CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 23050411155191571

Job options:

ID        	=	 23050411155191571
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


CRYST1  119.732   81.866  133.198  90.00  92.92  90.00 P 1 21 1      1
ATOM      1  N   MET A   1     -14.832 -38.609 -33.786  1.00 86.12           N  
ANISOU    1  N   MET A   1    12015   9386  11321  -2145   1092  -1270       N  
ATOM      2  CA  MET A   1     -13.631 -37.829 -34.184  1.00 84.83           C  
ANISOU    2  CA  MET A   1    11787   9303  11141  -1977    945  -1212       C  
ATOM      3  C   MET A   1     -13.669 -36.473 -33.459  1.00 79.16           C  
ANISOU    3  C   MET A   1    11018   8658  10401  -1922    926  -1132       C  
ATOM      4  O   MET A   1     -14.545 -35.642 -33.722  1.00 76.91           O  
ANISOU    4  O   MET A   1    10561   8512  10150  -1970    951  -1158       O  
ATOM      5  CB  MET A   1     -13.539 -37.665 -35.704  1.00 88.08           C  
ANISOU    5  CB  MET A   1    12005   9871  11592  -1959    874  -1283       C  
ATOM      6  CG  MET A   1     -12.202 -37.105 -36.162  1.00 92.59           C  
ANISOU    6  CG  MET A   1    12540  10491  12147  -1807    753  -1246       C  
ATOM      7  SD  MET A   1     -11.555 -37.858 -37.697  1.00105.04           S  
ANISOU    7  SD  MET A   1    14059  12102  13750  -1795    704  -1343       S  
ATOM      8  CE  MET A   1     -12.059 -36.677 -38.954  1.00100.93           C  
ANISOU    8  CE  MET A   1    13317  11812  13219  -1811    654  -1377       C  
ATOM      9  N   LEU A   2     -12.736 -36.310 -32.527  1.00 75.54           N  
ANISOU    9  N   LEU A   2    10717   8093   9893  -1820    877  -1043       N  
ATOM     10  CA  LEU A   2     -12.708 -35.294 -31.446  1.00 71.16           C  
ANISOU   10  CA  LEU A   2    10203   7537   9297  -1778    879   -955       C  
ATOM     11  C   LEU A   2     -11.786 -34.158 -31.835  1.00 67.06           C  
ANISOU   11  C   LEU A   2     9554   7143   8783  -1631    752   -911       C  
ATOM     12  O   LEU A   2     -11.697 -33.198 -31.050  1.00 65.46           O  
ANISOU   12  O   LEU A   2     9361   6960   8552  -1584    741   -840       O  
ATOM     13  CB  LEU A   2     -12.124 -35.948 -30.193  1.00 72.13           C  
ANISOU   13  CB  LEU A   2    10619   7437   9351  -1749    880   -888       C  
ATOM     14  CG  LEU A   2     -13.058 -36.055 -28.995  1.00 73.27           C  
ANISOU   14  CG  LEU A   2    10926   7473   9441  -1877   1024   -864       C  
ATOM     15  CD1 LEU A   2     -14.240 -36.986 -29.286  1.00 74.54           C  
ANISOU   15  CD1 LEU A   2    11087   7601   9635  -2059   1177   -960       C  
ATOM     16  CD2 LEU A   2     -12.271 -36.517 -27.780  1.00 73.57           C  
ANISOU   16  CD2 LEU A   2    11281   7287   9385  -1817    980   -781       C  
ATOM     17  N   GLN A   3     -11.028 -34.357 -32.912  1.00 65.52           N  
ANISOU   17  N   GLN A   3     9273   7002   8618  -1564    670   -953       N  
ATOM     18  CA  GLN A   3      -9.986 -33.411 -33.390  1.00 63.16           C  
ANISOU   18  CA  GLN A   3     8866   6803   8327  -1431    562   -930       C  
ATOM     19  C   GLN A   3     -10.149 -33.205 -34.890  1.00 59.07           C  
ANISOU   19  C   GLN A   3     8168   6441   7837  -1457    543  -1004       C  
ATOM     20  O   GLN A   3     -10.462 -34.179 -35.593  1.00 59.12           O  
ANISOU   20  O   GLN A   3     8175   6424   7862  -1529    575  -1079       O  
ATOM     21  CB  GLN A   3      -8.574 -33.922 -33.114  1.00 64.67           C  
ANISOU   21  CB  GLN A   3     9176   6865   8530  -1309    474   -921       C  
ATOM     22  CG  GLN A   3      -8.225 -34.054 -31.642  1.00 66.32           C  
ANISOU   22  CG  GLN A   3     9592   6907   8700  -1257    450   -843       C  
ATOM     23  CD  GLN A   3      -7.234 -35.176 -31.461  1.00 67.45           C  
ANISOU   23  CD  GLN A   3     9891   6868   8867  -1182    374   -870       C  
ATOM     24  NE2 GLN A   3      -7.596 -36.345 -31.976  1.00 66.84           N  
ANISOU   24  NE2 GLN A   3     9859   6729   8807  -1261    423   -935       N  
ATOM     25  OE1 GLN A   3      -6.146 -34.976 -30.925  1.00 67.30           O  
ANISOU   25  OE1 GLN A   3     9937   6770   8864  -1049    264   -844       O  
ATOM     26  N   ARG A   4      -9.945 -31.963 -35.326  1.00 55.17           N  
ANISOU   26  N   ARG A   4     7542   6088   7334  -1403    493   -981       N  
ATOM     27  CA  ARG A   4     -10.090 -31.483 -36.722  1.00 52.99           C  
ANISOU   27  CA  ARG A   4     7116   5962   7055  -1423    462  -1036       C  
ATOM     28  C   ARG A   4      -9.071 -30.342 -36.858  1.00 49.03           C  
ANISOU   28  C   ARG A   4     6564   5530   6535  -1313    397   -995       C  
ATOM     29  O   ARG A   4      -9.043 -29.444 -36.000  1.00 46.55           O  
ANISOU   29  O   ARG A   4     6249   5229   6208  -1263    383   -920       O  
ATOM     30  CB  ARG A   4     -11.560 -31.130 -36.992  1.00 54.61           C  
ANISOU   30  CB  ARG A   4     7221   6264   7266  -1524    492  -1059       C  
ATOM     31  CG  ARG A   4     -12.018 -31.211 -38.444  1.00 56.83           C  
ANISOU   31  CG  ARG A   4     7400   6649   7544  -1582    459  -1141       C  
ATOM     32  CD  ARG A   4     -12.330 -32.563 -39.099  1.00 60.05           C  
ANISOU   32  CD  ARG A   4     7840   7003   7974  -1669    496  -1232       C  
ATOM     33  NE  ARG A   4     -13.055 -33.565 -38.312  1.00 64.08           N  
ANISOU   33  NE  ARG A   4     8422   7401   8523  -1753    585  -1252       N  
ATOM     34  CZ  ARG A   4     -14.395 -33.689 -38.189  1.00 66.76           C  
ANISOU   34  CZ  ARG A   4     8698   7762   8904  -1859    636  -1299       C  
ATOM     35  NH1 ARG A   4     -14.904 -34.669 -37.456  1.00 67.20           N1+
ANISOU   35  NH1 ARG A   4     8847   7698   8989  -1944    739  -1323       N1+
ATOM     36  NH2 ARG A   4     -15.228 -32.842 -38.775  1.00 67.83           N  
ANISOU   36  NH2 ARG A   4     8684   8030   9059  -1883    585  -1331       N  
ATOM     37  N   ASP A   5      -8.186 -30.448 -37.851  1.00 46.96           N  
ANISOU   37  N   ASP A   5     6273   5295   6275  -1281    370  -1052       N  
ATOM     38  CA  ASP A   5      -7.220 -29.397 -38.260  1.00 44.32           C  
ANISOU   38  CA  ASP A   5     5881   5035   5926  -1203    330  -1043       C  
ATOM     39  C   ASP A   5      -7.977 -28.356 -39.076  1.00 18.68           C  
ATOM     40  O   ASP A   5      -8.050 -28.491 -40.287  1.00 42.76           O  
ANISOU   40  O   ASP A   5     5564   5043   5639  -1301    307  -1098       O  
ATOM     41  CB  ASP A   5      -6.087 -29.991 -39.089  1.00 44.90           C  
ANISOU   41  CB  ASP A   5     5961   5071   6029  -1178    334  -1132       C  
ATOM     42  CG  ASP A   5      -5.076 -28.983 -39.593  1.00 44.39           C  
ANISOU   42  CG  ASP A   5     5838   5074   5954  -1120    321  -1148       C  
ATOM     43  OD1 ASP A   5      -5.190 -27.786 -39.266  1.00 43.44           O  
ANISOU   43  OD1 ASP A   5     5680   5026   5798  -1088    298  -1078       O  
ATOM     44  OD2 ASP A   5      -4.213 -29.408 -40.345  1.00 44.65           O1-
ANISOU   44  OD2 ASP A   5     5865   5084   6018  -1116    345  -1239       O1-
ATOM     45  N   PHE A   6      -8.523 -27.345 -38.415  1.00 40.98           N  
ANISOU   45  N   PHE A   6     5328   4814   5430  -1230    291   -959       N  
ATOM     46  CA  PHE A   6      -9.451 -26.374 -39.037  1.00 40.29           C  
ANISOU   46  CA  PHE A   6     5155   4851   5301  -1269    253   -949       C  
ATOM     47  C   PHE A   6      -8.750 -25.750 -40.238  1.00 39.53           C  
ANISOU   47  C   PHE A   6     5046   4828   5144  -1255    220   -978       C  
ATOM     48  O   PHE A   6      -9.361 -25.593 -41.286  1.00 39.50           O  
ANISOU   48  O   PHE A   6     5020   4894   5094  -1313    183  -1017       O  
ATOM     49  CB  PHE A   6      -9.906 -25.333 -38.016  1.00 39.71           C  
ANISOU   49  CB  PHE A   6     5047   4807   5235  -1231    241   -866       C  
ATOM     50  CG  PHE A   6     -10.837 -25.897 -36.979  1.00 40.19           C  
ANISOU   50  CG  PHE A   6     5125   4801   5342  -1279    294   -854       C  
ATOM     51  CD1 PHE A   6     -10.327 -26.484 -35.839  1.00 40.29           C  
ANISOU   51  CD1 PHE A   6     5243   4693   5373  -1249    338   -818       C  
ATOM     52  CD2 PHE A   6     -12.207 -25.934 -37.184  1.00 41.16           C  
ANISOU   52  CD2 PHE A   6     5174   4970   5495  -1363    300   -894       C  
ATOM     53  CE1 PHE A   6     -11.169 -27.050 -34.901  1.00 40.91           C  
ANISOU   53  CE1 PHE A   6     5373   4695   5478  -1313    406   -812       C  
ATOM     54  CE2 PHE A   6     -13.050 -26.515 -36.253  1.00 41.77           C  
ANISOU   54  CE2 PHE A   6     5271   4977   5622  -1428    378   -903       C  
ATOM     55  CZ  PHE A   6     -12.529 -27.060 -35.110  1.00 41.85           C  
ANISOU   55  CZ  PHE A   6     5407   4864   5628  -1409    440   -858       C  
ATOM     56  N   ILE A   7      -7.475 -25.428 -40.070  1.00 38.69           N  
ANISOU   56  N   ILE A   7     4964   4696   5041  -1183    234   -969       N  
ATOM     57  CA  ILE A   7      -6.722 -24.570 -41.026  1.00 38.19           C  
ANISOU   57  CA  ILE A   7     4896   4698   4917  -1172    227   -991       C  
ATOM     58  C   ILE A   7      -6.415 -25.373 -42.285  1.00 38.75           C  
ANISOU   58  C   ILE A   7     5001   4760   4961  -1240    259  -1092       C  
ATOM     59  O   ILE A   7      -6.250 -24.747 -43.331  1.00 39.07           O  
ANISOU   59  O   ILE A   7     5062   4863   4919  -1275    253  -1119       O  
ATOM     60  CB  ILE A   7      -5.456 -23.994 -40.368  1.00 37.59           C  
ANISOU   60  CB  ILE A   7     4818   4590   4876  -1080    245   -969       C  
ATOM     61  CG1 ILE A   7      -5.787 -23.208 -39.099  1.00 36.61           C  
ANISOU   61  CG1 ILE A   7     4671   4470   4768  -1018    214   -868       C  
ATOM     62  CG2 ILE A   7      -4.639 -23.168 -41.348  1.00 37.46           C  
ANISOU   62  CG2 ILE A   7     4805   4628   4802  -1087    267  -1008       C  
ATOM     63  CD1 ILE A   7      -6.811 -22.144 -39.274  1.00 36.23           C  
ANISOU   63  CD1 ILE A   7     4585   4520   4662  -1042    170   -811       C  
ATOM     64  N   THR A   8      -6.364 -26.696 -42.194  1.00 39.17           N  
ANISOU   64  N   THR A   8     5078   4733   5073  -1262    292  -1147       N  
ATOM     65  CA  THR A   8      -6.230 -27.583 -43.374  1.00 40.14           C  
ANISOU   65  CA  THR A   8     5234   4844   5175  -1337    325  -1249       C  
ATOM     66  C   THR A   8      -7.619 -27.941 -43.904  1.00 40.51           C  
ANISOU   66  C   THR A   8     5276   4934   5181  -1424    286  -1259       C  
ATOM     67  O   THR A   8      -7.801 -27.944 -45.126  1.00 41.34           O  
ANISOU   67  O   THR A   8     5411   5086   5212  -1492    274  -1316       O  
ATOM     68  CB  THR A   8      -5.424 -28.832 -43.028  1.00 40.57           C  
ANISOU   68  CB  THR A   8     5311   4779   5323  -1311    374  -1314       C  
ATOM     69  CG2 THR A   8      -5.408 -29.856 -44.141  1.00 41.72           C  
ANISOU   69  CG2 THR A   8     5488   4904   5458  -1393    415  -1421       C  
ATOM     70  OG1 THR A   8      -4.111 -28.358 -42.755  1.00 40.17           O  
ANISOU   70  OG1 THR A   8     5246   4700   5317  -1231    396  -1331       O  
ATOM     71  N   ALA A   9      -8.549 -28.239 -43.009  1.00 40.19           N  
ANISOU   71  N   ALA A   9     5207   4872   5191  -1427    269  -1215       N  
ATOM     72  CA  ALA A   9      -9.855 -28.839 -43.344  1.00 41.24           C  
ANISOU   72  CA  ALA A   9     5319   5022   5329  -1513    247  -1251       C  
ATOM     73  C   ALA A   9     -10.680 -27.842 -44.152  1.00 41.27           C  
ANISOU   73  C   ALA A   9     5284   5135   5261  -1542    158  -1246       C  
ATOM     74  O   ALA A   9     -11.436 -28.276 -45.030  1.00 42.80           O  
ANISOU   74  O   ALA A   9     5475   5355   5432  -1616    118  -1310       O  
ATOM     75  CB  ALA A   9     -10.575 -29.261 -42.085  1.00 41.23           C  
ANISOU   75  CB  ALA A   9     5298   4963   5403  -1514    274  -1212       C  
ATOM     76  N   LEU A  10     -10.547 -26.554 -43.863  1.00 40.15           N  
ANISOU   76  N   LEU A  10     5120   5048   5087  -1482    117  -1174       N  
ATOM     77  CA  LEU A  10     -11.363 -25.515 -44.525  1.00 40.03           C  
ANISOU   77  CA  LEU A  10     5079   5122   5009  -1494      9  -1162       C  
ATOM     78  C   LEU A  10     -10.895 -25.341 -45.959  1.00 40.49           C  
ANISOU   78  C   LEU A  10     5227   5209   4949  -1533    -21  -1209       C  
ATOM     79  O   LEU A  10     -11.722 -25.384 -46.848  1.00 41.05           O  
ANISOU   79  O   LEU A  10     5311   5314   4974  -1588   -108  -1254       O  
ATOM     80  CB  LEU A  10     -11.293 -24.230 -43.703  1.00 39.06           C  
ANISOU   80  CB  LEU A  10     4917   5034   4891  -1416    -17  -1070       C  
ATOM     81  CG  LEU A  10     -12.083 -24.315 -42.402  1.00 38.70           C  
ANISOU   81  CG  LEU A  10     4789   4966   4948  -1401      4  -1034       C  
ATOM     82  CD1 LEU A  10     -11.658 -23.236 -41.435  1.00 37.65           C  
ANISOU   82  CD1 LEU A  10     4639   4845   4822  -1319     12   -944       C  
ATOM     83  CD2 LEU A  10     -13.570 -24.212 -42.663  1.00 39.37           C  
ANISOU   83  CD2 LEU A  10     4789   5096   5074  -1449    -76  -1078       C  
ATOM     84  N   PRO A  11      -9.593 -25.133 -46.247  1.00 40.35           N  
ANISOU   84  N   PRO A  11     5279   5173   4881  -1514     48  -1212       N  
ATOM     85  CA  PRO A  11      -9.115 -25.130 -47.623  1.00 41.52           C  
ANISOU   85  CA  PRO A  11     5534   5330   4913  -1577     55  -1276       C  
ATOM     86  C   PRO A  11      -9.541 -26.362 -48.428  1.00 43.46           C  
ANISOU   86  C   PRO A  11     5810   5550   5153  -1662     59  -1369       C  
ATOM     87  O   PRO A  11      -9.811 -26.238 -49.581  1.00 44.02           O  
ANISOU   87  O   PRO A  11     5966   5646   5114  -1725      5  -1411       O  
ATOM     88  CB  PRO A  11      -7.598 -25.116 -47.434  1.00 40.87           C  
ANISOU   88  CB  PRO A  11     5477   5204   4847  -1545    176  -1293       C  
ATOM     89  CG  PRO A  11      -7.404 -24.346 -46.172  1.00 39.37           C  
ANISOU   89  CG  PRO A  11     5215   5020   4723  -1450    171  -1202       C  
ATOM     90  CD  PRO A  11      -8.537 -24.784 -45.291  1.00 39.10           C  
ANISOU   90  CD  PRO A  11     5102   4982   4773  -1436    121  -1163       C  
ATOM     91  N   GLU A  12      -9.577 -27.523 -47.790  1.00 45.65           N  
ANISOU   91  N   GLU A  12     6033   5770   5541  -1664    120  -1398       N  
ATOM     92  CA  GLU A  12      -9.980 -28.805 -48.432  1.00 48.87           C  
ANISOU   92  CA  GLU A  12     6462   6144   5961  -1745    136  -1489       C  
ATOM     93  C   GLU A  12     -11.458 -28.733 -48.829  1.00 20.46           C  
ATOM     94  O   GLU A  12     -11.866 -29.454 -49.750  1.00 50.53           O  
ANISOU   94  O   GLU A  12     6679   6400   6120  -1870    -11  -1584       O  
ATOM     95  CB  GLU A  12      -9.756 -29.980 -47.479  1.00 50.76           C  
ANISOU   95  CB  GLU A  12     6660   6298   6329  -1728    220  -1504       C  
ATOM     96  CG  GLU A  12      -8.402 -30.646 -47.639  1.00 52.62           C  
ANISOU   96  CG  GLU A  12     6943   6461   6590  -1716    324  -1562       C  
ATOM     97  CD  GLU A  12      -8.080 -31.615 -46.516  1.00 54.60           C  
ANISOU   97  CD  GLU A  12     7170   6610   6965  -1670    379  -1557       C  
ATOM     98  OE1 GLU A  12      -8.888 -31.691 -45.530  1.00 55.37           O  
ANISOU   98  OE1 GLU A  12     7230   6694   7115  -1654    354  -1496       O  
ATOM     99  OE2 GLU A  12      -7.031 -32.300 -46.625  1.00 57.11           O1-
ANISOU   99  OE2 GLU A  12     7516   6854   7330  -1653    447  -1621       O1-
ATOM    100  N   GLN A  13     -12.213 -27.902 -48.117  1.00 48.59           N  
ANISOU  100  N   GLN A  13     6313   6201   5949  -1745    -60  -1436       N  
ATOM    101  CA  GLN A  13     -13.643 -27.613 -48.358  1.00 48.61           C  
ANISOU  101  CA  GLN A  13     6249   6252   5968  -1769   -194  -1457       C  
ATOM    102  C   GLN A  13     -13.784 -26.463 -49.378  1.00 48.61           C  
ANISOU  102  C   GLN A  13     6327   6309   5835  -1762   -331  -1444       C  
ATOM    103  O   GLN A  13     -14.914 -26.067 -49.674  1.00 49.63           O  
ANISOU  103  O   GLN A  13     6408   6475   5975  -1766   -476  -1466       O  
ATOM    104  CB  GLN A  13     -14.245 -27.241 -47.002  1.00 47.99           C  
ANISOU  104  CB  GLN A  13     6048   6177   6010  -1719   -184  -1401       C  
ATOM    105  CG  GLN A  13     -15.695 -27.629 -46.830  1.00 48.66           C  
ANISOU  105  CG  GLN A  13     6018   6271   6197  -1766   -242  -1464       C  
ATOM    106  CD  GLN A  13     -15.819 -29.109 -46.582  1.00 48.81           C  
ANISOU  106  CD  GLN A  13     6031   6224   6292  -1836   -134  -1530       C  
ATOM    107  NE2 GLN A  13     -14.823 -29.670 -45.906  1.00 47.93           N  
ANISOU  107  NE2 GLN A  13     5977   6044   6192  -1815     -5  -1490       N  
ATOM    108  OE1 GLN A  13     -16.786 -29.734 -47.009  1.00 49.29           O  
ANISOU  108  OE1 GLN A  13     6039   6286   6403  -1906   -176  -1620       O  
ATOM    109  N   GLY A  14     -12.678 -25.920 -49.889  1.00 47.42           N  
ANISOU  109  N   GLY A  14     6297   6157   5565  -1752   -289  -1416       N  
ATOM    110  CA  GLY A  14     -12.676 -24.698 -50.720  1.00 46.91           C  
ANISOU  110  CA  GLY A  14     6341   6128   5354  -1743   -402  -1384       C  
ATOM    111  C   GLY A  14     -12.860 -23.414 -49.912  1.00 44.88           C  
ANISOU  111  C   GLY A  14     6021   5907   5125  -1654   -459  -1290       C  
ATOM    112  O   GLY A  14     -13.100 -22.356 -50.523  1.00 45.07           O  
ANISOU  112  O   GLY A  14     6129   5956   5040  -1639   -584  -1261       O  
ATOM    113  N   LEU A  15     -12.732 -23.479 -48.591  1.00 42.82           N  
ANISOU  113  N   LEU A  15     5636   5640   4994  -1599   -376  -1242       N  
ATOM    114  CA  LEU A  15     -13.136 -22.380 -47.683  1.00 42.03           C  
ANISOU  114  CA  LEU A  15     5449   5573   4947  -1519   -430  -1163       C  
ATOM    115  C   LEU A  15     -11.902 -21.756 -47.044  1.00 40.79           C  
ANISOU  115  C   LEU A  15     5321   5406   4770  -1463   -324  -1089       C  
ATOM    116  O   LEU A  15     -11.947 -21.421 -45.864  1.00 39.85           O  
ANISOU  116  O   LEU A  15     5110   5289   4743  -1403   -291  -1031       O  
ATOM    117  CB  LEU A  15     -14.102 -22.936 -46.637  1.00 41.97           C  
ANISOU  117  CB  LEU A  15     5284   5560   5104  -1513   -418  -1178       C  
ATOM    118  CG  LEU A  15     -15.423 -23.485 -47.190  1.00 43.15           C  
ANISOU  118  CG  LEU A  15     5371   5721   5305  -1569   -527  -1269       C  
ATOM    119  CD1 LEU A  15     -16.360 -23.869 -46.068  1.00 43.18           C  
ANISOU  119  CD1 LEU A  15     5214   5715   5478  -1572   -487  -1292       C  
ATOM    120  CD2 LEU A  15     -16.109 -22.488 -48.105  1.00 43.80           C  
ANISOU  120  CD2 LEU A  15     5487   5845   5312  -1550   -726  -1280       C  
ATOM    121  N   ASP A  16     -10.869 -21.549 -47.849  1.00 41.03           N  
ANISOU  121  N   ASP A  16     5481   5424   4683  -1488   -273  -1100       N  
ATOM    122  CA  ASP A  16      -9.618 -20.845 -47.466  1.00 40.10           C  
ANISOU  122  CA  ASP A  16     5399   5298   4539  -1444   -176  -1053       C  
ATOM    123  C   ASP A  16      -9.907 -19.591 -46.632  1.00 14.44           C  
ATOM    124  O   ASP A  16      -9.292 -19.417 -45.587  1.00 37.14           O  
ANISOU  124  O   ASP A  16     4901   4946   4263  -1305   -157   -915       O  
ATOM    125  CB  ASP A  16      -8.835 -20.482 -48.721  1.00 41.19           C  
ANISOU  125  CB  ASP A  16     5703   5428   4520  -1505   -146  -1090       C  
ATOM    126  CG  ASP A  16      -8.272 -21.690 -49.451  1.00 42.30           C  
ANISOU  126  CG  ASP A  16     5900   5525   4646  -1585    -46  -1191       C  
ATOM    127  OD1 ASP A  16      -9.100 -22.528 -49.973  1.00 43.34           O  
ANISOU  127  OD1 ASP A  16     6036   5655   4777  -1637   -108  -1242       O  
ATOM    128  OD2 ASP A  16      -7.006 -21.784 -49.496  1.00 42.58           O1-
ANISOU  128  OD2 ASP A  16     5967   5526   4683  -1596     93  -1229       O1-
ATOM    129  N   HIS A  17     -10.790 -18.719 -47.097  1.00 40.12           N  
ANISOU  129  N   HIS A  17     5368   5373   4503  -1355   -382   -934       N  
ATOM    130  CA  HIS A  17     -11.020 -17.372 -46.491  1.00 39.93           C  
ANISOU  130  CA  HIS A  17     5309   5380   4483  -1280   -449   -850       C  
ATOM    131  C   HIS A  17     -11.399 -17.523 -45.024  1.00 38.59           C  
ANISOU  131  C   HIS A  17     4976   5215   4473  -1222   -410   -814       C  
ATOM    132  O   HIS A  17     -10.986 -16.675 -44.239  1.00 37.87           O  
ANISOU  132  O   HIS A  17     4856   5132   4401  -1160   -380   -746       O  
ATOM    133  CB  HIS A  17     -12.099 -16.559 -47.236  1.00 41.51           C  
ANISOU  133  CB  HIS A  17     5553   5604   4614  -1273   -645   -846       C  
ATOM    134  CG  HIS A  17     -13.439 -17.213 -47.272  1.00 42.85           C  
ANISOU  134  CG  HIS A  17     5616   5784   4879  -1287   -754   -906       C  
ATOM    135  CD2 HIS A  17     -14.539 -17.039 -46.508  1.00 43.46           C  
ANISOU  135  CD2 HIS A  17     5533   5882   5096  -1245   -828   -910       C  
ATOM    136  ND1 HIS A  17     -13.753 -18.193 -48.197  1.00 44.65           N  
ANISOU  136  ND1 HIS A  17     5897   5997   5073  -1361   -786   -989       N  
ATOM    137  CE1 HIS A  17     -15.002 -18.578 -48.016  1.00 45.70           C  
ANISOU  137  CE1 HIS A  17     5901   6142   5322  -1361   -884  -1042       C  
ATOM    138  NE2 HIS A  17     -15.507 -17.900 -46.960  1.00 44.74           N  
ANISOU  138  NE2 HIS A  17     5640   6041   5317  -1292   -903  -1000       N  
ATOM    139  N   ILE A  18     -12.158 -18.561 -44.682  1.00 38.31           N  
ANISOU  139  N   ILE A  18     4848   5166   4540  -1250   -402   -863       N  
ATOM    140  CA  ILE A  18     -12.610 -18.838 -43.292  1.00 37.30           C  
ANISOU  140  CA  ILE A  18     4591   5026   4555  -1220   -347   -840       C  
ATOM    141  C   ILE A  18     -11.373 -19.066 -42.429  1.00 35.77           C  
ANISOU  141  C   ILE A  18     4420   4790   4380  -1185   -211   -798       C  
ATOM    142  O   ILE A  18     -11.216 -18.377 -41.415  1.00 34.57           O  
ANISOU  142  O   ILE A  18     4227   4641   4268  -1125   -188   -733       O  
ATOM    143  CB  ILE A  18     -13.527 -20.068 -43.241  1.00 38.54           C  
ANISOU  143  CB  ILE A  18     4680   5160   4802  -1282   -337   -917       C  
ATOM    144  CG1 ILE A  18     -14.650 -20.064 -44.287  1.00 40.14           C  
ANISOU  144  CG1 ILE A  18     4864   5395   4991  -1323   -483   -989       C  
ATOM    145  CG2 ILE A  18     -14.028 -20.261 -41.825  1.00 38.04           C  
ANISOU  145  CG2 ILE A  18     4513   5074   4867  -1268   -266   -898       C  
ATOM    146  CD1 ILE A  18     -15.749 -19.094 -44.036  1.00 40.75           C  
ANISOU  146  CD1 ILE A  18     4839   5510   5133  -1282   -607   -986       C  
ATOM    147  N   ALA A  19     -10.518 -20.004 -42.839  1.00 35.59           N  
ANISOU  147  N   ALA A  19     4461   4726   4336  -1219   -132   -843       N  
ATOM    148  CA  ALA A  19      -9.247 -20.332 -42.166  1.00 35.10           C  
ANISOU  148  CA  ALA A  19     4421   4610   4305  -1180    -24   -829       C  
ATOM    149  C   ALA A  19      -8.431 -19.052 -41.960  1.00 34.93           C  
ANISOU  149  C   ALA A  19     4420   4614   4239  -1119    -21   -770       C  
ATOM    150  O   ALA A  19      -7.865 -18.861 -40.882  1.00 34.16           O  
ANISOU  150  O   ALA A  19     4293   4487   4199  -1057     24   -726       O  
ATOM    151  CB  ALA A  19      -8.516 -21.361 -42.968  1.00 35.35           C  
ANISOU  151  CB  ALA A  19     4516   4600   4315  -1229     36   -909       C  
ATOM    152  N   GLU A  20      -8.408 -18.185 -42.965  1.00 36.07           N  
ANISOU  152  N   GLU A  20     4625   4803   4276  -1139    -72   -769       N  
ATOM    153  CA  GLU A  20      -7.699 -16.884 -42.912  1.00 36.43           C  
ANISOU  153  CA  GLU A  20     4706   4872   4265  -1095    -67   -718       C  
ATOM    154  C   GLU A  20      -8.309 -16.037 -41.794  1.00 16.07           C  
ATOM    155  O   GLU A  20      -7.544 -15.516 -40.995  1.00 35.61           O  
ANISOU  155  O   GLU A  20     4501   4781   4246   -969    -66   -594       O  
ATOM    156  CB  GLU A  20      -7.791 -16.162 -44.261  1.00 37.97           C  
ANISOU  156  CB  GLU A  20     5017   5096   4315  -1145   -126   -732       C  
ATOM    157  CG  GLU A  20      -6.992 -16.832 -45.368  1.00 38.98           C  
ANISOU  157  CG  GLU A  20     5249   5193   4370  -1223    -47   -818       C  
ATOM    158  CD  GLU A  20      -7.176 -16.367 -46.817  1.00 40.28           C  
ANISOU  158  CD  GLU A  20     5573   5367   4366  -1298   -103   -844       C  
ATOM    159  OE1 GLU A  20      -6.634 -17.080 -47.723  1.00 40.18           O  
ANISOU  159  OE1 GLU A  20     5647   5324   4296  -1377    -28   -927       O  
ATOM    160  OE2 GLU A  20      -7.818 -15.291 -47.057  1.00 40.46           O1-
ANISOU  160  OE2 GLU A  20     5647   5417   4309  -1279   -221   -786       O1-
ATOM    161  N   ASN A  21      -9.634 -15.912 -41.755  1.00 37.42           N  
ANISOU  161  N   ASN A  21     4694   5051   4471  -1032   -210   -626       N  
ATOM    162  CA  ASN A  21     -10.380 -15.154 -40.712  1.00 37.99           C  
ANISOU  162  CA  ASN A  21     4674   5145   4614   -977   -250   -566       C  
ATOM    163  C   ASN A  21      -9.967 -15.683 -39.337  1.00 36.68           C  
ANISOU  163  C   ASN A  21     4462   4934   4541   -946   -150   -541       C  
ATOM    164  O   ASN A  21      -9.635 -14.857 -38.439  1.00 35.73           O  
ANISOU  164  O   ASN A  21     4321   4816   4439   -886   -132   -478       O  
ATOM    165  CB  ASN A  21     -11.907 -15.251 -40.840  1.00 40.31           C  
ANISOU  165  CB  ASN A  21     4889   5464   4964  -1000   -349   -599       C  
ATOM    166  CG  ASN A  21     -12.432 -14.799 -42.188  1.00 42.87           C  
ANISOU  166  CG  ASN A  21     5272   5818   5199  -1023   -486   -630       C  
ATOM    167  ND2 ASN A  21     -13.608 -15.275 -42.584  1.00 44.55           N  
ANISOU  167  ND2 ASN A  21     5425   6039   5464  -1058   -575   -695       N  
ATOM    168  OD1 ASN A  21     -11.743 -14.075 -42.904  1.00 44.87           O  
ANISOU  168  OD1 ASN A  21     5638   6078   5333  -1016   -509   -603       O  
ATOM    169  N   ILE A  22      -9.953 -17.005 -39.165  1.00 35.75           N  
ANISOU  169  N   ILE A  22     4345   4766   4472   -985    -92   -588       N  
ATOM    170  CA  ILE A  22      -9.535 -17.594 -37.869  1.00 34.44           C  
ANISOU  170  CA  ILE A  22     4175   4533   4377   -956    -10   -564       C  
ATOM    171  C   ILE A  22      -8.166 -17.021 -37.519  1.00 33.44           C  
ANISOU  171  C   ILE A  22     4087   4389   4229   -888     22   -527       C  
ATOM    172  O   ILE A  22      -8.046 -16.407 -36.469  1.00 32.45           O  
ANISOU  172  O   ILE A  22     3945   4255   4131   -835     31   -468       O  
ATOM    173  CB  ILE A  22      -9.536 -19.123 -37.928  1.00 34.89           C  
ANISOU  173  CB  ILE A  22     4261   4524   4471  -1007     40   -624       C  
ATOM    174  CG1 ILE A  22     -10.970 -19.650 -37.892  1.00 35.68           C  
ANISOU  174  CG1 ILE A  22     4306   4631   4621  -1074     27   -660       C  
ATOM    175  CG2 ILE A  22      -8.706 -19.692 -36.795  1.00 34.45           C  
ANISOU  175  CG2 ILE A  22     4251   4378   4460   -963    104   -600       C  
ATOM    176  CD1 ILE A  22     -11.120 -21.102 -38.271  1.00 36.38           C  
ANISOU  176  CD1 ILE A  22     4425   4667   4733  -1142     66   -731       C  
ATOM    177  N   LEU A  23      -7.183 -17.160 -38.409  1.00 33.53           N  
ANISOU  177  N   LEU A  23     4146   4397   4196   -897     43   -573       N  
ATOM    178  CA  LEU A  23      -5.793 -16.766 -38.105  1.00 32.97           C  
ANISOU  178  CA  LEU A  23     4094   4299   4133   -839     86   -571       C  
ATOM    179  C   LEU A  23      -5.690 -15.259 -37.896  1.00 32.58           C  
ANISOU  179  C   LEU A  23     4031   4304   4044   -796     60   -506       C  
ATOM    180  O   LEU A  23      -4.801 -14.821 -37.162  1.00 31.51           O  
ANISOU  180  O   LEU A  23     3887   4144   3942   -735     86   -486       O  
ATOM    181  CB  LEU A  23      -4.927 -17.234 -39.260  1.00 33.68           C  
ANISOU  181  CB  LEU A  23     4227   4377   4191   -881    130   -658       C  
ATOM    182  CG  LEU A  23      -4.743 -18.741 -39.309  1.00 34.35           C  
ANISOU  182  CG  LEU A  23     4324   4392   4335   -906    164   -727       C  
ATOM    183  CD1 LEU A  23      -4.172 -19.197 -40.643  1.00 35.03           C  
ANISOU  183  CD1 LEU A  23     4452   4478   4379   -971    210   -824       C  
ATOM    184  CD2 LEU A  23      -3.821 -19.154 -38.181  1.00 34.27           C  
ANISOU  184  CD2 LEU A  23     4303   4298   4419   -828    186   -729       C  
ATOM    185  N   SER A  24      -6.585 -14.499 -38.520  1.00 33.62           N  
ANISOU  185  N   SER A  24     4162   4499   4112   -824     -2   -481       N  
ATOM    186  CA  SER A  24      -6.611 -13.014 -38.474  1.00 33.76           C  
ANISOU  186  CA  SER A  24     4181   4565   4081   -787    -41   -421       C  
ATOM    187  C   SER A  24      -6.816 -12.493 -37.047  1.00 33.45           C  
ANISOU  187  C   SER A  24     4081   4519   4109   -721    -41   -352       C  
ATOM    188  O   SER A  24      -6.678 -11.303 -36.853  1.00 32.97           O  
ANISOU  188  O   SER A  24     4017   4489   4021   -683    -61   -303       O  
ATOM    189  CB  SER A  24      -7.692 -12.515 -39.339  1.00 34.29           C  
ANISOU  189  CB  SER A  24     4263   4680   4084   -822   -134   -415       C  
ATOM    190  OG  SER A  24      -8.921 -12.779 -38.701  1.00 34.20           O  
ANISOU  190  OG  SER A  24     4170   4676   4149   -818   -180   -402       O  
ATOM    191  N   TYR A  25      -7.227 -13.345 -36.109  1.00 34.25           N  
ANISOU  191  N   TYR A  25     4151   4578   4286   -718    -18   -349       N  
ATOM    192  CA  TYR A  25      -7.456 -12.977 -34.683  1.00 34.36           C  
ANISOU  192  CA  TYR A  25     4134   4570   4353   -670     -5   -289       C  
ATOM    193  C   TYR A  25      -6.152 -13.028 -33.889  1.00 33.24           C  
ANISOU  193  C   TYR A  25     4026   4371   4234   -609     35   -277       C  
ATOM    194  O   TYR A  25      -6.091 -12.366 -32.868  1.00 32.04           O  
ANISOU  194  O   TYR A  25     3866   4210   4099   -561     36   -222       O  
ATOM    195  CB  TYR A  25      -8.473 -13.910 -34.028  1.00 35.34           C  
ANISOU  195  CB  TYR A  25     4238   4655   4534   -711     17   -300       C  
ATOM    196  CG  TYR A  25      -9.874 -13.697 -34.518  1.00 36.89           C  
ANISOU  196  CG  TYR A  25     4367   4904   4744   -759    -29   -322       C  
ATOM    197  CD1 TYR A  25     -10.495 -12.478 -34.319  1.00 37.57           C  
ANISOU  197  CD1 TYR A  25     4395   5042   4838   -731    -75   -286       C  
ATOM    198  CD2 TYR A  25     -10.571 -14.690 -35.191  1.00 38.68           C  
ANISOU  198  CD2 TYR A  25     4581   5126   4988   -828    -37   -387       C  
ATOM    199  CE1 TYR A  25     -11.799 -12.252 -34.739  1.00 38.96           C  
ANISOU  199  CE1 TYR A  25     4492   5259   5051   -763   -137   -322       C  
ATOM    200  CE2 TYR A  25     -11.861 -14.472 -35.650  1.00 40.21           C  
ANISOU  200  CE2 TYR A  25     4699   5366   5215   -865    -97   -424       C  
ATOM    201  CZ  TYR A  25     -12.480 -13.253 -35.413  1.00 40.44           C  
ANISOU  201  CZ  TYR A  25     4660   5441   5264   -829   -153   -395       C  
ATOM    202  OH  TYR A  25     -13.751 -13.056 -35.860  1.00 42.22           O  
ANISOU  202  OH  TYR A  25     4796   5703   5544   -855   -230   -449       O  
ATOM    203  N   LEU A  26      -5.162 -13.774 -34.372  1.00 33.61           N  
ANISOU  203  N   LEU A  26     4105   4378   4289   -610     60   -337       N  
ATOM    204  CA  LEU A  26      -3.919 -14.073 -33.617  1.00 33.89           C  
ANISOU  204  CA  LEU A  26     4162   4337   4375   -546     78   -353       C  
ATOM    205  C   LEU A  26      -3.023 -12.830 -33.552  1.00 34.60           C  
ANISOU  205  C   LEU A  26     4230   4459   4456   -494     80   -339       C  
ATOM    206  O   LEU A  26      -2.955 -12.078 -34.543  1.00 34.69           O  
ANISOU  206  O   LEU A  26     4235   4535   4411   -526     91   -352       O  
ATOM    207  CB  LEU A  26      -3.171 -15.224 -34.282  1.00 33.89           C  
ANISOU  207  CB  LEU A  26     4184   4286   4408   -564    102   -444       C  
ATOM    208  CG  LEU A  26      -3.984 -16.494 -34.465  1.00 34.81           C  
ANISOU  208  CG  LEU A  26     4327   4368   4533   -622    106   -467       C  
ATOM    209  CD1 LEU A  26      -3.183 -17.559 -35.177  1.00 35.57           C  
ANISOU  209  CD1 LEU A  26     4441   4412   4663   -637    131   -564       C  
ATOM    210  CD2 LEU A  26      -4.449 -17.026 -33.134  1.00 35.19           C  
ANISOU  210  CD2 LEU A  26     4418   4340   4613   -600     97   -418       C  
ATOM    211  N   ASP A  27      -2.372 -12.644 -32.396  1.00 35.24           N  
ANISOU  211  N   ASP A  27     4317   4488   4586   -420     67   -315       N  
ATOM    212  CA  ASP A  27      -1.282 -11.680 -32.152  1.00 35.53           C  
ANISOU  212  CA  ASP A  27     4327   4530   4644   -361     69   -324       C  
ATOM    213  C   ASP A  27      -0.033 -12.215 -32.863  1.00 21.12           C  
ATOM    214  O   ASP A  27       0.060 -13.412 -33.076  1.00 35.80           O  
ANISOU  214  O   ASP A  27     4360   4472   4769   -372    101   -494       O  
ATOM    215  CB  ASP A  27      -1.093 -11.504 -30.647  1.00 36.28           C  
ANISOU  215  CB  ASP A  27     4445   4566   4776   -285     29   -270       C  
ATOM    216  CG  ASP A  27      -0.578 -12.771 -29.967  1.00 38.59           C  
ANISOU  216  CG  ASP A  27     4790   4740   5132   -243     -6   -308       C  
ATOM    217  OD1 ASP A  27      -1.096 -13.868 -30.320  1.00 39.28           O  
ANISOU  217  OD1 ASP A  27     4910   4798   5215   -291      4   -330       O  
ATOM    218  OD2 ASP A  27       0.361 -12.658 -29.099  1.00 40.70           O1-
ANISOU  218  OD2 ASP A  27     5071   4938   5454   -160    -54   -321       O1-
ATOM    219  N   ALA A  28       0.906 -11.343 -33.185  1.00 36.87           N  
ANISOU  219  N   ALA A  28     4442   4687   4881   -344    135   -482       N  
ATOM    220  CA  ALA A  28       2.175 -11.684 -33.854  1.00 39.37           C  
ANISOU  220  CA  ALA A  28     4721   4968   5269   -350    188   -616       C  
ATOM    221  C   ALA A  28       2.751 -12.997 -33.328  1.00 41.55           C  
ANISOU  221  C   ALA A  28     4990   5141   5658   -294    146   -686       C  
ATOM    222  O   ALA A  28       3.002 -13.878 -34.153  1.00 41.46           O  
ANISOU  222  O   ALA A  28     4974   5106   5674   -337    184   -777       O  
ATOM    223  CB  ALA A  28       3.157 -10.557 -33.673  1.00 39.57           C  
ANISOU  223  CB  ALA A  28     4699   5007   5330   -316    219   -650       C  
ATOM    224  N   ARG A  29       2.980 -13.107 -32.018  1.00 45.94           N  
ANISOU  224  N   ARG A  29     5556   5627   6271   -201     64   -650       N  
ATOM    225  CA  ARG A  29       3.713 -14.257 -31.414  1.00 50.23           C  
ANISOU  225  CA  ARG A  29     6109   6046   6929   -127     -6   -723       C  
ATOM    226  C   ARG A  29       3.014 -15.570 -31.790  1.00 48.60           C  
ANISOU  226  C   ARG A  29     5962   5803   6699   -176     -5   -725       C  
ATOM    227  O   ARG A  29       3.733 -16.551 -32.135  1.00 50.37           O  
ANISOU  227  O   ARG A  29     6167   5953   7017   -158    -12   -838       O  
ATOM    228  CB  ARG A  29       3.826 -14.182 -29.883  1.00 54.93           C  
ANISOU  228  CB  ARG A  29     6759   6561   7549    -27   -114   -657       C  
ATOM    229  CG  ARG A  29       4.889 -15.142 -29.338  1.00 60.55           C  
ANISOU  229  CG  ARG A  29     7477   7132   8395     71   -212   -758       C  
ATOM    230  CD  ARG A  29       4.802 -15.574 -27.874  1.00 65.24           C  
ANISOU  230  CD  ARG A  29     8196   7605   8988    158   -342   -688       C  
ATOM    231  NE  ARG A  29       5.592 -14.698 -27.008  1.00 69.02           N  
ANISOU  231  NE  ARG A  29     8650   8058   9518    250   -417   -694       N  
ATOM    232  CZ  ARG A  29       5.092 -13.773 -26.178  1.00 71.86           C  
ANISOU  232  CZ  ARG A  29     9060   8452   9791    257   -428   -579       C  
ATOM    233  NH1 ARG A  29       3.781 -13.610 -26.038  1.00 71.54           N1+
ANISOU  233  NH1 ARG A  29     9095   8467   9619    179   -368   -453       N1+
ATOM    234  NH2 ARG A  29       5.922 -13.021 -25.476  1.00 72.94           N  
ANISOU  234  NH2 ARG A  29     9165   8562   9986    342   -499   -604       N  
ATOM    235  N   SER A  30       1.676 -15.593 -31.702  1.00 44.92           N  
ANISOU  235  N   SER A  30     5557   5383   6129   -234      4   -616       N  
ATOM    236  CA  SER A  30       0.855 -16.793 -31.994  1.00 43.54           C  
ANISOU  236  CA  SER A  30     5440   5177   5927   -291     12   -611       C  
ATOM    237  C   SER A  30       0.866 -17.096 -33.499  1.00 41.79           C  
ANISOU  237  C   SER A  30     5176   5013   5690   -375     84   -694       C  
ATOM    238  O   SER A  30       0.982 -18.268 -33.878  1.00 41.63           O  
ANISOU  238  O   SER A  30     5175   4933   5709   -394     89   -762       O  
ATOM    239  CB  SER A  30      -0.538 -16.615 -31.454  1.00 43.58           C  
ANISOU  239  CB  SER A  30     5499   5214   5845   -335     12   -495       C  
ATOM    240  OG  SER A  30      -0.505 -16.316 -30.064  1.00 42.77           O  
ANISOU  240  OG  SER A  30     5455   5051   5746   -269    -40   -424       O  
ATOM    241  N   LEU A  31       0.772 -16.056 -34.322  1.00 40.62           N  
ANISOU  241  N   LEU A  31     4989   4968   5479   -425    137   -689       N  
ATOM    242  CA  LEU A  31       0.827 -16.156 -35.799  1.00 40.37           C  
ANISOU  242  CA  LEU A  31     4947   4988   5405   -514    210   -765       C  
ATOM    243  C   LEU A  31       2.133 -16.820 -36.233  1.00 41.39           C  
ANISOU  243  C   LEU A  31     5036   5050   5641   -499    252   -913       C  
ATOM    244  O   LEU A  31       2.084 -17.675 -37.153  1.00 43.54           O  
ANISOU  244  O   LEU A  31     5323   5312   5910   -564    297   -988       O  
ATOM    245  CB  LEU A  31       0.709 -14.763 -36.406  1.00 39.55           C  
ANISOU  245  CB  LEU A  31     4838   4979   5211   -554    247   -731       C  
ATOM    246  CG  LEU A  31       0.552 -14.731 -37.924  1.00 40.14           C  
ANISOU  246  CG  LEU A  31     4949   5103   5198   -660    312   -786       C  
ATOM    247  CD1 LEU A  31      -0.601 -15.588 -38.398  1.00 40.40           C  
ANISOU  247  CD1 LEU A  31     5025   5149   5178   -718    281   -762       C  
ATOM    248  CD2 LEU A  31       0.360 -13.304 -38.410  1.00 40.21           C  
ANISOU  248  CD2 LEU A  31     4990   5187   5101   -693    329   -735       C  
ATOM    249  N   CYS A  32       3.254 -16.453 -35.611  1.00 40.97           N  
ANISOU  249  N   CYS A  32     4926   4949   5689   -418    238   -966       N  
ATOM    250  CA  CYS A  32       4.593 -17.062 -35.856  1.00 42.08           C  
ANISOU  250  CA  CYS A  32     5000   5012   5977   -385    266  -1132       C  
ATOM    251  C   CYS A  32       4.550 -18.557 -35.551  1.00 41.93           C  
ANISOU  251  C   CYS A  32     5010   4890   6032   -348    203  -1169       C  
ATOM    252  O   CYS A  32       5.144 -19.325 -36.316  1.00 43.33           O  
ANISOU  252  O   CYS A  32     5152   5027   6284   -377    255  -1303       O  
ATOM    253  CB  CYS A  32       5.666 -16.440 -34.975  1.00 43.01           C  
ANISOU  253  CB  CYS A  32     5047   5085   6211   -283    222  -1175       C  
ATOM    254  SG  CYS A  32       6.065 -14.743 -35.453  1.00 45.05           S  
ANISOU  254  SG  CYS A  32     5259   5443   6414   -332    321  -1180       S  
ATOM    255  N   ALA A  33       3.915 -18.935 -34.441  1.00 40.44           N  
ANISOU  255  N   ALA A  33     4891   4649   5824   -290    103  -1060       N  
ATOM    256  CA  ALA A  33       3.759 -20.332 -33.997  1.00 40.34           C  
ANISOU  256  CA  ALA A  33     4945   4522   5859   -257     35  -1072       C  
ATOM    257  C   ALA A  33       2.967 -21.089 -35.055  1.00 40.18           C  
ANISOU  257  C   ALA A  33     4955   4541   5773   -367    106  -1086       C  
ATOM    258  O   ALA A  33       3.362 -22.200 -35.450  1.00 41.42           O  
ANISOU  258  O   ALA A  33     5111   4622   6005   -368    110  -1186       O  
ATOM    259  CB  ALA A  33       3.062 -20.360 -32.663  1.00 40.14           C  
ANISOU  259  CB  ALA A  33     5021   4446   5783   -207    -55   -937       C  
ATOM    260  N   ALA A  34       1.879 -20.487 -35.503  1.00 39.67           N  
ANISOU  260  N   ALA A  34     4910   4585   5576   -453    151   -994       N  
ATOM    261  CA  ALA A  34       0.975 -21.087 -36.499  1.00 40.39           C  
ANISOU  261  CA  ALA A  34     5033   4723   5591   -560    202   -999       C  
ATOM    262  C   ALA A  34       1.771 -21.418 -37.775  1.00 41.63           C  
ANISOU  262  C   ALA A  34     5147   4885   5784   -612    284  -1143       C  
ATOM    263  O   ALA A  34       1.567 -22.519 -38.322  1.00 41.14           O  
ANISOU  263  O   ALA A  34     5112   4786   5735   -658    303  -1201       O  
ATOM    264  CB  ALA A  34      -0.196 -20.168 -36.739  1.00 39.21           C  
ANISOU  264  CB  ALA A  34     4896   4687   5314   -623    212   -893       C  
ATOM    265  N   GLU A  35       2.666 -20.529 -38.218  1.00 43.02           N  
ANISOU  265  N   GLU A  35     5266   5099   5981   -613    342  -1209       N  
ATOM    266  CA  GLU A  35       3.499 -20.759 -39.433  1.00 45.50           C  
ANISOU  266  CA  GLU A  35     5546   5412   6331   -680    449  -1365       C  
ATOM    267  C   GLU A  35       4.204 -22.118 -39.312  1.00 23.68           C  
ATOM    268  O   GLU A  35       4.296 -22.821 -40.326  1.00 46.58           O  
ANISOU  268  O   GLU A  35     5659   5422   6617   -711    510  -1588       O  
ATOM    269  CB  GLU A  35       4.562 -19.671 -39.633  1.00 47.39           C  
ANISOU  269  CB  GLU A  35     5720   5675   6609   -674    521  -1440       C  
ATOM    270  CG  GLU A  35       4.052 -18.323 -40.118  1.00 47.60           C  
ANISOU  270  CG  GLU A  35     5794   5810   6481   -743    564  -1354       C  
ATOM    271  CD  GLU A  35       5.136 -17.273 -40.397  1.00 48.54           C  
ANISOU  271  CD  GLU A  35     5864   5944   6634   -757    660  -1440       C  
ATOM    272  OE1 GLU A  35       6.155 -17.248 -39.666  1.00 49.18           O  
ANISOU  272  OE1 GLU A  35     5848   5965   6872   -669    644  -1518       O  
ATOM    273  OE2 GLU A  35       4.950 -16.459 -41.345  1.00 49.34           O1-
ANISOU  273  OE2 GLU A  35     6035   6111   6602   -859    745  -1433       O1-
ATOM    274  N   LEU A  36       4.658 -22.471 -38.103  1.00 46.77           N  
ANISOU  274  N   LEU A  36     5655   5358   6757   -510    329  -1481       N  
ATOM    275  CA  LEU A  36       5.576 -23.608 -37.829  1.00 48.44           C  
ANISOU  275  CA  LEU A  36     5829   5433   7143   -431    283  -1613       C  
ATOM    276  C   LEU A  36       4.812 -24.924 -37.647  1.00 48.58           C  
ANISOU  276  C   LEU A  36     5939   5379   7139   -438    227  -1571       C  
ATOM    277  O   LEU A  36       5.491 -25.979 -37.568  1.00 49.65           O  
ANISOU  277  O   LEU A  36     6059   5394   7410   -382    189  -1684       O  
ATOM    278  CB  LEU A  36       6.370 -23.296 -36.563  1.00 49.37           C  
ANISOU  278  CB  LEU A  36     5909   5468   7380   -287    165  -1615       C  
ATOM    279  CG  LEU A  36       7.624 -22.462 -36.794  1.00 51.28           C  
ANISOU  279  CG  LEU A  36     6020   5724   7741   -259    219  -1751       C  
ATOM    280  CD1 LEU A  36       7.961 -21.597 -35.571  1.00 51.71           C  
ANISOU  280  CD1 LEU A  36     6057   5760   7830   -148    113  -1684       C  
ATOM    281  CD2 LEU A  36       8.787 -23.382 -37.170  1.00 52.24           C  
ANISOU  281  CD2 LEU A  36     6044   5737   8069   -219    230  -1969       C  
ATOM    282  N   VAL A  37       3.481 -24.872 -37.593  1.00 46.75           N  
ANISOU  282  N   VAL A  37     5793   5211   6757   -504    225  -1428       N  
ATOM    283  CA  VAL A  37       2.641 -26.055 -37.278  1.00 45.94           C  
ANISOU  283  CA  VAL A  37     5789   5039   6629   -520    180  -1377       C  
ATOM    284  C   VAL A  37       2.739 -27.072 -38.407  1.00 45.64           C  
ANISOU  284  C   VAL A  37     5741   4981   6618   -593    250  -1497       C  
ATOM    285  O   VAL A  37       2.810 -28.252 -38.103  1.00 46.05           O  
ANISOU  285  O   VAL A  37     5841   4916   6738   -560    204  -1533       O  
ATOM    286  CB  VAL A  37       1.189 -25.645 -37.013  1.00 45.73           C  
ANISOU  286  CB  VAL A  37     5828   5093   6453   -585    180  -1222       C  
ATOM    287  CG1 VAL A  37       0.269 -26.863 -36.933  1.00 45.95           C  
ANISOU  287  CG1 VAL A  37     5945   5062   6453   -636    172  -1195       C  
ATOM    288  CG2 VAL A  37       1.094 -24.763 -35.770  1.00 45.10           C  
ANISOU  288  CG2 VAL A  37     5770   5013   6355   -510    113  -1109       C  
ATOM    289  N   CYS A  38       2.717 -26.625 -39.654  1.00 45.47           N  
ANISOU  289  N   CYS A  38     5678   5063   6537   -693    357  -1553       N  
ATOM    290  CA  CYS A  38       2.951 -27.489 -40.837  1.00 47.41           C  
ANISOU  290  CA  CYS A  38     5914   5293   6806   -773    441  -1687       C  
ATOM    291  C   CYS A  38       2.861 -26.639 -42.097  1.00 48.34           C  
ANISOU  291  C   CYS A  38     6022   5532   6812   -889    554  -1718       C  
ATOM    292  O   CYS A  38       2.436 -25.494 -41.995  1.00 46.66           O  
ANISOU  292  O   CYS A  38     5820   5410   6499   -903    547  -1618       O  
ATOM    293  CB  CYS A  38       1.961 -28.639 -40.932  1.00 47.20           C  
ANISOU  293  CB  CYS A  38     5968   5231   6734   -824    420  -1650       C  
ATOM    294  SG  CYS A  38       0.272 -28.062 -41.197  1.00 46.76           S  
ANISOU  294  SG  CYS A  38     5973   5308   6486   -927    420  -1498       S  
ATOM    295  N   LYS A  39       3.327 -27.179 -43.227  1.00 51.00           N  
ANISOU  295  N   LYS A  39     6354   5858   7164   -970    652  -1856       N  
ATOM    296  CA  LYS A  39       3.409 -26.448 -44.524  1.00 51.91           C  
ANISOU  296  CA  LYS A  39     6490   6059   7175  -1091    776  -1918       C  
ATOM    297  C   LYS A  39       2.062 -25.851 -44.952  1.00 50.05           C  
ANISOU  297  C   LYS A  39     6345   5933   6740  -1166    741  -1772       C  
ATOM    298  O   LYS A  39       2.075 -24.754 -45.545  1.00 49.36           O  
ANISOU  298  O   LYS A  39     6286   5920   6547  -1213    783  -1745       O  
ATOM    299  CB  LYS A  39       3.959 -27.372 -45.616  1.00 54.59           C  
ANISOU  299  CB  LYS A  39     6831   6349   7562  -1171    883  -2090       C  
ATOM    300  CG  LYS A  39       5.459 -27.628 -45.559  1.00 57.22           C  
ANISOU  300  CG  LYS A  39     7054   6597   8091  -1127    962  -2282       C  
ATOM    301  CD  LYS A  39       6.206 -27.086 -46.758  1.00 60.31           C  
ANISOU  301  CD  LYS A  39     7444   7025   8444  -1245   1140  -2421       C  
ATOM    302  CE  LYS A  39       6.670 -25.656 -46.572  1.00 61.10           C  
ANISOU  302  CE  LYS A  39     7489   7160   8567  -1216   1177  -2423       C  
ATOM    303  NZ  LYS A  39       7.371 -25.145 -47.774  1.00 62.23           N1+
ANISOU  303  NZ  LYS A  39     7637   7314   8693  -1344   1378  -2589       N1+
ATOM    304  N   GLU A  40       0.951 -26.535 -44.669  1.00 48.79           N  
ANISOU  304  N   GLU A  40     6229   5774   6536  -1176    666  -1690       N  
ATOM    305  CA  GLU A  40      -0.383 -26.057 -45.119  1.00 47.45           C  
ANISOU  305  CA  GLU A  40     6128   5699   6202  -1250    622  -1583       C  
ATOM    306  C   GLU A  40      -0.766 -24.808 -44.330  1.00 21.19           C  
ATOM    307  O   GLU A  40      -1.266 -23.870 -44.941  1.00 46.11           O  
ANISOU  307  O   GLU A  40     5988   5672   5859  -1247    547  -1402       O  
ATOM    308  CB  GLU A  40      -1.427 -27.151 -44.984  1.00 48.32           C  
ANISOU  308  CB  GLU A  40     6264   5784   6311  -1274    566  -1552       C  
ATOM    309  CG  GLU A  40      -2.801 -26.733 -45.464  1.00 49.07           C  
ANISOU  309  CG  GLU A  40     6406   5969   6269  -1345    509  -1470       C  
ATOM    310  CD  GLU A  40      -2.898 -26.399 -46.948  1.00 50.56           C  
ANISOU  310  CD  GLU A  40     6672   6215   6323  -1455    548  -1528       C  
ATOM    311  OE1 GLU A  40      -1.918 -26.659 -47.676  1.00 52.66           O  
ANISOU  311  OE1 GLU A  40     6961   6447   6600  -1496    649  -1644       O  
ATOM    312  OE2 GLU A  40      -3.969 -25.910 -47.389  1.00 50.38           O1-
ANISOU  312  OE2 GLU A  40     6694   6261   6187  -1502    475  -1466       O1-
ATOM    313  N   TRP A  41      -0.516 -24.790 -43.025  1.00 43.59           N  
ANISOU  313  N   TRP A  41     5571   5223   5768  -1085    502  -1396       N  
ATOM    314  CA  TRP A  41      -0.711 -23.598 -42.160  1.00 41.33           C  
ANISOU  314  CA  TRP A  41     5263   4984   5458  -1021    449  -1281       C  
ATOM    315  C   TRP A  41       0.148 -22.444 -42.670  1.00 41.17           C  
ANISOU  315  C   TRP A  41     5229   5008   5404  -1032    512  -1319       C  
ATOM    316  O   TRP A  41      -0.386 -21.365 -42.885  1.00 40.98           O  
ANISOU  316  O   TRP A  41     5236   5063   5272  -1058    492  -1240       O  
ATOM    317  CB  TRP A  41      -0.373 -23.921 -40.706  1.00 40.18           C  
ANISOU  317  CB  TRP A  41     5085   4753   5426   -907    390  -1241       C  
ATOM    318  CG  TRP A  41      -1.446 -24.711 -40.039  1.00 39.44           C  
ANISOU  318  CG  TRP A  41     5032   4625   5328   -909    334  -1167       C  
ATOM    319  CD1 TRP A  41      -2.081 -25.807 -40.530  1.00 40.24           C  
ANISOU  319  CD1 TRP A  41     5169   4701   5418   -977    346  -1202       C  
ATOM    320  CD2 TRP A  41      -2.023 -24.456 -38.751  1.00 38.28           C  
ANISOU  320  CD2 TRP A  41     4902   4458   5185   -854    273  -1054       C  
ATOM    321  CE2 TRP A  41      -3.011 -25.431 -38.545  1.00 38.72           C  
ANISOU  321  CE2 TRP A  41     5006   4476   5232   -901    263  -1032       C  
ATOM    322  CE3 TRP A  41      -1.807 -23.495 -37.766  1.00 37.58           C  
ANISOU  322  CE3 TRP A  41     4798   4378   5104   -778    235   -976       C  
ATOM    323  NE1 TRP A  41      -3.032 -26.237 -39.649  1.00 40.17           N  
ANISOU  323  NE1 TRP A  41     5194   4659   5408   -973    303  -1122       N  
ATOM    324  CZ2 TRP A  41      -3.779 -25.474 -37.395  1.00 38.31           C  
ANISOU  324  CZ2 TRP A  41     4993   4389   5176   -884    231   -940       C  
ATOM    325  CZ3 TRP A  41      -2.546 -23.549 -36.610  1.00 37.51           C  
ANISOU  325  CZ3 TRP A  41     4831   4334   5087   -753    194   -881       C  
ATOM    326  CH2 TRP A  41      -3.522 -24.521 -36.435  1.00 38.07           C  
ANISOU  326  CH2 TRP A  41     4955   4362   5146   -810    199   -865       C  
ATOM    327  N   GLN A  42       1.440 -22.681 -42.866  1.00 41.36           N  
ANISOU  327  N   GLN A  42     5210   4975   5529  -1016    588  -1447       N  
ATOM    328  CA  GLN A  42       2.365 -21.669 -43.427  1.00 41.09           C  
ANISOU  328  CA  GLN A  42     5164   4970   5477  -1047    682  -1516       C  
ATOM    329  C   GLN A  42       1.767 -21.183 -44.746  1.00 41.02           C  
ANISOU  329  C   GLN A  42     5263   5035   5287  -1177    733  -1508       C  
ATOM    330  O   GLN A  42       1.740 -19.940 -44.943  1.00 40.40           O  
ANISOU  330  O   GLN A  42     5226   5013   5112  -1199    746  -1455       O  
ATOM    331  CB  GLN A  42       3.762 -22.260 -43.603  1.00 42.39           C  
ANISOU  331  CB  GLN A  42     5253   5052   5801  -1031    771  -1697       C  
ATOM    332  CG  GLN A  42       4.733 -21.328 -44.300  1.00 43.56           C  
ANISOU  332  CG  GLN A  42     5390   5222   5940  -1092    904  -1800       C  
ATOM    333  CD  GLN A  42       6.100 -21.941 -44.481  1.00 45.54           C  
ANISOU  333  CD  GLN A  42     5540   5386   6377  -1081   1002  -2007       C  
ATOM    334  NE2 GLN A  42       7.122 -21.270 -43.957  1.00 45.66           N  
ANISOU  334  NE2 GLN A  42     5457   5378   6515  -1020   1030  -2076       N  
ATOM    335  OE1 GLN A  42       6.240 -23.003 -45.097  1.00 47.15           O  
ANISOU  335  OE1 GLN A  42     5747   5541   6625  -1127   1052  -2116       O  
ATOM    336  N   ARG A  43       1.301 -22.104 -45.606  1.00 40.96           N  
ANISOU  336  N   ARG A  43     5314   5018   5229  -1258    751  -1557       N  
ATOM    337  CA  ARG A  43       0.786 -21.758 -46.955  1.00 41.50           C  
ANISOU  337  CA  ARG A  43     5513   5139   5117  -1386    789  -1566       C  
ATOM    338  C   ARG A  43      -0.399 -20.799 -46.808  1.00 40.40           C  
ANISOU  338  C   ARG A  43     5427   5075   4846  -1378    670  -1411       C  
ATOM    339  O   ARG A  43      -0.439 -19.787 -47.518  1.00 39.92           O  
ANISOU  339  O   ARG A  43     5467   5054   4648  -1438    689  -1391       O  
ATOM    340  CB  ARG A  43       0.399 -22.996 -47.764  1.00 42.61           C  
ANISOU  340  CB  ARG A  43     5701   5252   5237  -1463    806  -1639       C  
ATOM    341  CG  ARG A  43      -0.009 -22.665 -49.191  1.00 44.10           C  
ANISOU  341  CG  ARG A  43     6046   5478   5233  -1598    841  -1663       C  
ATOM    342  CD  ARG A  43      -0.830 -23.737 -49.866  1.00 45.52           C  
ANISOU  342  CD  ARG A  43     6281   5652   5364  -1663    802  -1689       C  
ATOM    343  NE  ARG A  43      -2.128 -23.926 -49.252  1.00 45.58           N  
ANISOU  343  NE  ARG A  43     6253   5694   5370  -1611    650  -1571       N  
ATOM    344  CZ  ARG A  43      -3.166 -23.102 -49.384  1.00 46.46           C  
ANISOU  344  CZ  ARG A  43     6419   5870   5365  -1617    534  -1467       C  
ATOM    345  NH1 ARG A  43      -3.075 -22.005 -50.127  1.00 47.06           N1+
ANISOU  345  NH1 ARG A  43     6614   5977   5291  -1668    539  -1450       N1+
ATOM    346  NH2 ARG A  43      -4.303 -23.386 -48.764  1.00 46.97           N  
ANISOU  346  NH2 ARG A  43     6422   5957   5466  -1573    415  -1388       N  
ATOM    347  N   VAL A  44      -1.322 -21.101 -45.903  1.00 39.77           N  
ANISOU  347  N   VAL A  44     5291   5008   4813  -1308    556  -1312       N  
ATOM    348  CA  VAL A  44      -2.564 -20.307 -45.691  1.00 39.51           C  
ANISOU  348  CA  VAL A  44     5280   5042   4689  -1294    436  -1182       C  
ATOM    349  C   VAL A  44      -2.195 -18.918 -45.177  1.00 38.92           C  
ANISOU  349  C   VAL A  44     5194   4999   4595  -1240    430  -1114       C  
ATOM    350  O   VAL A  44      -2.727 -17.936 -45.715  1.00 39.46           O  
ANISOU  350  O   VAL A  44     5341   5117   4535  -1273    381  -1058       O  
ATOM    351  CB  VAL A  44      -3.517 -21.031 -44.731  1.00 39.40           C  
ANISOU  351  CB  VAL A  44     5193   5018   4758  -1241    351  -1120       C  
ATOM    352  CG1 VAL A  44      -4.593 -20.109 -44.180  1.00 38.92           C  
ANISOU  352  CG1 VAL A  44     5111   5017   4659  -1204    246  -1002       C  
ATOM    353  CG2 VAL A  44      -4.143 -22.242 -45.405  1.00 40.27           C  
ANISOU  353  CG2 VAL A  44     5332   5110   4857  -1312    342  -1179       C  
ATOM    354  N   ILE A  45      -1.336 -18.841 -44.165  1.00 38.31           N  
ANISOU  354  N   ILE A  45     5028   4887   4641  -1157    466  -1118       N  
ATOM    355  CA  ILE A  45      -0.823 -17.547 -43.619  1.00 38.20           C  
ANISOU  355  CA  ILE A  45     4993   4897   4626  -1104    473  -1067       C  
ATOM    356  C   ILE A  45      -0.194 -16.750 -44.762  1.00 39.16           C  
ANISOU  356  C   ILE A  45     5210   5033   4635  -1192    566  -1128       C  
ATOM    357  O   ILE A  45      -0.493 -15.554 -44.887  1.00 38.59           O  
ANISOU  357  O   ILE A  45     5197   5003   4461  -1198    534  -1053       O  
ATOM    358  CB  ILE A  45       0.183 -17.799 -42.477  1.00 38.00           C  
ANISOU  358  CB  ILE A  45     4862   4814   4764  -1007    499  -1099       C  
ATOM    359  CG1 ILE A  45      -0.546 -18.305 -41.230  1.00 37.75           C  
ANISOU  359  CG1 ILE A  45     4780   4761   4802   -925    401  -1010       C  
ATOM    360  CG2 ILE A  45       1.039 -16.567 -42.188  1.00 37.28           C  
ANISOU  360  CG2 ILE A  45     4747   4735   4681   -974    542  -1098       C  
ATOM    361  CD1 ILE A  45       0.313 -19.110 -40.301  1.00 37.99           C  
ANISOU  361  CD1 ILE A  45     4749   4701   4985   -842    401  -1062       C  
ATOM    362  N   SER A  46       0.654 -17.400 -45.554  1.00 40.58           N  
ANISOU  362  N   SER A  46     5414   5169   4835  -1262    684  -1265       N  
ATOM    363  CA  SER A  46       1.395 -16.728 -46.641  1.00 42.43           C  
ANISOU  363  CA  SER A  46     5755   5399   4968  -1366    811  -1348       C  
ATOM    364  C   SER A  46       0.403 -16.208 -47.693  1.00 43.51           C  
ANISOU  364  C   SER A  46     6068   5574   4888  -1455    752  -1283       C  
ATOM    365  O   SER A  46       0.430 -15.018 -47.949  1.00 44.09           O  
ANISOU  365  O   SER A  46     6235   5668   4850  -1480    756  -1235       O  
ATOM    366  CB  SER A  46       2.483 -17.600 -47.196  1.00 43.75           C  
ANISOU  366  CB  SER A  46     5896   5503   5222  -1426    961  -1525       C  
ATOM    367  OG  SER A  46       2.015 -18.526 -48.164  1.00 45.41           O  
ANISOU  367  OG  SER A  46     6192   5702   5359  -1514    972  -1576       O  
ATOM    368  N   GLU A  47      -0.470 -17.050 -48.247  1.00 44.76           N  
ANISOU  368  N   GLU A  47     6276   5737   4992  -1496    684  -1281       N  
ATOM    369  CA  GLU A  47      -1.360 -16.658 -49.372  1.00 46.24           C  
ANISOU  369  CA  GLU A  47     6647   5947   4975  -1583    611  -1243       C  
ATOM    370  C   GLU A  47      -2.523 -15.803 -48.877  1.00 20.12           C  
ATOM    371  O   GLU A  47      -2.977 -14.948 -49.638  1.00 45.62           O  
ANISOU  371  O   GLU A  47     6724   5930   4681  -1557    367  -1055       O  
ATOM    372  CB  GLU A  47      -1.881 -17.889 -50.084  1.00 48.51           C  
ANISOU  372  CB  GLU A  47     6971   6218   5241  -1645    590  -1304       C  
ATOM    373  CG  GLU A  47      -0.804 -18.565 -50.890  1.00 51.36           C  
ANISOU  373  CG  GLU A  47     7382   6524   5606  -1744    771  -1459       C  
ATOM    374  CD  GLU A  47      -1.423 -19.163 -52.139  1.00 54.62           C  
ANISOU  374  CD  GLU A  47     7953   6927   5873  -1855    745  -1503       C  
ATOM    375  OE1 GLU A  47      -1.394 -20.436 -52.294  1.00 55.77           O  
ANISOU  375  OE1 GLU A  47     8045   7047   6100  -1877    781  -1585       O  
ATOM    376  OE2 GLU A  47      -1.973 -18.334 -52.936  1.00 57.23           O1-
ANISOU  376  OE2 GLU A  47     8471   7268   6005  -1915    673  -1451       O1-
ATOM    377  N   GLY A  48      -2.987 -16.025 -47.651  1.00 43.96           N  
ANISOU  377  N   GLY A  48     6190   5732   4779  -1403    356  -1030       N  
ATOM    378  CA  GLY A  48      -4.032 -15.194 -47.011  1.00 42.88           C  
ANISOU  378  CA  GLY A  48     6017   5642   4633  -1328    207   -907       C  
ATOM    379  C   GLY A  48      -3.560 -13.788 -46.676  1.00 41.63           C  
ANISOU  379  C   GLY A  48     5885   5498   4436  -1292    223   -847       C  
ATOM    380  O   GLY A  48      -4.404 -12.974 -46.303  1.00 39.98           O  
ANISOU  380  O   GLY A  48     5666   5323   4203  -1238    100   -753       O  
ATOM    381  N   MET A  49      -2.261 -13.511 -46.800  1.00 41.80           N  
ANISOU  381  N   MET A  49     5931   5489   4462  -1322    372   -912       N  
ATOM    382  CA  MET A  49      -1.697 -12.145 -46.681  1.00 42.29           C  
ANISOU  382  CA  MET A  49     6044   5555   4468  -1313    412   -875       C  
ATOM    383  C   MET A  49      -1.920 -11.695 -45.228  1.00 39.74           C  
ANISOU  383  C   MET A  49     5566   5263   4272  -1187    345   -783       C  
ATOM    384  O   MET A  49      -2.306 -10.521 -45.006  1.00 39.05           O  
ANISOU  384  O   MET A  49     5512   5200   4124  -1153    275   -695       O  
ATOM    385  CB  MET A  49      -2.378 -11.221 -47.705  1.00 44.82           C  
ANISOU  385  CB  MET A  49     6567   5880   4582  -1375    326   -822       C  
ATOM    386  CG  MET A  49      -1.436 -10.277 -48.505  1.00 47.76           C  
ANISOU  386  CG  MET A  49     7117   6214   4816  -1468    455   -864       C  
ATOM    387  SD  MET A  49       0.212 -10.865 -49.163  1.00 51.04           S  
ANISOU  387  SD  MET A  49     7565   6570   5258  -1590    727  -1048       S  
ATOM    388  CE  MET A  49      -0.265 -12.290 -50.148  1.00 52.72           C  
ANISOU  388  CE  MET A  49     7844   6764   5422  -1672    714  -1124       C  
ATOM    389  N   LEU A  50      -1.640 -12.595 -44.270  1.00 37.33           N  
ANISOU  389  N   LEU A  50     5111   4944   4131  -1123    367   -807       N  
ATOM    390  CA  LEU A  50      -2.051 -12.450 -42.851  1.00 35.07           C  
ANISOU  390  CA  LEU A  50     4695   4674   3956  -1012    292   -721       C  
ATOM    391  C   LEU A  50      -1.215 -11.385 -42.148  1.00 34.28           C  
ANISOU  391  C   LEU A  50     4558   4575   3893   -958    338   -697       C  
ATOM    392  O   LEU A  50      -1.722 -10.726 -41.210  1.00 34.01           O  
ANISOU  392  O   LEU A  50     4470   4566   3886   -884    264   -602       O  
ATOM    393  CB  LEU A  50      -1.897 -13.789 -42.138  1.00 34.66           C  
ANISOU  393  CB  LEU A  50     4541   4583   4044   -973    306   -763       C  
ATOM    394  CG  LEU A  50      -3.158 -14.648 -42.012  1.00 34.69           C  
ANISOU  394  CG  LEU A  50     4524   4596   4060   -977    218   -728       C  
ATOM    395  CD1 LEU A  50      -4.237 -13.943 -41.222  1.00 34.00           C  
ANISOU  395  CD1 LEU A  50     4394   4550   3976   -923    117   -620       C  
ATOM    396  CD2 LEU A  50      -3.712 -15.024 -43.371  1.00 35.98           C  
ANISOU  396  CD2 LEU A  50     4783   4773   4114  -1071    198   -772       C  
ATOM    397  N   TRP A  51       0.039 -11.239 -42.551  1.00 34.65           N  
ANISOU  397  N   TRP A  51     4624   4591   3951   -998    464   -792       N  
ATOM    398  CA  TRP A  51       0.959 -10.249 -41.935  1.00 33.61           C  
ANISOU  398  CA  TRP A  51     4449   4454   3867   -956    522   -794       C  
ATOM    399  C   TRP A  51       0.584  -8.844 -42.395  1.00 33.91           C  
ANISOU  399  C   TRP A  51     4602   4525   3758   -988    500   -718       C  
ATOM    400  O   TRP A  51       0.489  -7.973 -41.543  1.00 32.89           O  
ANISOU  400  O   TRP A  51     4426   4417   3655   -917    455   -640       O  
ATOM    401  CB  TRP A  51       2.407 -10.618 -42.204  1.00 33.47           C  
ANISOU  401  CB  TRP A  51     4392   4386   3939   -991    669   -947       C  
ATOM    402  CG  TRP A  51       2.851 -11.803 -41.407  1.00 32.87           C  
ANISOU  402  CG  TRP A  51     4186   4265   4039   -917    655  -1008       C  
ATOM    403  CD1 TRP A  51       3.016 -13.085 -41.856  1.00 33.52           C  
ANISOU  403  CD1 TRP A  51     4255   4307   4174   -949    687  -1102       C  
ATOM    404  CD2 TRP A  51       3.254 -11.805 -40.026  1.00 32.01           C  
ANISOU  404  CD2 TRP A  51     3958   4131   4072   -797    601   -985       C  
ATOM    405  CE2 TRP A  51       3.611 -13.130 -39.704  1.00 32.41           C  
ANISOU  405  CE2 TRP A  51     3942   4120   4251   -758    588  -1063       C  
ATOM    406  CE3 TRP A  51       3.304 -10.837 -39.014  1.00 31.10           C  
ANISOU  406  CE3 TRP A  51     3801   4034   3982   -718    551   -904       C  
ATOM    407  NE1 TRP A  51       3.472 -13.890 -40.842  1.00 33.12           N  
ANISOU  407  NE1 TRP A  51     4089   4204   4290   -852    647  -1136       N  
ATOM    408  CZ2 TRP A  51       4.052 -13.480 -38.424  1.00 31.99           C  
ANISOU  408  CZ2 TRP A  51     3799   4014   4341   -641    518  -1061       C  
ATOM    409  CZ3 TRP A  51       3.720 -11.191 -37.753  1.00 30.48           C  
ANISOU  409  CZ3 TRP A  51     3629   3911   4043   -608    490   -903       C  
ATOM    410  CH2 TRP A  51       4.091 -12.497 -37.463  1.00 30.91           C  
ANISOU  410  CH2 TRP A  51     3634   3895   4214   -569    468   -980       C  
ATOM    411  N   LYS A  52       0.307  -8.644 -43.678  1.00 35.70           N  
ANISOU  411  N   LYS A  52     4988   4749   3827  -1090    516   -735       N  
ATOM    412  CA  LYS A  52      -0.246  -7.357 -44.153  1.00 36.68           C  
ANISOU  412  CA  LYS A  52     5255   4890   3793  -1114    455   -649       C  
ATOM    413  C   LYS A  52      -1.489  -7.050 -43.319  1.00 36.03           C  
ANISOU  413  C   LYS A  52     5099   4850   3740  -1014    283   -523       C  
ATOM    414  O   LYS A  52      -1.601  -5.920 -42.782  1.00 35.29           O  
ANISOU  414  O   LYS A  52     5001   4773   3635   -962    243   -447       O  
ATOM    415  CB  LYS A  52      -0.569  -7.431 -45.641  1.00 38.87           C  
ANISOU  415  CB  LYS A  52     5738   5143   3888  -1231    456   -681       C  
ATOM    416  CG  LYS A  52      -1.164  -6.169 -46.253  1.00 40.21           C  
ANISOU  416  CG  LYS A  52     6096   5307   3874  -1257    368   -596       C  
ATOM    417  CD  LYS A  52      -1.544  -6.389 -47.712  1.00 42.84           C  
ANISOU  417  CD  LYS A  52     6657   5603   4018  -1370    342   -628       C  
ATOM    418  CE  LYS A  52      -1.760  -5.130 -48.526  1.00 45.16           C  
ANISOU  418  CE  LYS A  52     7203   5857   4100  -1425    292   -573       C  
ATOM    419  NZ  LYS A  52      -3.110  -4.544 -48.314  1.00 46.03           N1+
ANISOU  419  NZ  LYS A  52     7324   5989   4177  -1332     51   -454       N1+
ATOM    420  N   LYS A  53      -2.378  -8.035 -43.177  1.00 36.08           N  
ANISOU  420  N   LYS A  53     5042   4872   3796   -991    195   -512       N  
ATOM    421  CA  LYS A  53      -3.685  -7.860 -42.484  1.00 35.45           C  
ANISOU  421  CA  LYS A  53     4887   4828   3754   -915     44   -418       C  
ATOM    422  C   LYS A  53      -3.444  -7.476 -41.025  1.00 34.14           C  
ANISOU  422  C   LYS A  53     4585   4675   3713   -821     57   -367       C  
ATOM    423  O   LYS A  53      -4.215  -6.659 -40.481  1.00 33.67           O  
ANISOU  423  O   LYS A  53     4495   4642   3657   -765    -34   -286       O  
ATOM    424  CB  LYS A  53      -4.518  -9.142 -42.568  1.00 35.67           C  
ANISOU  424  CB  LYS A  53     4860   4859   3832   -926    -13   -444       C  
ATOM    425  CG  LYS A  53      -5.316  -9.295 -43.854  1.00 36.89           C  
ANISOU  425  CG  LYS A  53     5141   5015   3863   -995   -102   -462       C  
ATOM    426  CD  LYS A  53      -5.894 -10.661 -44.065  1.00 37.20           C  
ANISOU  426  CD  LYS A  53     5131   5050   3952  -1024   -126   -514       C  
ATOM    427  CE  LYS A  53      -6.723 -10.728 -45.325  1.00 38.79           C  
ANISOU  427  CE  LYS A  53     5460   5250   4028  -1086   -236   -533       C  
ATOM    428  NZ  LYS A  53      -6.706 -12.091 -45.904  1.00 39.89           N1+
ANISOU  428  NZ  LYS A  53     5607   5371   4177  -1152   -195   -617       N1+
ATOM    429  N   LEU A  54      -2.437  -8.071 -40.407  1.00 34.13           N  
ANISOU  429  N   LEU A  54     4506   4647   3816   -800    155   -421       N  
ATOM    430  CA  LEU A  54      -2.162  -7.823 -38.981  1.00 34.27           C  
ANISOU  430  CA  LEU A  54     4412   4663   3947   -709    156   -378       C  
ATOM    431  C   LEU A  54      -1.683  -6.386 -38.815  1.00 34.42           C  
ANISOU  431  C   LEU A  54     4459   4695   3925   -688    177   -339       C  
ATOM    432  O   LEU A  54      -2.224  -5.624 -37.953  1.00 33.98           O  
ANISOU  432  O   LEU A  54     4359   4663   3890   -624    113   -255       O  
ATOM    433  CB  LEU A  54      -1.093  -8.799 -38.500  1.00 34.99           C  
ANISOU  433  CB  LEU A  54     4435   4705   4153   -689    234   -461       C  
ATOM    434  CG  LEU A  54      -0.716  -8.614 -37.036  1.00 34.51           C  
ANISOU  434  CG  LEU A  54     4286   4626   4201   -594    220   -424       C  
ATOM    435  CD1 LEU A  54      -1.969  -8.610 -36.178  1.00 34.55           C  
ANISOU  435  CD1 LEU A  54     4261   4651   4217   -552    131   -326       C  
ATOM    436  CD2 LEU A  54       0.248  -9.689 -36.564  1.00 34.72           C  
ANISOU  436  CD2 LEU A  54     4257   4587   4348   -561    259   -510       C  
ATOM    437  N   ILE A  55      -0.696  -6.029 -39.627  1.00 35.60           N  
ANISOU  437  N   ILE A  55     4683   4825   4018   -751    275   -408       N  
ATOM    438  CA  ILE A  55      -0.126  -4.661 -39.641  1.00 36.32           C  
ANISOU  438  CA  ILE A  55     4824   4919   4057   -754    320   -388       C  
ATOM    439  C   ILE A  55      -1.270  -3.663 -39.813  1.00 36.33           C  
ANISOU  439  C   ILE A  55     4901   4950   3953   -740    203   -280       C  
ATOM    440  O   ILE A  55      -1.279  -2.666 -39.075  1.00 35.72           O  
ANISOU  440  O   ILE A  55     4791   4886   3895   -682    180   -217       O  
ATOM    441  CB  ILE A  55       0.940  -4.530 -40.739  1.00 37.79           C  
ANISOU  441  CB  ILE A  55     5112   5071   4176   -859    461   -495       C  
ATOM    442  CG1 ILE A  55       2.163  -5.376 -40.395  1.00 37.84           C  
ANISOU  442  CG1 ILE A  55     5006   5043   4330   -853    572   -621       C  
ATOM    443  CG2 ILE A  55       1.290  -3.063 -40.996  1.00 37.64           C  
ANISOU  443  CG2 ILE A  55     5194   5047   4060   -889    504   -466       C  
ATOM    444  CD1 ILE A  55       3.214  -5.321 -41.471  1.00 39.36           C  
ANISOU  444  CD1 ILE A  55     5280   5197   4480   -969    735   -753       C  
ATOM    445  N   GLU A  56      -2.196  -3.924 -40.733  1.00 37.70           N  
ANISOU  445  N   GLU A  56     5166   5129   4030   -784    121   -266       N  
ATOM    446  CA  GLU A  56      -3.355  -3.022 -40.914  1.00 39.38           C  
ANISOU  446  CA  GLU A  56     5441   5359   4163   -757    -23   -176       C  
ATOM    447  C   GLU A  56      -4.150  -2.970 -39.614  1.00 23.24           C  
ATOM    448  O   GLU A  56      -4.499  -1.858 -39.234  1.00 40.56           O  
ANISOU  448  O   GLU A  56     5435   5552   4424   -610   -161    -46       O  
ATOM    449  CB  GLU A  56      -4.231  -3.432 -42.086  1.00 40.90           C  
ANISOU  449  CB  GLU A  56     5748   5543   4249   -812   -122   -188       C  
ATOM    450  CG  GLU A  56      -3.591  -3.107 -43.412  1.00 42.64           C  
ANISOU  450  CG  GLU A  56     6181   5719   4300   -917    -57   -232       C  
ATOM    451  CD  GLU A  56      -4.180  -3.878 -44.568  1.00 45.11           C  
ANISOU  451  CD  GLU A  56     6608   6014   4516   -986   -123   -272       C  
ATOM    452  OE1 GLU A  56      -4.844  -4.933 -44.315  1.00 46.21           O  
ANISOU  452  OE1 GLU A  56     6630   6180   4750   -961   -179   -289       O  
ATOM    453  OE2 GLU A  56      -3.954  -3.457 -45.714  1.00 47.07           O1-
ANISOU  453  OE2 GLU A  56     7074   6218   4592  -1072   -110   -290       O1-
ATOM    454  N   ARG A  57      -4.399  -4.097 -38.950  1.00 39.98           N  
ANISOU  454  N   ARG A  57     5239   5475   4476   -634    -97   -133       N  
ATOM    455  CA  ARG A  57      -5.186  -4.115 -37.687  1.00 40.76           C  
ANISOU  455  CA  ARG A  57     5207   5593   4686   -560   -150    -80       C  
ATOM    456  C   ARG A  57      -4.448  -3.321 -36.600  1.00 40.87           C  
ANISOU  456  C   ARG A  57     5172   5605   4751   -501    -95    -44       C  
ATOM    457  O   ARG A  57      -5.116  -2.632 -35.781  1.00 41.95           O  
ANISOU  457  O   ARG A  57     5252   5760   4928   -446   -147     18       O  
ATOM    458  CB  ARG A  57      -5.446  -5.545 -37.211  1.00 41.40           C  
ANISOU  458  CB  ARG A  57     5207   5663   4861   -564   -130   -117       C  
ATOM    459  CG  ARG A  57      -6.426  -5.676 -36.057  1.00 40.82           C  
ANISOU  459  CG  ARG A  57     5028   5599   4883   -517   -171    -77       C  
ATOM    460  CD  ARG A  57      -6.618  -7.160 -35.756  1.00 41.95           C  
ANISOU  460  CD  ARG A  57     5130   5714   5094   -542   -139   -121       C  
ATOM    461  NE  ARG A  57      -5.698  -7.568 -34.697  1.00 42.76           N  
ANISOU  461  NE  ARG A  57     5211   5775   5260   -505    -64   -120       N  
ATOM    462  CZ  ARG A  57      -5.318  -8.820 -34.411  1.00 43.90           C  
ANISOU  462  CZ  ARG A  57     5354   5871   5453   -515    -22   -163       C  
ATOM    463  NH1 ARG A  57      -5.735  -9.853 -35.131  1.00 45.13           N1+
ANISOU  463  NH1 ARG A  57     5523   6019   5603   -571    -27   -212       N1+
ATOM    464  NH2 ARG A  57      -4.491  -9.049 -33.402  1.00 43.31           N  
ANISOU  464  NH2 ARG A  57     5274   5747   5433   -466     15   -159       N  
ATOM    465  N   MET A  58      -3.121  -3.385 -36.585  1.00 40.30           N  
ANISOU  465  N   MET A  58     5115   5510   4688   -513      8    -91       N  
ATOM    466  CA  MET A  58      -2.344  -2.588 -35.607  1.00 39.44           C  
ANISOU  466  CA  MET A  58     4960   5395   4629   -457     53    -68       C  
ATOM    467  C   MET A  58      -2.516  -1.100 -35.933  1.00 40.42           C  
ANISOU  467  C   MET A  58     5154   5537   4667   -456     26    -13       C  
ATOM    468  O   MET A  58      -2.739  -0.303 -35.013  1.00 41.54           O  
ANISOU  468  O   MET A  58     5246   5692   4846   -395     -2     46       O  
ATOM    469  CB  MET A  58      -0.869  -2.970 -35.649  1.00 38.80           C  
ANISOU  469  CB  MET A  58     4870   5281   4594   -473    161   -156       C  
ATOM    470  CG  MET A  58      -0.602  -4.342 -35.067  1.00 37.72           C  
ANISOU  470  CG  MET A  58     4661   5110   4561   -448    170   -205       C  
ATOM    471  SD  MET A  58      -1.363  -4.432 -33.457  1.00 35.12           S  
ANISOU  471  SD  MET A  58     4260   4778   4308   -363     99   -120       S  
ATOM    472  CE  MET A  58      -0.625  -5.932 -32.806  1.00 35.70           C  
ANISOU  472  CE  MET A  58     4296   4780   4488   -333    116   -189       C  
ATOM    473  N   VAL A  59      -2.470  -0.737 -37.208  1.00 41.48           N  
ANISOU  473  N   VAL A  59     5415   5663   4681   -524     28    -32       N  
ATOM    474  CA  VAL A  59      -2.558   0.688 -37.625  1.00 42.90           C  
ANISOU  474  CA  VAL A  59     5701   5840   4758   -530      0     18       C  
ATOM    475  C   VAL A  59      -3.952   1.203 -37.274  1.00 43.98           C  
ANISOU  475  C   VAL A  59     5806   6000   4904   -469   -147     99       C  
ATOM    476  O   VAL A  59      -4.057   2.343 -36.777  1.00 42.59           O  
ANISOU  476  O   VAL A  59     5627   5827   4727   -422   -174    155       O  
ATOM    477  CB  VAL A  59      -2.214   0.859 -39.116  1.00 43.77           C  
ANISOU  477  CB  VAL A  59     5997   5918   4717   -630     36    -23       C  
ATOM    478  CG1 VAL A  59      -2.682   2.196 -39.668  1.00 44.70           C  
ANISOU  478  CG1 VAL A  59     6264   6016   4705   -635    -43     42       C  
ATOM    479  CG2 VAL A  59      -0.729   0.679 -39.358  1.00 42.92           C  
ANISOU  479  CG2 VAL A  59     5908   5782   4617   -695    210   -118       C  
ATOM    480  N   ARG A  60      -4.977   0.376 -37.491  1.00 47.21           N  
ANISOU  480  N   ARG A  60     6178   6421   5338   -469   -234     92       N  
ATOM    481  CA  ARG A  60      -6.388   0.798 -37.328  1.00 50.13           C  
ANISOU  481  CA  ARG A  60     6506   6807   5734   -418   -381    138       C  
ATOM    482  C   ARG A  60      -6.685   0.949 -35.845  1.00 48.37           C  
ANISOU  482  C   ARG A  60     6129   6605   5643   -349   -364    171       C  
ATOM    483  O   ARG A  60      -7.616   1.722 -35.539  1.00 49.01           O  
ANISOU  483  O   ARG A  60     6170   6696   5756   -300   -458    207       O  
ATOM    484  CB  ARG A  60      -7.370  -0.131 -38.059  1.00 54.66           C  
ANISOU  484  CB  ARG A  60     7079   7384   6306   -448   -475    100       C  
ATOM    485  CG  ARG A  60      -7.899   0.458 -39.370  1.00 60.63           C  
ANISOU  485  CG  ARG A  60     7994   8114   6929   -472   -607    106       C  
ATOM    486  CD  ARG A  60      -8.032  -0.494 -40.563  1.00 66.90           C  
ANISOU  486  CD  ARG A  60     8884   8891   7643   -546   -637     49       C  
ATOM    487  NE  ARG A  60      -8.989  -1.589 -40.355  1.00 72.49           N  
ANISOU  487  NE  ARG A  60     9461   9623   8460   -538   -694      8       N  
ATOM    488  CZ  ARG A  60      -8.710  -2.862 -40.009  1.00 74.28           C  
ANISOU  488  CZ  ARG A  60     9601   9862   8760   -570   -593    -37       C  
ATOM    489  NH1 ARG A  60      -9.703  -3.729 -39.876  1.00 76.92           N1+
ANISOU  489  NH1 ARG A  60     9832  10210   9185   -570   -653    -75       N1+
ATOM    490  NH2 ARG A  60      -7.470  -3.272 -39.783  1.00 72.13           N  
ANISOU  490  NH2 ARG A  60     9341   9581   8482   -600   -439    -55       N  
ATOM    491  N   THR A  61      -5.920   0.296 -34.962  1.00 46.49           N  
ANISOU  491  N   THR A  61     5821   6366   5477   -343   -257    153       N  
ATOM    492  CA  THR A  61      -6.159   0.380 -33.493  1.00 45.62           C  
ANISOU  492  CA  THR A  61     5597   6262   5474   -285   -235    185       C  
ATOM    493  C   THR A  61      -5.120   1.315 -32.835  1.00 45.48           C  
ANISOU  493  C   THR A  61     5590   6238   5453   -250   -170    213       C  
ATOM    494  O   THR A  61      -5.539   2.305 -32.234  1.00 47.63           O  
ANISOU  494  O   THR A  61     5834   6520   5744   -205   -201    262       O  
ATOM    495  CB  THR A  61      -6.307  -1.023 -32.897  1.00 43.52           C  
ANISOU  495  CB  THR A  61     5266   5984   5287   -299   -194    151       C  
ATOM    496  CG2 THR A  61      -7.255  -1.898 -33.689  1.00 44.07           C  
ANISOU  496  CG2 THR A  61     5330   6060   5355   -343   -252    112       C  
ATOM    497  OG1 THR A  61      -5.043  -1.666 -32.856  1.00 43.59           O  
ANISOU  497  OG1 THR A  61     5302   5966   5295   -311   -112    113       O  
ATOM    498  N   ASP A  62      -3.822   1.066 -32.990  1.00 44.32           N  
ANISOU  498  N   ASP A  62     5477   6071   5290   -271    -84    173       N  
ATOM    499  CA  ASP A  62      -2.741   1.768 -32.251  1.00 43.34           C  
ANISOU  499  CA  ASP A  62     5340   5936   5192   -238    -18    177       C  
