.254   9.433  1.00 37.48           C  
ANISOU 4076  CD1 LEU A 544     5029   4766   4446    282   -499  -1024       C  
ATOM   4077  CD2 LEU A 544       0.754 -21.182  10.520  1.00 31.64           C  
ANISOU 4077  CD2 LEU A 544     4314   4006   3700    302   -350   -791       C  
ATOM   4078  N   TYR A 545      -0.571 -22.951   5.895  1.00 40.49           N  
ANISOU 4078  N   TYR A 545     5588   5208   4588    572   -554  -1279       N  
ATOM   4079  CA  TYR A 545      -0.890 -22.014   4.826  1.00 39.31           C  
ANISOU 4079  CA  TYR A 545     5486   5176   4273    681   -574  -1309       C  
ATOM   4080  C   TYR A 545      -2.139 -21.248   5.232  1.00 38.77           C  
ANISOU 4080  C   TYR A 545     5351   5179   4202    637   -639  -1302       C  
ATOM   4081  O   TYR A 545      -3.236 -21.544   4.760  1.00 40.13           O  
ANISOU 4081  O   TYR A 545     5496   5386   4364    635   -744  -1423       O  
ATOM   4082  CB  TYR A 545      -1.156 -22.757   3.513  1.00 41.66           C  
ANISOU 4082  CB  TYR A 545     5844   5488   4495    761   -646  -1470       C  
ATOM   4083  CG  TYR A 545       0.093 -23.198   2.790  1.00 58.35           C  
ANISOU 4083  CG  TYR A 545     8042   7571   6556    850   -570  -1485       C  
ATOM   4084  CD1 TYR A 545       0.579 -22.480   1.702  1.00 64.68           C  
ANISOU 4084  CD1 TYR A 545     8932   8461   7181    978   -523  -1478       C  
ATOM   4085  CD2 TYR A 545       0.794 -24.328   3.197  1.00 65.64           C  
ANISOU 4085  CD2 TYR A 545     8958   8375   7608    809   -540  -1503       C  
ATOM   4086  CE1 TYR A 545       1.726 -22.881   1.037  1.00 73.86           C  
ANISOU 4086  CE1 TYR A 545    10163   9603   8295   1059   -438  -1496       C  
ATOM   4087  CE2 TYR A 545       1.942 -24.734   2.537  1.00 71.46           C  
ANISOU 4087  CE2 TYR A 545     9759   9086   8305    899   -466  -1525       C  
ATOM   4088  CZ  TYR A 545       2.403 -24.007   1.459  1.00 76.68           C  
ANISOU 4088  CZ  TYR A 545    10499   9847   8790   1022   -410  -1525       C  
ATOM   4089  OH  TYR A 545       3.546 -24.405   0.796  1.00 83.17           O  
ANISOU 4089  OH  TYR A 545    11378  10652   9571   1110   -322  -1552       O  
ATOM   4090  N   GLY A 546      -1.977 -20.278   6.123  1.00 36.40           N  
ANISOU 4090  N   GLY A 546     5017   4898   3916    601   -579  -1171       N  
ATOM   4091  CA  GLY A 546      -3.120 -19.581   6.676  1.00 34.49           C  
ANISOU 4091  CA  GLY A 546     4700   4713   3691    554   -628  -1163       C  
ATOM   4092  C   GLY A 546      -2.872 -19.154   8.108  1.00 33.11           C  
ANISOU 4092  C   GLY A 546     4469   4504   3605    458   -558  -1037       C  
ATOM   4093  O   GLY A 546      -1.729 -18.985   8.519  1.00 32.38           O  
ANISOU 4093  O   GLY A 546     4410   4370   3524    457   -472   -935       O  
ATOM   4094  N   ALA A 547      -3.944 -18.979   8.872  1.00 32.99           N  
ANISOU 4094  N   ALA A 547     4367   4513   3654    377   -596  -1049       N  
ATOM   4095  CA  ALA A 547      -3.822 -18.531  10.253  1.00 31.97           C  
ANISOU 4095  CA  ALA A 547     4189   4363   3594    287   -533   -939       C  
ATOM   4096  C   ALA A 547      -4.203 -19.645  11.213  1.00 38.36           C  
ANISOU 4096  C   ALA A 547     4937   5097   4540    148   -539   -956       C  
ATOM   4097  O   ALA A 547      -5.204 -20.339  11.010  1.00 40.56           O  
ANISOU 4097  O   ALA A 547     5162   5376   4871    100   -607  -1063       O  
ATOM   4098  CB  ALA A 547      -4.685 -17.292  10.497  1.00 31.71           C  
ANISOU 4098  CB  ALA A 547     4110   4420   3520    306   -548   -922       C  
ATOM   4099  N   LEU A 548      -3.395 -19.806  12.256  1.00 31.40           N  
ANISOU 4099  N   LEU A 548     4066   4149   3717     82   -469   -849       N  
ATOM   4100  CA  LEU A 548      -3.596 -20.852  13.249  1.00 35.49           C  
ANISOU 4100  CA  LEU A 548     4548   4583   4354    -49   -463   -838       C  
ATOM   4101  C   LEU A 548      -3.239 -20.347  14.639  1.00 35.03           C  
ANISOU 4101  C   LEU A 548     4476   4514   4321   -120   -396   -710       C  
ATOM   4102  O   LEU A 548      -2.233 -19.666  14.827  1.00 35.48           O  
ANISOU 4102  O   LEU A 548     4573   4575   4332    -71   -348   -620       O  
ATOM   4103  CB  LEU A 548      -2.745 -22.081  12.916  1.00 34.44           C  
ANISOU 4103  CB  LEU A 548     4473   4340   4273    -43   -467   -856       C  
ATOM   4104  CG  LEU A 548      -2.619 -23.180  13.982  1.00 36.30           C  
ANISOU 4104  CG  LEU A 548     4704   4460   4630   -165   -452   -810       C  
ATOM   4105  CD1 LEU A 548      -3.960 -23.868  14.248  1.00 33.25           C  
ANISOU 4105  CD1 LEU A 548     4251   4057   4324   -280   -495   -890       C  
ATOM   4106  CD2 LEU A 548      -1.561 -24.209  13.575  1.00 32.77           C  
ANISOU 4106  CD2 LEU A 548     4324   3902   4223   -124   -454   -819       C  
ATOM   4107  N   THR A 549      -4.082 -20.684  15.607  1.00 35.57           N  
ANISOU 4107  N   THR A 549     4484   4572   4459   -240   -391   -706       N  
ATOM   4108  CA  THR A 549      -3.786 -20.462  17.011  1.00 32.88           C  
ANISOU 4108  CA  THR A 549     4139   4210   4142   -323   -331   -592       C  
ATOM   4109  C   THR A 549      -3.706 -21.811  17.707  1.00 36.65           C  
ANISOU 4109  C   THR A 549     4632   4575   4717   -433   -327   -567       C  
ATOM   4110  O   THR A 549      -4.597 -22.643  17.555  1.00 38.45           O  
ANISOU 4110  O   THR A 549     4822   4775   5013   -503   -357   -645       O  
ATOM   4111  CB  THR A 549      -4.871 -19.603  17.667  1.00 33.98           C  
ANISOU 4111  CB  THR A 549     4203   4441   4266   -371   -312   -598       C  
ATOM   4112  CG2 THR A 549      -4.667 -19.522  19.186  1.00 32.43           C  
ANISOU 4112  CG2 THR A 549     4010   4224   4090   -470   -249   -491       C  
ATOM   4113  OG1 THR A 549      -4.813 -18.286  17.118  1.00 29.73           O  
ANISOU 4113  OG1 THR A 549     3667   3990   3638   -261   -315   -601       O  
ATOM   4114  N   ILE A 550      -2.624 -22.043  18.445  1.00 34.96           N  
ANISOU 4114  N   ILE A 550     4474   4292   4516   -446   -294   -460       N  
ATOM   4115  CA  ILE A 550      -2.499 -23.269  19.228  1.00 34.99           C  
ANISOU 4115  CA  ILE A 550     4508   4180   4607   -547   -291   -414       C  
ATOM   4116  C   ILE A 550      -2.479 -22.900  20.704  1.00 35.10           C  
ANISOU 4116  C   ILE A 550     4524   4206   4608   -632   -240   -300       C  
ATOM   4117  O   ILE A 550      -1.692 -22.054  21.134  1.00 32.26           O  
ANISOU 4117  O   ILE A 550     4185   3882   4189   -585   -216   -224       O  
ATOM   4118  CB  ILE A 550      -1.223 -24.059  18.862  1.00 33.44           C  
ANISOU 4118  CB  ILE A 550     4384   3876   4444   -483   -310   -388       C  
ATOM   4119  CG1 ILE A 550      -1.142 -24.262  17.348  1.00 37.55           C  
ANISOU 4119  CG1 ILE A 550     4912   4404   4952   -380   -350   -505       C  
ATOM   4120  CG2 ILE A 550      -1.178 -25.392  19.599  1.00 34.16           C  
ANISOU 4120  CG2 ILE A 550     4515   3832   4633   -580   -317   -344       C  
ATOM   4121  CD1 ILE A 550       0.159 -24.873  16.868  1.00 37.87           C  
ANISOU 4121  CD1 ILE A 550     5014   4359   5015   -295   -357   -492       C  
ATOM   4122  N   ARG A 551      -3.356 -23.521  21.481  1.00 34.13           N  
ANISOU 4122  N   ARG A 551     4378   4052   4536   -760   -220   -291       N  
ATOM   4123  CA  ARG A 551      -3.437 -23.212  22.901  1.00 36.69           C  
ANISOU 4123  CA  ARG A 551     4712   4395   4833   -847   -165   -188       C  
ATOM   4124  C   ARG A 551      -3.103 -24.432  23.737  1.00 40.92           C  
ANISOU 4124  C   ARG A 551     5317   4801   5429   -938   -159   -102       C  
ATOM   4125  O   ARG A 551      -3.616 -25.522  23.493  1.00 44.49           O  
ANISOU 4125  O   ARG A 551     5770   5167   5966  -1005   -173   -143       O  
ATOM   4126  CB  ARG A 551      -4.829 -22.695  23.263  1.00 41.43           C  
ANISOU 4126  CB  ARG A 551     5224   5094   5422   -924   -124   -238       C  
ATOM   4127  CG  ARG A 551      -5.230 -21.434  22.517  1.00 45.10           C  
ANISOU 4127  CG  ARG A 551     5624   5685   5827   -828   -136   -317       C  
ATOM   4128  CD  ARG A 551      -6.401 -20.739  23.196  1.00 51.54           C  
ANISOU 4128  CD  ARG A 551     6356   6602   6623   -893    -84   -341       C  
ATOM   4129  NE  ARG A 551      -6.767 -19.510  22.500  1.00 54.01           N  
ANISOU 4129  NE  ARG A 551     6614   7025   6883   -789   -104   -412       N  
ATOM   4130  CZ  ARG A 551      -7.827 -19.389  21.707  1.00 58.23           C  
ANISOU 4130  CZ  ARG A 551     7060   7621   7442   -769   -138   -529       C  
ATOM   4131  NH1 ARG A 551      -8.641 -20.418  21.523  1.00 56.40           N1+
ANISOU 4131  NH1 ARG A 551     6776   7356   7297   -857   -153   -597       N1+
ATOM   4132  NH2 ARG A 551      -8.079 -18.232  21.107  1.00 61.65           N  
ANISOU 4132  NH2 ARG A 551     7460   8146   7819   -662   -162   -578       N  
ATOM   4133  N   GLY A 552      -2.233 -24.244  24.722  1.00 34.90           N  
ANISOU 4133  N   GLY A 552     4617   4018   4624   -938   -144     18       N  
ATOM   4134  CA  GLY A 552      -1.894 -25.312  25.640  1.00 38.48           C  
ANISOU 4134  CA  GLY A 552     5150   4352   5118  -1018   -142    119       C  
ATOM   4135  C   GLY A 552      -2.150 -24.858  27.059  1.00 40.17           C  
ANISOU 4135  C   GLY A 552     5385   4618   5261  -1103    -86    216       C  
ATOM   4136  O   GLY A 552      -2.609 -23.735  27.276  1.00 38.74           O  
ANISOU 4136  O   GLY A 552     5148   4563   5009  -1098    -47    191       O  
ATOM   4137  N   PRO A 553      -1.835 -25.719  28.035  1.00 40.99           N  
ANISOU 4137  N   PRO A 553     5576   4621   5376  -1175    -82    328       N  
ATOM   4138  CA  PRO A 553      -1.993 -25.403  29.457  1.00 40.21           C  
ANISOU 4138  CA  PRO A 553     5520   4564   5193  -1257    -29    432       C  
ATOM   4139  C   PRO A 553      -1.342 -24.069  29.813  1.00 43.81           C  
ANISOU 4139  C   PRO A 553     5967   5133   5547  -1176    -34    452       C  
ATOM   4140  O   PRO A 553      -0.217 -23.808  29.383  1.00 40.87           O  
ANISOU 4140  O   PRO A 553     5609   4744   5176  -1065    -94    459       O  
ATOM   4141  CB  PRO A 553      -1.235 -26.540  30.144  1.00 45.23           C  
ANISOU 4141  CB  PRO A 553     6276   5053   5856  -1285    -64    556       C  
ATOM   4142  CG  PRO A 553      -1.322 -27.676  29.182  1.00 48.65           C  
ANISOU 4142  CG  PRO A 553     6711   5359   6415  -1282   -102    498       C  
ATOM   4143  CD  PRO A 553      -1.234 -27.048  27.825  1.00 42.80           C  
ANISOU 4143  CD  PRO A 553     5881   4686   5695  -1171   -133    365       C  
ATOM   4144  N   THR A 554      -2.039 -23.246  30.593  1.00 43.96           N  
ANISOU 4144  N   THR A 554     5958   5262   5483  -1233     32    456       N  
ATOM   4145  CA  THR A 554      -1.497 -21.962  31.029  1.00 47.13           C  
ANISOU 4145  CA  THR A 554     6356   5763   5788  -1168     29    469       C  
ATOM   4146  C   THR A 554      -0.454 -22.147  32.126  1.00 45.43           C  
ANISOU 4146  C   THR A 554     6246   5504   5512  -1168     -6    595       C  
ATOM   4147  O   THR A 554       0.243 -21.203  32.493  1.00 44.56           O  
ANISOU 4147  O   THR A 554     6143   5455   5334  -1109    -29    612       O  
ATOM   4148  CB  THR A 554      -2.601 -21.031  31.565  1.00 49.93           C  
ANISOU 4148  CB  THR A 554     6651   6246   6074  -1225    112    424       C  
ATOM   4149  CG2 THR A 554      -3.475 -20.525  30.429  1.00 47.67           C  
ANISOU 4149  CG2 THR A 554     6250   6025   5836  -1188    125    292       C  
ATOM   4150  OG1 THR A 554      -3.410 -21.751  32.507  1.00 49.05           O  
ANISOU 4150  OG1 THR A 554     6571   6118   5948  -1360    182    477       O  
ATOM   4151  N   ASP A 555      -0.361 -23.362  32.653  1.00 41.09           N  
ANISOU 4151  N   ASP A 555     5779   4845   4990  -1233    -16    683       N  
ATOM   4152  CA  ASP A 555       0.623 -23.675  33.683  1.00 49.54           C  
ANISOU 4152  CA  ASP A 555     6958   5862   6002  -1226    -65    810       C  
ATOM   4153  C   ASP A 555       1.905 -24.210  33.047  1.00 51.38           C  
ANISOU 4153  C   ASP A 555     7215   5994   6314  -1118   -166    829       C  
ATOM   4154  O   ASP A 555       1.890 -25.246  32.383  1.00 50.52           O  
ANISOU 4154  O   ASP A 555     7117   5774   6307  -1116   -187    817       O  
ATOM   4155  CB  ASP A 555       0.051 -24.699  34.666  1.00 52.50           C  
ANISOU 4155  CB  ASP A 555     7427   6166   6355  -1352    -21    911       C  
ATOM   4156  CG  ASP A 555       1.072 -25.173  35.683  1.00 60.00           C  
ANISOU 4156  CG  ASP A 555     8506   7046   7246  -1336    -88   1051       C  
ATOM   4157  OD1 ASP A 555       2.088 -24.475  35.892  1.00 57.98           O  
ANISOU 4157  OD1 ASP A 555     8256   6834   6941  -1244   -157   1064       O  
ATOM   4158  OD2 ASP A 555       0.852 -26.249  36.279  1.00 71.12           O1-
ANISOU 4158  OD2 ASP A 555    10012   8352   8660  -1417    -75   1148       O1-
ATOM   4159  N   SER A 556       3.012 -23.504  33.261  1.00 49.92           N  
ANISOU 4159  N   SER A 556     7034   5846   6088  -1030   -226    852       N  
ATOM   4160  CA  SER A 556       4.280 -23.871  32.636  1.00 53.36           C  
ANISOU 4160  CA  SER A 556     7468   6205   6602   -918   -313    858       C  
ATOM   4161  C   SER A 556       4.770 -25.261  33.050  1.00 58.07           C  
ANISOU 4161  C   SER A 556     8162   6653   7249   -925   -372    956       C  
ATOM   4162  O   SER A 556       5.579 -25.869  32.349  1.00 62.34           O  
ANISOU 4162  O   SER A 556     8696   7104   7885   -840   -433    945       O  
ATOM   4163  CB  SER A 556       5.353 -22.819  32.933  1.00 53.31           C  
ANISOU 4163  CB  SER A 556     7439   6272   6545   -839   -363    867       C  
ATOM   4164  OG  SER A 556       5.665 -22.786  34.314  1.00 59.69           O  
ANISOU 4164  OG  SER A 556     8330   7091   7259   -876   -396    967       O  
ATOM   4165  N   MET A 557       4.274 -25.764  34.178  1.00 55.20           N  
ANISOU 4165  N   MET A 557     7893   6260   6820  -1024   -350   1054       N  
ATOM   4166  CA  MET A 557       4.713 -27.059  34.695  1.00 54.01           C  
ANISOU 4166  CA  MET A 557     7856   5959   6705  -1034   -408   1167       C  
ATOM   4167  C   MET A 557       3.800 -28.214  34.295  1.00 55.11           C  
ANISOU 4167  C   MET A 557     8024   5982   6933  -1119   -359   1161       C  
ATOM   4168  O   MET A 557       4.082 -29.368  34.613  1.00 56.76           O  
ANISOU 4168  O   MET A 557     8332   6044   7190  -1131   -402   1250       O  
ATOM   4169  CB  MET A 557       4.838 -27.014  36.218  1.00 53.73           C  
ANISOU 4169  CB  MET A 557     7933   5944   6539  -1087   -421   1297       C  
ATOM   4170  CG  MET A 557       5.961 -26.125  36.726  1.00 52.51           C  
ANISOU 4170  CG  MET A 557     7770   5869   6311   -997   -504   1318       C  
ATOM   4171  SD  MET A 557       6.106 -26.176  38.524  1.00133.20           S  
ANISOU 4171  SD  MET A 557    18141  16109  16359  -1054   -535   1469       S  
ATOM   4172  CE  MET A 557       4.484 -25.591  39.013  1.00 70.87           C  
ANISOU 4172  CE  MET A 557    10241   8331   8354  -1204   -374   1438       C  
ATOM   4173  N   ALA A 558       2.701 -27.911  33.610  1.00 53.46           N  
ANISOU 4173  N   ALA A 558     7729   5834   6751  -1179   -275   1054       N  
ATOM   4174  CA  ALA A 558       1.782 -28.959  33.168  1.00 55.07           C  
ANISOU 4174  CA  ALA A 558     7941   5934   7049  -1269   -232   1028       C  
ATOM   4175  C   ALA A 558       2.339 -29.686  31.945  1.00 52.58           C  
ANISOU 4175  C   ALA A 558     7603   5505   6871  -1176   -297    957       C  
ATOM   4176  O   ALA A 558       3.267 -29.198  31.299  1.00 46.47           O  
ANISOU 4176  O   ALA A 558     6779   4765   6113  -1046   -353    907       O  
ATOM   4177  CB  ALA A 558       0.411 -28.373  32.863  1.00 55.54           C  
ANISOU 4177  CB  ALA A 558     7903   6105   7094  -1359   -130    929       C  
ATOM   4178  N   LEU A 559       1.772 -30.849  31.632  1.00 54.74           N  
ANISOU 4178  N   LEU A 559     7911   5641   7245  -1246   -285    948       N  
ATOM   4179  CA  LEU A 559       2.193 -31.614  30.459  1.00 55.22           C  
ANISOU 4179  CA  LEU A 559     7956   5587   7437  -1164   -342    866       C  
ATOM   4180  C   LEU A 559       1.849 -30.870  29.167  1.00 54.05           C  
ANISOU 4180  C   LEU A 559     7679   5550   7308  -1108   -324    700       C  
ATOM   4181  O   LEU A 559       0.728 -30.384  29.005  1.00 54.99           O  
ANISOU 4181  O   LEU A 559     7727   5765   7402  -1189   -257    632       O  
ATOM   4182  CB  LEU A 559       1.552 -33.004  30.457  1.00 60.51           C  
ANISOU 4182  CB  LEU A 559     8698   6081   8213  -1267   -330    886       C  
ATOM   4183  CG  LEU A 559       1.855 -33.879  31.676  1.00 67.99           C  
ANISOU 4183  CG  LEU A 559     9795   6891   9147  -1324   -349   1062       C  
ATOM   4184  CD1 LEU A 559       1.417 -35.312  31.422  1.00 66.55           C  
ANISOU 4184  CD1 LEU A 559     9684   6503   9100  -1401   -351   1067       C  
ATOM   4185  CD2 LEU A 559       3.340 -33.825  32.024  1.00 70.54           C  
ANISOU 4185  CD2 LEU A 559    10176   7184   9443  -1178   -449   1144       C  
ATOM   4186  N   PRO A 560       2.814 -30.792  28.236  1.00 50.45           N  
ANISOU 4186  N   PRO A 560     7192   5083   6895   -965   -383    636       N  
ATOM   4187  CA  PRO A 560       2.668 -29.955  27.038  1.00 45.17           C  
ANISOU 4187  CA  PRO A 560     6415   4530   6217   -892   -369    496       C  
ATOM   4188  C   PRO A 560       1.663 -30.497  26.030  1.00 43.49           C  
ANISOU 4188  C   PRO A 560     6161   4283   6079   -938   -351    369       C  
ATOM   4189  O   PRO A 560       1.480 -31.711  25.896  1.00 42.30           O  
ANISOU 4189  O   PRO A 560     6065   3981   6027   -980   -373    364       O  
ATOM   4190  CB  PRO A 560       4.068 -29.982  26.407  1.00 48.61           C  
ANISOU 4190  CB  PRO A 560     6850   4934   6688   -734   -430    480       C  
ATOM   4191  CG  PRO A 560       4.959 -30.720  27.380  1.00 51.47           C  
ANISOU 4191  CG  PRO A 560     7307   5176   7075   -719   -486    613       C  
ATOM   4192  CD  PRO A 560       4.072 -31.554  28.229  1.00 49.16           C  
ANISOU 4192  CD  PRO A 560     7095   4789   6796   -861   -464    690       C  
ATOM   4193  N   HIS A 561       1.021 -29.580  25.318  1.00 41.33           N  
ANISOU 4193  N   HIS A 561     5795   4148   5763   -925   -320    263       N  
ATOM   4194  CA  HIS A 561       0.222 -29.923  24.155  1.00 42.29           C  
ANISOU 4194  CA  HIS A 561     5864   4262   5944   -933   -324    120       C  
ATOM   4195  C   HIS A 561       1.182 -30.070  22.982  1.00 42.16           C  
ANISOU 4195  C   HIS A 561     5847   4214   5956   -783   -374     43       C  
ATOM   4196  O   HIS A 561       1.783 -29.092  22.535  1.00 40.37           O  
ANISOU 4196  O   HIS A 561     5583   4095   5662   -679   -371     23       O  
ATOM   4197  CB  HIS A 561      -0.801 -28.817  23.876  1.00 44.41           C  
ANISOU 4197  CB  HIS A 561     6034   4697   6143   -961   -281     43       C  
ATOM   4198  CG  HIS A 561      -1.613 -29.034  22.632  1.00 51.24           C  
ANISOU 4198  CG  HIS A 561     6837   5578   7055   -954   -300   -114       C  
ATOM   4199  CD2 HIS A 561      -2.491 -28.223  21.994  1.00 53.72           C  
ANISOU 4199  CD2 HIS A 561     7061   6022   7328   -946   -290   -217       C  
ATOM   4200  ND1 HIS A 561      -1.568 -30.200  21.903  1.00 54.65           N  
ANISOU 4200  ND1 HIS A 561     7302   5878   7586   -947   -346   -185       N  
ATOM   4201  CE1 HIS A 561      -2.383 -30.103  20.867  1.00 56.03           C  
ANISOU 4201  CE1 HIS A 561     7408   6107   7773   -939   -365   -329       C  
ATOM   4202  NE2 HIS A 561      -2.954 -28.913  20.898  1.00 55.03           N  
ANISOU 4202  NE2 HIS A 561     7206   6141   7562   -936   -334   -348       N  
ATOM   4203  N   VAL A 562       1.339 -31.295  22.497  1.00 40.58           N  
ANISOU 4203  N   VAL A 562     5695   3865   5859   -774   -414      0       N  
ATOM   4204  CA  VAL A 562       2.271 -31.576  21.415  1.00 44.00           C  
ANISOU 4204  CA  VAL A 562     6136   4257   6325   -631   -454    -78       C  
ATOM   4205  C   VAL A 562       1.531 -31.629  20.086  1.00 44.67           C  
ANISOU 4205  C   VAL A 562     6173   4379   6421   -610   -464   -246       C  
ATOM   4206  O   VAL A 562       0.526 -32.324  19.954  1.00 46.00           O  
ANISOU 4206  O   VAL A 562     6338   4486   6653   -710   -473   -310       O  
ATOM   4207  CB  VAL A 562       3.019 -32.914  21.639  1.00 46.27           C  
ANISOU 4207  CB  VAL A 562     6513   4347   6722   -607   -501    -33       C  
ATOM   4208  CG1 VAL A 562       4.090 -33.100  20.580  1.00 44.92           C  
ANISOU 4208  CG1 VAL A 562     6340   4150   6578   -445   -532   -113       C  
ATOM   4209  CG2 VAL A 562       3.641 -32.947  23.026  1.00 44.52           C  
ANISOU 4209  CG2 VAL A 562     6349   4082   6485   -634   -506    139       C  
ATOM   4210  N   VAL A 563       2.032 -30.880  19.110  1.00 41.76           N  
ANISOU 4210  N   VAL A 563     5766   4113   5987   -485   -462   -318       N  
ATOM   4211  CA  VAL A 563       1.454 -30.855  17.777  1.00 41.27           C  
ANISOU 4211  CA  VAL A 563     5671   4100   5911   -441   -479   -477       C  
ATOM   4212  C   VAL A 563       2.338 -31.654  16.817  1.00 42.85           C  
ANISOU 4212  C   VAL A 563     5916   4206   6160   -323   -511   -557       C  
ATOM   4213  O   VAL A 563       3.530 -31.369  16.675  1.00 43.97           O  
ANISOU 4213  O   VAL A 563     6068   4361   6277   -210   -497   -519       O  
ATOM   4214  CB  VAL A 563       1.296 -29.405  17.272  1.00 43.68           C  
ANISOU 4214  CB  VAL A 563     5913   4592   6091   -380   -450   -505       C  
ATOM   4215  CG1 VAL A 563       0.877 -29.379  15.812  1.00 37.89           C  
ANISOU 4215  CG1 VAL A 563     5162   3910   5324   -308   -477   -664       C  
ATOM   4216  CG2 VAL A 563       0.300 -28.641  18.143  1.00 45.95           C  
ANISOU 4216  CG2 VAL A 563     6150   4971   6336   -491   -420   -451       C  
ATOM   4217  N   ARG A 564       1.753 -32.662  16.177  1.00 45.05           N  
ANISOU 4217  N   ARG A 564     6216   4387   6514   -351   -552   -675       N  
ATOM   4218  CA  ARG A 564       2.473 -33.494  15.216  1.00 48.02           C  
ANISOU 4218  CA  ARG A 564     6638   4667   6939   -241   -584   -774       C  
ATOM   4219  C   ARG A 564       1.632 -33.700  13.961  1.00 47.35           C  
ANISOU 4219  C   ARG A 564     6537   4615   6837   -228   -619   -957       C  
ATOM   4220  O   ARG A 564       0.411 -33.827  14.041  1.00 45.48           O  
ANISOU 4220  O   ARG A 564     6269   4388   6626   -344   -642  -1007       O  
ATOM   4221  CB  ARG A 564       2.790 -34.869  15.810  1.00 50.33           C  
ANISOU 4221  CB  ARG A 564     7004   4747   7373   -283   -616   -733       C  
ATOM   4222  CG  ARG A 564       3.135 -34.891  17.287  1.00 54.04           C  
ANISOU 4222  CG  ARG A 564     7501   5162   7872   -353   -600   -547       C  
ATOM   4223  CD  ARG A 564       3.264 -36.340  17.774  1.00 61.89           C  
ANISOU 4223  CD  ARG A 564     8580   5927   9008   -401   -641   -514       C  
ATOM   4224  NE  ARG A 564       3.662 -36.424  19.177  1.00 65.24           N  
ANISOU 4224  NE  ARG A 564     9048   6291   9448   -455   -634   -330       N  
ATOM   4225  CZ  ARG A 564       2.808 -36.424  20.197  1.00 68.20           C  
ANISOU 4225  CZ  ARG A 564     9434   6656   9821   -611   -612   -234       C  
ATOM   4226  NH1 ARG A 564       3.257 -36.502  21.444  1.00 69.00           N1+
ANISOU 4226  NH1 ARG A 564     9590   6707   9919   -645   -609    -66       N1+
ATOM   4227  NH2 ARG A 564       1.504 -36.342  19.969  1.00 70.05           N  
ANISOU 4227  NH2 ARG A 564     9623   6938  10055   -731   -591   -311       N  
ATOM   4228  N   ASN A 565       2.296 -33.759  12.810  1.00 46.44           N  
ANISOU 4228  N   ASN A 565     6443   4519   6682    -87   -625  -1061       N  
ATOM   4229  CA  ASN A 565       1.632 -33.973  11.525  1.00 49.09           C  
ANISOU 4229  CA  ASN A 565     6779   4890   6984    -52   -668  -1245       C  
ATOM   4230  C   ASN A 565       0.392 -33.116  11.321  1.00 50.50           C  
ANISOU 4230  C   ASN A 565     6891   5216   7080   -117   -682  -1287       C  
ATOM   4231  O   ASN A 565      -0.637 -33.599  10.849  1.00 51.67           O  
ANISOU 4231  O   ASN A 565     7024   5346   7264   -179   -740  -1413       O  
ATOM   4232  CB  ASN A 565       1.280 -35.448  11.339  1.00 53.88           C  
ANISOU 4232  CB  ASN A 565     7433   5309   7728   -105   -728  -1348       C  
ATOM   4233  CG  ASN A 565       2.475 -36.345  11.523  1.00 55.81           C  
ANISOU 4233  CG  ASN A 565     7747   5395   8064    -30   -723  -1313       C  
ATOM   4234  ND2 ASN A 565       3.497 -36.144  10.696  1.00 56.78           N  
ANISOU 4234  ND2 ASN A 565     7887   5564   8124    131   -697  -1363       N  
ATOM   4235  OD1 ASN A 565       2.494 -37.194  12.411  1.00 59.66           O  
ANISOU 4235  OD1 ASN A 565     8271   5721   8677   -113   -739  -1237       O  
ATOM   4236  N   ALA A 566       0.491 -31.841  11.676  1.00 43.36           N  
ANISOU 4236  N   ALA A 566     5944   4456   6074   -100   -633  -1188       N  
ATOM   4237  CA  ALA A 566      -0.619 -30.923  11.462  1.00 43.19           C  
ANISOU 4237  CA  ALA A 566     5858   4580   5971   -138   -647  -1226       C  
ATOM   4238  C   ALA A 566      -0.523 -30.284  10.081  1.00 45.28           C  
ANISOU 4238  C   ALA A 566     6134   4969   6102     -1   -661  -1333       C  
ATOM   4239  O   ALA A 566       0.563 -29.928   9.626  1.00 49.14           O  
ANISOU 4239  O   ALA A 566     6662   5487   6521    120   -615  -1306       O  
ATOM   4240  CB  ALA A 566      -0.649 -29.851  12.550  1.00 41.44           C  
ANISOU 4240  CB  ALA A 566     5591   4445   5708   -189   -591  -1072       C  
ATOM   4241  N   VAL A 567      -1.667 -30.150   9.421  1.00 43.00           N  
ANISOU 4241  N   VAL A 567     5810   4752   5776    -21   -723  -1453       N  
ATOM   4242  CA  VAL A 567      -1.752 -29.499   8.121  1.00 42.94           C  
ANISOU 4242  CA  VAL A 567     5820   4871   5624    105   -749  -1553       C  
ATOM   4243  C   VAL A 567      -2.933 -28.548   8.163  1.00 44.92           C  
ANISOU 4243  C   VAL A 567     5996   5256   5815     66   -783  -1563       C  
ATOM   4244  O   VAL A 567      -4.079 -28.981   8.291  1.00 42.66           O  
ANISOU 4244  O   VAL A 567     5651   4956   5603    -33   -847  -1644       O  
ATOM   4245  CB  VAL A 567      -1.974 -30.516   6.983  1.00 48.40           C  
ANISOU 4245  CB  VAL A 567     6557   5506   6328    150   -825  -1740       C  
ATOM   4246  CG1 VAL A 567      -2.126 -29.795   5.649  1.00 49.78           C  
ANISOU 4246  CG1 VAL A 567     6760   5825   6330    282   -856  -1838       C  
ATOM   4247  CG2 VAL A 567      -0.830 -31.524   6.926  1.00 50.00           C  