ATOM    500  C   ASP A  62      -2.295   2.992 -33.047  1.00 33.18           C  
ATOM    501  O   ASP A  62      -1.749   2.866 -34.141  1.00 47.96           O  
ANISOU  501  O   ASP A  62     6103   6507   5612   -329     44    136       O  
ATOM    502  CB  ASP A  62      -1.566   0.826 -31.989  1.00 43.50           C  
ANISOU  502  CB  ASP A  62     5332   5925   5270   -242     56    105       C  
ATOM    503  CG  ASP A  62      -0.614   1.277 -30.895  1.00 44.09           C  
ANISOU  503  CG  ASP A  62     5360   5980   5411   -187     94    100       C  
ATOM    504  OD1 ASP A  62      -0.543   2.507 -30.622  1.00 44.24           O  
ANISOU  504  OD1 ASP A  62     5388   6014   5409   -166     96    141       O  
ATOM    505  OD2 ASP A  62       0.050   0.378 -30.316  1.00 43.66           O1-
ANISOU  505  OD2 ASP A  62     5266   5890   5433   -163    110     51       O1-
ATOM    506  N   PRO A  63      -2.487   4.223 -32.512  1.00 43.52           N  
ANISOU  506  N   PRO A  63     5451   5967   5118   -221    -24    243       N  
ATOM    507  CA  PRO A  63      -2.060   5.450 -33.192  1.00 41.85           C  
ANISOU  507  CA  PRO A  63     5345   5743   4813   -247     -4    256       C  
ATOM    508  C   PRO A  63      -0.541   5.529 -33.381  1.00 40.08           C  
ANISOU  508  C   PRO A  63     5146   5496   4586   -291    125    184       C  
ATOM    509  O   PRO A  63      -0.079   6.235 -34.271  1.00 42.43           O  
ANISOU  509  O   PRO A  63     5562   5771   4788   -351    175    167       O  
ATOM    510  CB  PRO A  63      -2.492   6.569 -32.235  1.00 41.34           C  
ANISOU  510  CB  PRO A  63     5236   5690   4782   -179    -45    325       C  
ATOM    511  CG  PRO A  63      -2.537   5.881 -30.902  1.00 41.23           C  
ANISOU  511  CG  PRO A  63     5095   5687   4885   -128    -33    325       C  
ATOM    512  CD  PRO A  63      -3.104   4.507 -31.208  1.00 41.98           C  
ANISOU  512  CD  PRO A  63     5164   5785   5002   -152    -60    295       C  
ATOM    513  N   LEU A  64       0.198   4.837 -32.520  1.00 36.65           N  
ANISOU  513  N   LEU A  64     4607   5058   4261   -261    175    136       N  
ATOM    514  CA  LEU A  64       1.660   4.678 -32.671  1.00 35.68           C  
ANISOU  514  CA  LEU A  64     4470   4908   4179   -296    289     34       C  
ATOM    515  C   LEU A  64       1.949   4.030 -34.022  1.00 35.07           C  
ANISOU  515  C   LEU A  64     4474   4814   4036   -389    349    -41       C  
ATOM    516  O   LEU A  64       2.791   4.575 -34.786  1.00 33.97           O  
ANISOU  516  O   LEU A  64     4412   4650   3845   -464    455   -106       O  
ATOM    517  CB  LEU A  64       2.194   3.819 -31.526  1.00 35.86           C  
ANISOU  517  CB  LEU A  64     4370   4917   4338   -230    283     -7       C  
ATOM    518  CG  LEU A  64       3.700   3.546 -31.611  1.00 36.53           C  
ANISOU  518  CG  LEU A  64     4408   4968   4506   -250    379   -137       C  
ATOM    519  CD1 LEU A  64       4.485   4.805 -31.896  1.00 36.66           C  
ANISOU  519  CD1 LEU A  64     4456   4977   4494   -289    469   -171       C  
ATOM    520  CD2 LEU A  64       4.239   2.921 -30.351  1.00 36.77           C  
ANISOU  520  CD2 LEU A  64     4333   4970   4670   -164    336   -169       C  
ATOM    521  N   TRP A  65       1.272   2.914 -34.309  1.00 34.08           N  
ANISOU  521  N   TRP A  65     4340   4696   3912   -394    295    -40       N  
ATOM    522  CA  TRP A  65       1.448   2.159 -35.580  1.00 35.24           C  
ANISOU  522  CA  TRP A  65     4567   4826   3996   -484    344   -111       C  
ATOM    523  C   TRP A  65       1.011   3.050 -36.742  1.00 37.72           C  
ANISOU  523  C   TRP A  65     5054   5133   4146   -555    335    -74       C  
ATOM    524  O   TRP A  65       1.748   3.150 -37.723  1.00 38.26           O  
ANISOU  524  O   TRP A  65     5228   5168   4140   -650    442   -149       O  
ATOM    525  CB  TRP A  65       0.702   0.822 -35.544  1.00 33.93           C  
ANISOU  525  CB  TRP A  65     4354   4670   3868   -468    275   -109       C  
ATOM    526  CG  TRP A  65       1.421  -0.226 -34.747  1.00 32.65           C  
ANISOU  526  CG  TRP A  65     4075   4487   3844   -427    305   -176       C  
ATOM    527  CD1 TRP A  65       1.623  -0.234 -33.399  1.00 31.64           C  
ANISOU  527  CD1 TRP A  65     3850   4351   3819   -340    273   -153       C  
ATOM    528  CD2 TRP A  65       2.085  -1.399 -35.248  1.00 32.20           C  
ANISOU  528  CD2 TRP A  65     3999   4400   3836   -466    365   -284       C  
ATOM    529  CE2 TRP A  65       2.642  -2.072 -34.145  1.00 31.48           C  
ANISOU  529  CE2 TRP A  65     3799   4279   3883   -391    349   -319       C  
ATOM    530  CE3 TRP A  65       2.245  -1.954 -36.519  1.00 32.99           C  
ANISOU  530  CE3 TRP A  65     4174   4488   3874   -559    426   -357       C  
ATOM    531  NE1 TRP A  65       2.345  -1.336 -33.032  1.00 31.23           N  
ANISOU  531  NE1 TRP A  65     3733   4260   3873   -317    291   -234       N  
ATOM    532  CZ2 TRP A  65       3.323  -3.280 -34.268  1.00 31.50           C  
ANISOU  532  CZ2 TRP A  65     3754   4238   3974   -395    380   -424       C  
ATOM    533  CZ3 TRP A  65       2.947  -3.128 -36.649  1.00 33.22           C  
ANISOU  533  CZ3 TRP A  65     4147   4482   3993   -572    477   -466       C  
ATOM    534  CH2 TRP A  65       3.468  -3.784 -35.537  1.00 32.61           C  
ANISOU  534  CH2 TRP A  65     3951   4375   4065   -486    449   -500       C  
ATOM    535  N   LYS A  66      -0.131   3.717 -36.591  1.00 40.88           N  
ANISOU  535  N   LYS A  66     5486   5551   4494   -509    211     30       N  
ATOM    536  CA  LYS A  66      -0.615   4.776 -37.521  1.00 43.21           C  
ANISOU  536  CA  LYS A  66     5960   5825   4635   -550    162     82       C  
ATOM    537  C   LYS A  66       0.523   5.775 -37.780  1.00 41.59           C  
ANISOU  537  C   LYS A  66     5845   5583   4373   -609    295     44       C  
ATOM    538  O   LYS A  66       0.936   5.925 -38.950  1.00 41.79           O  
ANISOU  538  O   LYS A  66     6044   5564   4270   -714    369     -2       O  
ATOM    539  CB  LYS A  66      -1.869   5.450 -36.947  1.00 46.13           C  
ANISOU  539  CB  LYS A  66     6294   6216   5016   -461      8    185       C  
ATOM    540  CG  LYS A  66      -2.607   6.329 -37.948  1.00 50.72           C  
ANISOU  540  CG  LYS A  66     7059   6763   5449   -483   -100    237       C  
ATOM    541  CD  LYS A  66      -4.093   6.450 -37.719  1.00 55.66           C  
ANISOU  541  CD  LYS A  66     7632   7406   6109   -404   -285    299       C  
ATOM    542  CE  LYS A  66      -4.711   7.421 -38.700  1.00 60.62           C  
ANISOU  542  CE  LYS A  66     8457   7983   6594   -413   -414    344       C  
ATOM    543  NZ  LYS A  66      -3.995   8.729 -38.705  1.00 64.22           N1+
ANISOU  543  NZ  LYS A  66     9033   8398   6969   -428   -350    375       N1+
ATOM    544  N   GLY A  67       1.032   6.393 -36.717  1.00 39.41           N  
ANISOU  544  N   GLY A  67     5464   5320   4191   -551    333     55       N  
ATOM    545  CA  GLY A  67       2.120   7.383 -36.790  1.00 40.36           C  
ANISOU  545  CA  GLY A  67     5641   5407   4285   -602    464     11       C  
ATOM    546  C   GLY A  67       3.262   6.867 -37.637  1.00 41.01           C  
ANISOU  546  C   GLY A  67     5775   5455   4353   -716    631   -123       C  
ATOM    547  O   GLY A  67       3.488   7.397 -38.729  1.00 44.28           O  
ANISOU  547  O   GLY A  67     6383   5820   4620   -824    706   -146       O  
ATOM    548  N   LEU A  68       3.932   5.826 -37.157  1.00 39.97           N  
ANISOU  548  N   LEU A  68     5482   5336   4368   -696    685   -215       N  
ATOM    549  CA  LEU A  68       5.083   5.186 -37.842  1.00 39.81           C  
ANISOU  549  CA  LEU A  68     5462   5281   4383   -795    849   -373       C  
ATOM    550  C   LEU A  68       4.743   4.865 -39.298  1.00 40.16           C  
ANISOU  550  C   LEU A  68     5701   5296   4263   -911    882   -389       C  
ATOM    551  O   LEU A  68       5.633   5.015 -40.132  1.00 41.30           O  
ANISOU  551  O   LEU A  68     5941   5392   4357  -1035   1051   -501       O  
ATOM    552  CB  LEU A  68       5.464   3.913 -37.087  1.00 39.53           C  
ANISOU  552  CB  LEU A  68     5229   5262   4530   -725    830   -444       C  
ATOM    553  CG  LEU A  68       6.399   4.113 -35.904  1.00 39.64           C  
ANISOU  553  CG  LEU A  68     5071   5273   4717   -650    857   -504       C  
ATOM    554  CD1 LEU A  68       6.728   2.780 -35.244  1.00 40.00           C  
ANISOU  554  CD1 LEU A  68     4959   5313   4926   -577    811   -572       C  
ATOM    555  CD2 LEU A  68       7.678   4.813 -36.326  1.00 40.53           C  
ANISOU  555  CD2 LEU A  68     5198   5347   4856   -741   1037   -639       C  
ATOM    556  N   SER A  69       3.525   4.415 -39.599  1.00 39.61           N  
ANISOU  556  N   SER A  69     5687   5246   4115   -881    733   -296       N  
ATOM    557  CA  SER A  69       3.122   4.026 -40.976  1.00 40.21           C  
ANISOU  557  CA  SER A  69     5958   5291   4031   -983    735   -310       C  
ATOM    558  C   SER A  69       3.350   5.232 -41.890  1.00 40.80           C  
ANISOU  558  C   SER A  69     6281   5304   3918  -1089    808   -300       C  
ATOM    559  O   SER A  69       3.862   5.042 -43.016  1.00 41.80           O  
ANISOU  559  O   SER A  69     6574   5377   3931  -1227    937   -387       O  
ATOM    560  CB  SER A  69       1.694   3.495 -41.056  1.00 39.52           C  
ANISOU  560  CB  SER A  69     5877   5233   3903   -920    537   -211       C  
ATOM    561  OG  SER A  69       0.740   4.547 -41.100  1.00 39.47           O  
ANISOU  561  OG  SER A  69     5980   5223   3793   -877    397    -91       O  
ATOM    562  N   GLU A  70       3.030   6.424 -41.389  1.00 40.11           N  
ANISOU  562  N   GLU A  70     6224   5216   3799  -1032    739   -204       N  
ATOM    563  CA  GLU A  70       3.141   7.702 -42.127  1.00 41.70           C  
ANISOU  563  CA  GLU A  70     6679   5348   3815  -1117    783   -173       C  
ATOM    564  C   GLU A  70       4.597   8.155 -42.153  1.00 22.26           C  
ATOM    565  O   GLU A  70       5.155   8.323 -43.243  1.00 45.80           O  
ANISOU  565  O   GLU A  70     7411   5759   4232  -1371   1178   -374       O  
ATOM    566  CB  GLU A  70       2.265   8.748 -41.458  1.00 41.15           C  
ANISOU  566  CB  GLU A  70     6609   5293   3733  -1004    614    -33       C  
ATOM    567  CG  GLU A  70       0.799   8.432 -41.599  1.00 41.83           C  
ANISOU  567  CG  GLU A  70     6715   5400   3779   -921    379     68       C  
ATOM    568  CD  GLU A  70      -0.103   9.086 -40.583  1.00 41.41           C  
ANISOU  568  CD  GLU A  70     6541   5385   3807   -779    214    176       C  
ATOM    569  OE1 GLU A  70       0.426   9.722 -39.643  1.00 40.96           O  
ANISOU  569  OE1 GLU A  70     6372   5348   3844   -737    280    181       O  
ATOM    570  OE2 GLU A  70      -1.339   8.934 -40.742  1.00 42.89           O1-
ANISOU  570  OE2 GLU A  70     6742   5581   3973   -715     20    242       O1-
ATOM    571  N   ARG A  71       5.197   8.339 -40.994  1.00 42.38           N  
ANISOU  571  N   ARG A  71     6544   5438   4122  -1142   1068   -327       N  
ATOM    572  CA  ARG A  71       6.547   8.930 -40.891  1.00 43.76           C  
ANISOU  572  CA  ARG A  71     6693   5576   4356  -1224   1284   -451       C  
ATOM    573  C   ARG A  71       7.563   8.048 -41.632  1.00 45.37           C  
ANISOU  573  C   ARG A  71     6887   5748   4603  -1352   1484   -636       C  
ATOM    574  O   ARG A  71       8.515   8.595 -42.218  1.00 47.51           O  
ANISOU  574  O   ARG A  71     7266   5957   4829  -1494   1696   -752       O  
ATOM    575  CB  ARG A  71       6.927   9.081 -39.419  1.00 43.51           C  
ANISOU  575  CB  ARG A  71     6395   5598   4536  -1096   1251   -454       C  
ATOM    576  CG  ARG A  71       5.897   9.776 -38.542  1.00 43.06           C  
ANISOU  576  CG  ARG A  71     6309   5581   4471   -960   1057   -286       C  
ATOM    577  CD  ARG A  71       6.699  10.759 -37.743  1.00 44.21           C  
ANISOU  577  CD  ARG A  71     6373   5722   4703   -943   1140   -317       C  
ATOM    578  NE  ARG A  71       5.968  11.454 -36.711  1.00 44.81           N  
ANISOU  578  NE  ARG A  71     6381   5834   4809   -814    990   -185       N  
ATOM    579  CZ  ARG A  71       6.464  12.480 -36.026  1.00 47.76           C  
ANISOU  579  CZ  ARG A  71     6715   6202   5231   -793   1037   -185       C  
ATOM    580  NH1 ARG A  71       7.697  12.928 -36.279  1.00 48.25           N1+
ANISOU  580  NH1 ARG A  71     6791   6223   5321   -894   1230   -316       N1+
ATOM    581  NH2 ARG A  71       5.721  13.034 -35.064  1.00 48.29           N  
ANISOU  581  NH2 ARG A  71     6717   6304   5328   -674    897    -66       N  
ATOM    582  N   ARG A  72       7.395   6.726 -41.596  1.00 45.20           N  
ANISOU  582  N   ARG A  72     6737   5762   4674  -1312   1433   -675       N  
ATOM    583  CA  ARG A  72       8.308   5.753 -42.255  1.00 46.57           C  
ANISOU  583  CA  ARG A  72     6874   5906   4915  -1420   1610   -859       C  
ATOM    584  C   ARG A  72       7.843   5.497 -43.688  1.00 46.51           C  
ANISOU  584  C   ARG A  72     7139   5850   4683  -1553   1642   -852       C  
ATOM    585  O   ARG A  72       8.630   4.947 -44.476  1.00 46.87           O  
ANISOU  585  O   ARG A  72     7225   5851   4732  -1686   1831  -1012       O  
ATOM    586  CB  ARG A  72       8.344   4.430 -41.484  1.00 47.43           C  
ANISOU  586  CB  ARG A  72     6723   6066   5233  -1304   1525   -902       C  
ATOM    587  CG  ARG A  72       8.789   4.558 -40.039  1.00 47.56           C  
ANISOU  587  CG  ARG A  72     6489   6119   5464  -1166   1468   -910       C  
ATOM    588  CD  ARG A  72      10.007   5.436 -39.933  1.00 50.20           C  
ANISOU  588  CD  ARG A  72     6787   6414   5871  -1234   1650  -1040       C  
ATOM    589  NE  ARG A  72      10.844   5.136 -38.783  1.00 51.90           N  
ANISOU  589  NE  ARG A  72     6737   6644   6340  -1131   1638  -1139       N  
ATOM    590  CZ  ARG A  72      11.971   5.775 -38.498  1.00 53.49           C  
ANISOU  590  CZ  ARG A  72     6846   6816   6662  -1166   1776  -1276       C  
ATOM    591  NH1 ARG A  72      12.395   6.768 -39.270  1.00 55.95           N1+
ANISOU  591  NH1 ARG A  72     7316   7083   6858  -1314   1958  -1328       N1+
ATOM    592  NH2 ARG A  72      12.665   5.424 -37.431  1.00 52.82           N  
ANISOU  592  NH2 ARG A  72     6521   6738   6811  -1055   1726  -1365       N  
ATOM    593  N   GLY A  73       6.580   5.798 -43.976  1.00 46.27           N  
ANISOU  593  N   GLY A  73     7274   5826   4481  -1510   1451   -683       N  
ATOM    594  CA  GLY A  73       5.983   5.686 -45.321  1.00 47.42           C  
ANISOU  594  CA  GLY A  73     7715   5916   4387  -1621   1430   -652       C  
ATOM    595  C   GLY A  73       5.814   4.251 -45.773  1.00 46.18           C  
ANISOU  595  C   GLY A  73     7501   5778   4268  -1638   1419   -717       C  
ATOM    596  O   GLY A  73       5.981   4.007 -46.971  1.00 46.79           O  
ANISOU  596  O   GLY A  73     7797   5793   4189  -1786   1525   -784       O  
ATOM    597  N   TRP A  74       5.513   3.335 -44.855  1.00 43.63           N  
ANISOU  597  N   TRP A  74     6912   5530   4137  -1501   1304   -700       N  
ATOM    598  CA  TRP A  74       5.085   1.975 -45.247  1.00 43.50           C  
ANISOU  598  CA  TRP A  74     6855   5531   4141  -1499   1247   -730       C  
ATOM    599  C   TRP A  74       3.559   1.924 -45.238  1.00 43.50           C  
ANISOU  599  C   TRP A  74     6914   5565   4048  -1407    991   -567       C  
ATOM    600  O   TRP A  74       3.024   0.910 -45.651  1.00 43.06           O  
ANISOU  600  O   TRP A  74     6857   5521   3981  -1410    923   -575       O  
ATOM    601  CB  TRP A  74       5.740   0.858 -44.422  1.00 41.88           C  
ANISOU  601  CB  TRP A  74     6358   5364   4190  -1429   1294   -836       C  
ATOM    602  CG  TRP A  74       5.882   1.060 -42.945  1.00 39.73           C  
ANISOU  602  CG  TRP A  74     5845   5140   4110  -1279   1218   -795       C  
ATOM    603  CD1 TRP A  74       7.022   1.369 -42.265  1.00 39.36           C  
ANISOU  603  CD1 TRP A  74     5649   5084   4223  -1263   1337   -897       C  
ATOM    604  CD2 TRP A  74       4.881   0.838 -41.938  1.00 37.90           C  
ANISOU  604  CD2 TRP A  74     5489   4966   3945  -1126   1011   -660       C  
ATOM    605  CE2 TRP A  74       5.481   1.085 -40.692  1.00 36.72           C  
ANISOU  605  CE2 TRP A  74     5146   4834   3969  -1030   1016   -675       C  
ATOM    606  CE3 TRP A  74       3.530   0.494 -41.972  1.00 37.34           C  
ANISOU  606  CE3 TRP A  74     5456   4928   3805  -1069    827   -536       C  
ATOM    607  NE1 TRP A  74       6.788   1.397 -40.918  1.00 37.73           N  
ANISOU  607  NE1 TRP A  74     5256   4922   4157  -1109   1205   -822       N  
ATOM    608  CZ2 TRP A  74       4.776   1.000 -39.501  1.00 35.23           C  
ANISOU  608  CZ2 TRP A  74     4827   4691   3867   -888    855   -565       C  
ATOM    609  CZ3 TRP A  74       2.834   0.415 -40.794  1.00 35.66           C  
ANISOU  609  CZ3 TRP A  74     5091   4762   3694   -933    681   -439       C  
ATOM    610  CH2 TRP A  74       3.454   0.660 -39.577  1.00 34.64           C  
ANISOU  610  CH2 TRP A  74     4796   4646   3719   -848    701   -450       C  
ATOM    611  N   ASP A  75       2.896   3.019 -44.872  1.00 44.53           N  
ANISOU  611  N   ASP A  75     7105   5701   4112  -1338    860   -436       N  
ATOM    612  CA  ASP A  75       1.436   3.209 -45.095  1.00 47.07           C  
ANISOU  612  CA  ASP A  75     7527   6032   4325  -1271    618   -300       C  
ATOM    613  C   ASP A  75       1.117   3.065 -46.589  1.00 26.80           C  
ATOM    614  O   ASP A  75       0.019   2.626 -46.942  1.00 53.64           O  
ANISOU  614  O   ASP A  75     8698   6806   4876  -1353    417   -258       O  
ATOM    615  CB  ASP A  75       0.926   4.554 -44.576  1.00 47.73           C  
ANISOU  615  CB  ASP A  75     7652   6113   4370  -1192    502   -180       C  
ATOM    616  CG  ASP A  75       1.585   5.784 -45.174  1.00 49.59           C  
ANISOU  616  CG  ASP A  75     8127   6270   4446  -1295    620   -188       C  
ATOM    617  OD1 ASP A  75       2.603   5.622 -45.881  1.00 51.41           O1-
ANISOU  617  OD1 ASP A  75     8467   6451   4616  -1438    831   -304       O1-
ATOM    618  OD2 ASP A  75       1.087   6.902 -44.890  1.00 27.79           O1-
ATOM    619  N   GLN A  76       2.054   3.390 -47.464  1.00 53.16           N  
ANISOU  619  N   GLN A  76     8796   6661   4739  -1550    802   -404       N  
ATOM    620  CA  GLN A  76       1.813   3.380 -48.924  1.00 55.54           C  
ANISOU  620  CA  GLN A  76     9436   6878   4789  -1686    802   -417       C  
ATOM    621  C   GLN A  76       1.780   1.930 -49.429  1.00 55.84           C  
ANISOU  621  C   GLN A  76     9419   6935   4862  -1731    832   -505       C  
ATOM    622  O   GLN A  76       1.454   1.750 -50.593  1.00 58.21           O  
ANISOU  622  O   GLN A  76     9982   7172   4962  -1832    804   -515       O  
ATOM    623  CB  GLN A  76       2.850   4.250 -49.623  1.00 57.45           C  
ANISOU  623  CB  GLN A  76     9925   7025   4877  -1852   1031   -489       C  
ATOM    624  CG  GLN A  76       2.896   5.680 -49.081  1.00 57.89           C  
ANISOU  624  CG  GLN A  76    10031   7060   4906  -1806   1005   -403       C  
ATOM    625  CD  GLN A  76       4.274   6.274 -49.268  1.00 60.56           C  
ANISOU  625  CD  GLN A  76    10446   7339   5226  -1953   1305   -523       C  
ATOM    626  NE2 GLN A  76       4.881   6.800 -48.204  1.00 58.74           N  
ANISOU  626  NE2 GLN A  76     9995   7152   5173  -1887   1380   -538       N  
ATOM    627  OE1 GLN A  76       4.798   6.248 -50.381  1.00 64.24           O  
ANISOU  627  OE1 GLN A  76    11175   7715   5519  -2135   1476   -612       O  
ATOM    628  N   TYR A  77       2.064   0.929 -48.587  1.00 54.24           N  
ANISOU  628  N   TYR A  77     8904   6808   4896  -1657    870   -564       N  
ATOM    629  CA  TYR A  77       1.984  -0.523 -48.923  1.00 53.93           C  
ANISOU  629  CA  TYR A  77     8781   6790   4920  -1680    884   -643       C  
ATOM    630  C   TYR A  77       0.720  -1.158 -48.332  1.00 52.07           C  
ANISOU  630  C   TYR A  77     8385   6623   4776  -1535    641   -546       C  
ATOM    631  O   TYR A  77       0.461  -2.359 -48.519  1.00 49.78           O  
ANISOU  631  O   TYR A  77     8018   6354   4542  -1538    618   -593       O  
ATOM    632  CB  TYR A  77       3.205  -1.282 -48.406  1.00 53.48           C  
ANISOU  632  CB  TYR A  77     8494   6752   5074  -1697   1093   -791       C  
ATOM    633  CG  TYR A  77       4.534  -0.784 -48.899  1.00 55.27           C  
ANISOU  633  CG  TYR A  77     8820   6914   5266  -1843   1362   -926       C  
ATOM    634  CD1 TYR A  77       5.030  -1.140 -50.141  1.00 58.30           C  
ANISOU  634  CD1 TYR A  77     9409   7228   5514  -2020   1533  -1047       C  
ATOM    635  CD2 TYR A  77       5.313   0.036 -48.115  1.00 55.79           C  
ANISOU  635  CD2 TYR A  77     8771   6985   5442  -1813   1458   -949       C  
ATOM    636  CE1 TYR A  77       6.263  -0.685 -50.596  1.00 60.50           C  
ANISOU  636  CE1 TYR A  77     9775   7441   5772  -2172   1809  -1193       C  
ATOM    637  CE2 TYR A  77       6.551   0.492 -48.542  1.00 57.85           C  
ANISOU  637  CE2 TYR A  77     9102   7184   5694  -1955   1720  -1094       C  
ATOM    638  CZ  TYR A  77       7.032   0.134 -49.787  1.00 59.46           C  
ANISOU  638  CZ  TYR A  77     9508   7316   5768  -2139   1905  -1222       C  
ATOM    639  OH  TYR A  77       8.255   0.583 -50.188  1.00 60.18           O  
ANISOU  639  OH  TYR A  77     9661   7342   5864  -2292   2187  -1384       O  
ATOM    640  N   LEU A  78      -0.090  -0.358 -47.657  1.00 52.11           N  
ANISOU  640  N   LEU A  78     8346   6657   4796  -1419    465   -420       N  
ATOM    641  CA  LEU A  78      -1.245  -0.880 -46.888  1.00 52.67           C  
ANISOU  641  CA  LEU A  78     8226   6795   4993  -1281    262   -343       C  
ATOM    642  C   LEU A  78      -2.554  -0.496 -47.580  1.00 57.70           C  
ANISOU  642  C   LEU A  78     9035   7409   5481  -1261     30   -259       C  
ATOM    643  O   LEU A  78      -2.587   0.528 -48.298  1.00 61.94           O  
ANISOU  643  O   LEU A  78     9824   7880   5831  -1312     -5   -220       O  
ATOM    644  CB  LEU A  78      -1.182  -0.331 -45.466  1.00 49.25           C  
ANISOU  644  CB  LEU A  78     7575   6411   4725  -1158    243   -284       C  
ATOM    645  CG  LEU A  78       0.032  -0.753 -44.639  1.00 46.72           C  
ANISOU  645  CG  LEU A  78     7063   6111   4579  -1150    426   -369       C  
ATOM    646  CD1 LEU A  78      -0.122  -0.268 -43.200  1.00 45.13           C  
ANISOU  646  CD1 LEU A  78     6664   5956   4526  -1019    366   -296       C  
ATOM    647  CD2 LEU A  78       0.257  -2.257 -44.655  1.00 45.71           C  
ANISOU  647  CD2 LEU A  78     6813   5997   4559  -1164    479   -459       C  
ATOM    648  N   PHE A  79      -3.584  -1.321 -47.379  1.00 61.76           N  
ANISOU  648  N   PHE A  79     9422   7965   6078  -1192   -125   -241       N  
ATOM    649  CA  PHE A  79      -4.923  -1.188 -48.011  1.00 64.50           C  
ANISOU  649  CA  PHE A  79     9884   8293   6329  -1160   -371   -188       C  
ATOM    650  C   PHE A  79      -4.692  -1.277 -49.525  1.00 70.12           C  
ANISOU  650  C   PHE A  79    10910   8925   6806  -1297   -349   -234       C  
ATOM    651  O   PHE A  79      -3.846  -2.100 -49.930  1.00 66.78           O  
ANISOU  651  O   PHE A  79    10505   8495   6375  -1398   -163   -327       O  
ATOM    652  CB  PHE A  79      -5.606   0.063 -47.442  1.00 62.13           C  
ANISOU  652  CB  PHE A  79     9571   7994   6043  -1054   -529    -89       C  
ATOM    653  CG  PHE A  79      -5.466   0.220 -45.939  1.00 59.44           C  
ANISOU  653  CG  PHE A  79     8953   7722   5912   -952   -475    -58       C  
ATOM    654  CD1 PHE A  79      -6.224  -0.542 -45.053  1.00 58.68           C  
ANISOU  654  CD1 PHE A  79     8606   7688   6000   -867   -546    -56       C  
ATOM    655  CD2 PHE A  79      -4.518   1.079 -45.400  1.00 57.72           C  
ANISOU  655  CD2 PHE A  79     8731   7497   5701   -954   -337    -40       C  
ATOM    656  CE1 PHE A  79      -6.070  -0.412 -43.677  1.00 56.20           C  
ANISOU  656  CE1 PHE A  79     8073   7423   5856   -786   -489    -29       C  
ATOM    657  CE2 PHE A  79      -4.379   1.220 -44.022  1.00 55.40           C  
ANISOU  657  CE2 PHE A  79     8202   7260   5589   -862   -297    -13       C  
ATOM    658  CZ  PHE A  79      -5.147   0.470 -43.164  1.00 54.59           C  
ANISOU  658  CZ  PHE A  79     7877   7213   5651   -780   -373     -5       C  
ATOM    659  N   LYS A  80      -5.355  -0.433 -50.314  1.00 80.70           N  
ANISOU  659  N   LYS A  80    12502  10198   7964  -1302   -527   -178       N  
ATOM    660  CA  LYS A  80      -5.237  -0.412 -51.802  1.00 92.37           C  
ANISOU  660  CA  LYS A  80    14338  11579   9180  -1435   -535   -210       C  
ATOM    661  C   LYS A  80      -5.536  -1.821 -52.385  1.00106.74           C  
ANISOU  661  C   LYS A  80    16128  13416  11011  -1486   -547   -288       C  
ATOM    662  O   LYS A  80      -4.866  -2.195 -53.382  1.00115.40           O  
ANISOU  662  O   LYS A  80    17443  14454  11949  -1632   -405   -360       O  
ATOM    663  CB  LYS A  80      -3.861   0.157 -52.192  1.00 89.09           C  
ANISOU  663  CB  LYS A  80    14115  11102   8634  -1572   -270   -252       C  
ATOM    664  CG  LYS A  80      -3.624   1.597 -51.762  1.00 85.87           C  
ANISOU  664  CG  LYS A  80    13780  10662   8186  -1535   -270   -175       C  
ATOM    665  CD  LYS A  80      -2.206   2.106 -51.957  1.00 84.66           C  
ANISOU  665  CD  LYS A  80    13754  10459   7953  -1669     24   -236       C  
ATOM    666  CE  LYS A  80      -1.606   2.751 -50.714  1.00 82.74           C  
ANISOU  666  CE  LYS A  80    13277  10271   7888  -1594    132   -214       C  
ATOM    667  NZ  LYS A  80      -2.513   3.696 -50.009  1.00 79.78           N1+
ANISOU  667  NZ  LYS A  80    12840   9914   7558  -1444    -92    -91       N1+
ATOM    668  N   ASN A  81      -6.518  -2.554 -51.802  1.00117.84           N  
ANISOU  668  N   ASN A  81    17285  14893  12595  -1378   -701   -281       N  
ATOM    669  CA  ASN A  81      -7.202  -3.814 -52.266  1.00120.14           C  
ANISOU  669  CA  ASN A  81    17525  15204  12919  -1393   -791   -340       C  
ATOM    670  C   ASN A  81      -6.286  -4.738 -53.105  1.00128.05           C  
ANISOU  670  C   ASN A  81    18652  16177  13825  -1545   -583   -440       C  
ATOM    671  O   ASN A  81      -5.831  -5.758 -52.529  1.00129.67           O  
ANISOU  671  O   ASN A  81    18629  16440  14201  -1546   -432   -501       O  
ATOM    672  CB  ASN A  81      -8.531  -3.552 -53.005  1.00116.43           C  
ANISOU  672  CB  ASN A  81    17203  14689  12346  -1349  -1106   -309       C  
ATOM    673  CG  ASN A  81      -9.240  -2.268 -52.611  1.00111.81           C  
ANISOU  673  CG  ASN A  81    16631  14084  11768  -1232  -1312   -220       C  
ATOM    674  ND2 ASN A  81      -9.509  -1.416 -53.591  1.00109.27           N  
ANISOU  674  ND2 ASN A  81    16639  13660  11220  -1258  -1473   -184       N  
ATOM    675  OD1 ASN A  81      -9.559  -2.048 -51.441  1.00101.55           O  
ANISOU  675  OD1 ASN A  81    15059  12853  10673  -1121  -1330   -186       O  
ATOM    676  N   ARG A  82      -6.059  -4.438 -54.402  1.00133.18           N  
ANISOU  676  N   ARG A  82    19657  16732  14215  -1669   -579   -461       N  
ATOM    677  CA  ARG A  82      -5.293  -5.294 -55.367  1.00133.68           C  
ANISOU  677  CA  ARG A  82    19880  16753  14161  -1830   -388   -569       C  
ATOM    678  C   ARG A  82      -3.784  -5.072 -55.193  1.00137.61           C  
ANISOU  678  C   ARG A  82    20382  17236  14668  -1928    -63   -632       C  
ATOM    679  O   ARG A  82      -3.350  -3.977 -54.830  1.00137.32           O  
ANISOU  679  O   ARG A  82    20390  17180  14605  -1914    -10   -583       O  
ATOM    680  CB  ARG A  82      -5.751  -5.061 -56.819  1.00129.52           C  
ANISOU  680  CB  ARG A  82    19753  16120  13340  -1928   -527   -569       C  
ATOM    681  CG  ARG A  82      -5.178  -3.833 -57.524  1.00126.23           C  
ANISOU  681  CG  ARG A  82    19707  15591  12664  -2028   -464   -538       C  
ATOM    682  CD  ARG A  82      -4.784  -4.115 -58.967  1.00125.74           C  
ANISOU  682  CD  ARG A  82    20031  15420  12324  -2219   -371   -611       C  
ATOM    683  NE  ARG A  82      -5.215  -3.100 -59.929  1.00128.31           N  
ANISOU  683  NE  ARG A  82    20791  15615  12346  -2265   -550   -545       N  
ATOM    684  CZ  ARG A  82      -4.500  -2.055 -60.369  1.00129.90           C  
ANISOU  684  CZ  ARG A  82    21307  15712  12337  -2374   -418   -527       C  
ATOM    685  NH1 ARG A  82      -3.274  -1.826 -59.930  1.00131.32           N1+
ANISOU  685  NH1 ARG A  82    21397  15910  12589  -2453    -91   -580       N1+
ATOM    686  NH2 ARG A  82      -5.025  -1.223 -61.254  1.00129.00           N  
ANISOU  686  NH2 ARG A  82    21608  15465  11939  -2404   -623   -460       N  
ATOM    687  N   PRO A  83      -2.928  -6.101 -55.433  1.00137.53           N  
ANISOU  687  N   PRO A  83    20312  17231  14711  -2028    165   -754       N  
ATOM    688  CA  PRO A  83      -1.471  -5.936 -55.336  1.00133.36           C  
ANISOU  688  CA  PRO A  83    19774  16680  14215  -2126    477   -847       C  
ATOM    689  C   PRO A  83      -0.909  -4.671 -56.031  1.00129.06           C  
ANISOU  689  C   PRO A  83    19562  16040  13436  -2244    576   -836       C  
ATOM    690  O   PRO A  83      -0.318  -3.857 -55.319  1.00124.37           O  
ANISOU  690  O   PRO A  83    18878  15457  12919  -2210    671   -815       O  
ATOM    691  CB  PRO A  83      -0.890  -7.239 -55.935  1.00134.01           C  
ANISOU  691  CB  PRO A  83    19842  16751  14324  -2240    655   -993       C  
ATOM    692  CG  PRO A  83      -2.077  -8.106 -56.352  1.00133.12           C  
ANISOU  692  CG  PRO A  83    19742  16657  14180  -2203    432   -966       C  
ATOM    693  CD  PRO A  83      -3.317  -7.488 -55.743  1.00134.11           C  
ANISOU  693  CD  PRO A  83    19791  16825  14339  -2043    135   -822       C  
ATOM    694  N   THR A  84      -1.103  -4.524 -57.357  1.00123.32           N  
ANISOU  694  N   THR A  84    19216  15213  12427  -2380    551   -850       N  
ATOM    695  CA  THR A  84      -0.617  -3.404 -58.230  1.00121.19           C  
ANISOU  695  CA  THR A  84    19348  14821  11878  -2526    651   -847       C  
ATOM    696  C   THR A  84       0.854  -3.668 -58.588  1.00116.22           C  
ANISOU  696  C   THR A  84    18757  14150  11252  -2710   1040  -1013       C  
ATOM    697  O   THR A  84       1.112  -4.343 -59.597  1.00109.23           O  
ANISOU  697  O   THR A  84    18065  13206  10234  -2863   1160  -1116       O  
ATOM    698  CB  THR A  84      -0.851  -2.012 -57.601  1.00121.25           C  
ANISOU  698  CB  THR A  84    19377  14821  11870  -2426    534   -719       C  
ATOM    699  CG2 THR A  84      -0.503  -0.865 -58.530  1.00120.64           C  
ANISOU  699  CG2 THR A  84    19749  14603  11484  -2572    601   -701       C  
ATOM    700  OG1 THR A  84      -2.216  -1.875 -57.197  1.00120.49           O  
ANISOU  700  OG1 THR A  84    19190  14769  11820  -2248    182   -592       O  
ATOM    701  N   ASP A  85       1.774  -3.146 -57.776  1.00116.07           N  
ANISOU  701  N   ASP A  85    18553  14159  11391  -2695   1229  -1049       N  
ATOM    702  CA  ASP A  85       3.216  -3.511 -57.743  1.00113.72           C  
ANISOU  702  CA  ASP A  85    18139  13850  11218  -2822   1592  -1233       C  
ATOM    703  C   ASP A  85       3.349  -4.834 -56.973  1.00108.61           C  
ANISOU  703  C   ASP A  85    17084  13306  10878  -2716   1604  -1306       C  
ATOM    704  O   ASP A  85       4.348  -5.561 -57.181  1.00107.73           O  
ANISOU  704  O   ASP A  85    16881  13180  10873  -2820   1861  -1483       O  
ATOM    705  CB  ASP A  85       4.006  -2.352 -57.134  1.00112.07           C  
ANISOU  705  CB  ASP A  85    17892  13628  11063  -2826   1736  -1233       C  
ATOM    706  CG  ASP A  85       3.703  -1.041 -57.842  1.00113.69           C  
ANISOU  706  CG  ASP A  85    18516  13724  10955  -2910   1679  -1135       C  
ATOM    707  OD1 ASP A  85       4.226  -0.848 -58.964  1.00114.15           O  
ANISOU  707  OD1 ASP A  85    18926  13666  10781  -3124   1875  -1223       O  
ATOM    708  OD2 ASP A  85       2.895  -0.255 -57.297  1.00109.86           O1-
ANISOU  708  OD2 ASP A  85    18021  13264  10455  -2764   1431   -972       O1-
ATOM    709  N   GLY A  86       2.356  -5.105 -56.115  1.00101.39           N  
ANISOU  709  N   GLY A  86    15943  12481  10098  -2519   1335  -1180       N  
ATOM    710  CA  GLY A  86       2.125  -6.370 -55.395  1.00 91.98           C  
ANISOU  710  CA  GLY A  86    14415  11378   9156  -2402   1271  -1207       C  
ATOM    711  C   GLY A  86       3.294  -6.749 -54.495  1.00 84.38           C  
ANISOU  711  C   GLY A  86    13141  10450   8469  -2371   1478  -1326       C  
ATOM    712  O   GLY A  86       3.910  -7.785 -54.732  1.00 86.49           O  
ANISOU  712  O   GLY A  86    13312  10708   8840  -2432   1629  -1471       O  
ATOM    713  N   PRO A  87       3.643  -5.947 -53.453  1.00 74.29           N  
ANISOU  713  N   PRO A  87    11698   9206   7322  -2273   1481  -1279       N  
ATOM    714  CA  PRO A  87       4.633  -6.383 -52.468  1.00 68.41           C  
ANISOU  714  CA  PRO A  87    10633   8496   6863  -2209   1618  -1384       C  
ATOM    715  C   PRO A  87       4.144  -7.723 -51.939  1.00 64.39           C  
ANISOU  715  C   PRO A  87     9895   8043   6527  -2097   1495  -1382       C  
ATOM    716  O   PRO A  87       3.002  -7.822 -51.504  1.00 63.61           O  
ANISOU  716  O   PRO A  87     9751   7995   6422  -1981   1262  -1241       O  
ATOM    717  CB  PRO A  87       4.676  -5.275 -51.411  1.00 66.24           C  
ANISOU  717  CB  PRO A  87    10248   8256   6663  -2095   1553  -1284       C  
ATOM    718  CG  PRO A  87       4.096  -4.074 -52.113  1.00 68.19           C  
ANISOU  718  CG  PRO A  87    10814   8459   6636  -2159   1480  -1172       C  
ATOM    719  CD  PRO A  87       3.138  -4.592 -53.172  1.00 71.36           C  
ANISOU  719  CD  PRO A  87    11442   8833   6837  -2217   1350  -1130       C  
ATOM    720  N   PRO A  88       4.958  -8.801 -51.971  1.00 61.81           N  
ANISOU  720  N   PRO A  88     9420   7702   6363  -2131   1647  -1545       N  
ATOM    721  CA  PRO A  88       4.474 -10.140 -51.615  1.00 61.32           C  
ANISOU  721  CA  PRO A  88     9187   7675   6438  -2044   1537  -1547       C  
ATOM    722  C   PRO A  88       4.237 -10.264 -50.095  1.00 58.19           C  
ANISOU  722  C   PRO A  88     8516   7337   6256  -1850   1391  -1459       C  
ATOM    723  O   PRO A  88       4.644  -9.360 -49.420  1.00 56.70           O  
ANISOU  723  O   PRO A  88     8264   7159   6121  -1800   1409  -1428       O  
ATOM    724  CB  PRO A  88       5.611 -11.046 -52.136  1.00 62.10           C  
ANISOU  724  CB  PRO A  88     9230   7720   6645  -2150   1770  -1767       C  
ATOM    725  CG  PRO A  88       6.848 -10.196 -51.994  1.00 62.26           C  
ANISOU  725  CG  PRO A  88     9219   7704   6733  -2207   1977  -1879       C  
ATOM    726  CD  PRO A  88       6.396  -8.778 -52.268  1.00 62.26           C  
ANISOU  726  CD  PRO A  88     9448   7702   6506  -2248   1930  -1746       C  
ATOM    727  N   ASN A  89       3.626 -11.344 -49.588  1.00 57.17           N  
ANISOU  727  N   ASN A  89     8245   7237   6239  -1756   1263  -1426       N  
ATOM    728  CA  ASN A  89       3.463 -11.559 -48.120  1.00 56.43           C  
ANISOU  728  CA  ASN A  89     7915   7182   6343  -1587   1143  -1355       C  
ATOM    729  C   ASN A  89       4.840 -11.475 -47.446  1.00 55.59           C  
ANISOU  729  C   ASN A  89     7643   7046   6434  -1553   1282  -1477       C  
ATOM    730  O   ASN A  89       4.954 -10.718 -46.446  1.00 54.51           O  
ANISOU  730  O   ASN A  89     7411   6933   6369  -1455   1226  -1405       O  
ATOM    731  CB  ASN A  89       2.787 -12.878 -47.713  1.00 57.14           C  
ANISOU  731  CB  ASN A  89     7892   7285   6533  -1514   1028  -1335       C  
ATOM    732  CG  ASN A  89       2.522 -12.972 -46.208  1.00 57.75           C  
ANISOU  732  CG  ASN A  89     7782   7388   6772  -1355    905  -1245       C  
ATOM    733  ND2 ASN A  89       3.199 -13.902 -45.539  1.00 57.07           N  
ANISOU  733  ND2 ASN A  89     7540   7266   6877  -1293    937  -1330       N  
ATOM    734  OD1 ASN A  89       1.718 -12.210 -45.631  1.00 56.69           O  
ANISOU  734  OD1 ASN A  89     7651   7298   6590  -1289    779  -1105       O  
ATOM    735  N   SER A  90       5.829 -12.205 -47.984  1.00 54.59           N  
ANISOU  735  N   SER A  90     7480   6867   6396  -1631   1450  -1663       N  
ATOM    736  CA  SER A  90       7.224 -12.272 -47.471  1.00 53.39           C  
ANISOU  736  CA  SER A  90     7151   6672   6464  -1605   1586  -1826       C  
ATOM    737  C   SER A  90       7.677 -10.900 -46.955  1.00 50.81           C  
ANISOU  737  C   SER A  90     6810   6358   6137  -1583   1619  -1791       C  
ATOM    738  O   SER A  90       8.369 -10.874 -45.921  1.00 49.42           O  
ANISOU  738  O   SER A  90     6441   6173   6165  -1475   1603  -1837       O  
ATOM    739  CB  SER A  90       8.163 -12.757 -48.540  1.00 56.18           C  
ANISOU  739  CB  SER A  90     7544   6964   6838  -1752   1809  -2041       C  
ATOM    740  OG  SER A  90       8.367 -11.751 -49.535  1.00 58.48           O  
ANISOU  740  OG  SER A  90     8047   7241   6934  -1912   1961  -2067       O  
ATOM    741  N   PHE A  91       7.300  -9.818 -47.651  1.00 48.69           N  
ANISOU  741  N   PHE A  91     6751   6103   5647  -1679   1653  -1715       N  
ATOM    742  CA  PHE A  91       7.711  -8.412 -47.372  1.00 47.34           C  
ANISOU  742  CA  PHE A  91     6615   5936   5438  -1689   1708  -1684       C  
ATOM    743  C   PHE A  91       7.137  -7.926 -46.035  1.00 45.33           C  
ANISOU  743  C   PHE A  91     6239   5736   5251  -1518   1513  -1518       C  
ATOM    744  O   PHE A  91       7.892  -7.363 -45.201  1.00 44.40           O  
ANISOU  744  O   PHE A  91     5985   5614   5271  -1455   1546  -1555       O  
ATOM    745  CB  PHE A  91       7.250  -7.485 -48.502  1.00 47.88           C  
ANISOU  745  CB  PHE A  91     6980   5990   5220  -1831   1757  -1621       C  
ATOM    746  CG  PHE A  91       7.234  -6.032 -48.127  1.00 46.85           C  
ANISOU  746  CG  PHE A  91     6916   5872   5013  -1814   1741  -1524       C  
ATOM    747  CD1 PHE A  91       8.411  -5.332 -47.977  1.00 47.17           C  
ANISOU  747  CD1 PHE A  91     6905   5879   5140  -1866   1926  -1647       C  
ATOM    748  CD2 PHE A  91       6.040  -5.394 -47.859  1.00 45.91           C  
ANISOU  748  CD2 PHE A  91     6888   5795   4759  -1737   1535  -1320       C  
ATOM    749  CE1 PHE A  91       8.391  -4.012 -47.556  1.00 47.15           C  
ANISOU  749  CE1 PHE A  91     6952   5886   5076  -1843   1906  -1555       C  
ATOM    750  CE2 PHE A  91       6.011  -4.082 -47.417  1.00 45.43           C  
ANISOU  750  CE2 PHE A  91     6869   5744   4647  -1705   1507  -1229       C  
ATOM    751  CZ  PHE A  91       7.189  -3.390 -47.275  1.00 46.16           C  
ANISOU  751  CZ  PHE A  91     6925   5804   4812  -1761   1694  -1341       C  
ATOM    752  N   TYR A  92       5.813  -8.086 -45.880  1.00 44.23           N  
ANISOU  752  N   TYR A  92     6156   5641   5009  -1455   1320  -1349       N  
ATOM    753  CA  TYR A  92       5.027  -7.663 -44.695  1.00 41.89           C  
ANISOU  753  CA  TYR A  92     5771   5395   4750  -1308   1133  -1183       C  
ATOM    754  C   TYR A  92       5.403  -8.535 -43.505  1.00 41.45           C  
ANISOU  754  C   TYR A  92     5491   5334   4925  -1180   1079  -1218       C  
ATOM    755  O   TYR A  92       5.394  -8.056 -42.368  1.00 39.95           O  
ANISOU  755  O   TYR A  92     5198   5161   4818  -1070    998  -1146       O  
ATOM    756  CB  TYR A  92       3.546  -7.793 -44.981  1.00 41.14           C  
ANISOU  756  CB  TYR A  92     5782   5338   4511  -1294    965  -1038       C  
ATOM    757  CG  TYR A  92       3.083  -6.933 -46.117  1.00 42.06           C  
ANISOU  757  CG  TYR A  92     6143   5446   4393  -1402    970   -992       C  
ATOM    758  CD1 TYR A  92       2.779  -5.597 -45.934  1.00 41.32           C  
ANISOU  758  CD1 TYR A  92     6133   5365   4202  -1382    916   -887       C  
ATOM    759  CD2 TYR A  92       2.901  -7.473 -47.375  1.00 43.77           C  
ANISOU  759  CD2 TYR A  92     6523   5633   4474  -1522   1015  -1049       C  
ATOM    760  CE1 TYR A  92       2.325  -4.807 -46.976  1.00 42.19           C  
ANISOU  760  CE1 TYR A  92     6495   5450   4085  -1473    897   -839       C  
ATOM    761  CE2 TYR A  92       2.420  -6.701 -48.422  1.00 44.82           C  
ANISOU  761  CE2 TYR A  92     6916   5743   4371  -1617    992  -1000       C  
ATOM    762  CZ  TYR A  92       2.144  -5.361 -48.227  1.00 43.98           C  
ANISOU  762  CZ  TYR A  92     6902   5640   4169  -1591    929   -894       C  
ATOM    763  OH  TYR A  92       1.676  -4.629 -49.277  1.00 45.60           O  
ANISOU  763  OH  TYR A  92     7388   5804   4133  -1680    889   -847       O  
ATOM    764  N   ARG A  93       5.733  -9.793 -43.771  1.00 42.66           N  
ANISOU  764  N   ARG A  93     5585   5453   5172  -1196   1119  -1330       N  
ATOM    765  CA  ARG A  93       6.225 -10.722 -42.732  1.00 43.16           C  
ANISOU  765  CA  ARG A  93     5459   5484   5456  -1079   1068  -1387       C  
ATOM    766  C   ARG A  93       7.556 -10.186 -42.215  1.00 43.40           C  
ANISOU  766  C   ARG A  93     5368   5480   5643  -1048   1160  -1507       C  
ATOM    767  O   ARG A  93       7.742 -10.224 -40.999  1.00 45.08           O  
ANISOU  767  O   ARG A  93     5456   5683   5991   -918   1058  -1475       O  
ATOM    768  CB  ARG A  93       6.351 -12.134 -43.299  1.00 44.86           C  
ANISOU  768  CB  ARG A  93     5657   5659   5730  -1117   1104  -1497       C  
ATOM    769  CG  ARG A  93       6.687 -13.175 -42.248  1.00 45.30           C  
ANISOU  769  CG  ARG A  93     5554   5667   5992   -989   1017  -1536       C  
ATOM    770  CD  ARG A  93       7.343 -14.381 -42.848  1.00 47.70           C  
ANISOU  770  CD  ARG A  93     5811   5908   6403  -1032   1102  -1710       C  
ATOM    771  NE  ARG A  93       7.771 -15.247 -41.773  1.00 48.65           N  
ANISOU  771  NE  ARG A  93     5792   5966   6726   -896   1002  -1750       N  
ATOM    772  CZ  ARG A  93       8.724 -16.157 -41.876  1.00 51.48           C  
ANISOU  772  CZ  ARG A  93     6049   6246   7264   -880   1053  -1931       C  
ATOM    773  NH1 ARG A  93       9.333 -16.382 -43.035  1.00 53.64           N1+
ANISOU  773  NH1 ARG A  93     6335   6500   7545  -1002   1224  -2098       N1+
ATOM    774  NH2 ARG A  93       9.021 -16.883 -40.812  1.00 52.33           N  
ANISOU  774  NH2 ARG A  93     6057   6286   7540   -741    924  -1946       N  
ATOM    775  N   SER A  94       8.417  -9.670 -43.091  1.00 44.07           N  
ANISOU  775  N   SER A  94     5497   5543   5706  -1168   1346  -1643       N  
ATOM    776  CA  SER A  94       9.774  -9.165 -42.748  1.00 45.35           C  
ANISOU  776  CA  SER A  94     5529   5665   6035  -1162   1464  -1800       C  
ATOM    777  C   SER A  94       9.668  -7.840 -41.989  1.00 44.05           C  
ANISOU  777  C   SER A  94     5367   5538   5832  -1106   1411  -1684       C  
ATOM    778  O   SER A  94      10.559  -7.525 -41.190  1.00 43.58           O  
ANISOU  778  O   SER A  94     5159   5454   5945  -1034   1420  -1766       O  
ATOM    779  CB  SER A  94      10.632  -8.989 -43.987  1.00 47.31           C  
ANISOU  779  CB  SER A  94     5844   5875   6256  -1335   1707  -1988       C  
ATOM    780  OG  SER A  94      10.731 -10.208 -44.709  1.00 48.51           O  
ANISOU  780  OG  SER A  94     5997   5991   6444  -1392   1765  -2102       O  
ATOM    781  N   LEU A  95       8.627  -7.077 -42.277  1.00 43.23           N  
ANISOU  781  N   LEU A  95     5427   5485   5513  -1139   1354  -1510       N  
ATOM    782  CA  LEU A  95       8.452  -5.688 -41.801  1.00 42.51           C  
ANISOU  782  CA  LEU A  95     5378   5427   5348  -1114   1325  -1399       C  
ATOM    783  C   LEU A  95       8.016  -5.693 -40.336  1.00 41.74           C  
ANISOU  783  C   LEU A  95     5157   5356   5347   -945   1140  -1276       C  
ATOM    784  O   LEU A  95       8.587  -4.925 -39.546  1.00 42.06           O  
ANISOU  784  O   LEU A  95     5114   5394   5473   -886   1140  -1285       O  
ATOM    785  CB  LEU A  95       7.401  -5.040 -42.700  1.00 42.48           C  
ANISOU  785  CB  LEU A  95     5604   5454   5085  -1202   1303  -1265       C  
ATOM    786  CG  LEU A  95       7.009  -3.618 -42.350  1.00 41.77           C  
ANISOU  786  CG  LEU A  95     5590   5393   4889  -1179   1254  -1133       C  
ATOM    787  CD1 LEU A  95       8.224  -2.705 -42.353  1.00 42.61           C  
ANISOU  787  CD1 LEU A  95     5673   5466   5051  -1237   1424  -1251       C  
ATOM    788  CD2 LEU A  95       5.954  -3.097 -43.316  1.00 42.33           C  
ANISOU  788  CD2 LEU A  95     5898   5475   4710  -1257   1204  -1015       C  
ATOM    789  N   TYR A  96       7.073  -6.548 -39.964  1.00 41.03           N  
ANISOU  789  N   TYR A  96     5059   5283   5248   -875    995  -1176       N  
ATOM    790  CA  TYR A  96       6.497  -6.555 -38.601  1.00 39.68           C  
ANISOU  790  CA  TYR A  96     4810   5130   5135   -735    830  -1047       C  
ATOM    791  C   TYR A  96       7.601  -6.467 -37.555  1.00 38.86           C  
ANISOU  791  C   TYR A  96     4556   4985   5224   -641    825  -1134       C  
ATOM    792  O   TYR A  96       7.608  -5.541 -36.748  1.00 39.34           O  
ANISOU  792  O   TYR A  96     4593   5065   5291   -581    779  -1062       O  
ATOM    793  CB  TYR A  96       5.624  -7.778 -38.366  1.00 40.52           C  
ANISOU  793  CB  TYR A  96     4912   5233   5250   -690    718   -988       C  
ATOM    794  CG  TYR A  96       4.672  -7.583 -37.217  1.00 40.61           C  
ANISOU  794  CG  TYR A  96     4909   5272   5249   -591    571   -829       C  
ATOM    795  CD1 TYR A  96       5.100  -7.666 -35.904  1.00 41.19           C  
ANISOU  795  CD1 TYR A  96     4888   5311   5452   -478    502   -822       C  
ATOM    796  CD2 TYR A  96       3.350  -7.266 -37.447  1.00 41.14           C  
ANISOU  796  CD2 TYR A  96     5062   5391   5178   -613    503   -697       C  
ATOM    797  CE1 TYR A  96       4.231  -7.473 -34.845  1.00 41.24           C  
ANISOU  797  CE1 TYR A  96     4899   5334   5436   -403    389   -684       C  
ATOM    798  CE2 TYR A  96       2.471  -7.060 -36.402  1.00 41.66           C  
ANISOU  798  CE2 TYR A  96     5106   5478   5245   -535    392   -570       C  
ATOM    799  CZ  TYR A  96       2.902  -7.184 -35.095  1.00 41.65           C  
ANISOU  799  CZ  TYR A  96     5024   5441   5360   -436    345   -562       C  
ATOM    800  OH  TYR A  96       1.999  -7.005 -34.083  1.00 42.89           O  
ANISOU  800  OH  TYR A  96     5179   5612   5505   -377    255   -444       O  
ATOM    801  N   PRO A  97       8.591  -7.380 -37.522  1.00 38.72           N  
ANISOU  801  N   PRO A  97     4429   4905   5378   -620    863  -1299       N  
ATOM    802  CA  PRO A  97       9.661  -7.285 -36.526  1.00 39.03           C  
ANISOU  802  CA  PRO A  97     4321   4894   5614   -519    830  -1396       C  
ATOM    803  C   PRO A  97      10.491  -5.984 -36.577  1.00 39.69           C  
ANISOU  803  C   PRO A  97     4370   4988   5722   -558    941  -1466       C  
ATOM    804  O   PRO A  97      11.009  -5.542 -35.540  1.00 39.71           O  
ANISOU  804  O   PRO A  97     4277   4972   5838   -460    872  -1476       O  
ATOM    805  CB  PRO A  97      10.551  -8.507 -36.805  1.00 39.58           C  
ANISOU  805  CB  PRO A  97     4289   4888   5860   -512    865  -1589       C  
ATOM    806  CG  PRO A  97      10.173  -8.970 -38.174  1.00 39.76           C  
ANISOU  806  CG  PRO A  97     4412   4930   5766   -648    983  -1622       C  
ATOM    807  CD  PRO A  97       8.750  -8.528 -38.418  1.00 38.88           C  
ANISOU  807  CD  PRO A  97     4457   4892   5423   -686    927  -1412       C  
ATOM    808  N   LYS A  98      10.607  -5.387 -37.765  1.00 40.31           N  
ANISOU  808  N   LYS A  98     4540   5088   5687   -704   1109  -1514       N  
ATOM    809  CA  LYS A  98      11.339  -4.116 -37.989  1.00 41.09           C  
ANISOU  809  CA  LYS A  98     4642   5191   5780   -774   1247  -1583       C  
ATOM    810  C   LYS A  98      10.557  -2.942 -37.393  1.00 40.10           C  
ANISOU  810  C   LYS A  98     4596   5120   5521   -732   1160  -1387       C  
ATOM    811  O   LYS A  98      11.195  -1.963 -36.944  1.00 40.58           O  
ANISOU  811  O   LYS A  98     4604   5177   5636   -720   1204  -1423       O  
ATOM    812  CB  LYS A  98      11.572  -3.909 -39.480  1.00 42.37           C  
ANISOU  812  CB  LYS A  98     4930   5345   5826   -958   1455  -1679       C  
ATOM    813  CG  LYS A  98      12.636  -4.823 -40.026  1.00 44.15           C  
ANISOU  813  CG  LYS A  98     5046   5509   6222  -1013   1589  -1921       C  
ATOM    814  CD  LYS A  98      12.633  -4.850 -41.515  1.00 45.77           C  
ANISOU  814  CD  LYS A  98     5411   5701   6278  -1201   1781  -1995       C  
ATOM    815  CE  LYS A  98      14.011  -5.088 -42.075  1.00 47.44           C  
ANISOU  815  CE  LYS A  98     5514   5847   6665  -1300   2001  -2278       C  
ATOM    816  NZ  LYS A  98      13.909  -5.170 -43.540  1.00 49.13           N1+
ANISOU  816  NZ  LYS A  98     5920   6042   6704  -1494   2192  -2338       N1+
ATOM    817  N   ILE A  99       9.231  -3.022 -37.420  1.00 38.59           N  
ANISOU  817  N   ILE A  99     4520   4974   5170   -716   1048  -1201       N  
ATOM    818  CA  ILE A  99       8.351  -2.030 -36.752  1.00 37.18           C  
ANISOU  818  CA  ILE A  99     4399   4843   4884   -658    942  -1015       C  
ATOM    819  C   ILE A  99       8.527  -2.185 -35.247  1.00 36.94           C  
ANISOU  819  C   ILE A  99     4235   4801   4999   -510    812   -984       C  
ATOM    820  O   ILE A  99       8.699  -1.159 -34.562  1.00 37.41           O  
ANISOU  820  O   ILE A  99     4272   4874   5068   -468    795   -939       O  
ATOM    821  CB  ILE A  99       6.893  -2.199 -37.186  1.00 36.38           C  
ANISOU  821  CB  ILE A  99     4430   4785   4609   -677    852   -856       C  
ATOM    822  CG1 ILE A  99       6.718  -1.896 -38.670  1.00 37.82           C  
ANISOU  822  CG1 ILE A  99     4780   4967   4623   -822    960   -879       C  
ATOM    823  CG2 ILE A  99       6.002  -1.309 -36.358  1.00 35.35           C  
ANISOU  823  CG2 ILE A  99     4322   4696   4415   -602    734   -688       C  
ATOM    824  CD1 ILE A  99       5.363  -2.275 -39.219  1.00 38.18           C  
ANISOU  824  CD1 ILE A  99     4942   5042   4521   -839    857   -759       C  
ATOM    825  N   ILE A 100       8.516  -3.417 -34.753  1.00 37.14           N  
ANISOU  825  N   ILE A 100     4190   4793   5128   -436    722  -1010       N  
ATOM    826  CA  ILE A 100       8.678  -3.668 -33.295  1.00 37.37           C  
ANISOU  826  CA  ILE A 100     4130   4791   5280   -296    583   -979       C  
ATOM    827  C   ILE A 100      10.033  -3.094 -32.847  1.00 38.38           C  
ANISOU  827  C   ILE A 100     4139   4881   5564   -260    625  -1120       C  
ATOM    828  O   ILE A 100      10.078  -2.341 -31.841  1.00 36.17           O  
ANISOU  828  O   ILE A 100     3834   4605   5303   -185    553  -1056       O  
ATOM    829  CB  ILE A 100       8.541  -5.170 -32.983  1.00 37.92           C  
ANISOU  829  CB  ILE A 100     4172   4808   5427   -236    489  -1003       C  
ATOM    830  CG1 ILE A 100       7.128  -5.698 -33.260  1.00 37.48           C  
ANISOU  830  CG1 ILE A 100     4222   4789   5228   -266    439   -861       C  
ATOM    831  CG2 ILE A 100       8.984  -5.453 -31.555  1.00 38.17           C  
ANISOU  831  CG2 ILE A 100     4135   4777   5591    -98    351  -1007       C  
ATOM    832  CD1 ILE A 100       6.016  -4.982 -32.516  1.00 36.07           C  
ANISOU  832  CD1 ILE A 100     4103   4658   4943   -230    358   -681       C  
ATOM    833  N   GLN A 101      11.098  -3.419 -33.591  1.00 41.02           N  
ANISOU  833  N   GLN A 101     4398   5176   6012   -320    746  -1318       N  
ATOM    834  CA  GLN A 101      12.445  -2.875 -33.332  1.00 43.00           C  
ANISOU  834  CA  GLN A 101     4515   5387   6435   -306    812  -1492       C  
ATOM    835  C   GLN A 101      12.359  -1.340 -33.284  1.00 41.97           C  
ANISOU  835  C   GLN A 101     4436   5306   6203   -352    881  -1419       C  
ATOM    836  O   GLN A 101      12.769  -0.745 -32.280  1.00 42.18           O  
ANISOU  836  O   GLN A 101     4389   5321   6315   -266    810  -1417       O  
ATOM    837  CB  GLN A 101      13.434  -3.330 -34.404  1.00 46.21           C  
ANISOU  837  CB  GLN A 101     4852   5754   6952   -406    982  -1721       C  
ATOM    838  CG  GLN A 101      14.847  -2.821 -34.124  1.00 48.92           C  
ANISOU  838  CG  GLN A 101     5028   6050   7507   -394   1056  -1932       C  
ATOM    839  CD  GLN A 101      15.317  -3.271 -32.758  1.00 50.43           C  
ANISOU  839  CD  GLN A 101     5087   6183   7890   -215    850  -1966       C  
ATOM    840  NE2 GLN A 101      16.399  -4.033 -32.748  1.00 53.19           N  
ANISOU  840  NE2 GLN A 101     5274   6454   8480   -173    846  -2194       N  
ATOM    841  OE1 GLN A 101      14.704  -3.000 -31.722  1.00 50.64           O  
ANISOU  841  OE1 GLN A 101     5164   6226   7851   -113    690  -1795       O  
ATOM    842  N   ASP A 102      11.837  -0.730 -34.347  1.00 40.39           N  
ANISOU  842  N   ASP A 102     4374   5150   5821   -482   1006  -1360       N  
ATOM    843  CA  ASP A 102      11.607   0.724 -34.430  1.00 39.21           C  
ANISOU  843  CA  ASP A 102     4313   5040   5544   -534   1067  -1273       C  
ATOM    844  C   ASP A 102      11.032   1.158 -33.089  1.00 21.57           C  
ATOM    845  O   ASP A 102      11.693   1.940 -32.383  1.00 37.53           O  
ANISOU  845  O   ASP A 102     4004   4842   5416   -359    897  -1158       O  
ATOM    846  CB  ASP A 102      10.664   1.048 -35.588  1.00 39.51           C  
ANISOU  846  CB  ASP A 102     4549   5114   5350   -652   1132  -1165       C  
ATOM    847  CG  ASP A 102      10.859   2.411 -36.227  1.00 39.87           C  
ANISOU  847  CG  ASP A 102     4712   5164   5274   -764   1273  -1164       C  
ATOM    848  OD1 ASP A 102      11.325   3.333 -35.526  1.00 40.08           O  
ANISOU  848  OD1 ASP A 102     4678   5190   5359   -726   1279  -1170       O  
ATOM    849  OD2 ASP A 102      10.543   2.532 -37.411  1.00 40.38           O1-
ANISOU  849  OD2 ASP A 102     4940   5225   5180   -889   1369  -1156       O1-
ATOM    850  N   ILE A 103       9.872   0.603 -32.745  1.00 36.74           N  
ANISOU  850  N   ILE A 103     4041   4776   5141   -344    762   -960       N  
ATOM    851  CA  ILE A 103       9.101   0.997 -31.537  1.00 35.87           C  
ANISOU  851  CA  ILE A 103     3941   4690   4997   -240    617   -798       C  
ATOM    852  C   ILE A 103       9.983   0.896 -30.299  1.00 36.83           C  
ANISOU  852  C   ILE A 103     3939   4763   5291   -126    534   -871       C  
ATOM    853  O   ILE A 103       9.976   1.863 -29.526  1.00 36.33           O  
ANISOU  853  O   ILE A 103     3871   4714   5219    -82    500   -809       O  
ATOM    854  CB  ILE A 103       7.836   0.155 -31.402  1.00 34.74           C  
ANISOU  854  CB  ILE A 103     3864   4565   4770   -210    509   -666       C  
ATOM    855  CG1 ILE A 103       6.806   0.603 -32.437  1.00 35.07           C  
ANISOU  855  CG1 ILE A 103     4034   4659   4631   -302    552   -568       C  
ATOM    856  CG2 ILE A 103       7.290   0.228 -29.992  1.00 33.80           C  
ANISOU  856  CG2 ILE A 103     3733   4443   4666   -100    372   -550       C  
ATOM    857  CD1 ILE A 103       5.568  -0.258 -32.491  1.00 35.06           C  
ANISOU  857  CD1 ILE A 103     4083   4677   4562   -291    461   -468       C  
ATOM    858  N   GLU A 104      10.710  -0.201 -30.108  1.00 39.17           N  
ANISOU  858  N   GLU A 104     4145   4998   5740    -77    492   -999       N  
ATOM    859  CA  GLU A 104      11.487  -0.395 -28.859  1.00 41.70           C  
ANISOU  859  CA  GLU A 104     4365   5255   6223     50    367  -1064       C  
ATOM    860  C   GLU A 104      12.589   0.659 -28.762  1.00 25.86           C  
ATOM    861  O   GLU A 104      12.848   1.131 -27.628  1.00 41.52           O  
ANISOU  861  O   GLU A 104     4209   5204   6362    134    339  -1167       O  
ATOM    862  CB  GLU A 104      12.085  -1.797 -28.768  1.00 46.25           C  
ANISOU  862  CB  GLU A 104     4870   5751   6952    110    293  -1193       C  
ATOM    863  CG  GLU A 104      11.177  -2.812 -28.080  1.00 48.93           C  
ANISOU  863  CG  GLU A 104     5298   6061   7233    183    142  -1062       C  
ATOM    864  CD  GLU A 104      11.196  -4.226 -28.676  1.00 52.09           C  
ANISOU  864  CD  GLU A 104     5695   6416   7682    171    135  -1136       C  
ATOM    865  OE1 GLU A 104      12.191  -4.588 -29.376  1.00 55.00           O  
ANISOU  865  OE1 GLU A 104     5958   6750   8189    142    211  -1327       O  
ATOM    866  OE2 GLU A 104      10.228  -4.996 -28.411  1.00 53.97           O1-
ANISOU  866  OE2 GLU A 104     6032   6646   7830    188     58  -1014       O1-
ATOM    867  N   THR A 105      13.207   1.033 -29.885  1.00 41.77           N  
ANISOU  867  N   THR A 105     4245   5269   6357    -79    627  -1322       N  
ATOM    868  CA  THR A 105      14.307   2.027 -29.882  1.00 42.90           C  
ANISOU  868  CA  THR A 105     4290   5399   6610   -111    732  -1468       C  
ATOM    869  C   THR A 105      13.691   3.390 -29.574  1.00 41.44           C  
ANISOU  869  C   THR A 105     4200   5271   6273   -129    746  -1308       C  
ATOM    870  O   THR A 105      14.344   4.167 -28.891  1.00 42.85           O  
ANISOU  870  O   THR A 105     4302   5437   6542    -88    735  -1362       O  
ATOM    871  CB  THR A 105      15.175   2.008 -31.152  1.00 44.21           C  
ANISOU  871  CB  THR A 105     4406   5548   6843   -249    948  -1672       C  
ATOM    872  CG2 THR A 105      15.731   0.636 -31.488  1.00 44.74           C  
ANISOU  872  CG2 THR A 105     4375   5558   7067   -231    937  -1836       C  
ATOM    873  OG1 THR A 105      14.363   2.525 -32.200  1.00 46.01           O  
ANISOU  873  OG1 THR A 105     4807   5830   6846   -382   1076  -1558       O  
ATOM    874  N   ILE A 106      12.473   3.673 -30.014  1.00 39.97           N  
ANISOU  874  N   ILE A 106     4168   5141   5877   -180    757  -1124       N  
ATOM    875  CA  ILE A 106      11.772   4.937 -29.622  1.00 39.53           C  
ANISOU  875  CA  ILE A 106     4202   5133   5686   -178    742   -963       C  
ATOM    876  C   ILE A 106      11.621   4.966 -28.094  1.00 38.93           C  
ANISOU  876  C   ILE A 106     4078   5046   5669    -36    569   -885       C  
ATOM    877  O   ILE A 106      12.084   5.943 -27.475  1.00 37.43           O  
ANISOU  877  O   ILE A 106     3847   4853   5520    -10    572   -900       O  
ATOM    878  CB  ILE A 106      10.417   5.089 -30.343  1.00 38.85           C  
ANISOU  878  CB  ILE A 106     4278   5097   5384   -239    748   -791       C  
ATOM    879  CG1 ILE A 106      10.625   5.267 -31.851  1.00 40.43           C  
ANISOU  879  CG1 ILE A 106     4567   5297   5499   -389    920   -865       C  
ATOM    880  CG2 ILE A 106       9.611   6.236 -29.758  1.00 37.60           C  
ANISOU  880  CG2 ILE A 106     4191   4978   5116   -207    694   -627       C  
ATOM    881  CD1 ILE A 106       9.348   5.254 -32.688  1.00 40.40           C  
ANISOU  881  CD1 ILE A 106     4730   5328   5293   -446    902   -720       C  
ATOM    882  N   GLU A 107      11.024   3.927 -27.506  1.00 39.93           N  
ANISOU  882  N   GLU A 107     4220   5156   5796     44    431   -812       N  
ATOM    883  CA  GLU A 107      10.816   3.878 -26.037  1.00 40.88           C  
ANISOU  883  CA  GLU A 107     4336   5250   5947    167    269   -733       C  
ATOM    884  C   GLU A 107      12.154   4.041 -25.323  1.00 25.72           C  
ATOM    885  O   GLU A 107      12.201   4.753 -24.292  1.00 37.93           O  
ANISOU  885  O   GLU A 107     3839   4810   5762    304    149   -837       O  
ATOM    886  CB  GLU A 107      10.134   2.597 -25.599  1.00 44.39           C  
ANISOU  886  CB  GLU A 107     4831   5663   6373    225    148   -663       C  
ATOM    887  CG  GLU A 107       8.674   2.831 -25.290  1.00 47.83           C  
ANISOU  887  CG  GLU A 107     5380   6146   6647    218    115   -467       C  
ATOM    888  CD  GLU A 107       7.733   1.906 -26.048  1.00 53.44           C  
ANISOU  888  CD  GLU A 107     6153   6877   7275    165    129   -412       C  
ATOM    889  OE1 GLU A 107       8.013   0.645 -26.086  1.00 54.82           O  
ANISOU  889  OE1 GLU A 107     6312   6999   7520    190     82   -479       O  
ATOM    890  OE2 GLU A 107       6.696   2.437 -26.582  1.00 57.76           O1-
ANISOU  890  OE2 GLU A 107     6766   7487   7694    105    174   -304       O1-
ATOM    891  N   SER A 108      13.195   3.419 -25.865  1.00 38.55           N  
ANISOU  891  N   SER A 108     3808   4850   5989    225    267  -1081       N  
ATOM    892  CA  SER A 108      14.558   3.484 -25.294  1.00 38.77           C  
ANISOU  892  CA  SER A 108     3687   4812   6233    295    217  -1271       C  
ATOM    893  C   SER A 108      15.026   4.935 -25.294  1.00 38.12           C  
ANISOU  893  C   SER A 108     3564   4763   6157    245    324  -1307       C  
ATOM    894  O   SER A 108      15.614   5.370 -24.305  1.00 38.01           O  
ANISOU  894  O   SER A 108     3483   4715   6244    331    227  -1354       O  
ATOM    895  CB  SER A 108      15.509   2.612 -26.024  1.00 39.45           C  
ANISOU  895  CB  SER A 108     3652   4848   6491    272    270  -1486       C  
ATOM    896  OG  SER A 108      16.645   2.420 -25.215  1.00 40.68           O  
ANISOU  896  OG  SER A 108     3666   4922   6870    382    148  -1656       O  
ATOM    897  N   ASN A 109      14.735   5.658 -26.364  1.00 38.36           N  
ANISOU  897  N   ASN A 109     3653   4852   6071    111    511  -1280       N  
ATOM    898  CA  ASN A 109      15.107   7.080 -26.541  1.00 39.02           C  
ANISOU  898  CA  ASN A 109     3730   4963   6132     38    642  -1307       C  
ATOM    899  C   ASN A 109      14.441   7.920 -25.457  1.00 38.36           C  
ANISOU  899  C   ASN A 109     3714   4906   5954    112    534  -1133       C  
ATOM    900  O   ASN A 109      15.141   8.758 -24.859  1.00 37.95           O  
ANISOU  900  O   ASN A 109     3589   4840   5990    138    534  -1202       O  
ATOM    901  CB  ASN A 109      14.721   7.585 -27.930  1.00 39.12           C  
ANISOU  901  CB  ASN A 109     3854   5018   5992   -122    842  -1278       C  
ATOM    902  CG  ASN A 109      15.565   6.992 -29.030  1.00 39.88           C  
ANISOU  902  CG  ASN A 109     3885   5080   6187   -222    996  -1483       C  
ATOM    903  ND2 ASN A 109      15.145   7.176 -30.267  1.00 40.29           N  
ANISOU  903  ND2 ASN A 109     4069   5156   6085   -361   1151  -1451       N  
ATOM    904  OD1 ASN A 109      16.585   6.370 -28.766  1.00 40.91           O  
ANISOU  904  OD1 ASN A 109     3852   5157   6533   -175    971  -1676       O  
ATOM    905  N   TRP A 110      13.146   7.711 -25.220  1.00 38.14           N  
ANISOU  905  N   TRP A 110     3813   4914   5764    139    453   -928       N  
ATOM    906  CA  TRP A 110      12.424   8.412 -24.133  1.00 39.03           C  
ANISOU  906  CA  TRP A 110     3991   5047   5791    208    353   -767       C  
ATOM    907  C   TRP A 110      13.092   8.100 -22.786  1.00 41.63           C  
ANISOU  907  C   TRP A 110     4246   5314   6257    335    191   -827       C  
ATOM    908  O   TRP A 110      13.385   9.073 -22.038  1.00 42.96           O  
ANISOU  908  O   TRP A 110     4395   5482   6445    369    170   -821       O  
ATOM    909  CB  TRP A 110      10.947   8.034 -24.109  1.00 37.23           C  
ANISOU  909  CB  TRP A 110     3889   4856   5400    212    297   -573       C  
ATOM    910  CG  TRP A 110      10.116   8.688 -25.162  1.00 37.05           C  
ANISOU  910  CG  TRP A 110     3962   4891   5223    111    409   -480       C  
ATOM    911  CD1 TRP A 110       9.887   8.221 -26.423  1.00 38.54           C  
ANISOU  911  CD1 TRP A 110     4195   5095   5353     23    493   -501       C  
ATOM    912  CD2 TRP A 110       9.349   9.897 -25.039  1.00 36.35           C  
ANISOU  912  CD2 TRP A 110     3952   4844   5016     94    429   -349       C  
ATOM    913  CE2 TRP A 110       8.696  10.095 -26.274  1.00 36.74           C  
ANISOU  913  CE2 TRP A 110     4095   4924   4940      1    511   -299       C  
ATOM    914  CE3 TRP A 110       9.127  10.815 -24.007  1.00 36.20           C  
ANISOU  914  CE3 TRP A 110     3939   4833   4984    150    378   -272       C  
ATOM    915  NE1 TRP A 110       9.041   9.062 -27.101  1.00 37.74           N  
ANISOU  915  NE1 TRP A 110     4205   5035   5099    -45    551   -391       N  
ATOM    916  CZ2 TRP A 110       7.830  11.166 -26.490  1.00 36.82           C  
ANISOU  916  CZ2 TRP A 110     4202   4967   4823    -26    525   -176       C  
ATOM    917  CZ3 TRP A 110       8.283  11.880 -24.232  1.00 35.76           C  
ANISOU  917  CZ3 TRP A 110     3966   4815   4808    116    413   -155       C  
ATOM    918  CH2 TRP A 110       7.641  12.052 -25.459  1.00 35.89           C  
ANISOU  918  CH2 TRP A 110     4072   4855   4709     34    478   -109       C  
ATOM    919  N   ARG A 111      13.343   6.807 -22.525  1.00 42.41           N  
ANISOU  919  N   ARG A 111     4316   5356   6444    403     78   -887       N  
ATOM    920  CA  ARG A 111      13.850   6.288 -21.227  1.00 42.84           C  
ANISOU  920  CA  ARG A 111     4345   5328   6606    538   -118   -928       C  
ATOM    921  C   ARG A 111      15.230   6.866 -20.938  1.00 42.68           C  
ANISOU  921  C   ARG A 111     4176   5267   6774    572   -127  -1120       C  
ATOM    922  O   ARG A 111      15.464   7.303 -19.781  1.00 41.90           O  
ANISOU  922  O   ARG A 111     4084   5132   6703    659   -254  -1104       O  
ATOM    923  CB  ARG A 111      13.872   4.759 -21.214  1.00 44.88           C  
ANISOU  923  CB  ARG A 111     4614   5520   6919    592   -227   -967       C  
ATOM    924  CG  ARG A 111      12.727   4.158 -20.391  1.00 46.56           C  
ANISOU  924  CG  ARG A 111     4989   5713   6989    641   -347   -781       C  
ATOM    925  CD  ARG A 111      12.059   2.866 -20.872  1.00 48.18           C  
ANISOU  925  CD  ARG A 111     5261   5903   7141    622   -359   -734       C  
ATOM    926  NE  ARG A 111      13.017   2.045 -21.628  1.00 50.80           N  
ANISOU  926  NE  ARG A 111     5477   6193   7631    623   -347   -919       N  
ATOM    927  CZ  ARG A 111      12.715   1.072 -22.493  1.00 50.34           C  
ANISOU  927  CZ  ARG A 111     5428   6138   7560    576   -299   -934       C  
ATOM    928  NH1 ARG A 111      11.456   0.718 -22.729  1.00 48.88           N1+
ANISOU  928  NH1 ARG A 111     5363   5995   7212    526   -268   -776       N1+
ATOM    929  NH2 ARG A 111      13.704   0.461 -23.124  1.00 51.68           N  
ANISOU  929  NH2 ARG A 111     5476   6265   7895    578   -278  -1125       N  
ATOM    930  N   CYS A 112      16.096   6.852 -21.947  1.00 43.70           N  
ANISOU  930  N   CYS A 112     4178   5398   7028    500      8  -1303       N  
ATOM    931  CA  CYS A 112      17.514   7.282 -21.846  1.00 46.72           C  
ANISOU  931  CA  CYS A 112     4382   5736   7632    517     26  -1537       C  
ATOM    932  C   CYS A 112      17.668   8.748 -22.244  1.00 46.66           C  
ANISOU  932  C   CYS A 112     4360   5788   7580    412    209  -1544       C  
ATOM    933  O   CYS A 112      18.814   9.256 -22.155  1.00 47.15           O  
ANISOU  933  O   CYS A 112     4272   5819   7825    409    248  -1742       O  
ATOM    934  CB  CYS A 112      18.397   6.443 -22.744  1.00 49.06           C  
ANISOU  934  CB  CYS A 112     4540   5992   8107    481     98  -1760       C  
ATOM    935  SG  CYS A 112      18.044   4.682 -22.563  1.00 53.38           S  
ANISOU  935  SG  CYS A 112     5134   6474   8673    577    -82  -1731       S  
ATOM    936  N   GLY A 113      16.573   9.395 -22.662  1.00 44.75           N  
ANISOU  936  N   GLY A 113     4266   5620   7116    331    310  -1348       N  
ATOM    937  CA  GLY A 113      16.561  10.842 -22.951  1.00 43.68           C  
ANISOU  937  CA  GLY A 113     4159   5531   6906    240    462  -1320       C  
ATOM    938  C   GLY A 113      17.511  11.215 -24.085  1.00 43.16           C  
ANISOU  938  C   GLY A 113     4004   5459   6936    109    681  -1520       C  
ATOM    939  O   GLY A 113      18.134  12.284 -24.025  1.00 41.15           O  
ANISOU  939  O   GLY A 113     3699   5203   6734     61    779  -1604       O  
ATOM    940  N   ARG A 114      17.627  10.329 -25.071  1.00 44.31           N  
ANISOU  940  N   ARG A 114     4137   5595   7105     45    763  -1602       N  
ATOM    941  CA  ARG A 114      18.236  10.595 -26.400  1.00 46.84           C  
ANISOU  941  CA  ARG A 114     4437   5912   7450   -120   1013  -1759       C  
ATOM    942  C   ARG A 114      17.188  11.288 -27.267  1.00 42.73           C  
ANISOU  942  C   ARG A 114     4128   5444   6663   -237   1138  -1572       C  
ATOM    943  O   ARG A 114      16.111  10.751 -27.405  1.00 41.66           O  
ANISOU  943  O   ARG A 114     4110   5339   6379   -211   1057  -1399       O  
ATOM    944  CB  ARG A 114      18.666   9.279 -27.056  1.00 50.74           C  
ANISOU  944  CB  ARG A 114     4849   6369   8062   -134   1033  -1909       C  
ATOM    945  CG  ARG A 114      20.141   8.945 -26.842  1.00 55.84           C  
ANISOU  945  CG  ARG A 114     5258   6945   9014   -103   1041  -2209       C  
ATOM    946  CD  ARG A 114      20.576   7.616 -27.433  1.00 58.66           C  
ANISOU  946  CD  ARG A 114     5522   7258   9508   -105   1049  -2368       C  
ATOM    947  NE  ARG A 114      19.549   6.598 -27.194  1.00 59.65           N  
ANISOU  947  NE  ARG A 114     5761   7397   9508    -16    875  -2176       N  
ATOM    948  CZ  ARG A 114      19.671   5.526 -26.407  1.00 60.83           C  
ANISOU  948  CZ  ARG A 114     5842   7493   9778    135    653  -2199       C  
ATOM    949  NH1 ARG A 114      18.649   4.680 -26.291  1.00 59.39           N1+
ANISOU  949  NH1 ARG A 114     5790   7324   9453    186    534  -2015       N1+
ATOM    950  NH2 ARG A 114      20.815   5.291 -25.771  1.00 61.81           N  
ANISOU  950  NH2 ARG A 114     5773   7542  10169    231    549  -2416       N  
ATOM    951  N   HIS A 115      17.498  12.434 -27.851  1.00 39.90           N  
ANISOU  951  N   HIS A 115     3823   5087   6251   -362   1327  -1614       N  
ATOM    952  CA  HIS A 115      16.541  13.174 -28.714  1.00 37.63           C  
ANISOU  952  CA  HIS A 115     3762   4831   5705   -471   1431  -1442       C  
ATOM    953  C   HIS A 115      17.328  14.077 -29.653  1.00 37.78           C  
ANISOU  953  C   HIS A 115     3825   4815   5717   -646   1690  -1588       C  
ATOM    954  O   HIS A 115      18.444  14.446 -29.277  1.00 38.72           O  
ANISOU  954  O   HIS A 115     3787   4902   6024   -656   1760  -1778       O  
ATOM    955  CB  HIS A 115      15.547  13.998 -27.871  1.00 34.97           C  
ANISOU  955  CB  HIS A 115     3521   4534   5232   -386   1297  -1214       C  
ATOM    956  CG  HIS A 115      16.218  15.016 -27.020  1.00 34.52           C  
ANISOU  956  CG  HIS A 115     3378   4465   5274   -355   1302  -1273       C  
ATOM    957  CD2 HIS A 115      16.525  16.307 -27.227  1.00 34.43           C  
ANISOU  957  CD2 HIS A 115     3421   4443   5219   -443   1440  -1294       C  
ATOM    958  ND1 HIS A 115      16.727  14.718 -25.780  1.00 34.41           N  
ANISOU  958  ND1 HIS A 115     3202   4439   5433   -220   1148  -1335       N  
ATOM    959  CE1 HIS A 115      17.301  15.784 -25.248  1.00 33.80           C  
ANISOU  959  CE1 HIS A 115     3074   4351   5418   -223   1187  -1391       C  
ATOM    960  NE2 HIS A 115      17.189  16.760 -26.109  1.00 34.10           N  
ANISOU  960  NE2 HIS A 115     3237   4391   5330   -359   1370  -1368       N  
ATOM    961  N   ASN A 116      16.734  14.441 -30.792  1.00 37.14           N  
ANISOU  961  N   ASN A 116     3961   4731   5419   -778   1817  -1500       N  
ATOM    962  CA  ASN A 116      17.144  15.611 -31.611  1.00 38.17           C  
ANISOU  962  CA  ASN A 116     4227   4820   5453   -950   2050  -1560       C  
ATOM    963  C   ASN A 116      16.476  16.866 -31.056  1.00 35.97           C  
ANISOU  963  C   ASN A 116     4064   4561   5041   -908   1980  -1375       C  
ATOM    964  O   ASN A 116      15.256  16.825 -30.891  1.00 34.85           O  
ANISOU  964  O   ASN A 116     4037   4458   4747   -828   1820  -1154       O  
ATOM    965  CB  ASN A 116      16.808  15.432 -33.099  1.00 39.56           C  
ANISOU  965  CB  ASN A 116     4626   4967   5439  -1112   2205  -1548       C  
ATOM    966  CG  ASN A 116      17.494  16.456 -33.984  1.00 40.84           C  
ANISOU  966  CG  ASN A 116     4927   5062   5529  -1313   2479  -1667       C  
ATOM    967  ND2 ASN A 116      16.726  17.135 -34.831  1.00 40.68           N  
ANISOU  967  ND2 ASN A 116     5204   5014   5237  -1410   2530  -1516       N  
ATOM    968  OD1 ASN A 116      18.709  16.626 -33.887  1.00 41.53           O  
ANISOU  968  OD1 ASN A 116     4858   5113   5809  -1380   2639  -1900       O  
ATOM    969  N   LEU A 117      17.251  17.903 -30.762  1.00 35.72           N  
ANISOU  969  N   LEU A 117     3989   4501   5082   -957   2094  -1473       N  
ATOM    970  CA  LEU A 117      16.706  19.176 -30.243  1.00 34.92           C  
ANISOU  970  CA  LEU A 117     3995   4409   4863   -925   2044  -1314       C  
ATOM    971  C   LEU A 117      16.763  20.222 -31.351  1.00 35.99           C  
ANISOU  971  C   LEU A 117     4372   4485   4819  -1111   2261  -1315       C  
ATOM    972  O   LEU A 117      17.861  20.389 -31.917  1.00 39.27           O  
ANISOU  972  O   LEU A 117     4756   4846   5320  -1257   2491  -1531       O  
ATOM    973  CB  LEU A 117      17.514  19.649 -29.037  1.00 34.45           C  
ANISOU  973  CB  LEU A 117     3727   4354   5007   -843   2003  -1417       C  
ATOM    974  CG  LEU A 117      16.907  20.836 -28.293  1.00 33.37           C  
ANISOU  974  CG  LEU A 117     3671   4234   4772   -781   1919  -1247       C  
ATOM    975  CD1 LEU A 117      15.719  20.379 -27.456  1.00 32.34           C  
ANISOU  975  CD1 LEU A 117     3545   4164   4581   -612   1664  -1032       C  
ATOM    976  CD2 LEU A 117      17.912  21.536 -27.418  1.00 33.56           C  
ANISOU  976  CD2 LEU A 117     3529   4244   4978   -760   1954  -1390       C  
ATOM    977  N   GLN A 118      15.644  20.887 -31.650  1.00 34.74           N  
ANISOU  977  N   GLN A 118     4449   4326   4426  -1108   2191  -1096       N  
ATOM    978  CA  GLN A 118      15.612  22.099 -32.496  1.00 35.27           C  
ANISOU  978  CA  GLN A 118     4779   4321   4302  -1260   2355  -1063       C  
ATOM    979  C   GLN A 118      15.025  23.251 -31.698  1.00 33.93           C  
ANISOU  979  C   GLN A 118     4659   4161   4071  -1171   2241   -904       C  
ATOM    980  O   GLN A 118      14.015  23.051 -30.968  1.00 32.70           O  
ANISOU  980  O   GLN A 118     4464   4067   3896  -1010   2011   -730       O  
ATOM    981  CB  GLN A 118      14.811  21.896 -33.770  1.00 36.15           C  
ANISOU  981  CB  GLN A 118     5174   4394   4169  -1350   2371   -957       C  
ATOM    982  CG  GLN A 118      15.509  20.987 -34.756  1.00 37.65           C  
ANISOU  982  CG  GLN A 118     5367   4549   4388  -1487   2548  -1135       C  
ATOM    983  CD  GLN A 118      14.484  19.995 -35.196  1.00 37.16           C  
ANISOU  983  CD  GLN A 118     5381   4523   4217  -1426   2387  -1005       C  
ATOM    984  NE2 GLN A 118      14.101  20.161 -36.445  1.00 38.37           N  
ANISOU  984  NE2 GLN A 118     5830   4610   4141  -1559   2470   -959       N  
ATOM    985  OE1 GLN A 118      14.000  19.164 -34.412  1.00 36.14           O  
ANISOU  985  OE1 GLN A 118     5069   4470   4193  -1263   2187   -938       O  
ATOM    986  N   ARG A 119      15.655  24.407 -31.848  1.00 34.50           N  
ANISOU  986  N   ARG A 119     4816   4171   4119  -1282   2412   -974       N  
ATOM    987  CA  ARG A 119      15.368  25.592 -31.022  1.00 34.19           C  
ANISOU  987  CA  ARG A 119     4795   4135   4061  -1212   2340   -868       C  
ATOM    988  C   ARG A 119      14.874  26.681 -31.962  1.00 35.04           C  
ANISOU  988  C   ARG A 119     5244   4154   3914  -1329   2424   -758       C  
ATOM    989  O   ARG A 119      15.619  27.064 -32.829  1.00 36.13           O  
ANISOU  989  O   ARG A 119     5521   4211   3995  -1513   2659   -885       O  
ATOM    990  CB  ARG A 119      16.605  26.019 -30.229  1.00 34.61           C  
ANISOU  990  CB  ARG A 119     4629   4186   4334  -1226   2451  -1058       C  
ATOM    991  CG  ARG A 119      16.386  27.223 -29.333  1.00 34.03           C  
ANISOU  991  CG  ARG A 119     4562   4116   4253  -1157   2385   -963       C  
ATOM    992  CD  ARG A 119      17.552  27.490 -28.407  1.00 34.62           C  
ANISOU  992  CD  ARG A 119     4386   4199   4567  -1142   2448  -1151       C  
ATOM    993  NE  ARG A 119      17.589  26.632 -27.226  1.00 33.71           N  
ANISOU  993  NE  ARG A 119     4008   4161   4640   -964   2245  -1165       N  
ATOM    994  CZ  ARG A 119      18.477  25.655 -26.980  1.00 34.34           C  
ANISOU  994  CZ  ARG A 119     3857   4256   4936   -941   2248  -1358       C  
ATOM    995  NH1 ARG A 119      19.429  25.338 -27.846  1.00 36.03           N1+
ANISOU  995  NH1 ARG A 119     4035   4423   5231  -1088   2458  -1572       N1+
ATOM    996  NH2 ARG A 119      18.401  24.987 -25.838  1.00 33.45           N  
ANISOU  996  NH2 ARG A 119     3554   4197   4960   -769   2035  -1341       N  
ATOM    997  N   ILE A 120      13.629  27.122 -31.774  1.00 34.63           N  
ANISOU  997  N   ILE A 120     5325   4114   3720  -1222   2229   -536       N  
ATOM    998  CA  ILE A 120      13.085  28.331 -32.440  1.00 35.33           C  
ANISOU  998  CA  ILE A 120     5735   4110   3580  -1295   2254   -413       C  