ANISOU 4247  CG2 VAL A 567     6831   5564   6601    197   -794  -1744       C  
ATOM   4248  N   VAL A 568      -2.649 -27.252   8.079  1.00 45.68           N  
ANISOU 4248  N   VAL A 568     6091   5476   5788    142   -737  -1482       N  
ATOM   4249  CA  VAL A 568      -3.678 -26.229   8.214  1.00 43.93           C  
ANISOU 4249  CA  VAL A 568     5800   5379   5512    119   -763  -1474       C  
ATOM   4250  C   VAL A 568      -3.651 -25.289   7.018  1.00 41.99           C  
ANISOU 4250  C   VAL A 568     5594   5262   5096    264   -784  -1520       C  
ATOM   4251  O   VAL A 568      -2.608 -24.725   6.684  1.00 41.42           O  
ANISOU 4251  O   VAL A 568     5588   5218   4933    362   -716  -1449       O  
ATOM   4252  CB  VAL A 568      -3.488 -25.405   9.510  1.00 41.29           C  
ANISOU 4252  CB  VAL A 568     5424   5065   5197     55   -685  -1308       C  
ATOM   4253  CG1 VAL A 568      -4.501 -24.267   9.578  1.00 42.73           C  
ANISOU 4253  CG1 VAL A 568     5538   5379   5317     54   -708  -1308       C  
ATOM   4254  CG2 VAL A 568      -3.601 -26.300  10.732  1.00 41.32           C  
ANISOU 4254  CG2 VAL A 568     5399   4950   5351    -91   -665  -1253       C  
ATOM   4255  N   ARG A 569      -4.804 -25.133   6.380  1.00 40.16           N  
ANISOU 4255  N   ARG A 569     5324   5109   4826    275   -878  -1637       N  
ATOM   4256  CA  ARG A 569      -4.950 -24.276   5.213  1.00 43.01           C  
ANISOU 4256  CA  ARG A 569     5731   5594   5018    414   -919  -1687       C  
ATOM   4257  C   ARG A 569      -6.245 -23.497   5.338  1.00 45.03           C  
ANISOU 4257  C   ARG A 569     5898   5954   5259    393   -988  -1713       C  
ATOM   4258  O   ARG A 569      -7.321 -24.088   5.470  1.00 45.21           O  
ANISOU 4258  O   ARG A 569     5836   5968   5376    307  -1070  -1819       O  
ATOM   4259  CB  ARG A 569      -5.015 -25.103   3.925  1.00 53.12           C  
ANISOU 4259  CB  ARG A 569     7074   6866   6244    488   -999  -1854       C  
ATOM   4260  CG  ARG A 569      -3.786 -25.946   3.617  1.00 63.62           C  
ANISOU 4260  CG  ARG A 569     8492   8096   7584    530   -938  -1861       C  
ATOM   4261  CD  ARG A 569      -3.972 -26.696   2.298  1.00 74.59           C  
ANISOU 4261  CD  ARG A 569     9946   9490   8906    610  -1025  -2045       C  
ATOM   4262  NE  ARG A 569      -2.912 -27.669   2.049  1.00 81.78           N  
ANISOU 4262  NE  ARG A 569    10928  10290   9853    642   -973  -2077       N  
ATOM   4263  CZ  ARG A 569      -1.788 -27.399   1.392  1.00 86.03           C  
ANISOU 4263  CZ  ARG A 569    11557  10857  10275    766   -891  -2046       C  
ATOM   4264  NH1 ARG A 569      -1.574 -26.179   0.917  1.00 88.05           N1+
ANISOU 4264  NH1 ARG A 569    11850  11239  10365    861   -849  -1973       N1+
ATOM   4265  NH2 ARG A 569      -0.878 -28.346   1.211  1.00 85.16           N  
ANISOU 4265  NH2 ARG A 569    11497  10643  10216    795   -848  -2087       N  
ATOM   4266  N   ASN A 570      -6.143 -22.174   5.295  1.00 37.99           N  
ANISOU 4266  N   ASN A 570     5021   5156   4256    470   -955  -1622       N  
ATOM   4267  CA  ASN A 570      -7.322 -21.319   5.269  1.00 43.17           C  
ANISOU 4267  CA  ASN A 570     5603   5919   4882    485  -1027  -1651       C  
ATOM   4268  C   ASN A 570      -7.002 -19.955   4.652  1.00 42.73           C  
ANISOU 4268  C   ASN A 570     5622   5958   4658    627  -1009  -1577       C  
ATOM   4269  O   ASN A 570      -5.874 -19.712   4.219  1.00 40.57           O  
ANISOU 4269  O   ASN A 570     5454   5669   4292    704   -934  -1507       O  
ATOM   4270  CB  ASN A 570      -7.949 -21.186   6.667  1.00 40.99           C  
ANISOU 4270  CB  ASN A 570     5207   5626   4743    347   -994  -1591       C  
ATOM   4271  CG  ASN A 570      -6.969 -20.678   7.713  1.00 39.85           C  
ANISOU 4271  CG  ASN A 570     5088   5437   4617    311   -864  -1418       C  
ATOM   4272  ND2 ASN A 570      -6.788 -21.453   8.781  1.00 35.65           N  
ANISOU 4272  ND2 ASN A 570     4518   4810   4217    179   -813  -1375       N  
ATOM   4273  OD1 ASN A 570      -6.411 -19.589   7.583  1.00 38.16           O  
ANISOU 4273  OD1 ASN A 570     4928   5271   4302    398   -816  -1325       O  
ATOM   4274  N   ALA A 571      -7.998 -19.078   4.598  1.00 43.05           N  
ANISOU 4274  N   ALA A 571     5604   6090   4662    662  -1076  -1594       N  
ATOM   4275  CA  ALA A 571      -7.838 -17.768   3.968  1.00 43.83           C  
ANISOU 4275  CA  ALA A 571     5780   6272   4602    802  -1074  -1527       C  
ATOM   4276  C   ALA A 571      -6.815 -16.898   4.692  1.00 40.15           C  
ANISOU 4276  C   ALA A 571     5358   5774   4124    797   -936  -1351       C  
ATOM   4277  O   ALA A 571      -6.250 -15.971   4.107  1.00 41.63           O  
ANISOU 4277  O   ALA A 571     5644   5996   4180    905   -898  -1274       O  
ATOM   4278  CB  ALA A 571      -9.188 -17.043   3.881  1.00 42.70           C  
ANISOU 4278  CB  ALA A 571     5552   6224   4447    839  -1183  -1585       C  
ATOM   4279  N   GLY A 572      -6.590 -17.196   5.967  1.00 35.49           N  
ANISOU 4279  N   GLY A 572     4698   5116   3671    668   -863  -1287       N  
ATOM   4280  CA  GLY A 572      -5.609 -16.474   6.759  1.00 36.67           C  
ANISOU 4280  CA  GLY A 572     4877   5229   3825    648   -741  -1131       C  
ATOM   4281  C   GLY A 572      -5.941 -15.010   6.997  1.00 35.52           C  
ANISOU 4281  C   GLY A 572     4727   5144   3624    701   -731  -1055       C  
ATOM   4282  O   GLY A 572      -7.108 -14.606   6.995  1.00 34.25           O  
ANISOU 4282  O   GLY A 572     4498   5047   3469    717   -811  -1115       O  
ATOM   4283  N   TRP A 573      -4.898 -14.212   7.211  1.00 32.90           N  
ANISOU 4283  N   TRP A 573     4463   4789   3248    727   -631   -926       N  
ATOM   4284  CA  TRP A 573      -5.059 -12.789   7.471  1.00 32.50           C  
ANISOU 4284  CA  TRP A 573     4423   4774   3152    774   -610   -844       C  
ATOM   4285  C   TRP A 573      -4.476 -11.983   6.336  1.00 35.84           C  
ANISOU 4285  C   TRP A 573     4973   5221   3423    907   -591   -793       C  
ATOM   4286  O   TRP A 573      -3.708 -12.496   5.522  1.00 33.34           O  
ANISOU 4286  O   TRP A 573     4735   4891   3041    948   -562   -802       O  
ATOM   4287  CB  TRP A 573      -4.303 -12.384   8.732  1.00 31.26           C  
ANISOU 4287  CB  TRP A 573     4244   4561   3071    687   -505   -727       C  
ATOM   4288  CG  TRP A 573      -4.875 -12.879   9.999  1.00 30.82           C  
ANISOU 4288  CG  TRP A 573     4078   4486   3145    560   -507   -747       C  
ATOM   4289  CD1 TRP A 573      -5.952 -13.700  10.163  1.00 34.88           C  
ANISOU 4289  CD1 TRP A 573     4503   5021   3730    501   -578   -853       C  
ATOM   4290  CD2 TRP A 573      -4.398 -12.571  11.302  1.00 30.72           C  
ANISOU 4290  CD2 TRP A 573     4035   4433   3202    471   -429   -656       C  
ATOM   4291  CE2 TRP A 573      -5.226 -13.244  12.220  1.00 34.01           C  
ANISOU 4291  CE2 TRP A 573     4354   4849   3721    362   -450   -705       C  
ATOM   4292  CE3 TRP A 573      -3.341 -11.795  11.782  1.00 29.16           C  
ANISOU 4292  CE3 TRP A 573     3886   4200   2992    469   -344   -541       C  
ATOM   4293  NE1 TRP A 573      -6.170 -13.927  11.502  1.00 35.67           N  
ANISOU 4293  NE1 TRP A 573     4523   5094   3936    378   -537   -824       N  
ATOM   4294  CZ2 TRP A 573      -5.034 -13.157  13.593  1.00 29.59           C  
ANISOU 4294  CZ2 TRP A 573     3753   4259   3230    260   -388   -639       C  
ATOM   4295  CZ3 TRP A 573      -3.153 -11.713  13.145  1.00 31.41           C  
ANISOU 4295  CZ3 TRP A 573     4125   4456   3355    369   -296   -485       C  
ATOM   4296  CH2 TRP A 573      -3.995 -12.391  14.034  1.00 29.76           C  
ANISOU 4296  CH2 TRP A 573     3829   4251   3228    269   -318   -532       C  
ATOM   4297  N   SER A 574      -4.809 -10.701   6.314  1.00 33.81           N  
ANISOU 4297  N   SER A 574     4740   4996   3111    972   -597   -736       N  
ATOM   4298  CA  SER A 574      -4.238  -9.793   5.330  1.00 35.12           C  
ANISOU 4298  CA  SER A 574     5038   5174   3132   1091   -565   -663       C  
ATOM   4299  C   SER A 574      -3.986  -8.436   5.982  1.00 36.78           C  
ANISOU 4299  C   SER A 574     5265   5357   3352   1092   -500   -544       C  
ATOM   4300  O   SER A 574      -4.403  -8.207   7.113  1.00 34.29           O  
ANISOU 4300  O   SER A 574     4857   5029   3144   1016   -498   -538       O  
ATOM   4301  CB  SER A 574      -5.170  -9.669   4.121  1.00 34.87           C  
ANISOU 4301  CB  SER A 574     5054   5219   2978   1218   -688   -747       C  
ATOM   4302  OG  SER A 574      -6.401  -9.072   4.486  1.00 38.59           O  
ANISOU 4302  OG  SER A 574     5447   5732   3484   1240   -781   -786       O  
ATOM   4303  N   VAL A 575      -3.308  -7.538   5.273  1.00 39.75           N  
ANISOU 4303  N   VAL A 575     5763   5722   3618   1175   -443   -450       N  
ATOM   4304  CA  VAL A 575      -3.038  -6.203   5.801  1.00 32.77           C  
ANISOU 4304  CA  VAL A 575     4908   4798   2744   1179   -383   -338       C  
ATOM   4305  C   VAL A 575      -3.226  -5.157   4.708  1.00 37.83           C  
ANISOU 4305  C   VAL A 575     5679   5458   3237   1319   -409   -287       C  
ATOM   4306  O   VAL A 575      -2.830  -5.378   3.568  1.00 39.40           O  
ANISOU 4306  O   VAL A 575     5981   5678   3310   1392   -398   -281       O  
ATOM   4307  CB  VAL A 575      -1.610  -6.101   6.368  1.00 32.87           C  
ANISOU 4307  CB  VAL A 575     4938   4741   2812   1094   -243   -236       C  
ATOM   4308  CG1 VAL A 575      -0.576  -6.370   5.277  1.00 32.50           C  
ANISOU 4308  CG1 VAL A 575     4995   4690   2663   1142   -169   -198       C  
ATOM   4309  CG2 VAL A 575      -1.385  -4.725   7.004  1.00 31.53           C  
ANISOU 4309  CG2 VAL A 575     4789   4521   2669   1085   -189   -134       C  
ATOM   4310  N   HIS A 576      -3.850  -4.029   5.044  1.00 36.77           N  
ANISOU 4310  N   HIS A 576     5546   5313   3111   1362   -443   -251       N  
ATOM   4311  CA  HIS A 576      -3.980  -2.935   4.084  1.00 35.20           C  
ANISOU 4311  CA  HIS A 576     5484   5113   2776   1497   -464   -182       C  
ATOM   4312  C   HIS A 576      -3.858  -1.560   4.732  1.00 37.06           C  
ANISOU 4312  C   HIS A 576     5747   5278   3055   1497   -415    -81       C  
ATOM   4313  O   HIS A 576      -4.098  -1.389   5.932  1.00 36.24           O  
ANISOU 4313  O   HIS A 576     5537   5150   3082   1416   -407    -98       O  
ATOM   4314  CB  HIS A 576      -5.295  -3.028   3.301  1.00 37.19           C  
ANISOU 4314  CB  HIS A 576     5736   5446   2947   1619   -626   -280       C  
ATOM   4315  CG  HIS A 576      -6.513  -2.848   4.146  1.00 42.06           C  
ANISOU 4315  CG  HIS A 576     6216   6090   3675   1609   -722   -361       C  
ATOM   4316  CD2 HIS A 576      -7.323  -1.774   4.329  1.00 48.60           C  
ANISOU 4316  CD2 HIS A 576     7039   6915   4510   1690   -786   -348       C  
ATOM   4317  ND1 HIS A 576      -7.027  -3.853   4.936  1.00 47.11           N  
ANISOU 4317  ND1 HIS A 576     6698   6763   4440   1505   -754   -470       N  
ATOM   4318  CE1 HIS A 576      -8.100  -3.410   5.568  1.00 50.69           C  
ANISOU 4318  CE1 HIS A 576     7049   7242   4971   1519   -826   -524       C  
ATOM   4319  NE2 HIS A 576      -8.299  -2.150   5.217  1.00 50.98           N  
ANISOU 4319  NE2 HIS A 576     7172   7258   4940   1635   -850   -456       N  
ATOM   4320  N   ALA A 577      -3.488  -0.583   3.912  1.00 36.22           N  
ANISOU 4320  N   ALA A 577     5792   5136   2834   1589   -381     24       N  
ATOM   4321  CA  ALA A 577      -3.299   0.787   4.358  1.00 35.94           C  
ANISOU 4321  CA  ALA A 577     5810   5016   2830   1599   -332    128       C  
ATOM   4322  C   ALA A 577      -4.633   1.449   4.670  1.00 36.40           C  
ANISOU 4322  C   ALA A 577     5822   5090   2918   1681   -457     74       C  
ATOM   4323  O   ALA A 577      -5.644   1.170   4.025  1.00 37.30           O  
ANISOU 4323  O   ALA A 577     5927   5280   2966   1784   -588     -7       O  
ATOM   4324  CB  ALA A 577      -2.564   1.581   3.285  1.00 37.09           C  
ANISOU 4324  CB  ALA A 577     6141   5113   2837   1675   -259    258       C  
ATOM   4325  N   ILE A 578      -4.623   2.326   5.666  1.00 35.89           N  
ANISOU 4325  N   ILE A 578     5724   4955   2957   1639   -420    111       N  
ATOM   4326  CA  ILE A 578      -5.770   3.162   5.965  1.00 36.49           C  
ANISOU 4326  CA  ILE A 578     5771   5029   3065   1729   -520     74       C  
ATOM   4327  C   ILE A 578      -5.855   4.236   4.885  1.00 39.08           C  
ANISOU 4327  C   ILE A 578     6275   5312   3263   1881   -552    170       C  
ATOM   4328  O   ILE A 578      -4.900   4.978   4.661  1.00 41.60           O  
ANISOU 4328  O   ILE A 578     6722   5538   3548   1867   -447    299       O  
ATOM   4329  CB  ILE A 578      -5.619   3.821   7.336  1.00 35.60           C  
ANISOU 4329  CB  ILE A 578     5588   4846   3093   1639   -458     87       C  
ATOM   4330  CG1 ILE A 578      -5.501   2.745   8.421  1.00 34.18           C  
ANISOU 4330  CG1 ILE A 578     5250   4711   3027   1489   -424      5       C  
ATOM   4331  CG2 ILE A 578      -6.781   4.777   7.604  1.00 38.99           C  
ANISOU 4331  CG2 ILE A 578     5994   5266   3554   1748   -553     47       C  
ATOM   4332  CD1 ILE A 578      -5.119   3.285   9.784  1.00 33.29           C  
ANISOU 4332  CD1 ILE A 578     5082   4531   3034   1384   -348     24       C  
ATOM   4333  N   LEU A 579      -6.989   4.299   4.201  1.00 40.05           N  
ANISOU 4333  N   LEU A 579     6405   5499   3313   2025   -699    107       N  
ATOM   4334  CA  LEU A 579      -7.155   5.242   3.105  1.00 46.81           C  
ANISOU 4334  CA  LEU A 579     7439   6319   4028   2186   -750    198       C  
ATOM   4335  C   LEU A 579      -7.253   6.670   3.620  1.00 55.60           C  
ANISOU 4335  C   LEU A 579     8608   7316   5202   2229   -732    277       C  
ATOM   4336  O   LEU A 579      -7.744   6.907   4.723  1.00 53.03           O  
ANISOU 4336  O   LEU A 579     8154   6977   5018   2187   -746    210       O  
ATOM   4337  CB  LEU A 579      -8.381   4.885   2.266  1.00 49.69           C  
ANISOU 4337  CB  LEU A 579     7787   6792   4302   2335   -933     98       C  
ATOM   4338  CG  LEU A 579      -8.280   3.555   1.518  1.00 52.32           C  
ANISOU 4338  CG  LEU A 579     8102   7229   4546   2315   -963     23       C  
ATOM   4339  CD1 LEU A 579      -9.511   3.330   0.660  1.00 57.20           C  
ANISOU 4339  CD1 LEU A 579     8711   7950   5074   2471  -1160    -78       C  
ATOM   4340  CD2 LEU A 579      -7.018   3.513   0.671  1.00 53.35           C  
ANISOU 4340  CD2 LEU A 579     8408   7322   4542   2298   -839    146       C  
ATOM   4341  N   SER A 580      -6.776   7.620   2.820  1.00 61.58           N  
ANISOU 4341  N   SER A 580     9562   7984   5851   2312   -696    419       N  
ATOM   4342  CA  SER A 580      -6.799   9.023   3.218  1.00 68.72           C  
ANISOU 4342  CA  SER A 580    10544   8755   6811   2356   -676    504       C  
ATOM   4343  C   SER A 580      -8.230   9.497   3.437  1.00 77.06           C  
ANISOU 4343  C   SER A 580    11530   9839   7912   2497   -839    412       C  
ATOM   4344  O   SER A 580      -8.481  10.377   4.259  1.00 80.13           O  
ANISOU 4344  O   SER A 580    11889  10143   8413   2502   -833    411       O  
ATOM   4345  CB  SER A 580      -6.101   9.896   2.174  1.00 70.76           C  
ANISOU 4345  CB  SER A 580    11043   8913   6930   2428   -613    680       C  
ATOM   4346  OG  SER A 580      -6.653   9.680   0.887  1.00 72.24           O  
ANISOU 4346  OG  SER A 580    11335   9176   6936   2583   -726    686       O  
ATOM   4347  N   LEU A 581      -9.165   8.898   2.707  1.00 85.28           N  
ANISOU 4347  N   LEU A 581    12535  11000   8867   2611   -988    323       N  
ATOM   4348  CA  LEU A 581     -10.573   9.263   2.821  1.00 95.07           C  
ANISOU 4348  CA  LEU A 581    13688  12286  10150   2756  -1156    222       C  
ATOM   4349  C   LEU A 581     -11.043   9.230   4.274  0.87100.17           C  
ANISOU 4349  C   LEU A 581    14128  12939  10992   2664  -1138    108       C  
ATOM   4350  O   LEU A 581     -11.815  10.085   4.708  1.00102.42           O  
ANISOU 4350  O   LEU A 581    14377  13185  11353   2759  -1204     75       O  
ATOM   4351  CB  LEU A 581     -11.441   8.349   1.946  1.00 96.66           C  
ANISOU 4351  CB  LEU A 581    13835  12638  10253   2852  -1314    113       C  
ATOM   4352  CG  LEU A 581     -11.598   6.874   2.330  1.00 95.01           C  
ANISOU 4352  CG  LEU A 581    13436  12557  10106   2722  -1316    -32       C  
ATOM   4353  CD1 LEU A 581     -12.683   6.698   3.383  0.97 94.43           C  
ANISOU 4353  CD1 LEU A 581    13131  12544  10203   2700  -1384   -185       C  
ATOM   4354  CD2 LEU A 581     -11.927   6.048   1.099  1.00 96.12           C  
ANISOU 4354  CD2 LEU A 581    13618  12810  10094   2806  -1431    -84       C  
ATOM   4355  N   CYS A 582     -10.561   8.243   5.022  0.69102.58           N  
ANISOU 4355  N   CYS A 582    14305  13294  11377   2484  -1044     49       N  
ATOM   4356  CA  CYS A 582     -10.946   8.080   6.419  0.63103.77           C  
ANISOU 4356  CA  CYS A 582    14268  13464  11697   2381  -1013    -56       C  
ATOM   4357  C   CYS A 582     -10.672   9.350   7.219  0.51105.56           C  
ANISOU 4357  C   CYS A 582    14545  13555  12009   2378   -943      7       C  
ATOM   4358  O   CYS A 582      -9.990   9.315   8.243  0.78105.86           O  
ANISOU 4358  O   CYS A 582    14535  13547  12140   2228   -824     15       O  
ATOM   4359  CB  CYS A 582     -10.209   6.890   7.038  1.00101.87           C  
ANISOU 4359  CB  CYS A 582    13929  13270  11507   2183   -906    -88       C  
ATOM   4360  SG  CYS A 582     -10.478   5.315   6.177  0.79 98.89           S  
ANISOU 4360  SG  CYS A 582    13490  13037  11048   2170   -981   -176       S  
TER    4361      CYS A 582 
ATOM   4362  N   SER A 587     -16.693   4.450  12.021  0.81 88.55           N  
ANISOU 4362  N   SER A 587    11000  12140  10506   2004  -1128   -962       N  
ATOM   4363  CA  SER A 587     -15.470   3.694  11.776  0.67 87.61           C  
ANISOU 4363  CA  SER A 587    10990  11978  10318   1879  -1052   -866       C  
ATOM   4364  C   SER A 587     -14.905   3.135  13.075  1.00 91.49           C  
ANISOU 4364  C   SER A 587    11419  12460  10884   1683   -909   -863       C  
ATOM   4365  O   SER A 587     -14.837   3.837  14.087  1.00 95.10           O  
ANISOU 4365  O   SER A 587    11862  12875  11397   1654   -833   -857       O  
ATOM   4366  CB  SER A 587     -14.418   4.575  11.101  0.70 83.78           C  
ANISOU 4366  CB  SER A 587    10728  11373   9730   1951  -1028   -715       C  
ATOM   4367  OG  SER A 587     -13.918   5.547  12.004  1.00 80.66           O  
ANISOU 4367  OG  SER A 587    10385  10880   9381   1922   -931   -656       O  
ATOM   4368  N   ARG A 588     -14.498   1.870  13.042  1.00 89.06           N  
ANISOU 4368  N   ARG A 588    11081  12186  10570   1552   -877   -868       N  
ATOM   4369  CA  ARG A 588     -13.885   1.242  14.204  1.00 85.81           C  
ANISOU 4369  CA  ARG A 588    10629  11760  10216   1368   -751   -850       C  
ATOM   4370  C   ARG A 588     -12.391   1.554  14.220  1.00 70.82           C  
ANISOU 4370  C   ARG A 588     8896   9753   8260   1320   -663   -711       C  
ATOM   4371  O   ARG A 588     -11.621   0.906  14.930  1.00 65.01           O  
ANISOU 4371  O   ARG A 588     8157   8996   7547   1175   -573   -676       O  
ATOM   4372  CB  ARG A 588     -14.123  -0.273  14.193  1.00 92.71           C  
ANISOU 4372  CB  ARG A 588    11399  12707  11121   1251   -758   -917       C  
ATOM   4373  CG  ARG A 588     -14.419  -0.900  15.562  1.00 96.04           C  
ANISOU 4373  CG  ARG A 588    11685  13166  11639   1093   -669   -970       C  
ATOM   4374  CD  ARG A 588     -13.201  -0.904  16.481  1.00 97.28           C  
ANISOU 4374  CD  ARG A 588    11926  13246  11790    971   -544   -869       C  
ATOM   4375  NE  ARG A 588     -13.282  -1.954  17.495  0.28 98.72           N  
ANISOU 4375  NE  ARG A 588    12012  13463  12035    805   -472   -901       N  
ATOM   4376  CZ  ARG A 588     -12.386  -2.141  18.460  0.69 99.57           C  
ANISOU 4376  CZ  ARG A 588    12166  13522  12145    685   -372   -831       C  
ATOM   4377  NH1 ARG A 588     -11.330  -1.343  18.558  1.00 98.07           N1+
ANISOU 4377  NH1 ARG A 588    12103  13249  11911    707   -333   -735       N1+
ATOM   4378  NH2 ARG A 588     -12.548  -3.127  19.332  0.66100.96           N  
ANISOU 4378  NH2 ARG A 588    12261  13730  12370    542   -315   -856       N  
ATOM   4379  N   LEU A 589     -11.982   2.545  13.431  1.00 60.84           N  
ANISOU 4379  N   LEU A 589     7775   8418   6924   1441   -691   -630       N  
ATOM   4380  CA  LEU A 589     -10.591   2.989  13.457  1.00 49.97           C  
ANISOU 4380  CA  LEU A 589     6546   6934   5508   1396   -601   -499       C  
ATOM   4381  C   LEU A 589     -10.292   3.775  14.727  1.00 39.66           C  
ANISOU 4381  C   LEU A 589     5232   5567   4269   1334   -515   -482       C  
ATOM   4382  O   LEU A 589     -10.935   4.776  15.032  1.00 38.24           O  
ANISOU 4382  O   LEU A 589     5040   5368   4121   1420   -539   -515       O  
ATOM   4383  CB  LEU A 589     -10.238   3.830  12.234  1.00 53.97           C  
ANISOU 4383  CB  LEU A 589     7214   7376   5916   1534   -643   -410       C  
ATOM   4384  CG  LEU A 589     -10.137   3.136  10.878  1.00 56.53           C  
ANISOU 4384  CG  LEU A 589     7600   7741   6138   1591   -706   -395       C  
ATOM   4385  CD1 LEU A 589      -9.606   4.119   9.845  1.00 64.62           C  
ANISOU 4385  CD1 LEU A 589     8810   8685   7057   1712   -715   -280       C  
ATOM   4386  CD2 LEU A 589      -9.251   1.915  10.953  1.00 53.37           C  
ANISOU 4386  CD2 LEU A 589     7189   7354   5735   1451   -637   -378       C  
ATOM   4387  N   SER A 590      -9.300   3.300  15.460  1.00 35.71           N  
ANISOU 4387  N   SER A 590     4741   5035   3791   1188   -421   -436       N  
ATOM   4388  CA  SER A 590      -8.872   3.913  16.696  1.00 33.96           C  
ANISOU 4388  CA  SER A 590     4520   4761   3624   1112   -341   -421       C  
ATOM   4389  C   SER A 590      -7.557   4.630  16.446  1.00 31.44           C  
ANISOU 4389  C   SER A 590     4346   4324   3275   1101   -286   -300       C  
ATOM   4390  O   SER A 590      -6.966   4.496  15.375  1.00 31.52           O  
ANISOU 4390  O   SER A 590     4447   4306   3222   1137   -294   -227       O  
ATOM   4391  CB  SER A 590      -8.631   2.813  17.727  1.00 31.25           C  
ANISOU 4391  CB  SER A 590     4084   4466   3322    951   -282   -451       C  
ATOM   4392  OG  SER A 590      -7.687   1.878  17.211  1.00 31.89           O  
ANISOU 4392  OG  SER A 590     4210   4536   3370    884   -262   -387       O  
ATOM   4393  N   GLU A 591      -7.102   5.377  17.448  1.00 31.20           N  
ANISOU 4393  N   GLU A 591     4335   4228   3290   1047   -226   -285       N  
ATOM   4394  CA  GLU A 591      -5.765   5.953  17.445  1.00 34.11           C  
ANISOU 4394  CA  GLU A 591     4817   4487   3656    998   -161   -180       C  
ATOM   4395  C   GLU A 591      -4.703   4.882  17.192  1.00 34.93           C  
ANISOU 4395  C   GLU A 591     4930   4604   3739    895   -119   -121       C  
ATOM   4396  O   GLU A 591      -3.768   5.111  16.426  1.00 32.14           O  
ANISOU 4396  O   GLU A 591     4673   4187   3353    903    -88    -29       O  
ATOM   4397  CB  GLU A 591      -5.485   6.695  18.762  1.00 33.44           C  
ANISOU 4397  CB  GLU A 591     4724   4348   3632    930   -111   -201       C  
ATOM   4398  CG  GLU A 591      -6.263   7.998  18.905  1.00 31.92           C  
ANISOU 4398  CG  GLU A 591     4559   4105   3465   1043   -141   -243       C  
ATOM   4399  CD  GLU A 591      -6.019   8.703  20.238  1.00 35.50           C  
ANISOU 4399  CD  GLU A 591     5006   4507   3975    977    -93   -281       C  
ATOM   4400  OE1 GLU A 591      -6.406   9.881  20.363  1.00 47.69           O  
ANISOU 4400  OE1 GLU A 591     6595   5979   5547   1063   -107   -305       O  
ATOM   4401  OE2 GLU A 591      -5.443   8.091  21.160  1.00 35.06           O1-
ANISOU 4401  OE2 GLU A 591     4905   4481   3933    845    -46   -290       O1-
ATOM   4402  N   VAL A 592      -4.849   3.712  17.816  1.00 29.27           N  
ANISOU 4402  N   VAL A 592     4112   3966   3043    802   -113   -173       N  
ATOM   4403  CA  VAL A 592      -3.877   2.631  17.613  1.00 28.52           C  
ANISOU 4403  CA  VAL A 592     4019   3879   2937    713    -79   -125       C  
ATOM   4404  C   VAL A 592      -3.696   2.274  16.139  1.00 28.85           C  
ANISOU 4404  C   VAL A 592     4122   3926   2911    788   -105    -84       C  
ATOM   4405  O   VAL A 592      -2.578   2.019  15.689  1.00 28.56           O  
ANISOU 4405  O   VAL A 592     4143   3852   2858    753    -57    -10       O  
ATOM   4406  CB  VAL A 592      -4.229   1.353  18.426  1.00 36.87           C  
ANISOU 4406  CB  VAL A 592     4967   5017   4027    613    -81   -188       C  
ATOM   4407  CG1 VAL A 592      -3.653   0.096  17.762  1.00 38.04           C  
ANISOU 4407  CG1 VAL A 592     5115   5186   4154    575    -81   -161       C  
ATOM   4408  CG2 VAL A 592      -3.710   1.477  19.837  1.00 33.75           C  
ANISOU 4408  CG2 VAL A 592     4548   4600   3676    504    -30   -184       C  
ATOM   4409  N   ASP A 593      -4.799   2.234  15.399  1.00 29.55           N  
ANISOU 4409  N   ASP A 593     4196   4070   2962    894   -180   -139       N  
ATOM   4410  CA  ASP A 593      -4.751   1.991  13.967  1.00 30.10           C  
ANISOU 4410  CA  ASP A 593     4335   4152   2948    983   -217   -109       C  
ATOM   4411  C   ASP A 593      -4.084   3.163  13.237  1.00 30.71           C  
ANISOU 4411  C   ASP A 593     4554   4138   2975   1056   -185     -6       C  
ATOM   4412  O   ASP A 593      -3.160   2.974  12.453  1.00 30.74           O  
ANISOU 4412  O   ASP A 593     4639   4114   2927   1052   -140     69       O  
ATOM   4413  CB  ASP A 593      -6.162   1.783  13.415  1.00 34.66           C  
ANISOU 4413  CB  ASP A 593     4858   4812   3500   1085   -322   -201       C  
ATOM   4414  CG  ASP A 593      -6.875   0.598  14.054  1.00 40.18           C  
ANISOU 4414  CG  ASP A 593     5413   5597   4255   1005   -348   -304       C  
ATOM   4415  OD1 ASP A 593      -6.246  -0.472  14.218  1.00 34.53           O  
ANISOU 4415  OD1 ASP A 593     4676   4891   3554    904   -311   -295       O  
ATOM   4416  OD2 ASP A 593      -8.067   0.745  14.397  1.00 42.68           O1-
ANISOU 4416  OD2 ASP A 593     5639   5971   4608   1042   -402   -392       O1-
ATOM   4417  N  AARG A 594      -4.548   4.376  13.511  0.60 31.30           N  
ANISOU 4417  N  AARG A 594     4661   4162   3069   1121   -202     -2       N  
ATOM   4418  N  BARG A 594      -4.561   4.372  13.517  0.40 31.30           N  
ANISOU 4418  N  BARG A 594     4660   4163   3070   1122   -202     -4       N  
ATOM   4419  CA AARG A 594      -4.088   5.538  12.754  0.60 32.31           C  