ATOM    999  C   ILE A 120      13.285  29.510 -31.496  1.00 35.50           C  
ANISOU  999  C   ILE A 120     5698   4127   3666  -1247   2253   -394       C  
ATOM   1000  O   ILE A 120      12.713  29.492 -30.392  1.00 34.46           O  
ANISOU 1000  O   ILE A 120     5398   4071   3626  -1077   2064   -298       O  
ATOM   1001  CB  ILE A 120      11.608  28.141 -32.779  1.00 34.35           C  
ANISOU 1001  CB  ILE A 120     5769   3991   3290  -1195   2024   -202       C  
ATOM   1002  CG1 ILE A 120      11.368  26.878 -33.591  1.00 34.59           C  
ANISOU 1002  CG1 ILE A 120     5827   4040   3277  -1224   2001   -221       C  
ATOM   1003  CG2 ILE A 120      11.101  29.359 -33.494  1.00 35.59           C  
ANISOU 1003  CG2 ILE A 120     6268   4036   3220  -1262   2029    -90       C  
ATOM   1004  CD1 ILE A 120       9.920  26.664 -33.966  1.00 34.38           C  
ANISOU 1004  CD1 ILE A 120     5946   4015   3101  -1130   1770    -33       C  
ATOM   1005  N   GLN A 121      14.065  30.498 -31.901  1.00 37.27           N  
ANISOU 1005  N   GLN A 121     6060   4259   3839  -1400   2466   -485       N  
ATOM   1006  CA  GLN A 121      14.031  31.824 -31.254  1.00 37.88           C  
ANISOU 1006  CA  GLN A 121     6179   4306   3908  -1372   2461   -428       C  
ATOM   1007  C   GLN A 121      12.819  32.541 -31.840  1.00 39.83           C  
ANISOU 1007  C   GLN A 121     6744   4480   3909  -1347   2327   -216       C  
ATOM   1008  O   GLN A 121      12.785  32.746 -33.057  1.00 42.46           O  
ANISOU 1008  O   GLN A 121     7380   4708   4044  -1488   2428   -209       O  
ATOM   1009  CB  GLN A 121      15.340  32.551 -31.509  1.00 38.74           C  
ANISOU 1009  CB  GLN A 121     6319   4338   4063  -1556   2750   -621       C  
ATOM   1010  CG  GLN A 121      16.519  31.874 -30.864  1.00 38.02           C  
ANISOU 1010  CG  GLN A 121     5885   4313   4246  -1560   2850   -846       C  
ATOM   1011  CD  GLN A 121      16.532  32.190 -29.404  1.00 36.65           C  
ANISOU 1011  CD  GLN A 121     5463   4216   4246  -1397   2707   -823       C  
ATOM   1012  NE2 GLN A 121      17.349  31.454 -28.681  1.00 36.34           N  
ANISOU 1012  NE2 GLN A 121     5114   4244   4452  -1346   2706   -987       N  
ATOM   1013  OE1 GLN A 121      15.785  33.048 -28.929  1.00 36.32           O  
ANISOU 1013  OE1 GLN A 121     5512   4169   4118  -1313   2585   -660       O  
ATOM   1014  N   CYS A 122      11.826  32.863 -31.022  1.00 40.63           N  
ANISOU 1014  N   CYS A 122     6785   4628   4023  -1171   2100    -57       N  
ATOM   1015  CA  CYS A 122      10.611  33.592 -31.464  1.00 42.69           C  
ANISOU 1015  CA  CYS A 122     7316   4818   4087  -1119   1937    135       C  
ATOM   1016  C   CYS A 122      10.901  35.091 -31.579  1.00 47.59           C  
ANISOU 1016  C   CYS A 122     8149   5324   4608  -1202   2045    149       C  
ATOM   1017  O   CYS A 122       9.957  35.838 -31.934  1.00 48.50           O  
ANISOU 1017  O   CYS A 122     8506   5360   4563  -1157   1906    300       O  
ATOM   1018  CB  CYS A 122       9.455  33.354 -30.520  1.00 39.89           C  
ANISOU 1018  CB  CYS A 122     6792   4553   3811   -906   1670    274       C  
ATOM   1019  SG  CYS A 122       9.198  31.595 -30.200  1.00 37.99           S  
ANISOU 1019  SG  CYS A 122     6282   4444   3707   -812   1561    247       S  
ATOM   1020  N   ARG A 123      12.146  35.518 -31.325  1.00 52.10           N  
ANISOU 1020  N   ARG A 123     8643   5880   5275  -1319   2277    -11       N  
ATOM   1021  CA  ARG A 123      12.601  36.911 -31.575  1.00 56.11           C  
ANISOU 1021  CA  ARG A 123     9376   6263   5679  -1441   2434    -28       C  
ATOM   1022  C   ARG A 123      11.444  37.850 -31.230  1.00 56.43           C  
ANISOU 1022  C   ARG A 123     9550   6266   5626  -1304   2216    170       C  
ATOM   1023  O   ARG A 123      10.973  38.542 -32.127  1.00 58.05           O  
ANISOU 1023  O   ARG A 123    10107   6337   5611  -1365   2196    263       O  
ATOM   1024  CB  ARG A 123      13.072  37.055 -33.021  1.00 60.66           C  
ANISOU 1024  CB  ARG A 123    10295   6701   6052  -1664   2644    -92       C  
ATOM   1025  CG  ARG A 123      14.121  36.026 -33.404  1.00 63.84           C  
ANISOU 1025  CG  ARG A 123    10552   7143   6563  -1794   2853   -297       C  
ATOM   1026  CD  ARG A 123      15.103  36.438 -34.479  1.00 71.26           C  
ANISOU 1026  CD  ARG A 123    11748   7947   7382  -2061   3177   -448       C  
ATOM   1027  NE  ARG A 123      15.906  35.271 -34.867  1.00 76.55           N  
ANISOU 1027  NE  ARG A 123    12254   8664   8167  -2159   3337   -637       N  
ATOM   1028  CZ  ARG A 123      16.948  34.757 -34.183  1.00 77.80           C  
ANISOU 1028  CZ  ARG A 123    12049   8910   8602  -2166   3459   -845       C  
ATOM   1029  NH1 ARG A 123      17.586  33.683 -34.642  1.00 77.00           N1+
ANISOU 1029  NH1 ARG A 123    11824   8836   8596  -2250   3588  -1012       N1+
ATOM   1030  NH2 ARG A 123      17.340  35.311 -33.040  1.00 76.90           N  
ANISOU 1030  NH2 ARG A 123    11697   8849   8674  -2083   3440   -889       N  
ATOM   1031  N   SER A 124      10.979  37.822 -29.979  1.00 55.75           N  
ANISOU 1031  N   SER A 124     9196   6286   5700  -1123   2049    226       N  
ATOM   1032  CA  SER A 124       9.886  38.691 -29.472  1.00 57.05           C  
ANISOU 1032  CA  SER A 124     9425   6428   5823   -978   1844    392       C  
ATOM   1033  C   SER A 124      10.416  40.123 -29.388  1.00 61.29           C  
ANISOU 1033  C   SER A 124    10119   6859   6309  -1065   1981    371       C  
ATOM   1034  O   SER A 124      11.659  40.272 -29.156  1.00 60.32           O  
ANISOU 1034  O   SER A 124     9894   6744   6283  -1184   2210    210       O  
ATOM   1035  CB  SER A 124       9.367  38.265 -28.112  1.00 54.61           C  
ANISOU 1035  CB  SER A 124     8787   6257   5707   -789   1674    431       C  
ATOM   1036  OG  SER A 124       8.131  37.580 -28.194  1.00 53.10           O  
ANISOU 1036  OG  SER A 124     8575   6108   5492   -658   1446    551       O  
ATOM   1037  N   GLU A 125       9.502  41.107 -29.486  1.00 65.61           N  
ANISOU 1037  N   GLU A 125    10875   7316   6736   -994   1837    517       N  
ATOM   1038  CA  GLU A 125       9.802  42.558 -29.659  1.00 69.07           C  
ANISOU 1038  CA  GLU A 125    11560   7615   7068  -1081   1942    529       C  
ATOM   1039  C   GLU A 125      10.353  43.110 -28.330  1.00 69.07           C  
ANISOU 1039  C   GLU A 125    11293   7688   7262  -1033   2006    463       C  
ATOM   1040  O   GLU A 125      11.593  43.055 -28.135  1.00 69.77           O  
ANISOU 1040  O   GLU A 125    11262   7802   7448  -1157   2234    299       O  
ATOM   1041  CB  GLU A 125       8.576  43.322 -30.188  1.00 69.52           C  
ANISOU 1041  CB  GLU A 125    11919   7547   6948   -998   1726    705       C  
ATOM   1042  CG  GLU A 125       7.860  42.694 -31.391  1.00 70.74           C  
ANISOU 1042  CG  GLU A 125    12314   7639   6926  -1007   1598    781       C  
ATOM   1043  CD  GLU A 125       8.528  42.681 -32.772  1.00 74.14           C  
ANISOU 1043  CD  GLU A 125    13098   7933   7137  -1227   1789    725       C  
ATOM   1044  OE1 GLU A 125       9.208  43.675 -33.136  1.00 74.57           O  
ANISOU 1044  OE1 GLU A 125    13400   7854   7077  -1377   1977    685       O  
ATOM   1045  OE2 GLU A 125       8.341  41.671 -33.517  1.00 72.67           O1-
ANISOU 1045  OE2 GLU A 125    12958   7767   6886  -1255   1754    720       O1-
ATOM   1046  N   ASN A 126       9.514  43.604 -27.418  1.00 67.02           N  
ANISOU 1046  N   ASN A 126    10928   7463   7072   -864   1820    568       N  
ATOM   1047  CA  ASN A 126      10.053  44.067 -26.113  1.00 67.18           C  
ANISOU 1047  CA  ASN A 126    10695   7557   7274   -820   1879    500       C  
ATOM   1048  C   ASN A 126       9.831  42.940 -25.119  1.00 61.97           C  
ANISOU 1048  C   ASN A 126     9681   7065   6799   -684   1761    482       C  
ATOM   1049  O   ASN A 126      10.794  42.171 -24.903  1.00 67.08           O  
ANISOU 1049  O   ASN A 126    10140   7788   7560   -744   1884    343       O  
ATOM   1050  CB  ASN A 126       9.548  45.441 -25.656  1.00 73.09           C  
ANISOU 1050  CB  ASN A 126    11554   8225   7990   -756   1810    591       C  
ATOM   1051  CG  ASN A 126      10.474  46.080 -24.629  1.00 75.95           C  
ANISOU 1051  CG  ASN A 126    11739   8623   8495   -787   1954    484       C  
ATOM   1052  ND2 ASN A 126       9.912  46.611 -23.547  1.00 79.14           N  
ANISOU 1052  ND2 ASN A 126    12009   9068   8993   -648   1829    546       N  
ATOM   1053  OD1 ASN A 126      11.696  46.093 -24.801  1.00 76.26           O  
ANISOU 1053  OD1 ASN A 126    11756   8651   8568   -939   2179    334       O  
ATOM   1054  N   SER A 127       8.616  42.821 -24.591  1.00 55.37           N  
ANISOU 1054  N   SER A 127     8772   6275   5992   -514   1536    607       N  
ATOM   1055  CA  SER A 127       8.175  41.675 -23.760  1.00 50.95           C  
ANISOU 1055  CA  SER A 127     7928   5857   5574   -387   1408    612       C  
ATOM   1056  C   SER A 127       8.694  40.366 -24.373  1.00 46.91           C  
ANISOU 1056  C   SER A 127     7359   5398   5069   -457   1470    532       C  
ATOM   1057  O   SER A 127       8.518  40.197 -25.574  1.00 48.20           O  
ANISOU 1057  O   SER A 127     7737   5490   5087   -531   1482    560       O  
ATOM   1058  CB  SER A 127       6.674  41.676 -23.648  1.00 51.27           C  
ANISOU 1058  CB  SER A 127     7990   5900   5593   -238   1178    754       C  
ATOM   1059  OG  SER A 127       6.224  42.538 -22.614  1.00 52.87           O  
ANISOU 1059  OG  SER A 127     8111   6106   5872   -140   1113    797       O  
ATOM   1060  N   LYS A 128       9.313  39.493 -23.568  1.00 42.85           N  
ANISOU 1060  N   LYS A 128     6577   4992   4712   -433   1500    435       N  
ATOM   1061  CA  LYS A 128       9.831  38.158 -23.981  1.00 39.80           C  
ANISOU 1061  CA  LYS A 128     6092   4663   4367   -480   1546    346       C  
ATOM   1062  C   LYS A 128       9.006  37.058 -23.330  1.00 35.42           C  
ANISOU 1062  C   LYS A 128     5355   4212   3892   -338   1366    406       C  
ATOM   1063  O   LYS A 128       8.640  37.214 -22.158  1.00 34.44           O  
ANISOU 1063  O   LYS A 128     5083   4141   3862   -228   1275    441       O  
ATOM   1064  CB  LYS A 128      11.308  37.986 -23.622  1.00 40.09           C  
ANISOU 1064  CB  LYS A 128     5970   4726   4536   -569   1722    160       C  
ATOM   1065  CG  LYS A 128      12.187  39.010 -24.308  1.00 42.88           C  
ANISOU 1065  CG  LYS A 128     6499   4973   4820   -734   1935     74       C  
ATOM   1066  CD  LYS A 128      13.303  38.393 -25.119  1.00 45.07           C  
ANISOU 1066  CD  LYS A 128     6772   5232   5121   -889   2130    -96       C  
ATOM   1067  CE  LYS A 128      14.004  39.428 -25.970  1.00 47.19           C  
ANISOU 1067  CE  LYS A 128     7274   5375   5283  -1075   2357   -168       C  
ATOM   1068  NZ  LYS A 128      14.236  40.671 -25.180  1.00 47.54           N1+
ANISOU 1068  NZ  LYS A 128     7303   5389   5370  -1063   2391   -170       N1+
ATOM   1069  N   GLY A 129       8.728  36.011 -24.102  1.00 33.63           N  
ANISOU 1069  N   GLY A 129     5156   4003   3619   -353   1329    415       N  
ATOM   1070  CA  GLY A 129       8.203  34.732 -23.593  1.00 31.87           C  
ANISOU 1070  CA  GLY A 129     4752   3877   3480   -252   1200    435       C  
ATOM   1071  C   GLY A 129       7.072  34.202 -24.452  1.00 31.05           C  
ANISOU 1071  C   GLY A 129     4767   3761   3270   -221   1075    538       C  
ATOM   1072  O   GLY A 129       6.461  35.009 -25.163  1.00 30.79           O  
ANISOU 1072  O   GLY A 129     4944   3646   3108   -235   1035    621       O  
ATOM   1073  N   VAL A 130       6.824  32.891 -24.367  1.00 30.02           N  
ANISOU 1073  N   VAL A 130     4510   3703   3194   -178   1007    528       N  
ATOM   1074  CA  VAL A 130       5.821  32.142 -25.174  1.00 29.75           C  
ANISOU 1074  CA  VAL A 130     4554   3670   3080   -152    889    603       C  
ATOM   1075  C   VAL A 130       4.914  31.349 -24.237  1.00 28.49           C  
ANISOU 1075  C   VAL A 130     4211   3593   3021    -24    744    653       C  
ATOM   1076  O   VAL A 130       5.300  30.264 -23.735  1.00 27.73           O  
ANISOU 1076  O   VAL A 130     3955   3565   3018     -9    754    594       O  
ATOM   1077  CB  VAL A 130       6.500  31.201 -26.172  1.00 30.47           C  
ANISOU 1077  CB  VAL A 130     4692   3758   3129   -258    984    520       C  
ATOM   1078  CG1 VAL A 130       5.462  30.448 -26.994  1.00 30.96           C  
ANISOU 1078  CG1 VAL A 130     4839   3819   3107   -231    855    595       C  
ATOM   1079  CG2 VAL A 130       7.454  31.964 -27.065  1.00 31.78           C  
ANISOU 1079  CG2 VAL A 130     5044   3834   3198   -407   1162    450       C  
ATOM   1080  N   TYR A 131       3.713  31.851 -24.055  1.00 28.10           N  
ANISOU 1080  N   TYR A 131     4194   3528   2953     61    612    753       N  
ATOM   1081  CA  TYR A 131       2.840  31.441 -22.934  1.00 26.96           C  
ANISOU 1081  CA  TYR A 131     3876   3450   2917    175    505    791       C  
ATOM   1082  C   TYR A 131       2.085  30.175 -23.314  1.00 26.78           C  
ANISOU 1082  C   TYR A 131     3807   3468   2899    202    413    808       C  
ATOM   1083  O   TYR A 131       1.752  29.418 -22.410  1.00 28.49           O  
ANISOU 1083  O   TYR A 131     3868   3747   3210    259    376    803       O  
ATOM   1084  CB  TYR A 131       1.887  32.581 -22.582  1.00 26.55           C  
ANISOU 1084  CB  TYR A 131     3864   3357   2866    249    418    867       C  
ATOM   1085  CG  TYR A 131       2.432  33.637 -21.649  1.00 25.61           C  
ANISOU 1085  CG  TYR A 131     3711   3227   2794    256    490    850       C  
ATOM   1086  CD1 TYR A 131       2.863  33.318 -20.375  1.00 24.57           C  
ANISOU 1086  CD1 TYR A 131     3410   3157   2768    285    531    806       C  
ATOM   1087  CD2 TYR A 131       2.408  34.976 -21.990  1.00 25.93           C  
ANISOU 1087  CD2 TYR A 131     3899   3184   2769    243    501    884       C  
ATOM   1088  CE1 TYR A 131       3.285  34.295 -19.482  1.00 24.34           C  
ANISOU 1088  CE1 TYR A 131     3350   3117   2781    297    584    792       C  
ATOM   1089  CE2 TYR A 131       2.801  35.962 -21.097  1.00 25.58           C  
ANISOU 1089  CE2 TYR A 131     3818   3129   2773    255    560    872       C  
ATOM   1090  CZ  TYR A 131       3.269  35.629 -19.841  1.00 24.66           C  
ANISOU 1090  CZ  TYR A 131     3523   3084   2765    280    605    822       C  
ATOM   1091  OH  TYR A 131       3.676  36.598 -18.961  1.00 24.07           O  
ANISOU 1091  OH  TYR A 131     3416   2996   2733    290    660    805       O  
ATOM   1092  N   CYS A 132       1.837  29.943 -24.599  1.00 27.11           N  
ANISOU 1092  N   CYS A 132     3994   3469   2837    156    380    826       N  
ATOM   1093  CA  CYS A 132       0.992  28.815 -25.099  1.00 26.51           C  
ANISOU 1093  CA  CYS A 132     3893   3423   2757    182    277    846       C  
ATOM   1094  C   CYS A 132       1.473  28.344 -26.480  1.00 27.20           C  
ANISOU 1094  C   CYS A 132     4136   3474   2726     84    321    818       C  
ATOM   1095  O   CYS A 132       2.158  29.094 -27.183  1.00 27.81           O  
ANISOU 1095  O   CYS A 132     4384   3482   2702      1    408    803       O  
ATOM   1096  CB  CYS A 132      -0.471  29.236 -25.180  1.00 26.12           C  
ANISOU 1096  CB  CYS A 132     3866   3347   2713    271    111    920       C  
ATOM   1097  SG  CYS A 132      -0.720  30.758 -26.136  1.00 26.83           S  
ANISOU 1097  SG  CYS A 132     4211   3312   2670    261     52    978       S  
ATOM   1098  N   LEU A 133       1.087  27.143 -26.865  1.00 27.50           N  
ANISOU 1098  N   LEU A 133     4129   3549   2770     86    269    808       N  
ATOM   1099  CA  LEU A 133       1.379  26.579 -28.202  1.00 28.95           C  
ANISOU 1099  CA  LEU A 133     4462   3699   2838     -4    298    783       C  
ATOM   1100  C   LEU A 133       0.473  25.370 -28.469  1.00 28.18           C  
ANISOU 1100  C   LEU A 133     4298   3645   2765     36    182    797       C  
ATOM   1101  O   LEU A 133      -0.028  24.729 -27.525  1.00 26.82           O  
ANISOU 1101  O   LEU A 133     3937   3540   2713    110    133    800       O  
ATOM   1102  CB  LEU A 133       2.857  26.194 -28.292  1.00 29.80           C  
ANISOU 1102  CB  LEU A 133     4547   3819   2957   -107    484    679       C  
ATOM   1103  CG  LEU A 133       3.221  24.917 -27.532  1.00 29.97           C  
ANISOU 1103  CG  LEU A 133     4352   3924   3111    -79    508    616       C  
ATOM   1104  CD1 LEU A 133       3.003  23.671 -28.380  1.00 31.09           C  
ANISOU 1104  CD1 LEU A 133     4515   4082   3218   -113    482    595       C  
ATOM   1105  CD2 LEU A 133       4.653  24.942 -27.071  1.00 30.07           C  
ANISOU 1105  CD2 LEU A 133     4280   3946   3198   -132    662    508       C  
ATOM   1106  N   GLN A 134       0.303  25.069 -29.747  1.00 29.16           N  
ANISOU 1106  N   GLN A 134     4591   3723   2767    -22    148    802       N  
ATOM   1107  CA  GLN A 134      -0.327  23.819 -30.248  1.00 29.28           C  
ANISOU 1107  CA  GLN A 134     4569   3772   2785    -14     65    796       C  
ATOM   1108  C   GLN A 134       0.322  23.490 -31.593  1.00 30.45           C  
ANISOU 1108  C   GLN A 134     4913   3869   2787   -135    142    756       C  
ATOM   1109  O   GLN A 134       0.670  24.460 -32.315  1.00 31.37           O  
ANISOU 1109  O   GLN A 134     5252   3898   2770   -201    183    770       O  
ATOM   1110  CB  GLN A 134      -1.842  24.024 -30.360  1.00 29.24           C  
ANISOU 1110  CB  GLN A 134     4571   3750   2790     83   -142    864       C  
ATOM   1111  CG  GLN A 134      -2.616  22.823 -30.888  1.00 28.78           C  
ANISOU 1111  CG  GLN A 134     4474   3721   2742     96   -244    855       C  
ATOM   1112  CD  GLN A 134      -4.093  23.124 -30.953  1.00 28.94           C  
ANISOU 1112  CD  GLN A 134     4478   3717   2801    195   -452    900       C  
ATOM   1113  NE2 GLN A 134      -4.734  22.622 -31.989  1.00 29.58           N  
ANISOU 1113  NE2 GLN A 134     4660   3766   2812    188   -576    902       N  
ATOM   1114  OE1 GLN A 134      -4.665  23.804 -30.098  1.00 28.59           O  
ANISOU 1114  OE1 GLN A 134     4330   3678   2855    277   -505    922       O  
ATOM   1115  N   TYR A 135       0.482  22.205 -31.915  1.00 30.13           N  
ANISOU 1115  N   TYR A 135     4811   3872   2766   -170    170    706       N  
ATOM   1116  CA  TYR A 135       1.105  21.794 -33.187  1.00 31.43           C  
ANISOU 1116  CA  TYR A 135     5155   3988   2798   -295    259    654       C  
ATOM   1117  C   TYR A 135       0.327  20.663 -33.827  1.00 32.14           C  
ANISOU 1117  C   TYR A 135     5247   4099   2865   -285    148    660       C  
ATOM   1118  O   TYR A 135      -0.582  20.088 -33.181  1.00 30.17           O  
ANISOU 1118  O   TYR A 135     4827   3910   2726   -185     25    690       O  
ATOM   1119  CB  TYR A 135       2.562  21.393 -32.978  1.00 31.87           C  
ANISOU 1119  CB  TYR A 135     5129   4069   2913   -383    473    541       C  
ATOM   1120  CG  TYR A 135       2.814  20.078 -32.278  1.00 31.36           C  
ANISOU 1120  CG  TYR A 135     4826   4089   3000   -346    492    480       C  
ATOM   1121  CD1 TYR A 135       2.688  18.870 -32.945  1.00 31.86           C  
ANISOU 1121  CD1 TYR A 135     4890   4169   3045   -381    482    444       C  
ATOM   1122  CD2 TYR A 135       3.234  20.041 -30.962  1.00 30.60           C  
ANISOU 1122  CD2 TYR A 135     4523   4047   3058   -280    522    455       C  
ATOM   1123  CE1 TYR A 135       2.919  17.659 -32.318  1.00 31.34           C  
ANISOU 1123  CE1 TYR A 135     4625   4168   3114   -346    493    390       C  
ATOM   1124  CE2 TYR A 135       3.495  18.844 -30.319  1.00 30.25           C  
ANISOU 1124  CE2 TYR A 135     4293   4062   3140   -244    527    401       C  
ATOM   1125  CZ  TYR A 135       3.342  17.648 -31.002  1.00 30.78           C  
ANISOU 1125  CZ  TYR A 135     4365   4141   3190   -277    514    369       C  
ATOM   1126  OH  TYR A 135       3.597  16.465 -30.366  1.00 31.08           O  
ANISOU 1126  OH  TYR A 135     4235   4224   3349   -239    512    317       O  
ATOM   1127  N   ASP A 136       0.712  20.397 -35.082  1.00 34.96           N  
ANISOU 1127  N   ASP A 136     5807   4399   3076   -398    207    625       N  
ATOM   1128  CA  ASP A 136       0.312  19.235 -35.924  1.00 36.40           C  
ANISOU 1128  CA  ASP A 136     6029   4590   3210   -430    152    604       C  
ATOM   1129  C   ASP A 136       1.485  18.872 -36.848  1.00 21.35           C  
ATOM   1130  O   ASP A 136       2.569  19.480 -36.720  1.00 38.12           O  
ANISOU 1130  O   ASP A 136     6416   4741   3327   -663    528    451       O  
ATOM   1131  CB  ASP A 136      -0.968  19.536 -36.704  1.00 36.87           C  
ANISOU 1131  CB  ASP A 136     6261   4592   3157   -383    -68    685       C  
ATOM   1132  CG  ASP A 136      -0.895  20.823 -37.505  1.00 38.50           C  
ANISOU 1132  CG  ASP A 136     6775   4676   3177   -436    -88    731       C  
ATOM   1133  OD1 ASP A 136       0.131  21.040 -38.195  1.00 39.34           O  
ANISOU 1133  OD1 ASP A 136     7067   4723   3157   -575     90    680       O  
ATOM   1134  OD2 ASP A 136      -1.850  21.607 -37.422  1.00 38.40           O1-
ANISOU 1134  OD2 ASP A 136     6817   4621   3150   -341   -274    808       O1-
ATOM   1135  N   ASP A 137       1.260  17.919 -37.753  1.00 42.78           N  
ANISOU 1135  N   ASP A 137     7056   5351   3849   -639    325    481       N  
ATOM   1136  CA  ASP A 137       2.256  17.462 -38.759  1.00 45.82           C  
ANISOU 1136  CA  ASP A 137     7586   5690   4132   -799    513    380       C  
ATOM   1137  C   ASP A 137       2.820  18.680 -39.497  1.00 26.89           C  
ATOM   1138  O   ASP A 137       4.020  18.641 -39.765  1.00 47.86           O  
ANISOU 1138  O   ASP A 137     8167   5812   4205  -1046    856    267       O  
ATOM   1139  CB  ASP A 137       1.663  16.397 -39.693  1.00 48.57           C  
ANISOU 1139  CB  ASP A 137     8017   6036   4402   -828    427    374       C  
ATOM   1140  CG  ASP A 137       1.436  15.033 -39.027  1.00 50.71           C  
ANISOU 1140  CG  ASP A 137     8005   6411   4853   -753    390    340       C  
ATOM   1141  OD1 ASP A 137       1.875  14.842 -37.849  1.00 51.22           O  
ANISOU 1141  OD1 ASP A 137     7818   6543   5098   -689    446    311       O  
ATOM   1142  OD2 ASP A 137       0.781  14.166 -39.662  1.00 54.57           O1-
ANISOU 1142  OD2 ASP A 137     8533   6905   5297   -756    293    345       O1-
ATOM   1143  N   GLU A 138       2.021  19.732 -39.741  1.00 48.61           N  
ANISOU 1143  N   GLU A 138     8427   5859   4183   -871    468    489       N  
ATOM   1144  CA  GLU A 138       2.349  20.840 -40.688  1.00 49.59           C  
ANISOU 1144  CA  GLU A 138     8916   5844   4081   -990    536    506       C  
ATOM   1145  C   GLU A 138       2.792  22.133 -39.988  1.00 46.12           C  
ANISOU 1145  C   GLU A 138     8474   5376   3673   -977    608    528       C  
ATOM   1146  O   GLU A 138       3.574  22.867 -40.581  1.00 47.90           O  
ANISOU 1146  O   GLU A 138     8937   5504   3760  -1117    778    489       O  
ATOM   1147  CB  GLU A 138       1.141  21.212 -41.540  1.00 54.34           C  
ANISOU 1147  CB  GLU A 138     9790   6354   4502   -946    284    614       C  
ATOM   1148  CG  GLU A 138       0.444  20.039 -42.179  1.00 58.74           C  
ANISOU 1148  CG  GLU A 138    10349   6938   5033   -932    153    610       C  
ATOM   1149  CD  GLU A 138      -0.362  20.477 -43.386  1.00 64.02           C  
ANISOU 1149  CD  GLU A 138    11393   7472   5459   -952    -40    682       C  
ATOM   1150  OE1 GLU A 138      -1.234  19.692 -43.813  1.00 67.41           O  
ANISOU 1150  OE1 GLU A 138    11815   7917   5880   -898   -224    699       O  
ATOM   1151  OE2 GLU A 138      -0.105  21.601 -43.902  1.00 67.79           O1-
ANISOU 1151  OE2 GLU A 138    12181   7820   5755  -1023    -11    718       O1-
ATOM   1152  N   LYS A 139       2.280  22.469 -38.816  1.00 41.88           N  
ANISOU 1152  N   LYS A 139     7705   4910   3297   -824    489    587       N  
ATOM   1153  CA  LYS A 139       2.622  23.776 -38.219  1.00 40.35           C  
ANISOU 1153  CA  LYS A 139     7537   4678   3115   -811    542    615       C  
ATOM   1154  C   LYS A 139       2.581  23.726 -36.690  1.00 37.58           C  
ANISOU 1154  C   LYS A 139     6831   4444   3002   -678    518    617       C  
ATOM   1155  O   LYS A 139       1.976  22.801 -36.098  1.00 35.88           O  
ANISOU 1155  O   LYS A 139     6384   4325   2924   -574    408    628       O  
ATOM   1156  CB  LYS A 139       1.640  24.834 -38.708  1.00 41.56           C  
ANISOU 1156  CB  LYS A 139     7955   4722   3112   -757    338    734       C  
ATOM   1157  CG  LYS A 139       0.225  24.662 -38.177  1.00 41.25           C  
ANISOU 1157  CG  LYS A 139     7759   4734   3178   -571     55    821       C  
ATOM   1158  CD  LYS A 139      -0.841  25.496 -38.841  1.00 42.34           C  
ANISOU 1158  CD  LYS A 139     8159   4755   3175   -509   -188    920       C  
ATOM   1159  CE  LYS A 139      -2.230  25.037 -38.436  1.00 42.23           C  
ANISOU 1159  CE  LYS A 139     7952   4800   3294   -339   -455    965       C  
ATOM   1160  NZ  LYS A 139      -2.634  23.759 -39.086  1.00 42.42           N1+
ANISOU 1160  NZ  LYS A 139     7957   4860   3301   -356   -524    934       N1+
ATOM   1161  N   ILE A 140       3.229  24.730 -36.106  1.00 36.42           N  
ANISOU 1161  N   ILE A 140     6672   4277   2889   -694    629    605       N  
ATOM   1162  CA  ILE A 140       3.167  25.103 -34.669  1.00 34.53           C  
ANISOU 1162  CA  ILE A 140     6170   4114   2833   -574    598    624       C  
ATOM   1163  C   ILE A 140       2.591  26.511 -34.590  1.00 34.59           C  
ANISOU 1163  C   ILE A 140     6335   4044   2766   -522    495    721       C  
ATOM   1164  O   ILE A 140       3.173  27.410 -35.222  1.00 35.23           O  
ANISOU 1164  O   ILE A 140     6661   4021   2705   -631    605    711       O  
ATOM   1165  CB  ILE A 140       4.552  25.061 -34.008  1.00 34.02           C  
ANISOU 1165  CB  ILE A 140     5943   4092   2892   -639    823    506       C  
ATOM   1166  CG1 ILE A 140       5.281  23.745 -34.281  1.00 34.27           C  
ANISOU 1166  CG1 ILE A 140     5861   4173   2988   -709    940    388       C  
ATOM   1167  CG2 ILE A 140       4.445  25.351 -32.523  1.00 32.21           C  
ANISOU 1167  CG2 ILE A 140     5460   3939   2840   -513    772    528       C  
ATOM   1168  CD1 ILE A 140       6.793  23.888 -34.253  1.00 35.16           C  
ANISOU 1168  CD1 ILE A 140     5932   4270   3159   -832   1192    238       C  
ATOM   1169  N   ILE A 141       1.492  26.674 -33.854  1.00 33.46           N  
ANISOU 1169  N   ILE A 141     6057   3940   2715   -369    299    802       N  
ATOM   1170  CA  ILE A 141       0.930  28.012 -33.523  1.00 33.92           C  
ANISOU 1170  CA  ILE A 141     6201   3935   2753   -294    193    882       C  
ATOM   1171  C   ILE A 141       1.245  28.309 -32.063  1.00 32.35           C  
ANISOU 1171  C   ILE A 141     5738   3818   2736   -224    256    864       C  
ATOM   1172  O   ILE A 141       1.107  27.383 -31.244  1.00 31.64           O  
ANISOU 1172  O   ILE A 141     5391   3835   2797   -162    244    837       O  
ATOM   1173  CB  ILE A 141      -0.572  28.071 -33.806  1.00 34.50           C  
ANISOU 1173  CB  ILE A 141     6322   3977   2809   -174    -79    968       C  
ATOM   1174  CG1 ILE A 141      -0.868  27.526 -35.206  1.00 36.19           C  
ANISOU 1174  CG1 ILE A 141     6775   4123   2855   -239   -155    975       C  
ATOM   1175  CG2 ILE A 141      -1.056  29.491 -33.602  1.00 34.97           C  
ANISOU 1175  CG2 ILE A 141     6497   3949   2839   -105   -183   1038       C  
ATOM   1176  CD1 ILE A 141      -2.272  27.734 -35.704  1.00 37.26           C  
ANISOU 1176  CD1 ILE A 141     7015   4195   2949   -130   -441   1047       C  
ATOM   1177  N   SER A 142       1.626  29.550 -31.768  1.00 32.16           N  
ANISOU 1177  N   SER A 142     5797   3737   2687   -238    317    880       N  
ATOM   1178  CA  SER A 142       2.194  29.984 -30.467  1.00 30.60           C  
ANISOU 1178  CA  SER A 142     5392   3599   2635   -202    413    848       C  
ATOM   1179  C   SER A 142       1.652  31.361 -30.091  1.00 30.70           C  
ANISOU 1179  C   SER A 142     5482   3547   2635   -132    327    923       C  
ATOM   1180  O   SER A 142       1.418  32.177 -30.982  1.00 32.36           O  
ANISOU 1180  O   SER A 142     5964   3639   2691   -166    277    971       O  
ATOM   1181  CB  SER A 142       3.688  29.993 -30.549  1.00 30.52           C  
ANISOU 1181  CB  SER A 142     5390   3586   2621   -336    653    742       C  
ATOM   1182  OG  SER A 142       4.122  30.874 -31.574  1.00 31.82           O  
ANISOU 1182  OG  SER A 142     5855   3626   2608   -456    743    742       O  
ATOM   1183  N   GLY A 143       1.455  31.600 -28.807  1.00 29.99           N  
ANISOU 1183  N   GLY A 143     5174   3524   2697    -37    306    929       N  
ATOM   1184  CA  GLY A 143       1.055  32.911 -28.256  1.00 30.55           C  
ANISOU 1184  CA  GLY A 143     5278   3544   2786     30    250    983       C  
ATOM   1185  C   GLY A 143       2.145  33.518 -27.390  1.00 29.87           C  
ANISOU 1185  C   GLY A 143     5106   3478   2764    -12    423    929       C  
ATOM   1186  O   GLY A 143       2.738  32.779 -26.558  1.00 27.96           O  
ANISOU 1186  O   GLY A 143     4646   3334   2644    -12    508    863       O  
ATOM   1187  N   LEU A 144       2.389  34.815 -27.574  1.00 31.14           N  
ANISOU 1187  N   LEU A 144     5441   3545   2848    -45    463    952       N  
ATOM   1188  CA  LEU A 144       3.581  35.483 -27.009  1.00 32.01           C  
ANISOU 1188  CA  LEU A 144     5518   3653   2993   -118    651    885       C  
ATOM   1189  C   LEU A 144       3.203  36.649 -26.103  1.00 31.31           C  
ANISOU 1189  C   LEU A 144     5390   3543   2964    -35    603    931       C  
ATOM   1190  O   LEU A 144       2.133  37.175 -26.256  1.00 31.60           O  
ANISOU 1190  O   LEU A 144     5509   3525   2972     51    441   1014       O  
ATOM   1191  CB  LEU A 144       4.466  35.952 -28.160  1.00 34.21           C  
ANISOU 1191  CB  LEU A 144     6065   3826   3109   -278    803    845       C  
ATOM   1192  CG  LEU A 144       5.172  34.837 -28.925  1.00 35.17           C  
ANISOU 1192  CG  LEU A 144     6196   3973   3193   -390    917    761       C  
ATOM   1193  CD1 LEU A 144       4.228  34.103 -29.887  1.00 36.44           C  
ANISOU 1193  CD1 LEU A 144     6479   4113   3253   -364    763    825       C  
ATOM   1194  CD2 LEU A 144       6.344  35.442 -29.674  1.00 36.67           C  
ANISOU 1194  CD2 LEU A 144     6590   4069   3274   -568   1141    679       C  
ATOM   1195  N   ARG A 145       4.123  37.017 -25.224  1.00 30.70           N  
ANISOU 1195  N   ARG A 145     5191   3501   2973    -64    741    865       N  
ATOM   1196  CA  ARG A 145       3.996  38.111 -24.252  1.00 30.73           C  
ANISOU 1196  CA  ARG A 145     5141   3493   3043     -2    732    889       C  
ATOM   1197  C   ARG A 145       3.920  39.461 -24.972  1.00 32.19           C  
ANISOU 1197  C   ARG A 145     5602   3537   3093    -45    737    939       C  
ATOM   1198  O   ARG A 145       3.298  40.391 -24.399  1.00 32.85           O  
ANISOU 1198  O   ARG A 145     5683   3586   3212     42    653    994       O  
ATOM   1199  CB  ARG A 145       5.157  38.062 -23.258  1.00 30.67           C  
ANISOU 1199  CB  ARG A 145     4951   3552   3150    -41    884    788       C  
ATOM   1200  CG  ARG A 145       4.964  39.014 -22.094  1.00 31.24           C  
ANISOU 1200  CG  ARG A 145     4935   3630   3306     34    864    809       C  
ATOM   1201  CD  ARG A 145       5.408  38.465 -20.773  1.00 31.37           C  
ANISOU 1201  CD  ARG A 145     4700   3749   3469     77    892    746       C  
ATOM   1202  NE  ARG A 145       5.028  39.393 -19.724  1.00 32.05           N  
ANISOU 1202  NE  ARG A 145     4729   3831   3617    151    858    779       N  
ATOM   1203  CZ  ARG A 145       5.885  40.199 -19.097  1.00 33.26           C  
ANISOU 1203  CZ  ARG A 145     4856   3971   3810    115    963    721       C  
ATOM   1204  NH1 ARG A 145       7.162  40.192 -19.431  1.00 34.64           N1+
ANISOU 1204  NH1 ARG A 145     5047   4134   3980      5   1109    620       N1+
ATOM   1205  NH2 ARG A 145       5.487  41.003 -18.127  1.00 32.75           N  
ANISOU 1205  NH2 ARG A 145     4740   3904   3800    184    929    751       N  
ATOM   1206  N   ASP A 146       4.501  39.563 -26.172  1.00 32.92           N  
ANISOU 1206  N   ASP A 146     5934   3541   3033   -175    833    918       N  
ATOM   1207  CA  ASP A 146       4.444  40.782 -27.020  1.00 34.49           C  
ANISOU 1207  CA  ASP A 146     6459   3580   3065   -235    838    970       C  
ATOM   1208  C   ASP A 146       3.064  40.912 -27.687  1.00 15.67           C  
ATOM   1209  O   ASP A 146       2.928  41.711 -28.594  1.00 36.28           O  
ANISOU 1209  O   ASP A 146     7164   3582   3040   -179    559   1134       O  
ATOM   1210  CB  ASP A 146       5.612  40.819 -28.022  1.00 35.78           C  
ANISOU 1210  CB  ASP A 146     6833   3668   3092   -431   1055    891       C  
ATOM   1211  CG  ASP A 146       5.448  39.916 -29.226  1.00 36.52           C  
ANISOU 1211  CG  ASP A 146     7082   3736   3059   -494   1028    897       C  
ATOM   1212  OD1 ASP A 146       4.391  39.243 -29.316  1.00 35.30           O  
ANISOU 1212  OD1 ASP A 146     6868   3622   2922   -378    825    965       O  
ATOM   1213  OD2 ASP A 146       6.375  39.924 -30.091  1.00 39.30           O1-
ANISOU 1213  OD2 ASP A 146     7621   4019   3294   -668   1220    824       O1-
ATOM   1214  N   ASN A 147       2.076  40.131 -27.272  1.00 33.74           N  
ANISOU 1214  N   ASN A 147     6331   3496   2993     -2    421   1115       N  
ATOM   1215  CA  ASN A 147       0.664  40.277 -27.710  1.00 34.67           C  
ANISOU 1215  CA  ASN A 147     6540   3549   3084    121    163   1203       C  
ATOM   1216  C   ASN A 147       0.402  39.647 -29.093  1.00 36.22           C  
ANISOU 1216  C   ASN A 147     6959   3681   3121     70     81   1227       C  
ATOM   1217  O   ASN A 147      -0.756  39.728 -29.551  1.00 36.61           O  
ANISOU 1217  O   ASN A 147     7095   3668   3147    174   -154   1289       O  
ATOM   1218  CB  ASN A 147       0.249  41.752 -27.757  1.00 35.63           C  
ANISOU 1218  CB  ASN A 147     6853   3533   3152    170     75   1264       C  
ATOM   1219  CG  ASN A 147       0.371  42.489 -26.446  1.00 34.22           C  
ANISOU 1219  CG  ASN A 147     6480   3401   3121    228    134   1247       C  
ATOM   1220  ND2 ASN A 147      -0.031  43.737 -26.468  1.00 34.78           N  
ANISOU 1220  ND2 ASN A 147     6705   3351   3157    278     51   1298       N  
ATOM   1221  OD1 ASN A 147       0.790  41.941 -25.432  1.00 33.32           O  
ANISOU 1221  OD1 ASN A 147     6094   3421   3145    232    240   1191       O  
ATOM   1222  N   SER A 148       1.417  39.078 -29.759  1.00 37.06           N  
ANISOU 1222  N   SER A 148     7162   3793   3126    -82    261   1170       N  
ATOM   1223  CA  SER A 148       1.299  38.492 -31.124  1.00 38.38           C  
ANISOU 1223  CA  SER A 148     7572   3890   3120   -157    215   1184       C  
ATOM   1224  C   SER A 148       1.023  36.984 -31.049  1.00 37.33           C  
ANISOU 1224  C   SER A 148     7211   3890   3082   -123    174   1150       C  
ATOM   1225  O   SER A 148       1.368  36.356 -30.022  1.00 35.65           O  
ANISOU 1225  O   SER A 148     6687   3817   3041    -96    262   1093       O  
ATOM   1226  CB  SER A 148       2.531  38.773 -31.936  1.00 39.92           C  
ANISOU 1226  CB  SER A 148     8021   4000   3148   -356    450   1130       C  
ATOM   1227  OG  SER A 148       3.567  37.834 -31.667  1.00 39.29           O  
ANISOU 1227  OG  SER A 148     7739   4036   3152   -452    664   1019       O  
ATOM   1228  N   ILE A 149       0.392  36.436 -32.086  1.00 38.23           N  
ANISOU 1228  N   ILE A 149     7487   3954   3084   -122     34   1183       N  
ATOM   1229  CA  ILE A 149       0.355  34.969 -32.368  1.00 37.99           C  
ANISOU 1229  CA  ILE A 149     7325   4022   3087   -141     37   1141       C  
ATOM   1230  C   ILE A 149       1.325  34.703 -33.505  1.00 39.62           C  
ANISOU 1230  C   ILE A 149     7785   4162   3109   -325    211   1093       C  
ATOM   1231  O   ILE A 149       1.215  35.406 -34.521  1.00 42.51           O  
ANISOU 1231  O   ILE A 149     8508   4373   3270   -385    165   1140       O  
ATOM   1232  CB  ILE A 149      -1.043  34.501 -32.786  1.00 38.50           C  
ANISOU 1232  CB  ILE A 149     7395   4074   3158    -18   -241   1198       C  
ATOM   1233  CG1 ILE A 149      -2.064  34.713 -31.665  1.00 38.33           C  
ANISOU 1233  CG1 ILE A 149     7107   4118   3340    155   -399   1223       C  
ATOM   1234  CG2 ILE A 149      -1.002  33.059 -33.251  1.00 37.54           C  
ANISOU 1234  CG2 ILE A 149     7194   4032   3036    -62   -223   1155       C  
ATOM   1235  CD1 ILE A 149      -3.490  34.906 -32.171  1.00 39.69           C  
ANISOU 1235  CD1 ILE A 149     7363   4211   3507    283   -699   1278       C  
ATOM   1236  N   LYS A 150       2.209  33.717 -33.382  1.00 38.49           N  
ANISOU 1236  N   LYS A 150     7480   4117   3027   -413    397    999       N  
ATOM   1237  CA  LYS A 150       3.155  33.391 -34.476  1.00 39.34           C  
ANISOU 1237  CA  LYS A 150     7809   4162   2976   -600    587    930       C  
ATOM   1238  C   LYS A 150       2.912  31.945 -34.919  1.00 38.89           C  
ANISOU 1238  C   LYS A 150     7660   4181   2937   -602    542    899       C  
ATOM   1239  O   LYS A 150       2.726  31.071 -34.072  1.00 37.32           O  
ANISOU 1239  O   LYS A 150     7139   4117   2922   -512    507    874       O  
ATOM   1240  CB  LYS A 150       4.579  33.691 -34.004  1.00 39.33           C  
ANISOU 1240  CB  LYS A 150     7720   4185   3040   -722    874    818       C  
ATOM   1241  CG  LYS A 150       5.004  35.153 -34.097  1.00 40.56           C  
ANISOU 1241  CG  LYS A 150     8104   4215   3093   -793    969    834       C  
ATOM   1242  CD  LYS A 150       6.433  35.417 -33.611  1.00 40.63           C  
ANISOU 1242  CD  LYS A 150     7997   4251   3189   -917   1258    701       C  
ATOM   1243  CE  LYS A 150       7.147  36.577 -34.272  1.00 42.81           C  
ANISOU 1243  CE  LYS A 150     8599   4372   3297  -1082   1441    674       C  
ATOM   1244  NZ  LYS A 150       7.270  37.721 -33.340  1.00 43.13           N1+
ANISOU 1244  NZ  LYS A 150     8567   4401   3419  -1027   1454    694       N1+
ATOM   1245  N   ILE A 151       2.883  31.720 -36.224  1.00 40.61           N  
ANISOU 1245  N   ILE A 151     8174   4301   2955   -705    540    904       N  
ATOM   1246  CA  ILE A 151       2.720  30.369 -36.833  1.00 40.29           C  
ANISOU 1246  CA  ILE A 151     8095   4313   2900   -732    514    868       C  
ATOM   1247  C   ILE A 151       4.049  29.987 -37.478  1.00 40.97           C  
ANISOU 1247  C   ILE A 151     8279   4376   2911   -936    806    745       C  
ATOM   1248  O   ILE A 151       4.582  30.807 -38.262  1.00 43.20           O  
ANISOU 1248  O   ILE A 151     8887   4521   3006  -1079    935    733       O  
ATOM   1249  CB  ILE A 151       1.587  30.360 -37.865  1.00 41.30           C  
ANISOU 1249  CB  ILE A 151     8493   4342   2857   -689    267    960       C  
ATOM   1250  CG1 ILE A 151       0.281  30.857 -37.261  1.00 41.12           C  
ANISOU 1250  CG1 ILE A 151     8372   4325   2928   -489    -19   1059       C  
ATOM   1251  CG2 ILE A 151       1.416  28.977 -38.433  1.00 41.23           C  
ANISOU 1251  CG2 ILE A 151     8431   4393   2843   -715    243    920       C  
ATOM   1252  CD1 ILE A 151      -0.758  31.184 -38.295  1.00 42.85           C  
ANISOU 1252  CD1 ILE A 151     8901   4408   2973   -444   -280   1142       C  
ATOM   1253  N   TRP A 152       4.549  28.795 -37.136  1.00 39.10           N  
ANISOU 1253  N   TRP A 152     7773   4261   2823   -949    907    650       N  
ATOM   1254  CA  TRP A 152       5.858  28.252 -37.576  1.00 38.72           C  
ANISOU 1254  CA  TRP A 152     7726   4214   2773  -1126   1190    498       C  
ATOM   1255  C   TRP A 152       5.639  27.076 -38.519  1.00 39.44           C  
ANISOU 1255  C   TRP A 152     7892   4309   2784  -1179   1166    472       C  
ATOM   1256  O   TRP A 152       4.764  26.249 -38.220  1.00 38.55           O  
ANISOU 1256  O   TRP A 152     7609   4282   2756  -1046    971    526       O  
ATOM   1257  CB  TRP A 152       6.677  27.850 -36.348  1.00 36.42           C  
ANISOU 1257  CB  TRP A 152     7049   4050   2740  -1085   1312    395       C  
ATOM   1258  CG  TRP A 152       6.786  28.960 -35.359  1.00 35.11           C  
ANISOU 1258  CG  TRP A 152     6796   3886   2656  -1018   1309    428       C  
ATOM   1259  CD1 TRP A 152       5.959  29.212 -34.308  1.00 33.37           C  
ANISOU 1259  CD1 TRP A 152     6395   3732   2551   -841   1118    524       C  
ATOM   1260  CD2 TRP A 152       7.750  30.023 -35.382  1.00 35.57           C  
ANISOU 1260  CD2 TRP A 152     6970   3867   2678  -1139   1515    360       C  
ATOM   1261  CE2 TRP A 152       7.462  30.857 -34.283  1.00 34.54           C  
ANISOU 1261  CE2 TRP A 152     6706   3767   2649  -1017   1426    425       C  
ATOM   1262  CE3 TRP A 152       8.833  30.348 -36.208  1.00 37.02           C  
ANISOU 1262  CE3 TRP A 152     7353   3955   2758  -1348   1781    241       C  
ATOM   1263  NE1 TRP A 152       6.373  30.332 -33.640  1.00 33.00           N  
ANISOU 1263  NE1 TRP A 152     6332   3661   2546   -838   1188    522       N  
ATOM   1264  CZ2 TRP A 152       8.226  31.989 -34.004  1.00 34.98           C  
ANISOU 1264  CZ2 TRP A 152     6822   3764   2706  -1091   1583    379       C  
ATOM   1265  CZ3 TRP A 152       9.578  31.469 -35.929  1.00 37.43           C  
ANISOU 1265  CZ3 TRP A 152     7461   3945   2814  -1427   1944    190       C  
ATOM   1266  CH2 TRP A 152       9.277  32.279 -34.843  1.00 36.28           C  
ANISOU 1266  CH2 TRP A 152     7181   3835   2770  -1296   1840    262       C  
ATOM   1267  N   ASP A 153       6.420  27.000 -39.595  1.00 41.55           N  
ANISOU 1267  N   ASP A 153     8404   4486   2898  -1375   1372    382       N  
ATOM   1268  CA  ASP A 153       6.486  25.777 -40.422  1.00 42.52           C  
ANISOU 1268  CA  ASP A 153     8559   4623   2972  -1451   1411    318       C  
ATOM   1269  C   ASP A 153       7.110  24.693 -39.546  1.00 40.92           C  
ANISOU 1269  C   ASP A 153     7943   4569   3037  -1405   1501    202       C  
ATOM   1270  O   ASP A 153       8.145  24.936 -38.917  1.00 40.30           O  
ANISOU 1270  O   ASP A 153     7693   4518   3100  -1450   1690     91       O  
ATOM   1271  CB  ASP A 153       7.211  25.961 -41.757  1.00 45.15           C  
ANISOU 1271  CB  ASP A 153     9260   4817   3078  -1686   1634    236       C  
ATOM   1272  CG  ASP A 153       7.042  24.722 -42.624  1.00 46.22           C  
ANISOU 1272  CG  ASP A 153     9449   4964   3148  -1743   1625    194       C  
ATOM   1273  OD1 ASP A 153       7.685  23.689 -42.310  1.00 46.14           O1-
ANISOU 1273  OD1 ASP A 153     9158   5055   3319  -1760   1753     67       O1-
ATOM   1274  OD2 ASP A 153       6.176  24.746 -43.522  1.00 17.36           O1-
ATOM   1275  N   LYS A 154       6.437  23.554 -39.474  1.00 40.64           N  
ANISOU 1275  N   LYS A 154     7755   4618   3070  -1308   1346    231       N  
ATOM   1276  CA  LYS A 154       6.806  22.418 -38.600  1.00 39.54           C  
ANISOU 1276  CA  LYS A 154     7236   4611   3175  -1235   1371    146       C  
ATOM   1277  C   LYS A 154       8.146  21.849 -39.071  1.00 40.16           C  
ANISOU 1277  C   LYS A 154     7286   4676   3299  -1401   1650    -44       C  
ATOM   1278  O   LYS A 154       8.922  21.446 -38.215  1.00 39.81           O  
ANISOU 1278  O   LYS A 154     6950   4706   3472  -1369   1740   -152       O  
ATOM   1279  CB  LYS A 154       5.678  21.385 -38.608  1.00 39.04           C  
ANISOU 1279  CB  LYS A 154     7084   4614   3134  -1114   1144    227       C  
ATOM   1280  CG  LYS A 154       5.891  20.193 -37.706  1.00 37.91           C  
ANISOU 1280  CG  LYS A 154     6589   4594   3222  -1028   1137    163       C  
ATOM   1281  CD  LYS A 154       5.510  20.446 -36.296  1.00 36.83           C  
ANISOU 1281  CD  LYS A 154     6206   4536   3252   -867   1016    226       C  
ATOM   1282  CE  LYS A 154       5.630  19.197 -35.442  1.00 36.51           C  
ANISOU 1282  CE  LYS A 154     5863   4598   3411   -782    988    173       C  
ATOM   1283  NZ  LYS A 154       6.972  18.577 -35.559  1.00 37.13           N1+
ANISOU 1283  NZ  LYS A 154     5843   4680   3585   -880   1193      4       N1+
ATOM   1284  N   THR A 155       8.413  21.840 -40.374  1.00 41.30           N  
ANISOU 1284  N   THR A 155     7727   4719   3247  -1574   1781    -93       N  
ATOM   1285  CA  THR A 155       9.623  21.222 -40.958  1.00 42.07           C  
ANISOU 1285  CA  THR A 155     7809   4793   3383  -1749   2060   -292       C  
ATOM   1286  C   THR A 155      10.761  22.262 -40.971  1.00 43.58           C  
ANISOU 1286  C   THR A 155     8076   4908   3574  -1896   2325   -410       C  
ATOM   1287  O   THR A 155      11.815  22.018 -40.351  1.00 43.99           O  
ANISOU 1287  O   THR A 155     7857   5009   3848  -1917   2489   -573       O  
ATOM   1288  CB  THR A 155       9.305  20.697 -42.363  1.00 43.21           C  
ANISOU 1288  CB  THR A 155     8255   4860   3304  -1874   2081   -291       C  
ATOM   1289  CG2 THR A 155      10.427  19.883 -42.954  1.00 44.49           C  
ANISOU 1289  CG2 THR A 155     8373   5007   3524  -2044   2356   -502       C  
ATOM   1290  OG1 THR A 155       8.173  19.841 -42.416  1.00 41.85           O  
ANISOU 1290  OG1 THR A 155     8037   4748   3117  -1743   1825   -179       O  
ATOM   1291  N   SER A 156      10.547  23.405 -41.622  1.00 44.43           N  
ANISOU 1291  N   SER A 156     8542   4892   3448  -1989   2354   -333       N  
ATOM   1292  CA  SER A 156      11.583  24.428 -41.893  1.00 45.76           C  
ANISOU 1292  CA  SER A 156     8869   4956   3561  -2171   2635   -446       C  
ATOM   1293  C   SER A 156      11.841  25.328 -40.675  1.00 44.87           C  
ANISOU 1293  C   SER A 156     8549   4888   3611  -2070   2616   -430       C  
ATOM   1294  O   SER A 156      12.865  26.012 -40.657  1.00 45.50           O  
ANISOU 1294  O   SER A 156     8649   4912   3728  -2207   2864   -563       O  
ATOM   1295  CB  SER A 156      11.167  25.240 -43.080  1.00 47.76           C  
ANISOU 1295  CB  SER A 156     9623   5047   3478  -2306   2650   -356       C  
ATOM   1296  OG  SER A 156      10.186  26.196 -42.722  1.00 47.17           O  
ANISOU 1296  OG  SER A 156     9672   4943   3306  -2168   2404   -158       O  
ATOM   1297  N   LEU A 157      10.893  25.391 -39.742  1.00 43.82           N  
ANISOU 1297  N   LEU A 157     8249   4842   3557  -1850   2335   -272       N  
ATOM   1298  CA  LEU A 157      10.894  26.260 -38.528  1.00 43.03           C  
ANISOU 1298  CA  LEU A 157     7970   4787   3593  -1727   2266   -222       C  
ATOM   1299  C   LEU A 157      10.807  27.737 -38.912  1.00 44.63           C  
ANISOU 1299  C   LEU A 157     8501   4858   3599  -1808   2313   -149       C  
ATOM   1300  O   LEU A 157      11.040  28.579 -38.034  1.00 43.50           O  
ANISOU 1300  O   LEU A 157     8242   4730   3555  -1753   2321   -140       O  
ATOM   1301  CB  LEU A 157      12.151  25.990 -37.697  1.00 42.87           C  
ANISOU 1301  CB  LEU A 157     7613   4836   3840  -1748   2451   -415       C  
ATOM   1302  CG  LEU A 157      12.398  24.522 -37.339  1.00 42.14           C  
ANISOU 1302  CG  LEU A 157     7211   4852   3949  -1680   2420   -512       C  
ATOM   1303  CD1 LEU A 157      13.555  24.386 -36.365  1.00 41.73           C  
ANISOU 1303  CD1 LEU A 157     6822   4858   4174  -1663   2543   -690       C  
ATOM   1304  CD2 LEU A 157      11.151  23.859 -36.768  1.00 40.13           C  
ANISOU 1304  CD2 LEU A 157     6835   4691   3722  -1473   2114   -343       C  
ATOM   1305  N   GLU A 158      10.475  28.052 -40.165  1.00 47.50           N  
ANISOU 1305  N   GLU A 158     9274   5088   3686  -1932   2333    -95       N  
ATOM   1306  CA  GLU A 158      10.255  29.453 -40.607  1.00 50.06           C  
ANISOU 1306  CA  GLU A 158     9968   5263   3789  -2000   2339     -2       C  
ATOM   1307  C   GLU A 158       8.940  29.966 -39.994  1.00 19.27           C  
ATOM   1308  O   GLU A 158       8.047  29.159 -39.689  1.00 46.21           O  
ANISOU 1308  O   GLU A 158     9291   4898   3369  -1615   1764    284       O  
ATOM   1309  CB  GLU A 158      10.237  29.566 -42.131  1.00 54.12           C  
ANISOU 1309  CB  GLU A 158    10956   5613   3994  -2194   2435     -1       C  
ATOM   1310  CG  GLU A 158      11.561  29.217 -42.792  1.00 57.59           C  
ANISOU 1310  CG  GLU A 158    11447   6004   4431  -2444   2811   -221       C  
ATOM   1311  CD  GLU A 158      12.666  30.270 -42.737  1.00 60.13           C  
ANISOU 1311  CD  GLU A 158    11860   6234   4752  -2620   3117   -347       C  
ATOM   1312  OE1 GLU A 158      13.498  30.241 -43.654  1.00 62.82           O  
ANISOU 1312  OE1 GLU A 158    12419   6470   4980  -2864   3415   -496       O  
ATOM   1313  OE2 GLU A 158      12.704  31.118 -41.787  1.00 60.88           O1-
ANISOU 1313  OE2 GLU A 158    11812   6359   4962  -2524   3070   -307       O1-
ATOM   1314  N   CYS A 159       8.836  31.279 -39.816  1.00 47.63           N  
ANISOU 1314  N   CYS A 159     9819   4890   3388  -1774   1983    277       N  
ATOM   1315  CA  CYS A 159       7.604  31.971 -39.393  1.00 46.15           C  
ANISOU 1315  CA  CYS A 159     9680   4688   3166  -1585   1676    461       C  
ATOM   1316  C   CYS A 159       6.745  32.297 -40.621  1.00 47.85           C  
ANISOU 1316  C   CYS A 159    10348   4746   3086  -1616   1511    581       C  
ATOM   1317  O   CYS A 159       7.188  33.066 -41.472  1.00 49.25           O  
ANISOU 1317  O   CYS A 159    10912   4760   3043  -1786   1657    567       O  
ATOM   1318  CB  CYS A 159       7.954  33.251 -38.663  1.00 45.80           C  
ANISOU 1318  CB  CYS A 159     9625   4608   3169  -1574   1742    473       C  
ATOM   1319  SG  CYS A 159       6.469  34.066 -38.047  1.00 45.07           S  
ANISOU 1319  SG  CYS A 159     9543   4503   3077  -1333   1374    675       S  
ATOM   1320  N   LEU A 160       5.541  31.745 -40.694  1.00 47.35           N  
ANISOU 1320  N   LEU A 160    10246   4722   3022  -1456   1212    689       N  
ATOM   1321  CA  LEU A 160       4.650  31.872 -41.870  1.00 49.66           C  
ANISOU 1321  CA  LEU A 160    10944   4872   3054  -1463   1008    792       C  
ATOM   1322  C   LEU A 160       3.670  33.034 -41.704  1.00 50.81           C  
ANISOU 1322  C   LEU A 160    11258   4917   3128  -1322    741    938       C  
ATOM   1323  O   LEU A 160       3.393  33.712 -42.706  1.00 53.49           O  
ANISOU 1323  O   LEU A 160    12053   5070   3203  -1391    664   1004       O  
ATOM   1324  CB  LEU A 160       3.905  30.555 -42.031  1.00 49.00           C  
ANISOU 1324  CB  LEU A 160    10691   4891   3037  -1366    828    805       C  
ATOM   1325  CG  LEU A 160       4.803  29.333 -42.140  1.00 48.66           C  
ANISOU 1325  CG  LEU A 160    10454   4949   3085  -1483   1065    661       C  
ATOM   1326  CD1 LEU A 160       3.960  28.066 -42.127  1.00 48.03           C  
ANISOU 1326  CD1 LEU A 160    10172   4979   3097  -1360    863    686       C  
ATOM   1327  CD2 LEU A 160       5.659  29.412 -43.392  1.00 50.69           C  
ANISOU 1327  CD2 LEU A 160    11092   5064   3102  -1735   1315    577       C  
ATOM   1328  N   LYS A 161       3.125  33.239 -40.507  1.00 49.88           N  
ANISOU 1328  N   LYS A 161    10805   4911   3236  -1130    593    985       N  
ATOM   1329  CA  LYS A 161       2.215  34.387 -40.201  1.00 50.91           C  
ANISOU 1329  CA  LYS A 161    11042   4955   3346   -983    347   1106       C  
ATOM   1330  C   LYS A 161       2.576  34.980 -38.833  1.00 47.80           C  
ANISOU 1330  C   LYS A 161    10331   4658   3173   -909    438   1086       C  
ATOM   1331  O   LYS A 161       3.215  34.298 -38.027  1.00 45.62           O  
ANISOU 1331  O   LYS A 161     9702   4538   3095   -916    601    997       O  
ATOM   1332  CB  LYS A 161       0.734  33.989 -40.161  1.00 52.19           C  
ANISOU 1332  CB  LYS A 161    11111   5146   3572   -776    -23   1195       C  
ATOM   1333  CG  LYS A 161       0.167  33.223 -41.345  1.00 54.96           C  
ANISOU 1333  CG  LYS A 161    11692   5434   3756   -802   -176   1215       C  
ATOM   1334  CD  LYS A 161      -0.626  34.096 -42.286  1.00 59.11           C  
ANISOU 1334  CD  LYS A 161    12665   5748   4047   -768   -434   1316       C  
ATOM   1335  CE  LYS A 161      -1.051  33.354 -43.544  1.00 61.93           C  
ANISOU 1335  CE  LYS A 161    13298   6026   4208   -820   -567   1326       C  
ATOM   1336  NZ  LYS A 161      -1.488  34.281 -44.627  1.00 65.39           N1+
ANISOU 1336  NZ  LYS A 161    14278   6216   4351   -845   -760   1411       N1+
ATOM   1337  N   VAL A 162       2.165  36.215 -38.608  1.00 47.67           N  
ANISOU 1337  N   VAL A 162    10457   4540   3116   -838    322   1166       N  
ATOM   1338  CA  VAL A 162       2.195  36.897 -37.285  1.00 46.27           C  
ANISOU 1338  CA  VAL A 162     9998   4440   3143   -729    334   1172       C  
ATOM   1339  C   VAL A 162       0.865  37.630 -37.113  1.00 47.17           C  
ANISOU 1339  C   VAL A 162    10169   4482   3269   -537      3   1288       C  
ATOM   1340  O   VAL A 162       0.705  38.736 -37.716  1.00 49.87           O  
ANISOU 1340  O   VAL A 162    10883   4640   3427   -562    -71   1353       O  
ATOM   1341  CB  VAL A 162       3.366  37.890 -37.179  1.00 46.44           C  
ANISOU 1341  CB  VAL A 162    10157   4386   3101   -883    611   1119       C  
ATOM   1342  CG1 VAL A 162       3.339  38.663 -35.873  1.00 44.90           C  
ANISOU 1342  CG1 VAL A 162     9706   4255   3097   -769    603   1131       C  
ATOM   1343  CG2 VAL A 162       4.699  37.206 -37.388  1.00 46.10           C  
ANISOU 1343  CG2 VAL A 162    10048   4400   3067  -1077    941    977       C  
ATOM   1344  N   LEU A 163      -0.057  37.067 -36.334  1.00 45.54           N  
ANISOU 1344  N   LEU A 163     9625   4405   3275   -357   -187   1306       N  
ATOM   1345  CA  LEU A 163      -1.384  37.687 -36.127  1.00 46.66           C  
ANISOU 1345  CA  LEU A 163     9771   4487   3472   -165   -506   1389       C  
ATOM   1346  C   LEU A 163      -1.272  38.696 -34.980  1.00 46.81           C  
ANISOU 1346  C   LEU A 163     9626   4527   3633    -95   -458   1397       C  
ATOM   1347  O   LEU A 163      -0.740  38.335 -33.897  1.00 45.80           O  
ANISOU 1347  O   LEU A 163     9158   4554   3690    -95   -288   1338       O  
ATOM   1348  CB  LEU A 163      -2.393  36.573 -35.869  1.00 45.55           C  
ANISOU 1348  CB  LEU A 163     9344   4468   3495    -29   -700   1382       C  
ATOM   1349  CG  LEU A 163      -2.282  35.444 -36.889  1.00 46.27           C  
ANISOU 1349  CG  LEU A 163     9552   4566   3461   -121   -690   1356       C  
ATOM   1350  CD1 LEU A 163      -3.237  34.311 -36.569  1.00 45.58           C  
ANISOU 1350  CD1 LEU A 163     9163   4606   3550      5   -860   1338       C  
ATOM   1351  CD2 LEU A 163      -2.500  35.953 -38.304  1.00 48.68           C  
ANISOU 1351  CD2 LEU A 163    10348   4665   3485   -182   -822   1412       C  
ATOM   1352  N   THR A 164      -1.717  39.935 -35.211  1.00 48.43           N  
ANISOU 1352  N   THR A 164    10080   4570   3749    -40   -602   1466       N  
ATOM   1353  CA  THR A 164      -1.751  40.982 -34.162  1.00 48.28           C  
ANISOU 1353  CA  THR A 164     9927   4555   3864     41   -588   1478       C  
ATOM   1354  C   THR A 164      -3.179  41.504 -33.999  1.00 49.51           C  
ANISOU 1354  C   THR A 164    10056   4644   4112    248   -927   1536       C  
ATOM   1355  O   THR A 164      -3.983  41.367 -34.924  1.00 51.01           O  
ANISOU 1355  O   THR A 164    10453   4728   4201    304  -1172   1576       O  
ATOM   1356  CB  THR A 164      -0.736  42.080 -34.472  1.00 49.31           C  
ANISOU 1356  CB  THR A 164    10362   4552   3820   -108   -388   1484       C  
ATOM   1357  CG2 THR A 164       0.541  41.507 -35.031  1.00 49.37           C  
ANISOU 1357  CG2 THR A 164    10475   4582   3703   -327    -88   1412       C  
ATOM   1358  OG1 THR A 164      -1.333  42.989 -35.388  1.00 51.56           O  
ANISOU 1358  OG1 THR A 164    11060   4618   3912    -79   -596   1567       O  
ATOM   1359  N   GLY A 165      -3.460  42.105 -32.840  1.00 49.19           N  
ANISOU 1359  N   GLY A 165     9767   4658   4266    356   -939   1530       N  
ATOM   1360  CA  GLY A 165      -4.816  42.541 -32.461  1.00 49.80           C  
ANISOU 1360  CA  GLY A 165     9728   4698   4497    561  -1234   1554       C  
ATOM   1361  C   GLY A 165      -4.999  42.592 -30.955  1.00 47.69           C  
ANISOU 1361  C   GLY A 165     9047   4577   4495    650  -1162   1509       C  
ATOM   1362  O   GLY A 165      -5.467  43.631 -30.476  1.00 48.53           O  
ANISOU 1362  O   GLY A 165     9147   4611   4680    750  -1261   1527       O  
ATOM   1363  N   HIS A 166      -4.607  41.538 -30.228  1.00 44.98           N  
ANISOU 1363  N   HIS A 166     8390   4423   4277    611   -992   1452       N  
ATOM   1364  CA  HIS A 166      -4.683  41.528 -28.754  1.00 42.15           C  
ANISOU 1364  CA  HIS A 166     7666   4201   4148    676   -900   1408       C  
ATOM   1365  C   HIS A 166      -3.832  42.701 -28.274  1.00 41.49           C  
ANISOU 1365  C   HIS A 166     7674   4066   4024    618   -736   1419       C  
ATOM   1366  O   HIS A 166      -2.838  43.009 -28.932  1.00 41.89           O  
ANISOU 1366  O   HIS A 166     7979   4047   3892    479   -591   1431       O  
ATOM   1367  CB  HIS A 166      -4.272  40.177 -28.159  1.00 40.31           C  
ANISOU 1367  CB  HIS A 166     7149   4155   4015    625   -744   1350       C  
ATOM   1368  CG  HIS A 166      -5.336  39.125 -28.177  1.00 40.42           C  
ANISOU 1368  CG  HIS A 166     6972   4238   4146    716   -906   1327       C  
ATOM   1369  CD2 HIS A 166      -5.410  37.932 -28.818  1.00 40.52           C  
ANISOU 1369  CD2 HIS A 166     6978   4302   4116    677   -929   1312       C  
ATOM   1370  ND1 HIS A 166      -6.472  39.213 -27.419  1.00 40.08           N  
ANISOU 1370  ND1 HIS A 166     6699   4225   4304    856  -1047   1302       N  
ATOM   1371  CE1 HIS A 166      -7.211  38.132 -27.599  1.00 40.52           C  
ANISOU 1371  CE1 HIS A 166     6614   4343   4437    897  -1149   1270       C  
ATOM   1372  NE2 HIS A 166      -6.580  37.330 -28.457  1.00 40.20           N  
ANISOU 1372  NE2 HIS A 166     6709   4318   4246    792  -1086   1281       N  
ATOM   1373  N   THR A 167      -4.293  43.379 -27.226  1.00 41.13           N  
ANISOU 1373  N   THR A 167     7445   4039   4143    721   -769   1409       N  
ATOM   1374  CA  THR A 167      -3.660  44.562 -26.600  1.00 41.09           C  
ANISOU 1374  CA  THR A 167     7487   3990   4137    691   -638   1414       C  
ATOM   1375  C   THR A 167      -2.925  44.092 -25.351  1.00 38.94           C  
ANISOU 1375  C   THR A 167     6915   3886   3994    645   -414   1353       C  
ATOM   1376  O   THR A 167      -2.451  44.948 -24.572  1.00 39.03           O  
ANISOU 1376  O   THR A 167     6888   3893   4048    634   -301   1342       O  
ATOM   1377  CB  THR A 167      -4.701  45.637 -26.298  1.00 42.90           C  
ANISOU 1377  CB  THR A 167     7723   4115   4463    842   -838   1437       C  
ATOM   1378  CG2 THR A 167      -5.452  46.075 -27.530  1.00 45.72           C  
ANISOU 1378  CG2 THR A 167     8385   4291   4696    903  -1098   1492       C  
ATOM   1379  OG1 THR A 167      -5.666  45.123 -25.386  1.00 42.63           O  
ANISOU 1379  OG1 THR A 167     7348   4189   4660    964   -926   1390       O  
ATOM   1380  N   GLY A 168      -2.845  42.774 -25.169  1.00 37.41           N  
ANISOU 1380  N   GLY A 168     6528   3828   3858    623   -364   1314       N  
ATOM   1381  CA  GLY A 168      -2.096  42.142 -24.069  1.00 35.39           C  
ANISOU 1381  CA  GLY A 168     6015   3724   3709    577   -172   1255       C  
ATOM   1382  C   GLY A 168      -1.582  40.786 -24.492  1.00 34.30           C  
ANISOU 1382  C   GLY A 168     5829   3673   3529    496    -96   1223       C  
ATOM   1383  O   GLY A 168      -2.042  40.276 -25.518  1.00 34.72           O  
ANISOU 1383  O   GLY A 168     6006   3686   3499    496   -211   1247       O  
ATOM   1384  N   SER A 169      -0.646  40.236 -23.723  1.00 32.81           N  
ANISOU 1384  N   SER A 169     5473   3594   3399    433     81   1165       N  
ATOM   1385  CA  SER A 169      -0.083  38.871 -23.879  1.00 31.74           C  
ANISOU 1385  CA  SER A 169     5241   3556   3263    366    164   1117       C  
ATOM   1386  C   SER A 169      -1.167  37.863 -24.289  1.00 31.48           C  
ANISOU 1386  C   SER A 169     5146   3556   3260    435      2   1138       C  
ATOM   1387  O   SER A 169      -2.314  37.928 -23.774  1.00 31.76           O  
ANISOU 1387  O   SER A 169     5057   3603   3406    549   -135   1156       O  
ATOM   1388  CB  SER A 169       0.603  38.456 -22.610  1.00 30.35           C  
ANISOU 1388  CB  SER A 169     4830   3492   3209    358    294   1056       C  
ATOM   1389  OG  SER A 169       1.383  39.539 -22.122  1.00 31.16           O  
ANISOU 1389  OG  SER A 169     4971   3558   3309    319    409   1036       O  
ATOM   1390  N   VAL A 170      -0.820  36.960 -25.204  1.00 31.04           N  
ANISOU 1390  N   VAL A 170     5170   3510   3114    361     25   1124       N  
ATOM   1391  CA  VAL A 170      -1.675  35.810 -25.605  1.00 30.79           C  
ANISOU 1391  CA  VAL A 170     5067   3523   3110    406   -102   1129       C  
ATOM   1392  C   VAL A 170      -1.316  34.645 -24.692  1.00 29.16           C  
ANISOU 1392  C   VAL A 170     4609   3450   3020    398     -7   1074       C  
ATOM   1393  O   VAL A 170      -0.202  34.149 -24.812  1.00 28.61           O  
ANISOU 1393  O   VAL A 170     4543   3415   2913    304    138   1026       O  
ATOM   1394  CB  VAL A 170      -1.501  35.442 -27.083  1.00 31.88           C  
ANISOU 1394  CB  VAL A 170     5440   3593   3080    327   -130   1142       C  
ATOM   1395  CG1 VAL A 170      -2.344  34.230 -27.451  1.00 32.15           C  
ANISOU 1395  CG1 VAL A 170     5386   3679   3150    371   -257   1140       C  
ATOM   1396  CG2 VAL A 170      -1.830  36.618 -27.989  1.00 33.50           C  
ANISOU 1396  CG2 VAL A 170     5940   3644   3146    331   -236   1202       C  
ATOM   1397  N   LEU A 171      -2.249  34.250 -23.823  1.00 28.19           N  
ANISOU 1397  N   LEU A 171     4286   3389   3036    492    -88   1072       N  
ATOM   1398  CA  LEU A 171      -1.976  33.406 -22.643  1.00 26.64           C  
ANISOU 1398  CA  LEU A 171     3868   3301   2955    497      0   1027       C  
ATOM   1399  C   LEU A 171      -2.386  31.975 -22.944  1.00 26.43           C  
ANISOU 1399  C   LEU A 171     3760   3332   2949    495    -45   1009       C  
ATOM   1400  O   LEU A 171      -1.743  31.005 -22.402  1.00 26.10           O  
ANISOU 1400  O   LEU A 171     3606   3364   2945    459     48    967       O  
ATOM   1401  CB  LEU A 171      -2.781  33.958 -21.473  1.00 26.89           C  
ANISOU 1401  CB  LEU A 171     3759   3345   3114    586    -39   1032       C  
ATOM   1402  CG  LEU A 171      -2.392  35.364 -21.012  1.00 26.87           C  
ANISOU 1402  CG  LEU A 171     3814   3289   3105    593     11   1045       C  
ATOM   1403  CD1 LEU A 171      -3.275  35.827 -19.858  1.00 26.51           C  
ANISOU 1403  CD1 LEU A 171     3622   3257   3193    678    -25   1039       C  
ATOM   1404  CD2 LEU A 171      -0.936  35.396 -20.619  1.00 25.95           C  
ANISOU 1404  CD2 LEU A 171     3702   3202   2955    511    176   1008       C  
ATOM   1405  N   CYS A 172      -3.430  31.821 -23.739  1.00 26.93           N  
ANISOU 1405  N   CYS A 172     3874   3360   2998    538   -193   1035       N  
ATOM   1406  CA  CYS A 172      -3.953  30.486 -24.099  1.00 27.51           C  
ANISOU 1406  CA  CYS A 172     3874   3483   3096    538   -250   1016       C  
ATOM   1407  C   CYS A 172      -4.383  30.545 -25.553  1.00 28.50           C  
ANISOU 1407  C   CYS A 172     4185   3534   3110    531   -379   1044       C  
ATOM   1408  O   CYS A 172      -4.707  31.651 -26.018  1.00 29.89           O  
ANISOU 1408  O   CYS A 172     4505   3618   3233    563   -469   1081       O  
ATOM   1409  CB  CYS A 172      -5.121  30.096 -23.192  1.00 27.97           C  
ANISOU 1409  CB  CYS A 172     3732   3586   3309    617   -316    995       C  
ATOM   1410  SG  CYS A 172      -6.316  31.440 -22.969  1.00 29.12           S  
ANISOU 1410  SG  CYS A 172     3866   3658   3540    723   -452   1011       S  
ATOM   1411  N   LEU A 173      -4.355  29.405 -26.237  1.00 28.06           N  
ANISOU 1411  N   LEU A 173     4141   3508   3012    488   -390   1026       N  
ATOM   1412  CA  LEU A 173      -4.926  29.264 -27.598  1.00 28.83           C  
ANISOU 1412  CA  LEU A 173     4407   3538   3008    486   -536   1047       C  
ATOM   1413  C   LEU A 173      -5.288  27.808 -27.821  1.00 28.18           C  
ANISOU 1413  C   LEU A 173     4219   3524   2964    474   -561   1013       C  
ATOM   1414  O   LEU A 173      -4.784  26.949 -27.109  1.00 27.57           O  
ANISOU 1414  O   LEU A 173     3995   3531   2950    443   -439    978       O  
ATOM   1415  CB  LEU A 173      -3.944  29.777 -28.663  1.00 30.00           C  
ANISOU 1415  CB  LEU A 173     4827   3607   2965    388   -469   1068       C  
ATOM   1416  CG  LEU A 173      -2.644  29.002 -28.914  1.00 29.43           C  
ANISOU 1416  CG  LEU A 173     4777   3578   2825    266   -279   1024       C  
ATOM   1417  CD1 LEU A 173      -2.829  27.828 -29.861  1.00 29.79           C  
ANISOU 1417  CD1 LEU A 173     4870   3637   2810    224   -323   1005       C  
ATOM   1418  CD2 LEU A 173      -1.570  29.939 -29.473  1.00 30.04           C  
ANISOU 1418  CD2 LEU A 173     5078   3574   2760    168   -155   1026       C  
ATOM   1419  N   GLN A 174      -6.163  27.562 -28.770  1.00 29.25           N  
ANISOU 1419  N   GLN A 174     4436   3615   3065    504   -730   1021       N  
ATOM   1420  CA  GLN A 174      -6.486  26.223 -29.302  1.00 29.66           C  
ANISOU 1420  CA  GLN A 174     4441   3710   3117    479   -769    990       C  
ATOM   1421  C   GLN A 174      -6.944  26.467 -30.730  1.00 31.53           C  
ANISOU 1421  C   GLN A 174     4912   3849   3219    479   -939   1016       C  
ATOM   1422  O   GLN A 174      -7.523  27.546 -30.988  1.00 32.64           O  
ANISOU 1422  O   GLN A 174     5162   3899   3343    546  -1084   1048       O  
ATOM   1423  CB  GLN A 174      -7.571  25.585 -28.445  1.00 29.63           C  
ANISOU 1423  CB  GLN A 174     4183   3772   3302    554   -829    950       C  
ATOM   1424  CG  GLN A 174      -7.817  24.112 -28.706  1.00 29.82           C  
ANISOU 1424  CG  GLN A 174     4121   3857   3354    522   -829    911       C  
ATOM   1425  CD  GLN A 174      -9.217  23.714 -28.288  1.00 30.39           C  
ANISOU 1425  CD  GLN A 174     4001   3951   3594    599   -948    865       C  
ATOM   1426  NE2 GLN A 174      -9.854  22.895 -29.095  1.00 31.97           N  
ANISOU 1426  NE2 GLN A 174     4208   4148   3791    598  -1060    837       N  
ATOM   1427  OE1 GLN A 174      -9.753  24.156 -27.280  1.00 30.57           O  
ANISOU 1427  OE1 GLN A 174     3874   3988   3754    655   -938    845       O  
ATOM   1428  N   TYR A 175      -6.646  25.553 -31.639  1.00 32.67           N  
ANISOU 1428  N   TYR A 175     5154   3999   3262    405   -925   1002       N  
ATOM   1429  CA  TYR A 175      -7.074  25.676 -33.050  1.00 35.37           C  
ANISOU 1429  CA  TYR A 175     5747   4240   3453    395  -1094   1025       C  
ATOM   1430  C   TYR A 175      -7.615  24.337 -33.542  1.00 36.67           C  
ANISOU 1430  C   TYR A 175     5838   4451   3643    387  -1165    985       C  
ATOM   1431  O   TYR A 175      -7.316  23.300 -32.916  1.00 35.56           O  
ANISOU 1431  O   TYR A 175     5501   4415   3596    356  -1033    944       O  
ATOM   1432  CB  TYR A 175      -5.917  26.216 -33.885  1.00 36.30           C  
ANISOU 1432  CB  TYR A 175     6158   4279   3354    278   -975   1053       C  
ATOM   1433  CG  TYR A 175      -4.739  25.301 -34.125  1.00 35.59           C  
ANISOU 1433  CG  TYR A 175     6081   4245   3198    147   -757   1011       C  
ATOM   1434  CD1 TYR A 175      -4.777  24.346 -35.127  1.00 36.20           C  
ANISOU 1434  CD1 TYR A 175     6259   4315   3180     84   -785    988       C  
ATOM   1435  CD2 TYR A 175      -3.555  25.439 -33.412  1.00 34.45           C  
ANISOU 1435  CD2 TYR A 175     5857   4149   3083     83   -529    984       C  
ATOM   1436  CE1 TYR A 175      -3.693  23.525 -35.391  1.00 36.00           C  
ANISOU 1436  CE1 TYR A 175     6244   4331   3102    -37   -585    936       C  
ATOM   1437  CE2 TYR A 175      -2.461  24.626 -33.664  1.00 34.25           C  
ANISOU 1437  CE2 TYR A 175     5833   4164   3018    -32   -340    926       C  
ATOM   1438  CZ  TYR A 175      -2.529  23.659 -34.658  1.00 35.15           C  
ANISOU 1438  CZ  TYR A 175     6040   4271   3045    -92   -363    900       C  
ATOM   1439  OH  TYR A 175      -1.451  22.868 -34.965  1.00 34.85           O  
ANISOU 1439  OH  TYR A 175     6005   4263   2974   -207   -175    830       O  
ATOM   1440  N   ASP A 176      -8.410  24.372 -34.613  1.00 39.72           N  
ANISOU 1440  N   ASP A 176     6386   4755   3952    418  -1381    993       N  
ATOM   1441  CA  ASP A 176      -8.866  23.157 -35.332  1.00 41.13           C  
ANISOU 1441  CA  ASP A 176     6552   4958   4116    396  -1461    955       C  
ATOM   1442  C   ASP A 176      -8.728  23.429 -36.823  1.00 22.15           C  
ATOM   1443  O   ASP A 176      -8.025  24.377 -37.203  1.00 45.02           O  
ANISOU 1443  O   ASP A 176     7649   5241   4215    287  -1513   1034       O  
ATOM   1444  CB  ASP A 176     -10.278  22.754 -34.900  1.00 41.39           C  
ANISOU 1444  CB  ASP A 176     6345   5027   4356    512  -1642    907       C  
ATOM   1445  CG  ASP A 176     -11.373  23.741 -35.273  1.00 43.42           C  
ANISOU 1445  CG  ASP A 176     6678   5175   4644    631  -1919    914       C  
ATOM   1446  OD1 ASP A 176     -11.044  24.796 -35.889  1.00 44.09           O  
ANISOU 1446  OD1 ASP A 176     7037   5146   4568    627  -1983    973       O  
ATOM   1447  OD2 ASP A 176     -12.561  23.424 -34.983  1.00 44.09           O1-
ANISOU 1447  OD2 ASP A 176     6554   5281   4916    724  -2073    851       O1-
ATOM   1448  N   GLU A 177      -9.396  22.609 -37.629  1.00 48.30           N  
ANISOU 1448  N   GLU A 177     7857   5732   4763    346  -1721    959       N  
ATOM   1449  CA  GLU A 177      -9.402  22.678 -39.108  1.00 51.20           C  
ANISOU 1449  CA  GLU A 177     8576   5978   4898    291  -1852    982       C  
ATOM   1450  C   GLU A 177      -9.820  24.096 -39.543  1.00 24.54           C  
ATOM   1451  O   GLU A 177      -9.301  24.558 -40.548  1.00 51.66           O  
ANISOU 1451  O   GLU A 177     9248   5766   4615    278  -2058   1081       O  
ATOM   1452  CB  GLU A 177     -10.282  21.544 -39.654  1.00 54.66           C  
ANISOU 1452  CB  GLU A 177     8938   6443   5385    317  -2013    930       C  
ATOM   1453  CG  GLU A 177     -10.092  20.193 -38.943  1.00 55.84           C  
ANISOU 1453  CG  GLU A 177     8782   6746   5689    280  -1836    872       C  
ATOM   1454  CD  GLU A 177     -11.110  19.810 -37.847  1.00 58.95           C  
ANISOU 1454  CD  GLU A 177     8808   7230   6361    392  -1901    820       C  
ATOM   1455  OE1 GLU A 177     -12.315  20.252 -37.936  1.00 61.58           O  
ANISOU 1455  OE1 GLU A 177     9093   7510   6794    509  -2154    798       O  
ATOM   1456  OE2 GLU A 177     -10.722  19.031 -36.886  1.00 58.66           O1-
ANISOU 1456  OE2 GLU A 177     8528   7310   6450    360  -1701    790       O1-
ATOM   1457  N   ARG A 178     -10.702  24.765 -38.791  1.00 51.41           N  
ANISOU 1457  N   ARG A 178     8673   5849   5011    504  -2205   1034       N  
ATOM   1458  CA  ARG A 178     -11.415  25.999 -39.219  1.00 53.09           C  
ANISOU 1458  CA  ARG A 178     9087   5908   5178    610  -2475   1071       C  
ATOM   1459  C   ARG A 178     -10.826  27.239 -38.531  1.00 50.26           C  
ANISOU 1459  C   ARG A 178     8768   5517   4813    615  -2354   1121       C  
ATOM   1460  O   ARG A 178     -10.705  28.231 -39.232  1.00 52.13           O  
ANISOU 1460  O   ARG A 178     9336   5602   4871    612  -2461   1178       O  
ATOM   1461  CB  ARG A 178     -12.934  25.840 -39.003  1.00 55.91           C  
ANISOU 1461  CB  ARG A 178     9212   6265   5764    773  -2764   1006       C  
ATOM   1462  CG  ARG A 178     -13.650  25.228 -40.205  1.00 59.87           C  
ANISOU 1462  CG  ARG A 178     9871   6694   6182    792  -3020    977       C  
ATOM   1463  CD  ARG A 178     -14.920  24.463 -39.875  1.00 62.37           C  
ANISOU 1463  CD  ARG A 178     9855   7078   6764    901  -3195    874       C  
ATOM   1464  NE  ARG A 178     -14.606  23.144 -39.312  1.00 63.71           N  
ANISOU 1464  NE  ARG A 178     9759   7415   7033    817  -2956    828       N  
ATOM   1465  CZ  ARG A 178     -14.925  22.682 -38.081  1.00 64.06           C  
ANISOU 1465  CZ  ARG A 178     9419   7590   7332    849  -2825    766       C  
ATOM   1466  NH1 ARG A 178     -14.556  21.459 -37.714  1.00 62.59           N1+
ANISOU 1466  NH1 ARG A 178     9060   7530   7191    762  -2619    735       N1+
ATOM   1467  NH2 ARG A 178     -15.619  23.415 -37.222  1.00 65.20           N  
ANISOU 1467  NH2 ARG A 178     9361   7729   7683    961  -2898    730       N  
ATOM   1468  N   VAL A 179     -10.524  27.225 -37.227  1.00 46.32           N  
ANISOU 1468  N   VAL A 179     7964   5140   4494    626  -2158   1101       N  
ATOM   1469  CA  VAL A 179     -10.225  28.486 -36.470  1.00 44.68           C  
ANISOU 1469  CA  VAL A 179     7755   4899   4323    663  -2093   1139       C  
ATOM   1470  C   VAL A 179      -9.120  28.305 -35.434  1.00 41.81           C  
ANISOU 1470  C   VAL A 179     7215   4658   4012    578  -1767   1134       C  
ATOM   1471  O   VAL A 179      -8.891  27.175 -34.970  1.00 39.24           O  
ANISOU 1471  O   VAL A 179     6670   4462   3778    535  -1626   1089       O  
ATOM   1472  CB  VAL A 179     -11.443  29.047 -35.716  1.00 44.94           C  
ANISOU 1472  CB  VAL A 179     7559   4924   4594    832  -2291   1105       C  
ATOM   1473  CG1 VAL A 179     -12.468  29.650 -36.650  1.00 47.08           C  
ANISOU 1473  CG1 VAL A 179     8030   5036   4823    943  -2645   1109       C  
ATOM   1474  CG2 VAL A 179     -12.058  28.005 -34.784  1.00 43.73           C  
ANISOU 1474  CG2 VAL A 179     7003   4920   4693    873  -2241   1023       C  
ATOM   1475  N   ILE A 180      -8.553  29.452 -35.046  1.00 41.43           N  
ANISOU 1475  N   ILE A 180     7260   4559   3921    569  -1679   1174       N  
ATOM   1476  CA  ILE A 180      -7.717  29.673 -33.837  1.00 39.65           C  
ANISOU 1476  CA  ILE A 180     6846   4429   3790    534  -1428   1167       C  
ATOM   1477  C   ILE A 180      -8.551  30.479 -32.858  1.00 39.92           C  
ANISOU 1477  C   ILE A 180     6692   4462   4014    670  -1534   1162       C  
ATOM   1478  O   ILE A 180      -9.178  31.454 -33.306  1.00 41.54           O  
ANISOU 1478  O   ILE A 180     7059   4539   4183    750  -1737   1192       O  
ATOM   1479  CB  ILE A 180      -6.453  30.482 -34.155  1.00 39.68           C  
ANISOU 1479  CB  ILE A 180     7106   4364   3607    417  -1248   1204       C  
ATOM   1480  CG1 ILE A 180      -5.672  29.886 -35.328  1.00 40.10           C  
ANISOU 1480  CG1 ILE A 180     7410   4380   3448    271  -1153   1201       C  
ATOM   1481  CG2 ILE A 180      -5.599  30.609 -32.895  1.00 37.87           C  
ANISOU 1481  CG2 ILE A 180     6658   4238   3492    386  -1007   1181       C  
ATOM   1482  CD1 ILE A 180      -4.635  30.828 -35.894  1.00 41.08           C  
ANISOU 1482  CD1 ILE A 180     7852   4392   3365    151  -1011   1230       C  
ATOM   1483  N   VAL A 181      -8.492  30.117 -31.578  1.00 38.39           N  
ANISOU 1483  N   VAL A 181     6192   4393   4003    688  -1394   1124       N  
ATOM   1484  CA  VAL A 181      -9.192  30.847 -30.485  1.00 38.18           C  
ANISOU 1484  CA  VAL A 181     5963   4377   4167    799  -1443   1106       C  
ATOM   1485  C   VAL A 181      -8.168  31.210 -29.424  1.00 35.96           C  
ANISOU 1485  C   VAL A 181     5596   4160   3907    744  -1199   1114       C  
ATOM   1486  O   VAL A 181      -7.448  30.308 -29.006  1.00 35.35           O  
ANISOU 1486  O   VAL A 181     5409   4184   3839    667  -1020   1091       O  
ATOM   1487  CB  VAL A 181     -10.302  29.976 -29.878  1.00 38.49           C  
ANISOU 1487  CB  VAL A 181     5701   4499   4425    874  -1519   1034       C  
ATOM   1488  CG1 VAL A 181     -11.101  30.760 -28.846  1.00 38.96           C  
ANISOU 1488  CG1 VAL A 181     5566   4554   4684    981  -1570    999       C  
ATOM   1489  CG2 VAL A 181     -11.202  29.396 -30.960  1.00 40.11           C  
ANISOU 1489  CG2 VAL A 181     5971   4656   4614    913  -1746   1009       C  
ATOM   1490  N   THR A 182      -8.144  32.454 -28.964  1.00 35.34           N  
ANISOU 1490  N   THR A 182     5556   4023   3850    789  -1205   1139       N  
ATOM   1491  CA  THR A 182      -7.103  32.939 -28.022  1.00 33.81           C  
ANISOU 1491  CA  THR A 182     5312   3875   3661    734   -982   1146       C  
ATOM   1492  C   THR A 182      -7.723  33.760 -26.898  1.00 33.15           C  
ANISOU 1492  C   THR A 182     5057   3794   3746    832  -1010   1131       C  
ATOM   1493  O   THR A 182      -8.683  34.501 -27.193  1.00 34.61           O  
ANISOU 1493  O   THR A 182     5287   3885   3976    931  -1207   1135       O  
ATOM   1494  CB  THR A 182      -6.085  33.784 -28.779  1.00 34.83           C  
ANISOU 1494  CB  THR A 182     5740   3908   3587    648   -910   1194       C  
ATOM   1495  CG2 THR A 182      -5.303  32.951 -29.765  1.00 35.10           C  
ANISOU 1495  CG2 THR A 182     5928   3946   3460    527   -825   1191       C  
ATOM   1496  OG1 THR A 182      -6.808  34.826 -29.446  1.00 36.33           O  
ANISOU 1496  OG1 THR A 182     6128   3954   3720    722  -1116   1235       O  
ATOM   1497  N   GLY A 183      -7.182  33.615 -25.684  1.00 31.10           N  
ANISOU 1497  N   GLY A 183     4617   3627   3571    804   -826   1107       N  
ATOM   1498  CA  GLY A 183      -7.426  34.516 -24.546  1.00 30.91           C  