ANISOU 4419  CA AARG A 594     4934   4194   3150   1203   -180     97       C  
ATOM   4420  CA BARG A 594      -4.106   5.569  12.812  0.40 32.14           C  
ANISOU 4420  CA BARG A 594     4909   4171   3132   1201   -180     95       C  
ATOM   4421  C  AARG A 594      -2.600   5.855  12.926  0.60 32.67           C  
ANISOU 4421  C  AARG A 594     5048   4146   3218   1104    -70    199       C  
ATOM   4422  C  BARG A 594      -2.598   5.787  12.912  0.40 32.47           C  
ANISOU 4422  C  BARG A 594     5020   4126   3191   1102    -70    197       C  
ATOM   4423  O  AARG A 594      -1.966   6.349  12.000  0.60 33.04           O  
ANISOU 4423  O  AARG A 594     5215   4133   3206   1146    -30    296       O  
ATOM   4424  O  BARG A 594      -1.954   6.149  11.930  0.40 32.33           O  
ANISOU 4424  O  BARG A 594     5118   4058   3110   1142    -32    291       O  
ATOM   4425  CB AARG A 594      -4.953   6.766  13.049  0.60 33.01           C  
ANISOU 4425  CB AARG A 594     5041   4235   3265   1300   -229     72       C  
ATOM   4426  CB BARG A 594      -4.853   6.810  13.313  0.40 32.85           C  
ANISOU 4426  CB BARG A 594     5010   4206   3264   1276   -215     69       C  
ATOM   4427  CG AARG A 594      -6.391   6.619  12.562  0.60 33.81           C  
ANISOU 4427  CG AARG A 594     5090   4423   3335   1431   -347    -16       C  
ATOM   4428  CG BARG A 594      -6.369   6.705  13.195  0.40 34.42           C  
ANISOU 4428  CG BARG A 594     5129   4492   3457   1386   -325    -37       C  
ATOM   4429  CD AARG A 594      -7.163   7.920  12.706  0.60 36.79           C  
ANISOU 4429  CD AARG A 594     5501   4741   3737   1550   -396    -30       C  
ATOM   4430  CD BARG A 594      -7.065   8.011  13.574  0.40 34.41           C  
ANISOU 4430  CD BARG A 594     5149   4427   3498   1483   -359    -59       C  
ATOM   4431  NE AARG A 594      -8.602   7.706  12.600  0.60 44.43           N  
ANISOU 4431  NE AARG A 594     6365   5807   4710   1654   -508   -144       N  
ATOM   4432  NE BARG A 594      -8.505   7.815  13.717  0.40 37.91           N  
ANISOU 4432  NE BARG A 594     5474   4968   3964   1567   -454   -181       N  
ATOM   4433  CZ AARG A 594      -9.266   7.624  11.452  0.60 50.91           C  
ANISOU 4433  CZ AARG A 594     7219   6673   5450   1790   -609   -152       C  
ATOM   4434  CZ BARG A 594      -9.172   7.949  14.858  0.40 38.86           C  
ANISOU 4434  CZ BARG A 594     5477   5120   4168   1538   -449   -279       C  
ATOM   4435  NH1AARG A 594      -8.621   7.738  10.298  0.60 53.71           N1+
ANISOU 4435  NH1AARG A 594     7724   6986   5699   1841   -606    -45       N1+
ATOM   4436  NH2AARG A 594     -10.578   7.424  11.461  0.60 54.24           N  
ANISOU 4436  NH2AARG A 594     7523   7189   5897   1875   -713   -268       N  
ATOM   4437  NH1BARG A 594     -10.481   7.739  14.887  0.40 45.67           N1+
ANISOU 4437  NH1BARG A 594     6220   6078   5053   1617   -530   -391       N1+
ATOM   4438  NH2BARG A 594      -8.538   8.306  15.965  0.40 37.37           N  
ANISOU 4438  NH2BARG A 594     5288   4873   4039   1432   -364   -269       N  
ATOM   4439  N   ILE A 595      -2.036   5.556  14.093  1.00 30.80           N  
ANISOU 4439  N   ILE A 595     4734   3903   3064    973    -20    178       N  
ATOM   4440  CA  ILE A 595      -0.618   5.843  14.322  1.00 30.51           C  
ANISOU 4440  CA  ILE A 595     4743   3785   3066    875     76    263       C  
ATOM   4441  C   ILE A 595       0.347   4.911  13.576  1.00 32.45           C  
ANISOU 4441  C   ILE A 595     5001   4057   3272    833    127    314       C  
ATOM   4442  O   ILE A 595       1.540   5.208  13.482  1.00 32.03           O  
ANISOU 4442  O   ILE A 595     4991   3938   3242    772    211    393       O  
ATOM   4443  CB  ILE A 595      -0.246   5.888  15.828  1.00 30.05           C  
ANISOU 4443  CB  ILE A 595     4604   3708   3104    754    103    224       C  
ATOM   4444  CG1 ILE A 595      -0.290   4.488  16.445  1.00 28.78           C  
ANISOU 4444  CG1 ILE A 595     4330   3643   2961    671     90    163       C  
ATOM   4445  CG2 ILE A 595      -1.135   6.885  16.588  1.00 30.18           C  
ANISOU 4445  CG2 ILE A 595     4615   3695   3159    797     65    166       C  
ATOM   4446  CD1 ILE A 595       0.238   4.433  17.879  1.00 28.13           C  
ANISOU 4446  CD1 ILE A 595     4186   3548   2955    549    117    139       C  
ATOM   4447  N   ARG A 596      -0.158   3.794  13.051  1.00 30.03           N  
ANISOU 4447  N   ARG A 596     4652   3844   2913    866     80    264       N  
ATOM   4448  CA  ARG A 596       0.665   2.892  12.249  1.00 29.93           C  
ANISOU 4448  CA  ARG A 596     4658   3858   2855    846    125    299       C  
ATOM   4449  C   ARG A 596       0.295   2.919  10.757  1.00 30.92           C  
ANISOU 4449  C   ARG A 596     4882   4010   2857    972     97    324       C  
ATOM   4450  O   ARG A 596       1.088   2.500   9.910  1.00 32.20           O  
ANISOU 4450  O   ARG A 596     5096   4177   2963    973    155    372       O  
ATOM   4451  CB  ARG A 596       0.659   1.453  12.818  1.00 29.00           C  
ANISOU 4451  CB  ARG A 596     4426   3813   2778    767    105    227       C  
ATOM   4452  CG  ARG A 596      -0.580   0.600  12.539  1.00 29.05           C  
ANISOU 4452  CG  ARG A 596     4378   3911   2750    821     11    130       C  
ATOM   4453  CD  ARG A 596      -0.713  -0.536  13.603  1.00 28.15           C  
ANISOU 4453  CD  ARG A 596     4143   3840   2712    715     -4     62       C  
ATOM   4454  NE  ARG A 596      -0.760   0.086  14.920  1.00 30.27           N  
ANISOU 4454  NE  ARG A 596     4368   4079   3054    648     11     57       N  
ATOM   4455  CZ  ARG A 596       0.111  -0.097  15.907  1.00 27.09           C  
ANISOU 4455  CZ  ARG A 596     3930   3645   2716    540     60     83       C  
ATOM   4456  NH1 ARG A 596       1.117  -0.966  15.800  1.00 26.71           N1+
ANISOU 4456  NH1 ARG A 596     3872   3592   2685    482     97    114       N1+
ATOM   4457  NH2 ARG A 596      -0.043   0.599  17.027  1.00 26.92           N  
ANISOU 4457  NH2 ARG A 596     3884   3601   2744    496     65     70       N  
ATOM   4458  N   GLY A 597      -0.911   3.387  10.447  1.00 31.57           N  
ANISOU 4458  N   GLY A 597     4987   4115   2895   1081      7    285       N  
ATOM   4459  CA  GLY A 597      -1.318   3.617   9.066  1.00 32.75           C  
ANISOU 4459  CA  GLY A 597     5245   4281   2915   1215    -35    314       C  
ATOM   4460  C   GLY A 597      -1.831   2.405   8.303  1.00 32.87           C  
ANISOU 4460  C   GLY A 597     5230   4401   2856   1261   -103    238       C  
ATOM   4461  O   GLY A 597      -2.046   2.477   7.094  1.00 33.91           O  
ANISOU 4461  O   GLY A 597     5461   4558   2865   1370   -137    260       O  
ATOM   4462  N   PHE A 598      -2.028   1.292   8.999  1.00 31.92           N  
ANISOU 4462  N   PHE A 598     4982   4340   2808   1178   -126    149       N  
ATOM   4463  CA  PHE A 598      -2.535   0.078   8.364  1.00 32.07           C  
ANISOU 4463  CA  PHE A 598     4961   4448   2777   1206   -194     63       C  
ATOM   4464  C   PHE A 598      -3.415  -0.703   9.330  1.00 31.40           C  
ANISOU 4464  C   PHE A 598     4725   4418   2787   1142   -258    -51       C  
ATOM   4465  O   PHE A 598      -3.425  -0.430  10.530  1.00 30.69           O  
ANISOU 4465  O   PHE A 598     4564   4301   2795   1062   -230    -54       O  
ATOM   4466  CB  PHE A 598      -1.388  -0.812   7.854  1.00 31.84           C  
ANISOU 4466  CB  PHE A 598     4962   4420   2717   1156   -114     93       C  
ATOM   4467  CG  PHE A 598      -0.466  -1.305   8.936  1.00 31.09           C  
ANISOU 4467  CG  PHE A 598     4785   4290   2738   1015    -34    106       C  
ATOM   4468  CD1 PHE A 598       0.808  -0.779   9.071  1.00 30.60           C  
ANISOU 4468  CD1 PHE A 598     4769   4159   2700    962     79    206       C  
ATOM   4469  CD2 PHE A 598      -0.871  -2.292   9.818  1.00 29.89           C  
ANISOU 4469  CD2 PHE A 598     4511   4174   2673    934    -74     22       C  
ATOM   4470  CE1 PHE A 598       1.662  -1.231  10.070  1.00 29.59           C  
ANISOU 4470  CE1 PHE A 598     4562   4003   2679    840    137    214       C  
ATOM   4471  CE2 PHE A 598      -0.018  -2.750  10.820  1.00 28.96           C  
ANISOU 4471  CE2 PHE A 598     4329   4022   2652    813    -10     42       C  
ATOM   4472  CZ  PHE A 598       1.247  -2.220  10.943  1.00 28.85           C  
ANISOU 4472  CZ  PHE A 598     4358   3946   2660    771     88    134       C  
ATOM   4473  N   VAL A 599      -4.154  -1.675   8.809  1.00 31.74           N  
ANISOU 4473  N   VAL A 599     4722   4539   2801   1173   -342   -145       N  
ATOM   4474  CA  VAL A 599      -4.981  -2.520   9.654  1.00 33.22           C  
ANISOU 4474  CA  VAL A 599     4764   4777   3082   1100   -393   -251       C  
ATOM   4475  C   VAL A 599      -4.852  -3.978   9.231  1.00 34.45           C  
ANISOU 4475  C   VAL A 599     4887   4971   3232   1057   -412   -315       C  
ATOM   4476  O   VAL A 599      -4.867  -4.294   8.036  1.00 32.00           O  
ANISOU 4476  O   VAL A 599     4644   4690   2823   1139   -453   -335       O  
ATOM   4477  CB  VAL A 599      -6.474  -2.099   9.613  1.00 38.73           C  
ANISOU 4477  CB  VAL A 599     5400   5533   3784   1185   -505   -336       C  
ATOM   4478  CG1 VAL A 599      -7.327  -3.098  10.383  1.00 44.92           C  
ANISOU 4478  CG1 VAL A 599     6028   6376   4664   1098   -546   -449       C  
ATOM   4479  CG2 VAL A 599      -6.654  -0.701  10.195  1.00 35.31           C  
ANISOU 4479  CG2 VAL A 599     4987   5052   3376   1223   -486   -287       C  
ATOM   4480  N   LEU A 600      -4.706  -4.866  10.211  1.00 31.66           N  
ANISOU 4480  N   LEU A 600     4438   4612   2979    931   -381   -347       N  
ATOM   4481  CA  LEU A 600      -4.775  -6.290   9.921  1.00 30.43           C  
ANISOU 4481  CA  LEU A 600     4239   4484   2841    887   -412   -422       C  
ATOM   4482  C   LEU A 600      -6.230  -6.676   9.745  1.00 35.56           C  
ANISOU 4482  C   LEU A 600     4801   5205   3506    916   -526   -544       C  
ATOM   4483  O   LEU A 600      -7.085  -6.256  10.522  1.00 34.12           O  
ANISOU 4483  O   LEU A 600     4532   5047   3386    896   -549   -576       O  
ATOM   4484  CB  LEU A 600      -4.170  -7.109  11.056  1.00 29.46           C  
ANISOU 4484  CB  LEU A 600     4051   4321   2822    745   -347   -407       C  
ATOM   4485  CG  LEU A 600      -2.654  -7.050  11.194  1.00 30.99           C  
ANISOU 4485  CG  LEU A 600     4308   4449   3016    707   -247   -307       C  
ATOM   4486  CD1 LEU A 600      -2.200  -7.766  12.471  1.00 30.13           C  
ANISOU 4486  CD1 LEU A 600     4130   4305   3015    575   -204   -293       C  
ATOM   4487  CD2 LEU A 600      -2.012  -7.675   9.977  1.00 30.98           C  
ANISOU 4487  CD2 LEU A 600     4381   4449   2943    763   -239   -312       C  
ATOM   4488  N   LYS A 601      -6.508  -7.464   8.715  1.00 31.96           N  
ANISOU 4488  N   LYS A 601     4361   4786   2995    964   -596   -618       N  
ATOM   4489  CA  LYS A 601      -7.819  -8.071   8.540  1.00 32.77           C  
ANISOU 4489  CA  LYS A 601     4363   4956   3131    970   -708   -750       C  
ATOM   4490  C   LYS A 601      -7.737  -9.530   8.971  1.00 33.88           C  
ANISOU 4490  C   LYS A 601     4431   5078   3363    845   -697   -811       C  
ATOM   4491  O   LYS A 601      -7.092 -10.346   8.313  1.00 33.22           O  
ANISOU 4491  O   LYS A 601     4406   4972   3243    846   -690   -824       O  
ATOM   4492  CB  LYS A 601      -8.275  -7.978   7.085  1.00 36.39           C  
ANISOU 4492  CB  LYS A 601     4890   5470   3467   1112   -814   -806       C  
ATOM   4493  CG  LYS A 601      -9.690  -7.455   6.933  1.00 53.40           C  
ANISOU 4493  CG  LYS A 601     6966   7697   5626   1190   -935   -890       C  
ATOM   4494  CD  LYS A 601      -9.802  -6.024   7.441  1.00 59.15           C  
ANISOU 4494  CD  LYS A 601     7712   8409   6354   1244   -904   -809       C  
ATOM   4495  CE  LYS A 601     -11.156  -5.768   8.087  1.00 68.58           C  
ANISOU 4495  CE  LYS A 601     8755   9661   7642   1243   -974   -900       C  
ATOM   4496  NZ  LYS A 601     -12.295  -6.098   7.185  1.00 76.55           N1+
ANISOU 4496  NZ  LYS A 601     9708  10756   8623   1333  -1129  -1027       N1+
ATOM   4497  N   LYS A 602      -8.393  -9.857  10.076  1.00 32.20           N  
ANISOU 4497  N   LYS A 602     4095   4872   3267    738   -690   -849       N  
ATOM   4498  CA  LYS A 602      -8.270 -11.189  10.658  1.00 34.83           C  
ANISOU 4498  CA  LYS A 602     4369   5169   3697    605   -665   -885       C  
ATOM   4499  C   LYS A 602      -9.421 -12.063  10.190  1.00 38.18           C  
ANISOU 4499  C   LYS A 602     4703   5642   4162    592   -770  -1028       C  
ATOM   4500  O   LYS A 602     -10.300 -12.439  10.965  1.00 41.01           O  
ANISOU 4500  O   LYS A 602     4938   6022   4623    499   -779  -1086       O  
ATOM   4501  CB  LYS A 602      -8.209 -11.095  12.178  1.00 33.31           C  
ANISOU 4501  CB  LYS A 602     4110   4948   3598    484   -582   -830       C  
ATOM   4502  CG  LYS A 602      -7.065 -10.213  12.653  1.00 32.41           C  
ANISOU 4502  CG  LYS A 602     4079   4785   3450    493   -491   -700       C  
ATOM   4503  CD  LYS A 602      -7.083 -10.043  14.151  1.00 30.49           C  
ANISOU 4503  CD  LYS A 602     3776   4525   3284    384   -423   -657       C  
ATOM   4504  CE  LYS A 602      -5.868  -9.242  14.608  1.00 29.72           C  
ANISOU 4504  CE  LYS A 602     3759   4374   3158    387   -342   -538       C  
ATOM   4505  NZ  LYS A 602      -5.867  -9.029  16.079  1.00 28.01           N1+
ANISOU 4505  NZ  LYS A 602     3496   4147   3001    287   -283   -501       N1+
ATOM   4506  N   THR A 603      -9.382 -12.385   8.904  1.00 37.59           N  
ANISOU 4506  N   THR A 603     4692   5587   4004    683   -844  -1087       N  
ATOM   4507  CA  THR A 603     -10.500 -12.986   8.198  1.00 35.84           C  
ANISOU 4507  CA  THR A 603     4399   5424   3795    706   -971  -1234       C  
ATOM   4508  C   THR A 603     -10.803 -14.411   8.630  1.00 38.66           C  
ANISOU 4508  C   THR A 603     4668   5743   4276    565   -977  -1317       C  
ATOM   4509  O   THR A 603     -11.957 -14.750   8.912  1.00 36.83           O  
ANISOU 4509  O   THR A 603     4304   5553   4135    507  -1036  -1416       O  
ATOM   4510  CB  THR A 603     -10.229 -12.958   6.697  1.00 40.45           C  
ANISOU 4510  CB  THR A 603     5099   6035   4236    845  -1045  -1269       C  
ATOM   4511  CG2 THR A 603     -11.448 -13.429   5.912  1.00 43.69           C  
ANISOU 4511  CG2 THR A 603     5435   6518   4646    887  -1198  -1431       C  
ATOM   4512  OG1 THR A 603      -9.895 -11.619   6.316  1.00 41.12           O  
ANISOU 4512  OG1 THR A 603     5280   6142   4203    969  -1027  -1174       O  
ATOM   4513  N   ALA A 604      -9.774 -15.247   8.676  1.00 38.08           N  
ANISOU 4513  N   ALA A 604     4667   5587   4215    510   -914  -1276       N  
ATOM   4514  CA  ALA A 604      -9.964 -16.638   9.059  1.00 40.42           C  
ANISOU 4514  CA  ALA A 604     4902   5825   4630    379   -918  -1343       C  
ATOM   4515  C   ALA A 604      -8.966 -17.044  10.134  1.00 42.74           C  
ANISOU 4515  C   ALA A 604     5225   6024   4990    273   -798  -1229       C  
ATOM   4516  O   ALA A 604      -7.907 -16.433  10.280  1.00 37.50           O  
ANISOU 4516  O   ALA A 604     4647   5336   4266    316   -723  -1114       O  
ATOM   4517  CB  ALA A 604      -9.847 -17.547   7.842  1.00 37.65           C  
ANISOU 4517  CB  ALA A 604     4609   5460   4237    429   -998  -1450       C  
ATOM   4518  N   MET A 605      -9.312 -18.076  10.890  1.00 39.03           N  
ANISOU 4518  N   MET A 605     4684   5499   4645    132   -784  -1259       N  
ATOM   4519  CA  MET A 605      -8.429 -18.567  11.933  1.00 39.39           C  
ANISOU 4519  CA  MET A 605     4761   5451   4754     32   -686  -1152       C  
ATOM   4520  C   MET A 605      -8.806 -19.974  12.366  1.00 43.99           C  
ANISOU 4520  C   MET A 605     5294   5956   5464   -106   -694  -1208       C  
ATOM   4521  O   MET A 605      -9.940 -20.226  12.775  1.00 45.51           O  
ANISOU 4521  O   MET A 605     5377   6177   5739   -194   -717  -1274       O  
ATOM   4522  CB  MET A 605      -8.470 -17.639  13.144  1.00 41.31           C  
ANISOU 4522  CB  MET A 605     4967   5722   5007    -12   -608  -1050       C  
ATOM   4523  CG  MET A 605      -7.717 -18.174  14.344  1.00 44.85           C  
ANISOU 4523  CG  MET A 605     5438   6082   5520   -125   -520   -946       C  
ATOM   4524  SD  MET A 605      -5.934 -18.220  14.079  1.00 42.77           S  
ANISOU 4524  SD  MET A 605     5308   5743   5200    -58   -472   -843       S  
ATOM   4525  CE  MET A 605      -5.536 -16.485  14.199  1.00 32.86           C  
ANISOU 4525  CE  MET A 605     4083   4558   3846     35   -428   -755       C  
ATOM   4526  N   ALA A 606      -7.847 -20.886  12.277  1.00 36.18           N  
ANISOU 4526  N   ALA A 606     4384   4863   4498   -124   -671  -1180       N  
ATOM   4527  CA  ALA A 606      -8.019 -22.219  12.829  1.00 40.53           C  
ANISOU 4527  CA  ALA A 606     4912   5312   5177   -258   -665  -1203       C  
ATOM   4528  C   ALA A 606      -7.567 -22.210  14.286  1.00 40.90           C  
ANISOU 4528  C   ALA A 606     4963   5306   5273   -360   -569  -1064       C  
ATOM   4529  O   ALA A 606      -6.656 -21.468  14.660  1.00 32.98           O  
ANISOU 4529  O   ALA A 606     4014   4311   4205   -309   -513   -953       O  
ATOM   4530  CB  ALA A 606      -7.219 -23.226  12.030  1.00 39.95           C  
ANISOU 4530  CB  ALA A 606     4926   5145   5109   -218   -694  -1247       C  
ATOM   4531  N   VAL A 607      -8.211 -23.029  15.110  1.00 39.44           N  
ANISOU 4531  N   VAL A 607     4721   5067   5199   -507   -550  -1070       N  
ATOM   4532  CA  VAL A 607      -7.829 -23.131  16.513  1.00 39.90           C  
ANISOU 4532  CA  VAL A 607     4795   5072   5293   -608   -463   -938       C  
ATOM   4533  C   VAL A 607      -7.591 -24.581  16.927  1.00 43.11           C  
ANISOU 4533  C   VAL A 607     5241   5333   5807   -718   -455   -920       C  
ATOM   4534  O   VAL A 607      -8.419 -25.453  16.671  1.00 44.31           O  
ANISOU 4534  O   VAL A 607     5344   5444   6049   -799   -492  -1016       O  
ATOM   4535  CB  VAL A 607      -8.895 -22.505  17.434  1.00 39.77           C  
ANISOU 4535  CB  VAL A 607     4676   5141   5293   -693   -418   -928       C  
ATOM   4536  CG1 VAL A 607      -8.474 -22.639  18.892  1.00 37.16           C  
ANISOU 4536  CG1 VAL A 607     4379   4760   4982   -796   -327   -791       C  
ATOM   4537  CG2 VAL A 607      -9.108 -21.041  17.075  1.00 40.91           C  
ANISOU 4537  CG2 VAL A 607     4788   5416   5339   -576   -429   -941       C  
ATOM   4538  N   MET A 608      -6.448 -24.836  17.553  1.00 42.94           N  
ANISOU 4538  N   MET A 608     5308   5227   5780   -718   -411   -799       N  
ATOM   4539  CA  MET A 608      -6.161 -26.151  18.120  1.00 44.75           C  
ANISOU 4539  CA  MET A 608     5587   5306   6108   -818   -399   -755       C  
ATOM   4540  C   MET A 608      -5.998 -26.036  19.630  1.00 46.28           C  
ANISOU 4540  C   MET A 608     5800   5481   6305   -915   -322   -611       C  
ATOM   4541  O   MET A 608      -4.972 -25.552  20.110  1.00 41.29           O  
ANISOU 4541  O   MET A 608     5227   4848   5612   -859   -295   -504       O  
ATOM   4542  CB  MET A 608      -4.885 -26.740  17.519  1.00 41.85           C  
ANISOU 4542  CB  MET A 608     5320   4840   5742   -723   -428   -743       C  
ATOM   4543  CG  MET A 608      -4.953 -27.037  16.034  1.00 47.61           C  
ANISOU 4543  CG  MET A 608     6053   5574   6463   -628   -500   -887       C  
ATOM   4544  SD  MET A 608      -3.393 -27.722  15.431  1.00 51.09           S  
ANISOU 4544  SD  MET A 608     6605   5901   6905   -514   -513   -870       S  
ATOM   4545  CE  MET A 608      -3.824 -28.096  13.733  1.00 86.99           C  
ANISOU 4545  CE  MET A 608    11151  10469  11434   -427   -596  -1065       C  
ATOM   4546  N   ASP A 609      -7.016 -26.469  20.371  1.00 55.57           N  
ANISOU 4546  N   ASP A 609     6921   6645   7547  -1062   -286   -612       N  
ATOM   4547  CA  ASP A 609      -6.973 -26.479  21.833  1.00 70.59           C  
ANISOU 4547  CA  ASP A 609     8850   8527   9444  -1168   -207   -477       C  
ATOM   4548  C   ASP A 609      -6.542 -27.841  22.365  1.00 81.59           C  
ANISOU 4548  C   ASP A 609    10332   9747  10922  -1256   -201   -403       C  
ATOM   4549  O   ASP A 609      -5.884 -28.615  21.668  1.00 85.33           O  
ANISOU 4549  O   ASP A 609    10866  10112  11442  -1200   -258   -432       O  
ATOM   4550  CB  ASP A 609      -8.347 -26.141  22.417  1.00 77.02           C  
ANISOU 4550  CB  ASP A 609     9555   9433  10276  -1283   -150   -511       C  
ATOM   4551  CG  ASP A 609      -8.790 -24.730  22.096  1.00 84.54           C  
ANISOU 4551  CG  ASP A 609    10423  10552  11146  -1195   -151   -569       C  
ATOM   4552  OD1 ASP A 609      -7.934 -23.820  22.083  1.00 86.93           O  
ANISOU 4552  OD1 ASP A 609    10773  10900  11354  -1083   -153   -514       O  
ATOM   4553  OD2 ASP A 609     -10.001 -24.531  21.860  1.00 86.42           O1-
ANISOU 4553  OD2 ASP A 609    10544  10871  11421  -1238   -151   -670       O1-
ATOM   4554  N   CYS A 610      -6.936 -28.121  23.606  1.00 88.69           N  
ANISOU 4554  N   CYS A 610    11244  10619  11836  -1392   -129   -307       N  
ATOM   4555  CA  CYS A 610      -6.645 -29.387  24.277  1.00 94.97           C  
ANISOU 4555  CA  CYS A 610    12133  11245  12706  -1491   -115   -215       C  
ATOM   4556  C   CYS A 610      -6.500 -30.558  23.307  1.00 95.67           C  
ANISOU 4556  C   CYS A 610    12253  11191  12907  -1479   -187   -299       C  
ATOM   4557  O   CYS A 610      -5.519 -31.303  23.359  1.00 95.06           O  
ANISOU 4557  O   CYS A 610    12282  10976  12860  -1439   -220   -235       O  
ATOM   4558  CB  CYS A 610      -7.743 -29.701  25.296  1.00 98.02           C  
ANISOU 4558  CB  CYS A 610    12481  11633  13129  -1675    -26   -173       C  
TER    4559      CYS A 610 
HETATM 4560  C1  GOL A 631     -11.913  -9.277   5.366  1.00 68.64           C  
HETATM 4561  O1  GOL A 631     -12.500 -10.065   6.380  1.00 68.86           O  
HETATM 4562  C2  GOL A 631     -12.493  -9.614   3.995  1.00 65.61           C  
HETATM 4563  O2  GOL A 631     -13.698 -10.336   4.117  1.00 64.58           O  
HETATM 4564  C3  GOL A 631     -11.499 -10.440   3.190  1.00 66.46           C  
HETATM 4565  O3  GOL A 631     -12.033 -10.632   1.899  1.00 69.21           O  
HETATM 4566  O   HOH A 632       3.742  -0.450  17.106  1.00 21.93           O  
HETATM 4567  O   HOH A 633       1.836   0.361  19.044  1.00 23.66           O  
HETATM 4568  O   HOH A 634       9.238  -3.966  18.449  1.00 24.76           O  
HETATM 4569  O   HOH A 635      -1.863  -6.505  27.180  1.00 21.77           O  
HETATM 4570  O   HOH A 636       3.179   4.623  29.923  1.00 27.90           O  
HETATM 4571  O   HOH A 637       3.838  -9.191  21.729  1.00 28.70           O  
HETATM 4572  O   HOH A 638       9.850 -28.714  15.537  1.00 30.97           O  
HETATM 4573  O   HOH A 639      12.362  -1.054  26.846  1.00 30.98           O  
HETATM 4574  O   HOH A 640      14.339 -11.435  39.058  1.00 29.33           O  
HETATM 4575  O   HOH A 641      17.458  -2.132  22.482  1.00 28.37           O  
HETATM 4576  O   HOH A 642       6.192  -9.811  41.883  1.00 30.97           O  
HETATM 4577  O   HOH A 643      19.379 -12.764  24.476  1.00 27.13           O  
HETATM 4578  O   HOH A 644      14.887   0.288  27.276  1.00 29.07           O  
HETATM 4579  O   HOH A 645       5.626  -2.107  18.362  1.00 26.47           O  
HETATM 4580  O   HOH A 646       6.426 -24.658  25.235  1.00 35.85           O  
HETATM 4581  O   HOH A 647      12.880 -12.703  41.063  1.00 36.00           O  
HETATM 4582  O   HOH A 648       7.992  -7.589   9.670  1.00 29.28           O  
HETATM 4583  O   HOH A 649       6.837 -14.516  24.803  1.00 31.99           O  
HETATM 4584  O   HOH A 650       9.230  -2.068  20.319  1.00 24.30           O  
HETATM 4585  O   HOH A 651      15.432   1.749  24.972  1.00 32.73           O  
HETATM 4586  O   HOH A 652      -2.312 -15.284   7.782  1.00 34.41           O  
HETATM 4587  O   HOH A 653       4.899 -14.781  33.218  1.00 30.21           O  
HETATM 4588  O   HOH A 654      22.090   2.654  27.445  1.00 40.00           O  
HETATM 4589  O   HOH A 655      21.583 -18.046  11.843  1.00 33.15           O  
HETATM 4590  O   HOH A 656      17.495  -2.577  25.187  1.00 28.51           O  
HETATM 4591  O   HOH A 657      -4.021  -1.267  13.126  1.00 25.06           O  
HETATM 4592  O   HOH A 658       5.249   6.217  29.426  1.00 36.25           O  
HETATM 4593  O   HOH A 659       0.959 -15.589  21.596  1.00 30.13           O  
HETATM 4594  O   HOH A 660      16.481 -21.410   9.366  1.00 34.60           O  
HETATM 4595  O   HOH A 661      -6.104   5.638  40.043  1.00 47.43           O  
HETATM 4596  O   HOH A 662       9.746  13.507  33.946  1.00 39.18           O  
HETATM 4597  O   HOH A 663      21.519 -21.430  22.266  1.00 31.13           O  
HETATM 4598  O   HOH A 664       3.692   6.142  15.053  1.00 32.79           O  
HETATM 4599  O   HOH A 665      15.031   1.859  48.973  1.00 43.90           O  
HETATM 4600  O   HOH A 666       8.797  15.097  38.102  1.00 36.59           O  
HETATM 4601  O   HOH A 667      10.173   1.505  15.638  1.00 39.47           O  
HETATM 4602  O   HOH A 668      12.047  16.472  43.475  1.00 42.35           O  
HETATM 4603  O   HOH A 669      20.534  -4.687  27.595  1.00 29.03           O  
HETATM 4604  O   HOH A 670      -3.976  -3.975  12.970  1.00 34.06           O  
HETATM 4605  O   HOH A 671      17.139  36.982  43.360  1.00 46.17           O  
HETATM 4606  O   HOH A 672       4.181 -11.371  22.964  1.00 33.49           O  
HETATM 4607  O   HOH A 673      11.740  -4.890  10.389  1.00 29.81           O  
HETATM 4608  O   HOH A 674      -7.530   0.379  39.007  1.00 39.49           O  
HETATM 4609  O   HOH A 675      -8.346 -10.956   4.514  1.00 38.48           O  
HETATM 4610  O   HOH A 676       7.837 -17.963   5.978  1.00 33.53           O  
HETATM 4611  O   HOH A 677      17.384 -14.397  25.351  1.00 35.72           O  
HETATM 4612  O   HOH A 678      -4.982  -7.058   1.461  1.00 43.35           O  
HETATM 4613  O   HOH A 679       4.343  13.714  37.906  1.00 33.33           O  
HETATM 4614  O   HOH A 680      10.144 -22.697  25.768  1.00 34.33           O  
HETATM 4615  O   HOH A 681      14.773  22.523  31.725  1.00 38.23           O  
HETATM 4616  O   HOH A 682      16.446  10.421  31.532  1.00 42.65           O  
HETATM 4617  O   HOH A 683       2.557   4.367  32.552  1.00 29.61           O  
HETATM 4618  O   HOH A 684      18.095 -15.445  11.443  1.00 35.22           O  
HETATM 4619  O   HOH A 685       6.825 -19.136   2.116  1.00 41.91           O  
HETATM 4620  O   HOH A 686      -1.955  -4.079   1.345  1.00 41.52           O  
HETATM 4621  O   HOH A 687       0.475 -11.443  36.317  1.00 40.74           O  
HETATM 4622  O   HOH A 688      21.955 -19.943  13.894  1.00 36.19           O  