ANISOU 1498  CA  GLY A 183     4469   3603   3672    865   -792   1095       C  
ATOM   1499  C   GLY A 183      -6.199  35.340 -24.239  1.00 30.50           C  
ANISOU 1499  C   GLY A 183     4527   3535   3527    798   -632   1125       C  
ATOM   1500  O   GLY A 183      -5.085  34.824 -24.353  1.00 30.86           O  
ANISOU 1500  O   GLY A 183     4616   3626   3482    698   -483   1123       O  
ATOM   1501  N   SER A 184      -6.372  36.590 -23.871  1.00 31.08           N  
ANISOU 1501  N   SER A 184     4639   3541   3631    849   -661   1141       N  
ATOM   1502  CA  SER A 184      -5.241  37.510 -23.628  1.00 31.14           C  
ANISOU 1502  CA  SER A 184     4763   3517   3550    785   -515   1164       C  
ATOM   1503  C   SER A 184      -5.346  38.125 -22.231  1.00 30.49           C  
ANISOU 1503  C   SER A 184     4507   3472   3607    831   -442   1140       C  
ATOM   1504  O   SER A 184      -6.445  38.105 -21.634  1.00 31.24           O  
ANISOU 1504  O   SER A 184     4435   3581   3854    922   -530   1110       O  
ATOM   1505  CB  SER A 184      -5.236  38.553 -24.711  1.00 33.17           C  
ANISOU 1505  CB  SER A 184     5308   3629   3669    786   -618   1217       C  
ATOM   1506  OG  SER A 184      -4.396  39.644 -24.364  1.00 33.59           O  
ANISOU 1506  OG  SER A 184     5459   3635   3669    742   -495   1232       O  
ATOM   1507  N   SER A 185      -4.237  38.656 -21.729  1.00 29.73           N  
ANISOU 1507  N   SER A 185     4447   3386   3464    766   -280   1140       N  
ATOM   1508  CA  SER A 185      -4.200  39.639 -20.619  1.00 29.35           C  
ANISOU 1508  CA  SER A 185     4319   3332   3502    801   -219   1130       C  
ATOM   1509  C   SER A 185      -5.219  40.765 -20.876  1.00 31.08           C  
ANISOU 1509  C   SER A 185     4608   3438   3762    901   -382   1153       C  
ATOM   1510  O   SER A 185      -5.717  41.340 -19.912  1.00 31.05           O  
ANISOU 1510  O   SER A 185     4474   3437   3885    964   -380   1128       O  
ATOM   1511  CB  SER A 185      -2.818  40.199 -20.454  1.00 28.96           C  
ANISOU 1511  CB  SER A 185     4365   3276   3364    709    -53   1129       C  
ATOM   1512  OG  SER A 185      -1.847  39.186 -20.273  1.00 28.06           O  
ANISOU 1512  OG  SER A 185     4183   3252   3226    626     78   1092       O  
ATOM   1513  N   ASP A 186      -5.525  41.087 -22.131  1.00 32.79           N  
ANISOU 1513  N   ASP A 186     5036   3547   3876    917   -526   1195       N  
ATOM   1514  CA  ASP A 186      -6.464  42.187 -22.475  1.00 34.60           C  
ANISOU 1514  CA  ASP A 186     5363   3645   4139   1023   -715   1215       C  
ATOM   1515  C   ASP A 186      -7.927  41.810 -22.175  1.00 17.16           C  
ATOM   1516  O   ASP A 186      -8.792  42.664 -22.459  1.00 36.38           O  
ANISOU 1516  O   ASP A 186     5434   3774   4615   1251  -1065   1164       O  
ATOM   1517  CB  ASP A 186      -6.314  42.590 -23.938  1.00 36.20           C  
ANISOU 1517  CB  ASP A 186     5891   3712   4153    999   -832   1275       C  
ATOM   1518  CG  ASP A 186      -6.825  41.569 -24.942  1.00 37.02           C  
ANISOU 1518  CG  ASP A 186     6042   3817   4208   1005   -970   1278       C  
ATOM   1519  OD1 ASP A 186      -7.662  40.703 -24.577  1.00 36.78           O  
ANISOU 1519  OD1 ASP A 186     5780   3868   4326   1066  -1038   1230       O  
ATOM   1520  OD2 ASP A 186      -6.394  41.659 -26.081  1.00 38.97           O1-
ANISOU 1520  OD2 ASP A 186     6565   3976   4266    941  -1001   1323       O1-
ATOM   1521  N   SER A 187      -8.219  40.583 -21.699  1.00 34.50           N  
ANISOU 1521  N   SER A 187     4924   3770   4413   1134   -832   1116       N  
ATOM   1522  CA  SER A 187      -9.562  40.158 -21.196  1.00 34.93           C  
ANISOU 1522  CA  SER A 187     4738   3855   4677   1228   -935   1041       C  
ATOM   1523  C   SER A 187     -10.497  39.707 -22.321  1.00 35.73           C  
ANISOU 1523  C   SER A 187     4887   3900   4790   1292  -1165   1030       C  
ATOM   1524  O   SER A 187     -11.651  39.318 -22.006  1.00 35.80           O  
ANISOU 1524  O   SER A 187     4688   3927   4988   1367  -1259    950       O  
ATOM   1525  CB  SER A 187     -10.245  41.233 -20.412  1.00 36.06           C  
ANISOU 1525  CB  SER A 187     4781   3945   4975   1318   -973   1000       C  
ATOM   1526  OG  SER A 187      -9.397  41.669 -19.360  1.00 36.59           O  
ANISOU 1526  OG  SER A 187     4812   4061   5028   1259   -769   1008       O  
ATOM   1527  N   THR A 188     -10.033  39.757 -23.573  1.00 36.01           N  
ANISOU 1527  N   THR A 188     5187   3861   4633   1257  -1248   1097       N  
ATOM   1528  CA  THR A 188     -10.821  39.337 -24.751  1.00 37.21           C  
ANISOU 1528  CA  THR A 188     5431   3946   4762   1311  -1481   1094       C  
ATOM   1529  C   THR A 188     -10.491  37.895 -25.085  1.00 36.38           C  
ANISOU 1529  C   THR A 188     5283   3945   4595   1225  -1403   1089       C  
ATOM   1530  O   THR A 188      -9.379  37.431 -24.762  1.00 34.59           O  
ANISOU 1530  O   THR A 188     5063   3804   4275   1113  -1186   1112       O  
ATOM   1531  CB  THR A 188     -10.564  40.210 -25.976  1.00 38.80           C  
ANISOU 1531  CB  THR A 188     5987   3987   4769   1318  -1628   1170       C  
ATOM   1532  CG2 THR A 188     -10.784  41.674 -25.682  1.00 40.10           C  
ANISOU 1532  CG2 THR A 188     6227   4034   4976   1397  -1702   1183       C  
ATOM   1533  OG1 THR A 188      -9.230  40.050 -26.439  1.00 37.97           O  
ANISOU 1533  OG1 THR A 188     6092   3896   4440   1176  -1452   1234       O  
ATOM   1534  N   VAL A 189     -11.455  37.227 -25.699  1.00 37.82           N  
ANISOU 1534  N   VAL A 189     5413   4116   4843   1283  -1586   1048       N  
ATOM   1535  CA  VAL A 189     -11.206  36.009 -26.511  1.00 38.23           C  
ANISOU 1535  CA  VAL A 189     5525   4216   4785   1211  -1584   1059       C  
ATOM   1536  C   VAL A 189     -11.378  36.416 -27.965  1.00 40.86           C  
ANISOU 1536  C   VAL A 189     6163   4405   4956   1237  -1805   1109       C  
ATOM   1537  O   VAL A 189     -12.340  37.159 -28.240  1.00 42.60           O  
ANISOU 1537  O   VAL A 189     6413   4514   5260   1359  -2041   1088       O  
ATOM   1538  CB  VAL A 189     -12.140  34.858 -26.123  1.00 37.79           C  
ANISOU 1538  CB  VAL A 189     5191   4252   4914   1243  -1616    972       C  
ATOM   1539  CG1 VAL A 189     -11.995  33.646 -27.031  1.00 37.78           C  
ANISOU 1539  CG1 VAL A 189     5258   4288   4807   1180  -1642    979       C  
ATOM   1540  CG2 VAL A 189     -11.906  34.474 -24.683  1.00 36.23           C  
ANISOU 1540  CG2 VAL A 189     4745   4178   4842   1202  -1387    930       C  
ATOM   1541  N   ARG A 190     -10.463  35.975 -28.828  1.00 41.80           N  
ANISOU 1541  N   ARG A 190     6506   4519   4855   1124  -1729   1164       N  
ATOM   1542  CA  ARG A 190     -10.542  36.252 -30.284  1.00 44.87           C  
ANISOU 1542  CA  ARG A 190     7234   4764   5049   1122  -1921   1214       C  
ATOM   1543  C   ARG A 190     -10.557  34.944 -31.061  1.00 43.79           C  
ANISOU 1543  C   ARG A 190     7119   4680   4841   1063  -1941   1200       C  
ATOM   1544  O   ARG A 190      -9.743  34.053 -30.748  1.00 42.33           O  
ANISOU 1544  O   ARG A 190     6840   4617   4628    954  -1714   1191       O  
ATOM   1545  CB  ARG A 190      -9.382  37.150 -30.709  1.00 47.12           C  
ANISOU 1545  CB  ARG A 190     7836   4960   5106   1023  -1796   1291       C  
ATOM   1546  CG  ARG A 190      -9.698  38.625 -30.551  1.00 50.28           C  
ANISOU 1546  CG  ARG A 190     8355   5227   5524   1112  -1914   1320       C  
ATOM   1547  CD  ARG A 190      -8.450  39.468 -30.614  1.00 52.16           C  
ANISOU 1547  CD  ARG A 190     8832   5409   5579    997  -1716   1379       C  
ATOM   1548  NE  ARG A 190      -8.577  40.765 -29.967  1.00 54.33           N  
ANISOU 1548  NE  ARG A 190     9106   5612   5924   1067  -1736   1392       N  
ATOM   1549  CZ  ARG A 190      -8.682  41.922 -30.639  1.00 58.32           C  
ANISOU 1549  CZ  ARG A 190     9929   5931   6301   1100  -1882   1447       C  
ATOM   1550  NH1 ARG A 190      -8.638  41.962 -31.975  1.00 58.89           N1+
ANISOU 1550  NH1 ARG A 190    10365   5863   6149   1060  -2016   1497       N1+
ATOM   1551  NH2 ARG A 190      -8.790  43.046 -29.947  1.00 59.83           N  
ANISOU 1551  NH2 ARG A 190    10088   6068   6577   1166  -1886   1452       N  
ATOM   1552  N   VAL A 191     -11.480  34.851 -32.008  1.00 44.68           N  
ANISOU 1552  N   VAL A 191     7343   4696   4936   1140  -2218   1190       N  
ATOM   1553  CA  VAL A 191     -11.571  33.744 -32.999  1.00 44.86           C  
ANISOU 1553  CA  VAL A 191     7457   4732   4856   1088  -2287   1182       C  
ATOM   1554  C   VAL A 191     -10.941  34.243 -34.297  1.00 45.19           C  
ANISOU 1554  C   VAL A 191     7948   4625   4599   1011  -2340   1261       C  
ATOM   1555  O   VAL A 191     -11.418  35.246 -34.816  1.00 46.54           O  
ANISOU 1555  O   VAL A 191     8338   4635   4709   1092  -2562   1293       O  
ATOM   1556  CB  VAL A 191     -13.036  33.332 -33.216  1.00 46.75           C  
ANISOU 1556  CB  VAL A 191     7536   4951   5275   1224  -2574   1107       C  
ATOM   1557  CG1 VAL A 191     -13.157  32.101 -34.105  1.00 47.28           C  
ANISOU 1557  CG1 VAL A 191     7653   5049   5260   1171  -2631   1089       C  
ATOM   1558  CG2 VAL A 191     -13.754  33.132 -31.892  1.00 46.23           C  
ANISOU 1558  CG2 VAL A 191     7055   4997   5514   1302  -2522   1018       C  
ATOM   1559  N   TRP A 192      -9.912  33.567 -34.795  1.00 43.80           N  
ANISOU 1559  N   TRP A 192     7908   4491   4243    856  -2142   1284       N  
ATOM   1560  CA  TRP A 192      -9.256  33.913 -36.080  1.00 44.98           C  
ANISOU 1560  CA  TRP A 192     8502   4500   4090    749  -2150   1345       C  
ATOM   1561  C   TRP A 192      -9.476  32.772 -37.079  1.00 45.79           C  
ANISOU 1561  C   TRP A 192     8694   4608   4095    703  -2235   1326       C  
ATOM   1562  O   TRP A 192      -9.621  31.615 -36.645  1.00 44.90           O  
ANISOU 1562  O   TRP A 192     8291   4645   4124    697  -2160   1270       O  
ATOM   1563  CB  TRP A 192      -7.768  34.194 -35.876  1.00 43.59           C  
ANISOU 1563  CB  TRP A 192     8433   4350   3780    588  -1818   1369       C  
ATOM   1564  CG  TRP A 192      -7.402  34.894 -34.605  1.00 41.92           C  
ANISOU 1564  CG  TRP A 192     8010   4202   3715    614  -1662   1364       C  
ATOM   1565  CD1 TRP A 192      -7.533  34.399 -33.341  1.00 40.41           C  
ANISOU 1565  CD1 TRP A 192     7423   4171   3759    663  -1558   1314       C  
ATOM   1566  CD2 TRP A 192      -6.729  36.156 -34.463  1.00 41.79           C  
ANISOU 1566  CD2 TRP A 192     8182   4092   3602    573  -1561   1406       C  
ATOM   1567  CE2 TRP A 192      -6.533  36.371 -33.085  1.00 40.22           C  
ANISOU 1567  CE2 TRP A 192     7671   4010   3602    611  -1417   1377       C  
ATOM   1568  CE3 TRP A 192      -6.257  37.119 -35.356  1.00 43.36           C  
ANISOU 1568  CE3 TRP A 192     8800   4116   3561    498  -1570   1463       C  
ATOM   1569  NE1 TRP A 192      -7.030  35.285 -32.424  1.00 39.35           N  
ANISOU 1569  NE1 TRP A 192     7218   4049   3684    664  -1419   1323       N  
ATOM   1570  CZ2 TRP A 192      -5.925  37.518 -32.579  1.00 40.37           C  
ANISOU 1570  CZ2 TRP A 192     7760   3980   3599    587  -1297   1401       C  
ATOM   1571  CZ3 TRP A 192      -5.661  38.260 -34.864  1.00 43.44           C  
ANISOU 1571  CZ3 TRP A 192     8884   4072   3549    471  -1444   1487       C  
ATOM   1572  CH2 TRP A 192      -5.491  38.452 -33.494  1.00 42.02           C  
ANISOU 1572  CH2 TRP A 192     8368   4017   3580    517  -1310   1455       C  
ATOM   1573  N   ASP A 193      -9.513  33.079 -38.372  1.00 48.00           N  
ANISOU 1573  N   ASP A 193     9380   4724   4134    667  -2390   1371       N  
ATOM   1574  CA  ASP A 193      -9.463  32.051 -39.446  1.00 49.02           C  
ANISOU 1574  CA  ASP A 193     9671   4845   4111    582  -2425   1359       C  
ATOM   1575  C   ASP A 193      -8.074  31.430 -39.403  1.00 16.10           C  
ATOM   1576  O   ASP A 193      -7.095  32.154 -39.530  1.00 46.82           O  
ANISOU 1576  O   ASP A 193     9617   4597   3575    279  -1867   1380       O  
ATOM   1577  CB  ASP A 193      -9.724  32.637 -40.833  1.00 52.61           C  
ANISOU 1577  CB  ASP A 193    10614   5078   4297    573  -2663   1415       C  
ATOM   1578  CG  ASP A 193     -10.076  31.620 -41.897  1.00 53.94           C  
ANISOU 1578  CG  ASP A 193    10919   5225   4351    538  -2798   1394       C  
ATOM   1579  OD1 ASP A 193      -9.231  30.785 -42.273  1.00 53.43           O1-
ANISOU 1579  OD1 ASP A 193    10910   5226   4166    378  -2564   1378       O1-
ATOM   1580  OD2 ASP A 193     -11.214  31.728 -42.381  1.00 18.43           O1-
ATOM   1581  N   VAL A 194      -8.012  30.125 -39.274  1.00 45.47           N  
ANISOU 1581  N   VAL A 194     8999   4632   3645    353  -1960   1293       N  
ATOM   1582  CA  VAL A 194      -6.730  29.376 -39.123  1.00 44.20           C  
ANISOU 1582  CA  VAL A 194     8776   4580   3440    188  -1618   1258       C  
ATOM   1583  C   VAL A 194      -5.857  29.543 -40.378  1.00 46.11           C  
ANISOU 1583  C   VAL A 194     9451   4694   3376     16  -1509   1278       C  
ATOM   1584  O   VAL A 194      -4.653  29.243 -40.281  1.00 45.18           O  
ANISOU 1584  O   VAL A 194     9322   4632   3211   -132  -1205   1240       O  
ATOM   1585  CB  VAL A 194      -6.991  27.896 -38.775  1.00 42.34           C  
ANISOU 1585  CB  VAL A 194     8219   4504   3365    200  -1582   1194       C  
ATOM   1586  CG1 VAL A 194      -7.532  27.115 -39.946  1.00 43.51           C  
ANISOU 1586  CG1 VAL A 194     8536   4600   3394    182  -1751   1184       C  
ATOM   1587  CG2 VAL A 194      -5.751  27.229 -38.219  1.00 40.41           C  
ANISOU 1587  CG2 VAL A 194     7813   4383   3157     78  -1249   1148       C  
ATOM   1588  N   ASN A 195      -6.427  30.004 -41.501  1.00 48.57           N  
ANISOU 1588  N   ASN A 195    10133   4833   3489     30  -1746   1325       N  
ATOM   1589  CA  ASN A 195      -5.735  30.118 -42.812  1.00 50.34           C  
ANISOU 1589  CA  ASN A 195    10823   4911   3391   -142  -1665   1343       C  
ATOM   1590  C   ASN A 195      -5.453  31.588 -43.127  1.00 52.36           C  
ANISOU 1590  C   ASN A 195    11449   4983   3463   -174  -1681   1409       C  
ATOM   1591  O   ASN A 195      -4.262  31.956 -43.179  1.00 51.99           O  
ANISOU 1591  O   ASN A 195    11546   4912   3297   -340  -1380   1396       O  
ATOM   1592  CB  ASN A 195      -6.554  29.521 -43.954  1.00 51.97           C  
ANISOU 1592  CB  ASN A 195    11247   5034   3467   -119  -1929   1350       C  
ATOM   1593  CG  ASN A 195      -7.165  28.185 -43.617  1.00 50.36           C  
ANISOU 1593  CG  ASN A 195    10671   4993   3470    -46  -1995   1291       C  
ATOM   1594  ND2 ASN A 195      -8.491  28.140 -43.603  1.00 51.20           N  
ANISOU 1594  ND2 ASN A 195    10672   5081   3701    129  -2334   1294       N  
ATOM   1595  OD1 ASN A 195      -6.437  27.219 -43.394  1.00 48.34           O  
ANISOU 1595  OD1 ASN A 195    10234   4869   3264   -149  -1742   1234       O  
ATOM   1596  N   THR A 196      -6.503  32.388 -43.350  1.00 54.54           N  
ANISOU 1596  N   THR A 196    11876   5125   3722    -23  -2022   1468       N  
ATOM   1597  CA  THR A 196      -6.389  33.819 -43.745  1.00 57.19           C  
ANISOU 1597  CA  THR A 196    12612   5252   3865    -35  -2095   1541       C  
ATOM   1598  C   THR A 196      -5.850  34.642 -42.568  1.00 55.91           C  
ANISOU 1598  C   THR A 196    12233   5156   3856    -19  -1900   1542       C  
ATOM   1599  O   THR A 196      -5.307  35.724 -42.822  1.00 56.76           O  
ANISOU 1599  O   THR A 196    12658   5117   3790    -97  -1820   1586       O  
ATOM   1600  CB  THR A 196      -7.722  34.400 -44.238  1.00 59.73           C  
ANISOU 1600  CB  THR A 196    13122   5412   4163    148  -2549   1592       C  
ATOM   1601  CG2 THR A 196      -8.298  33.643 -45.413  1.00 61.52           C  
ANISOU 1601  CG2 THR A 196    13581   5559   4234    142  -2775   1588       C  
ATOM   1602  OG1 THR A 196      -8.638  34.403 -43.139  1.00 58.70           O  
ANISOU 1602  OG1 THR A 196    12536   5400   4368    353  -2709   1563       O  
ATOM   1603  N   GLY A 197      -6.006  34.151 -41.335  1.00 54.04           N  
ANISOU 1603  N   GLY A 197    11491   5121   3922     73  -1828   1494       N  
ATOM   1604  CA  GLY A 197      -5.615  34.866 -40.108  1.00 52.78           C  
ANISOU 1604  CA  GLY A 197    11086   5036   3933    109  -1671   1490       C  
ATOM   1605  C   GLY A 197      -6.545  36.029 -39.813  1.00 54.40           C  
ANISOU 1605  C   GLY A 197    11335   5127   4207    282  -1945   1541       C  
ATOM   1606  O   GLY A 197      -6.201  36.844 -38.950  1.00 53.39           O  
ANISOU 1606  O   GLY A 197    11095   5018   4171    300  -1827   1549       O  
ATOM   1607  N   GLU A 198      -7.681  36.123 -40.510  1.00 57.22           N  
ANISOU 1607  N   GLU A 198    11850   5364   4527    407  -2306   1568       N  
ATOM   1608  CA  GLU A 198      -8.653  37.237 -40.343  1.00 59.38           C  
ANISOU 1608  CA  GLU A 198    12185   5504   4875    588  -2614   1604       C  
ATOM   1609  C   GLU A 198      -9.392  37.021 -39.022  1.00 21.10           C  
ATOM   1610  O   GLU A 198      -9.735  35.852 -38.718  1.00 55.69           O  
ANISOU 1610  O   GLU A 198    10869   5359   4930    772  -2645   1484       O  
ATOM   1611  CB  GLU A 198      -9.610  37.385 -41.538  1.00 63.76           C  
ANISOU 1611  CB  GLU A 198    13082   5862   5281    675  -3007   1636       C  
ATOM   1612  CG  GLU A 198     -10.611  36.242 -41.756  1.00 65.28           C  
ANISOU 1612  CG  GLU A 198    13049   6137   5618    778  -3233   1576       C  
ATOM   1613  CD  GLU A 198     -11.532  36.365 -42.986  1.00 69.13           C  
ANISOU 1613  CD  GLU A 198    13890   6422   5955    866  -3644   1597       C  
ATOM   1614  OE1 GLU A 198     -11.993  37.503 -43.240  1.00 70.72           O  
ANISOU 1614  OE1 GLU A 198    14345   6430   6097    970  -3895   1642       O  
ATOM   1615  OE2 GLU A 198     -11.827  35.316 -43.691  1.00 69.72           O1-
ANISOU 1615  OE2 GLU A 198    13989   6524   5976    839  -3736   1566       O1-
ATOM   1616  N   VAL A 199      -9.596  38.097 -38.258  1.00 55.45           N  
ANISOU 1616  N   VAL A 199    11076   5132   4859    845  -2697   1559       N  
ATOM   1617  CA  VAL A 199     -10.360  38.041 -36.984  1.00 53.56           C  
ANISOU 1617  CA  VAL A 199    10363   5026   4962    997  -2743   1497       C  
ATOM   1618  C   VAL A 199     -11.813  37.790 -37.353  1.00 55.05           C  
ANISOU 1618  C   VAL A 199    10472   5158   5288   1174  -3127   1453       C  
ATOM   1619  O   VAL A 199     -12.342  38.587 -38.103  1.00 58.54           O  
ANISOU 1619  O   VAL A 199    11216   5402   5626   1257  -3411   1488       O  
ATOM   1620  CB  VAL A 199     -10.242  39.340 -36.182  1.00 53.30           C  
ANISOU 1620  CB  VAL A 199    10307   4941   5005   1054  -2703   1520       C  
ATOM   1621  CG1 VAL A 199     -11.018  39.216 -34.891  1.00 52.18           C  
ANISOU 1621  CG1 VAL A 199     9687   4933   5205   1192  -2727   1445       C  
ATOM   1622  CG2 VAL A 199      -8.813  39.748 -35.912  1.00 52.42           C  
ANISOU 1622  CG2 VAL A 199    10314   4854   4748    882  -2350   1557       C  
ATOM   1623  N   LEU A 200     -12.437  36.740 -36.839  1.00 54.19           N  
ANISOU 1623  N   LEU A 200     9976   5205   5407   1229  -3141   1371       N  
ATOM   1624  CA  LEU A 200     -13.842  36.393 -37.178  1.00 56.55           C  
ANISOU 1624  CA  LEU A 200    10156   5461   5869   1391  -3497   1302       C  
ATOM   1625  C   LEU A 200     -14.798  36.843 -36.067  1.00 56.35           C  
ANISOU 1625  C   LEU A 200     9753   5476   6181   1556  -3597   1220       C  
ATOM   1626  O   LEU A 200     -15.967  37.118 -36.391  1.00 57.84           O  
ANISOU 1626  O   LEU A 200     9917   5559   6502   1717  -3942   1163       O  
ATOM   1627  CB  LEU A 200     -13.942  34.880 -37.418  1.00 56.10           C  
ANISOU 1627  CB  LEU A 200     9931   5542   5844   1329  -3440   1250       C  
ATOM   1628  CG  LEU A 200     -13.034  34.332 -38.522  1.00 56.19           C  
ANISOU 1628  CG  LEU A 200    10293   5519   5539   1161  -3331   1312       C  
ATOM   1629  CD1 LEU A 200     -13.258  32.846 -38.763  1.00 55.17           C  
ANISOU 1629  CD1 LEU A 200     9985   5516   5462   1119  -3307   1253       C  
ATOM   1630  CD2 LEU A 200     -13.236  35.112 -39.815  1.00 59.03           C  
ANISOU 1630  CD2 LEU A 200    11147   5638   5645   1185  -3610   1376       C  
ATOM   1631  N   ASN A 201     -14.320  36.906 -34.821  1.00 54.34           N  
ANISOU 1631  N   ASN A 201     9220   5364   6064   1515  -3311   1205       N  
ATOM   1632  CA  ASN A 201     -15.152  37.231 -33.634  1.00 53.65           C  
ANISOU 1632  CA  ASN A 201     8749   5335   6302   1644  -3341   1116       C  
ATOM   1633  C   ASN A 201     -14.241  37.715 -32.503  1.00 51.41           C  
ANISOU 1633  C   ASN A 201     8355   5143   6036   1568  -3018   1148       C  
ATOM   1634  O   ASN A 201     -13.050  37.333 -32.472  1.00 49.62           O  
ANISOU 1634  O   ASN A 201     8218   4996   5640   1412  -2742   1206       O  
ATOM   1635  CB  ASN A 201     -16.013  36.028 -33.219  1.00 52.99           C  
ANISOU 1635  CB  ASN A 201     8282   5389   6463   1685  -3365    999       C  
ATOM   1636  CG  ASN A 201     -17.323  36.410 -32.546  1.00 53.62           C  
ANISOU 1636  CG  ASN A 201     8050   5448   6875   1854  -3554    876       C  
ATOM   1637  ND2 ASN A 201     -18.325  35.548 -32.715  1.00 53.93           N  
ANISOU 1637  ND2 ASN A 201     7873   5524   7095   1917  -3711    765       N  
ATOM   1638  OD1 ASN A 201     -17.424  37.465 -31.888  1.00 52.70           O  
ANISOU 1638  OD1 ASN A 201     7886   5282   6858   1922  -3550    870       O  
ATOM   1639  N   THR A 202     -14.775  38.560 -31.623  1.00 51.82           N  
ANISOU 1639  N   THR A 202     8223   5174   6292   1676  -3058   1103       N  
ATOM   1640  CA  THR A 202     -14.105  38.983 -30.367  1.00 50.30           C  
ANISOU 1640  CA  THR A 202     7862   5079   6170   1623  -2769   1110       C  
ATOM   1641  C   THR A 202     -15.111  38.914 -29.225  1.00 50.69           C  
ANISOU 1641  C   THR A 202     7502   5205   6553   1729  -2785    991       C  
ATOM   1642  O   THR A 202     -16.112  39.652 -29.299  1.00 52.37           O  
ANISOU 1642  O   THR A 202     7678   5302   6919   1877  -3037    934       O  
ATOM   1643  CB  THR A 202     -13.553  40.398 -30.477  1.00 50.91           C  
ANISOU 1643  CB  THR A 202     8216   5019   6110   1626  -2771   1190       C  
ATOM   1644  CG2 THR A 202     -12.826  40.845 -29.231  1.00 49.23           C  
ANISOU 1644  CG2 THR A 202     7845   4901   5959   1568  -2483   1195       C  
ATOM   1645  OG1 THR A 202     -12.651  40.371 -31.575  1.00 52.12           O  
ANISOU 1645  OG1 THR A 202     8756   5096   5952   1508  -2737   1285       O  
ATOM   1646  N   LEU A 203     -14.867  38.041 -28.241  1.00 49.09           N  
ANISOU 1646  N   LEU A 203     7016   5178   6457   1653  -2531    947       N  
ATOM   1647  CA  LEU A 203     -15.747  37.906 -27.060  1.00 49.30           C  
ANISOU 1647  CA  LEU A 203     6662   5283   6787   1720  -2488    827       C  
ATOM   1648  C   LEU A 203     -15.269  38.847 -25.957  1.00 49.36           C  
ANISOU 1648  C   LEU A 203     6610   5306   6839   1710  -2304    843       C  
ATOM   1649  O   LEU A 203     -14.149  38.673 -25.446  1.00 46.07           O  
ANISOU 1649  O   LEU A 203     6228   4978   6298   1590  -2042    905       O  
ATOM   1650  CB  LEU A 203     -15.774  36.450 -26.618  1.00 47.63           C  
ANISOU 1650  CB  LEU A 203     6218   5233   6647   1638  -2323    773       C  
ATOM   1651  CG  LEU A 203     -16.308  35.495 -27.683  1.00 48.37           C  
ANISOU 1651  CG  LEU A 203     6351   5313   6713   1650  -2506    746       C  
ATOM   1652  CD1 LEU A 203     -16.329  34.076 -27.155  1.00 47.37           C  
ANISOU 1652  CD1 LEU A 203     5991   5343   6664   1565  -2325    691       C  
ATOM   1653  CD2 LEU A 203     -17.693  35.890 -28.161  1.00 50.21           C  
ANISOU 1653  CD2 LEU A 203     6513   5430   7133   1809  -2838    648       C  
ATOM   1654  N   ILE A 204     -16.088  39.865 -25.704  1.00 53.47           N  
ANISOU 1654  N   ILE A 204     7065   5724   7526   1838  -2464    785       N  
ATOM   1655  CA  ILE A 204     -16.018  40.779 -24.527  1.00 54.15           C  
ANISOU 1655  CA  ILE A 204     7021   5818   7735   1859  -2325    759       C  
ATOM   1656  C   ILE A 204     -16.903  40.181 -23.440  1.00 53.63           C  
ANISOU 1656  C   ILE A 204     6567   5854   7955   1880  -2234    616       C  
ATOM   1657  O   ILE A 204     -18.110  39.962 -23.735  1.00 56.74           O  
ANISOU 1657  O   ILE A 204     6807   6203   8549   1983  -2443    501       O  
ATOM   1658  CB  ILE A 204     -16.531  42.193 -24.855  1.00 57.13           C  
ANISOU 1658  CB  ILE A 204     7528   6017   8163   1995  -2560    756       C  
ATOM   1659  CG1 ILE A 204     -15.964  42.742 -26.164  1.00 58.00           C  
ANISOU 1659  CG1 ILE A 204     8057   5983   7997   1991  -2723    880       C  
ATOM   1660  CG2 ILE A 204     -16.244  43.090 -23.648  1.00 57.61           C  
ANISOU 1660  CG2 ILE A 204     7482   6097   8311   1990  -2375    744       C  
ATOM   1661  CD1 ILE A 204     -14.458  42.849 -26.115  1.00 56.98           C  
ANISOU 1661  CD1 ILE A 204     8142   5903   7606   1835  -2458   1003       C  
ATOM   1662  N   HIS A 205     -16.352  39.947 -22.251  1.00 50.61           N  
ANISOU 1662  N   HIS A 205     6043   5592   7594   1787  -1943    612       N  
ATOM   1663  CA  HIS A 205     -17.087  39.300 -21.138  1.00 48.89           C  
ANISOU 1663  CA  HIS A 205     5490   5471   7615   1773  -1807    479       C  
ATOM   1664  C   HIS A 205     -16.239  39.371 -19.886  1.00 45.78           C  
ANISOU 1664  C   HIS A 205     5047   5171   7176   1671  -1504    510       C  
ATOM   1665  O   HIS A 205     -16.582  40.135 -19.000  1.00 46.73           O  
ANISOU 1665  O   HIS A 205     5047   5269   7440   1707  -1444    449       O  
ATOM   1666  CB  HIS A 205     -17.454  37.854 -21.474  1.00 49.37           C  
ANISOU 1666  CB  HIS A 205     5441   5614   7703   1726  -1809    432       C  
ATOM   1667  CG  HIS A 205     -18.034  37.154 -20.300  1.00 50.33           C  
ANISOU 1667  CG  HIS A 205     5264   5832   8027   1679  -1622    309       C  
ATOM   1668  CD2 HIS A 205     -17.525  36.186 -19.499  1.00 49.66           C  
ANISOU 1668  CD2 HIS A 205     5104   5870   7895   1554  -1368    317       C  
ATOM   1669  ND1 HIS A 205     -19.269  37.499 -19.787  1.00 51.71           N  
ANISOU 1669  ND1 HIS A 205     5193   5965   8491   1761  -1683    148       N  
ATOM   1670  CE1 HIS A 205     -19.515  36.762 -18.730  1.00 51.68           C  
ANISOU 1670  CE1 HIS A 205     4980   6054   8602   1675  -1457     61       C  
ATOM   1671  NE2 HIS A 205     -18.453  35.942 -18.526  1.00 50.65           N  
ANISOU 1671  NE2 HIS A 205     4962   6023   8259   1550  -1267    170       N  
ATOM   1672  N   HIS A 206     -15.150  38.614 -19.840  1.00 43.35           N  
ANISOU 1672  N   HIS A 206     4838   4957   6676   1551  -1332    598       N  
ATOM   1673  CA  HIS A 206     -14.249  38.622 -18.671  1.00 41.69           C  
ANISOU 1673  CA  HIS A 206     4601   4832   6410   1456  -1065    629       C  
ATOM   1674  C   HIS A 206     -13.840  40.064 -18.463  1.00 41.62           C  
ANISOU 1674  C   HIS A 206     4708   4742   6363   1495  -1069    674       C  
ATOM   1675  O   HIS A 206     -13.654  40.752 -19.445  1.00 42.37           O  
ANISOU 1675  O   HIS A 206     5006   4740   6354   1542  -1227    738       O  
ATOM   1676  CB  HIS A 206     -13.086  37.639 -18.846  1.00 40.20           C  
ANISOU 1676  CB  HIS A 206     4521   4733   6019   1338   -927    712       C  
ATOM   1677  CG  HIS A 206     -13.573  36.234 -18.914  1.00 39.87           C  
ANISOU 1677  CG  HIS A 206     4349   4767   6035   1302   -913    658       C  
ATOM   1678  CD2 HIS A 206     -13.757  35.391 -19.949  1.00 40.16           C  
ANISOU 1678  CD2 HIS A 206     4433   4807   6017   1298  -1030    668       C  
ATOM   1679  ND1 HIS A 206     -14.042  35.582 -17.814  1.00 40.16           N  
ANISOU 1679  ND1 HIS A 206     4178   4873   6207   1263   -768    573       N  
ATOM   1680  CE1 HIS A 206     -14.463  34.379 -18.161  1.00 40.36           C  
ANISOU 1680  CE1 HIS A 206     4129   4944   6260   1234   -789    535       C  
ATOM   1681  NE2 HIS A 206     -14.294  34.236 -19.461  1.00 39.81           N  
ANISOU 1681  NE2 HIS A 206     4205   4840   6080   1258   -951    592       N  
ATOM   1682  N   ASN A 207     -13.798  40.458 -17.203  1.00 42.70           N  
ANISOU 1682  N   ASN A 207     4721   4913   6591   1474   -903    631       N  
ATOM   1683  CA  ASN A 207     -13.416  41.786 -16.677  1.00 44.02           C  
ANISOU 1683  CA  ASN A 207     4954   5021   6750   1499   -856    655       C  
ATOM   1684  C   ASN A 207     -11.891  41.869 -16.506  1.00 40.41           C  
ANISOU 1684  C   ASN A 207     4669   4611   6074   1397   -693    762       C  
ATOM   1685  O   ASN A 207     -11.364  42.959 -16.292  1.00 40.24           O  
ANISOU 1685  O   ASN A 207     4751   4536   6002   1404   -660    801       O  
ATOM   1686  CB  ASN A 207     -14.081  41.965 -15.310  1.00 46.75           C  
ANISOU 1686  CB  ASN A 207     5070   5396   7298   1503   -725    544       C  
ATOM   1687  CG  ASN A 207     -14.524  43.388 -15.069  1.00 50.24           C  
ANISOU 1687  CG  ASN A 207     5503   5733   7854   1596   -798    507       C  
ATOM   1688  ND2 ASN A 207     -15.338  43.899 -15.984  1.00 54.47           N  
ANISOU 1688  ND2 ASN A 207     6061   6158   8478   1715  -1046    479       N  
ATOM   1689  OD1 ASN A 207     -14.139  44.019 -14.076  1.00 51.07           O  
ANISOU 1689  OD1 ASN A 207     5588   5848   7967   1565   -644    502       O  
ATOM   1690  N   GLU A 208     -11.225  40.720 -16.540  1.00 37.24           N  
ANISOU 1690  N   GLU A 208     4279   4305   5566   1305   -590    793       N  
ATOM   1691  CA  GLU A 208      -9.791  40.552 -16.207  1.00 35.05           C  
ANISOU 1691  CA  GLU A 208     4108   4089   5122   1203   -419    860       C  
ATOM   1692  C   GLU A 208      -9.213  39.507 -17.168  1.00 18.21           C  
ATOM   1693  O   GLU A 208     -10.002  38.853 -17.904  1.00 31.91           O  
ANISOU 1693  O   GLU A 208     3777   3724   4625   1179   -570    886       O  
ATOM   1694  CB  GLU A 208      -9.624  40.126 -14.737  1.00 35.83           C  
ANISOU 1694  CB  GLU A 208     4055   4274   5283   1148   -228    811       C  
ATOM   1695  CG  GLU A 208      -9.080  41.211 -13.796  1.00 36.17           C  
ANISOU 1695  CG  GLU A 208     4120   4297   5324   1138   -118    816       C  
ATOM   1696  CD  GLU A 208      -9.336  40.948 -12.315  1.00 36.48           C  
ANISOU 1696  CD  GLU A 208     4009   4392   5461   1105     34    748       C  
ATOM   1697  OE1 GLU A 208     -10.515  40.668 -11.977  1.00 38.54           O  
ANISOU 1697  OE1 GLU A 208     4117   4650   5879   1138     16    666       O  
ATOM   1698  OE2 GLU A 208      -8.370  41.015 -11.488  1.00 35.80           O1-
ANISOU 1698  OE2 GLU A 208     3962   4344   5296   1043    170    767       O1-
ATOM   1699  N   ALA A 209      -7.888  39.346 -17.128  1.00 29.76           N  
ANISOU 1699  N   ALA A 209     3643   3500   4166   1057   -313    957       N  
ATOM   1700  CA  ALA A 209      -7.110  38.477 -18.030  1.00 28.47           C  
ANISOU 1700  CA  ALA A 209     3590   3367   3859    988   -303    997       C  
ATOM   1701  C   ALA A 209      -7.829  37.139 -18.214  1.00 28.02           C  
ANISOU 1701  C   ALA A 209     3414   3369   3862    991   -352    961       C  
ATOM   1702  O   ALA A 209      -8.264  36.533 -17.227  1.00 27.49           O  
ANISOU 1702  O   ALA A 209     3177   3364   3903    987   -280    909       O  
ATOM   1703  CB  ALA A 209      -5.724  38.294 -17.475  1.00 26.97           C  
ANISOU 1703  CB  ALA A 209     3429   3235   3582    898   -129   1008       C  
ATOM   1704  N   VAL A 210      -7.932  36.672 -19.451  1.00 28.25           N  
ANISOU 1704  N   VAL A 210     3547   3373   3813    988   -462    986       N  
ATOM   1705  CA  VAL A 210      -8.480  35.336 -19.782  1.00 27.82           C  
ANISOU 1705  CA  VAL A 210     3403   3374   3795    979   -507    956       C  
ATOM   1706  C   VAL A 210      -7.315  34.352 -19.824  1.00 26.89           C  
ANISOU 1706  C   VAL A 210     3325   3329   3562    880   -376    975       C  
ATOM   1707  O   VAL A 210      -6.451  34.523 -20.714  1.00 27.09           O  
ANISOU 1707  O   VAL A 210     3526   3324   3444    832   -370   1019       O  
ATOM   1708  CB  VAL A 210      -9.186  35.397 -21.131  1.00 28.94           C  
ANISOU 1708  CB  VAL A 210     3651   3439   3907   1030   -711    969       C  
ATOM   1709  CG1 VAL A 210      -9.653  34.012 -21.540  1.00 29.15           C  
ANISOU 1709  CG1 VAL A 210     3595   3522   3958   1012   -752    937       C  
ATOM   1710  CG2 VAL A 210     -10.331  36.380 -21.095  1.00 30.32           C  
ANISOU 1710  CG2 VAL A 210     3778   3528   4214   1142   -867    936       C  
ATOM   1711  N   LEU A 211      -7.292  33.379 -18.905  1.00 25.87           N  
ANISOU 1711  N   LEU A 211     3050   3283   3496    849   -274    938       N  
ATOM   1712  CA  LEU A 211      -6.078  32.605 -18.573  1.00 24.98           C  
ANISOU 1712  CA  LEU A 211     2954   3233   3303    768   -139    944       C  
ATOM   1713  C   LEU A 211      -6.104  31.267 -19.287  1.00 25.39           C  
ANISOU 1713  C   LEU A 211     3005   3325   3319    733   -168    937       C  
ATOM   1714  O   LEU A 211      -4.988  30.721 -19.563  1.00 25.77           O  
ANISOU 1714  O   LEU A 211     3118   3399   3273    669    -95    945       O  
ATOM   1715  CB  LEU A 211      -5.996  32.359 -17.074  1.00 24.25           C  
ANISOU 1715  CB  LEU A 211     2738   3190   3286    757    -23    910       C  
ATOM   1716  CG  LEU A 211      -5.845  33.605 -16.216  1.00 24.78           C  
ANISOU 1716  CG  LEU A 211     2803   3228   3386    781     29    911       C  
ATOM   1717  CD1 LEU A 211      -5.777  33.223 -14.751  1.00 24.60           C  
ANISOU 1717  CD1 LEU A 211     2681   3248   3418    760    140    876       C  
ATOM   1718  CD2 LEU A 211      -4.620  34.403 -16.594  1.00 24.71           C  
ANISOU 1718  CD2 LEU A 211     2928   3191   3270    750     69    946       C  
ATOM   1719  N   HIS A 212      -7.299  30.730 -19.523  1.00 25.39           N  
ANISOU 1719  N   HIS A 212     2919   3326   3402    771   -263    909       N  
ATOM   1720  CA  HIS A 212      -7.418  29.431 -20.214  1.00 24.98           C  
ANISOU 1720  CA  HIS A 212     2861   3310   3322    738   -296    898       C  
ATOM   1721  C   HIS A 212      -8.715  29.388 -20.978  1.00 25.77           C  
ANISOU 1721  C   HIS A 212     2928   3372   3490    796   -459    875       C  
ATOM   1722  O   HIS A 212      -9.589  30.166 -20.650  1.00 26.25           O  
ANISOU 1722  O   HIS A 212     2920   3394   3658    862   -523    849       O  
ATOM   1723  CB  HIS A 212      -7.244  28.244 -19.254  1.00 23.79           C  
ANISOU 1723  CB  HIS A 212     2598   3228   3212    694   -184    865       C  
ATOM   1724  CG  HIS A 212      -6.536  27.104 -19.919  1.00 23.49           C  
ANISOU 1724  CG  HIS A 212     2614   3223   3087    637   -164    871       C  
ATOM   1725  CD2 HIS A 212      -7.011  25.998 -20.545  1.00 23.49           C  
ANISOU 1725  CD2 HIS A 212     2589   3244   3091    622   -216    853       C  
ATOM   1726  ND1 HIS A 212      -5.150  27.090 -20.107  1.00 22.49           N  
ANISOU 1726  ND1 HIS A 212     2582   3105   2859    587    -88    890       N  
ATOM   1727  CE1 HIS A 212      -4.820  25.993 -20.743  1.00 22.27           C  
ANISOU 1727  CE1 HIS A 212     2576   3102   2784    545    -87    879       C  
ATOM   1728  NE2 HIS A 212      -5.928  25.305 -21.024  1.00 22.70           N  
ANISOU 1728  NE2 HIS A 212     2567   3166   2894    565   -165    863       N  
ATOM   1729  N   LEU A 213      -8.756  28.512 -21.976  1.00 26.46           N  
ANISOU 1729  N   LEU A 213     3068   3469   3518    771   -524    878       N  
ATOM   1730  CA  LEU A 213      -9.970  28.160 -22.734  1.00 28.18           C  
ANISOU 1730  CA  LEU A 213     3243   3660   3804    820   -688    842       C  
ATOM   1731  C   LEU A 213      -9.819  26.790 -23.369  1.00 28.52           C  
ANISOU 1731  C   LEU A 213     3296   3747   3792    764   -685    833       C  
ATOM   1732  O   LEU A 213      -8.690  26.324 -23.540  1.00 28.02           O  
ANISOU 1732  O   LEU A 213     3320   3713   3611    694   -584    865       O  
ATOM   1733  CB  LEU A 213     -10.233  29.230 -23.789  1.00 29.45           C  
ANISOU 1733  CB  LEU A 213     3560   3724   3905    877   -858    876       C  
ATOM   1734  CG  LEU A 213      -9.156  29.386 -24.863  1.00 29.58           C  
ANISOU 1734  CG  LEU A 213     3820   3704   3715    818   -853    943       C  
ATOM   1735  CD1 LEU A 213      -9.492  28.578 -26.113  1.00 30.45           C  
ANISOU 1735  CD1 LEU A 213     4018   3797   3755    804   -977    940       C  
ATOM   1736  CD2 LEU A 213      -9.011  30.854 -25.245  1.00 30.59           C  
ANISOU 1736  CD2 LEU A 213     4118   3732   3774    856   -926    989       C  
ATOM   1737  N   ARG A 214     -10.953  26.204 -23.707  1.00 30.70           N  
ANISOU 1737  N   ARG A 214     3476   4022   4167    797   -797    779       N  
ATOM   1738  CA  ARG A 214     -11.057  24.969 -24.495  1.00 32.59           C  
ANISOU 1738  CA  ARG A 214     3728   4289   4365    756   -836    764       C  
ATOM   1739  C   ARG A 214     -12.384  25.007 -25.233  1.00 33.99           C  
ANISOU 1739  C   ARG A 214     3857   4419   4638    826  -1042    711       C  
ATOM   1740  O   ARG A 214     -13.343  25.531 -24.670  1.00 34.80           O  
ANISOU 1740  O   ARG A 214     3819   4501   4903    891  -1094    652       O  
ATOM   1741  CB  ARG A 214     -10.962  23.760 -23.573  1.00 33.90           C  
ANISOU 1741  CB  ARG A 214     3756   4532   4592    698   -685    726       C  
ATOM   1742  CG  ARG A 214     -11.210  22.438 -24.281  1.00 36.62           C  
ANISOU 1742  CG  ARG A 214     4089   4904   4920    659   -722    699       C  
ATOM   1743  CD  ARG A 214     -10.933  21.176 -23.469  1.00 38.43           C  
ANISOU 1743  CD  ARG A 214     4230   5195   5175    593   -572    673       C  
ATOM   1744  NE  ARG A 214     -11.268  20.057 -24.343  1.00 41.28           N  
ANISOU 1744  NE  ARG A 214     4593   5570   5520    565   -635    646       N  
ATOM   1745  CZ  ARG A 214     -10.445  19.562 -25.264  1.00 43.44           C  
ANISOU 1745  CZ  ARG A 214     4998   5848   5657    523   -642    682       C  
ATOM   1746  NH1 ARG A 214      -9.228  20.085 -25.402  1.00 45.56           N1+
ANISOU 1746  NH1 ARG A 214     5398   6109   5804    500   -578    738       N1+
ATOM   1747  NH2 ARG A 214     -10.858  18.587 -26.066  1.00 43.43           N  
ANISOU 1747  NH2 ARG A 214     4997   5857   5650    500   -708    652       N  
ATOM   1748  N   PHE A 215     -12.415  24.499 -26.455  1.00 35.15           N  
ANISOU 1748  N   PHE A 215     4119   4545   4691    813  -1157    723       N  
ATOM   1749  CA  PHE A 215     -13.664  24.306 -27.217  1.00 38.34           C  
ANISOU 1749  CA  PHE A 215     4474   4907   5187    877  -1371    660       C  
ATOM   1750  C   PHE A 215     -13.633  22.929 -27.869  1.00 39.34           C  
ANISOU 1750  C   PHE A 215     4609   5076   5263    815  -1370    642       C  
ATOM   1751  O   PHE A 215     -12.557  22.473 -28.248  1.00 39.42           O  
ANISOU 1751  O   PHE A 215     4757   5111   5111    737  -1269    699       O  
ATOM   1752  CB  PHE A 215     -13.854  25.419 -28.243  1.00 40.27           C  
ANISOU 1752  CB  PHE A 215     4911   5040   5348    948  -1583    698       C  
ATOM   1753  CG  PHE A 215     -12.827  25.423 -29.347  1.00 41.17           C  
ANISOU 1753  CG  PHE A 215     5309   5119   5215    884  -1586    784       C  
ATOM   1754  CD1 PHE A 215     -11.621  26.099 -29.202  1.00 41.23           C  
ANISOU 1754  CD1 PHE A 215     5469   5116   5081    831  -1445    859       C  
ATOM   1755  CD2 PHE A 215     -13.041  24.737 -30.526  1.00 42.35           C  
ANISOU 1755  CD2 PHE A 215     5574   5242   5275    865  -1714    779       C  
ATOM   1756  CE1 PHE A 215     -10.673  26.107 -30.217  1.00 41.40           C  
ANISOU 1756  CE1 PHE A 215     5749   5097   4883    755  -1420    918       C  
ATOM   1757  CE2 PHE A 215     -12.088  24.738 -31.535  1.00 43.19           C  
ANISOU 1757  CE2 PHE A 215     5953   5308   5148    789  -1692    847       C  
ATOM   1758  CZ  PHE A 215     -10.907  25.423 -31.381  1.00 42.18           C  
ANISOU 1758  CZ  PHE A 215     5971   5167   4888    731  -1538    912       C  
ATOM   1759  N   SER A 216     -14.800  22.302 -27.970  1.00 41.73           N  
ANISOU 1759  N   SER A 216     4753   5384   5716    847  -1474    550       N  
ATOM   1760  CA  SER A 216     -15.023  21.013 -28.657  1.00 42.69           C  
ANISOU 1760  CA  SER A 216     4865   5537   5817    800  -1508    516       C  
ATOM   1761  C   SER A 216     -16.529  20.828 -28.848  1.00 45.44           C  
ANISOU 1761  C   SER A 216     5040   5859   6367    870  -1687    398       C  
ATOM   1762  O   SER A 216     -17.281  21.303 -27.985  1.00 45.13           O  
ANISOU 1762  O   SER A 216     4815   5815   6517    919  -1676    326       O  
ATOM   1763  CB  SER A 216     -14.398  19.890 -27.886  1.00 41.26           C  
ANISOU 1763  CB  SER A 216     4606   5444   5628    706  -1279    517       C  
ATOM   1764  OG  SER A 216     -15.012  18.666 -28.241  1.00 42.17           O  
ANISOU 1764  OG  SER A 216     4633   5588   5803    675  -1311    449       O  
ATOM   1765  N   ASN A 217     -16.933  20.220 -29.973  1.00 48.04           N  
ANISOU 1765  N   ASN A 217     5432   6165   6657    873  -1850    372       N  
ATOM   1766  CA  ASN A 217     -18.331  19.809 -30.293  1.00 50.20           C  
ANISOU 1766  CA  ASN A 217     5532   6416   7124    930  -2031    242       C  
ATOM   1767  C   ASN A 217     -19.284  20.960 -29.980  1.00 49.32           C  
ANISOU 1767  C   ASN A 217     5304   6237   7199   1048  -2184    170       C  
ATOM   1768  O   ASN A 217     -20.308  20.711 -29.350  1.00 50.11           O  
ANISOU 1768  O   ASN A 217     5143   6353   7542   1071  -2178     37       O  
ATOM   1769  CB  ASN A 217     -18.758  18.539 -29.548  1.00 51.80           C  
ANISOU 1769  CB  ASN A 217     5509   6702   7472    858  -1867    150       C  
ATOM   1770  CG  ASN A 217     -17.793  17.392 -29.771  1.00 53.25           C  
ANISOU 1770  CG  ASN A 217     5801   6946   7485    748  -1713    217       C  
ATOM   1771  ND2 ASN A 217     -17.517  16.619 -28.726  1.00 53.68           N  
ANISOU 1771  ND2 ASN A 217     5741   7068   7586    671  -1480    203       N  
ATOM   1772  OD1 ASN A 217     -17.284  17.211 -30.880  1.00 54.95           O  
ANISOU 1772  OD1 ASN A 217     6216   7139   7524    733  -1805    278       O  
ATOM   1773  N   GLY A 218     -18.935  22.170 -30.405  1.00 47.91           N  
ANISOU 1773  N   GLY A 218     5315   5979   6911   1113  -2307    249       N  
ATOM   1774  CA  GLY A 218     -19.845  23.328 -30.395  1.00 48.84           C  
ANISOU 1774  CA  GLY A 218     5367   6003   7186   1244  -2519    184       C  
ATOM   1775  C   GLY A 218     -20.028  23.889 -29.003  1.00 46.84           C  
ANISOU 1775  C   GLY A 218     4908   5782   7108   1256  -2350    138       C  
ATOM   1776  O   GLY A 218     -21.031  24.601 -28.751  1.00 47.96           O  
ANISOU 1776  O   GLY A 218     4892   5864   7466   1359  -2490     32       O  
ATOM   1777  N   LEU A 219     -19.069  23.600 -28.137  1.00 43.88           N  
ANISOU 1777  N   LEU A 219     4542   5490   6642   1157  -2066    210       N  
ATOM   1778  CA  LEU A 219     -19.012  24.126 -26.761  1.00 42.62           C  
ANISOU 1778  CA  LEU A 219     4237   5360   6594   1148  -1873    190       C  
ATOM   1779  C   LEU A 219     -17.628  24.716 -26.522  1.00 40.39           C  
ANISOU 1779  C   LEU A 219     4161   5090   6096   1104  -1731    336       C  
ATOM   1780  O   LEU A 219     -16.640  24.069 -26.870  1.00 39.77           O  
ANISOU 1780  O   LEU A 219     4229   5055   5828   1021  -1634    421       O  
ATOM   1781  CB  LEU A 219     -19.280  22.969 -25.804  1.00 42.16           C  
ANISOU 1781  CB  LEU A 219     3971   5392   6657   1056  -1654    108       C  
ATOM   1782  CG  LEU A 219     -19.589  23.400 -24.380  1.00 42.18           C  
ANISOU 1782  CG  LEU A 219     3792   5411   6822   1045  -1476     43       C  
ATOM   1783  CD1 LEU A 219     -21.090  23.594 -24.216  1.00 44.68           C  
ANISOU 1783  CD1 LEU A 219     3856   5686   7434   1113  -1588   -139       C  
ATOM   1784  CD2 LEU A 219     -19.057  22.388 -23.379  1.00 40.68           C  
ANISOU 1784  CD2 LEU A 219     3560   5305   6591    919  -1194     56       C  
ATOM   1785  N   MET A 220     -17.578  25.906 -25.951  1.00 39.85           N  
ANISOU 1785  N   MET A 220     4090   4981   6069   1157  -1721    352       N  
ATOM   1786  CA  MET A 220     -16.331  26.551 -25.500  1.00 38.23           C  
ANISOU 1786  CA  MET A 220     4038   4789   5700   1114  -1564    468       C  
ATOM   1787  C   MET A 220     -16.478  26.937 -24.033  1.00 36.92           C  
ANISOU 1787  C   MET A 220     3695   4657   5676   1107  -1387    421       C  
ATOM   1788  O   MET A 220     -17.556  27.346 -23.614  1.00 37.64           O  
ANISOU 1788  O   MET A 220     3607   4716   5980   1173  -1452    314       O  
ATOM   1789  CB  MET A 220     -16.040  27.808 -26.318  1.00 40.07           C  
ANISOU 1789  CB  MET A 220     4493   4919   5812   1184  -1733    544       C  
ATOM   1790  CG  MET A 220     -14.845  28.589 -25.810  1.00 39.74           C  
ANISOU 1790  CG  MET A 220     4586   4883   5632   1142  -1571    642       C  
ATOM   1791  SD  MET A 220     -14.130  29.626 -27.118  1.00 41.43           S  
ANISOU 1791  SD  MET A 220     5156   4980   5605   1161  -1722    755       S  
ATOM   1792  CE  MET A 220     -15.345  30.934 -27.241  1.00 43.42           C  
ANISOU 1792  CE  MET A 220     5377   5105   6017   1318  -1984    701       C  
ATOM   1793  N   VAL A 221     -15.401  26.813 -23.286  1.00 35.32           N  
ANISOU 1793  N   VAL A 221     3548   4512   5362   1029  -1173    492       N  
ATOM   1794  CA  VAL A 221     -15.324  27.245 -21.869  1.00 34.78           C  
ANISOU 1794  CA  VAL A 221     3366   4468   5381   1011   -994    468       C  
ATOM   1795  C   VAL A 221     -14.123  28.162 -21.745  1.00 33.12           C  
ANISOU 1795  C   VAL A 221     3331   4243   5009   1002   -930    577       C  
ATOM   1796  O   VAL A 221     -13.051  27.794 -22.206  1.00 32.08           O  
ANISOU 1796  O   VAL A 221     3353   4136   4699    945   -882    658       O  
ATOM   1797  CB  VAL A 221     -15.162  26.034 -20.939  1.00 34.37           C  
ANISOU 1797  CB  VAL A 221     3213   4497   5349    912   -787    436       C  
ATOM   1798  CG1 VAL A 221     -15.112  26.453 -19.482  1.00 34.13           C  
ANISOU 1798  CG1 VAL A 221     3095   4480   5391    886   -607    410       C  
ATOM   1799  CG2 VAL A 221     -16.270  25.030 -21.167  1.00 35.68           C  
ANISOU 1799  CG2 VAL A 221     3223   4675   5658    903   -835    328       C  
ATOM   1800  N   THR A 222     -14.305  29.295 -21.108  1.00 32.72           N  
ANISOU 1800  N   THR A 222     3245   4153   5034   1052   -920    564       N  
ATOM   1801  CA  THR A 222     -13.223  30.259 -20.846  1.00 32.39           C  
ANISOU 1801  CA  THR A 222     3350   4095   4863   1042   -846    653       C  
ATOM   1802  C   THR A 222     -13.114  30.387 -19.338  1.00 31.39           C  
ANISOU 1802  C   THR A 222     3102   4009   4815   1007   -653    620       C  
ATOM   1803  O   THR A 222     -14.116  30.099 -18.675  1.00 32.49           O  
ANISOU 1803  O   THR A 222     3058   4158   5128   1015   -622    522       O  
ATOM   1804  CB  THR A 222     -13.549  31.583 -21.546  1.00 34.60           C  
ANISOU 1804  CB  THR A 222     3729   4271   5145   1137  -1030    673       C  
ATOM   1805  CG2 THR A 222     -13.739  31.404 -23.042  1.00 35.85           C  
ANISOU 1805  CG2 THR A 222     4035   4373   5213   1168  -1236    701       C  
ATOM   1806  OG1 THR A 222     -14.733  32.158 -20.971  1.00 35.69           O  
ANISOU 1806  OG1 THR A 222     3686   4370   5503   1217  -1092    574       O  
ATOM   1807  N   CYS A 223     -11.959  30.772 -18.819  1.00 29.99           N  
ANISOU 1807  N   CYS A 223     3025   3852   4520    964   -526    689       N  
ATOM   1808  CA  CYS A 223     -11.783  30.998 -17.369  1.00 29.54           C  
ANISOU 1808  CA  CYS A 223     2886   3822   4516    933   -356    664       C  
ATOM   1809  C   CYS A 223     -10.774  32.112 -17.200  1.00 29.17           C  
ANISOU 1809  C   CYS A 223     2968   3750   4367    938   -317    734       C  
ATOM   1810  O   CYS A 223      -9.939  32.244 -18.050  1.00 29.65           O  
ANISOU 1810  O   CYS A 223     3179   3798   4289    925   -358    802       O  
ATOM   1811  CB  CYS A 223     -11.385  29.720 -16.647  1.00 28.69           C  
ANISOU 1811  CB  CYS A 223     2741   3785   4375    846   -206    654       C  
ATOM   1812  SG  CYS A 223      -9.687  29.186 -16.960  1.00 27.67           S  
ANISOU 1812  SG  CYS A 223     2779   3696   4038    781   -143    746       S  
ATOM   1813  N   SER A 224     -10.903  32.928 -16.165  1.00 29.85           N  
ANISOU 1813  N   SER A 224     2995   3820   4526    953   -239    708       N  
ATOM   1814  CA  SER A 224     -10.217  34.241 -16.078  1.00 29.88           C  
ANISOU 1814  CA  SER A 224     3106   3780   4468    977   -232    759       C  
ATOM   1815  C   SER A 224      -9.684  34.489 -14.664  1.00 29.31           C  
ANISOU 1815  C   SER A 224     3000   3737   4399    934    -61    749       C  
ATOM   1816  O   SER A 224     -10.084  33.793 -13.732  1.00 29.43           O  
ANISOU 1816  O   SER A 224     2910   3790   4483    896     38    695       O  
ATOM   1817  CB  SER A 224     -11.143  35.342 -16.547  1.00 31.26           C  
ANISOU 1817  CB  SER A 224     3265   3869   4744   1073   -381    734       C  
ATOM   1818  OG  SER A 224     -10.674  36.627 -16.152  1.00 31.18           O  
ANISOU 1818  OG  SER A 224     3325   3813   4710   1095   -349    764       O  
ATOM   1819  N   LYS A 225      -8.770  35.442 -14.560  1.00 29.14           N  
ANISOU 1819  N   LYS A 225     3085   3692   4294    933    -29    799       N  
ATOM   1820  CA  LYS A 225      -8.265  36.047 -13.306  1.00 28.69           C  
ANISOU 1820  CA  LYS A 225     3017   3642   4240    909    102    791       C  
ATOM   1821  C   LYS A 225      -9.453  36.617 -12.524  1.00 29.59           C  
ANISOU 1821  C   LYS A 225     2999   3724   4518    952    116    717       C  
ATOM   1822  O   LYS A 225      -9.361  36.667 -11.295  1.00 30.10           O  
ANISOU 1822  O   LYS A 225     3021   3806   4609    915    246    684       O  
ATOM   1823  CB  LYS A 225      -7.233  37.125 -13.679  1.00 28.77           C  
ANISOU 1823  CB  LYS A 225     3169   3616   4148    912     97    850       C  
ATOM   1824  CG  LYS A 225      -6.656  37.948 -12.537  1.00 28.66           C  
ANISOU 1824  CG  LYS A 225     3159   3597   4133    896    209    844       C  
ATOM   1825  CD  LYS A 225      -5.612  38.947 -12.971  1.00 28.75           C  
ANISOU 1825  CD  LYS A 225     3308   3571   4047    887    214    892       C  
ATOM   1826  CE  LYS A 225      -4.684  39.411 -11.865  1.00 28.53           C  
ANISOU 1826  CE  LYS A 225     3289   3559   3990    849    337    883       C  
ATOM   1827  NZ  LYS A 225      -4.644  40.896 -11.727  1.00 29.45           N1+
ANISOU 1827  NZ  LYS A 225     3455   3609   4124    881    339    891       N1+
ATOM   1828  N   ASP A 226     -10.540  36.998 -13.202  1.00 30.49           N  
ANISOU 1828  N   ASP A 226     3052   3786   4745   1026    -17    680       N  
ATOM   1829  CA  ASP A 226     -11.772  37.520 -12.561  1.00 31.39           C  
ANISOU 1829  CA  ASP A 226     3012   3862   5054   1073    -14    581       C  
ATOM   1830  C   ASP A 226     -12.448  36.421 -11.721  1.00 17.35           C  
ATOM   1831  O   ASP A 226     -13.481  36.716 -11.123  1.00 32.60           O  
ANISOU 1831  O   ASP A 226     2881   4036   5472   1031    141    390       O  
ATOM   1832  CB  ASP A 226     -12.723  38.131 -13.604  1.00 33.21           C  
ANISOU 1832  CB  ASP A 226     3214   4014   5390   1179   -218    552       C  
ATOM   1833  CG  ASP A 226     -13.387  37.141 -14.558  1.00 34.13           C  
ANISOU 1833  CG  ASP A 226     3283   4142   5544   1195   -344    526       C  
ATOM   1834  OD1 ASP A 226     -13.291  35.909 -14.325  1.00 33.64           O  
ANISOU 1834  OD1 ASP A 226     3178   4151   5453   1122   -254    515       O  
ATOM   1835  OD2 ASP A 226     -14.010  37.607 -15.523  1.00 35.32           O1-
ANISOU 1835  OD2 ASP A 226     3448   4220   5750   1284   -540    515       O1-
ATOM   1836  N   ARG A 227     -11.927  35.197 -11.695  1.00 29.94           N  
ANISOU 1836  N   ARG A 227     2726   3789   4860    940    166    526       N  
ATOM   1837  CA  ARG A 227     -12.373  34.089 -10.799  1.00 30.20           C  
ANISOU 1837  CA  ARG A 227     2675   3861   4940    861    303    458       C  
ATOM   1838  C   ARG A 227     -13.589  33.352 -11.377  1.00 29.99           C  
ANISOU 1838  C   ARG A 227     2511   3831   5053    875    233    373       C  
ATOM   1839  O   ARG A 227     -14.129  32.457 -10.696  1.00 29.56           O  
ANISOU 1839  O   ARG A 227     2378   3797   5058    804    353    299       O  
ATOM   1840  CB  ARG A 227     -12.735  34.594  -9.400  1.00 31.87           C  
ANISOU 1840  CB  ARG A 227     2827   4052   5232    825    459    386       C  
ATOM   1841  CG  ARG A 227     -11.647  35.380  -8.695  1.00 32.25           C  
ANISOU 1841  CG  ARG A 227     2993   4096   5162    811    529    451       C  
ATOM   1842  CD  ARG A 227     -12.142  35.852  -7.361  1.00 34.65           C  
ANISOU 1842  CD  ARG A 227     3241   4374   5550    774    680    369       C  
ATOM   1843  NE  ARG A 227     -11.129  36.610  -6.639  1.00 36.37           N  
ANISOU 1843  NE  ARG A 227     3573   4587   5661    760    742    424       N  
ATOM   1844  CZ  ARG A 227     -11.324  37.248  -5.482  1.00 38.58           C  
ANISOU 1844  CZ  ARG A 227     3841   4837   5982    730    868    370       C  
ATOM   1845  NH1 ARG A 227     -10.327  37.918  -4.919  1.00 37.94           N1+
ANISOU 1845  NH1 ARG A 227     3869   4752   5794    722    904    423       N1+
ATOM   1846  NH2 ARG A 227     -12.507  37.203  -4.878  1.00 40.92           N  
ANISOU 1846  NH2 ARG A 227     4015   5105   6429    702    964    252       N  
ATOM   1847  N   SER A 228     -13.985  33.703 -12.595  1.00 30.22           N  
ANISOU 1847  N   SER A 228     2528   3829   5126    960     45    380       N  
ATOM   1848  CA  SER A 228     -15.177  33.152 -13.277  1.00 31.08           C  
ANISOU 1848  CA  SER A 228     2500   3924   5385    994    -64    290       C  
ATOM   1849  C   SER A 228     -14.750  32.165 -14.353  1.00 30.17           C  
ANISOU 1849  C   SER A 228     2473   3845   5147    980   -158    358       C  
ATOM   1850  O   SER A 228     -13.622  32.273 -14.867  1.00 28.85           O  
ANISOU 1850  O   SER A 228     2473   3691   4798    974   -188    472       O  
ATOM   1851  CB  SER A 228     -16.062  34.227 -13.843  1.00 32.71           C  
ANISOU 1851  CB  SER A 228     2626   4053   5748   1109   -236    230       C  
ATOM   1852  OG  SER A 228     -15.690  34.574 -15.152  1.00 33.51           O  
ANISOU 1852  OG  SER A 228     2864   4121   5747   1179   -437    318       O  
ATOM   1853  N   ILE A 229     -15.657  31.227 -14.631  1.00 30.88           N  
ANISOU 1853  N   ILE A 229     2440   3947   5346    966   -187    273       N  
ATOM   1854  CA  ILE A 229     -15.679  30.334 -15.825  1.00 30.48           C  
ANISOU 1854  CA  ILE A 229     2428   3915   5238    972   -318    301       C  
ATOM   1855  C   ILE A 229     -16.894  30.739 -16.647  1.00 32.39           C  
ANISOU 1855  C   ILE A 229     2553   4097   5657   1070   -521    210       C  
ATOM   1856  O   ILE A 229     -17.965  30.969 -16.049  1.00 33.95           O  
ANISOU 1856  O   ILE A 229     2561   4268   6070   1088   -490     74       O  
ATOM   1857  CB  ILE A 229     -15.780  28.871 -15.413  1.00 29.64           C  
ANISOU 1857  CB  ILE A 229     2271   3866   5126    873   -187    264       C  
ATOM   1858  CG1 ILE A 229     -14.626  28.487 -14.484  1.00 28.31           C  
ANISOU 1858  CG1 ILE A 229     2220   3741   4797    786     -6    341       C  
ATOM   1859  CG2 ILE A 229     -15.848  28.001 -16.647  1.00 29.82           C  
ANISOU 1859  CG2 ILE A 229     2325   3905   5099    882   -324    285       C  
ATOM   1860  CD1 ILE A 229     -14.922  27.352 -13.541  1.00 28.16           C  
ANISOU 1860  CD1 ILE A 229     2146   3748   4807    685    167    279       C  
ATOM   1861  N   ALA A 230     -16.730  30.842 -17.953  1.00 32.54           N  
ANISOU 1861  N   ALA A 230     2685   4086   5591   1130   -722    271       N  
ATOM   1862  CA  ALA A 230     -17.828  31.106 -18.891  1.00 34.29           C  
ANISOU 1862  CA  ALA A 230     2829   4242   5960   1232   -960    191       C  
ATOM   1863  C   ALA A 230     -17.991  29.867 -19.760  1.00 34.09           C  
ANISOU 1863  C   ALA A 230     2811   4250   5892   1201  -1035    186       C  
ATOM   1864  O   ALA A 230     -16.968  29.275 -20.146  1.00 32.55           O  
ANISOU 1864  O   ALA A 230     2779   4100   5488   1137   -985    298       O  
ATOM   1865  CB  ALA A 230     -17.519  32.339 -19.693  1.00 35.37           C  
ANISOU 1865  CB  ALA A 230     3132   4293   6014   1328  -1148    270       C  
ATOM   1866  N   VAL A 231     -19.236  29.468 -19.995  1.00 35.69           N  
ANISOU 1866  N   VAL A 231     2827   4432   6301   1239  -1138     47       N  
ATOM   1867  CA  VAL A 231     -19.581  28.335 -20.897  1.00 36.33           C  
ANISOU 1867  CA  VAL A 231     2895   4534   6373   1221  -1240     20       C  
ATOM   1868  C   VAL A 231     -20.375  28.887 -22.075  1.00 38.36           C  
ANISOU 1868  C   VAL A 231     3157   4700   6717   1351  -1557    -27       C  
ATOM   1869  O   VAL A 231     -21.358  29.590 -21.842  1.00 40.06           O  
ANISOU 1869  O   VAL A 231     3208   4853   7159   1437  -1655   -151       O  
ATOM   1870  CB  VAL A 231     -20.345  27.215 -20.177  1.00 36.60           C  
ANISOU 1870  CB  VAL A 231     2711   4622   6574   1139  -1084   -115       C  
ATOM   1871  CG1 VAL A 231     -20.356  25.965 -21.039  1.00 36.63           C  
ANISOU 1871  CG1 VAL A 231     2747   4662   6507   1098  -1146   -106       C  
ATOM   1872  CG2 VAL A 231     -19.747  26.886 -18.817  1.00 35.10           C  
ANISOU 1872  CG2 VAL A 231     2517   4492   6328   1025   -783    -90       C  
ATOM   1873  N   TRP A 232     -19.941  28.586 -23.298  1.00 38.63           N  
ANISOU 1873  N   TRP A 232     3386   4719   6574   1363  -1714     65       N  
ATOM   1874  CA  TRP A 232     -20.512  29.134 -24.552  1.00 40.63           C  
ANISOU 1874  CA  TRP A 232     3727   4867   6844   1485  -2044     51       C  
ATOM   1875  C   TRP A 232     -21.032  27.999 -25.421  1.00 43.00           C  
ANISOU 1875  C   TRP A 232     3992   5183   7164   1473  -2167     -5       C  
ATOM   1876  O   TRP A 232     -20.323  26.987 -25.538  1.00 42.24           O  
ANISOU 1876  O   TRP A 232     3974   5165   6909   1366  -2028     65       O  
ATOM   1877  CB  TRP A 232     -19.450  29.925 -25.303  1.00 38.97           C  
ANISOU 1877  CB  TRP A 232     3840   4601   6364   1500  -2122    219       C  
ATOM   1878  CG  TRP A 232     -18.678  30.867 -24.443  1.00 36.98           C  
ANISOU 1878  CG  TRP A 232     3648   4353   6050   1482  -1956    293       C  
ATOM   1879  CD1 TRP A 232     -17.653  30.561 -23.609  1.00 34.85           C  
ANISOU 1879  CD1 TRP A 232     3405   4172   5664   1372  -1681    365       C  
ATOM   1880  CD2 TRP A 232     -18.847  32.287 -24.355  1.00 37.56           C  
ANISOU 1880  CD2 TRP A 232     3773   4328   6171   1580  -2067    299       C  
ATOM   1881  CE2 TRP A 232     -17.883  32.765 -23.447  1.00 35.97           C  
ANISOU 1881  CE2 TRP A 232     3623   4170   5874   1515  -1835    377       C  
ATOM   1882  CE3 TRP A 232     -19.706  33.208 -24.963  1.00 39.72           C  
ANISOU 1882  CE3 TRP A 232     4062   4472   6559   1722  -2354    244       C  
ATOM   1883  NE1 TRP A 232     -17.170  31.689 -23.007  1.00 34.36           N  
ANISOU 1883  NE1 TRP A 232     3401   4080   5574   1391  -1610    414       N  
ATOM   1884  CZ2 TRP A 232     -17.763  34.117 -23.126  1.00 36.45           C  
ANISOU 1884  CZ2 TRP A 232     3744   4156   5950   1578  -1863    403       C  
ATOM   1885  CZ3 TRP A 232     -19.588  34.549 -24.645  1.00 40.06           C  
ANISOU 1885  CZ3 TRP A 232     4170   4434   6616   1790  -2389    271       C  
ATOM   1886  CH2 TRP A 232     -18.633  34.995 -23.733  1.00 38.35           C  
ANISOU 1886  CH2 TRP A 232     3999   4270   6303   1715  -2137    350       C  
ATOM   1887  N   ASP A 233     -22.215  28.178 -26.010  1.00 47.45           N  
ANISOU 1887  N   ASP A 233     4438   5669   7922   1583  -2430   -133       N  
ATOM   1888  CA  ASP A 233     -22.650  27.413 -27.208  1.00 50.63           C  
ANISOU 1888  CA  ASP A 233     4891   6048   8300   1606  -2649   -163       C  
ATOM   1889  C   ASP A 233     -21.895  28.021 -28.400  1.00 22.33           C  
ATOM   1890  O   ASP A 233     -21.937  29.257 -28.561  1.00 52.83           O  
ANISOU 1890  O   ASP A 233     5641   6140   8293   1744  -2993     25       O  
ATOM   1891  CB  ASP A 233     -24.173  27.443 -27.378  1.00 53.80           C  
ANISOU 1891  CB  ASP A 233     5033   6386   9023   1715  -2875   -372       C  
ATOM   1892  CG  ASP A 233     -24.948  26.951 -26.167  1.00 54.65           C  
ANISOU 1892  CG  ASP A 233     4786   6561   9417   1661  -2659   -547       C  
ATOM   1893  OD1 ASP A 233     -24.553  25.871 -25.617  1.00 53.50           O  
ANISOU 1893  OD1 ASP A 233     4593   6523   9212   1521  -2391   -530       O  
ATOM   1894  OD2 ASP A 233     -25.939  27.671 -25.772  1.00 56.76           O1-
ANISOU 1894  OD2 ASP A 233     4835   6762   9967   1757  -2756   -707       O1-
ATOM   1895  N   MET A 234     -21.193  27.194 -29.175  1.00 52.12           N  
ANISOU 1895  N   MET A 234     5634   6190   7981   1564  -2819     90       N  
ATOM   1896  CA  MET A 234     -20.317  27.658 -30.283  1.00 53.20           C  
ANISOU 1896  CA  MET A 234     6145   6251   7816   1562  -2938    243       C  
ATOM   1897  C   MET A 234     -20.798  27.031 -31.601  1.00 55.63           C  
ANISOU 1897  C   MET A 234     6566   6505   8066   1590  -3195    217       C  
ATOM   1898  O   MET A 234     -20.162  26.065 -32.106  1.00 55.30           O  
ANISOU 1898  O   MET A 234     6643   6522   7845   1485  -3099    278       O  
ATOM   1899  CB  MET A 234     -18.870  27.272 -29.970  1.00 50.89           C  
ANISOU 1899  CB  MET A 234     5997   6050   7288   1419  -2638    378       C  
ATOM   1900  CG  MET A 234     -17.831  28.034 -30.720  1.00 50.74           C  
ANISOU 1900  CG  MET A 234     6333   5958   6989   1397  -2667    524       C  
ATOM   1901  SD  MET A 234     -16.368  27.020 -30.628  1.00 48.48           S  
ANISOU 1901  SD  MET A 234     6149   5789   6481   1223  -2355    620       S  
ATOM   1902  CE  MET A 234     -15.177  28.321 -30.908  1.00 49.35           C  
ANISOU 1902  CE  MET A 234     6581   5818   6352   1199  -2305    755       C  
ATOM   1903  N   ALA A 235     -21.896  27.567 -32.143  1.00 58.41           N  
ANISOU 1903  N   ALA A 235     6882   6742   8570   1732  -3523    120       N  
ATOM   1904  CA  ALA A 235     -22.557  27.061 -33.370  1.00 60.84           C  
ANISOU 1904  CA  ALA A 235     7276   6979   8862   1785  -3824     68       C  
ATOM   1905  C   ALA A 235     -21.586  27.164 -34.546  1.00 61.59           C  
ANISOU 1905  C   ALA A 235     7805   7007   8588   1731  -3891    232       C  
ATOM   1906  O   ALA A 235     -21.499  26.202 -35.337  1.00 62.98           O  
ANISOU 1906  O   ALA A 235     8075   7206   8649   1670  -3930    240       O  
ATOM   1907  CB  ALA A 235     -23.817  27.832 -33.642  1.00 63.21           C  
ANISOU 1907  CB  ALA A 235     7473   7147   9397   1963  -4178    -64       C  
ATOM   1908  N   SER A 236     -20.882  28.294 -34.630  1.00 61.53           N  
ANISOU 1908  N   SER A 236     8053   6918   8407   1743  -3887    351       N  
ATOM   1909  CA  SER A 236     -19.928  28.662 -35.709  1.00 61.30           C  
ANISOU 1909  CA  SER A 236     8475   6797   8021   1685  -3936    504       C  
ATOM   1910  C   SER A 236     -18.915  29.638 -35.123  1.00 59.38           C  
ANISOU 1910  C   SER A 236     8361   6547   7651   1639  -3724    616       C  
ATOM   1911  O   SER A 236     -19.090  30.028 -33.953  1.00 58.74           O  
ANISOU 1911  O   SER A 236     8023   6526   7771   1671  -3590    570       O  
ATOM   1912  CB  SER A 236     -20.650  29.294 -36.863  1.00 64.39           C  
ANISOU 1912  CB  SER A 236     9106   6999   8360   1813  -4353    491       C  
ATOM   1913  OG  SER A 236     -21.150  30.574 -36.491  1.00 66.66           O  
ANISOU 1913  OG  SER A 236     9369   7178   8782   1950  -4515    465       O  
ATOM   1914  N   ALA A 237     -17.949  30.076 -35.914  1.00 58.85           N  
ANISOU 1914  N   ALA A 237     8686   6400   7273   1566  -3702    746       N  
ATOM   1915  CA  ALA A 237     -16.980  31.106 -35.479  1.00 58.78           C  
ANISOU 1915  CA  ALA A 237     8835   6365   7135   1520  -3522    847       C  
ATOM   1916  C   ALA A 237     -17.701  32.423 -35.119  1.00 60.64           C  
ANISOU 1916  C   ALA A 237     9036   6482   7521   1675  -3723    818       C  
ATOM   1917  O   ALA A 237     -17.141  33.208 -34.306  1.00 59.80           O  
ANISOU 1917  O   ALA A 237     8905   6393   7423   1657  -3541    861       O  
ATOM   1918  CB  ALA A 237     -15.942  31.295 -36.556  1.00 59.39           C  
ANISOU 1918  CB  ALA A 237     9356   6354   6856   1408  -3486    968       C  
ATOM   1919  N   THR A 238     -18.878  32.688 -35.701  1.00 63.75           N  
ANISOU 1919  N   THR A 238     9433   6753   8035   1825  -4093    741       N  
ATOM   1920  CA  THR A 238     -19.603  33.986 -35.586  1.00 65.75           C  
ANISOU 1920  CA  THR A 238     9707   6858   8420   1989  -4349    708       C  
ATOM   1921  C   THR A 238     -20.842  33.854 -34.697  1.00 66.80           C  
ANISOU 1921  C   THR A 238     9380   7045   8957   2115  -4433    534       C  
ATOM   1922  O   THR A 238     -21.362  34.901 -34.284  1.00 67.70           O  
ANISOU 1922  O   THR A 238     9425   7068   9230   2240  -4565    489       O  
ATOM   1923  CB  THR A 238     -20.022  34.514 -36.962  1.00 67.88           C  
ANISOU 1923  CB  THR A 238    10356   6910   8525   2082  -4748    740       C  
ATOM   1924  CG2 THR A 238     -18.903  35.283 -37.629  1.00 67.91           C  
ANISOU 1924  CG2 THR A 238    10846   6797   8161   1988  -4683    905       C  
ATOM   1925  OG1 THR A 238     -20.431  33.397 -37.756  1.00 67.50           O  
ANISOU 1925  OG1 THR A 238    10310   6884   8451   2064  -4881    692       O  
ATOM   1926  N   ASP A 239     -21.312  32.627 -34.460  1.00 66.92           N  
ANISOU 1926  N   ASP A 239     9104   7190   9132   2080  -4362    431       N  
ATOM   1927  CA  ASP A 239     -22.532  32.337 -33.667  1.00 68.36           C  
ANISOU 1927  CA  ASP A 239     8840   7427   9708   2174  -4416    240       C  
ATOM   1928  C   ASP A 239     -22.106  31.697 -32.346  1.00 29.69           C  
ATOM   1929  O   ASP A 239     -22.123  30.454 -32.250  1.00 64.74           O  
ANISOU 1929  O   ASP A 239     7936   7282   9382   1962  -3865    178       O  
ATOM   1930  CB  ASP A 239     -23.499  31.454 -34.455  1.00 71.20           C  
ANISOU 1930  CB  ASP A 239     9108   7764  10180   2231  -4677    121       C  
ATOM   1931  CG  ASP A 239     -24.842  31.258 -33.771  1.00 73.19           C  
ANISOU 1931  CG  ASP A 239     8912   8042  10854   2335  -4768   -102       C  
ATOM   1932  OD1 ASP A 239     -25.107  31.984 -32.774  1.00 73.26           O  
ANISOU 1932  OD1 ASP A 239     8712   8056  11068   2385  -4677   -165       O  
ATOM   1933  OD2 ASP A 239     -25.620  30.377 -34.243  1.00 74.25           O1-
ANISOU 1933  OD2 ASP A 239     8905   8188  11117   2359  -4923   -222       O1-
ATOM   1934  N   ILE A 240     -21.707  32.527 -31.384  1.00 65.02           N  
ANISOU 1934  N   ILE A 240     8065   7214   9427   2047  -3822    252       N  
ATOM   1935  CA  ILE A 240     -21.157  32.075 -30.073  1.00 63.05           C  
ANISOU 1935  CA  ILE A 240     7593   7127   9235   1928  -3429    253       C  
ATOM   1936  C   ILE A 240     -21.856  32.825 -28.935  1.00 63.21           C  
ANISOU 1936  C   ILE A 240     7332   7141   9545   2007  -3388    137       C  
ATOM   1937  O   ILE A 240     -21.514  33.996 -28.711  1.00 63.66           O  
ANISOU 1937  O   ILE A 240     7512   7124   9553   2053  -3399    199       O  
ATOM   1938  CB  ILE A 240     -19.635  32.270 -30.032  1.00 61.61           C  
ANISOU 1938  CB  ILE A 240     7678   6984   8745   1802  -3188    431       C  
ATOM   1939  CG1 ILE A 240     -18.946  31.465 -31.132  1.00 61.82           C  
ANISOU 1939  CG1 ILE A 240     7965   7020   8503   1709  -3198    524       C  
ATOM   1940  CG2 ILE A 240     -19.099  31.918 -28.654  1.00 59.99           C  
ANISOU 1940  CG2 ILE A 240     7260   6926   8607   1701  -2827    427       C  
ATOM   1941  CD1 ILE A 240     -17.465  31.754 -31.246  1.00 60.95           C  
ANISOU 1941  CD1 ILE A 240     8134   6924   8101   1590  -2987    678       C  
ATOM   1942  N   THR A 241     -22.768  32.143 -28.233  1.00 63.06           N  
ANISOU 1942  N   THR A 241     6953   7195   9811   2010  -3321    -30       N  
ATOM   1943  CA  THR A 241     -23.668  32.696 -27.182  1.00 63.03           C  
ANISOU 1943  CA  THR A 241     6632   7182  10136   2081  -3287   -191       C  
ATOM   1944  C   THR A 241     -23.229  32.186 -25.800  1.00 60.47           C  
ANISOU 1944  C   THR A 241     6121   7003   9851   1943  -2884   -200       C  
ATOM   1945  O   THR A 241     -22.882  30.994 -25.673  1.00 58.62           O  
ANISOU 1945  O   THR A 241     5854   6880   9540   1821  -2700   -180       O  
ATOM   1946  CB  THR A 241     -25.118  32.323 -27.506  1.00 65.38           C  
ANISOU 1946  CB  THR A 241     6668   7431  10742   2184  -3529   -402       C  
ATOM   1947  CG2 THR A 241     -25.588  32.847 -28.849  1.00 67.69           C  
ANISOU 1947  CG2 THR A 241     7156   7563  10999   2333  -3962   -401       C  
ATOM   1948  OG1 THR A 241     -25.206  30.896 -27.508  1.00 65.20           O  
ANISOU 1948  OG1 THR A 241     6521   7522  10728   2073  -3392   -447       O  
ATOM   1949  N   LEU A 242     -23.222  33.071 -24.806  1.00 60.31           N  
ANISOU 1949  N   LEU A 242     6006   6973   9937   1961  -2757   -225       N  
ATOM   1950  CA  LEU A 242     -22.922  32.745 -23.384  1.00 58.16           C  
ANISOU 1950  CA  LEU A 242     5562   6815   9722   1842  -2393   -251       C  
ATOM   1951  C   LEU A 242     -24.079  31.931 -22.798  1.00 60.04           C  
ANISOU 1951  C   LEU A 242     5452   7098  10263   1819  -2319   -463       C  
ATOM   1952  O   LEU A 242     -25.180  32.498 -22.645  1.00 61.18           O  
ANISOU 1952  O   LEU A 242     5383   7166  10696   1923  -2456   -636       O  
ATOM   1953  CB  LEU A 242     -22.750  34.060 -22.623  1.00 56.88           C  
ANISOU 1953  CB  LEU A 242     5403   6602   9607   1890  -2334   -238       C  
ATOM   1954  CG  LEU A 242     -22.548  33.934 -21.121  1.00 55.18           C  
ANISOU 1954  CG  LEU A 242     5022   6477   9465   1784  -1989   -279       C  
ATOM   1955  CD1 LEU A 242     -21.509  32.874 -20.787  1.00 53.22           C  
ANISOU 1955  CD1 LEU A 242     4876   6354   8993   1627  -1732   -163       C  
ATOM   1956  CD2 LEU A 242     -22.141  35.276 -20.537  1.00 54.70           C  
ANISOU 1956  CD2 LEU A 242     5035   6364   9384   1827  -1944   -227       C  
ATOM   1957  N   ARG A 243     -23.836  30.660 -22.477  1.00 60.06           N  
ANISOU 1957  N   ARG A 243     5401   7210  10210   1685  -2106   -461       N  
ATOM   1958  CA  ARG A 243     -24.867  29.751 -21.920  1.00 62.11           C  
ANISOU 1958  CA  ARG A 243     5353   7513  10731   1631  -1997   -661       C  
ATOM   1959  C   ARG A 243     -24.970  29.969 -20.405  1.00 61.71           C  
ANISOU 1959  C   ARG A 243     5136   7502  10811   1552  -1692   -740       C  
ATOM   1960  O   ARG A 243     -26.100  30.203 -19.969  1.00 66.97           O  
ANISOU 1960  O   ARG A 243     5534   8125  11786   1591  -1702   -947       O  
ATOM   1961  CB  ARG A 243     -24.560  28.290 -22.257  1.00 62.34           C  
ANISOU 1961  CB  ARG A 243     5426   7630  10632   1518  -1905   -620       C  
ATOM   1962  CG  ARG A 243     -25.719  27.338 -22.004  1.00 64.86           C  
ANISOU 1962  CG  ARG A 243     5454   7972  11220   1475  -1854   -834       C  
ATOM   1963  CD  ARG A 243     -25.276  26.032 -21.377  1.00 64.46           C  
ANISOU 1963  CD  ARG A 243     5400   8026  11066   1303  -1556   -805       C  
ATOM   1964  NE  ARG A 243     -24.729  25.086 -22.334  1.00 64.08           N  
ANISOU 1964  NE  ARG A 243     5520   8017  10811   1268  -1634   -695       N  
ATOM   1965  CZ  ARG A 243     -24.538  23.798 -22.082  1.00 64.41           C  
ANISOU 1965  CZ  ARG A 243     5548   8134  10792   1140  -1448   -694       C  
ATOM   1966  NH1 ARG A 243     -24.812  23.284 -20.886  1.00 63.15           N1+
ANISOU 1966  NH1 ARG A 243     5240   8013  10740   1025  -1167   -788       N1+
ATOM   1967  NH2 ARG A 243     -24.046  23.022 -23.036  1.00 64.61           N  
ANISOU 1967  NH2 ARG A 243     5727   8186  10635   1120  -1541   -598       N  
ATOM   1968  N   ARG A 244     -23.872  29.894 -19.637  1.00 58.24           N  
ANISOU 1968  N   ARG A 244     4843   7130  10156   1445  -1436   -598       N  
ATOM   1969  CA  ARG A 244     -23.878  30.080 -18.156  1.00 56.60           C  
ANISOU 1969  CA  ARG A 244     4521   6954  10033   1357  -1139   -659       C  
ATOM   1970  C   ARG A 244     -22.533  30.622 -17.685  1.00 50.83           C  
ANISOU 1970  C   ARG A 244     4023   6251   9039   1318  -1007   -467       C  
ATOM   1971  O   ARG A 244     -21.526  30.309 -18.314  1.00 49.57           O  
ANISOU 1971  O   ARG A 244     4086   6125   8625   1297  -1046   -300       O  
ATOM   1972  CB  ARG A 244     -24.138  28.759 -17.422  1.00 59.82           C  
ANISOU 1972  CB  ARG A 244     4807   7435  10488   1205   -883   -745       C  
ATOM   1973  CG  ARG A 244     -25.591  28.301 -17.449  1.00 66.32           C  
ANISOU 1973  CG  ARG A 244     5334   8229  11636   1212   -918   -991       C  
ATOM   1974  CD  ARG A 244     -26.463  28.865 -16.329  1.00 69.73           C  
ANISOU 1974  CD  ARG A 244     5528   8623  12344   1191   -753  -1188       C  
ATOM   1975  NE  ARG A 244     -26.175  28.116 -15.114  1.00 70.86           N  
ANISOU 1975  NE  ARG A 244     5683   8825  12417   1011   -394  -1195       N  
ATOM   1976  CZ  ARG A 244     -26.579  26.869 -14.860  1.00 73.08           C  
ANISOU 1976  CZ  ARG A 244     5879   9143  12746    884   -232  -1287       C  
ATOM   1977  NH1 ARG A 244     -27.327  26.203 -15.736  1.00 75.15           N1+
ANISOU 1977  NH1 ARG A 244     6009   9399  13147    916   -391  -1394       N1+
ATOM   1978  NH2 ARG A 244     -26.209  26.288 -13.727  1.00 72.21           N  
ANISOU 1978  NH2 ARG A 244     5837   9067  12533    724     84  -1270       N  
ATOM   1979  N   VAL A 245     -22.527  31.355 -16.576  1.00 47.83           N  
ANISOU 1979  N   VAL A 245     3584   5859   8728   1297   -840   -504       N  
ATOM   1980  CA  VAL A 245     -21.299  31.774 -15.833  1.00 44.60           C  
ANISOU 1980  CA  VAL A 245     3361   5486   8099   1237   -663   -352       C  
ATOM   1981  C   VAL A 245     -21.205  30.965 -14.546  1.00 43.15           C  
ANISOU 1981  C   VAL A 245     3121   5364   7911   1086   -352   -397       C  
ATOM   1982  O   VAL A 245     -22.127  31.022 -13.794  1.00 46.28           O  
ANISOU 1982  O   VAL A 245     3323   5738   8523   1057   -238   -562       O  
ATOM   1983  CB  VAL A 245     -21.331  33.278 -15.527  1.00 43.95           C  
ANISOU 1983  CB  VAL A 245     3282   5333   8085   1327   -717   -357       C  
ATOM   1984  CG1 VAL A 245     -20.196  33.745 -14.633  1.00 42.31           C  
ANISOU 1984  CG1 VAL A 245     3229   5158   7690   1261   -523   -234       C  
ATOM   1985  CG2 VAL A 245     -21.342  34.067 -16.806  1.00 44.60           C  
ANISOU 1985  CG2 VAL A 245     3472   5337   8136   1469  -1029   -296       C  
ATOM   1986  N   LEU A 246     -20.124  30.249 -14.314  1.00 41.22           N  
ANISOU 1986  N   LEU A 246     3049   5183   7428    994   -224   -263       N  
ATOM   1987  CA  LEU A 246     -19.904  29.498 -13.052  1.00 40.71           C  
ANISOU 1987  CA  LEU A 246     2989   5161   7319    851     58   -285       C  
ATOM   1988  C   LEU A 246     -18.994  30.360 -12.184  1.00 41.11           C  
ANISOU 1988  C   LEU A 246     3169   5209   7241    837    171   -193       C  
ATOM   1989  O   LEU A 246     -17.820  30.519 -12.544  1.00 40.89           O  
ANISOU 1989  O   LEU A 246     3330   5206   7002    854    119    -35       O  
ATOM   1990  CB  LEU A 246     -19.258  28.134 -13.331  1.00 38.72           C  
ANISOU 1990  CB  LEU A 246     2853   4969   6888    768    104   -199       C  
ATOM   1991  CG  LEU A 246     -19.712  27.447 -14.612  1.00 39.01           C  
ANISOU 1991  CG  LEU A 246     2843   5013   6965    812    -84   -219       C  
ATOM   1992  CD1 LEU A 246     -19.108  26.061 -14.726  1.00 37.47           C  
ANISOU 1992  CD1 LEU A 246     2754   4875   6610    718     -5   -150       C  
ATOM   1993  CD2 LEU A 246     -21.230  27.372 -14.666  1.00 41.36           C  
ANISOU 1993  CD2 LEU A 246     2888   5273   7554    832   -121   -423       C  
ATOM   1994  N   VAL A 247     -19.506  30.914 -11.093  1.00 42.41           N  
ANISOU 1994  N   VAL A 247     3235   5343   7535    804    325   -297       N  
ATOM   1995  CA  VAL A 247     -18.630  31.541 -10.065  1.00 42.35           C  
ANISOU 1995  CA  VAL A 247     3360   5337   7394    763    472   -219       C  
ATOM   1996  C   VAL A 247     -18.522  30.574  -8.873  1.00 42.40           C  
ANISOU 1996  C   VAL A 247     3412   5365   7333    611    727   -250       C  
ATOM   1997  O   VAL A 247     -19.530  29.946  -8.509  1.00 44.54           O  
ANISOU 1997  O   VAL A 247     3544   5622   7758    540    841   -397       O  
ATOM   1998  CB  VAL A 247     -19.112  32.955  -9.712  1.00 43.13           C  