HETATM 4623  O   HOH A 689     -10.902  -6.403  33.548  1.00 29.94           O  
HETATM 4624  O   HOH A 690      19.389 -17.567  10.386  1.00 38.77           O  
HETATM 4625  O   HOH A 691      13.547   3.408  23.780  1.00 34.28           O  
HETATM 4626  O   HOH A 692      -0.691 -19.192  28.301  1.00 40.48           O  
HETATM 4627  O   HOH A 693      26.609  28.031  37.867  1.00 40.80           O  
HETATM 4628  O   HOH A 694       6.820 -10.950  27.072  1.00 35.25           O  
HETATM 4629  O   HOH A 695       9.373 -15.046  25.734  1.00 35.68           O  
HETATM 4630  O   HOH A 696      10.198  -6.061   8.656  1.00 37.43           O  
HETATM 4631  O   HOH A 697      16.152 -31.354  15.640  1.00 33.89           O  
HETATM 4632  O   HOH A 698      20.073 -19.876  23.959  1.00 31.33           O  
HETATM 4633  O   HOH A 699      -7.704  -7.505  38.176  1.00 33.75           O  
HETATM 4634  O   HOH A 700      28.224 -22.391  24.765  1.00 38.36           O  
HETATM 4635  O   HOH A 701      -2.710   9.947  37.237  1.00 37.35           O  
HETATM 4636  O   HOH A 702      16.933 -15.200  27.874  1.00 32.50           O  
HETATM 4637  O   HOH A 703      10.032   1.771   2.369  1.00 46.56           O  
HETATM 4638  O   HOH A 704      23.732  -2.751  13.443  1.00 41.06           O  
HETATM 4639  O   HOH A 705      28.025  31.924  35.464  1.00 41.86           O  
HETATM 4640  O   HOH A 706      22.411  -7.788  18.552  1.00 40.79           O  
HETATM 4641  O   HOH A 707      13.700 -14.576  21.134  1.00 31.27           O  
HETATM 4642  O   HOH A 708      24.304  -3.218  28.257  1.00 34.82           O  
HETATM 4643  O   HOH A 709      12.825   2.791  12.599  1.00 35.79           O  
HETATM 4644  O   HOH A 710      13.703   9.882  15.907  1.00 40.63           O  
HETATM 4645  O   HOH A 711      18.441  20.600  46.447  1.00 41.35           O  
HETATM 4646  O   HOH A 712      -1.040 -12.819   4.590  1.00 34.84           O  
HETATM 4647  O   HOH A 713      -6.270  -6.504   3.820  1.00 38.06           O  
HETATM 4648  O   HOH A 714      18.131  15.293  40.965  1.00 45.25           O  
HETATM 4649  O   HOH A 715      19.103 -17.708   7.923  1.00 40.51           O  
HETATM 4650  O   HOH A 716      15.397   9.140  13.834  1.00 45.35           O  
HETATM 4651  O   HOH A 717      24.868  -6.699  43.812  1.00 43.72           O  
HETATM 4652  O   HOH A 718      10.474  40.530  44.949  1.00 50.68           O  
HETATM 4653  O   HOH A 719       3.976 -16.571  31.627  1.00 39.66           O  
HETATM 4654  O   HOH A 720       1.661  23.593  42.793  1.00 38.64           O  
HETATM 4655  O   HOH A 721      -3.351   6.636   9.585  1.00 44.11           O  
HETATM 4656  O   HOH A 722       1.983 -13.520  23.262  1.00 42.38           O  
HETATM 4657  O   HOH A 723      25.709 -14.723  17.574  1.00 39.25           O  
HETATM 4658  O   HOH A 724       6.542  14.309  36.486  1.00 39.91           O  
HETATM 4659  O   HOH A 725      15.651 -16.957  34.363  1.00 34.11           O  
HETATM 4660  O   HOH A 726      14.761 -13.040  25.198  1.00 41.20           O  
HETATM 4661  O   HOH A 727      26.335  -4.203  35.473  1.00 36.71           O  
HETATM 4662  O   HOH A 728      -4.173  -3.983  23.889  1.00 39.66           O  
HETATM 4663  O   HOH A 729      12.622  41.643  45.542  1.00 47.63           O  
HETATM 4664  O   HOH A 730      20.866  -9.170  21.278  1.00 44.14           O  
HETATM 4665  O   HOH A 731      16.965  17.016  42.892  1.00 47.01           O  
HETATM 4666  O   HOH A 732      16.354 -19.592  34.989  1.00 44.51           O  
HETATM 4667  O   HOH A 733       7.076  13.057  34.150  1.00 41.56           O  
HETATM 4668  O   HOH A 734      17.531 -19.840   7.599  1.00 43.61           O  
HETATM 4669  O   HOH A 735      13.880  12.858  31.552  1.00 39.37           O  
HETATM 4670  O   HOH A 736     -10.356  -8.096  11.406  1.00 39.22           O  
HETATM 4671  O   HOH A 737       6.702 -12.929  13.261  1.00 32.13           O  
HETATM 4672  O   HOH A 738       9.557  24.217  50.764  1.00 40.44           O  
HETATM 4673  O   HOH A 739       2.762 -13.523  34.267  1.00 36.05           O  
HETATM 4674  O   HOH A 740      21.788 -11.061  38.488  1.00 37.85           O  
HETATM 4675  O   HOH A 741      14.090  18.914  52.188  1.00 44.13           O  
HETATM 4676  O   HOH A 742      -6.453  11.082  36.846  1.00 46.58           O  
HETATM 4677  O   HOH A 743      20.629  15.194  34.751  1.00 35.87           O  
HETATM 4678  O   HOH A 744      -1.379 -15.763  26.256  1.00 40.48           O  
HETATM 4679  O   HOH A 745      -5.733 -15.774  18.106  1.00 48.49           O  
HETATM 4680  O   HOH A 746      10.859   3.815  24.202  1.00 36.83           O  
HETATM 4681  O   HOH A 747      10.192  -1.796   8.652  1.00 43.07           O  
HETATM 4682  O   HOH A 748      12.458  25.946  51.513  1.00 41.01           O  
HETATM 4683  O   HOH A 749      14.896  35.204  42.867  1.00 44.33           O  
HETATM 4684  O   HOH A 750      -6.445   0.305   1.504  1.00 34.00           O  
HETATM 4685  O   HOH A 751      10.355   5.463  28.898  1.00 35.34           O  
HETATM 4686  O   HOH A 752       5.721  27.309  39.947  1.00 39.63           O  
HETATM 4687  O   HOH A 753       9.230  -3.889   7.109  1.00 37.03           O  
HETATM 4688  O   HOH A 754      34.754   2.571  30.076  1.00 43.40           O  
HETATM 4689  O   HOH A 755      23.840 -12.724  39.523  1.00 45.25           O  
HETATM 4690  O   HOH A 756      -4.256  -8.652  24.260  1.00 36.74           O  
HETATM 4691  O   HOH A 757       8.819 -22.807   8.236  1.00 37.52           O  
HETATM 4692  O   HOH A 758      31.296 -18.687  19.417  1.00 42.61           O  
HETATM 4693  O   HOH A 759      18.913  37.406  51.785  1.00 45.51           O  
HETATM 4694  O   HOH A 760      20.098  -2.259  21.764  1.00 39.48           O  
HETATM 4695  O   HOH A 761      -6.011  -9.527   0.723  1.00 46.35           O  
HETATM 4696  O   HOH A 762      22.671  26.169  44.488  1.00 38.48           O  
HETATM 4697  O   HOH A 763       2.780  14.333  34.413  1.00 48.69           O  
HETATM 4698  O   HOH A 764      28.306  29.246  36.216  1.00 46.63           O  
HETATM 4699  O   HOH A 765       0.788 -11.506   3.376  1.00 40.18           O  
HETATM 4700  O   HOH A 766      25.179   9.594  31.311  1.00 40.86           O  
HETATM 4701  O   HOH A 767      -2.177 -10.343  25.211  1.00 38.74           O  
HETATM 4702  O   HOH A 768     -10.656 -19.952   5.189  1.00 43.77           O  
HETATM 4703  O   HOH A 769      30.688   6.953  35.000  1.00 46.09           O  
HETATM 4704  O   HOH A 770      21.110  -4.080  12.899  1.00 42.76           O  
HETATM 4705  O   HOH A 771       0.000  -6.293  -0.000  0.50 45.24           O  
HETATM 4706  O   HOH A 772       8.597 -20.632   4.552  1.00 38.85           O  
HETATM 4707  O   HOH A 773       1.188  11.782  11.874  1.00 40.48           O  
HETATM 4708  O   HOH A 774       8.424   7.584  30.369  1.00 39.24           O  
HETATM 4709  O   HOH A 775      -7.588   1.259  29.718  0.50 36.74           O  
HETATM 4710  O   HOH A 776      12.586  24.054  31.272  1.00 43.84           O  
HETATM 4711  O   HOH A 777      -1.897 -14.551  22.135  1.00 41.57           O  
HETATM 4712  O   HOH A 778      22.102  23.929  33.964  1.00 46.61           O  
HETATM 4713  O   HOH A 779      14.804   5.646  22.869  1.00 45.16           O  
HETATM 4714  O   HOH A 780      17.624 -26.531  17.154  1.00 45.87           O  
HETATM 4715  O   HOH A 781      16.366 -26.801  23.757  1.00 37.23           O  
HETATM 4716  O   HOH A 782      12.817  36.193  31.538  1.00 39.51           O  
HETATM 4717  O   HOH A 783      -9.135   3.136  28.294  1.00 47.28           O  
HETATM 4718  O   HOH A 784      10.468  35.480  30.960  1.00 43.21           O  
HETATM 4719  O   HOH A 785      19.115  34.006  38.162  1.00 43.57           O  
HETATM 4720  O   HOH A 786      21.660  33.301  37.975  1.00 44.88           O  
HETATM 4721  O   HOH A 787       4.278  12.327  23.881  1.00 46.37           O  
HETATM 4722  O   HOH A 788       3.270  16.159  41.125  1.00 41.90           O  
HETATM 4723  O   HOH A 789       9.663   6.729  46.930  1.00 42.38           O  
HETATM 4724  O   HOH A 790      17.340   3.378  50.073  1.00 46.43           O  
HETATM 4725  O   HOH A 791       0.623  23.268  36.981  1.00 43.21           O  
HETATM 4726  O   HOH A 792      -4.107   8.888  15.990  1.00 47.02           O  
HETATM 4727  O   HOH A 793      10.551  15.240  41.505  1.00 46.66           O  
HETATM 4728  O   HOH A 794      10.823  -2.191  11.058  1.00 34.67           O  
HETATM 4729  O   HOH A 795      -3.824  11.193  31.724  1.00 47.35           O  
HETATM 4730  O   HOH A 796       2.916  12.707  28.912  1.00 41.96           O  
HETATM 4731  O   HOH A 797      -4.607 -13.259  17.994  1.00 44.90           O  
HETATM 4732  O   HOH A 798      16.196  11.992  47.787  1.00 47.56           O  
HETATM 4733  O   HOH A 799      11.159  39.318  54.453  1.00 45.65           O  
HETATM 4734  O   HOH A 800      10.594  39.829  47.593  1.00 47.52           O  
HETATM 4735  O   HOH A 801      13.945  40.996  48.536  1.00 48.63           O  
HETATM 4736  O   HOH A 802      21.694  37.984  51.678  1.00 50.87           O  
HETATM 4737  O   HOH A 803       3.539  33.466  36.125  1.00 48.26           O  
HETATM 4738  O   HOH A 804      -2.392  26.873  46.293  1.00 48.22           O  
HETATM 4739  O   HOH A 805       0.768  21.039  47.704  1.00 51.21           O  
HETATM 4740  O   HOH A 806       4.195  21.081  47.561  1.00 47.92           O  
HETATM 4741  O   HOH A 807      16.612  25.171  52.364  1.00 48.94           O  
HETATM 4742  O   HOH A 808      19.158  32.343  50.132  1.00 54.88           O  
HETATM 4743  O   HOH A 809      20.760  32.079  45.152  1.00 54.14           O  
HETATM 4744  O   HOH A 810      24.427  19.846  38.083  1.00 59.83           O  
HETATM 4745  O   HOH A 811      40.295  -0.412  26.644  1.00 55.52           O  
HETATM 4746  O   HOH A 812      29.608 -15.263  18.286  1.00 47.20           O  
HETATM 4747  O   HOH A 813      27.999 -11.516  15.730  1.00 56.94           O  
HETATM 4748  O   HOH A 814      26.547 -22.700  27.178  1.00 49.20           O  
HETATM 4749  O   HOH A 815      14.161 -18.099  32.480  1.00 46.32           O  
HETATM 4750  O   HOH A 816       8.913 -21.158  32.185  1.00 60.93           O  
HETATM 4751  O   HOH A 817       2.875 -20.702  34.482  1.00 51.04           O  
HETATM 4752  O   HOH A 818       1.393 -16.650  32.148  1.00 50.63           O  
HETATM 4753  O   HOH A 819      25.146  -6.833  36.875  1.00 51.66           O  
HETATM 4754  O   HOH A 820       7.877  11.293  30.606  1.00 47.47           O  
HETATM 4755  O   HOH A 821      -6.453  10.046  15.855  1.00 50.25           O  
HETATM 4756  O   HOH A 822      -6.862 -11.505  17.648  1.00 54.67           O  
HETATM 4757  O   HOH A 823      -4.027 -13.575  20.681  1.00 49.67           O  
HETATM 4758  O   HOH A 824      -8.101  -7.710  16.847  1.00 48.93           O  
HETATM 4759  O   HOH A 825      -5.973  -4.727  14.468  1.00 50.06           O  
HETATM 4760  O   HOH A 826      -2.071  -9.305  27.899  1.00 34.63           O  
HETATM 4761  O   HOH A 827       6.246 -12.917  21.799  1.00 49.71           O  
HETATM 4762  O   HOH A 828       9.831 -14.829  22.912  1.00 55.47           O  
HETATM 4763  O   HOH A 829       2.536 -14.146  27.845  1.00 52.51           O  
HETATM 4764  O   HOH A 830       6.865 -17.993  36.568  1.00 47.88           O  
HETATM 4765  O   HOH A 831       6.581 -18.313  39.924  1.00 50.28           O  
HETATM 4766  O   HOH A 832       9.904  -5.435  45.422  1.00 50.35           O  
HETATM 4767  O   HOH A 833      -7.974   5.523  37.737  1.00 57.33           O  
HETATM 4768  O   HOH A 834      -0.681  -6.996  41.241  1.00 47.02           O  
HETATM 4769  O   HOH A 835       6.585  33.024  32.062  1.00 59.61           O  
HETATM 4770  O   HOH A 836      18.788  37.851  31.457  1.00 45.86           O  
HETATM 4771  O   HOH A 837      11.314  27.266  29.091  1.00 53.29           O  
HETATM 4772  O   HOH A 838      17.358  12.261  41.271  1.00 52.60           O  
HETATM 4773  O   HOH A 839      22.339  -9.567  47.192  1.00 46.92           O  
HETATM 4774  O   HOH A 840      29.776  -3.685  45.205  1.00 62.70           O  
HETATM 4775  O   HOH A 841      18.844  -5.571  10.118  1.00 46.33           O  
HETATM 4776  O   HOH A 842      14.539  -6.967   7.918  1.00 48.55           O  
HETATM 4777  O   HOH A 843      13.990  -4.511   9.098  1.00 57.55           O  
HETATM 4778  O   HOH A 844      13.250   3.229   9.591  1.00 52.28           O  
HETATM 4779  O   HOH A 845      15.614 -11.856   7.971  1.00 44.95           O  
HETATM 4780  O   HOH A 846      -0.713  10.723  10.099  1.00 54.74           O  
HETATM 4781  O   HOH A 847      10.393   0.443   6.907  1.00 56.77           O  
HETATM 4782  O   HOH A 848       7.596 -18.320  -0.399  1.00 47.43           O  
HETATM 4783  O   HOH A 849       7.362 -13.333  -3.564  1.00 58.88           O  
HETATM 4784  O   HOH A 850       5.365 -12.025  -1.842  1.00 52.69           O  
HETATM 4785  O   HOH A 851       9.652 -14.018  -2.049  1.00 54.25           O  
HETATM 4786  O   HOH A 852       9.119 -34.647  14.898  1.00 52.17           O  
HETATM 4787  O   HOH A 853       2.886 -31.792   9.306  1.00 46.06           O  
HETATM 4788  O   HOH A 854       5.376 -31.168   8.416  1.00 49.54           O  
HETATM 4789  O   HOH A 855      -8.323 -24.016   8.899  1.00 46.85           O  
HETATM 4790  O   HOH A 856     -10.522 -24.377  14.042  1.00 61.61           O  
HETATM 4791  O   HOH A 857      -4.961 -24.108  31.477  1.00 55.08           O  
HETATM 4792  O   HOH A 858      -1.855  -8.676   2.806  1.00 48.66           O  
HETATM 4793  O   HOH A 859      -9.093   2.580   5.131  1.00 52.23           O  