ANISOU 1998  CB  VAL A 247     3365   5376   7646    837    452   -292       C  
ATOM   1999  CG1 VAL A 247     -20.418  32.933  -8.922  1.00 45.45           C  
ANISOU 1999  CG1 VAL A 247     3440   5633   8198    788    598   -504       C  
ATOM   2000  CG2 VAL A 247     -18.004  33.744  -9.012  1.00 42.09           C  
ANISOU 2000  CG2 VAL A 247     3402   5248   7343    825    533   -175       C  
ATOM   2001  N   GLY A 248     -17.307  30.383  -8.369  1.00 41.21           N  
ANISOU 2001  N   GLY A 248     3462   5242   6954    562    801   -117       N  
ATOM   2002  CA  GLY A 248     -16.965  29.210  -7.543  1.00 40.99           C  
ANISOU 2002  CA  GLY A 248     3543   5230   6801    431    977   -104       C  
ATOM   2003  C   GLY A 248     -15.628  29.346  -6.837  1.00 38.63           C  
ANISOU 2003  C   GLY A 248     3456   4942   6279    401   1035     24       C  
ATOM   2004  O   GLY A 248     -15.565  29.076  -5.647  1.00 41.70           O  
ANISOU 2004  O   GLY A 248     3926   5305   6612    302   1214     -4       O  
ATOM   2005  N   HIS A 249     -14.597  29.786  -7.540  1.00 34.83           N  
ANISOU 2005  N   HIS A 249     3069   4488   5678    481    888    151       N  
ATOM   2006  CA  HIS A 249     -13.222  29.916  -7.004  1.00 32.27           C  
ANISOU 2006  CA  HIS A 249     2930   4175   5156    465    915    265       C  
ATOM   2007  C   HIS A 249     -13.062  31.237  -6.253  1.00 32.13           C  
ANISOU 2007  C   HIS A 249     2924   4126   5157    488    966    257       C  
ATOM   2008  O   HIS A 249     -13.718  32.218  -6.625  1.00 31.72           O  
ANISOU 2008  O   HIS A 249     2753   4053   5246    558    907    208       O  
ATOM   2009  CB  HIS A 249     -12.220  29.730  -8.140  1.00 30.24           C  
ANISOU 2009  CB  HIS A 249     2751   3959   4781    525    755    379       C  
ATOM   2010  CG  HIS A 249     -12.192  28.323  -8.618  1.00 29.06           C  
ANISOU 2010  CG  HIS A 249     2622   3836   4582    483    736    390       C  
ATOM   2011  CD2 HIS A 249     -12.734  27.743  -9.704  1.00 28.85           C  
ANISOU 2011  CD2 HIS A 249     2517   3828   4615    508    636    372       C  
ATOM   2012  ND1 HIS A 249     -11.610  27.317  -7.881  1.00 28.28           N  
ANISOU 2012  ND1 HIS A 249     2643   3739   4364    405    827    415       N  
ATOM   2013  CE1 HIS A 249     -11.738  26.177  -8.522  1.00 28.41           C  
ANISOU 2013  CE1 HIS A 249     2652   3776   4365    383    788    418       C  
ATOM   2014  NE2 HIS A 249     -12.433  26.410  -9.635  1.00 28.91           N  
ANISOU 2014  NE2 HIS A 249     2592   3855   4538    442    677    390       N  
ATOM   2015  N   ARG A 250     -12.185  31.230  -5.249  1.00 32.20           N  
ANISOU 2015  N   ARG A 250     3081   4128   5026    436   1058    304       N  
ATOM   2016  CA  ARG A 250     -11.881  32.369  -4.353  1.00 33.36           C  
ANISOU 2016  CA  ARG A 250     3271   4245   5160    439   1127    301       C  
ATOM   2017  C   ARG A 250     -10.695  33.159  -4.924  1.00 32.11           C  
ANISOU 2017  C   ARG A 250     3185   4107   4907    518   1000    406       C  
ATOM   2018  O   ARG A 250     -10.380  34.249  -4.428  1.00 31.90           O  
ANISOU 2018  O   ARG A 250     3184   4059   4877    540   1025    412       O  
ATOM   2019  CB  ARG A 250     -11.578  31.808  -2.964  1.00 35.37           C  
ANISOU 2019  CB  ARG A 250     3668   4470   5301    332   1285    288       C  
ATOM   2020  CG  ARG A 250     -12.750  31.039  -2.386  1.00 38.64           C  
ANISOU 2020  CG  ARG A 250     4031   4851   5800    232   1440    175       C  
ATOM   2021  CD  ARG A 250     -12.513  30.520  -0.975  1.00 40.83           C  
ANISOU 2021  CD  ARG A 250     4490   5078   5946    113   1606    160       C  
ATOM   2022  NE  ARG A 250     -12.379  31.548   0.049  1.00 42.63           N  
ANISOU 2022  NE  ARG A 250     4776   5266   6157     93   1701    136       N  
ATOM   2023  CZ  ARG A 250     -13.374  32.303   0.529  1.00 45.24           C  
ANISOU 2023  CZ  ARG A 250     4991   5560   6636     64   1829     20       C  
ATOM   2024  NH1 ARG A 250     -14.611  32.175   0.062  1.00 47.66           N1+
ANISOU 2024  NH1 ARG A 250     5102   5865   7141     58   1868    -94       N1+
ATOM   2025  NH2 ARG A 250     -13.132  33.194   1.484  1.00 45.13           N  
ANISOU 2025  NH2 ARG A 250     5054   5510   6585     42   1915      6       N  
ATOM   2026  N   ALA A 251     -10.085  32.631  -5.984  1.00 30.28           N  
ANISOU 2026  N   ALA A 251     2984   3913   4608    553    877    478       N  
ATOM   2027  CA  ALA A 251      -8.943  33.235  -6.677  1.00 27.80           C  
ANISOU 2027  CA  ALA A 251     2742   3617   4205    611    771    565       C  
ATOM   2028  C   ALA A 251      -9.032  32.908  -8.167  1.00 27.43           C  
ANISOU 2028  C   ALA A 251     2660   3593   4170    659    634    598       C  
ATOM   2029  O   ALA A 251      -9.917  32.125  -8.582  1.00 27.51           O  
ANISOU 2029  O   ALA A 251     2591   3611   4251    650    615    556       O  
ATOM   2030  CB  ALA A 251      -7.694  32.709  -6.049  1.00 26.68           C  
ANISOU 2030  CB  ALA A 251     2734   3487   3914    568    803    613       C  
ATOM   2031  N   ALA A 252      -8.131  33.507  -8.938  1.00 26.49           N  
ANISOU 2031  N   ALA A 252     2608   3478   3978    701    549    665       N  
ATOM   2032  CA  ALA A 252      -7.958  33.271 -10.380  1.00 26.65           C  
ANISOU 2032  CA  ALA A 252     2647   3511   3969    734    425    707       C  
ATOM   2033  C   ALA A 252      -8.224  31.800 -10.712  1.00 26.69           C  
ANISOU 2033  C   ALA A 252     2628   3550   3962    697    416    695       C  
ATOM   2034  O   ALA A 252      -7.659  30.905 -10.017  1.00 26.34           O  
ANISOU 2034  O   ALA A 252     2632   3528   3850    641    488    699       O  
ATOM   2035  CB  ALA A 252      -6.562  33.659 -10.758  1.00 26.13           C  
ANISOU 2035  CB  ALA A 252     2695   3452   3782    733    406    770       C  
ATOM   2036  N   VAL A 253      -9.002  31.574 -11.776  1.00 26.83           N  
ANISOU 2036  N   VAL A 253     2591   3565   4039    731    314    683       N  
ATOM   2037  CA  VAL A 253      -9.163  30.249 -12.429  1.00 26.62           C  
ANISOU 2037  CA  VAL A 253     2553   3570   3991    703    278    681       C  
ATOM   2038  C   VAL A 253      -8.138  30.136 -13.557  1.00 26.27           C  
ANISOU 2038  C   VAL A 253     2615   3539   3826    710    198    750       C  
ATOM   2039  O   VAL A 253      -8.366  30.739 -14.618  1.00 27.92           O  
ANISOU 2039  O   VAL A 253     2848   3722   4039    757     88    770       O  
ATOM   2040  CB  VAL A 253     -10.586  30.079 -12.960  1.00 27.81           C  
ANISOU 2040  CB  VAL A 253     2580   3705   4281    735    206    615       C  
ATOM   2041  CG1 VAL A 253     -10.812  28.661 -13.453  1.00 27.95           C  
ANISOU 2041  CG1 VAL A 253     2579   3756   4285    695    189    602       C  
ATOM   2042  CG2 VAL A 253     -11.608  30.446 -11.910  1.00 28.97           C  
ANISOU 2042  CG2 VAL A 253     2609   3826   4571    728    295    525       C  
ATOM   2043  N   ASN A 254      -7.074  29.372 -13.331  1.00 25.08           N  
ANISOU 2043  N   ASN A 254     2532   3419   3578    663    250    776       N  
ATOM   2044  CA  ASN A 254      -5.856  29.330 -14.174  1.00 24.56           C  
ANISOU 2044  CA  ASN A 254     2565   3364   3402    653    218    821       C  
ATOM   2045  C   ASN A 254      -6.053  28.365 -15.344  1.00 25.62           C  
ANISOU 2045  C   ASN A 254     2707   3515   3511    642    145    826       C  
ATOM   2046  O   ASN A 254      -5.351  28.509 -16.372  1.00 25.98           O  
ANISOU 2046  O   ASN A 254     2838   3556   3479    636    104    856       O  
ATOM   2047  CB  ASN A 254      -4.635  28.912 -13.357  1.00 23.28           C  
ANISOU 2047  CB  ASN A 254     2450   3219   3175    615    295    823       C  
ATOM   2048  CG  ASN A 254      -4.291  29.933 -12.306  1.00 22.83           C  
ANISOU 2048  CG  ASN A 254     2406   3143   3127    624    355    820       C  
ATOM   2049  ND2 ASN A 254      -3.942  29.472 -11.118  1.00 22.45           N  
ANISOU 2049  ND2 ASN A 254     2368   3096   3064    598    419    802       N  
ATOM   2050  OD1 ASN A 254      -4.359  31.125 -12.562  1.00 22.91           O  
ANISOU 2050  OD1 ASN A 254     2428   3127   3150    654    338    834       O  
ATOM   2051  N   VAL A 255      -6.964  27.409 -15.214  1.00 26.50           N  
ANISOU 2051  N   VAL A 255     2742   3642   3684    631    141    792       N  
ATOM   2052  CA  VAL A 255      -7.076  26.335 -16.231  1.00 26.97           C  
ANISOU 2052  CA  VAL A 255     2810   3722   3715    613     81    792       C  
ATOM   2053  C   VAL A 255      -8.437  25.666 -16.114  1.00 27.65           C  
ANISOU 2053  C   VAL A 255     2787   3812   3908    612     64    739       C  
ATOM   2054  O   VAL A 255      -9.023  25.632 -15.034  1.00 27.25           O  
ANISOU 2054  O   VAL A 255     2666   3755   3932    598    143    697       O  
ATOM   2055  CB  VAL A 255      -5.916  25.331 -16.116  1.00 26.44           C  
ANISOU 2055  CB  VAL A 255     2800   3682   3563    565    133    803       C  
ATOM   2056  CG1 VAL A 255      -5.720  24.907 -14.683  1.00 27.30           C  
ANISOU 2056  CG1 VAL A 255     2895   3794   3686    540    226    784       C  
ATOM   2057  CG2 VAL A 255      -6.085  24.114 -17.017  1.00 26.38           C  
ANISOU 2057  CG2 VAL A 255     2792   3695   3535    540     88    795       C  
ATOM   2058  N   VAL A 256      -8.877  25.161 -17.252  1.00 28.77           N  
ANISOU 2058  N   VAL A 256     2924   3958   4051    620    -32    734       N  
ATOM   2059  CA  VAL A 256     -10.219  24.581 -17.460  1.00 29.34           C  
ANISOU 2059  CA  VAL A 256     2883   4029   4238    626    -80    670       C  
ATOM   2060  C   VAL A 256     -10.048  23.521 -18.551  1.00 29.51           C  
ANISOU 2060  C   VAL A 256     2946   4071   4196    602   -144    682       C  
ATOM   2061  O   VAL A 256      -9.225  23.743 -19.461  1.00 28.70           O  
ANISOU 2061  O   VAL A 256     2957   3965   3984    606   -197    734       O  
ATOM   2062  CB  VAL A 256     -11.190  25.726 -17.790  1.00 30.82           C  
ANISOU 2062  CB  VAL A 256     3009   4173   4530    699   -184    640       C  
ATOM   2063  CG1 VAL A 256     -11.078  26.210 -19.228  1.00 31.08           C  
ANISOU 2063  CG1 VAL A 256     3138   4175   4496    746   -344    682       C  
ATOM   2064  CG2 VAL A 256     -12.627  25.375 -17.429  1.00 32.41           C  
ANISOU 2064  CG2 VAL A 256     3043   4367   4906    704   -186    538       C  
ATOM   2065  N   ASP A 257     -10.648  22.350 -18.345  1.00 30.53           N  
ANISOU 2065  N   ASP A 257     3002   4220   4380    562   -110    632       N  
ATOM   2066  CA  ASP A 257     -10.768  21.240 -19.321  1.00 30.11           C  
ANISOU 2066  CA  ASP A 257     2960   4185   4297    538   -172    624       C  
ATOM   2067  C   ASP A 257     -12.193  20.712 -19.184  1.00 20.10           C  
ATOM   2068  O   ASP A 257     -12.911  21.120 -18.219  1.00 32.05           O  
ANISOU 2068  O   ASP A 257     2961   4411   4804    533   -118    478       O  
ATOM   2069  CB  ASP A 257      -9.750  20.141 -19.037  1.00 29.09           C  
ANISOU 2069  CB  ASP A 257     2900   4082   4071    478    -82    651       C  
ATOM   2070  CG  ASP A 257      -9.376  19.290 -20.240  1.00 30.27           C  
ANISOU 2070  CG  ASP A 257     3108   4247   4145    458   -147    665       C  
ATOM   2071  OD1 ASP A 257     -10.128  19.279 -21.225  1.00 31.62           O  
ANISOU 2071  OD1 ASP A 257     3258   4411   4345    479   -257    645       O  
ATOM   2072  OD2 ASP A 257      -8.300  18.674 -20.211  1.00 31.48           O1-
ANISOU 2072  OD2 ASP A 257     3334   4414   4213    424    -94    690       O1-
ATOM   2073  N   PHE A 258     -12.602  19.828 -20.084  1.00 32.05           N  
ANISOU 2073  N   PHE A 258     3043   4437   4696    519   -262    508       N  
ATOM   2074  CA  PHE A 258     -13.934  19.202 -20.044  1.00 33.19           C  
ANISOU 2074  CA  PHE A 258     3040   4578   4991    505   -275    406       C  
ATOM   2075  C   PHE A 258     -14.057  18.088 -21.070  1.00 33.53           C  
ANISOU 2075  C   PHE A 258     3099   4639   5002    479   -349    395       C  
ATOM   2076  O   PHE A 258     -13.258  17.976 -21.955  1.00 32.99           O  
ANISOU 2076  O   PHE A 258     3152   4578   4803    485   -413    461       O  
ATOM   2077  CB  PHE A 258     -14.992  20.260 -20.302  1.00 34.33           C  
ANISOU 2077  CB  PHE A 258     3079   4687   5279    581   -394    344       C  
ATOM   2078  CG  PHE A 258     -15.082  20.784 -21.713  1.00 35.54           C  
ANISOU 2078  CG  PHE A 258     3298   4814   5393    654   -606    372       C  
ATOM   2079  CD1 PHE A 258     -15.823  20.129 -22.685  1.00 37.09           C  
ANISOU 2079  CD1 PHE A 258     3449   5005   5638    665   -738    317       C  
ATOM   2080  CD2 PHE A 258     -14.541  22.019 -22.037  1.00 35.96           C  
ANISOU 2080  CD2 PHE A 258     3461   4834   5368    714   -681    443       C  
ATOM   2081  CE1 PHE A 258     -15.983  20.690 -23.954  1.00 37.79           C  
ANISOU 2081  CE1 PHE A 258     3623   5052   5684    736   -952    339       C  
ATOM   2082  CE2 PHE A 258     -14.701  22.576 -23.308  1.00 36.81           C  
ANISOU 2082  CE2 PHE A 258     3661   4895   5429    778   -882    467       C  
ATOM   2083  CZ  PHE A 258     -15.410  21.904 -24.275  1.00 37.27           C  
ANISOU 2083  CZ  PHE A 258     3694   4944   5522    790  -1024    418       C  
ATOM   2084  N   ASP A 259     -15.083  17.270 -20.898  1.00 35.61           N  
ANISOU 2084  N   ASP A 259     3236   4905   5391    443   -324    299       N  
ATOM   2085  CA  ASP A 259     -15.567  16.293 -21.901  1.00 36.49           C  
ANISOU 2085  CA  ASP A 259     3321   5026   5519    427   -416    257       C  
ATOM   2086  C   ASP A 259     -17.093  16.292 -21.817  1.00 22.40           C  
ATOM   2087  O   ASP A 259     -17.642  17.223 -21.196  1.00 37.20           O  
ANISOU 2087  O   ASP A 259     3121   5072   5943    475   -445     69       O  
ATOM   2088  CB  ASP A 259     -14.921  14.927 -21.691  1.00 36.36           C  
ANISOU 2088  CB  ASP A 259     3372   5035   5408    343   -300    283       C  
ATOM   2089  CG  ASP A 259     -15.333  14.192 -20.432  1.00 37.70           C  
ANISOU 2089  CG  ASP A 259     3475   5198   5651    263   -121    223       C  
ATOM   2090  OD1 ASP A 259     -16.312  14.645 -19.779  1.00 39.25           O  
ANISOU 2090  OD1 ASP A 259     3542   5374   5997    261    -75    135       O  
ATOM   2091  OD2 ASP A 259     -14.658  13.158 -20.115  1.00 38.31           O1-
ANISOU 2091  OD2 ASP A 259     3641   5281   5634    201    -27    258       O1-
ATOM   2092  N   ASP A 260     -17.732  15.288 -22.419  1.00 40.50           N  
ANISOU 2092  N   ASP A 260     3567   5521   6299    408   -506     48       N  
ATOM   2093  CA  ASP A 260     -19.211  15.116 -22.416  1.00 42.79           C  
ANISOU 2093  CA  ASP A 260     3648   5793   6818    410   -547   -112       C  
ATOM   2094  C   ASP A 260     -19.762  15.217 -21.001  1.00 22.34           C  
ATOM   2095  O   ASP A 260     -20.813  15.826 -20.870  1.00 41.75           O  
ANISOU 2095  O   ASP A 260     3222   5618   7021    391   -395   -322       O  
ATOM   2096  CB  ASP A 260     -19.642  13.772 -23.001  1.00 46.12           C  
ANISOU 2096  CB  ASP A 260     4029   6230   7265    351   -561   -174       C  
ATOM   2097  CG  ASP A 260     -19.684  13.776 -24.519  1.00 49.68           C  
ANISOU 2097  CG  ASP A 260     4537   6677   7663    417   -801   -153       C  
ATOM   2098  OD1 ASP A 260     -19.586  14.904 -25.120  1.00 51.15           O1-
ANISOU 2098  OD1 ASP A 260     4781   6835   7819    514   -971   -109       O1-
ATOM   2099  OD2 ASP A 260     -19.775  12.650 -25.092  1.00 34.73           O1-
ATOM   2100  N   LYS A 261     -19.083  14.639 -20.008  1.00 37.94           N  
ANISOU 2100  N   LYS A 261     3003   5176   6238    263   -142   -147       N  
ATOM   2101  CA  LYS A 261     -19.640  14.429 -18.652  1.00 37.95           C  
ANISOU 2101  CA  LYS A 261     2924   5152   6342    173     77   -239       C  
ATOM   2102  C   LYS A 261     -19.412  15.672 -17.784  1.00 37.53           C  
ANISOU 2102  C   LYS A 261     2882   5082   6297    208    135   -212       C  
ATOM   2103  O   LYS A 261     -20.402  16.229 -17.214  1.00 39.37           O  
ANISOU 2103  O   LYS A 261     2955   5286   6720    203    193   -341       O  
ATOM   2104  CB  LYS A 261     -19.018  13.203 -17.989  1.00 37.24           C  
ANISOU 2104  CB  LYS A 261     2967   5063   6120     61    252   -192       C  
ATOM   2105  CG  LYS A 261     -19.698  12.808 -16.678  1.00 38.86           C  
ANISOU 2105  CG  LYS A 261     3120   5227   6417    -56    486   -298       C  
ATOM   2106  CD  LYS A 261     -19.353  11.405 -16.192  1.00 38.43           C  
ANISOU 2106  CD  LYS A 261     3196   5153   6253   -173    635   -277       C  
ATOM   2107  CE  LYS A 261     -20.285  10.881 -15.127  1.00 39.09           C  
ANISOU 2107  CE  LYS A 261     3224   5183   6447   -308    862   -413       C  
ATOM   2108  NZ  LYS A 261     -19.807   9.570 -14.651  0.69 38.93           N1+
ANISOU 2108  NZ  LYS A 261     3382   5128   6283   -415    991   -369       N1+
ATOM   2109  N   TYR A 262     -18.152  16.087 -17.673  1.00 35.19           N  
ANISOU 2109  N   TYR A 262     2759   4799   5812    239    128    -65       N  
ATOM   2110  CA  TYR A 262     -17.673  17.028 -16.632  1.00 33.61           C  
ANISOU 2110  CA  TYR A 262     2614   4582   5573    246    227    -21       C  
ATOM   2111  C   TYR A 262     -16.873  18.166 -17.264  1.00 32.65           C  
ANISOU 2111  C   TYR A 262     2574   4472   5360    352     77     87       C  
ATOM   2112  O   TYR A 262     -16.100  17.947 -18.225  1.00 32.32           O  
ANISOU 2112  O   TYR A 262     2639   4452   5188    384    -36    177       O  
ATOM   2113  CB  TYR A 262     -16.789  16.296 -15.624  1.00 32.31           C  
ANISOU 2113  CB  TYR A 262     2608   4412   5256    158    398     48       C  
ATOM   2114  CG  TYR A 262     -17.484  15.307 -14.710  1.00 32.39           C  
ANISOU 2114  CG  TYR A 262     2591   4388   5326     34    588    -49       C  
ATOM   2115  CD1 TYR A 262     -18.589  15.652 -13.969  1.00 33.18           C  
ANISOU 2115  CD1 TYR A 262     2555   4454   5596    -15    710   -184       C  
ATOM   2116  CD2 TYR A 262     -16.977  14.030 -14.531  1.00 31.82           C  
ANISOU 2116  CD2 TYR A 262     2647   4308   5134    -42    659     -8       C  
ATOM   2117  CE1 TYR A 262     -19.172  14.754 -13.086  1.00 34.17           C  
ANISOU 2117  CE1 TYR A 262     2685   4537   5760   -149    914   -277       C  
ATOM   2118  CE2 TYR A 262     -17.562  13.109 -13.673  1.00 32.27           C  
ANISOU 2118  CE2 TYR A 262     2720   4320   5222   -167    843    -90       C  
ATOM   2119  CZ  TYR A 262     -18.660  13.478 -12.940  1.00 33.62           C  
ANISOU 2119  CZ  TYR A 262     2767   4455   5551   -228    980   -224       C  
ATOM   2120  OH  TYR A 262     -19.226  12.583 -12.091  1.00 34.99           O  
ANISOU 2120  OH  TYR A 262     2976   4573   5745   -369   1184   -311       O  
ATOM   2121  N   ILE A 263     -17.081  19.361 -16.727  1.00 32.38           N  
ANISOU 2121  N   ILE A 263     2493   4415   5395    396     89     69       N  
ATOM   2122  CA  ILE A 263     -16.126  20.500 -16.824  1.00 31.60           C  
ANISOU 2122  CA  ILE A 263     2506   4315   5184    467     25    179       C  
ATOM   2123  C   ILE A 263     -15.252  20.477 -15.573  1.00 30.71           C  
ANISOU 2123  C   ILE A 263     2503   4203   4963    408    198    236       C  
ATOM   2124  O   ILE A 263     -15.790  20.277 -14.475  1.00 30.92           O  
ANISOU 2124  O   ILE A 263     2478   4208   5061    341    354    162       O  
ATOM   2125  CB  ILE A 263     -16.856  21.848 -16.941  1.00 32.16           C  
ANISOU 2125  CB  ILE A 263     2472   4352   5397    555    -72    124       C  
ATOM   2126  CG1 ILE A 263     -17.716  21.914 -18.195  1.00 32.90           C  
ANISOU 2126  CG1 ILE A 263     2473   4429   5598    628   -281     64       C  
ATOM   2127  CG2 ILE A 263     -15.868  23.001 -16.877  1.00 31.63           C  
ANISOU 2127  CG2 ILE A 263     2530   4277   5211    610   -103    233       C  
ATOM   2128  CD1 ILE A 263     -18.792  22.932 -18.131  1.00 34.44           C  
ANISOU 2128  CD1 ILE A 263     2510   4576   5999    704   -365    -45       C  
ATOM   2129  N   VAL A 264     -13.961  20.702 -15.742  1.00 29.74           N  
ANISOU 2129  N   VAL A 264     2529   4096   4674    430    170    352       N  
ATOM   2130  CA  VAL A 264     -12.998  20.710 -14.613  1.00 29.15           C  
ANISOU 2130  CA  VAL A 264     2569   4016   4490    388    300    407       C  
ATOM   2131  C   VAL A 264     -12.274  22.057 -14.624  1.00 28.70           C  
ANISOU 2131  C   VAL A 264     2567   3956   4383    454    251    472       C  
ATOM   2132  O   VAL A 264     -11.697  22.406 -15.666  1.00 28.91           O  
ANISOU 2132  O   VAL A 264     2647   3994   4343    505    133    531       O  
ATOM   2133  CB  VAL A 264     -12.023  19.533 -14.733  1.00 28.66           C  
ANISOU 2133  CB  VAL A 264     2629   3972   4290    344    317    466       C  
ATOM   2134  CG1 VAL A 264     -11.017  19.510 -13.586  1.00 28.12           C  
ANISOU 2134  CG1 VAL A 264     2685   3885   4115    314    416    515       C  
ATOM   2135  CG2 VAL A 264     -12.782  18.223 -14.827  1.00 29.18           C  
ANISOU 2135  CG2 VAL A 264     2645   4035   4405    279    358    403       C  
ATOM   2136  N   SER A 265     -12.346  22.778 -13.504  1.00 27.76           N  
ANISOU 2136  N   SER A 265     2441   3812   4294    445    350    454       N  
ATOM   2137  CA  SER A 265     -11.674  24.070 -13.254  1.00 25.84           C  
ANISOU 2137  CA  SER A 265     2250   3560   4009    496    335    506       C  
ATOM   2138  C   SER A 265     -10.613  23.853 -12.184  1.00 24.22           C  
ANISOU 2138  C   SER A 265     2167   3351   3685    450    440    552       C  
ATOM   2139  O   SER A 265     -10.824  23.004 -11.336  1.00 23.62           O  
ANISOU 2139  O   SER A 265     2114   3259   3599    381    545    519       O  
ATOM   2140  CB  SER A 265     -12.683  25.090 -12.844  1.00 26.36           C  
ANISOU 2140  CB  SER A 265     2200   3595   4220    526    351    434       C  
ATOM   2141  OG  SER A 265     -13.325  24.711 -11.643  1.00 26.39           O  
ANISOU 2141  OG  SER A 265     2158   3578   4292    452    510    355       O  
ATOM   2142  N   ALA A 266      -9.512  24.592 -12.268  1.00 23.45           N  
ANISOU 2142  N   ALA A 266     2153   3258   3499    488    404    619       N  
ATOM   2143  CA  ALA A 266      -8.442  24.645 -11.249  1.00 23.20           C  
ANISOU 2143  CA  ALA A 266     2229   3215   3370    464    475    654       C  
ATOM   2144  C   ALA A 266      -7.979  26.083 -11.072  1.00 22.62           C  
ANISOU 2144  C   ALA A 266     2171   3133   3293    511    463    679       C  
ATOM   2145  O   ALA A 266      -8.021  26.831 -12.050  1.00 23.01           O  
ANISOU 2145  O   ALA A 266     2193   3187   3362    562    377    699       O  
ATOM   2146  CB  ALA A 266      -7.289  23.768 -11.643  1.00 23.16           C  
ANISOU 2146  CB  ALA A 266     2313   3228   3258    454    435    698       C  
ATOM   2147  N   SER A 267      -7.494  26.417  -9.881  1.00 22.16           N  
ANISOU 2147  N   SER A 267     2173   3052   3193    490    543    681       N  
ATOM   2148  CA  SER A 267      -7.478  27.816  -9.396  1.00 22.02           C  
ANISOU 2148  CA  SER A 267     2144   3015   3206    521    567    680       C  
ATOM   2149  C   SER A 267      -6.285  28.068  -8.493  1.00 20.95           C  
ANISOU 2149  C   SER A 267     2117   2869   2977    510    603    708       C  
ATOM   2150  O   SER A 267      -5.775  27.115  -7.938  1.00 19.96           O  
ANISOU 2150  O   SER A 267     2068   2735   2780    473    625    711       O  
ATOM   2151  CB  SER A 267      -8.771  28.089  -8.675  1.00 22.93           C  
ANISOU 2151  CB  SER A 267     2177   3104   3432    499    652    610       C  
ATOM   2152  OG  SER A 267      -8.721  29.326  -7.994  1.00 22.96           O  
ANISOU 2152  OG  SER A 267     2181   3082   3459    519    695    602       O  
ATOM   2153  N   GLY A 268      -5.913  29.336  -8.349  1.00 21.10           N  
ANISOU 2153  N   GLY A 268     2140   2878   3001    545    601    720       N  
ATOM   2154  CA  GLY A 268      -4.949  29.830  -7.337  1.00 21.29           C  
ANISOU 2154  CA  GLY A 268     2248   2883   2959    538    640    729       C  
ATOM   2155  C   GLY A 268      -5.407  29.556  -5.917  1.00 21.96           C  
ANISOU 2155  C   GLY A 268     2380   2930   3033    486    741    694       C  
ATOM   2156  O   GLY A 268      -4.562  29.563  -4.997  1.00 21.36           O  
ANISOU 2156  O   GLY A 268     2406   2831   2879    471    757    700       O  
ATOM   2157  N   ASP A 269      -6.709  29.311  -5.756  1.00 23.07           N  
ANISOU 2157  N   ASP A 269     2453   3060   3253    455    806    648       N  
ATOM   2158  CA  ASP A 269      -7.353  29.037  -4.452  1.00 24.29           C  
ANISOU 2158  CA  ASP A 269     2656   3168   3404    383    936    598       C  
ATOM   2159  C   ASP A 269      -7.067  27.594  -4.010  1.00 14.82           C  
ATOM   2160  O   ASP A 269      -7.634  27.180  -2.994  1.00 23.84           O  
ANISOU 2160  O   ASP A 269     2790   3041   3228    246   1069    563       O  
ATOM   2161  CB  ASP A 269      -8.837  29.381  -4.547  1.00 26.43           C  
ANISOU 2161  CB  ASP A 269     2789   3430   3823    369   1006    523       C  
ATOM   2162  CG  ASP A 269      -9.694  28.309  -5.199  1.00 28.54           C  
ANISOU 2162  CG  ASP A 269     2980   3712   4153    343   1002    488       C  
ATOM   2163  OD1 ASP A 269      -9.126  27.333  -5.725  1.00 28.80           O  
ANISOU 2163  OD1 ASP A 269     3067   3767   4110    341    935    533       O  
ATOM   2164  OD2 ASP A 269     -10.945  28.452  -5.163  1.00 32.54           O1-
ANISOU 2164  OD2 ASP A 269     3364   4204   4796    322   1068    402       O1-
ATOM   2165  N   ARG A 270      -6.222  26.850  -4.747  1.00 23.07           N  
ANISOU 2165  N   ARG A 270     2650   3021   3096    352    848    651       N  
ATOM   2166  CA  ARG A 270      -5.675  25.518  -4.370  1.00 22.38           C  
ANISOU 2166  CA  ARG A 270     2692   2905   2907    315    830    665       C  
ATOM   2167  C   ARG A 270      -6.668  24.385  -4.622  1.00 22.44           C  
ANISOU 2167  C   ARG A 270     2674   2906   2946    258    880    636       C  
ATOM   2168  O   ARG A 270      -6.386  23.280  -4.202  1.00 23.01           O  
ANISOU 2168  O   ARG A 270     2868   2940   2934    217    881    643       O  
ATOM   2169  CB  ARG A 270      -5.288  25.516  -2.898  1.00 22.97           C  
ANISOU 2169  CB  ARG A 270     2935   2910   2883    272    885    659       C  
ATOM   2170  CG  ARG A 270      -4.405  26.680  -2.503  1.00 23.09           C  
ANISOU 2170  CG  ARG A 270     2973   2926   2876    320    848    675       C  
ATOM   2171  CD  ARG A 270      -3.993  26.594  -1.053  1.00 24.09           C  
ANISOU 2171  CD  ARG A 270     3286   2975   2891    278    881    668       C  
ATOM   2172  NE  ARG A 270      -3.187  27.754  -0.730  1.00 23.88           N  
ANISOU 2172  NE  ARG A 270     3262   2952   2858    325    844    674       N  
ATOM   2173  CZ  ARG A 270      -2.640  27.989   0.442  1.00 24.84           C  
ANISOU 2173  CZ  ARG A 270     3534   3013   2889    310    844    667       C  
ATOM   2174  NH1 ARG A 270      -2.803  27.151   1.454  1.00 26.34           N1+
ANISOU 2174  NH1 ARG A 270     3913   3123   2972    245    879    660       N1+
ATOM   2175  NH2 ARG A 270      -1.927  29.079   0.604  1.00 24.87           N  
ANISOU 2175  NH2 ARG A 270     3516   3029   2905    355    807    666       N  
ATOM   2176  N   THR A 271      -7.779  24.637  -5.296  1.00 22.64           N  
ANISOU 2176  N   THR A 271     2548   2962   3092    258    909    597       N  
ATOM   2177  CA  THR A 271      -8.871  23.654  -5.508  1.00 23.22           C  
ANISOU 2177  CA  THR A 271     2571   3029   3224    198    970    546       C  
ATOM   2178  C   THR A 271      -9.006  23.315  -6.992  1.00 22.63           C  
ANISOU 2178  C   THR A 271     2379   3012   3209    248    859    560       C  
ATOM   2179  O   THR A 271      -8.857  24.181  -7.837  1.00 21.98           O  
ANISOU 2179  O   THR A 271     2211   2966   3173    320    772    581       O  
ATOM   2180  CB  THR A 271     -10.213  24.193  -4.996  1.00 24.10           C  
ANISOU 2180  CB  THR A 271     2584   3116   3456    149   1102    457       C  
ATOM   2181  CG2 THR A 271     -10.155  24.579  -3.542  1.00 24.74           C  
ANISOU 2181  CG2 THR A 271     2791   3135   3475     86   1230    435       C  
ATOM   2182  OG1 THR A 271     -10.609  25.354  -5.723  1.00 23.75           O  
ANISOU 2182  OG1 THR A 271     2381   3108   3534    225   1042    441       O  
ATOM   2183  N   ILE A 272      -9.315  22.068  -7.267  1.00 23.16           N  
ANISOU 2183  N   ILE A 272     2459   3075   3266    204    866    545       N  
ATOM   2184  CA  ILE A 272     -10.013  21.653  -8.506  1.00 23.90           C  
ANISOU 2184  CA  ILE A 272     2420   3210   3450    222    804    521       C  
ATOM   2185  C   ILE A 272     -11.508  21.575  -8.203  1.00 25.72           C  
ANISOU 2185  C   ILE A 272     2538   3419   3814    163    913    419       C  
ATOM   2186  O   ILE A 272     -11.879  21.040  -7.154  1.00 26.15           O  
ANISOU 2186  O   ILE A 272     2669   3423   3846     71   1053    375       O  
ATOM   2187  CB  ILE A 272      -9.440  20.314  -8.968  1.00 23.62           C  
ANISOU 2187  CB  ILE A 272     2461   3181   3333    205    752    555       C  
ATOM   2188  CG1 ILE A 272      -7.976  20.467  -9.394  1.00 23.02           C  
ANISOU 2188  CG1 ILE A 272     2458   3127   3161    268    643    629       C  
ATOM   2189  CG2 ILE A 272     -10.293  19.737 -10.074  1.00 24.10           C  
ANISOU 2189  CG2 ILE A 272     2400   3274   3482    204    709    517       C  
ATOM   2190  CD1 ILE A 272      -7.110  19.267  -9.074  1.00 22.93           C  
ANISOU 2190  CD1 ILE A 272     2581   3085   3045    243    625    655       C  
ATOM   2191  N   LYS A 273     -12.339  22.098  -9.087  1.00 27.37           N  
ANISOU 2191  N   LYS A 273     2581   3657   4162    211    850    373       N  
ATOM   2192  CA  LYS A 273     -13.811  21.941  -8.995  1.00 29.78           C  
ANISOU 2192  CA  LYS A 273     2737   3944   4633    163    932    249       C  
ATOM   2193  C   LYS A 273     -14.307  21.247 -10.261  1.00 30.15           C  
ANISOU 2193  C   LYS A 273     2682   4025   4749    188    821    226       C  
ATOM   2194  O   LYS A 273     -13.825  21.550 -11.336  1.00 29.27           O  
ANISOU 2194  O   LYS A 273     2564   3950   4609    271    664    290       O  
ATOM   2195  CB  LYS A 273     -14.482  23.286  -8.703  1.00 31.12           C  
ANISOU 2195  CB  LYS A 273     2787   4099   4938    201    955    185       C  
ATOM   2196  CG  LYS A 273     -14.143  23.814  -7.316  1.00 32.40           C  
ANISOU 2196  CG  LYS A 273     3056   4220   5036    152   1097    187       C  
ATOM   2197  CD  LYS A 273     -14.954  24.998  -6.825  1.00 34.41           C  
ANISOU 2197  CD  LYS A 273     3189   4448   5439    164   1164     97       C  
ATOM   2198  CE  LYS A 273     -14.422  25.566  -5.516  1.00 34.93           C  
ANISOU 2198  CE  LYS A 273     3389   4475   5409    120   1289    118       C  
ATOM   2199  NZ  LYS A 273     -15.512  26.012  -4.622  1.00 37.31           N1+
ANISOU 2199  NZ  LYS A 273     3600   4727   5848     50   1463    -19       N1+
ATOM   2200  N   VAL A 274     -15.237  20.319 -10.077  1.00 31.91           N  
ANISOU 2200  N   VAL A 274     2843   4228   5052    105    916    132       N  
ATOM   2201  CA  VAL A 274     -15.937  19.525 -11.125  1.00 32.33           C  
ANISOU 2201  CA  VAL A 274     2784   4306   5196    107    838     79       C  
ATOM   2202  C   VAL A 274     -17.373  20.049 -11.252  1.00 33.49           C  
ANISOU 2202  C   VAL A 274     2710   4438   5578    114    851    -71       C  
ATOM   2203  O   VAL A 274     -18.011  20.257 -10.211  1.00 33.82           O  
ANISOU 2203  O   VAL A 274     2709   4438   5704     41   1021   -168       O  
ATOM   2204  CB  VAL A 274     -15.949  18.055 -10.678  1.00 32.92           C  
ANISOU 2204  CB  VAL A 274     2953   4357   5199     -7    958     63       C  
ATOM   2205  CG1 VAL A 274     -16.552  17.118 -11.713  1.00 33.57           C  
ANISOU 2205  CG1 VAL A 274     2937   4462   5354    -14    885     14       C  
ATOM   2206  CG2 VAL A 274     -14.563  17.603 -10.245  1.00 31.53           C  
ANISOU 2206  CG2 VAL A 274     2999   4172   4809    -15    958    189       C  
ATOM   2207  N   TRP A 275     -17.836  20.227 -12.489  1.00 33.82           N  
ANISOU 2207  N   TRP A 275     2626   4505   5720    198    673    -97       N  
ATOM   2208  CA  TRP A 275     -19.183  20.724 -12.863  1.00 35.55           C  
ANISOU 2208  CA  TRP A 275     2615   4706   6184    237    618   -248       C  
ATOM   2209  C   TRP A 275     -19.778  19.810 -13.937  1.00 37.14           C  
ANISOU 2209  C   TRP A 275     2725   4926   6460    242    506   -303       C  
ATOM   2210  O   TRP A 275     -19.009  19.206 -14.702  1.00 36.88           O  
ANISOU 2210  O   TRP A 275     2810   4926   6275    260    407   -193       O  
ATOM   2211  CB  TRP A 275     -19.118  22.167 -13.364  1.00 34.70           C  
ANISOU 2211  CB  TRP A 275     2463   4593   6127    369    453   -218       C  
ATOM   2212  CG  TRP A 275     -18.077  23.005 -12.700  1.00 32.89           C  
ANISOU 2212  CG  TRP A 275     2381   4362   5752    386    501   -104       C  
ATOM   2213  CD1 TRP A 275     -16.727  22.945 -12.876  1.00 31.59           C  
ANISOU 2213  CD1 TRP A 275     2406   4225   5370    402    462     52       C  
ATOM   2214  CD2 TRP A 275     -18.298  24.073 -11.777  1.00 32.90           C  
ANISOU 2214  CD2 TRP A 275     2342   4331   5828    393    592   -149       C  
ATOM   2215  CE2 TRP A 275     -17.033  24.602 -11.440  1.00 31.49           C  
ANISOU 2215  CE2 TRP A 275     2341   4163   5460    412    598     -9       C  
ATOM   2216  CE3 TRP A 275     -19.440  24.621 -11.198  1.00 34.33           C  
ANISOU 2216  CE3 TRP A 275     2346   4471   6227    380    676   -307       C  
ATOM   2217  NE1 TRP A 275     -16.087  23.882 -12.108  1.00 30.56           N  
ANISOU 2217  NE1 TRP A 275     2355   4082   5174    416    520    106       N  
ATOM   2218  CZ2 TRP A 275     -16.883  25.648 -10.541  1.00 31.45           C  
ANISOU 2218  CZ2 TRP A 275     2352   4131   5466    419    680    -12       C  
ATOM   2219  CZ3 TRP A 275     -19.290  25.657 -10.310  1.00 34.35           C  
ANISOU 2219  CZ3 TRP A 275     2366   4446   6240    386    765   -311       C  
ATOM   2220  CH2 TRP A 275     -18.030  26.153  -9.980  1.00 32.92           C  
ANISOU 2220  CH2 TRP A 275     2374   4278   5856    404    766   -160       C  
ATOM   2221  N   SER A 276     -21.106  19.698 -13.976  1.00 39.96           N  
ANISOU 2221  N   SER A 276     2871   5259   7052    222    526   -481       N  
ATOM   2222  CA  SER A 276     -21.840  18.929 -15.008  1.00 41.60           C  
ANISOU 2222  CA  SER A 276     2958   5479   7371    234    402   -563       C  
ATOM   2223  C   SER A 276     -21.688  19.665 -16.332  1.00 42.27           C  
ANISOU 2223  C   SER A 276     3037   5574   7449    385    111   -501       C  
ATOM   2224  O   SER A 276     -22.008  20.872 -16.388  1.00 43.10           O  
ANISOU 2224  O   SER A 276     3065   5650   7661    479     12   -533       O  
ATOM   2225  CB  SER A 276     -23.282  18.760 -14.665  1.00 43.56           C  
ANISOU 2225  CB  SER A 276     2964   5691   7895    179    495   -790       C  
ATOM   2226  OG  SER A 276     -23.911  17.903 -15.605  1.00 44.82           O  
ANISOU 2226  OG  SER A 276     3019   5863   8149    180    385   -869       O  
ATOM   2227  N   THR A 277     -21.231  18.974 -17.368  1.00 42.52           N  
ANISOU 2227  N   THR A 277     3161   5636   7359    405    -22   -417       N  
ATOM   2228  CA  THR A 277     -21.148  19.597 -18.704  1.00 43.38           C  
ANISOU 2228  CA  THR A 277     3294   5740   7447    535   -301   -365       C  
ATOM   2229  C   THR A 277     -22.560  19.936 -19.179  1.00 46.17           C  
ANISOU 2229  C   THR A 277     3416   6053   8072    602   -449   -544       C  
ATOM   2230  O   THR A 277     -22.735  21.003 -19.780  1.00 47.25           O  
ANISOU 2230  O   THR A 277     3542   6154   8259    725   -653   -538       O  
ATOM   2231  CB  THR A 277     -20.384  18.712 -19.676  1.00 42.90           C  
ANISOU 2231  CB  THR A 277     3387   5715   7197    523   -386   -253       C  
ATOM   2232  CG2 THR A 277     -20.021  19.478 -20.931  1.00 43.66           C  
ANISOU 2232  CG2 THR A 277     3586   5797   7207    639   -639   -167       C  
ATOM   2233  OG1 THR A 277     -19.221  18.266 -18.978  1.00 40.81           O  
ANISOU 2233  OG1 THR A 277     3289   5480   6736    448   -215   -134       O  
ATOM   2234  N   SER A 278     -23.537  19.088 -18.873  1.00 47.94           N  
ANISOU 2234  N   SER A 278     3464   6275   8476    524   -347   -707       N  
ATOM   2235  CA  SER A 278     -24.921  19.242 -19.374  1.00 50.92           C  
ANISOU 2235  CA  SER A 278     3593   6613   9142    583   -494   -908       C  
ATOM   2236  C   SER A 278     -25.686  20.308 -18.576  1.00 51.51           C  
ANISOU 2236  C   SER A 278     3485   6639   9446    618   -441  -1048       C  
ATOM   2237  O   SER A 278     -26.372  21.137 -19.217  1.00 53.49           O  
ANISOU 2237  O   SER A 278     3611   6842   9870    750   -677  -1135       O  
ATOM   2238  CB  SER A 278     -25.620  17.924 -19.367  1.00 53.25           C  
ANISOU 2238  CB  SER A 278     3766   6922   9544    476   -393  -1040       C  
ATOM   2239  OG  SER A 278     -26.111  17.649 -18.067  1.00 55.84           O  
ANISOU 2239  OG  SER A 278     3983   7237   9996    349   -100  -1166       O  
ATOM   2240  N   THR A 279     -25.595  20.304 -17.243  1.00 50.26           N  
ANISOU 2240  N   THR A 279     3320   6482   9293    509   -154  -1076       N  
ATOM   2241  CA  THR A 279     -26.418  21.191 -16.371  1.00 51.23           C  
ANISOU 2241  CA  THR A 279     3251   6556   9657    514    -54  -1242       C  
ATOM   2242  C   THR A 279     -25.630  22.442 -15.974  1.00 50.44           C  
ANISOU 2242  C   THR A 279     3285   6445   9433    586    -69  -1107       C  
ATOM   2243  O   THR A 279     -26.274  23.443 -15.630  1.00 51.21           O  
ANISOU 2243  O   THR A 279     3231   6495   9732    647    -91  -1225       O  
ATOM   2244  CB  THR A 279     -26.906  20.472 -15.111  1.00 51.33           C  
ANISOU 2244  CB  THR A 279     3179   6561   9761    335    290  -1380       C  
ATOM   2245  CG2 THR A 279     -27.503  19.114 -15.399  1.00 52.16           C  
ANISOU 2245  CG2 THR A 279     3198   6679   9943    235    351  -1490       C  
ATOM   2246  OG1 THR A 279     -25.798  20.350 -14.220  1.00 48.70           O  
ANISOU 2246  OG1 THR A 279     3090   6251   9164    248    489  -1211       O  
ATOM   2247  N   CYS A 280     -24.293  22.385 -16.009  1.00 48.94           N  
ANISOU 2247  N   CYS A 280     3360   6296   8940    577    -56   -882       N  
ATOM   2248  CA  CYS A 280     -23.390  23.475 -15.562  1.00 48.11           C  
ANISOU 2248  CA  CYS A 280     3404   6185   8690    625    -41   -744       C  
ATOM   2249  C   CYS A 280     -23.531  23.686 -14.056  1.00 47.96           C  
ANISOU 2249  C   CYS A 280     3347   6150   8724    521    243   -815       C  
ATOM   2250  O   CYS A 280     -23.005  24.682 -13.576  1.00 47.56           O  
ANISOU 2250  O   CYS A 280     3376   6087   8609    560    264   -743       O  
ATOM   2251  CB  CYS A 280     -23.689  24.773 -16.301  1.00 50.24           C  
ANISOU 2251  CB  CYS A 280     3619   6408   9063    789   -299   -754       C  
ATOM   2252  SG  CYS A 280     -23.132  24.771 -18.029  1.00 51.15           S  
ANISOU 2252  SG  CYS A 280     3899   6526   9010    906   -630   -607       S  
ATOM   2253  N   GLU A 281     -24.208  22.776 -13.345  1.00 48.49           N  
ANISOU 2253  N   GLU A 281     3314   6211   8897    386    460   -955       N  
ATOM   2254  CA  GLU A 281     -24.260  22.761 -11.865  1.00 47.82           C  
ANISOU 2254  CA  GLU A 281     3252   6103   8814    252    767  -1014       C  
ATOM   2255  C   GLU A 281     -22.933  22.191 -11.335  1.00 21.13           C  
ATOM   2256  O   GLU A 281     -22.359  21.276 -11.968  1.00 42.58           O  
ANISOU 2256  O   GLU A 281     2993   5508   7679    165    811   -711       O  
ATOM   2257  CB  GLU A 281     -25.453  21.946 -11.349  1.00 50.75           C  
ANISOU 2257  CB  GLU A 281     3439   6444   9401    119    967  -1240       C  
ATOM   2258  CG  GLU A 281     -26.833  22.530 -11.654  1.00 54.14           C  
ANISOU 2258  CG  GLU A 281     3548   6831  10191    183    885  -1481       C  
ATOM   2259  CD  GLU A 281     -27.281  23.765 -10.871  1.00 56.36           C  
ANISOU 2259  CD  GLU A 281     3708   7062  10643    209    968  -1594       C  
ATOM   2260  OE1 GLU A 281     -27.336  24.841 -11.517  1.00 57.22           O  
ANISOU 2260  OE1 GLU A 281     3748   7157  10836    376    723  -1576       O  
ATOM   2261  OE2 GLU A 281     -27.622  23.663  -9.636  1.00 57.60           O1-
ANISOU 2261  OE2 GLU A 281     3845   7186  10856     61   1274  -1709       O1-
ATOM   2262  N   PHE A 282     -22.454  22.755 -10.228  1.00 41.61           N  
ANISOU 2262  N   PHE A 282     2863   5328   7620    128   1044   -775       N  
ATOM   2263  CA  PHE A 282     -21.326  22.248  -9.415  1.00 38.74           C  
ANISOU 2263  CA  PHE A 282     2761   4971   6987     40   1186   -629       C  
ATOM   2264  C   PHE A 282     -21.594  20.807  -9.012  1.00 38.39           C  
ANISOU 2264  C   PHE A 282     2770   4912   6903   -110   1359   -681       C  
ATOM   2265  O   PHE A 282     -22.747  20.495  -8.711  1.00 41.00           O  
ANISOU 2265  O   PHE A 282     2938   5208   7432   -195   1496   -869       O  
ATOM   2266  CB  PHE A 282     -21.213  23.055  -8.131  1.00 38.49           C  
ANISOU 2266  CB  PHE A 282     2786   4899   6940    -10   1365   -650       C  
ATOM   2267  CG  PHE A 282     -20.162  22.555  -7.182  1.00 37.28           C  
ANISOU 2267  CG  PHE A 282     2903   4735   6527   -102   1504   -524       C  
ATOM   2268  CD1 PHE A 282     -18.815  22.757  -7.450  1.00 35.72           C  
ANISOU 2268  CD1 PHE A 282     2886   4573   6114    -27   1372   -334       C  
ATOM   2269  CD2 PHE A 282     -20.524  21.874  -6.036  1.00 37.53           C  
ANISOU 2269  CD2 PHE A 282     3015   4711   6534   -267   1763   -607       C  
ATOM   2270  CE1 PHE A 282     -17.853  22.302  -6.567  1.00 34.95           C  
ANISOU 2270  CE1 PHE A 282     3028   4455   5795    -99   1474   -234       C  
ATOM   2271  CE2 PHE A 282     -19.565  21.433  -5.144  1.00 36.69           C  
ANISOU 2271  CE2 PHE A 282     3181   4577   6181   -343   1865   -493       C  
ATOM   2272  CZ  PHE A 282     -18.233  21.642  -5.415  1.00 35.74           C  
ANISOU 2272  CZ  PHE A 282     3222   4494   5863   -252   1708   -308       C  
ATOM   2273  N   VAL A 283     -20.563  19.972  -8.970  1.00 35.81           N  
ANISOU 2273  N   VAL A 283     2666   4602   6337   -146   1362   -533       N  
ATOM   2274  CA  VAL A 283     -20.695  18.552  -8.547  1.00 35.40           C  
ANISOU 2274  CA  VAL A 283     2713   4524   6214   -290   1522   -563       C  
ATOM   2275  C   VAL A 283     -19.853  18.335  -7.301  1.00 34.54           C  
ANISOU 2275  C   VAL A 283     2868   4370   5887   -381   1685   -473       C  
ATOM   2276  O   VAL A 283     -20.427  17.962  -6.295  1.00 36.07           O  
ANISOU 2276  O   VAL A 283     3103   4498   6104   -524   1916   -577       O  
ATOM   2277  CB  VAL A 283     -20.290  17.578  -9.658  1.00 34.38           C  
ANISOU 2277  CB  VAL A 283     2619   4439   6004   -251   1364   -481       C  
ATOM   2278  CG1 VAL A 283     -20.155  16.141  -9.156  1.00 34.51           C  
ANISOU 2278  CG1 VAL A 283     2793   4420   5899   -390   1517   -475       C  
ATOM   2279  CG2 VAL A 283     -21.252  17.669 -10.816  1.00 35.20           C  
ANISOU 2279  CG2 VAL A 283     2478   4573   6325   -179   1213   -590       C  
ATOM   2280  N   ARG A 284     -18.538  18.529  -7.386  1.00 32.95           N  
ANISOU 2280  N   ARG A 284     2844   4194   5483   -306   1565   -297       N  
ATOM   2281  CA  ARG A 284     -17.619  18.274  -6.245  1.00 32.25           C  
ANISOU 2281  CA  ARG A 284     3023   4055   5175   -376   1675   -205       C  
ATOM   2282  C   ARG A 284     -16.341  19.108  -6.392  1.00 30.38           C  
ANISOU 2282  C   ARG A 284     2883   3854   4804   -255   1519    -55       C  
ATOM   2283  O   ARG A 284     -15.992  19.472  -7.516  1.00 29.11           O  
ANISOU 2283  O   ARG A 284     2634   3757   4669   -137   1328      5       O  
ATOM   2284  CB  ARG A 284     -17.342  16.770  -6.117  1.00 32.35           C  
ANISOU 2284  CB  ARG A 284     3205   4033   5053   -468   1729   -171       C  
ATOM   2285  CG  ARG A 284     -16.240  16.206  -7.008  1.00 30.70           C  
ANISOU 2285  CG  ARG A 284     3082   3872   4710   -378   1531    -30       C  
ATOM   2286  CD  ARG A 284     -16.133  14.705  -6.780  1.00 31.19           C  
ANISOU 2286  CD  ARG A 284     3304   3884   4663   -479   1603    -21       C  
ATOM   2287  NE  ARG A 284     -17.441  14.057  -6.838  1.00 32.87           N  
ANISOU 2287  NE  ARG A 284     3393   4072   5023   -588   1742   -168       N  
ATOM   2288  CZ  ARG A 284     -17.999  13.495  -7.918  1.00 33.19           C  
ANISOU 2288  CZ  ARG A 284     3272   4158   5180   -569   1664   -219       C  
ATOM   2289  NH1 ARG A 284     -17.377  13.426  -9.081  1.00 31.98           N1+
ANISOU 2289  NH1 ARG A 284     3079   4076   4998   -452   1451   -129       N1+
ATOM   2290  NH2 ARG A 284     -19.201  12.964  -7.823  1.00 35.03           N  
ANISOU 2290  NH2 ARG A 284     3390   4360   5559   -678   1809   -372       N  
ATOM   2291  N   THR A 285     -15.712  19.411  -5.253  1.00 29.99           N  
ANISOU 2291  N   THR A 285     3017   3757   4620   -295   1609     -7       N  
ATOM   2292  CA  THR A 285     -14.373  20.026  -5.129  1.00 28.60           C  
ANISOU 2292  CA  THR A 285     2974   3599   4294   -208   1492    127       C  
ATOM   2293  C   THR A 285     -13.334  18.932  -4.883  1.00 27.94           C  
ANISOU 2293  C   THR A 285     3118   3486   4012   -233   1455    223       C  
ATOM   2294  O   THR A 285     -13.632  17.998  -4.138  1.00 28.75           O  
ANISOU 2294  O   THR A 285     3356   3518   4049   -349   1589    188       O  
ATOM   2295  CB  THR A 285     -14.318  20.967  -3.931  1.00 29.39           C  
ANISOU 2295  CB  THR A 285     3149   3651   4365   -240   1609    108       C  
ATOM   2296  CG2 THR A 285     -12.911  21.453  -3.652  1.00 28.56           C  
ANISOU 2296  CG2 THR A 285     3201   3552   4099   -168   1502    233       C  
ATOM   2297  OG1 THR A 285     -15.193  22.068  -4.169  1.00 30.04           O  
ANISOU 2297  OG1 THR A 285     3017   3756   4640   -201   1625     19       O  
ATOM   2298  N   LEU A 286     -12.156  19.051  -5.490  1.00 26.75           N  
ANISOU 2298  N   LEU A 286     3010   3378   3774   -131   1283    331       N  
ATOM   2299  CA  LEU A 286     -10.992  18.161  -5.267  1.00 25.62           C  
ANISOU 2299  CA  LEU A 286     3069   3205   3459   -129   1215    417       C  
ATOM   2300  C   LEU A 286      -9.934  19.001  -4.584  1.00 25.30           C  
ANISOU 2300  C   LEU A 286     3143   3148   3321    -78   1169    479       C  
ATOM   2301  O   LEU A 286      -9.249  19.773  -5.260  1.00 24.35           O  
ANISOU 2301  O   LEU A 286     2943   3088   3220     22   1046    525       O  
ATOM   2302  CB  LEU A 286     -10.480  17.631  -6.603  1.00 24.61           C  
ANISOU 2302  CB  LEU A 286     2870   3141   3339    -54   1057    465       C  
ATOM   2303  CG  LEU A 286     -10.981  16.243  -6.998  1.00 24.98           C  
ANISOU 2303  CG  LEU A 286     2926   3173   3391   -117   1083    435       C  
ATOM   2304  CD1 LEU A 286     -12.511  16.177  -6.950  1.00 26.00           C  
ANISOU 2304  CD1 LEU A 286     2920   3294   3663   -198   1219    322       C  
ATOM   2305  CD2 LEU A 286     -10.430  15.859  -8.378  1.00 23.54           C  
ANISOU 2305  CD2 LEU A 286     2668   3058   3218    -38    924    480       C  
ATOM   2306  N   ASN A 287      -9.885  18.921  -3.268  1.00 26.38           N  
ANISOU 2306  N   ASN A 287     3462   3201   3360   -153   1275    469       N  
ATOM   2307  CA  ASN A 287      -8.947  19.714  -2.449  1.00 26.00           C  
ANISOU 2307  CA  ASN A 287     3538   3124   3215   -115   1239    515       C  
ATOM   2308  C   ASN A 287      -7.849  18.773  -1.989  1.00 26.15           C  
ANISOU 2308  C   ASN A 287     3784   3078   3072   -110   1148    575       C  
ATOM   2309  O   ASN A 287      -8.069  17.541  -1.982  1.00 25.73           O  
ANISOU 2309  O   ASN A 287     3827   2979   2970   -169   1170    570       O  
ATOM   2310  CB  ASN A 287      -9.655  20.390  -1.293  1.00 26.86           C  
ANISOU 2310  CB  ASN A 287     3700   3176   3328   -198   1410    456       C  
ATOM   2311  CG  ASN A 287     -10.276  19.396  -0.345  1.00 28.12           C  
ANISOU 2311  CG  ASN A 287     4047   3233   3405   -341   1570    409       C  
ATOM   2312  ND2 ASN A 287     -10.125  19.649   0.936  1.00 29.32           N  
ANISOU 2312  ND2 ASN A 287     4404   3296   3440   -408   1661    403       N  
ATOM   2313  OD1 ASN A 287     -10.873  18.411  -0.756  1.00 28.09           O  
ANISOU 2313  OD1 ASN A 287     4018   3223   3433   -396   1614    376       O  
ATOM   2314  N   GLY A 288      -6.697  19.361  -1.691  1.00 26.73           N  
ANISOU 2314  N   GLY A 288     3927   3149   3080    -35   1037    623       N  
ATOM   2315  CA  GLY A 288      -5.499  18.598  -1.312  1.00 27.67           C  
ANISOU 2315  CA  GLY A 288     4238   3206   3069     -1    906    668       C  
ATOM   2316  C   GLY A 288      -4.231  19.354  -1.608  1.00 26.95           C  
ANISOU 2316  C   GLY A 288     4095   3158   2986    112    755    700       C  
ATOM   2317  O   GLY A 288      -3.305  19.287  -0.766  1.00 27.75           O  
ANISOU 2317  O   GLY A 288     4370   3188   2985    136    672    716       O  
ATOM   2318  N   HIS A 289      -4.182  20.083  -2.724  1.00 26.19           N  
ANISOU 2318  N   HIS A 289     3781   3165   3005    176    718    702       N  
ATOM   2319  CA  HIS A 289      -2.959  20.845  -3.068  1.00 25.23           C  
ANISOU 2319  CA  HIS A 289     3605   3084   2899    269    596    720       C  
ATOM   2320  C   HIS A 289      -2.775  21.837  -1.940  1.00 26.48           C  
ANISOU 2320  C   HIS A 289     3849   3201   3012    263    634    715       C  
ATOM   2321  O   HIS A 289      -3.822  22.288  -1.370  1.00 26.51           O  
ANISOU 2321  O   HIS A 289     3858   3188   3027    197    773    694       O  
ATOM   2322  CB  HIS A 289      -3.049  21.479  -4.444  1.00 24.01           C  
ANISOU 2322  CB  HIS A 289     3239   3030   2856    318    574    723       C  
ATOM   2323  CG  HIS A 289      -2.590  20.600  -5.563  1.00 23.50           C  
ANISOU 2323  CG  HIS A 289     3117   2999   2810    349    486    729       C  
ATOM   2324  CD2 HIS A 289      -3.238  20.092  -6.630  1.00 22.97           C  
ANISOU 2324  CD2 HIS A 289     2949   2981   2799    336    495    727       C  
ATOM   2325  ND1 HIS A 289      -1.269  20.194  -5.699  1.00 23.38           N  
ANISOU 2325  ND1 HIS A 289     3145   2971   2767    400    369    726       N  
ATOM   2326  CE1 HIS A 289      -1.129  19.452  -6.780  1.00 22.37           C  
ANISOU 2326  CE1 HIS A 289     2949   2880   2673    412    324    723       C  
ATOM   2327  NE2 HIS A 289      -2.322  19.377  -7.357  1.00 22.44           N  
ANISOU 2327  NE2 HIS A 289     2877   2925   2723    373    398    729       N  
ATOM   2328  N   LYS A 290      -1.509  22.084  -1.592  1.00 27.37           N  
ANISOU 2328  N   LYS A 290     4028   3290   3082    324    516    720       N  
ATOM   2329  CA  LYS A 290      -1.094  22.942  -0.456  1.00 28.41           C  
ANISOU 2329  CA  LYS A 290     4267   3372   3156    326    518    713       C  
ATOM   2330  C   LYS A 290      -0.949  24.372  -0.949  1.00 26.33           C  
ANISOU 2330  C   LYS A 290     3836   3185   2984    370    537    708       C  
ATOM   2331  O   LYS A 290      -0.807  25.255  -0.108  1.00 26.52           O  
ANISOU 2331  O   LYS A 290     3916   3182   2979    365    566    699       O  
ATOM   2332  CB  LYS A 290       0.233  22.433   0.105  1.00 31.06           C  
ANISOU 2332  CB  LYS A 290     4749   3637   3415    379    356    707       C  
ATOM   2333  CG  LYS A 290       0.233  20.986   0.582  1.00 33.91           C  
ANISOU 2333  CG  LYS A 290     5306   3902   3676    350    304    715       C  
ATOM   2334  CD  LYS A 290      -0.473  20.850   1.915  1.00 37.89           C  
ANISOU 2334  CD  LYS A 290     6044   4302   4050    258    403    722       C  
ATOM   2335  CE  LYS A 290      -0.706  19.419   2.370  1.00 41.38           C  
ANISOU 2335  CE  LYS A 290     6707   4636   4379    204    388    734       C  
ATOM   2336  NZ  LYS A 290      -1.865  19.292   3.306  1.00 42.79           N1+
ANISOU 2336  NZ  LYS A 290     7059   4739   4461     72    574    731       N1+
ATOM   2337  N   ARG A 291      -0.956  24.555  -2.265  1.00 24.22           N  
ANISOU 2337  N   ARG A 291     3391   3001   2811    406    518    713       N  
ATOM   2338  CA  ARG A 291      -0.716  25.851  -2.929  1.00 23.54           C  
ANISOU 2338  CA  ARG A 291     3162   2979   2803    449    521    712       C  
ATOM   2339  C   ARG A 291      -1.529  25.915  -4.219  1.00 22.88           C  
ANISOU 2339  C   ARG A 291     2928   2963   2804    450    554    724       C  
ATOM   2340  O   ARG A 291      -2.162  24.940  -4.562  1.00 22.32           O  
ANISOU 2340  O   ARG A 291     2853   2894   2735    421    568    727       O  
ATOM   2341  CB  ARG A 291       0.773  26.034  -3.220  1.00 23.57           C  
ANISOU 2341  CB  ARG A 291     3151   2992   2813    510    406    695       C  
ATOM   2342  CG  ARG A 291       1.630  26.225  -1.981  1.00 24.85           C  
ANISOU 2342  CG  ARG A 291     3443   3087   2912    525    348    672       C  
ATOM   2343  CD  ARG A 291       1.295  27.404  -1.076  1.00 25.03           C  
ANISOU 2343  CD  ARG A 291     3503   3091   2917    506    424    671       C  
ATOM   2344  NE  ARG A 291       1.583  28.669  -1.721  1.00 24.73           N  
ANISOU 2344  NE  ARG A 291     3330   3109   2955    536    444    665       N  
ATOM   2345  CZ  ARG A 291       2.797  29.156  -1.946  1.00 24.28           C  
ANISOU 2345  CZ  ARG A 291     3232   3063   2929    580    370    631       C  
ATOM   2346  NH1 ARG A 291       3.878  28.487  -1.592  1.00 24.73           N1+
ANISOU 2346  NH1 ARG A 291     3350   3081   2964    611    254    592       N1+
ATOM   2347  NH2 ARG A 291       2.914  30.315  -2.552  1.00 23.94           N  
ANISOU 2347  NH2 ARG A 291     3086   3062   2946    591    413    629       N  
ATOM   2348  N   GLY A 292      -1.496  27.062  -4.896  1.00 22.62           N  
ANISOU 2348  N   GLY A 292     2790   2974   2833    482    559    729       N  
ATOM   2349  CA  GLY A 292      -2.188  27.312  -6.169  1.00 22.43           C  
ANISOU 2349  CA  GLY A 292     2643   3000   2880    494    563    741       C  
ATOM   2350  C   GLY A 292      -1.884  26.235  -7.191  1.00 22.31           C  
ANISOU 2350  C   GLY A 292     2607   3011   2858    499    499    748       C  
ATOM   2351  O   GLY A 292      -0.811  25.597  -7.112  1.00 21.73           O  
ANISOU 2351  O   GLY A 292     2585   2926   2744    509    439    738       O  
ATOM   2352  N   ILE A 293      -2.812  26.023  -8.116  1.00 22.65           N  
ANISOU 2352  N   ILE A 293     2573   3084   2950    493    503    755       N  
ATOM   2353  CA  ILE A 293      -2.719  25.014  -9.203  1.00 22.34           C  
ANISOU 2353  CA  ILE A 293     2509   3072   2909    491    449    760       C  
ATOM   2354  C   ILE A 293      -2.527  25.805 -10.491  1.00 22.46           C  
ANISOU 2354  C   ILE A 293     2466   3120   2948    520    409    774       C  
ATOM   2355  O   ILE A 293      -3.367  26.704 -10.779  1.00 22.51           O  
ANISOU 2355  O   ILE A 293     2421   3128   3002    536    419    782       O  
ATOM   2356  CB  ILE A 293      -3.988  24.148  -9.234  1.00 22.89           C  
ANISOU 2356  CB  ILE A 293     2549   3139   3009    454    483    748       C  
ATOM   2357  CG1 ILE A 293      -4.104  23.320  -7.957  1.00 23.07           C  
ANISOU 2357  CG1 ILE A 293     2669   3112   2984    408    537    733       C  
ATOM   2358  CG2 ILE A 293      -4.033  23.309 -10.500  1.00 22.79           C  
ANISOU 2358  CG2 ILE A 293     2497   3159   3003    456    425    753       C  
ATOM   2359  CD1 ILE A 293      -5.494  23.162  -7.481  1.00 24.23           C  
ANISOU 2359  CD1 ILE A 293     2787   3240   3178    357    631    702       C  
ATOM   2360  N   ALA A 294      -1.448  25.506 -11.219  1.00 22.16           N  
ANISOU 2360  N   ALA A 294     2445   3096   2880    526    366    770       N  
ATOM   2361  CA  ALA A 294      -1.020  26.277 -12.399  1.00 22.07           C  
ANISOU 2361  CA  ALA A 294     2419   3100   2865    536    346    778       C  
ATOM   2362  C   ALA A 294      -1.447  25.545 -13.672  1.00 22.05           C  
ANISOU 2362  C   ALA A 294     2402   3119   2858    523    306    787       C  
ATOM   2363  O   ALA A 294      -1.505  26.210 -14.728  1.00 22.25           O  
ANISOU 2363  O   ALA A 294     2438   3146   2871    526    285    802       O  
ATOM   2364  CB  ALA A 294       0.470  26.481 -12.341  1.00 22.32           C  
ANISOU 2364  CB  ALA A 294     2478   3126   2876    534    348    746       C  
ATOM   2365  N   CYS A 295      -1.691  24.237 -13.599  1.00 21.36           N  
ANISOU 2365  N   CYS A 295     2308   3039   2769    506    294    776       N  
ATOM   2366  CA  CYS A 295      -1.929  23.437 -14.818  1.00 21.79           C  
ANISOU 2366  CA  CYS A 295     2352   3113   2813    490    255    776       C  
ATOM   2367  C   CYS A 295      -2.697  22.165 -14.462  1.00 21.69           C  
ANISOU 2367  C   CYS A 295     2321   3102   2818    471    253    767       C  
ATOM   2368  O   CYS A 295      -2.580  21.695 -13.337  1.00 20.91           O  
ANISOU 2368  O   CYS A 295     2249   2982   2715    463    283    757       O  
ATOM   2369  CB  CYS A 295      -0.607  23.132 -15.525  1.00 21.57           C  
ANISOU 2369  CB  CYS A 295     2356   3091   2751    474    249    749       C  
ATOM   2370  SG  CYS A 295       0.517  22.121 -14.528  1.00 21.48           S  
ANISOU 2370  SG  CYS A 295     2357   3061   2742    476    248    703       S  
ATOM   2371  N   LEU A 296      -3.394  21.601 -15.440  1.00 22.36           N  
ANISOU 2371  N   LEU A 296     2379   3204   2912    460    218    768       N  
ATOM   2372  CA  LEU A 296      -4.247  20.411 -15.256  1.00 23.63           C  
ANISOU 2372  CA  LEU A 296     2514   3366   3098    434    223    753       C  
ATOM   2373  C   LEU A 296      -4.577  19.783 -16.608  1.00 24.55           C  
ANISOU 2373  C   LEU A 296     2614   3505   3210    422    167    749       C  
ATOM   2374  O   LEU A 296      -4.664  20.528 -17.575  1.00 25.14           O  
ANISOU 2374  O   LEU A 296     2692   3587   3275    439    121    763       O  
ATOM   2375  CB  LEU A 296      -5.508  20.914 -14.552  1.00 24.81           C  
ANISOU 2375  CB  LEU A 296     2610   3504   3314    435    258    743       C  
ATOM   2376  CG  LEU A 296      -6.671  19.927 -14.419  1.00 25.15           C  
ANISOU 2376  CG  LEU A 296     2604   3543   3408    398    282    709       C  
ATOM   2377  CD1 LEU A 296      -7.561  20.314 -13.267  1.00 25.68           C  
ANISOU 2377  CD1 LEU A 296     2638   3584   3536    379    364    678       C  
ATOM   2378  CD2 LEU A 296      -7.491  19.889 -15.685  1.00 25.82           C  
ANISOU 2378  CD2 LEU A 296     2620   3650   3540    411    207    696       C  
ATOM   2379  N   GLN A 297      -4.787  18.466 -16.663  1.00 25.92           N  
ANISOU 2379  N   GLN A 297     2785   3680   3384    392    168    730       N  
ATOM   2380  CA  GLN A 297      -5.452  17.798 -17.813  1.00 27.70           C  
ANISOU 2380  CA  GLN A 297     2981   3924   3619    377    117    719       C  
ATOM   2381  C   GLN A 297      -6.496  16.823 -17.271  1.00 28.64           C  
ANISOU 2381  C   GLN A 297     3057   4036   3791    344    149    689       C  
ATOM   2382  O   GLN A 297      -6.243  16.219 -16.222  1.00 29.03           O  
ANISOU 2382  O   GLN A 297     3144   4059   3826    321    208    683       O  
ATOM   2383  CB  GLN A 297      -4.433  17.087 -18.695  1.00 28.75           C  
ANISOU 2383  CB  GLN A 297     3164   4067   3693    360     95    714       C  
ATOM   2384  CG  GLN A 297      -5.047  16.483 -19.950  1.00 30.33           C  
ANISOU 2384  CG  GLN A 297     3351   4283   3888    342     39    703       C  
ATOM   2385  CD  GLN A 297      -4.025  15.772 -20.821  1.00 31.29           C  
ANISOU 2385  CD  GLN A 297     3525   4410   3952    316     35    688       C  
ATOM   2386  NE2 GLN A 297      -4.529  14.826 -21.592  1.00 33.06           N  
ANISOU 2386  NE2 GLN A 297     3743   4645   4175    290      1    671       N  
ATOM   2387  OE1 GLN A 297      -2.814  16.028 -20.810  1.00 30.49           O  
ANISOU 2387  OE1 GLN A 297     3462   4302   3819    315     65    679       O  
ATOM   2388  N   TYR A 298      -7.634  16.682 -17.943  1.00 29.16           N  
ANISOU 2388  N   TYR A 298     3053   4113   3914    339    108    664       N  
ATOM   2389  CA  TYR A 298      -8.716  15.743 -17.550  1.00 30.66           C  
ANISOU 2389  CA  TYR A 298     3185   4294   4170    296    149    615       C  
ATOM   2390  C   TYR A 298      -8.965  14.790 -18.714  1.00 33.16           C  
ANISOU 2390  C   TYR A 298     3488   4630   4483    278     86    598       C  
ATOM   2391  O   TYR A 298      -9.088  15.289 -19.847  1.00 34.54           O  
ANISOU 2391  O   TYR A 298     3652   4821   4651    310     -8    606       O  
ATOM   2392  CB  TYR A 298      -9.967  16.536 -17.163  1.00 30.66           C  
ANISOU 2392  CB  TYR A 298     3083   4285   4280    307    163    573       C  
ATOM   2393  CG  TYR A 298     -11.277  15.790 -17.190  1.00 29.89           C  
ANISOU 2393  CG  TYR A 298     2888   4183   4286    265    185    497       C  
ATOM   2394  CD1 TYR A 298     -11.394  14.549 -16.600  1.00 29.64           C  
ANISOU 2394  CD1 TYR A 298     2886   4132   4243    194    275    471       C  
ATOM   2395  CD2 TYR A 298     -12.398  16.329 -17.800  1.00 30.40           C  
ANISOU 2395  CD2 TYR A 298     2832   4252   4466    297    110    442       C  
ATOM   2396  CE1 TYR A 298     -12.591  13.857 -16.597  1.00 30.29           C  
ANISOU 2396  CE1 TYR A 298     2876   4205   4426    142    315    388       C  
ATOM   2397  CE2 TYR A 298     -13.607  15.652 -17.799  1.00 31.23           C  
ANISOU 2397  CE2 TYR A 298     2825   4350   4690    256    134    350       C  
ATOM   2398  CZ  TYR A 298     -13.699  14.413 -17.197  1.00 30.82           C  
ANISOU 2398  CZ  TYR A 298     2800   4285   4625    172    248    321       C  
ATOM   2399  OH  TYR A 298     -14.869  13.735 -17.213  1.00 31.87           O  
ANISOU 2399  OH  TYR A 298     2823   4408   4879    119    286    220       O  
ATOM   2400  N   ARG A 299      -9.011  13.485 -18.444  1.00 36.29           N  
ANISOU 2400  N   ARG A 299     3904   5015   4871    228    132    576       N  
ATOM   2401  CA  ARG A 299      -9.395  12.452 -19.436  1.00 40.39           C  
ANISOU 2401  CA  ARG A 299     4401   5549   5398    201     85    548       C  
ATOM   2402  C   ARG A 299      -9.940  11.208 -18.724  1.00 40.61           C  
ANISOU 2402  C   ARG A 299     4426   5549   5455    135    168    506       C  
ATOM   2403  O   ARG A 299      -9.232  10.679 -17.860  1.00 40.42           O  
ANISOU 2403  O   ARG A 299     4493   5490   5373    114    230    527       O  
ATOM   2404  CB  ARG A 299      -8.201  12.075 -20.311  1.00 45.47           C  
ANISOU 2404  CB  ARG A 299     5124   6205   5948    210     38    580       C  
ATOM   2405  CG  ARG A 299      -8.613  11.375 -21.602  1.00 52.08           C  
ANISOU 2405  CG  ARG A 299     5943   7061   6783    192    -32    556       C  
ATOM   2406  CD  ARG A 299      -7.662  10.249 -22.010  1.00 58.45           C  
ANISOU 2406  CD  ARG A 299     6818   7865   7524    165    -21    556       C  
ATOM   2407  NE  ARG A 299      -6.679  10.716 -22.975  1.00 63.99           N  
ANISOU 2407  NE  ARG A 299     7580   8580   8153    181    -61    577       N  
ATOM   2408  CZ  ARG A 299      -5.486  10.158 -23.203  1.00 71.54           C  
ANISOU 2408  CZ  ARG A 299     8594   9530   9060    169    -36    571       C  
ATOM   2409  NH1 ARG A 299      -5.073   9.109 -22.494  1.00 70.43           N1+
ANISOU 2409  NH1 ARG A 299     8467   9364   8930    155      5    554       N1+
ATOM   2410  NH2 ARG A 299      -4.706  10.683 -24.143  1.00 73.62           N  
ANISOU 2410  NH2 ARG A 299     8908   9801   9264    168    -53    574       N  
ATOM   2411  N   ASP A 300     -11.144  10.763 -19.095  1.00 41.03           N  
ANISOU 2411  N   ASP A 300     4387   5607   5596    103    162    444       N  
ATOM   2412  CA  ASP A 300     -11.781   9.519 -18.579  1.00 40.91           C  
ANISOU 2412  CA  ASP A 300     4368   5562   5615     24    251    390       C  
ATOM   2413  C   ASP A 300     -12.179   9.745 -17.115  1.00 27.72           C  
ATOM   2414  O   ASP A 300     -13.147  10.544 -16.884  1.00 37.40           O  
ANISOU 2414  O   ASP A 300     3826   5075   5308    -18    408    312       O  
ATOM   2415  CB  ASP A 300     -10.888   8.300 -18.853  1.00 41.66           C  
ANISOU 2415  CB  ASP A 300     4568   5644   5618      2    245    420       C  
ATOM   2416  CG  ASP A 300     -10.790   8.064 -20.351  1.00 44.95           C  
ANISOU 2416  CG  ASP A 300     4953   6102   6022     26    134    418       C  
ATOM   2417  OD1 ASP A 300     -11.847   8.219 -21.012  1.00 46.96           O  
ANISOU 2417  OD1 ASP A 300     5104   6379   6360     24     83    367       O  
ATOM   2418  OD2 ASP A 300      -9.663   7.768 -20.873  1.00 47.54           O1-
ANISOU 2418  OD2 ASP A 300     5361   6437   6265     46     95    458       O1-
ATOM   2419  N   ARG A 301     -11.478   9.073 -16.189  1.00 35.19           N  
ANISOU 2419  N   ARG A 301     3799   4742   4831    -57    459    400       N  
ATOM   2420  CA  ARG A 301     -11.707   9.225 -14.738  1.00 33.79           C  
ANISOU 2420  CA  ARG A 301     3691   4504   4643   -109    589    387       C  
ATOM   2421  C   ARG A 301     -10.586  10.066 -14.140  1.00 31.66           C  
ANISOU 2421  C   ARG A 301     3515   4226   4289    -50    562    459       C  
ATOM   2422  O   ARG A 301     -10.703  10.430 -12.968  1.00 31.53           O  
ANISOU 2422  O   ARG A 301     3562   4163   4255    -81    654    455       O  
ATOM   2423  CB  ARG A 301     -11.840   7.863 -14.059  1.00 34.70           C  
ANISOU 2423  CB  ARG A 301     3929   4547   4709   -202    687    366       C  
ATOM   2424  CG  ARG A 301     -13.257   7.307 -14.141  1.00 36.54           C  
ANISOU 2424  CG  ARG A 301     4060   4770   5054   -291    782    264       C  
ATOM   2425  CD  ARG A 301     -13.500   6.013 -13.354  1.00 37.19           C  
ANISOU 2425  CD  ARG A 301     4284   4764   5083   -405    911    235       C  
ATOM   2426  NE  ARG A 301     -13.512   6.244 -11.916  1.00 37.17           N  
ANISOU 2426  NE  ARG A 301     4422   4681   5020   -467   1044    237       N  
ATOM   2427  CZ  ARG A 301     -14.145   5.493 -11.022  1.00 37.69           C  
ANISOU 2427  CZ  ARG A 301     4598   4657   5066   -594   1209    181       C  
ATOM   2428  NH1 ARG A 301     -14.111   5.794  -9.740  1.00 38.21           N1+
ANISOU 2428  NH1 ARG A 301     4815   4644   5060   -652   1327    186       N1+
ATOM   2429  NH2 ARG A 301     -14.818   4.429 -11.398  1.00 38.77           N  
ANISOU 2429  NH2 ARG A 301     4710   4774   5247   -674   1266    117       N  
ATOM   2430  N   LEU A 302      -9.570  10.400 -14.926  1.00 29.54           N  
ANISOU 2430  N   LEU A 302     3251   3998   3975     26    449    512       N  
ATOM   2431  CA  LEU A 302      -8.282  10.852 -14.368  1.00 27.88           C  
ANISOU 2431  CA  LEU A 302     3143   3769   3681     74    420    568       C  
ATOM   2432  C   LEU A 302      -8.129  12.338 -14.579  1.00 27.45           C  
ANISOU 2432  C   LEU A 302     3018   3757   3653    134    384    588       C  
ATOM   2433  O   LEU A 302      -8.229  12.788 -15.712  1.00 27.77           O  
ANISOU 2433  O   LEU A 302     2977   3849   3726    171    312    590       O  
ATOM   2434  CB  LEU A 302      -7.138  10.117 -15.038  1.00 27.17           C  
ANISOU 2434  CB  LEU A 302     3109   3683   3532    106    337    593       C  
ATOM   2435  CG  LEU A 302      -5.774  10.483 -14.480  1.00 26.93           C  
ANISOU 2435  CG  LEU A 302     3166   3627   3439    158    298    626       C  
ATOM   2436  CD1 LEU A 302      -5.635   9.916 -13.081  1.00 27.37           C  
ANISOU 2436  CD1 LEU A 302     3367   3594   3438    127    345    631       C  
ATOM   2437  CD2 LEU A 302      -4.659  10.011 -15.408  1.00 26.39           C  
ANISOU 2437  CD2 LEU A 302     3100   3575   3350    196    216    625       C  
ATOM   2438  N   VAL A 303      -7.899  13.043 -13.480  1.00 27.59           N  
ANISOU 2438  N   VAL A 303     3090   3744   3649    140    434    603       N  
ATOM   2439  CA  VAL A 303      -7.426  14.449 -13.459  1.00 26.29           C  
ANISOU 2439  CA  VAL A 303     2896   3606   3487    199    403    631       C  
ATOM   2440  C   VAL A 303      -5.994  14.395 -12.970  1.00 25.65           C  
ANISOU 2440  C   VAL A 303     2926   3497   3322    231    368    666       C  
ATOM   2441  O   VAL A 303      -5.749  13.751 -11.929  1.00 26.01           O  
ANISOU 2441  O   VAL A 303     3087   3481   3315    203    403    666       O  
ATOM   2442  CB  VAL A 303      -8.278  15.322 -12.535  1.00 26.63           C  
ANISOU 2442  CB  VAL A 303     2906   3630   3581    180    488    607       C  
ATOM   2443  CG1 VAL A 303      -7.747  16.735 -12.458  1.00 26.77           C  
ANISOU 2443  CG1 VAL A 303     2907   3668   3598    240    457    637       C  
ATOM   2444  CG2 VAL A 303      -9.710  15.345 -12.991  1.00 27.13           C  
ANISOU 2444  CG2 VAL A 303     2837   3713   3759    152    515    546       C  
ATOM   2445  N   VAL A 304      -5.110  15.025 -13.724  1.00 25.04           N  
ANISOU 2445  N   VAL A 304     2820   3457   3235    284    300    684       N  
ATOM   2446  CA  VAL A 304      -3.692  15.241 -13.351  1.00 24.33           C  
ANISOU 2446  CA  VAL A 304     2798   3348   3098    324    262    696       C  
ATOM   2447  C   VAL A 304      -3.496  16.740 -13.241  1.00 23.58           C  
ANISOU 2447  C   VAL A 304     2667   3274   3017    358    268    711       C  
ATOM   2448  O   VAL A 304      -3.970  17.477 -14.139  1.00 23.73           O  
ANISOU 2448  O   VAL A 304     2610   3335   3070    369    257    718       O  
ATOM   2449  CB  VAL A 304      -2.750  14.647 -14.402  1.00 24.63           C  
ANISOU 2449  CB  VAL A 304     2827   3406   3127    342    198    682       C  
ATOM   2450  CG1 VAL A 304      -1.373  15.287 -14.348  1.00 25.07           C  
ANISOU 2450  CG1 VAL A 304     2894   3458   3172    384    165    671       C  
ATOM   2451  CG2 VAL A 304      -2.661  13.148 -14.254  1.00 24.75           C  
ANISOU 2451  CG2 VAL A 304     2902   3381   3122    318    183    666       C  
ATOM   2452  N   SER A 305      -2.802  17.166 -12.192  1.00 22.28           N  
ANISOU 2452  N   SER A 305     2567   3075   2824    376    275    715       N  
ATOM   2453  CA  SER A 305      -2.695  18.599 -11.831  1.00 21.09           C  
ANISOU 2453  CA  SER A 305     2394   2934   2686    402    296    727       C  
ATOM   2454  C   SER A 305      -1.282  18.875 -11.349  1.00 20.10           C  
ANISOU 2454  C   SER A 305     2320   2785   2532    437    256    716       C  
ATOM   2455  O   SER A 305      -0.680  17.957 -10.737  1.00 19.66           O  
ANISOU 2455  O   SER A 305     2344   2682   2444    440    219    700       O  
ATOM   2456  CB  SER A 305      -3.723  18.963 -10.777  1.00 21.22           C  
ANISOU 2456  CB  SER A 305     2426   2924   2714    372    373    728       C  
ATOM   2457  OG  SER A 305      -3.495  18.235  -9.582  1.00 21.14           O  
ANISOU 2457  OG  SER A 305     2537   2848   2645    346    394    723       O  
ATOM   2458  N   GLY A 306      -0.809  20.096 -11.614  1.00 19.44           N  
ANISOU 2458  N   GLY A 306     2196   2725   2464    463    257    718       N  
ATOM   2459  CA  GLY A 306       0.499  20.601 -11.158  1.00 18.92           C  
ANISOU 2459  CA  GLY A 306     2156   2641   2393    495    227    692       C  
ATOM   2460  C   GLY A 306       0.330  21.871 -10.367  1.00 18.48           C  
ANISOU 2460  C   GLY A 306     2107   2577   2337    505    267    707       C  
ATOM   2461  O   GLY A 306      -0.450  22.744 -10.807  1.00 18.07           O  
ANISOU 2461  O   GLY A 306     2004   2553   2307    500    306    731       O  
ATOM   2462  N   SER A 307       1.030  21.983  -9.247  1.00 18.65           N  
ANISOU 2462  N   SER A 307     2195   2555   2337    523    245    689       N  
ATOM   2463  CA  SER A 307       0.795  23.081  -8.280  1.00 19.26           C  
ANISOU 2463  CA  SER A 307     2299   2614   2403    526    287    701       C  
ATOM   2464  C   SER A 307       2.060  23.896  -8.011  1.00 19.14           C  
ANISOU 2464  C   SER A 307     2280   2590   2401    560    252    666       C  
ATOM   2465  O   SER A 307       3.163  23.422  -8.278  1.00 18.68           O  
ANISOU 2465  O   SER A 307     2212   2523   2361    582    187    619       O  
ATOM   2466  CB  SER A 307       0.210  22.539  -7.005  1.00 19.70           C  
ANISOU 2466  CB  SER A 307     2464   2613   2408    499    311    712       C  
ATOM   2467  OG  SER A 307       0.162  23.529  -5.984  1.00 19.78           O  
ANISOU 2467  OG  SER A 307     2519   2598   2400    499    350    714       O  
ATOM   2468  N   SER A 308       1.829  25.095  -7.485  1.00 19.38           N  
ANISOU 2468  N   SER A 308     2311   2620   2434    561    300    679       N  
ATOM   2469  CA  SER A 308       2.803  26.002  -6.842  1.00 19.74           C  
ANISOU 2469  CA  SER A 308     2370   2645   2485    586    281    646       C  
ATOM   2470  C   SER A 308       3.443  25.309  -5.630  1.00 20.35           C  
ANISOU 2470  C   SER A 308     2555   2657   2520    604    205    617       C  
ATOM   2471  O   SER A 308       4.406  25.820  -5.091  1.00 20.68           O  
ANISOU 2471  O   SER A 308     2610   2675   2573    632    158    573       O  
ATOM   2472  CB  SER A 308       2.096  27.282  -6.495  1.00 19.79           C  
ANISOU 2472  CB  SER A 308     2365   2659   2495    577    357    675       C  
ATOM   2473  OG  SER A 308       2.788  28.004  -5.503  1.00 20.67           O  
ANISOU 2473  OG  SER A 308     2521   2738   2595    592    345    648       O  
ATOM   2474  N   ASP A 309       2.916  24.170  -5.212  1.00 21.10           N  
ANISOU 2474  N   ASP A 309     2736   2716   2566    587    187    636       N  
ATOM   2475  CA  ASP A 309       3.454  23.393  -4.071  1.00 22.21           C  
ANISOU 2475  CA  ASP A 309     3021   2772   2644    603     98    616       C  
ATOM   2476  C   ASP A 309       4.569  22.467  -4.573  1.00 15.24           C  
ATOM   2477  O   ASP A 309       5.090  21.704  -3.769  1.00 23.63           O  
ANISOU 2477  O   ASP A 309     3296   2857   2824    676   -130    538       O  
ATOM   2478  CB  ASP A 309       2.327  22.662  -3.323  1.00 22.67           C  
ANISOU 2478  CB  ASP A 309     3212   2781   2619    550    152    659       C  
ATOM   2479  CG  ASP A 309       1.579  21.581  -4.103  1.00 22.60           C  
ANISOU 2479  CG  ASP A 309     3176   2793   2618    518    182    680       C  
ATOM   2480  OD1 ASP A 309       2.163  21.003  -5.065  1.00 22.37           O  
ANISOU 2480  OD1 ASP A 309     3070   2794   2636    547    118    659       O  
ATOM   2481  OD2 ASP A 309       0.397  21.321  -3.734  1.00 22.83           O1-
ANISOU 2481  OD2 ASP A 309     3258   2806   2610    457    278    707       O1-
ATOM   2482  N   ASN A 310       4.878  22.498  -5.868  1.00 22.41           N  
ANISOU 2482  N   ASN A 310     2883   2847   2785    652     -7    538       N  
ATOM   2483  CA  ASN A 310       5.975  21.722  -6.516  1.00 22.45           C  
ANISOU 2483  CA  ASN A 310     2829   2845   2855    688    -97    465       C  
ATOM   2484  C   ASN A 310       5.568  20.273  -6.754  1.00 22.39           C  
ANISOU 2484  C   ASN A 310     2874   2813   2819    680   -133    483       C  
ATOM   2485  O   ASN A 310       6.418  19.528  -7.290  1.00 22.81           O  
ANISOU 2485  O   ASN A 310     2880   2855   2931    710   -208    418       O  
ATOM   2486  CB  ASN A 310       7.283  21.737  -5.721  1.00 22.82           C  
ANISOU 2486  CB  ASN A 310     2905   2828   2939    747   -225    380       C  
ATOM   2487  CG  ASN A 310       7.901  23.107  -5.667  1.00 22.50           C  
ANISOU 2487  CG  ASN A 310     2785   2814   2949    754   -191    337       C  
ATOM   2488  ND2 ASN A 310       9.159  23.156  -5.286  1.00 23.17           N  
ANISOU 2488  ND2 ASN A 310     2843   2856   3105    805   -299    235       N  
ATOM   2489  OD1 ASN A 310       7.254  24.098  -6.014  1.00 22.23           O  
ANISOU 2489  OD1 ASN A 310     2711   2834   2902    715    -74    388       O  
ATOM   2490  N   THR A 311       4.350  19.879  -6.390  1.00 22.22           N  
ANISOU 2490  N   THR A 311     2940   2781   2723    637    -75    555       N  
ATOM   2491  CA  THR A 311       3.851  18.500  -6.621  1.00 22.75           C  
ANISOU 2491  CA  THR A 311     3063   2823   2759    616    -92    574       C  
ATOM   2492  C   THR A 311       2.994  18.442  -7.880  1.00 22.06           C  
ANISOU 2492  C   THR A 311     2864   2817   2702    574      0    603       C  
ATOM   2493  O   THR A 311       2.431  19.479  -8.267  1.00 21.51           O  
ANISOU 2493  O   THR A 311     2719   2805   2650    554     83    629       O  
ATOM   2494  CB  THR A 311       3.032  17.964  -5.447  1.00 23.57           C  
ANISOU 2494  CB  THR A 311     3346   2850   2761    580    -74    620       C  
ATOM   2495  CG2 THR A 311       3.806  18.098  -4.164  1.00 24.76           C  
ANISOU 2495  CG2 THR A 311     3640   2908   2859    619   -174    598       C  
ATOM   2496  OG1 THR A 311       1.776  18.644  -5.324  1.00 23.57           O  
ANISOU 2496  OG1 THR A 311     3329   2886   2738    519     64    667       O  
ATOM   2497  N   ILE A 312       2.907  17.241  -8.448  1.00 22.38           N  
ANISOU 2497  N   ILE A 312     2908   2849   2746    566    -29    596       N  
ATOM   2498  CA  ILE A 312       1.831  16.785  -9.368  1.00 22.48           C  
ANISOU 2498  CA  ILE A 312     2867   2912   2761    517     43    629       C  
ATOM   2499  C   ILE A 312       0.950  15.799  -8.601  1.00 23.13           C  
ANISOU 2499  C   ILE A 312     3075   2934   2779    476     64    660       C  
ATOM   2500  O   ILE A 312       1.502  14.972  -7.876  1.00 23.32           O  
ANISOU 2500  O   ILE A 312     3222   2875   2762    495    -15    645       O  
ATOM   2501  CB  ILE A 312       2.433  16.124 -10.613  1.00 22.73           C  
ANISOU 2501  CB  ILE A 312     2817   2976   2844    529      5    589       C  
ATOM   2502  CG1 ILE A 312       3.237  17.129 -11.445  1.00 22.59           C  
ANISOU 2502  CG1 ILE A 312     2690   3012   2882    545     17    551       C  
ATOM   2503  CG2 ILE A 312       1.365  15.407 -11.432  1.00 22.52           C  
ANISOU 2503  CG2 ILE A 312     2764   2984   2810    482     53    618       C  
ATOM   2504  CD1 ILE A 312       4.269  16.474 -12.352  1.00 22.86           C  
ANISOU 2504  CD1 ILE A 312     2665   3050   2973    559    -25    477       C  
ATOM   2505  N   ARG A 313      -0.368  15.882  -8.776  1.00 23.47           N  
ANISOU 2505  N   ARG A 313     3090   3008   2820    420    163    691       N  
ATOM   2506  CA  ARG A 313      -1.334  14.932  -8.179  1.00 23.96           C  
ANISOU 2506  CA  ARG A 313     3256   3015   2831    357    217    705       C  
ATOM   2507  C   ARG A 313      -2.146  14.279  -9.298  1.00 23.54           C  
ANISOU 2507  C   ARG A 313     3108   3014   2823    322    253    702       C  
ATOM   2508  O   ARG A 313      -2.441  14.928 -10.323  1.00 23.42           O  
ANISOU 2508  O   ARG A 313     2952   3078   2867    332    267    702       O  
ATOM   2509  CB  ARG A 313      -2.203  15.667  -7.165  1.00 25.07           C  
ANISOU 2509  CB  ARG A 313     3449   3132   2943    310    320    719       C  
ATOM   2510  CG  ARG A 313      -1.584  15.727  -5.781  1.00 26.52           C  
ANISOU 2510  CG  ARG A 313     3813   3222   3041    319    285    723       C  
ATOM   2511  CD  ARG A 313      -2.309  16.686  -4.850  1.00 27.65           C  
ANISOU 2511  CD  ARG A 313     3994   3351   3162    274    395    729       C  
ATOM   2512  NE  ARG A 313      -1.991  16.496  -3.432  1.00 29.55           N  
ANISOU 2512  NE  ARG A 313     4458   3480   3289    253    383    734       N  
ATOM   2513  CZ  ARG A 313      -2.851  16.088  -2.479  1.00 30.52           C  
ANISOU 2513  CZ  ARG A 313     4741   3522   3332    160    493    733       C  
ATOM   2514  NH1 ARG A 313      -4.095  15.779  -2.769  1.00 30.70           N1+
ANISOU 2514  NH1 ARG A 313     4704   3566   3394     79    630    717       N1+
ATOM   2515  NH2 ARG A 313      -2.463  15.954  -1.223  1.00 31.33           N  
ANISOU 2515  NH2 ARG A 313     5079   3513   3313    142    467    741       N  
ATOM   2516  N   LEU A 314      -2.431  13.001  -9.119  1.00 23.97           N  
ANISOU 2516  N   LEU A 314     3252   3014   2841    284    254    698       N  
ATOM   2517  CA  LEU A 314      -3.373  12.207  -9.941  1.00 24.22           C  
ANISOU 2517  CA  LEU A 314     3220   3076   2905    234    300    689       C  
ATOM   2518  C   LEU A 314      -4.635  12.006  -9.115  1.00 25.51           C  
ANISOU 2518  C   LEU A 314     3447   3196   3049    148    423    683       C  
ATOM   2519  O   LEU A 314      -4.532  11.558  -7.949  1.00 26.87           O  
ANISOU 2519  O   LEU A 314     3799   3272   3138    114    445    690       O  
ATOM   2520  CB  LEU A 314      -2.748  10.854 -10.254  1.00 24.32           C  
ANISOU 2520  CB  LEU A 314     3299   3046   2893    245    224    678       C  
ATOM   2521  CG  LEU A 314      -1.688  10.880 -11.354  1.00 23.70           C  
ANISOU 2521  CG  LEU A 314     3122   3019   2861    310    132    658       C  
ATOM   2522  CD1 LEU A 314      -0.529  11.769 -10.971  1.00 23.49           C  
ANISOU 2522  CD1 LEU A 314     3097   2988   2840    375     70    649       C  
ATOM   2523  CD2 LEU A 314      -1.170   9.497 -11.640  1.00 23.89           C  
ANISOU 2523  CD2 LEU A 314     3205   2996   2876    318     65    635       C  
ATOM   2524  N   TRP A 315      -5.790  12.334  -9.674  1.00 25.50           N  
ANISOU 2524  N   TRP A 315     3312   3252   3124    110    499    662       N  
ATOM   2525  CA  TRP A 315      -7.066  12.193  -8.943  1.00 26.13           C  
ANISOU 2525  CA  TRP A 315     3419   3293   3217     17    638    629       C  
ATOM   2526  C   TRP A 315      -8.014  11.292  -9.730  1.00 26.37           C  
ANISOU 2526  C   TRP A 315     3366   3344   3308    -36    676    589       C  
ATOM   2527  O   TRP A 315      -7.926  11.264 -10.967  1.00 26.11           O  
ANISOU 2527  O   TRP A 315     3208   3383   3329      9    597    590       O  
ATOM   2528  CB  TRP A 315      -7.706  13.547  -8.733  1.00 26.27           C  
ANISOU 2528  CB  TRP A 315     3329   3350   3303     21    702    611       C  
ATOM   2529  CG  TRP A 315      -6.815  14.663  -8.293  1.00 25.83           C  
ANISOU 2529  CG  TRP A 315     3300   3299   3214     86    654    646       C  
ATOM   2530  CD1 TRP A 315      -5.936  15.370  -9.057  1.00 24.85           C  
ANISOU 2530  CD1 TRP A 315     3099   3235   3109    171    550    674       C  
ATOM   2531  CD2 TRP A 315      -6.858  15.318  -7.010  1.00 26.13           C  
ANISOU 2531  CD2 TRP A 315     3438   3284   3208     59    729    644       C  
ATOM   2532  CE2 TRP A 315      -5.958  16.396  -7.073  1.00 25.34           C  
ANISOU 2532  CE2 TRP A 315     3306   3217   3105    139    652    674       C  
ATOM   2533  CE3 TRP A 315      -7.562  15.091  -5.821  1.00 27.11           C  
ANISOU 2533  CE3 TRP A 315     3686   3326   3287    -35    863    615       C  
ATOM   2534  NE1 TRP A 315      -5.390  16.386  -8.321  1.00 24.65           N  
ANISOU 2534  NE1 TRP A 315     3114   3196   3056    202    549    689       N  
ATOM   2535  CZ2 TRP A 315      -5.728  17.220  -5.977  1.00 25.61           C  
ANISOU 2535  CZ2 TRP A 315     3423   3210   3095    136    691    679       C  
ATOM   2536  CZ3 TRP A 315      -7.357  15.923  -4.749  1.00 27.18           C  
ANISOU 2536  CZ3 TRP A 315     3787   3294   3246    -42    908    620       C  
ATOM   2537  CH2 TRP A 315      -6.444  16.967  -4.824  1.00 26.56           C  
ANISOU 2537  CH2 TRP A 315     3670   3254   3168     47    816    654       C  
ATOM   2538  N   ASP A 316      -8.910  10.631  -9.024  1.00 26.79           N  
ANISOU 2538  N   ASP A 316     3494   3334   3352   -137    801    549       N  
ATOM   2539  CA  ASP A 316     -10.119  10.029  -9.602  1.00 27.54           C  
ANISOU 2539  CA  ASP A 316     3477   3449   3538   -206    875    484       C  
ATOM   2540  C   ASP A 316     -11.249  11.048  -9.484  1.00 15.87           C  
ATOM   2541  O   ASP A 316     -11.535  11.442  -8.361  1.00 28.86           O  
ANISOU 2541  O   ASP A 316     3570   3595   3803   -288   1084    398       O  
ATOM   2542  CB  ASP A 316     -10.443   8.750  -8.850  1.00 28.79           C  
ANISOU 2542  CB  ASP A 316     3810   3505   3623   -313    976    462       C  
ATOM   2543  CG  ASP A 316     -11.715   8.126  -9.356  1.00 29.97           C  
ANISOU 2543  CG  ASP A 316     3841   3669   3878   -397   1070    379       C  
ATOM   2544  OD1 ASP A 316     -11.699   7.591 -10.470  1.00 30.32           O  
ANISOU 2544  OD1 ASP A 316     3787   3767   3966   -365    984    377       O  
ATOM   2545  OD2 ASP A 316     -12.707   8.216  -8.642  1.00 31.95           O1-
ANISOU 2545  OD2 ASP A 316     4091   3877   4171   -498   1232    306       O1-
ATOM   2546  N   ILE A 317     -11.876  11.454 -10.584  1.00 28.06           N  
ANISOU 2546  N   ILE A 317     3181   3628   3851   -193    915    383       N  
ATOM   2547  CA  ILE A 317     -12.897  12.547 -10.532  1.00 28.95           C  
ANISOU 2547  CA  ILE A 317     3129   3770   4102   -194    970    313       C  
ATOM   2548  C   ILE A 317     -14.149  12.038  -9.840  1.00 30.04           C  
ANISOU 2548  C   ILE A 317     3244   3852   4318   -319   1150    203       C  
ATOM   2549  O   ILE A 317     -14.942  12.894  -9.494  1.00 30.51           O  
ANISOU 2549  O   ILE A 317     3189   3913   4489   -334   1226    130       O  
ATOM   2550  CB  ILE A 317     -13.401  13.186 -11.855  1.00 29.49           C  
ANISOU 2550  CB  ILE A 317     2988   3918   4299   -116    850    286       C  
ATOM   2551  CG1 ILE A 317     -13.311  12.273 -13.065  1.00 29.96           C  
ANISOU 2551  CG1 ILE A 317     3014   4013   4356    -98    746    296       C  
ATOM   2552  CG2 ILE A 317     -12.841  14.571 -12.132  1.00 28.93           C  
ANISOU 2552  CG2 ILE A 317     2878   3888   4228    -13    752    340       C  
ATOM   2553  CD1 ILE A 317     -14.189  11.070 -12.907  1.00 31.73           C  
ANISOU 2553  CD1 ILE A 317     3228   4202   4627   -202    849    216       C  
ATOM   2554  N   GLU A 318     -14.376  10.732  -9.719  1.00 30.92           N  
ANISOU 2554  N   GLU A 318     3443   3916   4390   -408   1220    178       N  
ATOM   2555  CA  GLU A 318     -15.702  10.226  -9.260  1.00 32.87           C  
ANISOU 2555  CA  GLU A 318     3634   4114   4740   -541   1405     47       C  
ATOM   2556  C   GLU A 318     -15.753  10.305  -7.734  1.00 16.30           C  
ATOM   2557  O   GLU A 318     -16.734  10.816  -7.238  1.00 35.96           O  
ANISOU 2557  O   GLU A 318     4113   4389   5162   -715   1737    -79       O  
ATOM   2558  CB  GLU A 318     -16.024   8.835  -9.814  1.00 33.64           C  
ANISOU 2558  CB  GLU A 318     3742   4197   4842   -603   1415     15       C  
ATOM   2559  CG  GLU A 318     -16.047   8.743 -11.332  1.00 33.81           C  
ANISOU 2559  CG  GLU A 318     3591   4310   4945   -511   1238     21       C  
ATOM   2560  CD  GLU A 318     -17.039   9.636 -12.092  1.00 35.48           C  
ANISOU 2560  CD  GLU A 318     3536   4588   5358   -460   1182    -72       C  
ATOM   2561  OE1 GLU A 318     -17.859  10.292 -11.451  1.00 36.74           O  
ANISOU 2561  OE1 GLU A 318     3604   4726   5631   -503   1297   -166       O  
ATOM   2562  OE2 GLU A 318     -16.983   9.674 -13.357  1.00 37.23           O1-
ANISOU 2562  OE2 GLU A 318     3646   4875   5623   -375   1013    -55       O1-
ATOM   2563  N   CYS A 319     -14.723   9.878  -7.011  1.00 32.45           N  
ANISOU 2563  N   CYS A 319     4027   3896   4406   -652   1576    128       N  
ATOM   2564  CA  CYS A 319     -14.682   9.980  -5.534  1.00 33.15           C  
ANISOU 2564  CA  CYS A 319     4338   3877   4380   -749   1733    124       C  
ATOM   2565  C   CYS A 319     -13.782  11.134  -5.074  1.00 32.16           C  
ANISOU 2565  C   CYS A 319     4267   3767   4185   -654   1648    203       C  
ATOM   2566  O   CYS A 319     -13.742  11.432  -3.861  1.00 32.88           O  
ANISOU 2566  O   CYS A 319     4532   3776   4185   -723   1765    199       O  
ATOM   2567  CB  CYS A 319     -14.217   8.669  -4.936  1.00 34.12           C  
ANISOU 2567  CB  CYS A 319     4751   3887   4326   -829   1768    169       C  
ATOM   2568  SG  CYS A 319     -12.598   8.142  -5.524  1.00 34.96           S  
ANISOU 2568  SG  CYS A 319     4975   4010   4297   -685   1508    312       S  
ATOM   2569  N   GLY A 320     -13.053  11.767  -5.990  1.00 30.82           N  
ANISOU 2569  N   GLY A 320     3969   3693   4046   -508   1456    272       N  
ATOM   2570  CA  GLY A 320     -12.222  12.957  -5.699  1.00 29.46           C  
ANISOU 2570  CA  GLY A 320     3812   3547   3833   -413   1373    336       C  
ATOM   2571  C   GLY A 320     -10.956  12.620  -4.934  1.00 28.66           C  
ANISOU 2571  C   GLY A 320     3971   3375   3545   -391   1303    426       C  
ATOM   2572  O   GLY A 320     -10.294  13.549  -4.468  1.00 27.25           O  
ANISOU 2572  O   GLY A 320     3833   3199   3323   -333   1257    467       O  
ATOM   2573  N   ALA A 321     -10.626  11.329  -4.841  1.00 29.20           N  
ANISOU 2573  N   ALA A 321     4206   3377   3513   -430   1283    451       N  
ATOM   2574  CA  ALA A 321      -9.455  10.809  -4.100  1.00 29.48           C  
ANISOU 2574  CA  ALA A 321     4508   3320   3374   -406   1193    524       C  
ATOM   2575  C   ALA A 321      -8.191  11.080  -4.917  1.00 28.50           C  
ANISOU 2575  C   ALA A 321     4307   3266   3255   -258    980    589       C  
ATOM   2576  O   ALA A 321      -8.213  10.937  -6.130  1.00 28.22           O  
ANISOU 2576  O   ALA A 321     4093   3318   3310   -207    910    586       O  
ATOM   2577  CB  ALA A 321      -9.594   9.336  -3.824  1.00 30.22           C  
ANISOU 2577  CB  ALA A 321     4797   3311   3375   -492   1233    521       C  
ATOM   2578  N   CYS A 322      -7.121  11.465  -4.241  1.00 28.50           N  
ANISOU 2578  N   CYS A 322     4446   3223   3161   -197    886    637       N  
ATOM   2579  CA  CYS A 322      -5.790  11.582  -4.831  1.00 27.36           C  
ANISOU 2579  CA  CYS A 322     4261   3118   3015    -70    695    679       C  
ATOM   2580  C   CYS A 322      -5.167  10.200  -4.817  1.00 27.10           C  
ANISOU 2580  C   CYS A 322     4390   3004   2904    -63    600    696       C  
ATOM   2581  O   CYS A 322      -5.065   9.643  -3.721  1.00 26.96           O  
ANISOU 2581  O   CYS A 322     4624   2857   2761   -112    615    707       O  
ATOM   2582  CB  CYS A 322      -4.914  12.550  -4.066  1.00 27.85           C  
ANISOU 2582  CB  CYS A 322     4396   3159   3027    -10    630    703       C  
ATOM   2583  SG  CYS A 322      -3.283  12.650  -4.845  1.00 27.71           S  
ANISOU 2583  SG  CYS A 322     4301   3187   3039    133    413    724       S  
ATOM   2584  N   LEU A 323      -4.780   9.703  -5.999  1.00 26.26           N  
ANISOU 2584  N   LEU A 323     4152   2962   2865     -5    507    696       N  
ATOM   2585  CA  LEU A 323      -4.251   8.324  -6.185  1.00 26.49           C  
ANISOU 2585  CA  LEU A 323     4298   2922   2846      6    416    701       C  
ATOM   2586  C   LEU A 323      -2.737   8.333  -6.028  1.00 25.65           C  
ANISOU 2586  C   LEU A 323     4257   2778   2712    119    231    714       C  
ATOM   2587  O   LEU A 323      -2.161   7.316  -5.621  1.00 26.80           O  
ANISOU 2587  O   LEU A 323     4582   2814   2787    136    135    718       O  
ATOM   2588  CB  LEU A 323      -4.594   7.833  -7.587  1.00 26.08           C  
ANISOU 2588  CB  LEU A 323     4057   2961   2891     10    413    681       C  
ATOM   2589  CG  LEU A 323      -6.042   8.013  -7.996  1.00 26.56           C  
ANISOU 2589  CG  LEU A 323     3983   3083   3024    -76    564    649       C  
ATOM   2590  CD1 LEU A 323      -6.179   7.854  -9.504  1.00 26.03           C  
ANISOU 2590  CD1 LEU A 323     3710   3123   3058    -43    518    633       C  
ATOM   2591  CD2 LEU A 323      -6.917   7.034  -7.246  1.00 27.52           C  
ANISOU 2591  CD2 LEU A 323     4269   3103   3084   -196    689    628       C  
ATOM   2592  N   ARG A 324      -2.109   9.433  -6.434  1.00 23.84           N  
ANISOU 2592  N   ARG A 324     3873   2635   2551    195    178    710       N  
ATOM   2593  CA  ARG A 324      -0.639   9.549  -6.448  1.00 22.59           C  
ANISOU 2593  CA  ARG A 324     3719   2457   2406    303     10    696       C  
ATOM   2594  C   ARG A 324      -0.240  11.005  -6.323  1.00 21.78           C  
ANISOU 2594  C   ARG A 324     3514   2418   2342    347      9    694       C  
ATOM   2595  O   ARG A 324      -0.793  11.842  -7.038  1.00 20.59           O  
ANISOU 2595  O   ARG A 324     3190   2373   2259    331     95    697       O  
ATOM   2596  CB  ARG A 324      -0.076   8.965  -7.739  1.00 21.47           C  
ANISOU 2596  CB  ARG A 324     3433   2373   2351    352    -64    665       C  
ATOM   2597  CG  ARG A 324       1.434   9.058  -7.847  1.00 20.73           C  
ANISOU 2597  CG  ARG A 324     3309   2262   2305    456   -222    621       C  
ATOM   2598  CD  ARG A 324       2.170   8.222  -6.821  1.00 21.28           C  
ANISOU 2598  CD  ARG A 324     3596   2183   2307    501   -363    610       C  
ATOM   2599  NE  ARG A 324       2.215   6.824  -7.188  1.00 20.98           N  
ANISOU 2599  NE  ARG A 324     3620   2085   2266    500   -416    596       N  
ATOM   2600  CZ  ARG A 324       2.968   5.945  -6.592  1.00 21.47           C  
ANISOU 2600  CZ  ARG A 324     3849   2016   2294    557   -570    574       C  
ATOM   2601  NH1 ARG A 324       3.718   6.332  -5.582  1.00 22.00           N1+
ANISOU 2601  NH1 ARG A 324     4040   1997   2324    618   -691    563       N1+
ATOM   2602  NH2 ARG A 324       2.928   4.682  -6.967  1.00 21.74           N  
ANISOU 2602  NH2 ARG A 324     3938   1995   2326    551   -609    562       N  
ATOM   2603  N   VAL A 325       0.737  11.249  -5.472  1.00 22.55           N  
ANISOU 2603  N   VAL A 325     3724   2443   2400    406   -102    684       N  
ATOM   2604  CA  VAL A 325       1.513  12.512  -5.474  1.00 22.64           C  
ANISOU 2604  CA  VAL A 325     3627   2509   2466    469   -143    665       C  
ATOM   2605  C   VAL A 325       2.857  12.257  -6.168  1.00 22.82           C  
ANISOU 2605  C   VAL A 325     3551   2543   2577    560   -286    606       C  
ATOM   2606  O   VAL A 325       3.507  11.244  -5.891  1.00 23.37           O  
ANISOU 2606  O   VAL A 325     3729   2521   2631    602   -413    578       O  
ATOM   2607  CB  VAL A 325       1.671  13.014  -4.037  1.00 23.50           C  
ANISOU 2607  CB  VAL A 325     3918   2529   2483    468   -166    679       C  
ATOM   2608  CG1 VAL A 325       2.432  14.327  -4.002  1.00 23.66           C  
ANISOU 2608  CG1 VAL A 325     3826   2602   2561    527   -201    654       C  
ATOM   2609  CG2 VAL A 325       0.318  13.164  -3.378  1.00 23.61           C  
ANISOU 2609  CG2 VAL A 325     4030   2522   2417    362      1    719       C  
ATOM   2610  N   LEU A 326       3.239  13.131  -7.087  1.00 22.73           N  
ANISOU 2610  N   LEU A 326     3342   2636   2660    584   -260    578       N  
ATOM   2611  CA  LEU A 326       4.538  13.034  -7.790  1.00 23.01           C  
ANISOU 2611  CA  LEU A 326     3261   2686   2795    654   -362    499       C  
ATOM   2612  C   LEU A 326       5.425  14.179  -7.319  1.00 23.55           C  
ANISOU 2612  C   LEU A 326     3288   2757   2902    703   -407    458       C  
ATOM   2613  O   LEU A 326       5.117  15.344  -7.623  1.00 23.13           O  
ANISOU 2613  O   LEU A 326     3140   2783   2866    677   -308    479       O  
ATOM   2614  CB  LEU A 326       4.286  13.085  -9.298  1.00 22.12           C  
ANISOU 2614  CB  LEU A 326     2976   2679   2751    623   -279    489       C  
ATOM   2615  CG  LEU A 326       3.510  11.908  -9.887  1.00 22.02           C  
ANISOU 2615  CG  LEU A 326     2984   2667   2715    579   -247    514       C  
ATOM   2616  CD1 LEU A 326       3.348  12.058 -11.378  1.00 21.51           C  
ANISOU 2616  CD1 LEU A 326     2762   2702   2710    552   -180    500       C  
ATOM   2617  CD2 LEU A 326       4.175  10.581  -9.619  1.00 22.54           C  
ANISOU 2617  CD2 LEU A 326     3142   2638   2784    620   -369    473       C  
ATOM   2618  N   GLU A 327       6.531  13.839  -6.647  1.00 25.44           N  
ANISOU 2618  N   GLU A 327     3603   2905   3158    774   -560    399       N  
ATOM   2619  CA  GLU A 327       7.500  14.848  -6.140  1.00 27.34           C  
ANISOU 2619  CA  GLU A 327     3784   3144   3461    828   -623    334       C  
ATOM   2620  C   GLU A 327       8.833  14.696  -6.886  1.00 17.34           C  
ATOM   2621  O   GLU A 327       9.232  13.547  -7.160  1.00 27.53           O  
ANISOU 2621  O   GLU A 327     3609   3170   3681    894   -735    173       O  
ATOM   2622  CB  GLU A 327       7.695  14.690  -4.631  1.00 30.46           C  
ANISOU 2622  CB  GLU A 327     4378   3412   3783    877   -767    331       C  
ATOM   2623  CG  GLU A 327       6.404  14.415  -3.881  1.00 32.66           C  
ANISOU 2623  CG  GLU A 327     4833   3663   3914    811   -677    433       C  
ATOM   2624  CD  GLU A 327       6.571  14.218  -2.384  1.00 36.32           C  
ANISOU 2624  CD  GLU A 327     5571   3972   4255    832   -807    451       C  
ATOM   2625  OE1 GLU A 327       5.548  14.025  -1.698  1.00 40.38           O  
ANISOU 2625  OE1 GLU A 327     6250   4449   4643    754   -711    530       O  
ATOM   2626  OE2 GLU A 327       7.723  14.258  -1.909  1.00 39.29           O1-
ANISOU 2626  OE2 GLU A 327     6008   4258   4663    922  -1004    381       O1-
ATOM   2627  N   GLY A 328       9.483  15.823  -7.196  1.00 26.87           N  
ANISOU 2627  N   GLY A 328     3430   3146   3635    897   -674    145       N  
ATOM   2628  CA  GLY A 328      10.769  15.849  -7.902  1.00 27.13           C  
ANISOU 2628  CA  GLY A 328     3294   3189   3827    937   -720      1       C  
ATOM   2629  C   GLY A 328      11.061  17.199  -8.490  1.00 26.60           C  
ANISOU 2629  C   GLY A 328     3084   3206   3818    897   -595    -33       C  
ATOM   2630  O   GLY A 328      12.206  17.599  -8.467  1.00 27.37           O  
ANISOU 2630  O   GLY A 328     3078   3286   4035    934   -646   -160       O  
ATOM   2631  N   HIS A 329      10.065  17.876  -9.029  1.00 26.65           N  
ANISOU 2631  N   HIS A 329     3084   3294   3749    824   -438     67       N  
ATOM   2632  CA  HIS A 329      10.240  19.264  -9.519  1.00 27.69           C  
ANISOU 2632  CA  HIS A 329     3117   3492   3911    782   -318     52       C  
ATOM   2633  C   HIS A 329      10.695  20.095  -8.339  1.00 29.81           C  
ANISOU 2633  C   HIS A 329     3424   3720   4183    824   -382     30       C  
ATOM   2634  O   HIS A 329      10.099  19.935  -7.307  1.00 30.43           O  
ANISOU 2634  O   HIS A 329     3640   3755   4168    842   -436    106       O  
ATOM   2635  CB  HIS A 329       8.955  19.805 -10.115  1.00 26.63           C  
ANISOU 2635  CB  HIS A 329     3005   3430   3684    714   -178    174       C  
ATOM   2636  CG  HIS A 329       8.753  19.395 -11.528  1.00 26.36           C  
ANISOU 2636  CG  HIS A 329     2906   3446   3665    664    -99    169       C  
ATOM   2637  CD2 HIS A 329       7.703  18.829 -12.156  1.00 26.00           C  
ANISOU 2637  CD2 HIS A 329     2892   3432   3556    627    -54    250       C  
ATOM   2638  ND1 HIS A 329       9.721  19.617 -12.481  1.00 27.14           N  
ANISOU 2638  ND1 HIS A 329     2896   3563   3853    640    -50     61       N  
ATOM   2639  CE1 HIS A 329       9.277  19.197 -13.640  1.00 27.20           C  
ANISOU 2639  CE1 HIS A 329     2889   3609   3837    589     20     84       C  
ATOM   2640  NE2 HIS A 329       8.043  18.699 -13.470  1.00 26.09           N  
ANISOU 2640  NE2 HIS A 329     2829   3480   3606    586      8    200       N  
ATOM   2641  N   GLU A 330      11.728  20.910  -8.499  1.00 33.20           N  
ANISOU 2641  N   GLU A 330     3742   4157   4717    830   -370    -81       N  
ATOM   2642  CA  GLU A 330      12.275  21.747  -7.409  1.00 36.35           C  
ANISOU 2642  CA  GLU A 330     4162   4516   5133    870   -438   -120       C  
ATOM   2643  C   GLU A 330      11.576  23.113  -7.440  1.00 25.05           C  
ATOM   2644  O   GLU A 330      11.909  23.968  -6.618  1.00 34.32           O  
ANISOU 2644  O   GLU A 330     3933   4297   4812    833   -321    -53       O  
ATOM   2645  CB  GLU A 330      13.795  21.859  -7.545  1.00 42.76           C  
ANISOU 2645  CB  GLU A 330     4830   5298   6118    907   -506   -308       C  
ATOM   2646  CG  GLU A 330      14.554  20.552  -7.261  1.00 48.94           C  
ANISOU 2646  CG  GLU A 330     5607   5999   6988    989   -692   -411       C  
ATOM   2647  CD  GLU A 330      16.032  20.494  -7.707  1.00 56.85           C  
ANISOU 2647  CD  GLU A 330     6419   6977   8203   1018   -739   -630       C  
ATOM   2648  OE1 GLU A 330      16.332  20.705  -8.944  1.00 59.63           O  
ANISOU 2648  OE1 GLU A 330     6632   7388   8636    946   -583   -702       O  
ATOM   2649  OE2 GLU A 330      16.926  20.212  -6.832  1.00 62.09           O1-
ANISOU 2649  OE2 GLU A 330     7075   7554   8964   1112   -937   -746       O1-
ATOM   2650  N   GLU A 331      10.625  23.288  -8.357  1.00 31.77           N  
ANISOU 2650  N   GLU A 331     3589   4060   4424    751   -161     59       N  
ATOM   2651  CA  GLU A 331       9.903  24.582  -8.446  1.00 31.00           C  
ANISOU 2651  CA  GLU A 331     3504   4007   4267    706    -40    141       C  
ATOM   2652  C   GLU A 331       8.448  24.326  -8.846  1.00 22.67           C  
ATOM   2653  O   GLU A 331       8.063  23.149  -8.994  1.00 28.82           O  
ANISOU 2653  O   GLU A 331     3321   3758   3872    676    -15    294       O  
ATOM   2654  CB  GLU A 331      10.591  25.509  -9.450  1.00 32.62           C  
ANISOU 2654  CB  GLU A 331     3603   4248   4542    658     67     68       C  
ATOM   2655  CG  GLU A 331      11.566  26.478  -8.807  1.00 35.33           C  
ANISOU 2655  CG  GLU A 331     3902   4567   4956    674     53    -24       C  
ATOM   2656  CD  GLU A 331      10.930  27.741  -8.250  1.00 37.62           C  
ANISOU 2656  CD  GLU A 331     4248   4867   5177    660    115     60       C  
ATOM   2657  OE1 GLU A 331      11.643  28.515  -7.582  1.00 41.62           O  
ANISOU 2657  OE1 GLU A 331     4732   5351   5731    676     95     -7       O  
ATOM   2658  OE2 GLU A 331       9.723  27.947  -8.487  1.00 36.79           O1-
ANISOU 2658  OE2 GLU A 331     4204   4792   4983    636    177    182       O1-
ATOM   2659  N   LEU A 332       7.688  25.410  -9.009  1.00 28.34           N  
ANISOU 2659  N   LEU A 332     3235   3741   3791    638    122    342       N  
ATOM   2660  CA  LEU A 332       6.275  25.373  -9.417  1.00 27.47           C  
ANISOU 2660  CA  LEU A 332     3159   3664   3616    610    182    447       C  
ATOM   2661  C   LEU A 332       6.113  24.567 -10.709  1.00 26.15           C  
ANISOU 2661  C   LEU A 332     2954   3526   3455    583    198    447       C  
ATOM   2662  O   LEU A 332       6.876  24.747 -11.617  1.00 24.90           O  
ANISOU 2662  O   LEU A 332     2741   3381   3338    560    230    386       O  
ATOM   2663  CB  LEU A 332       5.792  26.810  -9.597  1.00 27.30           C  
ANISOU 2663  CB  LEU A 332     3128   3665   3581    589    266    491       C  
ATOM   2664  CG  LEU A 332       4.375  26.950 -10.140  1.00 27.39           C  
ANISOU 2664  CG  LEU A 332     3152   3704   3553    569    314    579       C  
ATOM   2665  CD1 LEU A 332       3.741  28.225  -9.654  1.00 26.64           C  
ANISOU 2665  CD1 LEU A 332     3070   3605   3446    572    363    621       C  
ATOM   2666  CD2 LEU A 332       4.359  26.903 -11.661  1.00 28.89           C  
ANISOU 2666  CD2 LEU A 332     3311   3923   3744    538    344    580       C  
ATOM   2667  N   VAL A 333       5.085  23.727 -10.774  1.00 26.42           N  
ANISOU 2667  N   VAL A 333     3023   3567   3447    576    188    508       N  
ATOM   2668  CA  VAL A 333       4.735  22.913 -11.970  1.00 26.12           C  
ANISOU 2668  CA  VAL A 333     2961   3558   3406    549    199    517       C  
ATOM   2669  C   VAL A 333       3.750  23.714 -12.833  1.00 26.23           C  
ANISOU 2669  C   VAL A 333     2967   3608   3391    520    262    581       C  
ATOM   2670  O   VAL A 333       2.585  23.864 -12.408  1.00 25.87           O  
ANISOU 2670  O   VAL A 333     2941   3566   3323    523    271    642       O  
ATOM   2671  CB  VAL A 333       4.182  21.547 -11.552  1.00 24.93           C  
ANISOU 2671  CB  VAL A 333     2856   3387   3231    557    148    540       C  
ATOM   2672  CG1 VAL A 333       3.946  20.683 -12.765  1.00 25.42           C  
ANISOU 2672  CG1 VAL A 333     2888   3476   3295    530    154    537       C  
ATOM   2673  CG2 VAL A 333       5.132  20.854 -10.605  1.00 24.87           C  
ANISOU 2673  CG2 VAL A 333     2885   3321   3242    597     60    482       C  
ATOM   2674  N   ARG A 334       4.221  24.227 -13.984  1.00 25.23           N  
ANISOU 2674  N   ARG A 334     2820   3497   3268    489    302    556       N  
ATOM   2675  CA  ARG A 334       3.524  25.312 -14.711  1.00 24.48           C  
ANISOU 2675  CA  ARG A 334     2746   3414   3140    470    344    610       C  
ATOM   2676  C   ARG A 334       2.785  24.785 -15.931  1.00 24.14           C  
ANISOU 2676  C   ARG A 334     2720   3389   3064    445    334    642       C  
ATOM   2677  O   ARG A 334       1.970  25.532 -16.477  1.00 24.42           O  
ANISOU 2677  O   ARG A 334     2785   3424   3071    443    334    694       O  
ATOM   2678  CB  ARG A 334       4.513  26.366 -15.169  1.00 24.63           C  
ANISOU 2678  CB  ARG A 334     2773   3421   3165    442    402    564       C  
ATOM   2679  CG  ARG A 334       3.892  27.485 -15.998  1.00 24.57           C  
ANISOU 2679  CG  ARG A 334     2821   3405   3108    421    435    620       C  
ATOM   2680  CD  ARG A 334       2.729  28.196 -15.337  1.00 23.65           C  
ANISOU 2680  CD  ARG A 334     2711   3285   2990    463    410    692       C  
ATOM   2681  NE  ARG A 334       2.412  29.421 -16.051  1.00 23.74           N  
ANISOU 2681  NE  ARG A 334     2784   3272   2966    452    428    728       N  
ATOM   2682  CZ  ARG A 334       1.748  29.477 -17.213  1.00 24.49           C  
ANISOU 2682  CZ  ARG A 334     2937   3354   3013    439    398    768       C  
ATOM   2683  NH1 ARG A 334       1.319  28.356 -17.804  1.00 24.25           N1+
ANISOU 2683  NH1 ARG A 334     2897   3345   2972    432    356    772       N1+
ATOM   2684  NH2 ARG A 334       1.532  30.664 -17.782  1.00 24.56           N  
ANISOU 2684  NH2 ARG A 334     3028   3322   2982    435    401    800       N  
ATOM   2685  N   CYS A 335       3.066  23.571 -16.364  1.00 24.03           N  
ANISOU 2685  N   CYS A 335     2692   3383   3054    430    314    609       N  
ATOM   2686  CA  CYS A 335       2.354  22.957 -17.502  1.00 24.82           C  
ANISOU 2686  CA  CYS A 335     2811   3499   3119    405    297    635       C  
ATOM   2687  C   CYS A 335       2.523  21.462 -17.377  1.00 24.70           C  
ANISOU 2687  C   CYS A 335     2770   3489   3125    405    266    603       C  
ATOM   2688  O   CYS A 335       3.461  21.031 -16.702  1.00 24.18           O  
ANISOU 2688  O   CYS A 335     2681   3407   3099    421    258    547       O  
ATOM   2689  CB  CYS A 335       2.870  23.460 -18.848  1.00 26.57           C  
ANISOU 2689  CB  CYS A 335     3084   3713   3297    353    340    614       C  
ATOM   2690  SG  CYS A 335       4.630  23.116 -19.169  1.00 28.04           S  
ANISOU 2690  SG  CYS A 335     3246   3886   3521    307    408    494       S  
ATOM   2691  N   ILE A 336       1.630  20.714 -18.006  1.00 25.59           N  
ANISOU 2691  N   ILE A 336     2888   3617   3217    393    238    633       N  
ATOM   2692  CA  ILE A 336       1.506  19.246 -17.790  1.00 26.16           C  
ANISOU 2692  CA  ILE A 336     2944   3689   3306    395    206    615       C  
ATOM   2693  C   ILE A 336       0.572  18.663 -18.846  1.00 26.93           C  
ANISOU 2693  C   ILE A 336     3049   3808   3377    368    184    640       C  
ATOM   2694  O   ILE A 336      -0.483  19.255 -19.104  1.00 28.09           O  
ANISOU 2694  O   ILE A 336     3199   3963   3511    374    166    687       O  
ATOM   2695  CB  ILE A 336       0.979  19.004 -16.369  1.00 26.62           C  
ANISOU 2695  CB  ILE A 336     3001   3730   3382    426    189    641       C  
ATOM   2696  CG1 ILE A 336       1.150  17.541 -15.957  1.00 27.27           C  
ANISOU 2696  CG1 ILE A 336     3097   3790   3473    427    156    615       C  
ATOM   2697  CG2 ILE A 336      -0.466  19.498 -16.230  1.00 26.53           C  
ANISOU 2697  CG2 ILE A 336     2980   3731   3368    427    194    697       C  
ATOM   2698  CD1 ILE A 336       1.378  17.360 -14.483  1.00 27.25           C  
ANISOU 2698  CD1 ILE A 336     3137   3743   3473    456    137    613       C  
ATOM   2699  N   ARG A 337       0.954  17.560 -19.471  1.00 27.64           N  
ANISOU 2699  N   ARG A 337     3139   3899   3464    344    177    601       N  
ATOM   2700  CA  ARG A 337       0.031  16.797 -20.335  1.00 28.71           C  
ANISOU 2700  CA  ARG A 337     3280   4052   3578    320    147    620       C  
ATOM   2701  C   ARG A 337       0.281  15.329 -20.041  1.00 28.69           C  
ANISOU 2701  C   ARG A 337     3262   4038   3600    317    134    584       C  
ATOM   2702  O   ARG A 337       1.268  15.039 -19.357  1.00 28.17           O  
ANISOU 2702  O   ARG A 337     3190   3948   3565    336    138    542       O  
ATOM   2703  CB  ARG A 337       0.241  17.108 -21.814  1.00 30.58           C  
ANISOU 2703  CB  ARG A 337     3565   4294   3761    278    157    609       C  
ATOM   2704  CG  ARG A 337       0.308  18.586 -22.175  1.00 32.66           C  
ANISOU 2704  CG  ARG A 337     3878   4546   3984    275    174    636       C  
ATOM   2705  CD  ARG A 337      -1.035  19.254 -22.341  1.00 34.42           C  
ANISOU 2705  CD  ARG A 337     4114   4769   4193    301    111    699       C  
ATOM   2706  NE  ARG A 337      -1.913  18.490 -23.199  1.00 36.17           N  
ANISOU 2706  NE  ARG A 337     4346   5000   4397    287     50    706       N  
ATOM   2707  CZ  ARG A 337      -3.233  18.366 -23.044  1.00 39.24           C  
ANISOU 2707  CZ  ARG A 337     4688   5396   4824    317    -18    731       C  
ATOM   2708  NH1 ARG A 337      -3.877  18.976 -22.048  1.00 40.87           N1+
ANISOU 2708  NH1 ARG A 337     4836   5601   5092    359    -22    750       N1+
ATOM   2709  NH2 ARG A 337      -3.908  17.612 -23.899  1.00 39.86           N  
ANISOU 2709  NH2 ARG A 337     4774   5481   4891    300    -76    723       N  
ATOM   2710  N   PHE A 338      -0.587  14.450 -20.537  1.00 29.95           N  
ANISOU 2710  N   PHE A 338     3418   4209   3752    297    109    596       N  
ATOM   2711  CA  PHE A 338      -0.399  12.979 -20.474  1.00 30.39           C  
ANISOU 2711  CA  PHE A 338     3473   4250   3825    286     96    561       C  
ATOM   2712  C   PHE A 338      -1.099  12.315 -21.653  1.00 31.06           C  
ANISOU 2712  C   PHE A 338     3559   4356   3886    247     78    560       C  
ATOM   2713  O   PHE A 338      -1.972  12.952 -22.251  1.00 30.14           O  
ANISOU 2713  O   PHE A 338     3443   4260   3748    240     57    593       O  
ATOM   2714  CB  PHE A 338      -0.888  12.425 -19.134  1.00 30.50           C  
ANISOU 2714  CB  PHE A 338     3495   4233   3859    304     89    580       C  
ATOM   2715  CG  PHE A 338      -2.360  12.588 -18.824  1.00 30.10           C  
ANISOU 2715  CG  PHE A 338     3426   4194   3816    292     98    621       C  
ATOM   2716  CD1 PHE A 338      -3.278  11.619 -19.201  1.00 30.75           C  
ANISOU 2716  CD1 PHE A 338     3495   4282   3908    259     91    615       C  
ATOM   2717  CD2 PHE A 338      -2.837  13.673 -18.108  1.00 29.44           C  
ANISOU 2717  CD2 PHE A 338     3329   4112   3743    310    118    651       C  
ATOM   2718  CE1 PHE A 338      -4.630  11.742 -18.883  1.00 30.54           C  
ANISOU 2718  CE1 PHE A 338     3430   4260   3913    242    107    627       C  
ATOM   2719  CE2 PHE A 338      -4.185  13.786 -17.794  1.00 28.92           C  
ANISOU 2719  CE2 PHE A 338     3229   4051   3710    295    135    664       C  
ATOM   2720  CZ  PHE A 338      -5.083  12.818 -18.172  1.00 29.28           C  
ANISOU 2720  CZ  PHE A 338     3249   4100   3776    261    131    646       C  
ATOM   2721  N   ASP A 339      -0.651  11.097 -21.979  1.00 32.91           N  
ANISOU 2721  N   ASP A 339     3798   4578   4128    229     75    516       N  
ATOM   2722  CA  ASP A 339      -1.361  10.086 -22.817  1.00 34.12           C  
ANISOU 2722  CA  ASP A 339     3953   4743   4269    193     55    509       C  
ATOM   2723  C   ASP A 339      -1.467   8.802 -21.978  1.00 27.72           C  
ATOM   2724  O   ASP A 339      -1.404   8.927 -20.749  1.00 34.43           O  
ANISOU 2724  O   ASP A 339     4006   4719   4358    227     52    513       O  
ATOM   2725  CB  ASP A 339      -0.689   9.915 -24.182  1.00 34.34           C  
ANISOU 2725  CB  ASP A 339     4007   4780   4261    153     69    464       C  
ATOM   2726  CG  ASP A 339       0.763   9.482 -24.148  1.00 34.93           C  
ANISOU 2726  CG  ASP A 339     4075   4829   4368    153    105    390       C  
ATOM   2727  OD1 ASP A 339       1.272   9.184 -23.026  1.00 34.07           O  
ANISOU 2727  OD1 ASP A 339     3945   4689   4311    196     93    375       O  
ATOM   2728  OD2 ASP A 339       1.378   9.446 -25.267  1.00 36.78           O1-
ANISOU 2728  OD2 ASP A 339     4331   5066   4577    107    143    338       O1-
ATOM   2729  N   ASN A 340      -1.603   7.623 -22.581  1.00 36.24           N  
ANISOU 2729  N   ASN A 340     4227   4973   4570    168     38    466       N  
ATOM   2730  CA  ASN A 340      -1.746   6.368 -21.793  1.00 38.10           C  
ANISOU 2730  CA  ASN A 340     4487   5162   4827    168     31    456       C  
ATOM   2731  C   ASN A 340      -0.397   5.959 -21.201  1.00 36.96           C  
ANISOU 2731  C   ASN A 340     4370   4965   4709    207     14    414       C  
ATOM   2732  O   ASN A 340      -0.409   5.227 -20.207  1.00 36.34           O  
ANISOU 2732  O   ASN A 340     4344   4828   4637    223     -7    419       O  
ATOM   2733  CB  ASN A 340      -2.308   5.177 -22.571  1.00 41.28           C  
ANISOU 2733  CB  ASN A 340     4889   5567   5228    124     24    434       C  
ATOM   2734  CG  ASN A 340      -3.041   5.554 -23.837  1.00 44.53           C  
ANISOU 2734  CG  ASN A 340     5271   6034   5616     90     13    439       C  
ATOM   2735  ND2 ASN A 340      -4.257   6.088 -23.716  1.00 46.42           N  
ANISOU 2735  ND2 ASN A 340     5477   6296   5864     85      2    471       N  
ATOM   2736  OD1 ASN A 340      -2.482   5.349 -24.916  1.00 48.96           O  
ANISOU 2736  OD1 ASN A 340     5843   6606   6152     69     11    404       O  
ATOM   2737  N   LYS A 341       0.717   6.366 -21.805  1.00 37.02           N  
ANISOU 2737  N   LYS A 341     4350   4982   4733    218     20    363       N  
ATOM   2738  CA  LYS A 341       2.050   5.832 -21.428  1.00 37.20           C  
ANISOU 2738  CA  LYS A 341     4371   4950   4812    258    -10    289       C  
ATOM   2739  C   LYS A 341       2.696   6.770 -20.407  1.00 34.82           C  
ANISOU 2739  C   LYS A 341     4070   4629   4533    310    -27    292       C  
ATOM   2740  O   LYS A 341       3.374   6.261 -19.461  1.00 34.17           O  
ANISOU 2740  O   LYS A 341     4017   4477   4488    362    -90    260       O  
ATOM   2741  CB  LYS A 341       2.905   5.595 -22.674  1.00 40.14           C  
ANISOU 2741  CB  LYS A 341     4702   5338   5213    229     22    203       C  
ATOM   2742  CG  LYS A 341       2.643   4.267 -23.377  1.00 43.94           C  
ANISOU 2742  CG  LYS A 341     5192   5808   5695    196     17    173       C  
ATOM   2743  CD  LYS A 341       2.762   4.282 -24.914  1.00 47.86           C  
ANISOU 2743  CD  LYS A 341     5673   6345   6166    130     75    128       C  
ATOM   2744  CE  LYS A 341       3.978   3.560 -25.479  1.00 49.34           C  
ANISOU 2744  CE  LYS A 341     5824   6498   6423    122     98      5       C  
ATOM   2745  NZ  LYS A 341       4.285   4.069 -26.837  1.00 50.53           N1+
ANISOU 2745  NZ  LYS A 341     5979   6685   6537     47    185    -42       N1+
ATOM   2746  N   ARG A 342       2.494   8.080 -20.543  1.00 32.79           N  
ANISOU 2746  N   ARG A 342     3791   4418   4249    300     13    327       N  
ATOM   2747  CA  ARG A 342       3.246   8.995 -19.657  1.00 32.84           C  
ANISOU 2747  CA  ARG A 342     3790   4404   4282    346      1    316       C  
ATOM   2748  C   ARG A 342       2.584  10.351 -19.444  1.00 30.39           C  
ANISOU 2748  C   ARG A 342     3481   4135   3931    339     38    386       C  
ATOM   2749  O   ARG A 342       1.587  10.688 -20.091  1.00 28.48           O  
ANISOU 2749  O   ARG A 342     3239   3936   3647    303     65    436       O  
ATOM   2750  CB  ARG A 342       4.657   9.185 -20.204  1.00 35.94           C  
ANISOU 2750  CB  ARG A 342     4125   4789   4743    351     17    209       C  
ATOM   2751  CG  ARG A 342       4.707   9.345 -21.713  1.00 37.78           C  
ANISOU 2751  CG  ARG A 342     4334   5067   4955    283     93    177       C  
ATOM   2752  CD  ARG A 342       6.123   9.246 -22.258  1.00 39.20           C  
ANISOU 2752  CD  ARG A 342     4453   5225   5216    272    130     43       C  
ATOM   2753  NE  ARG A 342       6.046   8.490 -23.494  1.00 40.26           N  
ANISOU 2753  NE  ARG A 342     4592   5372   5333    211    175      3       N  
ATOM   2754  CZ  ARG A 342       6.784   7.424 -23.756  1.00 42.10           C  
ANISOU 2754  CZ  ARG A 342     4784   5568   5644    216    164    -99       C  
ATOM   2755  NH1 ARG A 342       6.623   6.791 -24.912  1.00 44.23           N1+
ANISOU 2755  NH1 ARG A 342     5067   5852   5885    152    214   -130       N1+
ATOM   2756  NH2 ARG A 342       7.735   7.052 -22.904  1.00 41.14           N  
ANISOU 2756  NH2 ARG A 342     4609   5391   5633    285    100   -182       N  
ATOM   2757  N   ILE A 343       3.148  10.999 -18.433  1.00 29.01           N  
ANISOU 2757  N   ILE A 343     3313   3933   3777    382     19    381       N  
ATOM   2758  CA  ILE A 343       2.942  12.397 -17.986  1.00 27.75           C  
ANISOU 2758  CA  ILE A 343     3150   3796   3598    390     48    424       C  
ATOM   2759  C   ILE A 343       4.212  13.134 -18.383  1.00 27.19           C  
ANISOU 2759  C   ILE A 343     3032   3728   3571    395     72    350       C  
ATOM   2760  O   ILE A 343       5.315  12.592 -18.103  1.00 26.91           O  
ANISOU 2760  O   ILE A 343     2971   3651   3602    425     33    264       O  
ATOM   2761  CB  ILE A 343       2.763  12.479 -16.461  1.00 26.92           C  
ANISOU 2761  CB  ILE A 343     3099   3646   3484    430     11    459       C  
ATOM   2762  CG1 ILE A 343       1.677  11.542 -15.962  1.00 27.02           C  
ANISOU 2762  CG1 ILE A 343     3173   3634   3460    412      3    507       C  
ATOM   2763  CG2 ILE A 343       2.511  13.907 -16.025  1.00 26.88           C  
ANISOU 2763  CG2 ILE A 343     3086   3663   3463    436     47    499       C  
ATOM   2764  CD1 ILE A 343       1.535  11.563 -14.472  1.00 27.29           C  
ANISOU 2764  CD1 ILE A 343     3295   3608   3467    434    -19    535       C  
ATOM   2765  N   VAL A 344       4.051  14.313 -18.973  1.00 25.77           N  
ANISOU 2765  N   VAL A 344     2844   3586   3361    365    131    373       N  
ATOM   2766  CA  VAL A 344       5.181  15.232 -19.228  1.00 25.56           C  
ANISOU 2766  CA  VAL A 344     2785   3557   3371    356    178    304       C  
ATOM   2767  C   VAL A 344       4.844  16.562 -18.578  1.00 24.03           C  
ANISOU 2767  C   VAL A 344     2608   3372   3151    372    193    363       C  
ATOM   2768  O   VAL A 344       3.865  17.181 -19.006  1.00 24.06           O  
ANISOU 2768  O   VAL A 344     2643   3403   3096    352    214    438       O  
ATOM   2769  CB  VAL A 344       5.452  15.408 -20.732  1.00 26.74           C  
ANISOU 2769  CB  VAL A 344     2939   3726   3494    285    254    264       C  
ATOM   2770  CG1 VAL A 344       6.791  16.088 -20.945  1.00 27.00           C  
ANISOU 2770  CG1 VAL A 344     2932   3742   3584    261    322    158       C  
ATOM   2771  CG2 VAL A 344       5.383  14.096 -21.485  1.00 27.23           C  
ANISOU 2771  CG2 VAL A 344     2998   3787   3559    260    244    230       C  
ATOM   2772  N   SER A 345       5.655  16.982 -17.616  1.00 22.65           N  
ANISOU 2772  N   SER A 345     2410   3170   3026    412    174    321       N  
ATOM   2773  CA  SER A 345       5.474  18.233 -16.845  1.00 21.32           C  
ANISOU 2773  CA  SER A 345     2256   3003   2842    431    187    365       C  
ATOM   2774  C   SER A 345       6.598  19.206 -17.155  1.00 21.17           C  
ANISOU 2774  C   SER A 345     2200   2980   2865    411    245    287       C  
ATOM   2775  O   SER A 345       7.705  18.743 -17.418  1.00 21.76           O  
ANISOU 2775  O   SER A 345     2221   3035   3012    405    249    176       O  
ATOM   2776  CB  SER A 345       5.430  17.925 -15.392  1.00 20.66           C  
ANISOU 2776  CB  SER A 345     2197   2882   2770    487    115    381       C  
ATOM   2777  OG  SER A 345       6.492  17.070 -15.030  1.00 19.89           O  
ANISOU 2777  OG  SER A 345     2078   2741   2739    522     49    290       O  
ATOM   2778  N   GLY A 346       6.299  20.495 -17.123  1.00 20.88           N  
ANISOU 2778  N   GLY A 346     2186   2955   2791    398    291    334       N  
ATOM   2779  CA  GLY A 346       7.297  21.571 -17.161  1.00 21.46           C  
ANISOU 2779  CA  GLY A 346     2235   3017   2903    378    353    265       C  
ATOM   2780  C   GLY A 346       7.200  22.408 -15.918  1.00 21.21           C  
ANISOU 2780  C   GLY A 346     2208   2975   2877    425    324    299       C  
ATOM   2781  O   GLY A 346       6.083  22.663 -15.483  1.00 21.60           O  
ANISOU 2781  O   GLY A 346     2300   3035   2872    444    304    399       O  
ATOM   2782  N   ALA A 347       8.320  22.901 -15.420  1.00 21.79           N  
ANISOU 2782  N   ALA A 347     2234   3024   3020    435    332    208       N  
ATOM   2783  CA  ALA A 347       8.360  23.710 -14.187  1.00 22.01           C  
ANISOU 2783  CA  ALA A 347     2270   3037   3057    479    301    227       C  
ATOM   2784  C   ALA A 347       9.083  25.046 -14.376  1.00 22.76           C  
ANISOU 2784  C   ALA A 347     2342   3126   3178    443    384    174       C  
ATOM   2785  O   ALA A 347       9.828  25.240 -15.357  1.00 24.60           O  
ANISOU 2785  O   ALA A 347     2546   3358   3444    383    468     91       O  
ATOM   2786  CB  ALA A 347       9.024  22.906 -13.129  1.00 22.55           C  
ANISOU 2786  CB  ALA A 347     2314   3067   3187    540    193    163       C  
ATOM   2787  N   TYR A 348       8.915  25.918 -13.394  1.00 22.28           N  
ANISOU 2787  N   TYR A 348     2301   3057   3108    474    369    210       N  
ATOM   2788  CA  TYR A 348       9.437  27.303 -13.356  1.00 22.15           C  
ANISOU 2788  CA  TYR A 348     2276   3031   3109    446    444    176       C  
ATOM   2789  C   TYR A 348      10.968  27.304 -13.418  1.00 22.30           C  
ANISOU 2789  C   TYR A 348     2204   3026   3241    429    464     12       C  
ATOM   2790  O   TYR A 348      11.502  28.356 -13.720  1.00 22.76           O  
ANISOU 2790  O   TYR A 348     2253   3076   3320    380    557    -38       O  
ATOM   2791  CB  TYR A 348       8.913  28.004 -12.104  1.00 21.96           C  
ANISOU 2791  CB  TYR A 348     2287   2998   3057    494    404    242       C  
ATOM   2792  CG  TYR A 348       7.720  28.903 -12.296  1.00 21.97           C  
ANISOU 2792  CG  TYR A 348     2354   3014   2980    482    453    359       C  
ATOM   2793  CD1 TYR A 348       6.947  28.909 -13.450  1.00 21.95           C  
ANISOU 2793  CD1 TYR A 348     2390   3028   2922    447    491    422       C  
ATOM   2794  CD2 TYR A 348       7.377  29.786 -11.288  1.00 21.73           C  
ANISOU 2794  CD2 TYR A 348     2347   2972   2938    509    449    398       C  
ATOM   2795  CE1 TYR A 348       5.892  29.794 -13.603  1.00 21.74           C  
ANISOU 2795  CE1 TYR A 348     2415   3001   2843    449    511    514       C  
ATOM   2796  CE2 TYR A 348       6.338  30.681 -11.433  1.00 21.38           C  
ANISOU 2796  CE2 TYR A 348     2347   2932   2844    505    488    487       C  
ATOM   2797  CZ  TYR A 348       5.586  30.677 -12.583  1.00 21.81           C  
ANISOU 2797  CZ  TYR A 348     2432   2999   2857    481    511    543       C  
ATOM   2798  OH  TYR A 348       4.556  31.573 -12.609  1.00 22.71           O  
ANISOU 2798  OH  TYR A 348     2583   3104   2941    493    523    619       O  
ATOM   2799  N   ASP A 349      11.648  26.193 -13.146  1.00 22.02           N  
ANISOU 2799  N   ASP A 349     2105   2975   3288    467    380    -79       N  
ATOM   2800  CA  ASP A 349      13.130  26.153 -13.180  1.00 22.72           C  
ANISOU 2800  CA  ASP A 349     2080   3034   3519    458    387   -264       C  
ATOM   2801  C   ASP A 349      13.582  25.746 -14.578  1.00 13.88           C  
ATOM   2802  O   ASP A 349      14.757  25.467 -14.717  1.00 24.07           O  
ANISOU 2802  O   ASP A 349     2098   3187   3862    367    506   -520       O  
ATOM   2803  CB  ASP A 349      13.704  25.233 -12.095  1.00 23.03           C  
ANISOU 2803  CB  ASP A 349     2072   3033   3644    552    217   -338       C  
ATOM   2804  CG  ASP A 349      13.336  23.763 -12.202  1.00 22.70           C  
ANISOU 2804  CG  ASP A 349     2054   2985   3588    591    125   -309       C  
ATOM   2805  OD1 ASP A 349      12.492  23.436 -13.054  1.00 22.19           O  
ANISOU 2805  OD1 ASP A 349     2038   2955   3437    547    191   -217       O  
ATOM   2806  OD2 ASP A 349      13.911  22.958 -11.431  1.00 23.06           O1-
ANISOU 2806  OD2 ASP A 349     2074   2982   3708    667    -22   -382       O1-
ATOM   2807  N   GLY A 350      12.661  25.690 -15.546  1.00 22.72           N  
ANISOU 2807  N   GLY A 350     2125   3068   3438    326    565   -239       N  
ATOM   2808  CA  GLY A 350      12.960  25.423 -16.963  1.00 23.07           C  
ANISOU 2808  CA  GLY A 350     2172   3114   3479    233    685   -301       C  
ATOM   2809  C   GLY A 350      13.208  23.958 -17.230  1.00 23.28           C  
ANISOU 2809  C   GLY A 350     2141   3140   3566    255    623   -365       C  
ATOM   2810  O   GLY A 350      13.675  23.631 -18.346  1.00 24.64           O  
ANISOU 2810  O   GLY A 350     2296   3306   3762    175    727   -453       O  
ATOM   2811  N   LYS A 351      12.938  23.094 -16.252  1.00 22.69           N  
ANISOU 2811  N   LYS A 351     2049   3060   3513    354    468   -329       N  
ATOM   2812  CA  LYS A 351      13.174  21.632 -16.372  1.00 23.03           C  
ANISOU 2812  CA  LYS A 351     2045   3089   3618    390    386   -387       C  
ATOM   2813  C   LYS A 351      11.874  20.973 -16.819  1.00 22.14           C  
ANISOU 2813  C   LYS A 351     2030   3008   3375    385    370   -236       C  
ATOM   2814  O   LYS A 351      10.794  21.455 -16.430  1.00 21.61           O  
ANISOU 2814  O   LYS A 351     2049   2962   3202    401    352    -90       O  
ATOM   2815  CB  LYS A 351      13.684  21.048 -15.055  1.00 23.68           C  
ANISOU 2815  CB  LYS A 351     2079   3128   3792    498    215   -443       C  
ATOM   2816  CG  LYS A 351      15.065  21.524 -14.643  1.00 25.28           C  
ANISOU 2816  CG  LYS A 351     2158   3292   4156    515    203   -625       C  
ATOM   2817  CD  LYS A 351      15.676  20.812 -13.482  1.00 26.73           C  
ANISOU 2817  CD  LYS A 351     2300   3416   4442    628      6   -703       C  
ATOM   2818  CE  LYS A 351      16.908  21.537 -12.974  1.00 28.96           C  
ANISOU 2818  CE  LYS A 351     2463   3662   4879    648    -16   -874       C  
ATOM   2819  NZ  LYS A 351      17.554  20.810 -11.844  1.00 30.98           N1+
ANISOU 2819  NZ  LYS A 351     2687   3843   5240    772   -244   -963       N1+
ATOM   2820  N   ILE A 352      11.976  19.914 -17.599  1.00 22.20           N  
ANISOU 2820  N   ILE A 352     2017   3014   3403    362    377   -282       N  
ATOM   2821  CA  ILE A 352      10.809  19.105 -18.028  1.00 21.93           C  
ANISOU 2821  CA  ILE A 352     2062   3006   3266    359    349   -160       C  
ATOM   2822  C   ILE A 352      11.020  17.685 -17.540  1.00 22.07           C  
ANISOU 2822  C   ILE A 352     2046   2992   3348    426    228   -202       C  
ATOM   2823  O   ILE A 352      12.119  17.168 -17.717  1.00 22.77           O  
ANISOU 2823  O   ILE A 352     2042   3049   3562    432    219   -354       O  
ATOM   2824  CB  ILE A 352      10.642  19.123 -19.548  1.00 22.42           C  
ANISOU 2824  CB  ILE A 352     2160   3089   3269    261    472   -166       C  
ATOM   2825  CG1 ILE A 352      10.084  20.454 -20.024  1.00 22.54           C  
ANISOU 2825  CG1 ILE A 352     2264   3123   3179    204    560    -80       C  
ATOM   2826  CG2 ILE A 352       9.780  17.968 -20.002  1.00 22.28           C  
ANISOU 2826  CG2 ILE A 352     2185   3087   3192    265    424    -96       C  
ATOM   2827  CD1 ILE A 352      10.206  20.636 -21.506  1.00 23.78           C  
ANISOU 2827  CD1 ILE A 352     2483   3277   3276     96    687   -112       C  
ATOM   2828  N   LYS A 353       9.972  17.077 -17.005  1.00 21.49           N  
ANISOU 2828  N   LYS A 353     2048   2923   3196    467    147    -80       N  
ATOM   2829  CA  LYS A 353      10.053  15.714 -16.452  1.00 22.32           C  
ANISOU 2829  CA  LYS A 353     2158   2983   3339    528     25   -102       C  
ATOM   2830  C   LYS A 353       9.089  14.819 -17.213  1.00 22.31           C  
ANISOU 2830  C   LYS A 353     2206   3007   3263    493     45    -27       C  
ATOM   2831  O   LYS A 353       8.060  15.309 -17.675  1.00 22.33           O  
ANISOU 2831  O   LYS A 353     2259   3057   3169    448    107     78       O  
ATOM   2832  CB  LYS A 353       9.833  15.725 -14.938  1.00 22.48           C  
ANISOU 2832  CB  LYS A 353     2243   2960   3338    605    -93    -46       C  
ATOM   2833  CG  LYS A 353      11.019  16.256 -14.147  1.00 23.25           C  
ANISOU 2833  CG  LYS A 353     2283   3013   3537    658   -157   -156       C  
ATOM   2834  CD  LYS A 353      10.965  16.042 -12.666  1.00 23.50           C  
ANISOU 2834  CD  LYS A 353     2402   2980   3545    738   -300   -121       C  
ATOM   2835  CE  LYS A 353      12.143  16.682 -11.971  1.00 24.85           C  
ANISOU 2835  CE  LYS A 353     2510   3110   3822    790   -370   -238       C  
ATOM   2836  NZ  LYS A 353      13.245  15.718 -11.744  1.00 26.34           N1+
ANISOU 2836  NZ  LYS A 353     2642   3220   4145    863   -515   -384       N1+
ATOM   2837  N   VAL A 354       9.483  13.561 -17.381  1.00 22.85           N  
ANISOU 2837  N   VAL A 354     2251   3040   3389    514    -13    -95       N  
ATOM   2838  CA  VAL A 354       8.685  12.513 -18.057  1.00 22.59           C  
ANISOU 2838  CA  VAL A 354     2259   3022   3302    484     -7    -44       C  
ATOM   2839  C   VAL A 354       8.474  11.438 -17.011  1.00 22.32           C  
ANISOU 2839  C   VAL A 354     2287   2926   3268    553   -137    -17       C  
ATOM   2840  O   VAL A 354       9.492  10.998 -16.419  1.00 22.13           O  
ANISOU 2840  O   VAL A 354     2232   2836   3341    618   -235   -117       O  
ATOM   2841  CB  VAL A 354       9.412  11.940 -19.280  1.00 24.19           C  
ANISOU 2841  CB  VAL A 354     2391   3228   3573    437     54   -162       C  
ATOM   2842  CG1 VAL A 354       8.564  10.899 -20.013  1.00 24.40           C  
ANISOU 2842  CG1 VAL A 354     2464   3271   3537    403     61   -108       C  
ATOM   2843  CG2 VAL A 354       9.877  13.054 -20.217  1.00 24.81           C  
ANISOU 2843  CG2 VAL A 354     2431   3343   3653    360    191   -215       C  
ATOM   2844  N   TRP A 355       7.203  11.059 -16.813  1.00 21.42           N  
ANISOU 2844  N   TRP A 355     2260   2825   3053    537   -138    104       N  
ATOM   2845  CA  TRP A 355       6.782  10.138 -15.738  1.00 21.14           C  
ANISOU 2845  CA  TRP A 355     2327   2723   2984    581   -236    151       C  
ATOM   2846  C   TRP A 355       6.086   8.903 -16.316  1.00 20.95           C  
ANISOU 2846  C   TRP A 355     2337   2696   2927    548   -231    178       C  
ATOM   2847  O   TRP A 355       5.298   9.043 -17.260  1.00 19.91           O  
ANISOU 2847  O   TRP A 355     2181   2632   2753    486   -146    222       O  
ATOM   2848  CB  TRP A 355       5.875  10.890 -14.772  1.00 20.54           C  
ANISOU 2848  CB  TRP A 355     2332   2652   2821    577   -221    258       C  
ATOM   2849  CG  TRP A 355       6.366  12.233 -14.345  1.00 19.87           C  
ANISOU 2849  CG  TRP A 355     2212   2584   2755    595   -204    246       C  
ATOM   2850  CD1 TRP A 355       6.254  13.404 -15.023  1.00 19.46           C  
ANISOU 2850  CD1 TRP A 355     2095   2602   2699    556   -109    258       C  
ATOM   2851  CD2 TRP A 355       6.954  12.556 -13.080  1.00 19.90           C  
ANISOU 2851  CD2 TRP A 355     2266   2525   2770    655   -290    227       C  
ATOM   2852  CE2 TRP A 355       7.174  13.940 -13.072  1.00 19.50           C  
ANISOU 2852  CE2 TRP A 355     2160   2519   2731    646   -230    225       C  
ATOM   2853  CE3 TRP A 355       7.265  11.818 -11.936  1.00 20.41           C  
ANISOU 2853  CE3 TRP A 355     2439   2492   2825    713   -417    216       C  
ATOM   2854  NE1 TRP A 355       6.725  14.435 -14.261  1.00 19.31           N  
ANISOU 2854  NE1 TRP A 355     2072   2572   2695    585   -119    247       N  
ATOM   2855  CZ2 TRP A 355       7.737  14.591 -11.984  1.00 19.68           C  
ANISOU 2855  CZ2 TRP A 355     2211   2499   2767    693   -291    204       C  
ATOM   2856  CZ3 TRP A 355       7.823  12.462 -10.858  1.00 20.46           C  
ANISOU 2856  CZ3 TRP A 355     2489   2449   2835    763   -490    197       C  
ATOM   2857  CH2 TRP A 355       8.053  13.828 -10.887  1.00 20.12           C  
ANISOU 2857  CH2 TRP A 355     2370   2460   2813    753   -425    189       C  
ATOM   2858  N   ASP A 356       6.351   7.741 -15.725  1.00 21.69           N  
ANISOU 2858  N   ASP A 356     2498   2705   3038    592   -331    153       N  
ATOM   2859  CA  ASP A 356       5.639   6.493 -16.076  1.00 22.58           C  
ANISOU 2859  CA  ASP A 356     2666   2801   3114    562   -332    183       C  
ATOM   2860  C   ASP A 356       4.222   6.622 -15.541  1.00 13.73           C  
ATOM   2861  O   ASP A 356       4.061   6.511 -14.363  1.00 22.41           O  
ANISOU 2861  O   ASP A 356     2850   2724   2939    539   -329    338       O  
ATOM   2862  CB  ASP A 356       6.337   5.242 -15.542  1.00 23.67           C  
ANISOU 2862  CB  ASP A 356     2868   2827   3297    625   -461    122       C  
ATOM   2863  CG  ASP A 356       5.669   3.971 -16.047  1.00 24.64           C  
ANISOU 2863  CG  ASP A 356     3039   2935   3390    586   -448    143       C  
ATOM   2864  OD1 ASP A 356       4.520   4.089 -16.676  1.00 24.56           O  
ANISOU 2864  OD1 ASP A 356     3017   3000   3314    508   -340    214       O  
ATOM   2865  OD2 ASP A 356       6.287   2.861 -15.830  1.00 25.88           O1-
ANISOU 2865  OD2 ASP A 356     3241   2997   3593    637   -554     82       O1-
ATOM   2866  N   LEU A 357       3.241   6.849 -16.392  1.00 22.37           N  
ANISOU 2866  N   LEU A 357     2687   2868   2946    450   -186    348       N  
ATOM   2867  CA  LEU A 357       1.852   7.068 -15.929  1.00 22.63           C  
ANISOU 2867  CA  LEU A 357     2774   2917   2908    404   -128    436       C  
ATOM   2868  C   LEU A 357       1.322   5.796 -15.272  1.00 23.56           C  
ANISOU 2868  C   LEU A 357     3012   2955   2984    387   -152    457       C  
ATOM   2869  O   LEU A 357       0.727   5.896 -14.183  1.00 23.78           O  
ANISOU 2869  O   LEU A 357     3142   2936   2956    372   -135    504       O  
ATOM   2870  CB  LEU A 357       0.943   7.468 -17.093  1.00 22.32           C  
ANISOU 2870  CB  LEU A 357     2651   2969   2861    348    -51    461       C  
ATOM   2871  CG  LEU A 357      -0.534   7.497 -16.715  1.00 22.54           C  
ANISOU 2871  CG  LEU A 357     2706   3009   2850    300      3    523       C  
ATOM   2872  CD1 LEU A 357      -0.741   8.468 -15.576  1.00 22.40           C  
ANISOU 2872  CD1 LEU A 357     2726   2975   2811    314     24    560       C  
ATOM   2873  CD2 LEU A 357      -1.403   7.876 -17.893  1.00 22.81           C  
ANISOU 2873  CD2 LEU A 357     2654   3122   2891    260     44    534       C  
ATOM   2874  N   GLN A 358       1.496   4.653 -15.924  1.00 24.55           N  
ANISOU 2874  N   GLN A 358     3135   3061   3133    380   -178    419       N  
ATOM   2875  CA  GLN A 358       0.887   3.392 -15.439  1.00 25.99           C  
ANISOU 2875  CA  GLN A 358     3439   3166   3270    349   -188    439       C  
ATOM   2876  C   GLN A 358       1.514   3.072 -14.086  1.00 26.28           C  
ANISOU 2876  C   GLN A 358     3631   3079   3273    402   -280    441       C  
ATOM   2877  O   GLN A 358       0.790   2.674 -13.200  1.00 26.64           O  
ANISOU 2877  O   GLN A 358     3822   3057   3244    362   -254    487       O  
ATOM   2878  CB  GLN A 358       1.022   2.263 -16.467  1.00 27.21           C  
ANISOU 2878  CB  GLN A 358     3556   3322   3460    335   -201    393       C  
ATOM   2879  CG  GLN A 358       0.187   2.478 -17.736  1.00 27.24           C  
ANISOU 2879  CG  GLN A 358     3446   3433   3472    272   -118    401       C  
ATOM   2880  CD  GLN A 358      -1.240   2.887 -17.441  1.00 27.44           C  
ANISOU 2880  CD  GLN A 358     3478   3492   3456    211    -38    461       C  
ATOM   2881  NE2 GLN A 358      -1.791   3.782 -18.245  1.00 26.76           N  
ANISOU 2881  NE2 GLN A 358     3286   3498   3383    189      6    472       N  
ATOM   2882  OE1 GLN A 358      -1.853   2.411 -16.491  1.00 29.48           O  
ANISOU 2882  OE1 GLN A 358     3842   3684   3674    181    -15    488       O  
ATOM   2883  N   ALA A 359       2.811   3.309 -13.916  1.00 26.80           N  
ANISOU 2883  N   ALA A 359     3674   3113   3395    484   -381    384       N  
ATOM   2884  CA  ALA A 359       3.517   3.083 -12.633  1.00 27.60           C  
ANISOU 2884  CA  ALA A 359     3928   3089   3471    551   -506    375       C  
ATOM   2885  C   ALA A 359       2.946   4.035 -11.582  1.00 27.79           C  
ANISOU 2885  C   ALA A 359     4038   3108   3413    527   -458    444       C  
ATOM   2886  O   ALA A 359       2.741   3.605 -10.443  1.00 29.33           O  
ANISOU 2886  O   ALA A 359     4433   3190   3520    523   -499    479       O  
ATOM   2887  CB  ALA A 359       5.003   3.270 -12.789  1.00 27.51           C  
ANISOU 2887  CB  ALA A 359     3828   3056   3567    646   -625    277       C  
ATOM   2888  N   ALA A 360       2.690   5.287 -11.943  1.00 27.46           N  
ANISOU 2888  N   ALA A 360     3866   3175   3393    507   -371    460       N  
ATOM   2889  CA  ALA A 360       2.180   6.314 -11.012  1.00 27.82           C  
ANISOU 2889  CA  ALA A 360     3968   3224   3377    486   -317    514       C  
ATOM   2890  C   ALA A 360       0.861   5.814 -10.401  1.00 28.52           C  
ANISOU 2890  C   ALA A 360     4194   3271   3373    399   -224    574       C  
ATOM   2891  O   ALA A 360       0.741   5.882  -9.197  1.00 30.28           O  
ANISOU 2891  O   ALA A 360     4584   3406   3515    390   -233    603       O  
ATOM   2892  CB  ALA A 360       2.016   7.625 -11.733  1.00 26.72           C  
ANISOU 2892  CB  ALA A 360     3658   3210   3286    474   -235    518       C  
ATOM   2893  N   LEU A 361      -0.028   5.250 -11.222  1.00 28.11           N  
ANISOU 2893  N   LEU A 361     4079   3268   3335    336   -141    581       N  
ATOM   2894  CA  LEU A 361      -1.353   4.693 -10.836  1.00 28.06           C  
ANISOU 2894  CA  LEU A 361     4165   3229   3267    238    -30    613       C  
ATOM   2895  C   LEU A 361      -1.239   3.358 -10.094  1.00 29.65           C  
ANISOU 2895  C   LEU A 361     4587   3286   3391    222    -80    617       C  
ATOM   2896  O   LEU A 361      -2.234   3.008  -9.495  1.00 31.71           O  
ANISOU 2896  O   LEU A 361     4966   3497   3587    132     24    639       O  
ATOM   2897  CB  LEU A 361      -2.196   4.488 -12.091  1.00 26.79           C  
ANISOU 2897  CB  LEU A 361     3846   3166   3166    188     47    601       C  
ATOM   2898  CG  LEU A 361      -2.514   5.747 -12.868  1.00 25.82           C  
ANISOU 2898  CG  LEU A 361     3537   3169   3105    194     92    603       C  
ATOM   2899  CD1 LEU A 361      -3.121   5.408 -14.192  1.00 25.60           C  
ANISOU 2899  CD1 LEU A 361     3379   3219   3128    162    121    584       C  
ATOM   2900  CD2 LEU A 361      -3.470   6.617 -12.099  1.00 26.41           C  
ANISOU 2900  CD2 LEU A 361     3621   3251   3162    147    191    628       C  
ATOM   2901  N   ASP A 362      -0.132   2.620 -10.177  1.00 30.52           N  
ANISOU 2901  N   ASP A 362     4751   3329   3517    299   -224    586       N  
ATOM   2902  CA  ASP A 362       0.093   1.384  -9.370  1.00 32.93           C  
ANISOU 2902  CA  ASP A 362     5301   3470   3740    300   -306    591       C  
ATOM   2903  C   ASP A 362       0.539   1.846  -7.986  1.00 20.02           C  
ATOM   2904  O   ASP A 362       1.670   2.280  -7.803  1.00 33.94           O  
ANISOU 2904  O   ASP A 362     5597   3476   3822    436   -517    584       O  
ATOM   2905  CB  ASP A 362       1.071   0.410 -10.051  1.00 34.38           C  
ANISOU 2905  CB  ASP A 362     5452   3617   3993    378   -445    537       C  
ATOM   2906  CG  ASP A 362       1.536  -0.805  -9.239  1.00 36.61           C  
ANISOU 2906  CG  ASP A 362     5991   3715   4204    411   -577    534       C  
ATOM   2907  OD1 ASP A 362       1.091  -0.952  -8.087  1.00 38.02           O  
ANISOU 2907  OD1 ASP A 362     6412   3779   4254    364   -559    583       O  
ATOM   2908  OD2 ASP A 362       2.407  -1.585  -9.741  1.00 38.18           O1-
ANISOU 2908  OD2 ASP A 362     6157   3872   4476    488   -708    477       O1-
ATOM   2909  N   PRO A 363      -0.338   1.793  -6.960  1.00 33.69           N  
ANISOU 2909  N   PRO A 363     5795   3379   3626    241   -278    661       N  
ATOM   2910  CA  PRO A 363       0.018   2.269  -5.626  1.00 34.13           C  
ANISOU 2910  CA  PRO A 363     6061   3329   3579    260   -336    686       C  
ATOM   2911  C   PRO A 363       1.192   1.522  -4.984  1.00 35.26           C  
ANISOU 2911  C   PRO A 363     6414   3310   3675    361   -565    670       C  
ATOM   2912  O   PRO A 363       1.704   1.997  -4.026  1.00 35.64           O  
ANISOU 2912  O   PRO A 363     6604   3278   3658    404   -656    679       O  
ATOM   2913  CB  PRO A 363      -1.259   2.001  -4.819  1.00 34.89           C  
ANISOU 2913  CB  PRO A 363     6357   3352   3548    114   -158    724       C  
ATOM   2914  CG  PRO A 363      -1.967   0.884  -5.566  1.00 34.89           C  
ANISOU 2914  CG  PRO A 363     6328   3357   3571     42    -77    712       C  
ATOM   2915  CD  PRO A 363      -1.696   1.223  -7.015  1.00 33.98           C  
ANISOU 2915  CD  PRO A 363     5882   3412   3617    107   -100    678       C  
ATOM   2916  N   ARG A 364       1.531   0.343  -5.498  1.00 37.15           N  
ANISOU 2916  N   ARG A 364     6678   3493   3945    394   -655    644       N  
ATOM   2917  CA  ARG A 364       2.671  -0.500  -5.048  1.00 39.93           C  
ANISOU 2917  CA  ARG A 364     7205   3682   4283    506   -900    613       C  
ATOM   2918  C   ARG A 364       3.987   0.110  -5.522  1.00 37.99           C  
ANISOU 2918  C   ARG A 364     6740   3502   4193    649  -1061    537       C  
ATOM   2919  O   ARG A 364       4.974   0.010  -4.784  1.00 37.75           O  
ANISOU 2919  O   ARG A 364     6844   3345   4154    753  -1271    504       O  
ATOM   2920  CB  ARG A 364       2.503  -1.927  -5.554  1.00 43.61           C  
ANISOU 2920  CB  ARG A 364     7740   4079   4750    487   -920    602       C  
ATOM   2921  CG  ARG A 364       1.876  -2.806  -4.487  1.00 49.30           C  
ANISOU 2921  CG  ARG A 364     8842   4610   5281    401   -899    659       C  
ATOM   2922  CD  ARG A 364       1.089  -4.021  -4.950  1.00 54.22           C  
ANISOU 2922  CD  ARG A 364     9534   5195   5873    307   -795    670       C  
ATOM   2923  NE  ARG A 364       0.952  -4.844  -3.748  1.00 60.48           N  
ANISOU 2923  NE  ARG A 364    10748   5755   6476    263   -850    713       N  
ATOM   2924  CZ  ARG A 364       0.145  -5.898  -3.588  1.00 65.74           C  
ANISOU 2924  CZ  ARG A 364    11626   6316   7037    146   -744    739       C  
ATOM   2925  NH1 ARG A 364       0.130  -6.523  -2.412  1.00 68.48           N1+
ANISOU 2925  NH1 ARG A 364    12394   6434   7192    107   -806    780       N1+
ATOM   2926  NH2 ARG A 364      -0.633  -6.308  -4.586  1.00 65.66           N  
ANISOU 2926  NH2 ARG A 364    11422   6418   7106     64   -580    721       N  
ATOM   2927  N   ALA A 365       3.980   0.722  -6.704  1.00 35.49           N  
ANISOU 2927  N   ALA A 365     6106   3365   4012    647   -964    503       N  
ATOM   2928  CA  ALA A 365       5.162   1.350  -7.335  1.00 33.85           C  
ANISOU 2928  CA  ALA A 365     5661   3237   3966    754  -1066    415       C  
ATOM   2929  C   ALA A 365       5.778   2.357  -6.376  1.00 33.48           C  
ANISOU 2929  C   ALA A 365     5667   3155   3900    814  -1157    408       C  
ATOM   2930  O   ALA A 365       5.078   3.191  -5.801  1.00 32.97           O  
ANISOU 2930  O   ALA A 365     5659   3124   3745    747  -1041    474       O  
ATOM   2931  CB  ALA A 365       4.757   2.009  -8.611  1.00 32.03           C  
ANISOU 2931  CB  ALA A 365     5147   3196   3827    703   -900    406       C  
ATOM   2932  N   PRO A 366       7.105   2.300  -6.140  1.00 33.81           N  
ANISOU 2932  N   PRO A 366     5691   3121   4034    943  -1372    319       N  
ATOM   2933  CA  PRO A 366       7.786   3.348  -5.384  1.00 34.26           C  
ANISOU 2933  CA  PRO A 366     5749   3165   4105   1005  -1462    292       C  
ATOM   2934  C   PRO A 366       7.896   4.625  -6.222  1.00 33.32           C  
ANISOU 2934  C   PRO A 366     5332   3230   4099    986  -1324    260       C  
ATOM   2935  O   PRO A 366       8.010   4.519  -7.435  1.00 32.46           O  
ANISOU 2935  O   PRO A 366     5008   3224   4103    974  -1250    212       O  
ATOM   2936  CB  PRO A 366       9.185   2.787  -5.100  1.00 35.01           C  
ANISOU 2936  CB  PRO A 366     5868   3128   4307   1153  -1738    177       C  
ATOM   2937  CG  PRO A 366       9.072   1.330  -5.442  1.00 35.59           C  
ANISOU 2937  CG  PRO A 366     6035   3111   4375   1160  -1798    171       C  
ATOM   2938  CD  PRO A 366       8.019   1.227  -6.526  1.00 34.20           C  
ANISOU 2938  CD  PRO A 366     5720   3084   4192   1037  -1548    226       C  
ATOM   2939  N   ALA A 367       7.918   5.779  -5.553  1.00 33.52           N  
ANISOU 2939  N   ALA A 367     5370   3281   4086    984  -1302    283       N  
ATOM   2940  CA  ALA A 367       8.297   7.097  -6.120  1.00 33.36           C  
ANISOU 2940  CA  ALA A 367     5103   3400   4174    987  -1219    239       C  
ATOM   2941  C   ALA A 367       9.621   6.984  -6.908  1.00 34.14           C  
ANISOU 2941  C   ALA A 367     4987   3515   4469   1076  -1327     93       C  
ATOM   2942  O   ALA A 367       9.718   7.505  -8.034  1.00 33.34           O  
ANISOU 2942  O   ALA A 367     4657   3543   4466   1042  -1200     52       O  
ATOM   2943  CB  ALA A 367       8.401   8.109  -5.003  1.00 33.44           C  
ANISOU 2943  CB  ALA A 367     5212   3377   4115   1001  -1251    265       C  
ATOM   2944  N   SER A 368      10.590   6.295  -6.319  1.00 35.76           N  
ANISOU 2944  N   SER A 368     5279   3581   4728   1184  -1556      9       N  
ATOM   2945  CA  SER A 368      11.860   5.871  -6.928  1.00 36.56           C  
ANISOU 2945  CA  SER A 368     5202   3657   5031   1278  -1690   -154       C  
ATOM   2946  C   SER A 368      11.711   5.607  -8.422  1.00 35.52           C  
ANISOU 2946  C   SER A 368     4857   3645   4993   1218  -1530   -191       C  
ATOM   2947  O   SER A 368      12.554   6.083  -9.167  1.00 36.92           O  
ANISOU 2947  O   SER A 368     4806   3888   5334   1237  -1503   -315       O  
ATOM   2948  CB  SER A 368      12.350   4.655  -6.249  1.00 39.09           C  
ANISOU 2948  CB  SER A 368     5707   3795   5349   1375  -1932   -194       C  
ATOM   2949  OG  SER A 368      13.720   4.531  -6.540  1.00 42.11           O  
ANISOU 2949  OG  SER A 368     5910   4138   5950   1487  -2094   -377       O  
ATOM   2950  N   THR A 369      10.688   4.881  -8.852  1.00 34.33           N  
ANISOU 2950  N   THR A 369     4783   3518   4744   1142  -1422    -95       N  
ATOM   2951  CA  THR A 369      10.578   4.350 -10.235  1.00 33.57           C  
ANISOU 2951  CA  THR A 369     4524   3505   4727   1094  -1309   -135       C  
ATOM   2952  C   THR A 369       9.790   5.275 -11.176  1.00 31.72           C  
ANISOU 2952  C   THR A 369     4154   3438   4459    984  -1073    -73       C  
ATOM   2953  O   THR A 369       9.511   4.808 -12.296  1.00 31.66           O  
ANISOU 2953  O   THR A 369     4053   3495   4481    932   -975    -85       O  
ATOM   2954  CB  THR A 369       9.891   2.971 -10.264  1.00 34.42           C  
ANISOU 2954  CB  THR A 369     4787   3540   4751   1071  -1330    -75       C  
ATOM   2955  CG2 THR A 369      10.406   2.042  -9.192  1.00 36.40           C  
ANISOU 2955  CG2 THR A 369     5248   3602   4981   1169  -1565    -99       C  
ATOM   2956  OG1 THR A 369       8.476   3.073 -10.101  1.00 33.81           O  
ANISOU 2956  OG1 THR A 369     4831   3509   4507    966  -1180     73       O  
ATOM   2957  N   LEU A 370       9.358   6.472 -10.760  1.00 30.65           N  
ANISOU 2957  N   LEU A 370     4028   3364   4255    948   -991     -3       N  
ATOM   2958  CA  LEU A 370       8.195   7.152 -11.429  1.00 29.55           C  
ANISOU 2958  CA  LEU A 370     3839   3353   4036    842   -788     97       C  
ATOM   2959  C   LEU A 370       8.671   8.182 -12.441  1.00 28.38           C  
ANISOU 2959  C   LEU A 370     3489   3315   3979    817   -683     35       C  
ATOM   2960  O   LEU A 370       8.015   8.331 -13.454  1.00 26.13           O  
ANISOU 2960  O   LEU A 370     3137   3121   3671    743   -551     72       O  
ATOM   2961  CB  LEU A 370       7.250   7.798 -10.409  1.00 29.16           C  
ANISOU 2961  CB  LEU A 370     3931   3297   3851    806   -742    215       C  
ATOM   2962  CG  LEU A 370       6.499   6.815  -9.516  1.00 30.09           C  
ANISOU 2962  CG  LEU A 370     4275   3311   3846    790   -785    291       C  
ATOM   2963  CD1 LEU A 370       5.387   7.500  -8.740  1.00 29.39           C  
ANISOU 2963  CD1 LEU A 370     4298   3237   3633    722   -678    395       C  
ATOM   2964  CD2 LEU A 370       5.941   5.630 -10.311  1.00 30.32           C  
ANISOU 2964  CD2 LEU A 370     4306   3344   3870    746   -743    302       C  
ATOM   2965  N   CYS A 371       9.735   8.901 -12.129  1.00 29.69           N  
ANISOU 2965  N   CYS A 371     3578   3465   4236    871   -742    -57       N  
ATOM   2966  CA  CYS A 371      10.367   9.889 -13.040  1.00 30.32           C  
ANISOU 2966  CA  CYS A 371     3478   3632   4412    840   -639   -139       C  
ATOM   2967  C   CYS A 371      11.325   9.152 -13.967  1.00 31.43           C  
ANISOU 2967  C   CYS A 371     3489   3758   4695    854   -655   -287       C  
ATOM   2968  O   CYS A 371      12.383   8.762 -13.479  1.00 33.06           O  
ANISOU 2968  O   CYS A 371     3661   3880   5021    938   -798   -410       O  
ATOM   2969  CB  CYS A 371      11.140  10.958 -12.282  1.00 30.66           C  
ANISOU 2969  CB  CYS A 371     3485   3657   4506    885   -687   -193       C  
ATOM   2970  SG  CYS A 371      11.667  12.320 -13.351  1.00 30.82           S  
ANISOU 2970  SG  CYS A 371     3325   3780   4604    819   -518   -268       S  
ATOM   2971  N   LEU A 372      10.960   8.979 -15.238  1.00 31.64           N  
ANISOU 2971  N   LEU A 372     3452   3858   4714    775   -522   -284       N  
ATOM   2972  CA  LEU A 372      11.816   8.285 -16.236  1.00 33.51           C  
ANISOU 2972  CA  LEU A 372     3566   4085   5082    769   -504   -432       C  
ATOM   2973  C   LEU A 372      13.008   9.168 -16.610  1.00 34.13           C  
ANISOU 2973  C   LEU A 372     3488   4180   5300    761   -448   -588       C  
ATOM   2974  O   LEU A 372      14.110   8.607 -16.840  1.00 37.18           O  
ANISOU 2974  O   LEU A 372     3761   4512   5853    799   -501   -762       O  
ATOM   2975  CB  LEU A 372      11.028   7.959 -17.497  1.00 34.14           C  
ANISOU 2975  CB  LEU A 372     3643   4237   5090    673   -366   -379       C  
ATOM   2976  CG  LEU A 372       9.784   7.095 -17.299  1.00 35.39           C  
ANISOU 2976  CG  LEU A 372     3935   4390   5124    662   -393   -241       C  
ATOM   2977  CD1 LEU A 372       9.133   6.801 -18.667  1.00 36.30           C  
ANISOU 2977  CD1 LEU A 372     4027   4577   5189    570   -267   -215       C  
ATOM   2978  CD2 LEU A 372      10.099   5.825 -16.495  1.00 35.64           C  
ANISOU 2978  CD2 LEU A 372     4039   4309   5195    746   -558   -273       C  
ATOM   2979  N   ARG A 373      12.794  10.479 -16.702  1.00 32.51           N  
ANISOU 2979  N   ARG A 373     3273   4041   5040    708   -338   -538       N  
ATOM   2980  CA  ARG A 373      13.783  11.394 -17.299  1.00 32.48           C  
ANISOU 2980  CA  ARG A 373     3132   4062   5147    663   -230   -679       C  
ATOM   2981  C   ARG A 373      13.543  12.844 -16.893  1.00 30.53           C  
ANISOU 2981  C   ARG A 373     2911   3858   4831    638   -167   -606       C  
ATOM   2982  O   ARG A 373      12.386  13.256 -16.783  1.00 29.16           O  
ANISOU 2982  O   ARG A 373     2846   3730   4504    610   -130   -437       O  
ATOM   2983  CB  ARG A 373      13.683  11.309 -18.819  1.00 34.32           C  
ANISOU 2983  CB  ARG A 373     3325   4350   5364    552    -56   -712       C  
ATOM   2984  CG  ARG A 373      14.980  11.640 -19.537  1.00 36.67           C  
ANISOU 2984  CG  ARG A 373     3472   4637   5824    503     48   -924       C  
ATOM   2985  CD  ARG A 373      15.955  10.523 -19.303  1.00 39.78           C  
ANISOU 2985  CD  ARG A 373     3758   4952   6404    582    -73  -1097       C  
ATOM   2986  NE  ARG A 373      17.316  11.004 -19.306  1.00 43.04           N  
ANISOU 2986  NE  ARG A 373     4004   5331   7019    585    -43  -1318       N  
ATOM   2987  CZ  ARG A 373      18.345  10.259 -18.955  1.00 45.39           C  
ANISOU 2987  CZ  ARG A 373     4175   5548   7523    670   -170  -1505       C  
ATOM   2988  NH1 ARG A 373      18.145   9.003 -18.553  1.00 45.00           N1+
ANISOU 2988  NH1 ARG A 373     4173   5440   7486    763   -342  -1480       N1+
ATOM   2989  NH2 ARG A 373      19.554  10.802 -18.995  1.00 46.94           N  
ANISOU 2989  NH2 ARG A 373     4201   5718   7917    663   -128  -1722       N  
ATOM   2990  N   THR A 374      14.635  13.595 -16.758  1.00 29.71           N  
ANISOU 2990  N   THR A 374     2697   3738   4855    644   -147   -747       N  
ATOM   2991  CA  THR A 374      14.643  15.064 -16.588  1.00 28.38           C  
ANISOU 2991  CA  THR A 374     2527   3607   4648    604    -57   -717       C  
ATOM   2992  C   THR A 374      15.392  15.687 -17.764  1.00 28.56           C  
ANISOU 2992  C   THR A 374     2449   3658   4747    498    130   -853       C  
ATOM   2993  O   THR A 374      16.581  15.312 -17.995  1.00 30.02           O  
ANISOU 2993  O   THR A 374     2492   3799   5114    504    130  -1059       O  
ATOM   2994  CB  THR A 374      15.256  15.442 -15.242  1.00 28.63           C  
ANISOU 2994  CB  THR A 374     2538   3585   4755    699   -202   -766       C  
ATOM   2995  CG2 THR A 374      15.015  16.885 -14.879  1.00 27.73           C  
ANISOU 2995  CG2 THR A 374     2455   3508   4571    668   -128   -696       C  
ATOM   2996  OG1 THR A 374      14.692  14.550 -14.283  1.00 28.43           O  
ANISOU 2996  OG1 THR A 374     2628   3511   4664    787   -375   -669       O  
ATOM   2997  N   LEU A 375      14.700  16.600 -18.459  1.00 27.43           N  
ANISOU 2997  N   LEU A 375     2382   3571   4468    405    279   -747       N  
ATOM   2998  CA  LEU A 375      15.109  17.255 -19.725  1.00 27.51           C  