HETATM 4794  O   HOH A 860       2.530   0.274  44.130  1.00 52.38           O  
HETATM 4795  O   HOH A 861      15.422 -27.657  18.082  1.00 38.23           O  
HETATM 4796  O   HOH A 862      -2.349  -1.345   1.054  1.00 45.44           O  
HETATM 4797  O   HOH A 863      -8.216  -8.906  30.956  1.00 44.01           O  
HETATM 4798  O   HOH A 864      -4.354  -9.818  29.886  1.00 49.34           O  
HETATM 4799  O   HOH A 865      -5.811   8.087   9.616  1.00 47.46           O  
HETATM 4800  O   HOH A 866       5.699  11.093  26.493  1.00 52.33           O  
HETATM 4801  O   HOH A 867      14.449   8.192  30.250  1.00 53.54           O  
HETATM 4802  O   HOH A 868      -9.925 -11.442  37.446  1.00 46.14           O  
HETATM 4803  O   HOH A 869      33.505   5.931  35.296  1.00 55.93           O  
HETATM 4804  O   HOH A 870      27.107 -19.814  30.523  1.00 55.02           O  
HETATM 4805  O   HOH A 871       8.198 -16.585  42.498  1.00 53.31           O  
HETATM 4806  O   HOH A 872       9.358  27.969  57.783  1.00 65.55           O  
HETATM 4807  O   HOH A 873       0.000  -0.061  -0.000  0.50 50.65           O  
HETATM 4808  O   HOH A 874      21.030  -6.887  12.363  1.00 48.51           O  
HETATM 4809  O   HOH A 875      15.532 -26.970   6.714  1.00 53.08           O  
HETATM 4810  O   HOH A 876      20.462  20.448  48.037  1.00 51.81           O  
HETATM 4811  O   HOH A 877      -7.898  -6.293  13.243  1.00 52.98           O  
HETATM 4812  O   HOH A 878      10.979  16.505  32.341  1.00 49.70           O  
HETATM 4813  O   HOH A 879       0.102 -15.100  28.777  1.00 51.72           O  
HETATM 4814  O   HOH A 880      13.700   4.121  51.930  1.00 52.38           O  
HETATM 4815  O   HOH A 881       7.476   9.990  21.710  1.00 45.67           O  
HETATM 4816  O   HOH A 882      -3.064  24.080  46.828  1.00 55.29           O  
HETATM 4817  O   HOH A 883      35.190  14.642  35.574  1.00 59.09           O  
HETATM 4818  O   HOH A 884      -4.370 -21.508   1.870  1.00 55.57           O  
HETATM 4819  O   HOH A 885      -6.625 -17.146  24.708  1.00 55.43           O  
HETATM 4820  O   HOH A 886      18.633 -20.113  28.103  1.00 58.71           O  
HETATM 4821  O   HOH A 887      -3.731 -14.882   3.913  1.00 49.92           O  
HETATM 4822  O   HOH A 888      29.232   3.670  16.813  1.00 55.83           O  
HETATM 4823  O   HOH A 889       8.007 -12.249  48.138  1.00 52.69           O  
HETATM 4824  O   HOH A 890      13.598 -13.660   0.156  1.00 55.56           O  
HETATM 4825  O   HOH A 891      -5.113  13.644   3.272  1.00 52.51           O  
HETATM 4826  O   HOH A 892      -5.042  12.364  27.346  1.00 57.63           O  
HETATM 4827  O   HOH A 893       2.050 -28.339   2.921  1.00 59.43           O  
HETATM 4828  O   HOH A 894      11.317 -14.813  19.727  1.00 48.41           O  
HETATM 4829  O   HOH A 895      -0.252   6.082   6.576  1.00 57.46           O  
HETATM 4830  O   HOH A 896      -5.802  23.966  46.476  1.00 57.37           O  
HETATM 4831  O   HOH A 897      13.271 -28.388   5.962  1.00 53.40           O  
HETATM 4832  O   HOH A 898      -4.705  10.435  11.681  1.00 57.94           O  
HETATM 4833  O   HOH A 899      -1.757   4.430   5.272  1.00 54.57           O  
HETATM 4834  O   HOH A 900      -0.416  21.839  42.732  1.00 50.74           O  
HETATM 4835  O   HOH A 901       4.661  34.869  37.973  1.00 52.85           O  
HETATM 4836  O   HOH A 902      10.668  35.148  60.186  1.00 60.43           O  
HETATM 4837  O   HOH A 903      -2.779   9.786  13.760  1.00 51.97           O  
HETATM 4838  O   HOH A 904       7.261 -14.888  19.120  1.00 39.77           O  
HETATM 4839  O   HOH A 905       8.475 -12.278  22.700  1.00 33.70           O  
HETATM 4840  O   HOH A 906      34.926   3.218  34.550  1.00 52.63           O  
HETATM 4841  O   HOH A 907       8.981  39.446  42.201  1.00 59.79           O  
HETATM 4842  O   HOH A 908       7.767  42.152  44.511  1.00 54.73           O  
HETATM 4843  O   HOH A 909      28.872 -14.273  32.292  1.00 46.85           O  
HETATM 4844  O   HOH A 910      23.755 -17.978  10.288  1.00 55.01           O  
HETATM 4845  O   HOH A 911      10.173 -15.008  42.472  1.00 56.92           O  
HETATM 4846  O   HOH A 912      -0.634  24.507  39.180  1.00 56.16           O  
HETATM 4847  O   HOH A 913      10.653 -10.764  21.337  1.00 48.29           O  
HETATM 4848  O   HOH A 914      15.299  45.837  20.255  1.00 59.03           O  
HETATM 4849  O   HOH A 915      26.021  -8.772  39.674  1.00 55.11           O  
HETATM 4850  O   HOH A 916      27.925 -14.062  16.327  1.00 51.29           O  
HETATM 4851  O   HOH A 917      14.543  15.649  31.247  1.00 55.28           O  
HETATM 4852  O   HOH A 918      11.114  29.575  56.452  1.00 60.94           O  
HETATM 4853  O   HOH A 919      25.097  -7.661  18.344  1.00 50.13           O  
HETATM 4854  O   HOH A 920      14.713  15.516  43.755  1.00 48.73           O  
HETATM 4855  O   HOH A 921      -7.279 -22.245   1.868  1.00 52.95           O  
HETATM 4856  O   HOH A 922      14.932  13.481  41.890  1.00 50.47           O  
HETATM 4857  O   HOH A 923       9.139 -20.584  -1.337  1.00 56.52           O  
HETATM 4858  O   HOH A 924       3.418  26.328  30.314  1.00 57.33           O  
HETATM 4859  O   HOH A 925      11.926  33.812  58.184  1.00 49.31           O  
HETATM 4860  O   HOH A 926      19.112   2.146  51.707  1.00 53.33           O  
HETATM 4861  O   HOH A 927      20.098  -5.637  53.128  1.00 57.18           O  
HETATM 4862  O   HOH A 928      -2.310   7.286   7.384  1.00 52.78           O  
HETATM 4863  O   HOH A 929      -5.896 -16.007  21.106  1.00 55.48           O  
HETATM 4864  O   HOH A 930       5.479 -12.162  25.155  1.00 48.55           O  
HETATM 4865  O   HOH A 931       0.815 -12.216  25.118  1.00 50.49           O  
HETATM 4866  O   HOH A 932      14.313  -2.218  14.515  1.00 47.70           O  
HETATM 4867  O   HOH A 933      14.603  13.962  45.991  1.00 50.10           O  
HETATM 4868  O   HOH A 934      22.234  -8.481  11.095  1.00 50.45           O  
HETATM 4869  O   HOH A 935      -1.840 -21.341  35.329  1.00 54.26           O  
HETATM 4870  O   HOH A 936      13.240  -0.433  12.030  1.00 62.53           O  
HETATM 4871  O   HOH A 937      33.480  14.766  33.414  1.00 59.35           O  
HETATM 4872  O   HOH A 938      10.061  26.197  55.445  1.00 55.12           O  
HETATM 4873  O   HOH A 939      34.266  -7.007  22.223  1.00 53.76           O  
HETATM 4874  O   HOH A 940      21.460  23.222  30.467  1.00 52.22           O  
HETATM 4875  O   HOH A 941      18.738  18.529  44.462  1.00 46.59           O  
HETATM 4876  O   HOH A 942      16.581   6.339  24.585  1.00 59.54           O  
HETATM 4877  O   HOH A 943       3.582  14.969  16.609  1.00 51.91           O  
HETATM 4878  O   HOH A 944      11.675  43.617  47.168  1.00 61.42           O  
HETATM 4879  O   HOH A 945      27.574  -8.174  37.479  1.00 58.45           O  
HETATM 4880  O   HOH A 946       1.255   8.828  13.908  1.00 33.85           O  
HETATM 4881  O   HOH A 947      -8.720   3.005  38.970  1.00 49.57           O  
HETATM 4882  O   HOH A 948       0.186  19.355  39.329  1.00 50.71           O  
HETATM 4883  O   HOH A 949      -7.293   8.779  26.088  1.00 55.96           O  
HETATM 4884  O   HOH A 950       1.748  18.394  41.414  1.00 56.93           O  
HETATM 4885  O   HOH A 951      -2.662 -21.030  27.002  1.00 45.26           O  
HETATM 4886  O   HOH A 952       3.164 -11.864  26.409  1.00 56.18           O  
HETATM 4887  O   HOH A 953      37.309   1.402  23.519  1.00 57.13           O  
HETATM 4888  O   HOH A 954      -6.391   7.357  28.483  1.00 55.65           O  
HETATM 4889  O   HOH A 955      -3.688 -16.844  26.919  1.00 59.55           O  
HETATM 4890  O   HOH A 956      16.554 -26.417   9.080  1.00 57.92           O  
HETATM 4891  O   HOH A 957       2.114 -33.831   7.327  1.00 46.37           O  
HETATM 4892  O   HOH A 958      27.900  14.213  31.013  1.00 53.82           O  
HETATM 4893  O   HOH A 959       6.645  36.794  37.474  1.00 50.99           O  
HETATM 4894  O   HOH A 960       9.545  24.120  53.743  1.00 62.54           O  
HETATM 4895  O   HOH A 961       5.006  13.310  32.507  1.00 51.70           O  
HETATM 4896  O   HOH A 962       6.181  14.469   6.941  1.00 58.35           O  
HETATM 4897  O   HOH A 963      30.424  13.682  31.890  1.00 47.97           O  
HETATM 4898  O   HOH A 964      37.520  -7.164  30.992  1.00 64.52           O  
HETATM 4899  O   HOH A 965      22.208  38.858  54.232  1.00 46.44           O  
HETATM 4900  O   HOH A 966       4.915  39.049  37.740  1.00 48.90           O  
HETATM 4901  O   HOH A 967      28.211  26.639  39.626  1.00 65.00           O  
HETATM 4902  O   HOH A 968      23.320  19.690  40.292  1.00 60.52           O  
HETATM 4903  O   HOH A 969      -7.509  13.530  36.448  1.00 65.61           O  
HETATM 4904  O   HOH A 970      21.424  21.294  41.545  1.00 56.55           O  
HETATM 4905  O   HOH A 971      15.332 -20.085   5.701  1.00 50.21           O  
HETATM 4906  O   HOH A 972      11.558  11.766  44.307  1.00 59.21           O  
HETATM 4907  O   HOH A 973      30.048  -0.030  45.530  1.00 56.32           O  
HETATM 4908  O   HOH A 974      -0.070 -18.639   3.843  1.00 48.07           O  
HETATM 4909  O   HOH A 975      -6.790  23.899  48.867  1.00 63.32           O  
HETATM 4910  O   HOH A 976      -3.507 -18.209   3.413  1.00 57.15           O  
HETATM 4911  O   HOH A 977      21.773   6.947  28.434  1.00 41.09           O  
HETATM 4912  O   HOH A 978      30.715  -0.755  16.784  1.00 68.04           O  
HETATM 4913  O   HOH A 979      19.840  -8.336  14.126  1.00 43.27           O  
HETATM 4914  O   HOH A 980      -7.652   6.108  35.111  1.00 48.26           O  
HETATM 4915  O   HOH A 981      21.809   7.119  52.767  1.00 67.01           O  
HETATM 4916  O   HOH A 982      14.182 -15.231   4.941  1.00 58.56           O  
HETATM 4917  O   HOH A 983      18.919  40.590  26.748  1.00 51.55           O  
HETATM 4918  O   HOH A 984      -5.292 -26.630  26.525  1.00 59.48           O  
HETATM 4919  O   HOH A 985      15.316  28.292  23.011  1.00 51.89           O  
HETATM 4920  O   HOH A 986      -1.625  12.357  40.124  1.00 57.52           O  
HETATM 4921  O   HOH A 987      24.852  -9.273  10.516  1.00 73.23           O  
HETATM 4922  O   HOH A 988      30.552  11.085  15.491  1.00 66.23           O  
HETATM 4923  O   HOH A 989      -8.554 -14.247  13.083  1.00 54.73           O  
HETATM 4924  O   HOH A 990      18.565   1.381  11.540  1.00 65.76           O  
HETATM 4925  O   HOH A 991      24.362  -3.135  52.006  1.00 65.92           O  
HETATM 4926  O   HOH A 992      -9.885 -15.638  21.679  1.00 60.24           O  
HETATM 4927  O   HOH A 993      30.705  15.731  33.907  1.00 53.24           O  
HETATM 4928  O   HOH A 994      16.893  31.421  53.204  1.00 60.44           O  
HETATM 4929  O   HOH A 995      13.748  12.723  15.980  1.00 53.67           O  
HETATM 4930  O   HOH A 996      -0.638  17.264  35.869  1.00 53.34           O  
HETATM 4931  O   HOH A 997       7.541  11.496  24.029  1.00 63.96           O  
HETATM 4932  O   HOH A 998       7.463 -22.946   2.904  1.00 65.55           O  
HETATM 4933  O   HOH A 999       9.515  12.772  42.620  1.00 44.29           O  
HETATM 4934  O   HOH A1000      -3.525   8.704  34.682  1.00 36.65           O  
HETATM 4935  O   HOH A1001      -3.587  12.952  34.575  1.00 61.62           O  
HETATM 4936  O   HOH A1002      21.096 -20.466  26.473  1.00 50.21           O  
HETATM 4937  O   HOH A1003       3.331  14.776  14.050  1.00 47.68           O  
HETATM 4938  O   HOH A1004       5.255  16.803  12.805  1.00 61.60           O  
HETATM 4939  O   HOH A1005     -12.864  -3.852   5.660  1.00 77.06           O  
HETATM 4940  O   HOH A1006      13.934 -17.955  38.452  1.00 69.57           O  
HETATM 4941  O   HOH A1007      27.190  -5.559  17.854  1.00 68.56           O  
HETATM 4942  O   HOH A1008      26.478  -4.003  15.813  1.00 59.54           O  
HETATM 4943  O   HOH A1009      27.057  -8.459  15.385  1.00 68.33           O  
HETATM 4944  O   HOH A1010      23.786  -4.178   9.901  1.00 64.56           O  
HETATM 4945  O   HOH A1011      17.297  -1.361  12.314  1.00 51.73           O  
HETATM 4946  O   HOH A1012      18.415 -13.098   9.775  1.00 65.24           O  
HETATM 4947  O   HOH A1013      13.590 -16.038   2.455  1.00 65.99           O  
HETATM 4948  O   HOH A1014      -5.552 -29.938  18.563  1.00 63.79           O  
HETATM 4949  O   HOH A1015      -1.777 -32.309  16.062  1.00 59.52           O  
HETATM 4950  O   HOH A1016      -7.588   5.122  29.718  0.50 59.83           O  
HETATM 4951  O   HOH A1017       3.274 -16.178  37.035  1.00 72.08           O  
HETATM 4952  O   HOH A1018       5.085 -16.832  35.119  1.00 56.68           O  
HETATM 4953  O   HOH A1019       7.875   9.881  28.039  1.00 78.77           O  
HETATM 4954  O   HOH A1020       9.877 -16.538  -0.234  1.00 56.56           O  
HETATM 4955  O   HOH A1021      12.332  15.748   5.635  1.00 63.56           O  
HETATM 4956  O   HOH A1022      30.280   1.683  18.188  1.00 66.06           O  
HETATM 4957  O   HOH A1023      44.860   9.345  32.408  1.00 62.58           O  
HETATM 4958  O   HOH A1024      13.079  -0.082  14.716  1.00 63.71           O  
HETATM 4959  O   HOH A1025      14.391  -1.897   7.643  1.00 64.65           O  
HETATM 4960  O   HOH A1026       8.971 -32.046   6.366  1.00 64.84           O  
HETATM 4961  O   HOH A1027     -12.529 -17.445   5.350  1.00 68.40           O  
HETATM 4962  O   HOH A1028       6.667  20.310  59.921  1.00 68.74           O  
CONECT 4560 4561 4562
CONECT 4561 4560
CONECT 4562 4560 4563 4564
CONECT 4563 4562
CONECT 4564 4562 4565
CONECT 4565 4564
END



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