ANISOU 2998  CA  LEU A 375     2371   3603   4480    276    483   -829       C  
ATOM   2999  C   LEU A 375      15.348  18.742 -19.464  1.00 27.62           C  
ANISOU 2999  C   LEU A 375     2391   3625   4479    240    565   -828       C  
ATOM   3000  O   LEU A 375      14.411  19.456 -19.157  1.00 26.53           O  
ANISOU 3000  O   LEU A 375     2361   3517   4203    246    556   -661       O  
ATOM   3001  CB  LEU A 375      14.003  17.060 -20.758  1.00 26.61           C  
ANISOU 3001  CB  LEU A 375     2385   3531   4196    203    561   -689       C  
ATOM   3002  CG  LEU A 375      13.672  15.618 -21.129  1.00 26.31           C  
ANISOU 3002  CG  LEU A 375     2351   3489   4157    224    499   -682       C  
ATOM   3003  CD1 LEU A 375      12.477  15.570 -22.049  1.00 25.53           C  
ANISOU 3003  CD1 LEU A 375     2384   3433   3884    158    557   -535       C  
ATOM   3004  CD2 LEU A 375      14.847  14.929 -21.776  1.00 27.85           C  
ANISOU 3004  CD2 LEU A 375     2423   3647   4511    187    561   -896       C  
ATOM   3005  N   VAL A 376      16.585  19.179 -19.602  1.00 29.32           N  
ANISOU 3005  N   VAL A 376     2485   3810   4845    199    649  -1023       N  
ATOM   3006  CA  VAL A 376      17.042  20.518 -19.166  1.00 29.97           C  
ANISOU 3006  CA  VAL A 376     2545   3888   4956    176    709  -1061       C  
ATOM   3007  C   VAL A 376      17.681  21.210 -20.368  1.00 30.87           C  
ANISOU 3007  C   VAL A 376     2649   3993   5088     21    949  -1185       C  
ATOM   3008  O   VAL A 376      18.884  20.981 -20.619  1.00 32.53           O  
ANISOU 3008  O   VAL A 376     2709   4167   5486    -16   1017  -1416       O  
ATOM   3009  CB  VAL A 376      18.035  20.364 -18.009  1.00 31.24           C  
ANISOU 3009  CB  VAL A 376     2558   4004   5308    280    565  -1207       C  
ATOM   3010  CG1 VAL A 376      18.339  21.716 -17.362  1.00 31.97           C  
ANISOU 3010  CG1 VAL A 376     2639   4094   5413    274    595  -1218       C  
ATOM   3011  CG2 VAL A 376      17.549  19.343 -16.992  1.00 30.52           C  
ANISOU 3011  CG2 VAL A 376     2498   3895   5202    420    331  -1116       C  
ATOM   3012  N   GLU A 377      16.889  21.968 -21.117  1.00 30.33           N  
ANISOU 3012  N   GLU A 377     2742   3947   4833    -68   1069  -1047       N  
ATOM   3013  CA  GLU A 377      17.391  22.748 -22.265  1.00 31.17           C  
ANISOU 3013  CA  GLU A 377     2900   4031   4911   -231   1306  -1141       C  
ATOM   3014  C   GLU A 377      16.809  24.161 -22.235  1.00 16.24           C  
ATOM   3015  O   GLU A 377      17.426  25.047 -22.805  1.00 32.07           O  
ANISOU 3015  O   GLU A 377     3193   4115   4879   -393   1549  -1099       O  
ATOM   3016  CB  GLU A 377      17.083  22.001 -23.560  1.00 31.74           C  
ANISOU 3016  CB  GLU A 377     3061   4103   4897   -321   1399  -1135       C  
ATOM   3017  CG  GLU A 377      17.987  20.808 -23.783  1.00 32.97           C  
ANISOU 3017  CG  GLU A 377     3053   4237   5235   -319   1404  -1335       C  
ATOM   3018  CD  GLU A 377      19.455  21.157 -24.039  1.00 35.49           C  
ANISOU 3018  CD  GLU A 377     3223   4509   5754   -412   1572  -1612       C  
ATOM   3019  OE1 GLU A 377      19.758  22.359 -24.301  1.00 35.20           O  
ANISOU 3019  OE1 GLU A 377     3244   4452   5678   -516   1733  -1645       O  
ATOM   3020  OE2 GLU A 377      20.320  20.210 -23.988  1.00 38.21           O1-
ANISOU 3020  OE2 GLU A 377     3385   4828   6303   -382   1546  -1809       O1-
ATOM   3021  N   HIS A 378      15.656  24.379 -21.626  1.00 28.99           N  
ANISOU 3021  N   HIS A 378     2864   3792   4360   -183   1231   -794       N  
ATOM   3022  CA  HIS A 378      15.111  25.745 -21.460  1.00 28.71           C  
ANISOU 3022  CA  HIS A 378     2950   3754   4205   -202   1267   -671       C  
ATOM   3023  C   HIS A 378      15.965  26.486 -20.423  1.00 29.81           C  
ANISOU 3023  C   HIS A 378     2969   3879   4478   -167   1259   -774       C  
ATOM   3024  O   HIS A 378      16.458  25.821 -19.479  1.00 31.09           O  
ANISOU 3024  O   HIS A 378     2984   4046   4785    -68   1129   -854       O  
ATOM   3025  CB  HIS A 378      13.630  25.682 -21.074  1.00 26.82           C  
ANISOU 3025  CB  HIS A 378     2816   3552   3824   -113   1123   -443       C  
ATOM   3026  CG  HIS A 378      12.719  25.525 -22.231  1.00 26.11           C  
ANISOU 3026  CG  HIS A 378     2884   3463   3574   -171   1158   -332       C  
ATOM   3027  CD2 HIS A 378      11.714  24.661 -22.461  1.00 25.27           C  
ANISOU 3027  CD2 HIS A 378     2823   3385   3392   -125   1057   -220       C  
ATOM   3028  ND1 HIS A 378      12.771  26.360 -23.320  1.00 26.83           N  
ANISOU 3028  ND1 HIS A 378     3124   3513   3556   -293   1305   -332       N  
ATOM   3029  CE1 HIS A 378      11.839  26.009 -24.186  1.00 26.57           C  
ANISOU 3029  CE1 HIS A 378     3228   3482   3384   -313   1277   -222       C  
ATOM   3030  NE2 HIS A 378      11.183  24.967 -23.686  1.00 25.52           N  
ANISOU 3030  NE2 HIS A 378     3021   3396   3279   -212   1129   -157       N  
ATOM   3031  N   SER A 379      16.097  27.807 -20.563  1.00 29.96           N  
ANISOU 3031  N   SER A 379     3064   3873   4446   -239   1376   -768       N  
ATOM   3032  CA  SER A 379      16.783  28.689 -19.594  1.00 30.03           C  
ANISOU 3032  CA  SER A 379     2981   3868   4562   -212   1374   -847       C  
ATOM   3033  C   SER A 379      15.760  29.648 -18.988  1.00 28.99           C  
ANISOU 3033  C   SER A 379     2967   3750   4297   -157   1306   -653       C  
ATOM   3034  O   SER A 379      16.126  30.765 -18.591  1.00 30.29           O  
ANISOU 3034  O   SER A 379     3134   3893   4483   -182   1366   -683       O  
ATOM   3035  CB  SER A 379      17.935  29.402 -20.236  1.00 31.63           C  
ANISOU 3035  CB  SER A 379     3150   4022   4846   -353   1587  -1039       C  
ATOM   3036  OG  SER A 379      17.494  30.170 -21.331  1.00 32.49           O  
ANISOU 3036  OG  SER A 379     3463   4099   4781   -479   1746   -959       O  
ATOM   3037  N   GLY A 380      14.521  29.209 -18.858  1.00 27.38           N  
ANISOU 3037  N   GLY A 380     2847   3579   3977    -83   1184   -471       N  
ATOM   3038  CA  GLY A 380      13.464  30.028 -18.248  1.00 26.43           C  
ANISOU 3038  CA  GLY A 380     2821   3471   3750    -23   1113   -297       C  
ATOM   3039  C   GLY A 380      12.239  29.197 -17.956  1.00 25.43           C  
ANISOU 3039  C   GLY A 380     2727   3383   3552     68    968   -147       C  
ATOM   3040  O   GLY A 380      12.151  28.054 -18.413  1.00 25.53           O  
ANISOU 3040  O   GLY A 380     2718   3410   3571     71    935   -161       O  
ATOM   3041  N   ARG A 381      11.283  29.761 -17.246  1.00 25.02           N  
ANISOU 3041  N   ARG A 381     2728   3343   3437    132    894    -13       N  
ATOM   3042  CA  ARG A 381      10.050  29.041 -16.876  1.00 24.59           C  
ANISOU 3042  CA  ARG A 381     2697   3321   3325    210    771    119       C  
ATOM   3043  C   ARG A 381       9.484  28.364 -18.111  1.00 24.30           C  
ANISOU 3043  C   ARG A 381     2729   3291   3212    167    786    162       C  
ATOM   3044  O   ARG A 381       9.571  28.965 -19.202  1.00 25.16           O  
ANISOU 3044  O   ARG A 381     2934   3372   3253     84    885    160       O  
ATOM   3045  CB  ARG A 381       9.049  30.030 -16.288  1.00 25.21           C  
ANISOU 3045  CB  ARG A 381     2841   3399   3340    252    739    243       C  
ATOM   3046  CG  ARG A 381       9.518  30.688 -15.005  1.00 25.81           C  
ANISOU 3046  CG  ARG A 381     2861   3466   3478    295    718    208       C  
ATOM   3047  CD  ARG A 381       8.669  31.883 -14.662  1.00 26.59           C  
ANISOU 3047  CD  ARG A 381     3030   3555   3517    314    726    310       C  
ATOM   3048  NE  ARG A 381       8.742  32.164 -13.232  1.00 27.19           N  
ANISOU 3048  NE  ARG A 381     3061   3632   3637    374    672    305       N  
ATOM   3049  CZ  ARG A 381       8.155  33.184 -12.640  1.00 27.03           C  
ANISOU 3049  CZ  ARG A 381     3079   3601   3590    397    676    370       C  
ATOM   3050  NH1 ARG A 381       7.442  34.027 -13.371  1.00 27.50           N1+
ANISOU 3050  NH1 ARG A 381     3217   3644   3586    374    720    444       N1+
ATOM   3051  NH2 ARG A 381       8.288  33.343 -11.332  1.00 27.31           N  
ANISOU 3051  NH2 ARG A 381     3083   3634   3659    445    631    356       N  
ATOM   3052  N   VAL A 382       8.917  27.175 -17.938  1.00 23.76           N  
ANISOU 3052  N   VAL A 382     2631   3251   3146    218    693    201       N  
ATOM   3053  CA  VAL A 382       8.215  26.461 -19.037  1.00 24.43           C  
ANISOU 3053  CA  VAL A 382     2780   3347   3157    187    687    253       C  
ATOM   3054  C   VAL A 382       6.726  26.754 -18.927  1.00 25.07           C  
ANISOU 3054  C   VAL A 382     2927   3440   3159    233    615    397       C  
ATOM   3055  O   VAL A 382       6.125  26.380 -17.887  1.00 25.30           O  
ANISOU 3055  O   VAL A 382     2907   3489   3216    304    533    444       O  
ATOM   3056  CB  VAL A 382       8.449  24.955 -18.986  1.00 24.20           C  
ANISOU 3056  CB  VAL A 382     2676   3335   3184    210    633    200       C  
ATOM   3057  CG1 VAL A 382       7.883  24.313 -20.226  1.00 24.69           C  
ANISOU 3057  CG1 VAL A 382     2806   3405   3171    163    645    235       C  
ATOM   3058  CG2 VAL A 382       9.914  24.638 -18.868  1.00 25.23           C  
ANISOU 3058  CG2 VAL A 382     2708   3447   3430    188    677     39       C  
ATOM   3059  N   PHE A 383       6.143  27.371 -19.958  1.00 25.67           N  
ANISOU 3059  N   PHE A 383     3117   3495   3141    191    639    457       N  
ATOM   3060  CA  PHE A 383       4.751  27.879 -19.912  1.00 25.64           C  
ANISOU 3060  CA  PHE A 383     3169   3490   3084    240    562    575       C  
ATOM   3061  C   PHE A 383       3.794  26.860 -20.516  1.00 26.18           C  
ANISOU 3061  C   PHE A 383     3249   3578   3120    253    487    622       C  
ATOM   3062  O   PHE A 383       2.583  26.861 -20.176  1.00 26.09           O  
ANISOU 3062  O   PHE A 383     3224   3579   3112    310    404    694       O  
ATOM   3063  CB  PHE A 383       4.674  29.222 -20.619  1.00 26.62           C  
ANISOU 3063  CB  PHE A 383     3423   3561   3130    200    605    609       C  
ATOM   3064  CG  PHE A 383       5.318  30.350 -19.845  1.00 26.93           C  
ANISOU 3064  CG  PHE A 383     3446   3580   3205    201    666    581       C  
ATOM   3065  CD1 PHE A 383       5.163  30.450 -18.468  1.00 26.03           C  
ANISOU 3065  CD1 PHE A 383     3230   3493   3166    271    626    590       C  
ATOM   3066  CD2 PHE A 383       6.045  31.340 -20.498  1.00 27.69           C  
ANISOU 3066  CD2 PHE A 383     3646   3623   3252    123    768    546       C  
ATOM   3067  CE1 PHE A 383       5.739  31.499 -17.769  1.00 26.00           C  
ANISOU 3067  CE1 PHE A 383     3215   3469   3193    271    677    563       C  
ATOM   3068  CE2 PHE A 383       6.615  32.386 -19.786  1.00 27.41           C  
ANISOU 3068  CE2 PHE A 383     3593   3568   3255    121    825    516       C  
ATOM   3069  CZ  PHE A 383       6.464  32.460 -18.424  1.00 26.55           C  
ANISOU 3069  CZ  PHE A 383     3369   3493   3226    199    774    525       C  
ATOM   3070  N   ARG A 384       4.303  26.004 -21.401  1.00 26.78           N  
ANISOU 3070  N   ARG A 384     3343   3656   3175    197    519    569       N  
ATOM   3071  CA  ARG A 384       3.409  25.127 -22.183  1.00 26.72           C  
ANISOU 3071  CA  ARG A 384     3369   3662   3123    198    451    611       C  
ATOM   3072  C   ARG A 384       4.201  24.049 -22.886  1.00 26.26           C  
ANISOU 3072  C   ARG A 384     3302   3611   3067    138    501    531       C  
ATOM   3073  O   ARG A 384       5.275  24.349 -23.422  1.00 27.01           O  
ANISOU 3073  O   ARG A 384     3435   3679   3149     65    606    453       O  
ATOM   3074  CB  ARG A 384       2.707  25.954 -23.256  1.00 28.35           C  
ANISOU 3074  CB  ARG A 384     3724   3824   3224    174    421    674       C  
ATOM   3075  CG  ARG A 384       1.562  25.207 -23.898  1.00 29.57           C  
ANISOU 3075  CG  ARG A 384     3902   3989   3346    196    317    723       C  
ATOM   3076  CD  ARG A 384       0.385  25.158 -22.982  1.00 29.81           C  
ANISOU 3076  CD  ARG A 384     3834   4046   3446    284    222    775       C  
ATOM   3077  NE  ARG A 384      -0.693  24.330 -23.504  1.00 30.42           N  
ANISOU 3077  NE  ARG A 384     3902   4137   3520    303    127    800       N  
ATOM   3078  CZ  ARG A 384      -1.768  23.999 -22.786  1.00 30.59           C  
ANISOU 3078  CZ  ARG A 384     3822   4184   3618    363     59    822       C  
ATOM   3079  NH1 ARG A 384      -1.906  24.428 -21.546  1.00 30.44           N1+
ANISOU 3079  NH1 ARG A 384     3720   4177   3670    405     81    827       N1+
ATOM   3080  NH2 ARG A 384      -2.706  23.226 -23.282  1.00 30.95           N  
ANISOU 3080  NH2 ARG A 384     3847   4240   3672    374    -21    828       N  
ATOM   3081  N   LEU A 385       3.632  22.856 -22.957  1.00 25.86           N  
ANISOU 3081  N   LEU A 385     3207   3588   3029    161    437    543       N  
ATOM   3082  CA  LEU A 385       4.141  21.787 -23.846  1.00 25.61           C  
ANISOU 3082  CA  LEU A 385     3186   3559   2986    103    473    478       C  
ATOM   3083  C   LEU A 385       2.976  20.964 -24.389  1.00 25.30           C  
ANISOU 3083  C   LEU A 385     3170   3537   2905    118    383    536       C  
ATOM   3084  O   LEU A 385       1.855  21.000 -23.842  1.00 24.17           O  
ANISOU 3084  O   LEU A 385     2995   3411   2778    181    296    608       O  
ATOM   3085  CB  LEU A 385       5.145  20.920 -23.085  1.00 25.17           C  
ANISOU 3085  CB  LEU A 385     3008   3519   3039    119    498    384       C  
ATOM   3086  CG  LEU A 385       4.611  20.190 -21.860  1.00 24.24           C  
ANISOU 3086  CG  LEU A 385     2800   3424   2985    202    408    419       C  
ATOM   3087  CD1 LEU A 385       4.111  18.815 -22.235  1.00 23.92           C  
ANISOU 3087  CD1 LEU A 385     2746   3399   2942    202    360    422       C  
ATOM   3088  CD2 LEU A 385       5.695  20.099 -20.802  1.00 24.45           C  
ANISOU 3088  CD2 LEU A 385     2742   3440   3107    235    417    341       C  
ATOM   3089  N   GLN A 386       3.268  20.290 -25.486  1.00 26.35           N  
ANISOU 3089  N   GLN A 386     3360   3661   2991     53    416    494       N  
ATOM   3090  CA  GLN A 386       2.404  19.281 -26.131  1.00 26.57           C  
ANISOU 3090  CA  GLN A 386     3405   3704   2985     52    343    521       C  
ATOM   3091  C   GLN A 386       3.339  18.156 -26.546  1.00 26.89           C  
ANISOU 3091  C   GLN A 386     3411   3749   3055      0    412    424       C  
ATOM   3092  O   GLN A 386       4.494  18.447 -26.903  1.00 27.43           O  
ANISOU 3092  O   GLN A 386     3502   3793   3127    -64    522    340       O  
ATOM   3093  CB  GLN A 386       1.699  19.906 -27.334  1.00 27.15           C  
ANISOU 3093  CB  GLN A 386     3639   3743   2935     17    301    575       C  
ATOM   3094  CG  GLN A 386       0.897  18.912 -28.156  1.00 27.13           C  
ANISOU 3094  CG  GLN A 386     3668   3749   2892      6    224    589       C  
ATOM   3095  CD  GLN A 386       0.225  19.573 -29.323  1.00 27.78           C  
ANISOU 3095  CD  GLN A 386     3928   3782   2847    -20    156    640       C  
ATOM   3096  NE2 GLN A 386       0.074  18.815 -30.394  1.00 27.89           N  
ANISOU 3096  NE2 GLN A 386     4026   3784   2788    -73    137    621       N  
ATOM   3097  OE1 GLN A 386      -0.148  20.745 -29.263  1.00 28.16           O  
ANISOU 3097  OE1 GLN A 386     4047   3795   2859      8    112    693       O  
ATOM   3098  N   PHE A 387       2.873  16.924 -26.479  1.00 26.93           N  
ANISOU 3098  N   PHE A 387     3359   3779   3093     22    355    424       N  
ATOM   3099  CA  PHE A 387       3.684  15.774 -26.904  1.00 27.58           C  
ANISOU 3099  CA  PHE A 387     3407   3860   3212    -21    408    329       C  
ATOM   3100  C   PHE A 387       2.789  14.707 -27.507  1.00 27.33           C  
ANISOU 3100  C   PHE A 387     3394   3844   3146    -26    341    357       C  
ATOM   3101  O   PHE A 387       1.599  14.751 -27.381  1.00 26.48           O  
ANISOU 3101  O   PHE A 387     3294   3752   3016     13    251    437       O  
ATOM   3102  CB  PHE A 387       4.488  15.270 -25.712  1.00 27.99           C  
ANISOU 3102  CB  PHE A 387     3329   3916   3389     32    413    268       C  
ATOM   3103  CG  PHE A 387       3.733  14.361 -24.773  1.00 28.63           C  
ANISOU 3103  CG  PHE A 387     3345   4015   3519    103    318    316       C  
ATOM   3104  CD1 PHE A 387       2.756  14.858 -23.919  1.00 28.54           C  
ANISOU 3104  CD1 PHE A 387     3326   4016   3501    158    256    406       C  
ATOM   3105  CD2 PHE A 387       4.016  13.007 -24.717  1.00 29.00           C  
ANISOU 3105  CD2 PHE A 387     3344   4056   3619    109    300    261       C  
ATOM   3106  CE1 PHE A 387       2.081  14.027 -23.038  1.00 27.97           C  
ANISOU 3106  CE1 PHE A 387     3210   3949   3466    204    195    439       C  
ATOM   3107  CE2 PHE A 387       3.339  12.185 -23.821  1.00 28.57           C  
ANISOU 3107  CE2 PHE A 387     3256   4003   3596    164    223    304       C  
ATOM   3108  CZ  PHE A 387       2.374  12.695 -22.985  1.00 27.71           C  
ANISOU 3108  CZ  PHE A 387     3152   3906   3473    205    179    392       C  
ATOM   3109  N   ASP A 388       3.426  13.769 -28.176  1.00 29.15           N  
ANISOU 3109  N   ASP A 388     3624   4067   3385    -79    394    275       N  
ATOM   3110  CA  ASP A 388       2.800  12.568 -28.772  1.00 29.36           C  
ANISOU 3110  CA  ASP A 388     3659   4105   3391    -94    346    278       C  
ATOM   3111  C   ASP A 388       3.791  11.418 -28.617  1.00 19.45           C  
ATOM   3112  O   ASP A 388       4.782  11.561 -27.855  1.00 30.62           O  
ANISOU 3112  O   ASP A 388     3653   4243   3736    -76    436    106       O  
ATOM   3113  CB  ASP A 388       2.374  12.870 -30.213  1.00 30.79           C  
ANISOU 3113  CB  ASP A 388     3993   4269   3439   -169    350    297       C  
ATOM   3114  CG  ASP A 388       3.467  13.398 -31.143  1.00 31.57           C  
ANISOU 3114  CG  ASP A 388     4195   4326   3473   -270    484    218       C  
ATOM   3115  OD1 ASP A 388       4.632  12.994 -30.961  1.00 31.67           O  
ANISOU 3115  OD1 ASP A 388     4130   4331   3571   -297    586    109       O  
ATOM   3116  OD2 ASP A 388       3.133  14.198 -32.058  1.00 31.36           O1-
ANISOU 3116  OD2 ASP A 388     4334   4266   3314   -323    485    259       O1-
ATOM   3117  N   GLU A 389       3.573  10.332 -29.333  1.00 29.01           N  
ANISOU 3117  N   GLU A 389     3545   4054   3423   -137    389    142       N  
ATOM   3118  CA AGLU A 389       4.367   9.083 -29.183  0.50 29.01           C  
ANISOU 3118  CA AGLU A 389     3461   4040   3521   -135    415     41       C  
ATOM   3119  CA BGLU A 389       4.377   9.101 -29.117  0.50 28.77           C  
ANISOU 3119  CA BGLU A 389     3427   4009   3495   -131    413     42       C  
ATOM   3120  C   GLU A 389       5.846   9.360 -29.522  1.00 18.41           C  
ATOM   3121  O   GLU A 389       6.687   8.575 -29.064  1.00 29.45           O  
ANISOU 3121  O   GLU A 389     3389   4044   3755   -158    545   -192       O  
ATOM   3122  CB AGLU A 389       3.737   7.960 -30.026  0.50 29.02           C  
ANISOU 3122  CB AGLU A 389     3500   4047   3478   -172    387     41       C  
ATOM   3123  CB BGLU A 389       3.666   7.873 -29.714  0.50 28.33           C  
ANISOU 3123  CB BGLU A 389     3390   3962   3412   -150    368     51       C  
ATOM   3124  CG AGLU A 389       2.920   6.924 -29.241  0.50 28.34           C  
ANISOU 3124  CG AGLU A 389     3354   3973   3443   -107    289     90       C  
ATOM   3125  CG BGLU A 389       2.831   8.091 -30.975  0.50 28.57           C  
ANISOU 3125  CG BGLU A 389     3545   4002   3308   -216    359     98       C  
ATOM   3126  CD AGLU A 389       1.409   7.107 -29.258  0.50 28.40           C  
ANISOU 3126  CD AGLU A 389     3398   4009   3384    -91    204    200       C  
ATOM   3127  CD BGLU A 389       1.619   9.019 -30.980  0.50 27.98           C  
ANISOU 3127  CD BGLU A 389     3534   3945   3153   -191    273    214       C  
ATOM   3128  OE1AGLU A 389       0.955   8.076 -29.923  0.50 28.60           O  
ANISOU 3128  OE1AGLU A 389     3502   4044   3322   -119    196    245       O  
ATOM   3129  OE1BGLU A 389       0.676   8.785 -30.190  0.50 27.32           O  
ANISOU 3129  OE1BGLU A 389     3388   3883   3110   -126    184    279       O  
ATOM   3130  OE2AGLU A 389       0.683   6.295 -28.585  0.50 27.69           O1-
ANISOU 3130  OE2AGLU A 389     3261   3923   3336    -52    143    232       O1-
ATOM   3131  OE2BGLU A 389       1.599   9.953 -31.841  0.50 16.95           O1-
ATOM   3132  N   PHE A 390       6.149  10.454 -30.245  1.00 29.43           N  
ANISOU 3132  N   PHE A 390     3581   4050   3550   -262    630   -105       N  
ATOM   3133  CA  PHE A 390       7.470  10.679 -30.909  1.00 30.77           C  
ANISOU 3133  CA  PHE A 390     3753   4184   3754   -354    787   -254       C  
ATOM   3134  C   PHE A 390       8.222  11.932 -30.479  1.00 30.63           C  
ANISOU 3134  C   PHE A 390     3720   4151   3768   -364    862   -289       C  
ATOM   3135  O   PHE A 390       9.418  12.092 -30.862  1.00 31.31           O  
ANISOU 3135  O   PHE A 390     3775   4203   3920   -439   1004   -439       O  
ATOM   3136  CB  PHE A 390       7.293  10.888 -32.414  1.00 32.43           C  
ANISOU 3136  CB  PHE A 390     4137   4372   3812   -480    877   -261       C  
ATOM   3137  CG  PHE A 390       6.472   9.808 -33.044  1.00 33.25           C  
ANISOU 3137  CG  PHE A 390     4287   4491   3857   -488    808   -223       C  
ATOM   3138  CD1 PHE A 390       6.975   8.520 -33.113  1.00 33.88           C  
ANISOU 3138  CD1 PHE A 390     4271   4566   4037   -490    830   -326       C  
ATOM   3139  CD2 PHE A 390       5.185  10.057 -33.487  1.00 33.73           C  
ANISOU 3139  CD2 PHE A 390     4472   4565   3780   -481    706    -92       C  
ATOM   3140  CE1 PHE A 390       6.199   7.489 -33.601  1.00 33.93           C  
ANISOU 3140  CE1 PHE A 390     4309   4585   3998   -492    763   -291       C  
ATOM   3141  CE2 PHE A 390       4.421   9.024 -34.005  1.00 34.21           C  
ANISOU 3141  CE2 PHE A 390     4557   4639   3803   -484    634    -67       C  
ATOM   3142  CZ  PHE A 390       4.927   7.744 -34.047  1.00 33.91           C  
ANISOU 3142  CZ  PHE A 390     4426   4600   3857   -493    668   -163       C  
ATOM   3143  N   GLN A 391       7.533  12.886 -29.867  1.00 29.98           N  
ANISOU 3143  N   GLN A 391     3672   4085   3632   -309    790   -166       N  
ATOM   3144  CA  GLN A 391       8.173  14.199 -29.622  1.00 30.33           C  
ANISOU 3144  CA  GLN A 391     3733   4111   3682   -334    871   -191       C  
ATOM   3145  C   GLN A 391       7.468  14.954 -28.506  1.00 28.80           C  
ANISOU 3145  C   GLN A 391     3514   3941   3487   -235    761    -67       C  
ATOM   3146  O   GLN A 391       6.267  14.718 -28.280  1.00 27.18           O  
ANISOU 3146  O   GLN A 391     3334   3763   3231   -177    642     54       O  
ATOM   3147  CB  GLN A 391       8.106  15.042 -30.889  1.00 31.87           C  
ANISOU 3147  CB  GLN A 391     4121   4270   3719   -455    976   -180       C  
ATOM   3148  CG  GLN A 391       6.737  15.644 -31.123  1.00 31.92           C  
ANISOU 3148  CG  GLN A 391     4268   4283   3577   -426    862    -12       C  
ATOM   3149  CD  GLN A 391       6.549  16.058 -32.557  1.00 33.97           C  
ANISOU 3149  CD  GLN A 391     4752   4493   3660   -543    927      0       C  
ATOM   3150  NE2 GLN A 391       5.457  15.567 -33.129  1.00 34.54           N  
ANISOU 3150  NE2 GLN A 391     4911   4573   3638   -528    812     85       N  
ATOM   3151  OE1 GLN A 391       7.360  16.812 -33.129  1.00 34.75           O  
ANISOU 3151  OE1 GLN A 391     4956   4540   3707   -649   1077    -71       O  
ATOM   3152  N   ILE A 392       8.225  15.851 -27.889  1.00 28.51           N  
ANISOU 3152  N   ILE A 392     3430   3891   3513   -227    814   -113       N  
ATOM   3153  CA  ILE A 392       7.713  16.969 -27.064  1.00 28.25           C  
ANISOU 3153  CA  ILE A 392     3413   3868   3454   -167    757     -9       C  
ATOM   3154  C   ILE A 392       7.991  18.262 -27.824  1.00 28.71           C  
ANISOU 3154  C   ILE A 392     3604   3890   3415   -259    869    -14       C  
ATOM   3155  O   ILE A 392       9.109  18.440 -28.333  1.00 29.52           O  
ANISOU 3155  O   ILE A 392     3708   3959   3550   -349   1014   -145       O  
ATOM   3156  CB  ILE A 392       8.408  17.022 -25.691  1.00 28.26           C  
ANISOU 3156  CB  ILE A 392     3268   3873   3598    -87    723    -62       C  
ATOM   3157  CG1 ILE A 392       8.281  15.708 -24.925  1.00 27.79           C  
ANISOU 3157  CG1 ILE A 392     3107   3826   3625     -3    614    -70       C  
ATOM   3158  CG2 ILE A 392       7.885  18.194 -24.875  1.00 28.05           C  
ANISOU 3158  CG2 ILE A 392     3265   3855   3538    -35    678     40       C  
ATOM   3159  CD1 ILE A 392       9.342  15.521 -23.886  1.00 28.30           C  
ANISOU 3159  CD1 ILE A 392     3044   3869   3839     57    588   -175       C  
ATOM   3160  N   ILE A 393       7.028  19.176 -27.806  1.00 28.17           N  
ANISOU 3160  N   ILE A 393     3638   3820   3244   -233    806    117       N  
ATOM   3161  CA  ILE A 393       7.266  20.600 -28.143  1.00 28.14           C  
ANISOU 3161  CA  ILE A 393     3758   3773   3161   -292    887    131       C  
ATOM   3162  C   ILE A 393       6.865  21.426 -26.933  1.00 26.80           C  
ANISOU 3162  C   ILE A 393     3526   3622   3036   -196    809    208       C  
ATOM   3163  O   ILE A 393       5.731  21.268 -26.461  1.00 25.41           O  
ANISOU 3163  O   ILE A 393     3332   3475   2849   -111    677    316       O  
ATOM   3164  CB  ILE A 393       6.515  20.998 -29.416  1.00 29.02           C  
ANISOU 3164  CB  ILE A 393     4091   3842   3092   -358    878    207       C  
ATOM   3165  CG1 ILE A 393       6.946  20.120 -30.587  1.00 29.93           C  
ANISOU 3165  CG1 ILE A 393     4278   3936   3159   -462    965    122       C  
ATOM   3166  CG2 ILE A 393       6.723  22.471 -29.698  1.00 29.98           C  
ANISOU 3166  CG2 ILE A 393     4364   3904   3124   -414    949    230       C  
ATOM   3167  CD1 ILE A 393       6.488  20.625 -31.932  1.00 31.16           C  
ANISOU 3167  CD1 ILE A 393     4695   4027   3118   -555    982    173       C  
ATOM   3168  N   SER A 394       7.799  22.257 -26.474  1.00 26.81           N  
ANISOU 3168  N   SER A 394     3491   3603   3093   -218    901    140       N  
ATOM   3169  CA  SER A 394       7.715  23.048 -25.223  1.00 26.26           C  
ANISOU 3169  CA  SER A 394     3344   3547   3085   -136    851    182       C  
ATOM   3170  C   SER A 394       7.990  24.506 -25.550  1.00 27.04           C  
ANISOU 3170  C   SER A 394     3564   3597   3113   -198    941    189       C  
ATOM   3171  O   SER A 394       8.798  24.732 -26.471  1.00 28.45           O  
ANISOU 3171  O   SER A 394     3827   3731   3253   -315   1083    100       O  
ATOM   3172  CB  SER A 394       8.709  22.549 -24.234  1.00 25.77           C  
ANISOU 3172  CB  SER A 394     3109   3504   3180    -97    861     72       C  
ATOM   3173  OG  SER A 394      10.017  22.763 -24.710  1.00 26.21           O  
ANISOU 3173  OG  SER A 394     3144   3526   3290   -189   1008    -80       O  
ATOM   3174  N   SER A 395       7.349  25.438 -24.845  1.00 26.54           N  
ANISOU 3174  N   SER A 395     3516   3534   3034   -132    874    285       N  
ATOM   3175  CA  SER A 395       7.619  26.893 -24.966  1.00 27.64           C  
ANISOU 3175  CA  SER A 395     3762   3621   3118   -178    951    295       C  
ATOM   3176  C   SER A 395       7.883  27.493 -23.592  1.00 27.14           C  
ANISOU 3176  C   SER A 395     3574   3579   3158   -105    930    289       C  
ATOM   3177  O   SER A 395       7.489  26.885 -22.577  1.00 27.42           O  
ANISOU 3177  O   SER A 395     3483   3664   3272     -9    828    317       O  
ATOM   3178  CB  SER A 395       6.513  27.616 -25.690  1.00 28.28           C  
ANISOU 3178  CB  SER A 395     4032   3660   3054   -177    883    421       C  
ATOM   3179  OG  SER A 395       5.333  27.686 -24.923  1.00 28.12           O  
ANISOU 3179  OG  SER A 395     3954   3672   3058    -59    732    528       O  
ATOM   3180  N   SER A 396       8.513  28.655 -23.556  1.00 27.80           N  
ANISOU 3180  N   SER A 396     3709   3620   3233   -157   1029    252       N  
ATOM   3181  CA  SER A 396       9.216  29.122 -22.341  1.00 28.07           C  
ANISOU 3181  CA  SER A 396     3609   3669   3386   -116   1047    190       C  
ATOM   3182  C   SER A 396       9.362  30.649 -22.295  1.00 28.16           C  
ANISOU 3182  C   SER A 396     3718   3630   3352   -153   1119    210       C  
ATOM   3183  O   SER A 396       9.335  31.327 -23.356  1.00 28.94           O  
ANISOU 3183  O   SER A 396     3997   3665   3332   -243   1201    228       O  
ATOM   3184  CB  SER A 396      10.550  28.443 -22.262  1.00 28.81           C  
ANISOU 3184  CB  SER A 396     3572   3771   3604   -161   1131     20       C  
ATOM   3185  OG  SER A 396      11.399  29.120 -21.358  1.00 30.21           O  
ANISOU 3185  OG  SER A 396     3652   3941   3886   -149   1171    -64       O  
ATOM   3186  N   HIS A 397       9.555  31.150 -21.077  1.00 26.67           N  
ANISOU 3186  N   HIS A 397     3425   3460   3249    -88   1088    202       N  
ATOM   3187  CA  HIS A 397       9.901  32.559 -20.778  1.00 27.01           C  
ANISOU 3187  CA  HIS A 397     3518   3460   3284   -116   1162    194       C  
ATOM   3188  C   HIS A 397      11.197  32.955 -21.506  1.00 27.40           C  
ANISOU 3188  C   HIS A 397     3604   3458   3348   -253   1348     49       C  
ATOM   3189  O   HIS A 397      11.374  34.148 -21.775  1.00 27.23           O  
ANISOU 3189  O   HIS A 397     3703   3378   3267   -317   1440     54       O  
ATOM   3190  CB  HIS A 397       9.974  32.742 -19.260  1.00 26.51           C  
ANISOU 3190  CB  HIS A 397     3312   3434   3326    -20   1088    190       C  
ATOM   3191  CG  HIS A 397      10.576  34.039 -18.872  1.00 27.41           C  
ANISOU 3191  CG  HIS A 397     3444   3510   3462    -54   1173    147       C  
ATOM   3192  CD2 HIS A 397      10.070  35.283 -18.876  1.00 28.36           C  
ANISOU 3192  CD2 HIS A 397     3679   3587   3509    -57   1188    229       C  
ATOM   3193  ND1 HIS A 397      11.917  34.146 -18.562  1.00 28.58           N  
ANISOU 3193  ND1 HIS A 397     3487   3650   3723   -104   1266    -13       N  
ATOM   3194  CE1 HIS A 397      12.219  35.402 -18.338  1.00 29.61           C  
ANISOU 3194  CE1 HIS A 397     3663   3739   3847   -139   1342    -26       C  
ATOM   3195  NE2 HIS A 397      11.097  36.122 -18.532  1.00 29.87           N  
ANISOU 3195  NE2 HIS A 397     3839   3749   3760   -111   1297    126       N  
ATOM   3196  N   ASP A 398      12.082  31.990 -21.776  1.00 27.58           N  
ANISOU 3196  N   ASP A 398     3522   3498   3458   -299   1407    -88       N  
ATOM   3197  CA  ASP A 398      13.386  32.216 -22.455  1.00 28.50           C  
ANISOU 3197  CA  ASP A 398     3640   3567   3622   -440   1605   -265       C  
ATOM   3198  C   ASP A 398      13.143  32.586 -23.923  1.00 14.89           C  
ATOM   3199  O   ASP A 398      14.103  32.757 -24.661  1.00 30.25           O  
ANISOU 3199  O   ASP A 398     4147   3667   3679   -712   1912   -369       O  
ATOM   3200  CB  ASP A 398      14.295  30.999 -22.283  1.00 28.64           C  
ANISOU 3200  CB  ASP A 398     3461   3619   3801   -435   1611   -428       C  
ATOM   3201  CG  ASP A 398      13.822  29.756 -23.012  1.00 28.66           C  
ANISOU 3201  CG  ASP A 398     3488   3645   3756   -432   1562   -394       C  
ATOM   3202  OD1 ASP A 398      12.976  29.906 -23.923  1.00 29.13           O  
ANISOU 3202  OD1 ASP A 398     3738   3682   3648   -471   1565   -275       O  
ATOM   3203  OD2 ASP A 398      14.295  28.651 -22.659  1.00 28.30           O1-
ANISOU 3203  OD2 ASP A 398     3278   3634   3842   -385   1509   -490       O1-
ATOM   3204  N   ASP A 399      11.887  32.681 -24.336  1.00 29.06           N  
ANISOU 3204  N   ASP A 399     4112   3560   3370   -524   1611    -53       N  
ATOM   3205  CA  ASP A 399      11.457  33.181 -25.668  1.00 30.23           C  
ANISOU 3205  CA  ASP A 399     4540   3624   3322   -626   1674     15       C  
ATOM   3206  C   ASP A 399      11.773  32.144 -26.742  1.00 15.36           C  
ATOM   3207  O   ASP A 399      11.810  32.547 -27.912  1.00 33.67           O  
ANISOU 3207  O   ASP A 399     5262   3967   3565   -845   1858    -57       O  
ATOM   3208  CB  ASP A 399      12.101  34.527 -25.987  1.00 31.41           C  
ANISOU 3208  CB  ASP A 399     4841   3681   3412   -745   1843    -34       C  
ATOM   3209  CG  ASP A 399      11.301  35.387 -26.945  1.00 32.56           C  
ANISOU 3209  CG  ASP A 399     5304   3727   3339   -792   1827     99       C  
ATOM   3210  OD1 ASP A 399      10.071  35.575 -26.696  1.00 31.20           O  
ANISOU 3210  OD1 ASP A 399     5179   3565   3109   -667   1632    260       O  
ATOM   3211  OD2 ASP A 399      11.922  35.882 -27.947  1.00 34.86           O1-
ANISOU 3211  OD2 ASP A 399     5806   3920   3520   -959   2012     31       O1-
ATOM   3212  N   THR A 400      11.942  30.865 -26.382  1.00 29.64           N  
ANISOU 3212  N   THR A 400     4310   3619   3334   -659   1690   -119       N  
ATOM   3213  CA  THR A 400      12.211  29.783 -27.347  1.00 30.17           C  
ANISOU 3213  CA  THR A 400     4399   3683   3380   -737   1753   -194       C  
ATOM   3214  C   THR A 400      11.033  28.818 -27.406  1.00 29.51           C  
ANISOU 3214  C   THR A 400     4312   3652   3247   -631   1561    -63       C  
ATOM   3215  O   THR A 400      10.331  28.698 -26.410  1.00 28.74           O  
ANISOU 3215  O   THR A 400     4101   3612   3207   -491   1399     30       O  
ATOM   3216  CB  THR A 400      13.492  29.033 -26.988  1.00 30.65           C  
ANISOU 3216  CB  THR A 400     4229   3775   3641   -768   1853   -401       C  
ATOM   3217  CG2 THR A 400      14.689  29.956 -26.889  1.00 31.80           C  
ANISOU 3217  CG2 THR A 400     4346   3871   3866   -875   2047   -559       C  
ATOM   3218  OG1 THR A 400      13.273  28.319 -25.767  1.00 29.12           O  
ANISOU 3218  OG1 THR A 400     3813   3662   3588   -609   1679   -378       O  
ATOM   3219  N   ILE A 401      10.850  28.150 -28.547  1.00 30.16           N  
ANISOU 3219  N   ILE A 401     4520   3711   3228   -706   1592    -66       N  
ATOM   3220  CA  ILE A 401      10.106  26.868 -28.641  1.00 29.62           C  
ANISOU 3220  CA  ILE A 401     4387   3701   3166   -629   1451    -11       C  
ATOM   3221  C   ILE A 401      11.144  25.790 -28.880  1.00 30.26           C  
ANISOU 3221  C   ILE A 401     4333   3800   3363   -692   1564   -183       C  
ATOM   3222  O   ILE A 401      12.026  26.011 -29.737  1.00 32.57           O  
ANISOU 3222  O   ILE A 401     4717   4032   3624   -844   1760   -308       O  
ATOM   3223  CB  ILE A 401       9.079  26.901 -29.770  1.00 30.80           C  
ANISOU 3223  CB  ILE A 401     4781   3804   3116   -659   1383    109       C  
ATOM   3224  CG1 ILE A 401       7.935  27.854 -29.433  1.00 31.65           C  
ANISOU 3224  CG1 ILE A 401     4986   3896   3145   -564   1229    273       C  
ATOM   3225  CG2 ILE A 401       8.557  25.511 -30.071  1.00 30.22           C  
ANISOU 3225  CG2 ILE A 401     4647   3783   3055   -618   1286    124       C  
ATOM   3226  CD1 ILE A 401       7.145  28.345 -30.648  1.00 32.92           C  
ANISOU 3226  CD1 ILE A 401     5445   3968   3094   -614   1177    372       C  
ATOM   3227  N   LEU A 402      11.028  24.678 -28.164  1.00 29.22           N  
ANISOU 3227  N   LEU A 402     4004   3739   3359   -587   1449   -195       N  
ATOM   3228  CA  LEU A 402      11.939  23.525 -28.308  1.00 29.69           C  
ANISOU 3228  CA  LEU A 402     3916   3814   3551   -620   1519   -358       C  
ATOM   3229  C   LEU A 402      11.153  22.359 -28.889  1.00 29.65           C  
ANISOU 3229  C   LEU A 402     3949   3835   3482   -597   1426   -294       C  
ATOM   3230  O   LEU A 402      10.067  22.052 -28.386  1.00 28.67           O  
ANISOU 3230  O   LEU A 402     3809   3754   3329   -484   1251   -153       O  
ATOM   3231  CB  LEU A 402      12.539  23.203 -26.936  1.00 29.09           C  
ANISOU 3231  CB  LEU A 402     3592   3781   3680   -511   1447   -434       C  
ATOM   3232  CG  LEU A 402      13.580  24.215 -26.444  1.00 29.66           C  
ANISOU 3232  CG  LEU A 402     3596   3824   3850   -551   1561   -551       C  
ATOM   3233  CD1 LEU A 402      14.160  23.823 -25.100  1.00 28.74           C  
ANISOU 3233  CD1 LEU A 402     3247   3740   3932   -434   1460   -630       C  
ATOM   3234  CD2 LEU A 402      14.698  24.374 -27.476  1.00 31.74           C  
ANISOU 3234  CD2 LEU A 402     3897   4028   4135   -723   1798   -738       C  
ATOM   3235  N   ILE A 403      11.676  21.761 -29.948  1.00 31.22           N  
ANISOU 3235  N   ILE A 403     4202   4003   3656   -713   1552   -402       N  
ATOM   3236  CA  ILE A 403      11.174  20.451 -30.437  1.00 31.32           C  
ANISOU 3236  CA  ILE A 403     4208   4043   3649   -694   1478   -383       C  
ATOM   3237  C   ILE A 403      12.167  19.402 -29.955  1.00 31.77           C  
ANISOU 3237  C   ILE A 403     4033   4122   3915   -668   1507   -551       C  
ATOM   3238  O   ILE A 403      13.331  19.468 -30.377  1.00 32.96           O  
ANISOU 3238  O   ILE A 403     4143   4233   4146   -775   1685   -734       O  
ATOM   3239  CB  ILE A 403      11.037  20.415 -31.964  1.00 32.74           C  
ANISOU 3239  CB  ILE A 403     4619   4167   3653   -838   1587   -390       C  
ATOM   3240  CG1 ILE A 403      10.151  21.538 -32.487  1.00 33.19           C  
ANISOU 3240  CG1 ILE A 403     4932   4178   3501   -864   1546   -236       C  
ATOM   3241  CG2 ILE A 403      10.510  19.062 -32.406  1.00 32.99           C  
ANISOU 3241  CG2 ILE A 403     4632   4231   3673   -813   1504   -373       C  
ATOM   3242  CD1 ILE A 403      10.915  22.729 -32.969  1.00 34.40           C  
ANISOU 3242  CD1 ILE A 403     5237   4251   3583  -1000   1736   -304       C  
ATOM   3243  N   TRP A 404      11.706  18.475 -29.109  1.00 30.85           N  
ANISOU 3243  N   TRP A 404     3780   4058   3884   -534   1336   -499       N  
ATOM   3244  CA  TRP A 404      12.471  17.288 -28.662  1.00 30.72           C  
ANISOU 3244  CA  TRP A 404     3566   4051   4054   -486   1313   -638       C  
ATOM   3245  C   TRP A 404      12.022  16.093 -29.498  1.00 31.53           C  
ANISOU 3245  C   TRP A 404     3715   4162   4104   -513   1295   -630       C  
ATOM   3246  O   TRP A 404      10.865  15.653 -29.299  1.00 31.17           O  
ANISOU 3246  O   TRP A 404     3713   4151   3979   -436   1147   -477       O  
ATOM   3247  CB  TRP A 404      12.247  17.027 -27.170  1.00 28.93           C  
ANISOU 3247  CB  TRP A 404     3199   3858   3935   -326   1134   -581       C  
ATOM   3248  CG  TRP A 404      12.261  18.226 -26.277  1.00 27.89           C  
ANISOU 3248  CG  TRP A 404     3058   3729   3809   -282   1109   -529       C  
ATOM   3249  CD1 TRP A 404      11.321  19.204 -26.211  1.00 27.11           C  
ANISOU 3249  CD1 TRP A 404     3087   3642   3571   -272   1076   -369       C  
ATOM   3250  CD2 TRP A 404      13.250  18.543 -25.285  1.00 27.79           C  
ANISOU 3250  CD2 TRP A 404     2895   3704   3961   -232   1102   -643       C  
ATOM   3251  CE2 TRP A 404      12.825  19.720 -24.643  1.00 27.39           C  
ANISOU 3251  CE2 TRP A 404     2897   3662   3848   -199   1072   -535       C  
ATOM   3252  CE3 TRP A 404      14.425  17.930 -24.845  1.00 28.28           C  
ANISOU 3252  CE3 TRP A 404     2779   3742   4224   -202   1099   -831       C  
ATOM   3253  NE1 TRP A 404      11.642  20.090 -25.224  1.00 27.15           N  
ANISOU 3253  NE1 TRP A 404     3032   3646   3637   -223   1058   -370       N  
ATOM   3254  CZ2 TRP A 404      13.558  20.326 -23.619  1.00 27.33           C  
ANISOU 3254  CZ2 TRP A 404     2780   3644   3960   -150   1054   -606       C  
ATOM   3255  CZ3 TRP A 404      15.144  18.520 -23.827  1.00 28.50           C  
ANISOU 3255  CZ3 TRP A 404     2695   3756   4377   -145   1063   -905       C  
ATOM   3256  CH2 TRP A 404      14.724  19.712 -23.235  1.00 27.96           C  
ANISOU 3256  CH2 TRP A 404     2691   3700   4232   -124   1047   -793       C  
ATOM   3257  N   ASP A 405      12.875  15.580 -30.386  1.00 33.51           N  
ANISOU 3257  N   ASP A 405     3952   4379   4403   -621   1444   -796       N  
ATOM   3258  CA  ASP A 405      12.508  14.461 -31.302  1.00 34.92           C  
ANISOU 3258  CA  ASP A 405     4188   4558   4523   -664   1447   -801       C  
ATOM   3259  C   ASP A 405      13.146  13.161 -30.810  1.00 19.75           C  
ATOM   3260  O   ASP A 405      14.367  13.094 -30.743  1.00 36.88           O  
ANISOU 3260  O   ASP A 405     4097   4777   5139   -627   1499  -1130       O  
ATOM   3261  CB  ASP A 405      12.909  14.789 -32.742  1.00 36.75           C  
ANISOU 3261  CB  ASP A 405     4587   4738   4640   -848   1658   -888       C  
ATOM   3262  CG  ASP A 405      12.281  13.900 -33.796  1.00 37.28           C  
ANISOU 3262  CG  ASP A 405     4780   4802   4583   -904   1652   -851       C  
ATOM   3263  OD1 ASP A 405      11.226  13.244 -33.546  1.00 37.46           O  
ANISOU 3263  OD1 ASP A 405     4806   4867   4558   -805   1473   -711       O  
ATOM   3264  OD2 ASP A 405      12.811  13.939 -34.885  1.00 38.69           O1-
ANISOU 3264  OD2 ASP A 405     5070   4931   4700  -1056   1834   -961       O1-
ATOM   3265  N   PHE A 406      12.333  12.171 -30.451  1.00 35.76           N  
ANISOU 3265  N   PHE A 406     4068   4699   4820   -495   1232   -831       N  
ATOM   3266  CA  PHE A 406      12.772  10.850 -29.913  1.00 35.72           C  
ANISOU 3266  CA  PHE A 406     3898   4687   4986   -410   1144   -926       C  
ATOM   3267  C   PHE A 406      12.711   9.799 -31.027  1.00 36.93           C  
ANISOU 3267  C   PHE A 406     4096   4830   5108   -488   1208   -987       C  
ATOM   3268  O   PHE A 406      12.987   8.608 -30.733  1.00 36.93           O  
ANISOU 3268  O   PHE A 406     3979   4816   5236   -424   1136  -1062       O  
ATOM   3269  CB  PHE A 406      11.895  10.450 -28.722  1.00 34.22           C  
ANISOU 3269  CB  PHE A 406     3679   4527   4796   -261    932   -773       C  
ATOM   3270  CG  PHE A 406      12.066  11.356 -27.535  1.00 33.08           C  
ANISOU 3270  CG  PHE A 406     3481   4386   4702   -181    866   -735       C  
ATOM   3271  CD1 PHE A 406      13.087  11.139 -26.637  1.00 33.19           C  
ANISOU 3271  CD1 PHE A 406     3339   4366   4904   -106    816   -866       C  
ATOM   3272  CD2 PHE A 406      11.242  12.446 -27.347  1.00 32.44           C  
ANISOU 3272  CD2 PHE A 406     3506   4334   4485   -180    850   -581       C  
ATOM   3273  CE1 PHE A 406      13.275  11.981 -25.556  1.00 33.08           C  
ANISOU 3273  CE1 PHE A 406     3286   4352   4931    -36    753   -838       C  
ATOM   3274  CE2 PHE A 406      11.410  13.274 -26.249  1.00 32.56           C  
ANISOU 3274  CE2 PHE A 406     3474   4351   4547   -110    796   -552       C  
ATOM   3275  CZ  PHE A 406      12.451  13.065 -25.375  1.00 32.70           C  
ANISOU 3275  CZ  PHE A 406     3346   4338   4742    -44    755   -681       C  
ATOM   3276  N   LEU A 407      12.354  10.217 -32.251  1.00 37.92           N  
ANISOU 3276  N   LEU A 407     4397   4950   5061   -620   1331   -955       N  
ATOM   3277  CA  LEU A 407      12.239   9.320 -33.435  1.00 38.78           C  
ANISOU 3277  CA  LEU A 407     4584   5045   5107   -713   1405  -1007       C  
ATOM   3278  C   LEU A 407      13.479   9.488 -34.314  1.00 39.65           C  
ANISOU 3278  C   LEU A 407     4685   5101   5280   -863   1643  -1226       C  
ATOM   3279  O   LEU A 407      14.139   8.494 -34.583  1.00 39.50           O  
ANISOU 3279  O   LEU A 407     4556   5059   5394   -882   1697  -1385       O  
ATOM   3280  CB  LEU A 407      10.958   9.659 -34.199  1.00 39.11           C  
ANISOU 3280  CB  LEU A 407     4851   5105   4905   -759   1363   -825       C  
ATOM   3281  CG  LEU A 407      10.750   8.894 -35.508  1.00 40.29           C  
ANISOU 3281  CG  LEU A 407     5124   5234   4949   -868   1437   -863       C  
ATOM   3282  CD1 LEU A 407      10.694   7.398 -35.296  1.00 40.10           C  
ANISOU 3282  CD1 LEU A 407     4971   5226   5041   -801   1354   -908       C  
ATOM   3283  CD2 LEU A 407       9.486   9.355 -36.205  1.00 40.58           C  
ANISOU 3283  CD2 LEU A 407     5389   5280   4750   -899   1364   -687       C  
ATOM   3284  N   ASN A 408      13.712  10.708 -34.790  1.00 40.52           N  
ANISOU 3284  N   ASN A 408     4924   5185   5286   -974   1786  -1233       N  
ATOM   3285  CA  ASN A 408      14.786  11.089 -35.736  1.00 43.04           C  
ANISOU 3285  CA  ASN A 408     5290   5443   5622  -1154   2052  -1433       C  
ATOM   3286  C   ASN A 408      15.934  11.609 -34.891  1.00 44.85           C  
ANISOU 3286  C   ASN A 408     5313   5656   6071  -1124   2113  -1591       C  
ATOM   3287  O   ASN A 408      16.138  12.834 -34.818  1.00 45.16           O  
ANISOU 3287  O   ASN A 408     5425   5678   6056  -1179   2199  -1578       O  
ATOM   3288  CB  ASN A 408      14.298  12.120 -36.754  1.00 43.37           C  
ANISOU 3288  CB  ASN A 408     5631   5449   5397  -1297   2164  -1336       C  
ATOM   3289  CG  ASN A 408      13.054  11.645 -37.460  1.00 43.24           C  
ANISOU 3289  CG  ASN A 408     5810   5449   5171  -1296   2049  -1166       C  
ATOM   3290  ND2 ASN A 408      11.893  12.174 -37.087  1.00 41.60           N  
ANISOU 3290  ND2 ASN A 408     5701   5275   4831  -1202   1865   -947       N  
ATOM   3291  OD1 ASN A 408      13.149  10.783 -38.336  1.00 45.15           O  
ANISOU 3291  OD1 ASN A 408     6102   5670   5382  -1380   2124  -1245       O  
ATOM   3292  N   VAL A 409      16.655  10.684 -34.278  1.00 46.91           N  
ANISOU 3292  N   VAL A 409     5330   5916   6579  -1037   2058  -1742       N  
ATOM   3293  CA  VAL A 409      17.740  10.966 -33.304  1.00 49.52           C  
ANISOU 3293  CA  VAL A 409     5424   6229   7161   -968   2054  -1906       C  
ATOM   3294  C   VAL A 409      19.085  10.758 -33.998  1.00 54.15           C  
ANISOU 3294  C   VAL A 409     5891   6753   7928  -1104   2295  -2214       C  
ATOM   3295  O   VAL A 409      19.200   9.921 -34.894  1.00 57.71           O  
ANISOU 3295  O   VAL A 409     6369   7182   8376  -1189   2393  -2307       O  
ATOM   3296  CB  VAL A 409      17.539  10.034 -32.103  1.00 48.37           C  
ANISOU 3296  CB  VAL A 409     5108   6109   7160   -761   1791  -1858       C  
ATOM   3297  CG1 VAL A 409      18.641  10.199 -31.085  1.00 49.70           C  
ANISOU 3297  CG1 VAL A 409     5040   6249   7592   -673   1744  -2031       C  
ATOM   3298  CG2 VAL A 409      16.170  10.227 -31.477  1.00 45.80           C  
ANISOU 3298  CG2 VAL A 409     4908   5839   6654   -652   1588  -1570       C  
ATOM   3299  N   PRO A 410      20.134  11.562 -33.705  1.00 56.52           N  
ANISOU 3299  N   PRO A 410     6068   7020   8387  -1152   2423  -2394       N  
ATOM   3300  CA  PRO A 410      21.472  11.308 -34.259  1.00 59.12           C  
ANISOU 3300  CA  PRO A 410     6237   7286   8938  -1275   2653  -2724       C  
ATOM   3301  C   PRO A 410      22.621  10.718 -33.400  1.00 60.51           C  
ANISOU 3301  C   PRO A 410     6070   7433   9487  -1157   2572  -2978       C  
ATOM   3302  O   PRO A 410      23.831  10.568 -33.846  1.00 61.51           O  
ANISOU 3302  O   PRO A 410     6027   7500   9845  -1264   2777  -3296       O  
ATOM   3303  CB  PRO A 410      21.840  12.744 -34.696  1.00 61.28           C  
ANISOU 3303  CB  PRO A 410     6639   7529   9117  -1445   2892  -2768       C  
ATOM   3304  CG  PRO A 410      20.923  13.710 -33.910  1.00 58.84           C  
ANISOU 3304  CG  PRO A 410     6456   7269   8633  -1341   2715  -2490       C  
ATOM   3305  CD  PRO A 410      20.028  12.866 -33.030  1.00 56.31           C  
ANISOU 3305  CD  PRO A 410     6082   7008   8305  -1126   2397  -2294       C  
TER   
HETATM 3306  C1  GOL A 501      19.571  17.865 -21.082  1.00 59.58           C  
ANISOU 3306  C1  GOL A 501     5936   7545   9156     84    847  -1635       C  
HETATM 3307  O1  GOL A 501      19.031  17.233 -19.924  1.00 54.01           O  
ANISOU 3307  O1  GOL A 501     5257   6835   8428    240    598  -1511       O  
HETATM 3308  C2  GOL A 501      19.173  17.138 -22.358  1.00 62.55           C  
ANISOU 3308  C2  GOL A 501     6385   7936   9447    -11    966  -1616       C  
HETATM 3309  O2  GOL A 501      19.454  17.962 -23.496  1.00 62.00           O  
ANISOU 3309  O2  GOL A 501     6368   7867   9324   -183   1225  -1684       O  
HETATM 3310  C3  GOL A 501      19.863  15.789 -22.523  1.00 66.19           C  
ANISOU 3310  C3  GOL A 501     6704   8356  10091     33    904  -1791       C  
HETATM 3311  O3  GOL A 501      18.949  14.691 -22.483  1.00 64.93           O  
ANISOU 3311  O3  GOL A 501     6633   8211   9828    102    770  -1640       O  
HETATM 3312  C1  GOL A 502     -15.328  29.258  -2.814  1.00 68.19           C  
ANISOU 3312  C1  GOL A 502     7509   8571   9828    104   1600    -63       C  
HETATM 3313  O1  GOL A 502     -15.478  27.867  -2.527  1.00 68.91           O  
ANISOU 3313  O1  GOL A 502     7687   8648   9846     -5   1695    -81       O  
HETATM 3314  C2  GOL A 502     -16.616  30.058  -2.691  1.00 67.68           C  
ANISOU 3314  C2  GOL A 502     7232   8475  10006    108   1676   -221       C  
HETATM 3315  O2  GOL A 502     -16.863  30.269  -1.305  1.00 67.57           O  
ANISOU 3315  O2  GOL A 502     7294   8403   9975     -5   1900   -298       O  
HETATM 3316  C3  GOL A 502     -16.581  31.419  -3.371  1.00 65.84           C  
ANISOU 3316  C3  GOL A 502     6884   8254   9877    250   1517   -202       C  
HETATM 3317  O3  GOL A 502     -17.420  31.472  -4.521  1.00 63.92           O  
ANISOU 3317  O3  GOL A 502     6443   8024   9821    334   1374   -265       O  
HETATM 3318  C1  GOL A 503      -5.162  24.226   1.320  1.00 65.77           C  
ANISOU 3318  C1  GOL A 503     9008   8045   7936     51   1085    625       C  
HETATM 3319  O1  GOL A 503      -4.791  25.279   2.212  1.00 61.31           O  
ANISOU 3319  O1  GOL A 503     8514   7451   7330     57   1105    619       O  
HETATM 3320  C2  GOL A 503      -4.987  22.856   1.959  1.00 69.53           C  
ANISOU 3320  C2  GOL A 503     9718   8426   8273     -9   1072    636       C  
HETATM 3321  O2  GOL A 503      -5.546  21.838   1.122  1.00 68.03           O  
ANISOU 3321  O2  GOL A 503     9451   8263   8134    -30   1084    632       O  
HETATM 3322  C3  GOL A 503      -3.540  22.521   2.273  1.00 70.43           C  
ANISOU 3322  C3  GOL A 503     9984   8496   8280     63    885    677       C  
HETATM 3323  O3  GOL A 503      -3.368  22.036   3.602  1.00 71.14           O  
ANISOU 3323  O3  GOL A 503    10371   8455   8204     -1    897    679       O  
HETATM 3324 NA    NA A 504     -18.778  26.143  -4.545  1.00 30.75          NA  
HETATM 3325  O   HOH A 601       4.321  12.418  -0.692  1.00 32.30           O  
HETATM 3326  O   HOH A 602      -2.867  30.466 -18.609  1.00  7.30           O  
HETATM 3327  O   HOH A 603      -0.928   1.025 -13.228  1.00 40.22           O  
HETATM 3328  O   HOH A 604      -5.978  42.481 -12.982  1.00 13.08           O  
HETATM 3329  O   HOH A 605      -3.417 -12.824 -37.305  1.00 40.05           O  
HETATM 3330  O   HOH A 606      16.072  33.336 -26.506  1.00 23.15           O  
HETATM 3331  O   HOH A 607      16.002  23.032 -10.118  1.00 24.15           O  
HETATM 3332  O   HOH A 608      -4.065   4.766 -18.197  1.00 26.62           O  
HETATM 3333  O   HOH A 609       6.745  37.648 -26.119  1.00 42.84           O  
HETATM 3334  O   HOH A 610       0.688  14.668 -32.395  1.00 17.15           O  
HETATM 3335  O   HOH A 611       1.205  22.630 -45.785  1.00 30.03           O  
HETATM 3336  O   HOH A 612      11.830  20.896 -11.954  1.00 21.93           O  
HETATM 3337  O   HOH A 613      -3.128  29.743  -2.905  1.00 18.25           O  
HETATM 3338  O   HOH A 614      -8.503 -32.397 -39.459  1.00 34.50           O  
HETATM 3339  O   HOH A 615     -10.215  15.490  -2.821  1.00 24.72           O  
HETATM 3340  O   HOH A 616      14.109  22.337 -20.522  1.00 28.97           O  
HETATM 3341  O   HOH A 617       7.138 -18.762 -43.317  1.00 29.70           O  
HETATM 3342  O   HOH A 618      -6.513  20.745  -4.742  1.00 19.05           O  
HETATM 3343  O   HOH A 619       4.818   4.321  -3.472  1.00 28.96           O  
HETATM 3344  O   HOH A 620       8.022  17.942  -5.927  1.00 23.84           O  
HETATM 3345  O   HOH A 621       7.127  17.432  -8.731  1.00 25.85           O  
HETATM 3346  O   HOH A 622       0.059  41.747 -21.498  1.00 22.67           O  
HETATM 3347  O   HOH A 623      -3.538 -35.331 -31.271  1.00 33.91           O  
HETATM 3348  O   HOH A 624       2.837 -12.914 -51.581  1.00 49.36           O  
HETATM 3349  O   HOH A 625       2.566  42.458 -22.817  1.00 14.27           O  
HETATM 3350  O   HOH A 626      -0.148   8.988 -33.666  1.00 36.40           O  
HETATM 3351  O   HOH A 627      -2.909  20.643 -19.635  1.00 29.75           O  
HETATM 3352  O   HOH A 628      -3.229  20.660 -33.323  1.00 46.67           O  
HETATM 3353  O   HOH A 629      -2.652  39.000 -31.348  1.00 30.24           O  
HETATM 3354  O   HOH A 630      -4.951  -6.045 -46.792  1.00 41.06           O  
HETATM 3355  O   HOH A 631       1.051   6.815 -25.883  1.00 33.84           O  
HETATM 3356  O   HOH A 632     -13.935  37.817 -22.250  1.00 26.61           O  
HETATM 3357  O   HOH A 633      -6.799  22.852  -1.518  1.00 25.12           O  
HETATM 3358  O   HOH A 634      15.789  27.160 -25.201  1.00 33.72           O  
HETATM 3359  O   HOH A 635      -0.278  30.942 -19.854  1.00 19.28           O  
HETATM 3360  O   HOH A 636      19.931  22.211 -11.616  1.00 31.58           O  
HETATM 3361  O   HOH A 637     -10.101  25.164 -43.131  1.00 41.08           O  
HETATM 3362  O   HOH A 638       0.281   7.136  -4.317  1.00 23.04           O  
HETATM 3363  O   HOH A 639     -15.856  10.001 -16.438  1.00 36.17           O  
HETATM 3364  O   HOH A 640      -3.228  27.891 -18.231  1.00 15.29           O  
HETATM 3365  O   HOH A 641       0.124  15.906 -29.466  1.00 16.64           O  
HETATM 3366  O   HOH A 642       6.642   3.228 -49.586  1.00 42.26           O  
HETATM 3367  O   HOH A 643      18.046  31.204 -25.965  1.00 36.99           O  
HETATM 3368  O   HOH A 644       9.162   0.879 -39.225  1.00 16.15           O  
HETATM 3369  O   HOH A 645      -4.962 -19.299 -48.222  1.00 33.76           O  
HETATM 3370  O   HOH A 646      12.211  32.250 -16.286  1.00 33.28           O  
HETATM 3371  O   HOH A 647     -15.941  19.016 -38.043  1.00 38.46           O  
HETATM 3372  O   HOH A 648      -1.647  26.352 -25.859  1.00 33.48           O  
HETATM 3373  O   HOH A 649       4.153 -23.190 -47.009  1.00 31.76           O  
HETATM 3374  O   HOH A 650      11.841  25.882  -4.522  1.00 38.81           O  
HETATM 3375  O   HOH A 651     -14.440  35.127  -5.415  1.00 29.69           O  
HETATM 3376  O   HOH A 652     -18.803  24.602 -34.194  1.00 50.32           O  
HETATM 3377  O   HOH A 653      -0.227  28.253 -20.645  1.00 33.87           O  
HETATM 3378  O   HOH A 654       0.899  22.027 -21.308  1.00 29.60           O  
HETATM 3379  O   HOH A 655     -15.636  19.578 -32.484  1.00 35.09           O  
HETATM 3380  O   HOH A 656     -15.975  11.003 -18.689  1.00 15.58           O  
HETATM 3381  O   HOH A 657       6.327   5.984 -27.773  1.00 35.60           O  
HETATM 3382  O   HOH A 658      13.743  29.561 -15.151  1.00 46.88           O  
HETATM 3383  O   HOH A 659       1.760 -17.291 -28.473  1.00 29.28           O  
HETATM 3384  O   HOH A 660      -7.650 -16.340 -50.375  1.00 33.81           O  
HETATM 3385  O   HOH A 661      13.038  23.232  -3.990  1.00 40.23           O  
HETATM 3386  O   HOH A 662      14.443   5.959 -33.081  1.00 35.50           O  
HETATM 3387  O   HOH A 663     -14.828  25.395 -35.165  1.00 38.81           O  
HETATM 3388  O   HOH A 664      10.030  -1.460 -25.540  1.00 33.03           O  
HETATM 3389  O   HOH A 665      17.235  33.122 -21.174  1.00 31.01           O  
HETATM 3390  O   HOH A 666      -1.929  25.324 -17.530  1.00 29.61           O  
HETATM 3391  O   HOH A 667      14.561  30.649 -39.512  1.00 36.85           O  
HETATM 3392  O   HOH A 668      -2.775   8.220 -25.792  1.00 31.10           O  
HETATM 3393  O   HOH A 669       6.107 -19.430 -46.127  1.00 50.68           O  
HETATM 3394  O   HOH A 670       2.991  11.133 -37.136  1.00 32.98           O  
HETATM 3395  O   HOH A 671      13.421  29.662 -36.516  1.00 33.84           O  
HETATM 3396  O   HOH A 672       0.119  25.398 -19.209  1.00 20.76           O  
HETATM 3397  O   HOH A 673      13.463  36.277 -21.123  1.00 38.40           O  
HETATM 3398  O   HOH A 674      -8.445 -11.419 -48.336  1.00 29.04           O  
HETATM 3399  O   HOH A 675      -5.165  22.331 -21.011  1.00 15.26           O  
HETATM 3400  O   HOH A 676      -9.373  38.414  -8.762  1.00 44.43           O  
HETATM 3401  O   HOH A 677     -17.857  19.139  -3.061  1.00 33.64           O  
HETATM 3402  O   HOH A 678      -6.304  41.428 -15.496  1.00 34.19           O  
HETATM 3403  O   HOH A 679     -26.850  24.357 -18.820  1.00 39.56           O  
HETATM 3404  O   HOH A 680      -0.375  22.771 -19.199  1.00 20.03           O  
HETATM 3405  O   HOH A 681     -22.514  10.021 -13.160  1.00 33.92           O  
HETATM 3406  O   HOH A 682      13.858  19.262 -10.540  1.00 37.64           O  
HETATM 3407  O   HOH A 683      -3.744  43.575 -21.474  1.00 37.52           O  
HETATM 3408  O   HOH A 684      20.200  26.395 -22.209  1.00 32.74           O  
HETATM 3409  O   HOH A 685     -16.647  12.833 -24.100  1.00 24.56           O  
HETATM 3410  O   HOH A 686       8.739  26.841  -5.440  1.00 28.68           O  
HETATM 3411  O   HOH A 687      -3.187  23.200 -18.438  1.00 18.77           O  
HETATM 3412  O   HOH A 688      -2.853  16.634   4.744  1.00 50.39           O  
HETATM 3413  O   HOH A 689      -0.861  21.246 -25.532  1.00 21.33           O  
HETATM 3414  O   HOH A 690       9.466 -22.987 -45.324  1.00 39.54           O  
HETATM 3415  O   HOH A 691      -3.076  20.120 -28.098  1.00 31.37           O  
HETATM 3416  O   HOH A 692      15.052  34.154 -19.491  1.00 28.29           O  
HETATM 3417  O   HOH A 693       4.499  16.054 -36.220  1.00 27.91           O  
HETATM 3418  O   HOH A 694     -11.913  40.092 -40.981  1.00 57.27           O  
HETATM 3419  O   HOH A 695       6.215  25.288  -2.385  1.00 38.75           O  
HETATM 3420  O   HOH A 696      14.968  23.107 -40.533  1.00 32.02           O  
HETATM 3421  O   HOH A 697     -12.296  13.734  -1.785  1.00 18.91           O  
HETATM 3422  O   HOH A 698      20.560  27.753 -29.905  1.00 23.64           O  
HETATM 3423  O   HOH A 699       1.378   2.389 -27.829  1.00 20.54           O  
HETATM 3424  O   HOH A 700     -20.535  22.657 -33.357  1.00 41.95           O  
HETATM 3425  O   HOH A 701      13.427  -6.491 -31.908  1.00 45.82           O  
HETATM 3426  O   HOH A 702       6.876  23.044  -1.195  1.00 31.70           O  
HETATM 3427  O   HOH A 703     -16.956  13.651  -3.468  1.00 28.84           O  
HETATM 3428  O   HOH A 704      16.915  26.779 -12.269  1.00 31.93           O  
HETATM 3429  O   HOH A 705      -2.878  27.688 -22.952  1.00 31.74           O  
HETATM 3430  O   HOH A 706     -19.161  23.923 -37.133  1.00 36.57           O  
HETATM 3431  O   HOH A 707      -6.487 -12.908 -49.413  1.00 35.37           O  
HETATM 3432  O   HOH A 708       6.650   2.181  -2.437  1.00 35.06           O  
HETATM 3433  O   HOH A 709      16.921   0.842 -34.396  1.00 40.54           O  
HETATM 3434  O   HOH A 710      -9.853  43.312  -8.713  1.00 35.03           O  
HETATM 3435  O   HOH A 711      10.824   1.160 -41.067  1.00 15.11           O  
HETATM 3436  O   HOH A 712      -9.705  44.855 -10.912  1.00 33.59           O  
HETATM 3437  O   HOH A 713       3.848  21.011 -45.292  1.00 45.75           O  
HETATM 3438  O   HOH A 714       9.091  36.232 -36.945  1.00 30.10           O  
ATOM   3439  N   PRO B   2     -45.117 -15.471 -39.646  1.00 80.67           N  
ANISOU 3439  N   PRO B   2     6661  12336  11653   2610    839  -2422       N  
ATOM   3440  CA  PRO B   2     -45.478 -16.900 -39.478  1.00 78.93           C  
ANISOU 3440  CA  PRO B   2     6378  12451  11161   2340   1041  -2261       C  
ATOM   3441  C   PRO B   2     -44.303 -17.796 -39.047  1.00 74.86           C  
ANISOU 3441  C   PRO B   2     6148  11976  10318   2067   1159  -2015       C  
ATOM   3442  O   PRO B   2     -43.305 -17.274 -38.585  1.00 75.10           O  
ANISOU 3442  O   PRO B   2     6379  11873  10282   2091   1144  -2047       O  
ATOM   3443  CB  PRO B   2     -45.964 -17.332 -40.880  1.00 78.21           C  
ANISOU 3443  CB  PRO B   2     6264  12231  11221   2332    852  -2023       C  
ATOM   3444  CG  PRO B   2     -46.554 -16.070 -41.473  1.00 80.95           C  
ANISOU 3444  CG  PRO B   2     6467  12352  11936   2646    620  -2183       C  
ATOM   3445  CD  PRO B   2     -45.693 -14.952 -40.913  1.00 81.75           C  
ANISOU 3445  CD  PRO B   2     6722  12220  12121   2790    565  -2329       C  
ATOM   3446  N   SER B   3     -44.488 -19.113 -39.176  1.00 71.54           N  
ANISOU 3446  N   SER B   3     5714  11731   9736   1819   1259  -1791       N  
ATOM   3447  CA  SER B   3     -43.422 -20.147 -39.149  1.00 67.34           C  
ANISOU 3447  CA  SER B   3     5450  11154   8982   1562   1295  -1487       C  
ATOM   3448  C   SER B   3     -43.199 -20.654 -40.569  1.00 63.67           C  
ANISOU 3448  C   SER B   3     5114  10449   8629   1526   1098  -1239       C  
ATOM   3449  O   SER B   3     -44.069 -20.427 -41.429  1.00 64.07           O  
ANISOU 3449  O   SER B   3     5005  10465   8874   1647    973  -1283       O  
ATOM   3450  CB  SER B   3     -43.747 -21.289 -38.228  1.00 68.66           C  
ANISOU 3450  CB  SER B   3     5497  11666   8923   1300   1526  -1408       C  
ATOM   3451  OG  SER B   3     -42.969 -21.217 -37.043  1.00 69.37           O  
ANISOU 3451  OG  SER B   3     5701  11893   8764   1215   1665  -1434       O  
ATOM   3452  N   ILE B   4     -42.056 -21.296 -40.795  1.00 59.07           N  
ANISOU 3452  N   ILE B   4     4797   9727   7920   1373   1064  -1007       N  
ATOM   3453  CA  ILE B   4     -41.627 -21.788 -42.136  1.00 55.86           C  
ANISOU 3453  CA  ILE B   4     4531   9120   7572   1335    884   -803       C  
ATOM   3454  C   ILE B   4     -40.819 -23.061 -41.928  1.00 53.23           C  
ANISOU 3454  C   ILE B   4     4347   8789   7088   1088    950   -607       C  
ATOM   3455  O   ILE B   4     -40.100 -23.149 -40.926  1.00 52.87           O  
ANISOU 3455  O   ILE B   4     4412   8782   6894    999   1065   -577       O  
ATOM   3456  CB  ILE B   4     -40.827 -20.717 -42.897  1.00 54.65           C  
ANISOU 3456  CB  ILE B   4     4568   8698   7498   1507    695   -759       C  
ATOM   3457  CG1 ILE B   4     -39.542 -20.323 -42.168  1.00 53.90           C  
ANISOU 3457  CG1 ILE B   4     4700   8491   7287   1480    742   -730       C  
ATOM   3458  CG2 ILE B   4     -41.687 -19.500 -43.185  1.00 57.55           C  
ANISOU 3458  CG2 ILE B   4     4769   9012   8085   1755    581   -921       C  
ATOM   3459  CD1 ILE B   4     -38.304 -21.010 -42.680  1.00 51.79           C  
ANISOU 3459  CD1 ILE B   4     4672   8100   6906   1340    691   -506       C  
ATOM   3460  N   LYS B   5     -40.919 -24.008 -42.853  1.00 51.68           N  
ANISOU 3460  N   LYS B   5     4146   8547   6943    989    860   -493       N  
ATOM   3461  CA  LYS B   5     -40.325 -25.361 -42.695  1.00 50.01           C  
ANISOU 3461  CA  LYS B   5     4021   8310   6669    755    897   -333       C  
ATOM   3462  C   LYS B   5     -38.856 -25.371 -43.163  1.00 46.51           C  
ANISOU 3462  C   LYS B   5     3854   7657   6159    758    803   -221       C  
ATOM   3463  O   LYS B   5     -38.581 -24.997 -44.316  1.00 45.90           O  
ANISOU 3463  O   LYS B   5     3847   7473   6118    869    653   -220       O  
ATOM   3464  CB  LYS B   5     -41.243 -26.323 -43.448  1.00 51.27           C  
ANISOU 3464  CB  LYS B   5     3999   8518   6966    665    832   -331       C  
ATOM   3465  CG  LYS B   5     -42.565 -26.567 -42.750  1.00 54.59           C  
ANISOU 3465  CG  LYS B   5     4131   9170   7441    590    964   -398       C  
ATOM   3466  CD  LYS B   5     -43.782 -26.192 -43.536  1.00 56.83           C  
ANISOU 3466  CD  LYS B   5     4187   9532   7874    721    875   -539       C  
ATOM   3467  CE  LYS B   5     -45.029 -26.259 -42.671  1.00 59.51           C  
ANISOU 3467  CE  LYS B   5     4218  10140   8252    662   1041   -628       C  
ATOM   3468  NZ  LYS B   5     -45.898 -27.408 -43.034  1.00 61.01           N1+
ANISOU 3468  NZ  LYS B   5     4195  10399   8587    479   1016   -584       N1+
ATOM   3469  N   LEU B   6     -37.935 -25.770 -42.292  1.00 44.61           N  
ANISOU 3469  N   LEU B   6     3751   7386   5811    636    884   -121       N  
ATOM   3470  CA  LEU B   6     -36.534 -26.086 -42.688  1.00 42.16           C  
ANISOU 3470  CA  LEU B   6     3665   6892   5461    600    803    -11       C  
ATOM   3471  C   LEU B   6     -36.358 -27.600 -42.682  1.00 43.13           C  
ANISOU 3471  C   LEU B   6     3769   6970   5648    402    792     98       C  
ATOM   3472  O   LEU B   6     -36.893 -28.261 -41.777  1.00 45.87           O  
ANISOU 3472  O   LEU B   6     4004   7421   6002    249    890    167       O  
ATOM   3473  CB  LEU B   6     -35.533 -25.432 -41.740  1.00 40.22           C  
ANISOU 3473  CB  LEU B   6     3583   6613   5086    616    865     19       C  
ATOM   3474  CG  LEU B   6     -35.708 -23.933 -41.565  1.00 40.03           C  
ANISOU 3474  CG  LEU B   6     3561   6597   5052    804    866   -115       C  
ATOM   3475  CD1 LEU B   6     -34.608 -23.365 -40.693  1.00 38.69           C  
ANISOU 3475  CD1 LEU B   6     3556   6373   4771    805    900   -106       C  
ATOM   3476  CD2 LEU B   6     -35.750 -23.247 -42.916  1.00 39.64           C  
ANISOU 3476  CD2 LEU B   6     3532   6425   5105    957    710   -128       C  
ATOM   3477  N   GLN B   7     -35.650 -28.106 -43.686  1.00 41.68           N  
ANISOU 3477  N   GLN B   7     3673   6644   5522    406    668    109       N  
ATOM   3478  CA  GLN B   7     -35.476 -29.548 -43.917  1.00 40.92           C  
ANISOU 3478  CA  GLN B   7     3539   6447   5561    253    607    156       C  
ATOM   3479  C   GLN B   7     -33.990 -29.877 -43.820  1.00 38.74           C  
ANISOU 3479  C   GLN B   7     3446   6014   5260    225    567    233       C  
ATOM   3480  O   GLN B   7     -33.240 -29.510 -44.705  1.00 36.98           O  
ANISOU 3480  O   GLN B   7     3317   5741   4991    332    494    170       O  
ATOM   3481  CB  GLN B   7     -36.056 -29.929 -45.266  1.00 42.04           C  
ANISOU 3481  CB  GLN B   7     3569   6590   5813    300    481     21       C  
ATOM   3482  CG  GLN B   7     -36.494 -31.383 -45.294  1.00 43.77           C  
ANISOU 3482  CG  GLN B   7     3653   6730   6248    128    427     23       C  
ATOM   3483  CD  GLN B   7     -36.973 -31.773 -46.658  1.00 44.19           C  
ANISOU 3483  CD  GLN B   7     3596   6795   6400    180    283   -159       C  
ATOM   3484  NE2 GLN B   7     -38.252 -32.098 -46.727  1.00 46.00           N  
ANISOU 3484  NE2 GLN B   7     3619   7105   6754    120    272   -209       N  
ATOM   3485  OE1 GLN B   7     -36.213 -31.764 -47.626  1.00 43.59           O  
ANISOU 3485  OE1 GLN B   7     3603   6688   6272    270    187   -262       O  
ATOM   3486  N   SER B   8     -33.613 -30.536 -42.733  1.00 38.96           N  
ANISOU 3486  N   SER B   8     3502   5992   5308     76    615    383       N  
ATOM   3487  CA  SER B   8     -32.278 -31.110 -42.501  1.00 38.22           C  
ANISOU 3487  CA  SER B   8     3544   5730   5248     22    557    477       C  
ATOM   3488  C   SER B   8     -31.919 -32.050 -43.650  1.00 38.46           C  
ANISOU 3488  C   SER B   8     3539   5602   5471     31    415    368       C  
ATOM   3489  O   SER B   8     -32.823 -32.626 -44.271  1.00 38.54           O  
ANISOU 3489  O   SER B   8     3402   5617   5623      2    361    272       O  
ATOM   3490  CB  SER B   8     -32.249 -31.828 -41.209  1.00 39.28           C  
ANISOU 3490  CB  SER B   8     3662   5857   5407   -163    601    687       C  
ATOM   3491  OG  SER B   8     -33.140 -32.921 -41.245  1.00 42.06           O  
ANISOU 3491  OG  SER B   8     3846   6170   5966   -311    564    742       O  
ATOM   3492  N   SER B   9     -30.615 -32.189 -43.867  1.00 38.82           N  
ANISOU 3492  N   SER B   9     3701   5526   5522     71    356    361       N  
ATOM   3493  CA  SER B   9     -29.951 -33.121 -44.807  1.00 39.69           C  
ANISOU 3493  CA  SER B   9     3781   5488   5812     91    224    225       C  
ATOM   3494  C   SER B   9     -30.549 -34.519 -44.651  1.00 42.09           C  
ANISOU 3494  C   SER B   9     3942   5631   6418    -54    133    241       C  
ATOM   3495  O   SER B   9     -30.609 -35.231 -45.654  1.00 43.25           O  
ANISOU 3495  O   SER B   9     3993   5701   6740    -23     18     35       O  
ATOM   3496  CB  SER B   9     -28.459 -33.119 -44.571  1.00 38.68           C  
ANISOU 3496  CB  SER B   9     3778   5254   5664    120    199    271       C  
ATOM   3497  OG  SER B   9     -28.134 -33.825 -43.392  1.00 39.73           O  
ANISOU 3497  OG  SER B   9     3933   5241   5920    -15    178    474       O  
ATOM   3498  N   ASP B  10     -30.962 -34.883 -43.435  1.00 44.13           N  
ANISOU 3498  N   ASP B  10     4179   5857   6734   -216    176    479       N  
ATOM   3499  CA  ASP B  10     -31.464 -36.243 -43.090  1.00 47.27           C  
ANISOU 3499  CA  ASP B  10     4439   6067   7455   -401     77    588       C  
ATOM   3500  C   ASP B  10     -32.998 -36.257 -42.993  1.00 25.19           C  
ATOM   3501  O   ASP B  10     -33.485 -37.052 -42.237  1.00 48.73           O  
ANISOU 3501  O   ASP B  10     4363   6323   7829   -696    123    822       O  
ATOM   3502  CB  ASP B  10     -30.826 -36.759 -41.789  1.00 50.26           C  
ANISOU 3502  CB  ASP B  10     4880   6325   7893   -554     60    903       C  
ATOM   3503  CG  ASP B  10     -30.696 -35.730 -40.662  1.00 51.51           C  
ANISOU 3503  CG  ASP B  10     5153   6720   7699   -567    224   1088       C  
ATOM   3504  OD1 ASP B  10     -31.554 -34.835 -40.587  1.00 52.08           O  
ANISOU 3504  OD1 ASP B  10     5195   7039   7553   -525    365   1030       O  
ATOM   3505  OD2 ASP B  10     -29.715 -35.813 -39.863  1.00 52.98           O1-
ANISOU 3505  OD2 ASP B  10     5449   6844   7838   -608    198   1267       O1-
ATOM   3506  N   GLY B  11     -33.728 -35.402 -43.707  1.00 45.49           N  
ANISOU 3506  N   GLY B  11     4010   6187   7086   -370    204    426       N  
ATOM   3507  CA  GLY B  11     -35.196 -35.502 -43.844  1.00 47.48           C  
ANISOU 3507  CA  GLY B  11     4069   6563   7407   -439    232    390       C  
ATOM   3508  C   GLY B  11     -36.009 -34.695 -42.818  1.00 48.15           C  
ANISOU 3508  C   GLY B  11     4113   6906   7277   -485    419    538       C  
ATOM   3509  O   GLY B  11     -37.123 -34.232 -43.170  1.00 47.61           O  
ANISOU 3509  O   GLY B  11     3906   7010   7173   -438    466    425       O  
ATOM   3510  N   GLU B  12     -35.539 -34.543 -41.577  1.00 47.85           N  
ANISOU 3510  N   GLU B  12     4161   6920   7099   -574    519    764       N  
ATOM   3511  CA  GLU B  12     -36.324 -33.915 -40.479  1.00 49.21           C  
ANISOU 3511  CA  GLU B  12     4257   7382   7058   -641    705    881       C  
ATOM   3512  C   GLU B  12     -36.660 -32.458 -40.805  1.00 25.11           C  
ATOM   3513  O   GLU B  12     -35.758 -31.716 -41.217  1.00 44.09           O  
ANISOU 3513  O   GLU B  12     3809   6861   6082   -247    764    572       O  
ATOM   3514  CB  GLU B  12     -35.594 -33.961 -39.133  1.00 50.27           C  
ANISOU 3514  CB  GLU B  12     4496   7575   7028   -762    778   1135       C  
ATOM   3515  CG  GLU B  12     -36.384 -33.319 -37.999  1.00 51.51           C  
ANISOU 3515  CG  GLU B  12     4552   8096   6922   -827    982   1207       C  
ATOM   3516  CD  GLU B  12     -35.889 -33.680 -36.613  1.00 53.30           C  
ANISOU 3516  CD  GLU B  12     4822   8441   6987  -1020   1040   1507       C  
ATOM   3517  OE1 GLU B  12     -34.863 -34.447 -36.521  1.00 51.25           O  
ANISOU 3517  OE1 GLU B  12     4685   7931   6855  -1099    899   1689       O  
ATOM   3518  OE2 GLU B  12     -36.581 -33.254 -35.628  1.00 56.33           O1-
ANISOU 3518  OE2 GLU B  12     5090   9190   7124  -1099   1220   1561       O1-
ATOM   3519  N   ILE B  13     -37.918 -32.081 -40.543  1.00 49.51           N  
ANISOU 3519  N   ILE B  13     4132   7849   6832   -427    909    616       N  
ATOM   3520  CA  ILE B  13     -38.482 -30.716 -40.752  1.00 48.93           C  
ANISOU 3520  CA  ILE B  13     4024   7956   6613   -214    985    412       C  
ATOM   3521  C   ILE B  13     -38.512 -29.970 -39.415  1.00 48.34           C  
ANISOU 3521  C   ILE B  13     3949   8123   6296   -222   1165    447       C  
ATOM   3522  O   ILE B  13     -38.829 -30.595 -38.414  1.00 50.46           O  
ANISOU 3522  O   ILE B  13     4116   8549   6510   -428   1268    619       O  
ATOM   3523  CB  ILE B  13     -39.899 -30.815 -41.334  1.00 51.59           C  
ANISOU 3523  CB  ILE B  13     4109   8403   7089   -207    978    293       C  
ATOM   3524  CG1 ILE B  13     -39.924 -31.439 -42.730  1.00 52.10           C  
ANISOU 3524  CG1 ILE B  13     4159   8274   7362   -175    786    197       C  
ATOM   3525  CG2 ILE B  13     -40.575 -29.460 -41.303  1.00 52.08           C  
ANISOU 3525  CG2 ILE B  13     4094   8658   7037     -2   1058    108       C  
ATOM   3526  CD1 ILE B  13     -40.982 -32.543 -42.866  1.00 55.45           C  
ANISOU 3526  CD1 ILE B  13     4338   8708   8022   -363    749    226       C  
ATOM   3527  N   PHE B  14     -38.229 -28.666 -39.422  1.00 45.90           N  
ANISOU 3527  N   PHE B  14     3734   7853   5853    -10   1191    283       N  
ATOM   3528  CA  PHE B  14     -38.331 -27.758 -38.254  1.00 46.01           C  
ANISOU 3528  CA  PHE B  14     3725   8109   5648     36   1348    208       C  
ATOM   3529  C   PHE B  14     -39.181 -26.557 -38.654  1.00 46.75           C  
ANISOU 3529  C   PHE B  14     3696   8286   5780    268   1363    -56       C  
ATOM   3530  O   PHE B  14     -38.838 -25.892 -39.658  1.00 45.46           O  
ANISOU 3530  O   PHE B  14     3641   7919   5714    451   1225   -145       O  
ATOM   3531  CB  PHE B  14     -36.960 -27.286 -37.784  1.00 44.20           C  
ANISOU 3531  CB  PHE B  14     3741   7781   5273     79   1325    244       C  
ATOM   3532  CG  PHE B  14     -36.010 -28.402 -37.448  1.00 44.12           C  
ANISOU 3532  CG  PHE B  14     3857   7651   5256   -117   1273    503       C  
ATOM   3533  CD1 PHE B  14     -35.437 -29.189 -38.438  1.00 43.09           C  
ANISOU 3533  CD1 PHE B  14     3813   7237   5321   -140   1119    583       C  
ATOM   3534  CD2 PHE B  14     -35.655 -28.639 -36.139  1.00 45.31           C  
ANISOU 3534  CD2 PHE B  14     4029   7984   5204   -267   1366    652       C  
ATOM   3535  CE1 PHE B  14     -34.589 -30.235 -38.104  1.00 43.47           C  
ANISOU 3535  CE1 PHE B  14     3950   7147   5418   -304   1052    803       C  
ATOM   3536  CE2 PHE B  14     -34.780 -29.662 -35.810  1.00 45.66           C  
ANISOU 3536  CE2 PHE B  14     4178   7897   5272   -443   1289    918       C  
ATOM   3537  CZ  PHE B  14     -34.271 -30.478 -36.788  1.00 44.69           C  
ANISOU 3537  CZ  PHE B  14     4126   7452   5403   -457   1127    991       C  
ATOM   3538  N   GLU B  15     -40.269 -26.317 -37.911  1.00 49.09           N  
ANISOU 3538  N   GLU B  15     3754   8884   6013    253   1517   -165       N  
ATOM   3539  CA  GLU B  15     -41.113 -25.117 -38.073  1.00 50.38           C  
ANISOU 3539  CA  GLU B  15     3764   9145   6233    490   1538   -449       C  
ATOM   3540  C   GLU B  15     -40.492 -24.002 -37.222  1.00 21.95           C  
ATOM   3541  O   GLU B  15     -40.550 -24.084 -35.970  1.00 54.11           O  
ANISOU 3541  O   GLU B  15     4264   9968   6326    517   1769   -635       O  
ATOM   3542  CB  GLU B  15     -42.553 -25.455 -37.721  1.00 53.64           C  
ANISOU 3542  CB  GLU B  15     3841   9864   6675    413   1674   -517       C  
ATOM   3543  CG  GLU B  15     -43.072 -26.695 -38.419  1.00 54.53           C  
ANISOU 3543  CG  GLU B  15     3855   9913   6953    232   1609   -337       C  
ATOM   3544  CD  GLU B  15     -44.251 -27.365 -37.710  1.00 58.94           C  
ANISOU 3544  CD  GLU B  15     4093  10810   7492     32   1781   -291       C  
ATOM   3545  OE1 GLU B  15     -44.227 -28.627 -37.626  1.00 60.51           O  
ANISOU 3545  OE1 GLU B  15     4269  10980   7740   -236   1775    -31       O  
ATOM   3546  OE2 GLU B  15     -45.186 -26.634 -37.214  1.00 61.45           O1-
ANISOU 3546  OE2 GLU B  15     4164  11422   7760    139   1919   -514       O1-
ATOM   3547  N   VAL B  16     -39.886 -23.015 -37.892  1.00 48.85           N  
ANISOU 3547  N   VAL B  16     3833   8738   5991    835   1448   -711       N  
ATOM   3548  CA  VAL B  16     -39.108 -21.895 -37.286  1.00 47.98           C  
ANISOU 3548  CA  VAL B  16     3853   8570   5805    973   1441   -869       C  
ATOM   3549  C   VAL B  16     -39.788 -20.568 -37.626  1.00 49.35           C  
ANISOU 3549  C   VAL B  16     3897   8673   6179   1250   1369  -1153       C  
ATOM   3550  O   VAL B  16     -40.077 -20.327 -38.806  1.00 47.81           O  
ANISOU 3550  O   VAL B  16     3697   8271   6197   1363   1210  -1113       O  
ATOM   3551  CB  VAL B  16     -37.656 -21.893 -37.782  1.00 44.44           C  
ANISOU 3551  CB  VAL B  16     3709   7817   5361    955   1300   -695       C  
ATOM   3552  CG1 VAL B  16     -36.812 -20.913 -36.992  1.00 44.41           C  
ANISOU 3552  CG1 VAL B  16     3827   7775   5270   1043   1300   -837       C  
ATOM   3553  CG2 VAL B  16     -37.062 -23.293 -37.736  1.00 43.16           C  
ANISOU 3553  CG2 VAL B  16     3649   7653   5098    711   1318   -413       C  
ATOM   3554  N   ASP B  17     -40.052 -19.753 -36.607  1.00 52.11           N  
ANISOU 3554  N   ASP B  17     4130   9205   6463   1357   1472  -1440       N  
ATOM   3555  CA  ASP B  17     -40.407 -18.323 -36.751  1.00 54.31           C  
ANISOU 3555  CA  ASP B  17     4318   9342   6975   1646   1371  -1750       C  
ATOM   3556  C   ASP B  17     -39.539 -17.756 -37.868  1.00 22.32           C  
ATOM   3557  O   ASP B  17     -38.314 -17.912 -37.833  1.00 49.77           O  
ANISOU 3557  O   ASP B  17     4228   8182   6503   1644   1083  -1423       O  
ATOM   3558  CB  ASP B  17     -40.249 -17.541 -35.451  1.00 56.50           C  
ANISOU 3558  CB  ASP B  17     4534   9806   7129   1728   1481  -2083       C  
ATOM   3559  CG  ASP B  17     -40.923 -16.184 -35.482  1.00 59.11           C  
ANISOU 3559  CG  ASP B  17     4677  10032   7750   2034   1393  -2473       C  
ATOM   3560  OD1 ASP B  17     -41.211 -15.713 -36.608  1.00 58.45           O  
ANISOU 3560  OD1 ASP B  17     4589   9634   7986   2185   1193  -2408       O  
ATOM   3561  OD2 ASP B  17     -41.169 -15.614 -34.373  1.00 61.82           O1-
ANISOU 3561  OD2 ASP B  17     4864  10625   8000   2123   1516  -2847       O1-
ATOM   3562  N   VAL B  18     -40.183 -17.177 -38.868  1.00 55.37           N  
ANISOU 3562  N   VAL B  18     4595   8850   7595   1919    962  -1615       N  
ATOM   3563  CA  VAL B  18     -39.487 -16.674 -40.083  1.00 54.69           C  
ANISOU 3563  CA  VAL B  18     4699   8391   7690   1990    719  -1403       C  
ATOM   3564  C   VAL B  18     -38.483 -15.589 -39.673  1.00 54.95           C  
ANISOU 3564  C   VAL B  18     4889   8181   7806   2083    628  -1493       C  
ATOM   3565  O   VAL B  18     -37.375 -15.604 -40.195  1.00 53.99           O  
ANISOU 3565  O   VAL B  18     4999   7855   7661   2005    528  -1255       O  
ATOM   3566  CB  VAL B  18     -40.515 -16.191 -41.120  1.00 57.25           C  
ANISOU 3566  CB  VAL B  18     4852   8614   8288   2166    551  -1413       C  
ATOM   3567  CG1 VAL B  18     -41.520 -15.193 -40.538  1.00 61.15           C  
ANISOU 3567  CG1 VAL B  18     5081   9144   9009   2401    551  -1779       C  
ATOM   3568  CG2 VAL B  18     -39.823 -15.635 -42.342  1.00 56.48           C  
ANISOU 3568  CG2 VAL B  18     4934   8189   8339   2221    301  -1159       C  
ATOM   3569  N   GLU B  19     -38.844 -14.714 -38.740  1.00 57.90           N  
ANISOU 3569  N   GLU B  19     5125   8599   8277   2237    668  -1847       N  
ATOM   3570  CA  GLU B  19     -37.975 -13.621 -38.223  1.00 59.20           C  
ANISOU 3570  CA  GLU B  19     5401   8528   8564   2336    570  -2009       C  
ATOM   3571  C   GLU B  19     -36.633 -14.216 -37.777  1.00 55.54           C  
ANISOU 3571  C   GLU B  19     5191   8095   7817   2122    644  -1829       C  
ATOM   3572  O   GLU B  19     -35.592 -13.653 -38.146  1.00 54.45           O  
ANISOU 3572  O   GLU B  19     5241   7651   7795   2124    488  -1700       O  
ATOM   3573  CB  GLU B  19     -38.695 -12.860 -37.108  1.00 64.76           C  
ANISOU 3573  CB  GLU B  19     5869   9388   9347   2514    653  -2500       C  
ATOM   3574  CG  GLU B  19     -40.124 -12.490 -37.497  1.00 69.70           C  
ANISOU 3574  CG  GLU B  19     6200  10048  10234   2716    611  -2685       C  
ATOM   3575  CD  GLU B  19     -40.810 -11.369 -36.717  1.00 76.11           C  
ANISOU 3575  CD  GLU B  19     6755  10871  11292   2981    597  -3210       C  
ATOM   3576  OE1 GLU B  19     -40.085 -10.536 -36.111  1.00 78.54           O  
ANISOU 3576  OE1 GLU B  19     7141  11007  11693   3060    526  -3434       O  
ATOM   3577  OE2 GLU B  19     -42.076 -11.320 -36.726  1.00 78.97           O1-
ANISOU 3577  OE2 GLU B  19     6818  11411  11774   3117    647  -3423       O1-
ATOM   3578  N   ILE B  20     -36.647 -15.344 -37.065  1.00 53.91           N  
ANISOU 3578  N   ILE B  20     4978   8235   7269   1931    857  -1784       N  
ATOM   3579  CA  ILE B  20     -35.415 -16.013 -36.542  1.00 51.91           C  
ANISOU 3579  CA  ILE B  20     4942   8036   6746   1725    921  -1607       C  
ATOM   3580  C   ILE B  20     -34.677 -16.695 -37.692  1.00 48.39           C  
ANISOU 3580  C   ILE B  20     4686   7390   6311   1603    821  -1217       C  
ATOM   3581  O   ILE B  20     -33.453 -16.478 -37.801  1.00 46.97           O  
ANISOU 3581  O   ILE B  20     4704   7015   6130   1554    733  -1092       O  
ATOM   3582  CB  ILE B  20     -35.723 -16.993 -35.390  1.00 53.42           C  
ANISOU 3582  CB  ILE B  20     5045   8666   6588   1555   1156  -1648       C  
ATOM   3583  CG1 ILE B  20     -35.909 -16.245 -34.066  1.00 56.29           C  
ANISOU 3583  CG1 ILE B  20     5282   9264   6840   1644   1254  -2046       C  
ATOM   3584  CG2 ILE B  20     -34.650 -18.080 -35.270  1.00 50.83           C  
ANISOU 3584  CG2 ILE B  20     4923   8359   6031   1315   1185  -1324       C  
ATOM   3585  CD1 ILE B  20     -37.090 -16.722 -33.274  1.00 59.36           C  
ANISOU 3585  CD1 ILE B  20     5404  10123   7026   1603   1476  -2213       C  
ATOM   3586  N   ALA B  21     -35.386 -17.484 -38.503  1.00 47.37           N  
ANISOU 3586  N   ALA B  21     4480   7326   6193   1556    834  -1058       N  
ATOM   3587  CA  ALA B  21     -34.848 -18.213 -39.689  1.00 44.33           C  
ANISOU 3587  CA  ALA B  21     4229   6806   5809   1454    744   -744       C  
ATOM   3588  C   ALA B  21     -34.038 -17.267 -40.604  1.00 43.37           C  
ANISOU 3588  C   ALA B  21     4248   6367   5865   1547    546   -631       C  
ATOM   3589  O   ALA B  21     -32.966 -17.688 -41.080  1.00 40.90           O  
ANISOU 3589  O   ALA B  21     4103   5965   5474   1435    505   -417       O  
ATOM   3590  CB  ALA B  21     -35.973 -18.876 -40.457  1.00 44.14           C  
ANISOU 3590  CB  ALA B  21     4047   6891   5833   1449    750   -692       C  
ATOM   3591  N   LYS B  22     -34.519 -16.036 -40.839  1.00 44.02           N  
ANISOU 3591  N   LYS B  22     4247   6284   6196   1739    419   -759       N  
ATOM   3592  CA  LYS B  22     -33.921 -15.089 -41.812  1.00 43.56           C  
ANISOU 3592  CA  LYS B  22     4288   5918   6347   1815    203   -591       C  
ATOM   3593  C   LYS B  22     -32.658 -14.433 -41.231  1.00 43.68           C  
ANISOU 3593  C   LYS B  22     4460   5749   6388   1784    162   -605       C  
ATOM   3594  O   LYS B  22     -32.065 -13.589 -41.926  1.00 43.85           O  
ANISOU 3594  O   LYS B  22     4558   5503   6599   1820    -17   -448       O  
ATOM   3595  CB  LYS B  22     -34.962 -14.055 -42.245  1.00 45.90           C  
ANISOU 3595  CB  LYS B  22     4417   6075   6949   2028     52   -697       C  
ATOM   3596  CG  LYS B  22     -36.018 -14.588 -43.196  1.00 45.84           C  
ANISOU 3596  CG  LYS B  22     4274   6196   6946   2054     20   -598       C  
ATOM   3597  CD  LYS B  22     -36.917 -13.509 -43.749  1.00 48.59           C  
ANISOU 3597  CD  LYS B  22     4467   6370   7627   2270   -180   -645       C  
ATOM   3598  CE  LYS B  22     -37.814 -13.978 -44.881  1.00 49.21           C  
ANISOU 3598  CE  LYS B  22     4431   6565   7703   2287   -262   -492       C  
ATOM   3599  NZ  LYS B  22     -38.898 -13.002 -45.194  1.00 52.84           N1+
ANISOU 3599  NZ  LYS B  22     4685   6891   8500   2516   -445   -591       N1+
ATOM   3600  N   GLN B  23     -32.244 -14.784 -40.016  1.00 44.05           N  
ANISOU 3600  N   GLN B  23     4544   5940   6254   1706    306   -766       N  
ATOM   3601  CA  GLN B  23     -30.897 -14.438 -39.505  1.00 44.11           C  
ANISOU 3601  CA  GLN B  23     4715   5815   6230   1632    271   -745       C  
ATOM   3602  C   GLN B  23     -29.889 -15.087 -40.457  1.00 41.69           C  
ANISOU 3602  C   GLN B  23     4560   5451   5829   1484    233   -399       C  
ATOM   3603  O   GLN B  23     -28.752 -14.541 -40.627  1.00 41.24           O  
ANISOU 3603  O   GLN B  23     4625   5197   5849   1442    133   -285       O  
ATOM   3604  CB  GLN B  23     -30.712 -14.936 -38.075  1.00 45.95           C  
ANISOU 3604  CB  GLN B  23     4948   6297   6214   1552    437   -943       C  
ATOM   3605  CG  GLN B  23     -31.423 -14.086 -37.029  1.00 50.99           C  
ANISOU 3605  CG  GLN B  23     5437   7011   6926   1702    468  -1346       C  
ATOM   3606  CD  GLN B  23     -31.138 -14.519 -35.605  1.00 54.06           C  
ANISOU 3606  CD  GLN B  23     5827   7704   7010   1606    624  -1527       C  
ATOM   3607  NE2 GLN B  23     -32.148 -14.384 -34.753  1.00 57.60           N  
ANISOU 3607  NE2 GLN B  23     6084   8427   7376   1688    748  -1843       N  
ATOM   3608  OE1 GLN B  23     -30.035 -14.975 -35.255  1.00 55.71           O  
ANISOU 3608  OE1 GLN B  23     6190   7932   7046   1458    633  -1385       O  
ATOM   3609  N   SER B  24     -30.295 -16.213 -41.065  1.00 39.45           N  
ANISOU 3609  N   SER B  24     4250   5341   5400   1408    308   -258       N  
ATOM   3610  CA  SER B  24     -29.590 -16.878 -42.187  1.00 36.47           C  
ANISOU 3610  CA  SER B  24     3962   4951   4945   1302    269     18       C  
ATOM   3611  C   SER B  24     -29.960 -16.188 -43.497  1.00 37.33           C  
ANISOU 3611  C   SER B  24     4029   4941   5213   1390    113    167       C  
ATOM   3612  O   SER B  24     -31.093 -16.369 -43.998  1.00 37.20           O  
ANISOU 3612  O   SER B  24     3888   5016   5230   1461     99    141       O  
ATOM   3613  CB  SER B  24     -29.906 -18.327 -42.290  1.00 34.95           C  
ANISOU 3613  CB  SER B  24     3737   4969   4573   1196    384     60       C  
ATOM   3614  OG  SER B  24     -29.629 -18.776 -43.607  1.00 33.65           O  
ANISOU 3614  OG  SER B  24     3595   4808   4383   1156    319    248       O  
ATOM   3615  N   VAL B  25     -29.003 -15.448 -44.047  1.00 37.23           N  
ANISOU 3615  N   VAL B  25     4108   4750   5289   1369     -9    344       N  
ATOM   3616  CA  VAL B  25     -29.131 -14.744 -45.353  1.00 37.05           C  
ANISOU 3616  CA  VAL B  25     4059   4627   5392   1414   -179    577       C  
ATOM   3617  C   VAL B  25     -29.420 -15.800 -46.416  1.00 35.04           C  
ANISOU 3617  C   VAL B  25     3768   4611   4933   1353   -143    703       C  
ATOM   3618  O   VAL B  25     -30.310 -15.592 -47.211  1.00 36.23           O  
ANISOU 3618  O   VAL B  25     3824   4803   5138   1430   -238    767       O  
ATOM   3619  CB  VAL B  25     -27.858 -13.936 -45.634  1.00 37.18           C  
ANISOU 3619  CB  VAL B  25     4179   4450   5497   1342   -285    780       C  
ATOM   3620  CG1 VAL B  25     -27.830 -13.350 -47.029  1.00 38.49           C  
ANISOU 3620  CG1 VAL B  25     4321   4576   5728   1335   -450   1101       C  
ATOM   3621  CG2 VAL B  25     -27.675 -12.857 -44.578  1.00 38.76           C  
ANISOU 3621  CG2 VAL B  25     4393   4388   5945   1415   -350    603       C  
ATOM   3622  N   THR B  26     -28.736 -16.928 -46.384  1.00 32.60           N  
ANISOU 3622  N   THR B  26     3518   4453   4414   1228    -23    709       N  
ATOM   3623  CA  THR B  26     -28.984 -18.008 -47.359  1.00 32.15           C  
ANISOU 3623  CA  THR B  26     3412   4619   4185   1176      4    762       C  
ATOM   3624  C   THR B  26     -30.474 -18.287 -47.340  1.00 32.57           C  
ANISOU 3624  C   THR B  26     3330   4758   4286   1262      8    625       C  
ATOM   3625  O   THR B  26     -31.108 -18.069 -48.338  1.00 33.42           O  
ANISOU 3625  O   THR B  26     3360   4934   4405   1317    -99    712       O  
ATOM   3626  CB  THR B  26     -28.135 -19.250 -47.072  1.00 30.44           C  
ANISOU 3626  CB  THR B  26     3253   4501   3810   1052    127    714       C  
ATOM   3627  CG2 THR B  26     -28.380 -20.350 -48.073  1.00 30.04           C  
ANISOU 3627  CG2 THR B  26     3134   4653   3627   1012    136    709       C  
ATOM   3628  OG1 THR B  26     -26.757 -18.887 -47.122  1.00 29.23           O  
ANISOU 3628  OG1 THR B  26     3199   4275   3633    983    114    837       O  
ATOM   3629  N   ILE B  27     -31.006 -18.650 -46.188  1.00 33.07           N  
ANISOU 3629  N   ILE B  27     3356   4832   4378   1271    122    430       N  
ATOM   3630  CA  ILE B  27     -32.456 -18.960 -46.017  1.00 34.94           C  
ANISOU 3630  CA  ILE B  27     3432   5176   4666   1336    153    282       C  
ATOM   3631  C   ILE B  27     -33.307 -17.751 -46.445  1.00 37.33           C  
ANISOU 3631  C   ILE B  27     3637   5383   5162   1502      8    287       C  
ATOM   3632  O   ILE B  27     -34.348 -17.956 -47.089  1.00 37.87           O  
ANISOU 3632  O   ILE B  27     3570   5557   5260   1558    -48    272       O  
ATOM   3633  CB  ILE B  27     -32.700 -19.403 -44.568  1.00 35.09           C  
ANISOU 3633  CB  ILE B  27     3425   5249   4657   1294    314    103       C  
ATOM   3634  CG1 ILE B  27     -31.955 -20.712 -44.315  1.00 33.58           C  
ANISOU 3634  CG1 ILE B  27     3311   5134   4312   1127    411    153       C  
ATOM   3635  CG2 ILE B  27     -34.184 -19.537 -44.251  1.00 36.77           C  
ANISOU 3635  CG2 ILE B  27     3445   5590   4937   1360    364    -56       C  
ATOM   3636  CD1 ILE B  27     -32.260 -21.322 -42.991  1.00 34.16           C  
ANISOU 3636  CD1 ILE B  27     3345   5309   4327   1049    556     50       C  
ATOM   3637  N   LYS B  28     -32.899 -16.529 -46.111  1.00 38.26           N  
ANISOU 3637  N   LYS B  28     3808   5290   5440   1581    -75    302       N  
ATOM   3638  CA  LYS B  28     -33.662 -15.321 -46.530  1.00 40.75           C  
ANISOU 3638  CA  LYS B  28     4021   5451   6010   1750   -255    322       C  
ATOM   3639  C   LYS B  28     -33.870 -15.427 -48.042  1.00 41.64           C  
ANISOU 3639  C   LYS B  28     4106   5652   6065   1740   -400    573       C  
ATOM   3640  O   LYS B  28     -35.027 -15.416 -48.483  1.00 42.60           O  
ANISOU 3640  O   LYS B  28     4075   5849   6262   1837   -476    534       O  
ATOM   3641  CB  LYS B  28     -32.924 -14.047 -46.113  1.00 41.69           C  
ANISOU 3641  CB  LYS B  28     4222   5279   6340   1804   -360    347       C  
ATOM   3642  CG  LYS B  28     -33.684 -12.739 -46.289  1.00 44.52           C  
ANISOU 3642  CG  LYS B  28     4463   5402   7049   1995   -563    323       C  
ATOM   3643  CD  LYS B  28     -32.875 -11.508 -45.840  1.00 45.94           C  
ANISOU 3643  CD  LYS B  28     4722   5245   7490   2033   -688    331       C  
ATOM   3644  CE  LYS B  28     -33.721 -10.320 -45.398  1.00 49.64           C  
ANISOU 3644  CE  LYS B  28     5041   5456   8364   2256   -840    113       C  
ATOM   3645  NZ  LYS B  28     -34.563  -9.682 -46.453  1.00 51.97           N1+
ANISOU 3645  NZ  LYS B  28     5214   5626   8906   2383  -1081    308       N1+
ATOM   3646  N   THR B  29     -32.772 -15.627 -48.777  1.00 41.75           N  
ANISOU 3646  N   THR B  29     4244   5704   5914   1616   -423    803       N  
ATOM   3647  CA  THR B  29     -32.693 -15.619 -50.260  1.00 43.57           C  
ANISOU 3647  CA  THR B  29     4461   6069   6025   1580   -563   1073       C  
ATOM   3648  C   THR B  29     -33.572 -16.735 -50.822  1.00 44.21           C  
ANISOU 3648  C   THR B  29     4430   6424   5943   1570   -524    970       C  
ATOM   3649  O   THR B  29     -34.302 -16.507 -51.784  1.00 46.79           O  
ANISOU 3649  O   THR B  29     4656   6851   6272   1630   -677   1082       O  
ATOM   3650  CB  THR B  29     -31.243 -15.797 -50.730  1.00 42.63           C  
ANISOU 3650  CB  THR B  29     4476   6007   5714   1428   -530   1270       C  
ATOM   3651  CG2 THR B  29     -31.059 -15.554 -52.209  1.00 44.42           C  
ANISOU 3651  CG2 THR B  29     4678   6404   5795   1383   -675   1574       C  
ATOM   3652  OG1 THR B  29     -30.419 -14.899 -49.985  1.00 42.13           O  
ANISOU 3652  OG1 THR B  29     4508   5676   5822   1420   -543   1312       O  
ATOM   3653  N   MET B  30     -33.502 -17.911 -50.227  1.00 43.40           N  
ANISOU 3653  N   MET B  30     4337   6430   5724   1489   -344    771       N  
ATOM   3654  CA  MET B  30     -34.257 -19.101 -50.675  1.00 44.91           C  
ANISOU 3654  CA  MET B  30     4418   6848   5799   1453   -307    647       C  
ATOM   3655  C   MET B  30     -35.753 -18.842 -50.513  1.00 47.03           C  
ANISOU 3655  C   MET B  30     4508   7122   6238   1576   -363    528       C  
ATOM   3656  O   MET B  30     -36.519 -19.253 -51.389  1.00 47.97           O  
ANISOU 3656  O   MET B  30     4507   7413   6307   1592   -452    524       O  
ATOM   3657  CB  MET B  30     -33.845 -20.313 -49.846  1.00 44.37           C  
ANISOU 3657  CB  MET B  30     4393   6811   5655   1335   -120    484       C  
ATOM   3658  CG  MET B  30     -32.373 -20.609 -49.977  1.00 44.64           C  
ANISOU 3658  CG  MET B  30     4574   6835   5550   1230    -71    574       C  
ATOM   3659  SD  MET B  30     -31.971 -22.265 -49.480  1.00 47.56           S  
ANISOU 3659  SD  MET B  30     4957   7267   5848   1096     72    416       S  
ATOM   3660  CE  MET B  30     -32.894 -23.174 -50.727  1.00 49.19           C  
ANISOU 3660  CE  MET B  30     5005   7696   5990   1095    -14    322       C  
ATOM   3661  N   LEU B  31     -36.145 -18.186 -49.424  1.00 47.72           N  
ANISOU 3661  N   LEU B  31     4563   7051   6519   1665   -313    406       N  
ATOM   3662  CA  LEU B  31     -37.562 -17.849 -49.141  1.00 49.54           C  
ANISOU 3662  CA  LEU B  31     4592   7292   6941   1801   -350    252       C  
ATOM   3663  C   LEU B  31     -38.030 -16.742 -50.090  1.00 51.34           C  
ANISOU 3663  C   LEU B  31     4750   7434   7325   1948   -600    417       C  
ATOM   3664  O   LEU B  31     -39.134 -16.858 -50.653  1.00 51.39           O  
ANISOU 3664  O   LEU B  31     4582   7556   7388   2022   -700    385       O  
ATOM   3665  CB  LEU B  31     -37.675 -17.407 -47.679  1.00 50.03           C  
ANISOU 3665  CB  LEU B  31     4633   7240   7136   1857   -216     45       C  
ATOM   3666  CG  LEU B  31     -37.512 -18.528 -46.657  1.00 48.37           C  
ANISOU 3666  CG  LEU B  31     4440   7163   6775   1711     19    -98       C  
ATOM   3667  CD1 LEU B  31     -37.517 -17.965 -45.244  1.00 49.43           C  
ANISOU 3667  CD1 LEU B  31     4559   7242   6982   1763    140   -291       C  
ATOM   3668  CD2 LEU B  31     -38.595 -19.588 -46.823  1.00 48.38           C  
ANISOU 3668  CD2 LEU B  31     4262   7375   6744   1654     78   -189       C  
ATOM   3669  N   GLU B  32     -37.210 -15.709 -50.248  1.00 52.03           N  
ANISOU 3669  N   GLU B  32     4958   7314   7495   1978   -713    606       N  
ATOM   3670  CA  GLU B  32     -37.636 -14.438 -50.872  1.00 55.75           C  
ANISOU 3670  CA  GLU B  32     5359   7611   8211   2127   -973    784       C  
ATOM   3671  C   GLU B  32     -37.449 -14.543 -52.387  1.00 26.46           C  
ATOM   3672  O   GLU B  32     -38.432 -14.313 -53.099  1.00 58.77           O  
ANISOU 3672  O   GLU B  32     5612   8238   8482   2160  -1323   1172       O  
ATOM   3673  CB  GLU B  32     -36.896 -13.276 -50.216  1.00 57.26           C  
ANISOU 3673  CB  GLU B  32     5650   7470   8635   2179  -1025    822       C  
ATOM   3674  CG  GLU B  32     -37.336 -13.054 -48.775  1.00 58.19           C  
ANISOU 3674  CG  GLU B  32     5692   7472   8944   2285   -889    450       C  
ATOM   3675  CD  GLU B  32     -36.762 -11.809 -48.117  1.00 60.31           C  
ANISOU 3675  CD  GLU B  32     6021   7393   9503   2371   -979    415       C  
ATOM   3676  OE1 GLU B  32     -35.697 -11.340 -48.568  1.00 59.85           O  
ANISOU 3676  OE1 GLU B  32     6114   7183   9443   2281  -1080    690       O  
ATOM   3677  OE2 GLU B  32     -37.392 -11.281 -47.160  1.00 63.33           O1-
ANISOU 3677  OE2 GLU B  32     6276   7661  10125   2527   -956     95       O1-
ATOM   3678  N   ASP B  33     -36.252 -14.893 -52.865  1.00 55.05           N  
ANISOU 3678  N   ASP B  33     5448   7795   7672   1900  -1093   1287       N  
ATOM   3679  CA  ASP B  33     -35.941 -14.872 -54.318  1.00 55.70           C  
ANISOU 3679  CA  ASP B  33     5542   8095   7526   1825  -1249   1607       C  
ATOM   3680  C   ASP B  33     -36.416 -16.178 -54.967  1.00 23.87           C  
ATOM   3681  O   ASP B  33     -36.710 -16.141 -56.164  1.00 54.97           O  
ANISOU 3681  O   ASP B  33     5299   8597   6989   1757  -1354   1647       O  
ATOM   3682  CB  ASP B  33     -34.460 -14.621 -54.596  1.00 56.79           C  
ANISOU 3682  CB  ASP B  33     5846   8224   7508   1680  -1218   1852       C  
ATOM   3683  CG  ASP B  33     -33.846 -13.434 -53.868  1.00 59.41           C  
ANISOU 3683  CG  ASP B  33     6265   8172   8137   1711  -1270   1962       C  
ATOM   3684  OD1 ASP B  33     -34.601 -12.679 -53.234  1.00 61.24           O  
ANISOU 3684  OD1 ASP B  33     6423   8132   8713   1867  -1361   1853       O  
ATOM   3685  OD2 ASP B  33     -32.588 -13.290 -53.930  1.00 61.20           O1-
ANISOU 3685  OD2 ASP B  33     6618   8377   8258   1577  -1218   2129       O1-
ATOM   3686  N   LEU B  34     -36.500 -17.284 -54.227  1.00 49.63           N  
ANISOU 3686  N   LEU B  34     4688   7745   6423   1713   -974   1154       N  
ATOM   3687  CA  LEU B  34     -36.692 -18.633 -54.833  1.00 48.71           C  
ANISOU 3687  CA  LEU B  34     4511   7934   6062   1623   -915   1002       C  
ATOM   3688  C   LEU B  34     -38.020 -19.280 -54.405  1.00 49.39           C  
ANISOU 3688  C   LEU B  34     4424   8055   6285   1678   -881    736       C  
ATOM   3689  O   LEU B  34     -38.321 -20.387 -54.906  1.00 48.12           O  
ANISOU 3689  O   LEU B  34     4186   8114   5984   1607   -864    591       O  
ATOM   3690  CB  LEU B  34     -35.503 -19.522 -54.461  1.00 45.74           C  
ANISOU 3690  CB  LEU B  34     4269   7586   5524   1482   -719    906       C  
ATOM   3691  CG  LEU B  34     -34.126 -18.981 -54.851  1.00 45.15           C  
ANISOU 3691  CG  LEU B  34     4340   7508   5305   1409   -725   1147       C  
ATOM   3692  CD1 LEU B  34     -33.006 -19.899 -54.428  1.00 42.65           C  
ANISOU 3692  CD1 LEU B  34     4125   7211   4868   1290   -539   1018       C  
ATOM   3693  CD2 LEU B  34     -34.043 -18.759 -56.339  1.00 47.49           C  
ANISOU 3693  CD2 LEU B  34     4588   8098   5357   1383   -887   1370       C  
ATOM   3694  N   GLY B  35     -38.797 -18.633 -53.527  1.00 50.76           N  
ANISOU 3694  N   GLY B  35     4516   8034   6736   1797   -876    653       N  
ATOM   3695  CA  GLY B  35     -40.113 -19.127 -53.065  1.00 51.60           C  
ANISOU 3695  CA  GLY B  35     4421   8194   6989   1849   -834    414       C  
ATOM   3696  C   GLY B  35     -40.069 -20.560 -52.541  1.00 49.83           C  
ANISOU 3696  C   GLY B  35     4186   8072   6674   1699   -634    203       C  
ATOM   3697  O   GLY B  35     -41.106 -21.240 -52.618  1.00 49.94           O  
ANISOU 3697  O   GLY B  35     4017   8212   6745   1688   -638     50       O  
ATOM   3698  N   MET B  36     -38.933 -21.005 -51.991  1.00 47.66           N  
ANISOU 3698  N   MET B  36     4086   7728   6296   1583   -480    204       N  
ATOM   3699  CA  MET B  36     -38.788 -22.382 -51.460  1.00 46.73           C  
ANISOU 3699  CA  MET B  36     3965   7659   6130   1432   -317     46       C  
ATOM   3700  C   MET B  36     -39.697 -22.538 -50.226  1.00 46.92           C  
ANISOU 3700  C   MET B  36     3857   7643   6326   1433   -180   -104       C  
ATOM   3701  O   MET B  36     -39.624 -21.680 -49.308  1.00 47.07           O  
ANISOU 3701  O   MET B  36     3909   7543   6431   1507   -109   -109       O  
ATOM   3702  CB  MET B  36     -37.343 -22.679 -51.062  1.00 45.85           C  
ANISOU 3702  CB  MET B  36     4060   7457   5905   1330   -205    103       C  
ATOM   3703  CG  MET B  36     -36.300 -22.380 -52.139  1.00 47.02           C  
ANISOU 3703  CG  MET B  36     4331   7667   5869   1324   -304    260       C  
ATOM   3704  SD  MET B  36     -36.199 -23.575 -53.519  1.00 49.16           S  
ANISOU 3704  SD  MET B  36     4533   8205   5941   1245   -386    166       S  
ATOM   3705  CE  MET B  36     -35.626 -25.047 -52.685  1.00 48.70           C  
ANISOU 3705  CE  MET B  36     4512   8051   5941   1102   -222    -18       C  
ATOM   3706  N   ASP B  37     -40.566 -23.559 -50.233  1.00 46.65           N  
ANISOU 3706  N   ASP B  37     3655   7727   6345   1351   -151   -233       N  
ATOM   3707  CA  ASP B  37     -41.318 -24.080 -49.057  1.00 45.74           C  
ANISOU 3707  CA  ASP B  37     3399   7635   6347   1274     15   -352       C  
ATOM   3708  C   ASP B  37     -41.531 -25.575 -49.246  1.00 20.74           C  
ATOM   3709  O   ASP B  37     -42.248 -25.975 -50.155  1.00 45.91           O  
ANISOU 3709  O   ASP B  37     3194   7822   6426   1099    -96   -485       O  
ATOM   3710  CB  ASP B  37     -42.699 -23.447 -48.910  1.00 48.46           C  
ANISOU 3710  CB  ASP B  37     3503   8062   6850   1402    -15   -451       C  
ATOM   3711  CG  ASP B  37     -43.508 -24.077 -47.786  1.00 49.63           C  
ANISOU 3711  CG  ASP B  37     3467   8309   7083   1294    172   -566       C  
ATOM   3712  OD1 ASP B  37     -42.971 -24.095 -46.628  1.00 48.66           O  
ANISOU 3712  OD1 ASP B  37     3433   8155   6898   1223    349   -555       O  
ATOM   3713  OD2 ASP B  37     -44.646 -24.567 -48.080  1.00 50.60           O1-
ANISOU 3713  OD2 ASP B  37     3349   8561   7317   1266    135   -653       O1-
ATOM   3714  N   PRO B  38     -40.903 -26.456 -48.444  1.00 43.13           N  
ANISOU 3714  N   PRO B  38     3070   7299   6020    930    168   -391       N  
ATOM   3715  CA  PRO B  38     -39.992 -26.051 -47.379  1.00 42.51           C  
ANISOU 3715  CA  PRO B  38     3163   7125   5865    914    305   -309       C  
ATOM   3716  C   PRO B  38     -38.648 -25.526 -47.918  1.00 41.83           C  
ANISOU 3716  C   PRO B  38     3312   6933   5650    977    237   -218       C  
ATOM   3717  O   PRO B  38     -38.531 -25.260 -49.109  1.00 42.62           O  
ANISOU 3717  O   PRO B  38     3428   7068   5697   1054     92   -203       O  
ATOM   3718  CB  PRO B  38     -39.772 -27.375 -46.621  1.00 41.78           C  
ANISOU 3718  CB  PRO B  38     3063   7001   5811    697    410   -276       C  
ATOM   3719  CG  PRO B  38     -39.850 -28.409 -47.701  1.00 41.91           C  
ANISOU 3719  CG  PRO B  38     3021   7000   5901    629    274   -336       C  
ATOM   3720  CD  PRO B  38     -40.975 -27.917 -48.584  1.00 43.17           C  
ANISOU 3720  CD  PRO B  38     3007   7293   6103    750    159   -435       C  
ATOM   3721  N   VAL B  39     -37.667 -25.369 -47.033  1.00 40.16           N  
ANISOU 3721  N   VAL B  39     3261   6623   5373    935    341   -149       N  
ATOM   3722  CA  VAL B  39     -36.292 -24.945 -47.393  1.00 38.45           C  
ANISOU 3722  CA  VAL B  39     3256   6306   5048    965    298    -55       C  
ATOM   3723  C   VAL B  39     -35.382 -26.144 -47.162  1.00 37.16           C  
ANISOU 3723  C   VAL B  39     3177   6082   4862    813    342    -32       C  
ATOM   3724  O   VAL B  39     -35.132 -26.540 -46.031  1.00 37.98           O  
ANISOU 3724  O   VAL B  39     3315   6138   4979    715    451      4       O  
ATOM   3725  CB  VAL B  39     -35.894 -23.707 -46.577  1.00 38.17           C  
ANISOU 3725  CB  VAL B  39     3317   6187   4998   1053    350    -17       C  
ATOM   3726  CG1 VAL B  39     -34.506 -23.205 -46.936  1.00 37.58           C  
ANISOU 3726  CG1 VAL B  39     3437   6005   4837   1068    300     97       C  
ATOM   3727  CG2 VAL B  39     -36.919 -22.609 -46.760  1.00 39.58           C  
ANISOU 3727  CG2 VAL B  39     3373   6391   5276   1216    284    -71       C  
ATOM   3728  N   PRO B  40     -34.896 -26.801 -48.233  1.00 36.74           N  
ANISOU 3728  N   PRO B  40     3138   6041   4779    791    247    -63       N  
ATOM   3729  CA  PRO B  40     -33.964 -27.903 -48.078  1.00 35.86           C  
ANISOU 3729  CA  PRO B  40     3092   5839   4695    677    263    -71       C  
ATOM   3730  C   PRO B  40     -32.618 -27.336 -47.625  1.00 34.42           C  
ANISOU 3730  C   PRO B  40     3094   5567   4415    691    310     34       C  
ATOM   3731  O   PRO B  40     -32.228 -26.275 -48.090  1.00 34.13           O  
ANISOU 3731  O   PRO B  40     3130   5561   4277    787    278     90       O  
ATOM   3732  CB  PRO B  40     -33.829 -28.533 -49.470  1.00 36.22           C  
ANISOU 3732  CB  PRO B  40     3078   5964   4719    692    140   -196       C  
ATOM   3733  CG  PRO B  40     -34.842 -27.826 -50.337  1.00 37.48           C  
ANISOU 3733  CG  PRO B  40     3134   6287   4821    795     55   -226       C  
ATOM   3734  CD  PRO B  40     -35.189 -26.521 -49.642  1.00 37.41           C  
ANISOU 3734  CD  PRO B  40     3165   6251   4797    880    111   -104       C  
ATOM   3735  N   LEU B  41     -31.958 -28.079 -46.744  1.00 33.61           N  
ANISOU 3735  N   LEU B  41     3050   5352   4368    584    365     76       N  
ATOM   3736  CA  LEU B  41     -30.555 -27.853 -46.344  1.00 32.47           C  
ANISOU 3736  CA  LEU B  41     3061   5116   4159    576    389    157       C  
ATOM   3737  C   LEU B  41     -29.817 -29.176 -46.505  1.00 32.38           C  
ANISOU 3737  C   LEU B  41     3040   5008   4254    492    343    114       C  
ATOM   3738  O   LEU B  41     -29.573 -29.877 -45.533  1.00 32.29           O  
ANISOU 3738  O   LEU B  41     3046   4885   4337    389    367    189       O  
ATOM   3739  CB  LEU B  41     -30.530 -27.319 -44.909  1.00 32.07           C  
ANISOU 3739  CB  LEU B  41     3077   5030   4076    543    486    251       C  
ATOM   3740  CG  LEU B  41     -31.437 -26.116 -44.635  1.00 32.87           C  
ANISOU 3740  CG  LEU B  41     3141   5213   4135    639    526    227       C  
ATOM   3741  CD1 LEU B  41     -31.490 -25.843 -43.147  1.00 33.29           C  
ANISOU 3741  CD1 LEU B  41     3221   5284   4143    591    633    256       C  
ATOM   3742  CD2 LEU B  41     -30.978 -24.853 -45.356  1.00 32.78           C  
ANISOU 3742  CD2 LEU B  41     3206   5180   4068    767    463    246       C  
ATOM   3743  N   PRO B  42     -29.443 -29.559 -47.747  1.00 32.71           N  
ANISOU 3743  N   PRO B  42     3039   5101   4287    537    263    -14       N  
ATOM   3744  CA  PRO B  42     -28.718 -30.811 -47.975  1.00 32.68           C  
ANISOU 3744  CA  PRO B  42     2998   4991   4426    487    201   -119       C  
ATOM   3745  C   PRO B  42     -27.360 -30.814 -47.269  1.00 31.40           C  
ANISOU 3745  C   PRO B  42     2954   4707   4269    464    228    -20       C  
ATOM   3746  O   PRO B  42     -26.875 -31.880 -47.002  1.00 32.18           O  
ANISOU 3746  O   PRO B  42     3021   4654   4551    407    174    -55       O  
ATOM   3747  CB  PRO B  42     -28.571 -30.906 -49.495  1.00 33.44           C  
ANISOU 3747  CB  PRO B  42     3017   5253   4435    569    130   -312       C  
ATOM   3748  CG  PRO B  42     -29.660 -29.962 -50.013  1.00 34.07           C  
ANISOU 3748  CG  PRO B  42     3062   5512   4373    629    129   -280       C  
ATOM   3749  CD  PRO B  42     -29.722 -28.838 -48.998  1.00 32.79           C  
ANISOU 3749  CD  PRO B  42     3014   5294   4152    638    215    -74       C  
ATOM   3750  N   ASN B  43     -26.834 -29.637 -46.932  1.00 30.63           N  
ANISOU 3750  N   ASN B  43     2974   4655   4008    504    291    103       N  
ATOM   3751  CA  ASN B  43     -25.490 -29.466 -46.320  1.00 30.81           C  
ANISOU 3751  CA  ASN B  43     3104   4588   4016    488    308    192       C  
ATOM   3752  C   ASN B  43     -25.543 -29.485 -44.794  1.00 30.86           C  
ANISOU 3752  C   ASN B  43     3180   4486   4058    404    348    344       C  
ATOM   3753  O   ASN B  43     -24.450 -29.513 -44.178  1.00 28.90           O  
ANISOU 3753  O   ASN B  43     3009   4156   3817    378    338    420       O  
ATOM   3754  CB  ASN B  43     -24.833 -28.165 -46.759  1.00 30.52           C  
ANISOU 3754  CB  ASN B  43     3144   4649   3802    557    337    249       C  
ATOM   3755  CG  ASN B  43     -24.128 -28.353 -48.080  1.00 31.26           C  
ANISOU 3755  CG  ASN B  43     3175   4872   3832    603    304    137       C  
ATOM   3756  ND2 ASN B  43     -23.034 -27.633 -48.263  1.00 31.22           N  
ANISOU 3756  ND2 ASN B  43     3224   4911   3726    616    325    212       N  
ATOM   3757  OD1 ASN B  43     -24.557 -29.159 -48.910  1.00 31.77           O  
ANISOU 3757  OD1 ASN B  43     3126   5012   3933    620    259    -28       O  
ATOM   3758  N   VAL B  44     -26.733 -29.421 -44.196  1.00 32.22           N  
ANISOU 3758  N   VAL B  44     3315   4697   4229    363    393    386       N  
ATOM   3759  CA  VAL B  44     -26.851 -29.284 -42.713  1.00 32.89           C  
ANISOU 3759  CA  VAL B  44     3451   4773   4271    279    453    527       C  
ATOM   3760  C   VAL B  44     -27.783 -30.364 -42.155  1.00 34.64           C  
ANISOU 3760  C   VAL B  44     3567   4980   4615    152    454    592       C  
ATOM   3761  O   VAL B  44     -28.926 -30.406 -42.575  1.00 34.15           O  
ANISOU 3761  O   VAL B  44     3398   4994   4583    159    474    522       O  
ATOM   3762  CB  VAL B  44     -27.317 -27.883 -42.291  1.00 31.80           C  
ANISOU 3762  CB  VAL B  44     3358   4750   3973    348    534    521       C  
ATOM   3763  CG1 VAL B  44     -27.090 -27.704 -40.801  1.00 32.28           C  
ANISOU 3763  CG1 VAL B  44     3478   4844   3942    272    590    619       C  
ATOM   3764  CG2 VAL B  44     -26.625 -26.785 -43.067  1.00 30.52           C  
ANISOU 3764  CG2 VAL B  44     3270   4581   3744    462    508    480       C  
ATOM   3765  N   ASN B  45     -27.308 -31.154 -41.190  1.00 36.09           N  
ANISOU 3765  N   ASN B  45     3771   5075   4866     28    425    748       N  
ATOM   3766  CA  ASN B  45     -28.082 -32.264 -40.575  1.00 38.45           C  
ANISOU 3766  CA  ASN B  45     3962   5340   5306   -135    408    885       C  
ATOM   3767  C   ASN B  45     -28.913 -31.727 -39.401  1.00 39.38           C  
ANISOU 3767  C   ASN B  45     4059   5677   5227   -216    540   1001       C  
ATOM   3768  O   ASN B  45     -28.753 -30.551 -39.032  1.00 38.04           O  
ANISOU 3768  O   ASN B  45     3968   5643   4841   -128    623    942       O  
ATOM   3769  CB  ASN B  45     -27.172 -33.432 -40.182  1.00 39.26           C  
ANISOU 3769  CB  ASN B  45     4077   5228   5612   -236    279   1031       C  
ATOM   3770  CG  ASN B  45     -26.255 -33.117 -39.025  1.00 39.11           C  
ANISOU 3770  CG  ASN B  45     4175   5241   5443   -281    287   1211       C  
ATOM   3771  ND2 ASN B  45     -25.240 -33.928 -38.864  1.00 39.39           N  
ANISOU 3771  ND2 ASN B  45     4234   5076   5657   -318    152   1309       N  
ATOM   3772  OD1 ASN B  45     -26.493 -32.198 -38.249  1.00 40.10           O  
ANISOU 3772  OD1 ASN B  45     4354   5572   5310   -285    400   1250       O  
ATOM   3773  N   ALA B  46     -29.784 -32.569 -38.840  1.00 41.50           N  
ANISOU 3773  N   ALA B  46     4204   5986   5578   -382    555   1148       N  
ATOM   3774  CA  ALA B  46     -30.740 -32.174 -37.787  1.00 43.03           C  
ANISOU 3774  CA  ALA B  46     4322   6457   5572   -475    703   1238       C  
ATOM   3775  C   ALA B  46     -29.930 -31.709 -36.585  1.00 43.29           C  
ANISOU 3775  C   ALA B  46     4472   6612   5365   -511    744   1363       C  
ATOM   3776  O   ALA B  46     -30.084 -30.544 -36.159  1.00 43.36           O  
ANISOU 3776  O   ALA B  46     4513   6827   5135   -417    857   1234       O  
ATOM   3777  CB  ALA B  46     -31.645 -33.325 -37.448  1.00 45.29           C  
ANISOU 3777  CB  ALA B  46     4442   6751   6016   -685    693   1426       C  
ATOM   3778  N   ALA B  47     -29.063 -32.592 -36.096  1.00 44.15           N  
ANISOU 3778  N   ALA B  47     4635   6579   5561   -632    632   1589       N  
ATOM   3779  CA  ALA B  47     -28.205 -32.341 -34.926  1.00 45.01           C  
ANISOU 3779  CA  ALA B  47     4849   6802   5452   -691    631   1745       C  
ATOM   3780  C   ALA B  47     -27.753 -30.870 -34.958  1.00 43.30           C  
ANISOU 3780  C   ALA B  47     4745   6693   5016   -504    704   1501       C  
ATOM   3781  O   ALA B  47     -28.122 -30.093 -34.028  1.00 45.74           O  
ANISOU 3781  O   ALA B  47     5042   7291   5045   -514    825   1459       O  
ATOM   3782  CB  ALA B  47     -27.056 -33.322 -34.939  1.00 45.13           C  
ANISOU 3782  CB  ALA B  47     4927   6536   5684   -749    442   1928       C  
ATOM   3783  N   ILE B  48     -27.029 -30.485 -36.010  1.00 39.15           N  
ANISOU 3783  N   ILE B  48     4301   5955   4617   -343    633   1333       N  
ATOM   3784  CA  ILE B  48     -26.387 -29.144 -36.129  1.00 37.02           C  
ANISOU 3784  CA  ILE B  48     4142   5712   4210   -185    659   1148       C  
ATOM   3785  C   ILE B  48     -27.468 -28.085 -36.324  1.00 36.09           C  
ANISOU 3785  C   ILE B  48     3964   5755   3996    -78    779    945       C  
ATOM   3786  O   ILE B  48     -27.323 -26.999 -35.788  1.00 36.40           O  
ANISOU 3786  O   ILE B  48     4050   5905   3876     -4    828    825       O  
ATOM   3787  CB  ILE B  48     -25.369 -29.124 -37.293  1.00 34.89           C  
ANISOU 3787  CB  ILE B  48     3943   5200   4113    -72    554   1065       C  
ATOM   3788  CG1 ILE B  48     -24.234 -30.116 -37.066  1.00 34.53           C  
ANISOU 3788  CG1 ILE B  48     3937   4989   4196   -150    425   1225       C  
ATOM   3789  CG2 ILE B  48     -24.838 -27.717 -37.531  1.00 34.02           C  
ANISOU 3789  CG2 ILE B  48     3923   5102   3899     67    575    909       C  
ATOM   3790  CD1 ILE B  48     -23.405 -29.814 -35.840  1.00 35.32           C  
ANISOU 3790  CD1 ILE B  48     4123   5172   4124   -208    401   1343       C  
ATOM   3791  N   LEU B  49     -28.484 -28.384 -37.113  1.00 35.92           N  
ANISOU 3791  N   LEU B  49     3829   5721   4098    -58    802    889       N  
ATOM   3792  CA  LEU B  49     -29.536 -27.404 -37.431  1.00 36.89           C  
ANISOU 3792  CA  LEU B  49     3871   5966   4178     64    888    695       C  
ATOM   3793  C   LEU B  49     -30.213 -26.972 -36.135  1.00 39.66           C  
ANISOU 3793  C   LEU B  49     4147   6603   4318     15   1020    664       C  
ATOM   3794  O   LEU B  49     -30.500 -25.769 -36.021  1.00 39.93           O  
ANISOU 3794  O   LEU B  49     4172   6719   4280    155   1070    459       O  
ATOM   3795  CB  LEU B  49     -30.549 -28.026 -38.388  1.00 37.44           C  
ANISOU 3795  CB  LEU B  49     3808   6002   4417     60    875    669       C  
ATOM   3796  CG  LEU B  49     -31.589 -27.048 -38.926  1.00 37.80           C  
ANISOU 3796  CG  LEU B  49     3759   6137   4465    208    922    478       C  
ATOM   3797  CD1 LEU B  49     -30.917 -25.837 -39.554  1.00 36.19           C  
ANISOU 3797  CD1 LEU B  49     3673   5820   4259    384    861    366       C  
ATOM   3798  CD2 LEU B  49     -32.502 -27.748 -39.921  1.00 38.66           C  
ANISOU 3798  CD2 LEU B  49     3733   6215   4740    195    881    455       C  
ATOM   3799  N   LYS B  50     -30.452 -27.914 -35.209  1.00 42.37           N  
ANISOU 3799  N   LYS B  50     4424   7101   4574   -180   1067    861       N  
ATOM   3800  CA  LYS B  50     -31.007 -27.616 -33.857  1.00 45.67           C  
ANISOU 3800  CA  LYS B  50     4753   7880   4719   -263   1208    856       C  
ATOM   3801  C   LYS B  50     -30.131 -26.551 -33.204  1.00 44.52           C  
ANISOU 3801  C   LYS B  50     4733   7794   4389   -165   1203    712       C  
ATOM   3802  O   LYS B  50     -30.655 -25.482 -32.818  1.00 45.02           O  
ANISOU 3802  O   LYS B  50     4732   8042   4330    -47   1295    454       O  
ATOM   3803  CB  LYS B  50     -31.027 -28.850 -32.940  1.00 48.95           C  
ANISOU 3803  CB  LYS B  50     5115   8438   5047   -523   1219   1184       C  
ATOM   3804  CG  LYS B  50     -32.151 -29.865 -33.136  1.00 51.50           C  
ANISOU 3804  CG  LYS B  50     5252   8810   5505   -679   1260   1341       C  
ATOM   3805  CD  LYS B  50     -32.431 -30.653 -31.851  1.00 55.95           C  
ANISOU 3805  CD  LYS B  50     5716   9673   5871   -948   1329   1652       C  
ATOM   3806  CE  LYS B  50     -32.994 -32.045 -32.043  1.00 58.20           C  
ANISOU 3806  CE  LYS B  50     5872   9848   6392  -1170   1274   1955       C  
ATOM   3807  NZ  LYS B  50     -33.142 -32.690 -30.710  1.00 62.13           N1+
ANISOU 3807  NZ  LYS B  50     6283  10663   6659  -1448   1331   2313       N1+
ATOM   3808  N   LYS B  51     -28.828 -26.842 -33.131  1.00 43.14           N  
ANISOU 3808  N   LYS B  51     4715   7444   4232   -202   1081    850       N  
ATOM   3809  CA  LYS B  51     -27.805 -25.990 -32.475  1.00 42.52           C  
ANISOU 3809  CA  LYS B  51     4761   7395   3998   -143   1041    749       C  
ATOM   3810  C   LYS B  51     -27.875 -24.587 -33.075  1.00 40.44           C  
ANISOU 3810  C   LYS B  51     4523   7021   3820     77   1041    439       C  
ATOM   3811  O   LYS B  51     -27.804 -23.623 -32.311  1.00 41.55           O  
ANISOU 3811  O   LYS B  51     4666   7313   3809    143   1076    233       O  
ATOM   3812  CB  LYS B  51     -26.439 -26.651 -32.611  1.00 41.56           C  
ANISOU 3812  CB  LYS B  51     4778   7044   3971   -207    889    956       C  
ATOM   3813  CG  LYS B  51     -26.231 -27.799 -31.629  1.00 44.04           C  
ANISOU 3813  CG  LYS B  51     5073   7498   4164   -423    859   1270       C  
ATOM   3814  CD  LYS B  51     -24.937 -27.661 -30.847  1.00 44.84           C  
ANISOU 3814  CD  LYS B  51     5293   7614   4130   -458    753   1347       C  
ATOM   3815  CE  LYS B  51     -24.858 -28.432 -29.538  1.00 47.87           C  
ANISOU 3815  CE  LYS B  51     5645   8270   4272   -670    737   1637       C  
ATOM   3816  NZ  LYS B  51     -24.364 -27.591 -28.410  0.69 49.39           N1+
ANISOU 3816  NZ  LYS B  51     5883   8755   4126   -666    748   1516       N1+
ATOM   3817  N   VAL B  52     -28.089 -24.488 -34.376  1.00 37.25           N  
ANISOU 3817  N   VAL B  52     4119   6381   3654    180    994    403       N  
ATOM   3818  CA  VAL B  52     -28.095 -23.187 -35.093  1.00 36.24           C  
ANISOU 3818  CA  VAL B  52     4017   6100   3653    375    954    184       C  
ATOM   3819  C   VAL B  52     -29.364 -22.417 -34.719  1.00 37.93           C  
ANISOU 3819  C   VAL B  52     4081   6508   3824    474   1058    -54       C  
ATOM   3820  O   VAL B  52     -29.306 -21.219 -34.385  1.00 38.87           O  
ANISOU 3820  O   VAL B  52     4203   6620   3945    604   1045   -288       O  
ATOM   3821  CB  VAL B  52     -28.013 -23.416 -36.608  1.00 34.24           C  
ANISOU 3821  CB  VAL B  52     3787   5603   3620    433    871    257       C  
ATOM   3822  CG1 VAL B  52     -28.174 -22.111 -37.358  1.00 34.32           C  
ANISOU 3822  CG1 VAL B  52     3801   5478   3761    610    818     99       C  
ATOM   3823  CG2 VAL B  52     -26.719 -24.095 -37.004  1.00 32.58           C  
ANISOU 3823  CG2 VAL B  52     3694   5221   3464    362    775    429       C  
ATOM   3824  N   ILE B  53     -30.505 -23.081 -34.802  1.00 38.51           N  
ANISOU 3824  N   ILE B  53     4005   6735   3892    420   1149    -15       N  
ATOM   3825  CA  ILE B  53     -31.808 -22.447 -34.469  1.00 39.99           C  
ANISOU 3825  CA  ILE B  53     4004   7139   4051    515   1260   -252       C  
ATOM   3826  C   ILE B  53     -31.676 -21.903 -33.050  1.00 42.21           C  
ANISOU 3826  C   ILE B  53     4257   7701   4081    503   1348   -426       C  
ATOM   3827  O   ILE B  53     -31.896 -20.706 -32.850  1.00 44.22           O  
ANISOU 3827  O   ILE B  53     4464   7961   4377    676   1346   -732       O  
ATOM   3828  CB  ILE B  53     -32.959 -23.451 -34.629  1.00 40.53           C  
ANISOU 3828  CB  ILE B  53     3899   7370   4129    403   1353   -138       C  
ATOM   3829  CG1 ILE B  53     -33.147 -23.879 -36.084  1.00 38.42           C  
ANISOU 3829  CG1 ILE B  53     3643   6845   4110    440   1248    -39       C  
ATOM   3830  CG2 ILE B  53     -34.242 -22.855 -34.087  1.00 43.62           C  
ANISOU 3830  CG2 ILE B  53     4065   8052   4456    484   1491   -389       C  
ATOM   3831  CD1 ILE B  53     -33.966 -25.128 -36.241  1.00 39.04           C  
ANISOU 3831  CD1 ILE B  53     3585   7021   4229    281   1297    121       C  
ATOM   3832  N   GLN B  54     -31.272 -22.766 -32.123  1.00 42.88           N  
ANISOU 3832  N   GLN B  54     4367   7998   3926    305   1400   -232       N  
ATOM   3833  CA  GLN B  54     -30.981 -22.399 -30.723  1.00 45.32           C  
ANISOU 3833  CA  GLN B  54     4663   8633   3924    258   1470   -358       C  
ATOM   3834  C   GLN B  54     -30.132 -21.123 -30.703  1.00 45.51           C  
ANISOU 3834  C   GLN B  54     4805   8462   4022    431   1359   -622       C  
ATOM   3835  O   GLN B  54     -30.531 -20.152 -30.060  1.00 47.70           O  
ANISOU 3835  O   GLN B  54     4983   8922   4218    552   1414   -971       O  
ATOM   3836  CB  GLN B  54     -30.292 -23.574 -30.045  1.00 45.97           C  
ANISOU 3836  CB  GLN B  54     4821   8841   3806     15   1455     -3       C  
ATOM   3837  CG  GLN B  54     -30.019 -23.330 -28.572  1.00 49.45           C  
ANISOU 3837  CG  GLN B  54     5235   9690   3862    -67   1522    -84       C  
ATOM   3838  CD  GLN B  54     -29.308 -24.482 -27.909  1.00 50.43           C  
ANISOU 3838  CD  GLN B  54     5435   9927   3800   -311   1472    318       C  
ATOM   3839  NE2 GLN B  54     -29.133 -24.347 -26.600  1.00 53.99           N  
ANISOU 3839  NE2 GLN B  54     5848  10802   3862   -407   1528    284       N  
ATOM   3840  OE1 GLN B  54     -28.952 -25.486 -28.545  1.00 48.85           O  
ANISOU 3840  OE1 GLN B  54     5308   9451   3801   -411   1375    644       O  
ATOM   3841  N   TRP B  55     -29.011 -21.106 -31.420  1.00 43.91           N  
ANISOU 3841  N   TRP B  55     4789   7897   3999    446   1203   -480       N  
ATOM   3842  CA  TRP B  55     -28.074 -19.955 -31.402  1.00 44.14           C  
ANISOU 3842  CA  TRP B  55     4932   7716   4126    571   1079   -676       C  
ATOM   3843  C   TRP B  55     -28.801 -18.708 -31.892  1.00 44.94           C  
ANISOU 3843  C   TRP B  55     4942   7677   4458    792   1059   -990       C  
ATOM   3844  O   TRP B  55     -28.604 -17.679 -31.270  1.00 46.98           O  
ANISOU 3844  O   TRP B  55     5184   7952   4713    895   1024  -1291       O  
ATOM   3845  CB  TRP B  55     -26.798 -20.238 -32.201  1.00 42.08           C  
ANISOU 3845  CB  TRP B  55     4850   7112   4026    530    931   -435       C  
ATOM   3846  CG  TRP B  55     -25.821 -19.103 -32.168  1.00 42.56           C  
ANISOU 3846  CG  TRP B  55     5009   6961   4201    623    803   -598       C  
ATOM   3847  CD1 TRP B  55     -24.723 -18.965 -31.368  1.00 42.85           C  
ANISOU 3847  CD1 TRP B  55     5136   7034   4111    558    731   -613       C  
ATOM   3848  CD2 TRP B  55     -25.878 -17.918 -32.972  1.00 42.53           C  
ANISOU 3848  CD2 TRP B  55     5007   6665   4489    790    710   -757       C  
ATOM   3849  CE2 TRP B  55     -24.776 -17.122 -32.600  1.00 42.61           C  
ANISOU 3849  CE2 TRP B  55     5108   6529   4552    804    589   -861       C  
ATOM   3850  CE3 TRP B  55     -26.748 -17.466 -33.973  1.00 42.62           C  
ANISOU 3850  CE3 TRP B  55     4945   6519   4732    919    699   -798       C  
ATOM   3851  NE1 TRP B  55     -24.085 -17.783 -31.623  1.00 42.45           N  
ANISOU 3851  NE1 TRP B  55     5140   6724   4266    666    606   -786       N  
ATOM   3852  CZ2 TRP B  55     -24.541 -15.888 -33.190  1.00 43.60           C  
ANISOU 3852  CZ2 TRP B  55     5249   6337   4980    932    459   -989       C  
ATOM   3853  CZ3 TRP B  55     -26.521 -16.236 -34.544  1.00 43.52           C  
ANISOU 3853  CZ3 TRP B  55     5078   6332   5126   1054    564   -911       C  
ATOM   3854  CH2 TRP B  55     -25.427 -15.465 -34.159  1.00 43.99           C  
ANISOU 3854  CH2 TRP B  55     5226   6229   5257   1053    446   -995       C  
ATOM   3855  N   CYS B  56     -29.624 -18.798 -32.937  1.00 44.50           N  
ANISOU 3855  N   CYS B  56     4815   7487   4607    863   1064   -934       N  
ATOM   3856  CA  CYS B  56     -30.378 -17.644 -33.505  1.00 46.54           C  
ANISOU 3856  CA  CYS B  56     4972   7581   5131   1081   1012  -1187       C  
ATOM   3857  C   CYS B  56     -31.485 -17.202 -32.538  1.00 50.56           C  
ANISOU 3857  C   CYS B  56     5266   8421   5525   1169   1146  -1540       C  
ATOM   3858  O   CYS B  56     -31.625 -15.996 -32.309  1.00 52.37           O  
ANISOU 3858  O   CYS B  56     5432   8556   5910   1350   1083  -1878       O  
ATOM   3859  CB  CYS B  56     -31.009 -18.005 -34.840  1.00 45.59           C  
ANISOU 3859  CB  CYS B  56     4816   7295   5210   1115    977  -1006       C  
ATOM   3860  SG  CYS B  56     -29.797 -18.437 -36.111  1.00 43.63           S  
ANISOU 3860  SG  CYS B  56     4774   6715   5087   1039    831   -655       S  
ATOM   3861  N   THR B  57     -32.257 -18.155 -32.020  1.00 51.93           N  
ANISOU 3861  N   THR B  57     5311   8965   5456   1041   1320  -1465       N  
ATOM   3862  CA  THR B  57     -33.286 -17.931 -30.990  1.00 56.05           C  
ANISOU 3862  CA  THR B  57     5597   9918   5782   1078   1492  -1773       C  
ATOM   3863  C   THR B  57     -32.653 -17.109 -29.863  1.00 60.51           C  
ANISOU 3863  C   THR B  57     6184  10626   6181   1130   1481  -2090       C  
ATOM   3864  O   THR B  57     -33.127 -16.000 -29.629  1.00 62.64           O  
ANISOU 3864  O   THR B  57     6320  10893   6588   1337   1466  -2513       O  
ATOM   3865  CB  THR B  57     -33.879 -19.280 -30.585  1.00 55.63           C  
ANISOU 3865  CB  THR B  57     5442  10235   5458    850   1665  -1512       C  
ATOM   3866  CG2 THR B  57     -35.067 -19.185 -29.662  1.00 58.84           C  
ANISOU 3866  CG2 THR B  57     5566  11144   5648    857   1873  -1776       C  
ATOM   3867  OG1 THR B  57     -34.287 -19.872 -31.811  1.00 52.44           O  
ANISOU 3867  OG1 THR B  57     5045   9584   5294    835   1613  -1268       O  
ATOM   3868  N  AHIS B  58     -31.590 -17.619 -29.235  0.50 61.99           N  
ANISOU 3868  N  AHIS B  58     6528  10907   6117    958   1463  -1904       N  
ATOM   3869  N  BHIS B  58     -31.590 -17.619 -29.235  0.50 61.99           N  
ANISOU 3869  N  BHIS B  58     6528  10907   6117    958   1463  -1904       N  
ATOM   3870  CA AHIS B  58     -30.919 -17.011 -28.049  0.50 66.36           C  
ANISOU 3870  CA AHIS B  58     7104  11672   6438    965   1449  -2182       C  
ATOM   3871  CA BHIS B  58     -30.919 -17.011 -28.049  0.50 66.36           C  
ANISOU 3871  CA BHIS B  58     7104  11672   6438    965   1449  -2182       C  
ATOM   3872  C  AHIS B  58     -30.271 -15.672 -28.421  0.50 66.48           C  
ANISOU 3872  C  AHIS B  58     7206  11259   6796   1169   1251  -2464       C  
ATOM   3873  C  BHIS B  58     -30.271 -15.672 -28.421  0.50 66.48           C  
ANISOU 3873  C  BHIS B  58     7206  11259   6796   1169   1251  -2464       C  
ATOM   3874  O  AHIS B  58     -30.112 -14.835 -27.523  0.50 70.41           O  
ANISOU 3874  O  AHIS B  58     7640  11907   7205   1259   1235  -2870       O  
ATOM   3875  O  BHIS B  58     -30.112 -14.835 -27.523  0.50 70.41           O  
ANISOU 3875  O  BHIS B  58     7640  11907   7205   1259   1235  -2870       O  
ATOM   3876  CB AHIS B  58     -29.949 -18.007 -27.388  0.50 67.02           C  
ANISOU 3876  CB AHIS B  58     7332  11945   6188    717   1449  -1841       C  
ATOM   3877  CB BHIS B  58     -29.949 -18.007 -27.388  0.50 67.02           C  
ANISOU 3877  CB BHIS B  58     7332  11945   6188    717   1449  -1841       C  
ATOM   3878  CG AHIS B  58     -30.606 -18.741 -26.270  0.50 71.53           C  
ANISOU 3878  CG AHIS B  58     7743  13126   6311    550   1649  -1800       C  
ATOM   3879  CG BHIS B  58     -30.606 -18.741 -26.270  0.50 71.53           C  
ANISOU 3879  CG BHIS B  58     7743  13126   6311    550   1649  -1800       C  
ATOM   3880  CD2AHIS B  58     -31.558 -19.703 -26.280  0.50 72.79           C  
ANISOU 3880  CD2AHIS B  58     7763  13548   6347    411   1807  -1564       C  
ATOM   3881  CD2BHIS B  58     -31.558 -19.703 -26.280  0.50 72.79           C  
ANISOU 3881  CD2BHIS B  58     7763  13548   6347    411   1807  -1564       C  
ATOM   3882  ND1AHIS B  58     -30.362 -18.436 -24.936  0.50 76.03           N  
ANISOU 3882  ND1AHIS B  58     8252  14149   6486    506   1704  -2038       N  
ATOM   3883  ND1BHIS B  58     -30.362 -18.436 -24.936  0.50 76.03           N  
ANISOU 3883  ND1BHIS B  58     8252  14149   6486    506   1704  -2038       N  
ATOM   3884  CE1AHIS B  58     -31.117 -19.205 -24.171  0.50 79.07           C  
ANISOU 3884  CE1AHIS B  58     8471  15080   6493    335   1898  -1914       C  
ATOM   3885  CE1BHIS B  58     -31.117 -19.205 -24.171  0.50 79.07           C  
ANISOU 3885  CE1BHIS B  58     8471  15080   6493    335   1898  -1914       C  
ATOM   3886  NE2AHIS B  58     -31.862 -19.990 -24.975  0.50 77.75           N  
ANISOU 3886  NE2AHIS B  58     8250  14786   6505    269   1963  -1613       N  
ATOM   3887  NE2BHIS B  58     -31.862 -19.990 -24.975  0.50 77.75           N  
ANISOU 3887  NE2BHIS B  58     8250  14786   6505    269   1963  -1613       N  
ATOM   3888  N   HIS B  59     -29.941 -15.464 -29.694  1.00 63.75           N  
ANISOU 3888  N   HIS B  59     6981  10415   6827   1232   1101  -2264       N  
ATOM   3889  CA  HIS B  59     -29.518 -14.146 -30.220  1.00 65.67           C  
ANISOU 3889  CA  HIS B  59     7273  10210   7470   1419    901  -2476       C  
ATOM   3890  C   HIS B  59     -30.735 -13.431 -30.793  1.00 70.64           C  
ANISOU 3890  C   HIS B  59     7719  10714   8406   1634    892  -2704       C  
ATOM   3891  O   HIS B  59     -30.542 -12.690 -31.786  1.00 71.61           O  
ANISOU 3891  O   HIS B  59     7899  10379   8931   1750    709  -2645       O  
ATOM   3892  CB  HIS B  59     -28.414 -14.330 -31.252  1.00 62.18           C  
ANISOU 3892  CB  HIS B  59     7047   9354   7223   1340    745  -2090       C  
ATOM   3893  CG  HIS B  59     -27.096 -14.592 -30.622  1.00 61.39           C  
ANISOU 3893  CG  HIS B  59     7101   9293   6934   1195    693  -1990       C  
ATOM   3894  CD2 HIS B  59     -26.559 -15.726 -30.134  1.00 60.34           C  
ANISOU 3894  CD2 HIS B  59     7046   9404   6477    997    765  -1730       C  
ATOM   3895  ND1 HIS B  59     -26.200 -13.599 -30.362  1.00 62.79           N  
ANISOU 3895  ND1 HIS B  59     7345   9243   7272   1250    533  -2183       N  
ATOM   3896  CE1 HIS B  59     -25.133 -14.120 -29.785  1.00 62.89           C  
ANISOU 3896  CE1 HIS B  59     7474   9368   7053   1094    512  -2043       C  
ATOM   3897  NE2 HIS B  59     -25.331 -15.424 -29.634  1.00 60.85           N  
ANISOU 3897  NE2 HIS B  59     7226   9394   6498    943    648  -1757       N  
ATOM   3898  N   LYS B  60     -31.937 -13.618 -30.224  1.00 77.42           N  
ANISOU 3898  N   LYS B  60     8351  11965   9098   1682   1071  -2935       N  
ATOM   3899  CA  LYS B  60     -33.205 -13.055 -30.806  1.00 79.65           C  
ANISOU 3899  CA  LYS B  60     8426  12155   9684   1891   1067  -3138       C  
ATOM   3900  C   LYS B  60     -32.850 -11.746 -31.525  1.00 84.26           C  
ANISOU 3900  C   LYS B  60     9061  12183  10771   2094    804  -3267       C  
ATOM   3901  O   LYS B  60     -33.269 -11.614 -32.689  1.00 82.29           O  
ANISOU 3901  O   LYS B  60     8807  11636  10825   2170    700  -3066       O  
ATOM   3902  CB  LYS B  60     -34.329 -12.860 -29.769  1.00 80.80           C  
ANISOU 3902  CB  LYS B  60     8276  12781   9642   1988   1256  -3592       C  
ATOM   3903  CG  LYS B  60     -33.967 -12.142 -28.472  1.00 81.57           C  
ANISOU 3903  CG  LYS B  60     8307  13121   9565   2053   1277  -4074       C  
ATOM   3904  CD  LYS B  60     -34.482 -12.841 -27.209  1.00 82.17           C  
ANISOU 3904  CD  LYS B  60     8210  13922   9090   1918   1552  -4216       C  
ATOM   3905  CE  LYS B  60     -33.953 -12.238 -25.919  1.00 84.02           C  
ANISOU 3905  CE  LYS B  60     8404  14453   9065   1948   1563  -4663       C  
ATOM   3906  NZ  LYS B  60     -32.958 -13.093 -25.227  1.00 81.76           N1+
ANISOU 3906  NZ  LYS B  60     8303  14444   8318   1675   1609  -4351       N1+
ATOM   3907  N   ASP B  61     -32.029 -10.899 -30.864  1.00 91.81           N  
ANISOU 3907  N   ASP B  61    10075  13014  11793   2146    691  -3543       N  
ATOM   3908  CA  ASP B  61     -31.648  -9.492 -31.193  1.00 96.78           C  
ANISOU 3908  CA  ASP B  61    10717  13133  12921   2335    427  -3767       C  
ATOM   3909  C   ASP B  61     -30.146  -9.391 -31.554  1.00100.19           C  
ANISOU 3909  C   ASP B  61    11410  13224  13432   2194    260  -3460       C  
ATOM   3910  O   ASP B  61     -29.474  -8.427 -31.086  1.00 99.47           O  
ANISOU 3910  O   ASP B  61    11340  12910  13543   2261    100  -3739       O  
ATOM   3911  CB  ASP B  61     -32.006  -8.609 -29.992  1.00 98.06           C  
ANISOU 3911  CB  ASP B  61    10679  13480  13098   2512    441  -4427       C  
ATOM   3912  CG  ASP B  61     -32.168  -7.147 -30.336  1.00 99.43           C  
ANISOU 3912  CG  ASP B  61    10756  13141  13882   2772    178  -4756       C  
ATOM   3913  OD1 ASP B  61     -31.160  -6.516 -30.714  1.00 96.91           O  
ANISOU 3913  OD1 ASP B  61    10598  12360  13862   2749    -53  -4630       O  
ATOM   3914  OD2 ASP B  61     -33.300  -6.658 -30.223  1.00102.49           O1-
ANISOU 3914  OD2 ASP B  61    10891  13587  14463   2991    198  -5128       O1-
ATOM   3915  N   ASP B  62     -29.668 -10.316 -32.411  1.00105.08           N  
ANISOU 3915  N   ASP B  62    12199  13792  13936   2014    284  -2928       N  
ATOM   3916  CA  ASP B  62     -28.247 -10.723 -32.688  1.00107.36           C  
ANISOU 3916  CA  ASP B  62    12720  13934  14137   1819    215  -2566       C  
ATOM   3917  C   ASP B  62     -27.233  -9.820 -31.958  1.00113.29           C  
ANISOU 3917  C   ASP B  62    13527  14515  15001   1831     67  -2823       C  
ATOM   3918  O   ASP B  62     -26.603  -8.957 -32.576  1.00113.37           O  
ANISOU 3918  O   ASP B  62    13603  14078  15396   1864   -146  -2744       O  
ATOM   3919  CB  ASP B  62     -28.045 -10.859 -34.219  1.00104.35           C  
ANISOU 3919  CB  ASP B  62    12437  13223  13987   1780    109  -2110       C  
ATOM   3920  CG  ASP B  62     -27.465 -12.184 -34.719  1.00101.07           C  
ANISOU 3920  CG  ASP B  62    12161  12950  13290   1572    209  -1676       C  
ATOM   3921  OD1 ASP B  62     -26.289 -12.461 -34.406  1.00101.71           O  
ANISOU 3921  OD1 ASP B  62    12376  13027  13242   1435    188  -1558       O  
ATOM   3922  OD2 ASP B  62     -28.179 -12.918 -35.445  1.00 94.96           O1-
ANISOU 3922  OD2 ASP B  62    11350  12274  12457   1556    289  -1474       O1-
ATOM   3923  N   PRO B  63     -27.013  -9.975 -30.620  1.00118.96           N  
ANISOU 3923  N   PRO B  63    14214  15596  15390   1789    161  -3128       N  
ATOM   3924  CA  PRO B  63     -25.914  -9.293 -29.931  1.00121.30           C  
ANISOU 3924  CA  PRO B  63    14579  15768  15742   1763     14  -3340       C  
ATOM   3925  C   PRO B  63     -24.676 -10.161 -29.640  1.00122.38           C  
ANISOU 3925  C   PRO B  63    14893  16049  15558   1531     37  -3029       C  
ATOM   3926  O   PRO B  63     -24.356 -10.373 -28.462  1.00126.99           O  
ANISOU 3926  O   PRO B  63    15465  16985  15801   1468     92  -3245       O  
ATOM   3927  CB  PRO B  63     -26.628  -8.843 -28.634  1.00120.94           C  
ANISOU 3927  CB  PRO B  63    14342  16087  15524   1897     97  -3945       C  
ATOM   3928  CG  PRO B  63     -27.670  -9.929 -28.361  1.00119.82           C  
ANISOU 3928  CG  PRO B  63    14099  16464  14964   1847    370  -3861       C  
ATOM   3929  CD  PRO B  63     -27.841 -10.716 -29.652  1.00119.23           C  
ANISOU 3929  CD  PRO B  63    14119  16201  14981   1764    399  -3312       C  
ATOM   3930  N   PRO B  64     -23.915 -10.687 -30.652  1.00116.00           N  
ANISOU 3930  N   PRO B  64    14236  15006  14832   1399    -11  -2535       N  
ATOM   3931  CA  PRO B  64     -22.597 -11.280 -30.381  1.00113.83           C  
ANISOU 3931  CA  PRO B  64    14104  14785  14361   1212    -42  -2302       C  
ATOM   3932  C   PRO B  64     -21.489 -10.203 -30.367  1.00115.65           C  
ANISOU 3932  C   PRO B  64    14386  14646  14910   1213   -271  -2415       C  
ATOM   3933  O   PRO B  64     -20.942  -9.906 -31.429  1.00112.51           O  
ANISOU 3933  O   PRO B  64    14052  13877  14820   1178   -384  -2129       O  
ATOM   3934  CB  PRO B  64     -22.426 -12.340 -31.492  1.00105.65           C  
ANISOU 3934  CB  PRO B  64    13159  13696  13286   1097     25  -1790       C  
ATOM   3935  CG  PRO B  64     -23.294 -11.846 -32.643  1.00104.10           C  
ANISOU 3935  CG  PRO B  64    12904  13239  13411   1224     -4  -1724       C  
ATOM   3936  CD  PRO B  64     -24.271 -10.829 -32.078  1.00108.44           C  
ANISOU 3936  CD  PRO B  64    13303  13782  14117   1418    -30  -2183       C  
ATOM   3937  N   ASP B  65     -21.196  -9.627 -29.187  1.00119.41           N  
ANISOU 3937  N   ASP B  65    14817  15249  15306   1243   -337  -2831       N  
ATOM   3938  CA  ASP B  65     -20.138  -8.584 -29.006  1.00119.37           C  
ANISOU 3938  CA  ASP B  65    14839  14905  15612   1234   -573  -3001       C  
ATOM   3939  C   ASP B  65     -18.777  -9.267 -29.251  1.00116.78           C  
ANISOU 3939  C   ASP B  65    14650  14548  15173   1028   -611  -2596       C  
ATOM   3940  O   ASP B  65     -18.304  -9.246 -30.408  1.00116.52           O  
ANISOU 3940  O   ASP B  65    14677  14194  15403    969   -670  -2223       O  
ATOM   3941  CB  ASP B  65     -20.156  -7.831 -27.660  1.00121.16           C  
ANISOU 3941  CB  ASP B  65    14967  15302  15766   1321   -646  -3601       C  
ATOM   3942  CG  ASP B  65     -21.439  -7.787 -26.834  1.00123.48           C  
ANISOU 3942  CG  ASP B  65    15101  15993  15820   1473   -495  -4046       C  
ATOM   3943  OD1 ASP B  65     -22.537  -7.948 -27.402  1.00122.26           O  
ANISOU 3943  OD1 ASP B  65    14876  15845  15730   1573   -377  -3980       O  
ATOM   3944  OD2 ASP B  65     -21.323  -7.573 -25.612  1.00124.94           O1-
ANISOU 3944  OD2 ASP B  65    15217  16508  15745   1490   -499  -4476       O1-
ATOM   3945  N   ASP B  66     -18.190  -9.899 -28.230  1.00112.63           N  
ANISOU 3945  N   ASP B  66    14159  14380  14257    922   -576  -2649       N  
ATOM   3946  CA  ASP B  66     -16.954 -10.717 -28.355  1.00106.40           C  
ANISOU 3946  CA  ASP B  66    13477  13621  13329    739   -604  -2273       C  
ATOM   3947  C   ASP B  66     -17.403 -12.180 -28.383  1.00 98.30           C  
ANISOU 3947  C   ASP B  66    12485  12947  11918    665   -404  -1963       C  
ATOM   3948  O   ASP B  66     -18.122 -12.549 -29.336  1.00 90.42           O  
ANISOU 3948  O   ASP B  66    11483  11861  11010    703   -299  -1746       O  
ATOM   3949  CB  ASP B  66     -15.984 -10.392 -27.219  1.00112.92           C  
ANISOU 3949  CB  ASP B  66    14305  14571  14028    673   -746  -2528       C  
ATOM   3950  CG  ASP B  66     -16.652 -10.387 -25.852  1.00119.73           C  
ANISOU 3950  CG  ASP B  66    15090  15900  14502    732   -678  -2950       C  
ATOM   3951  OD1 ASP B  66     -17.736  -9.762 -25.705  1.00122.63           O  
ANISOU 3951  OD1 ASP B  66    15355  16296  14945    889   -624  -3301       O  
ATOM   3952  OD2 ASP B  66     -16.094 -11.030 -24.947  1.00123.51           O1-
ANISOU 3952  OD2 ASP B  66    15595  16738  14594    620   -680  -2919       O1-
ATOM   3953  N   ILE B  67     -16.995 -12.958 -27.371  1.00 95.37           N  
ANISOU 3953  N   ILE B  67    12136  12950  11151    560   -377  -1939       N  
ATOM   3954  CA  ILE B  67     -17.643 -14.230 -26.926  1.00 90.49           C  
ANISOU 3954  CA  ILE B  67    11510  12754  10117    491   -201  -1752       C  
ATOM   3955  C   ILE B  67     -18.432 -13.961 -25.635  1.00 88.61           C  
ANISOU 3955  C   ILE B  67    11173  12959   9538    538   -127  -2145       C  
ATOM   3956  O   ILE B  67     -17.848 -14.016 -24.549  1.00 88.38           O  
ANISOU 3956  O   ILE B  67    11143  13217   9219    463   -194  -2269       O  
ATOM   3957  CB  ILE B  67     -16.569 -15.337 -26.758  1.00 88.58           C  
ANISOU 3957  CB  ILE B  67    11350  12606   9700    325   -251  -1380       C  
ATOM   3958  CG1 ILE B  67     -15.451 -15.224 -27.799  1.00 85.49           C  
ANISOU 3958  CG1 ILE B  67    11022  11800   9661    291   -370  -1147       C  
ATOM   3959  CG2 ILE B  67     -17.200 -16.724 -26.799  1.00 86.91           C  
ANISOU 3959  CG2 ILE B  67    11139  12642   9241    246    -98  -1054       C  
ATOM   3960  CD1 ILE B  67     -15.958 -15.330 -29.214  1.00 83.65           C  
ANISOU 3960  CD1 ILE B  67    10792  11296   9694    345   -287   -943       C  
ATOM   3961  N   PRO B  68     -19.759 -13.640 -25.696  1.00 84.12           N  
ANISOU 3961  N   PRO B  68    10495  12490   8976    664      9  -2372       N  
ATOM   3962  CA  PRO B  68     -20.596 -13.578 -24.489  1.00 84.80           C  
ANISOU 3962  CA  PRO B  68    10452  13096   8671    695    129  -2721       C  
ATOM   3963  C   PRO B  68     -20.617 -14.912 -23.714  1.00 82.15           C  
ANISOU 3963  C   PRO B  68    10127  13268   7819    507    245  -2411       C  
ATOM   3964  O   PRO B  68     -20.224 -15.945 -24.251  1.00 81.00           O  
ANISOU 3964  O   PRO B  68    10076  13016   7684    382    249  -1930       O  
ATOM   3965  CB  PRO B  68     -22.009 -13.232 -24.994  1.00 84.79           C  
ANISOU 3965  CB  PRO B  68    10324  13060   8831    852    268  -2897       C  
ATOM   3966  CG  PRO B  68     -21.761 -12.583 -26.343  1.00 83.90           C  
ANISOU 3966  CG  PRO B  68    10277  12326   9274    947    140  -2788       C  
ATOM   3967  CD  PRO B  68     -20.515 -13.253 -26.899  1.00 80.12           C  
ANISOU 3967  CD  PRO B  68     9961  11633   8848    789     46  -2330       C  
ATOM   3968  N   VAL B  69     -21.070 -14.879 -22.460  1.00 81.03           N  
ANISOU 3968  N   VAL B  69     9871  13680   7235    484    330  -2689       N  
ATOM   3969  CA  VAL B  69     -20.982 -16.053 -21.538  1.00 77.91           C  
ANISOU 3969  CA  VAL B  69     9476  13819   6308    276    404  -2378       C  
ATOM   3970  C   VAL B  69     -21.814 -17.209 -22.116  1.00 71.51           C  
ANISOU 3970  C   VAL B  69     8650  13052   5470    186    574  -1934       C  
ATOM   3971  O   VAL B  69     -21.298 -18.323 -22.101  1.00 68.59           O  
ANISOU 3971  O   VAL B  69     8364  12716   4982     12    538  -1458       O  
ATOM   3972  CB  VAL B  69     -21.360 -15.685 -20.085  1.00 82.72           C  
ANISOU 3972  CB  VAL B  69     9940  15081   6408    267    471  -2793       C  
ATOM   3973  CG1 VAL B  69     -22.854 -15.401 -19.906  1.00 84.62           C  
ANISOU 3973  CG1 VAL B  69     9979  15642   6529    375    701  -3114       C  
ATOM   3974  CG2 VAL B  69     -20.855 -16.749 -19.111  1.00 84.02           C  
ANISOU 3974  CG2 VAL B  69    10137  15740   6047     28    456  -2424       C  
ATOM   3975  N   TRP B  70     -23.026 -16.933 -22.613  1.00 67.72           N  
ANISOU 3975  N   TRP B  70     8053  12543   5132    306    729  -2100       N  
ATOM   3976  CA  TRP B  70     -23.943 -17.953 -23.188  1.00 64.19           C  
ANISOU 3976  CA  TRP B  70     7563  12137   4691    229    888  -1735       C  
ATOM   3977  C   TRP B  70     -23.254 -18.693 -24.341  1.00 59.88           C  
ANISOU 3977  C   TRP B  70     7177  11098   4478    169    783  -1271       C  
ATOM   3978  O   TRP B  70     -23.313 -19.933 -24.387  1.00 58.53           O  
ANISOU 3978  O   TRP B  70     7026  11020   4193      3    823   -839       O  
ATOM   3979  CB  TRP B  70     -25.251 -17.319 -23.669  1.00 63.01           C  
ANISOU 3979  CB  TRP B  70     7257  11952   4730    407   1028  -2049       C  
ATOM   3980  CG  TRP B  70     -26.233 -18.350 -24.121  1.00 60.75           C  
ANISOU 3980  CG  TRP B  70     6897  11771   4414    313   1190  -1715       C  
ATOM   3981  CD1 TRP B  70     -27.102 -19.017 -23.327  1.00 62.77           C  
ANISOU 3981  CD1 TRP B  70     6996  12577   4278    181   1377  -1639       C  
ATOM   3982  CD2 TRP B  70     -26.389 -18.903 -25.443  1.00 56.80           C  
ANISOU 3982  CD2 TRP B  70     6467  10841   4274    317   1168  -1389       C  
ATOM   3983  CE2 TRP B  70     -27.408 -19.873 -25.362  1.00 56.78           C  
ANISOU 3983  CE2 TRP B  70     6339  11128   4106    193   1338  -1160       C  
ATOM   3984  CE3 TRP B  70     -25.790 -18.665 -26.687  1.00 52.84           C  
ANISOU 3984  CE3 TRP B  70     6103   9773   4202    405   1025  -1277       C  
ATOM   3985  NE1 TRP B  70     -27.828 -19.908 -24.065  1.00 60.96           N  
ANISOU 3985  NE1 TRP B  70     6728  12250   4183    105   1467  -1301       N  
ATOM   3986  CZ2 TRP B  70     -27.843 -20.600 -26.468  1.00 53.74           C  
ANISOU 3986  CZ2 TRP B  70     5967  10462   3990    167   1352   -864       C  
ATOM   3987  CZ3 TRP B  70     -26.211 -19.395 -27.781  1.00 50.09           C  
ANISOU 3987  CZ3 TRP B  70     5766   9194   4070    381   1053   -982       C  
ATOM   3988  CH2 TRP B  70     -27.229 -20.347 -27.671  1.00 50.49           C  
ANISOU 3988  CH2 TRP B  70     5696   9516   3972    270   1207   -798       C  
ATOM   3989  N   ASP B  71     -22.638 -17.929 -25.237  1.00 57.57           N  
ANISOU 3989  N   ASP B  71     6975  10304   4593    299    648  -1374       N  
ATOM   3990  CA  ASP B  71     -21.974 -18.422 -26.464  1.00 53.89           C  
ANISOU 3990  CA  ASP B  71     6635   9376   4464    276    555  -1020       C  
ATOM   3991  C   ASP B  71     -20.822 -19.355 -26.073  1.00 23.80           C  
ATOM   3992  O   ASP B  71     -20.614 -20.381 -26.743  1.00 47.42           O  
ANISOU 3992  O   ASP B  71     5967   8435   3618     24    435   -304       O  
ATOM   3993  CB  ASP B  71     -21.535 -17.222 -27.303  1.00 54.62           C  
ANISOU 3993  CB  ASP B  71     6775   9018   4963    433    433  -1234       C  
ATOM   3994  CG  ASP B  71     -22.639 -16.595 -28.149  1.00 56.06           C  
ANISOU 3994  CG  ASP B  71     6872   9019   5408    594    503  -1399       C  
ATOM   3995  OD1 ASP B  71     -23.402 -17.361 -28.764  1.00 56.24           O  
ANISOU 3995  OD1 ASP B  71     6860   9062   5445    570    611  -1183       O  
ATOM   3996  OD2 ASP B  71     -22.689 -15.345 -28.259  1.00 59.62           O1-
ANISOU 3996  OD2 ASP B  71     7291   9268   6095    743    423  -1728       O1-
ATOM   3997  N   GLN B  72     -20.100 -19.008 -25.012  1.00 54.96           N  
ANISOU 3997  N   GLN B  72     6890   9772   4222     60    353   -820       N  
ATOM   3998  CA  GLN B  72     -18.970 -19.841 -24.530  1.00 56.20           C  
ANISOU 3998  CA  GLN B  72     7128   9991   4235    -95    219   -502       C  
ATOM   3999  C   GLN B  72     -19.507 -21.222 -24.169  1.00 56.39           C  
ANISOU 3999  C   GLN B  72     7115  10297   4014   -260    306   -109       C  
ATOM   4000  O   GLN B  72     -18.912 -22.214 -24.625  1.00 54.16           O  
ANISOU 4000  O   GLN B  72     6895   9805   3880   -347    220    274       O  
ATOM   4001  CB  GLN B  72     -18.269 -19.259 -23.296  1.00 60.81           C  
ANISOU 4001  CB  GLN B  72     7711  10862   4532   -127    105   -739       C  
ATOM   4002  CG  GLN B  72     -17.776 -17.828 -23.458  1.00 62.14           C  
ANISOU 4002  CG  GLN B  72     7892  10773   4946     20     -2  -1171       C  
ATOM   4003  CD  GLN B  72     -16.499 -17.549 -22.697  1.00 64.87           C  
ANISOU 4003  CD  GLN B  72     8283  11178   5184    -41   -204  -1244       C  
ATOM   4004  NE2 GLN B  72     -15.538 -16.926 -23.366  1.00 64.16           N  
ANISOU 4004  NE2 GLN B  72     8253  10649   5475     10   -354  -1294       N  
ATOM   4005  OE1 GLN B  72     -16.365 -17.896 -21.525  1.00 67.99           O  
ANISOU 4005  OE1 GLN B  72     8651  12029   5152   -146   -231  -1239       O  
ATOM   4006  N   GLU B  73     -20.568 -21.282 -23.359  1.00 59.51           N  
ANISOU 4006  N   GLU B  73     7394  11155   4062   -307    462   -206       N  
ATOM   4007  CA  GLU B  73     -21.106 -22.577 -22.891  1.00 61.55           C  
ANISOU 4007  CA  GLU B  73     7595  11723   4066   -503    539    205       C  
ATOM   4008  C   GLU B  73     -21.730 -23.275 -24.096  1.00 25.39           C  
ATOM   4009  O   GLU B  73     -21.486 -24.475 -24.271  1.00 56.89           O  
ANISOU 4009  O   GLU B  73     7025  10693   3896   -628    546    862       O  
ATOM   4010  CB  GLU B  73     -22.036 -22.427 -21.689  1.00 67.79           C  
ANISOU 4010  CB  GLU B  73     8238  13159   4361   -577    700     47       C  
ATOM   4011  CG  GLU B  73     -22.170 -23.731 -20.898  1.00 72.10           C  
ANISOU 4011  CG  GLU B  73     8740  14085   4571   -839    709    549       C  
ATOM   4012  CD  GLU B  73     -21.026 -24.073 -19.936  1.00 76.06           C  
ANISOU 4012  CD  GLU B  73     9314  14794   4792   -979    513    770       C  
ATOM   4013  OE1 GLU B  73     -19.986 -23.340 -19.924  1.00 75.53           O  
ANISOU 4013  OE1 GLU B  73     9342  14537   4820   -872    354    532       O  
ATOM   4014  OE2 GLU B  73     -21.154 -25.080 -19.198  1.00 80.13           O1-
ANISOU 4014  OE2 GLU B  73     9782  15655   5008  -1205    502   1205       O1-
ATOM   4015  N   PHE B  74     -22.409 -22.529 -24.963  1.00 55.06           N  
ANISOU 4015  N   PHE B  74     6731  10349   3839   -318    703    150       N  
ATOM   4016  CA  PHE B  74     -23.018 -23.075 -26.198  1.00 51.66           C  
ANISOU 4016  CA  PHE B  74     6287   9606   3736   -286    758    313       C  
ATOM   4017  C   PHE B  74     -21.944 -23.770 -27.030  1.00 48.57           C  
ANISOU 4017  C   PHE B  74     6017   8797   3641   -313    598    601       C  
ATOM   4018  O   PHE B  74     -22.293 -24.759 -27.711  1.00 48.45           O  
ANISOU 4018  O   PHE B  74     5981   8627   3801   -372    612    860       O  
ATOM   4019  CB  PHE B  74     -23.670 -21.965 -27.019  1.00 50.84           C  
ANISOU 4019  CB  PHE B  74     6144   9305   3869    -76    826    -50       C  
ATOM   4020  CG  PHE B  74     -24.166 -22.403 -28.372  1.00 48.96           C  
ANISOU 4020  CG  PHE B  74     5900   8743   3960    -28    850     90       C  
ATOM   4021  CD1 PHE B  74     -25.257 -23.256 -28.476  1.00 50.27           C  
ANISOU 4021  CD1 PHE B  74     5953   9061   4085   -114    973    254       C  
ATOM   4022  CD2 PHE B  74     -23.542 -21.982 -29.539  1.00 46.33           C  
ANISOU 4022  CD2 PHE B  74     5658   7983   3962     87    747     66       C  
ATOM   4023  CE1 PHE B  74     -25.717 -23.684 -29.714  1.00 47.61           C  
ANISOU 4023  CE1 PHE B  74     5602   8446   4042    -72    978    356       C  
ATOM   4024  CE2 PHE B  74     -23.993 -22.419 -30.774  1.00 44.55           C  
ANISOU 4024  CE2 PHE B  74     5418   7523   3988    123    765    185       C  
ATOM   4025  CZ  PHE B  74     -25.094 -23.249 -30.855  1.00 45.54           C  
ANISOU 4025  CZ  PHE B  74     5435   7795   4073     53    875    306       C  
ATOM   4026  N   LEU B  75     -20.728 -23.217 -27.044  1.00 47.33           N  
ANISOU 4026  N   LEU B  75     5959   8457   3568   -259    452    515       N  
ATOM   4027  CA  LEU B  75     -19.624 -23.683 -27.931  1.00 43.69           C  
ANISOU 4027  CA  LEU B  75     5586   7601   3413   -252    308    711       C  
ATOM   4028  C   LEU B  75     -18.696 -24.629 -27.188  1.00 44.29           C  
ANISOU 4028  C   LEU B  75     5696   7756   3375   -399    166   1017       C  
ATOM   4029  O   LEU B  75     -17.711 -24.990 -27.797  1.00 41.39           O  
ANISOU 4029  O   LEU B  75     5379   7095   3253   -384     40   1142       O  
ATOM   4030  CB  LEU B  75     -18.857 -22.486 -28.497  1.00 41.97           C  
ANISOU 4030  CB  LEU B  75     5428   7121   3398   -114    234    456       C  
ATOM   4031  CG  LEU B  75     -19.620 -21.699 -29.560  1.00 40.49           C  
ANISOU 4031  CG  LEU B  75     5214   6738   3435     32    323    256       C  
ATOM   4032  CD1 LEU B  75     -18.889 -20.447 -29.964  1.00 40.03           C  
ANISOU 4032  CD1 LEU B  75     5201   6439   3570    138    232     41       C  
ATOM   4033  CD2 LEU B  75     -19.897 -22.547 -30.781  1.00 38.10           C  
ANISOU 4033  CD2 LEU B  75     4900   6222   3356     34    353    465       C  
ATOM   4034  N   LYS B  76     -19.041 -25.074 -25.977  1.00 48.06           N  
ANISOU 4034  N   LYS B  76     6131   8627   3503   -540    185   1154       N  
ATOM   4035  CA  LYS B  76     -18.237 -26.125 -25.292  1.00 50.62           C  
ANISOU 4035  CA  LYS B  76     6478   9017   3740   -698     21   1532       C  
ATOM   4036  C   LYS B  76     -18.652 -27.477 -25.879  1.00 49.25           C  
ANISOU 4036  C   LYS B  76     6264   8652   3796   -786     14   1888       C  
ATOM   4037  O   LYS B  76     -19.296 -28.232 -25.166  1.00 51.29           O  
ANISOU 4037  O   LYS B  76     6457   9176   3854   -949     47   2153       O  
ATOM   4038  CB  LYS B  76     -18.354 -26.057 -23.764  1.00 56.11           C  
ANISOU 4038  CB  LYS B  76     7138  10237   3945   -833     17   1576       C  
ATOM   4039  CG  LYS B  76     -17.300 -25.180 -23.087  1.00 59.06           C  
ANISOU 4039  CG  LYS B  76     7568  10715   4159   -790   -115   1353       C  
ATOM   4040  CD  LYS B  76     -17.708 -24.575 -21.730  1.00 64.14           C  
ANISOU 4040  CD  LYS B  76     8153  11940   4278   -851    -51   1150       C  
ATOM   4041  CE  LYS B  76     -16.955 -23.293 -21.375  1.00 65.50           C  
ANISOU 4041  CE  LYS B  76     8362  12136   4389   -735   -138    716       C  
ATOM   4042  NZ  LYS B  76     -17.087 -22.943 -19.935  1.00 70.09           N1+
ANISOU 4042  NZ  LYS B  76     8882  13322   4427   -820   -135    560       N1+
ATOM   4043  N   VAL B  77     -18.279 -27.739 -27.140  1.00 45.68           N  
ANISOU 4043  N   VAL B  77     5836   7769   3751   -684    -31   1879       N  
ATOM   4044  CA  VAL B  77     -18.572 -28.982 -27.923  1.00 44.05           C  
ANISOU 4044  CA  VAL B  77     5584   7299   3856   -729    -63   2128       C  
ATOM   4045  C   VAL B  77     -17.256 -29.531 -28.500  1.00 42.51           C  
ANISOU 4045  C   VAL B  77     5420   6746   3986   -681   -258   2228       C  
ATOM   4046  O   VAL B  77     -16.268 -28.781 -28.478  1.00 41.87           O  
ANISOU 4046  O   VAL B  77     5394   6621   3894   -600   -324   2069       O  
ATOM   4047  CB  VAL B  77     -19.600 -28.680 -29.027  1.00 41.50           C  
ANISOU 4047  CB  VAL B  77     5219   6858   3691   -624    102   1919       C  
ATOM   4048  CG1 VAL B  77     -20.873 -28.125 -28.426  1.00 42.74           C  
ANISOU 4048  CG1 VAL B  77     5314   7374   3550   -656    289   1795       C  
ATOM   4049  CG2 VAL B  77     -19.069 -27.714 -30.079  1.00 38.30           C  
ANISOU 4049  CG2 VAL B  77     4867   6216   3470   -437    113   1621       C  
ATOM   4050  N   ASP B  78     -17.221 -30.780 -28.983  1.00 42.31           N  
ANISOU 4050  N   ASP B  78     5343   6471   4261   -726   -356   2460       N  
ATOM   4051  CA  ASP B  78     -15.971 -31.352 -29.546  1.00 41.79           C  
ANISOU 4051  CA  ASP B  78     5272   6072   4535   -660   -543   2511       C  
ATOM   4052  C   ASP B  78     -15.585 -30.540 -30.793  1.00 20.43           C  
ATOM   4053  O   ASP B  78     -16.448 -29.859 -31.369  1.00 36.97           O  
ANISOU 4053  O   ASP B  78     4683   5343   4021   -415   -290   1966       O  
ATOM   4054  CB  ASP B  78     -16.086 -32.852 -29.813  1.00 42.91           C  
ANISOU 4054  CB  ASP B  78     5332   5962   5011   -731   -678   2782       C  
ATOM   4055  CG  ASP B  78     -17.184 -33.265 -30.776  1.00 41.86           C  
ANISOU 4055  CG  ASP B  78     5134   5701   5068   -710   -560   2696       C  
ATOM   4056  OD1 ASP B  78     -17.299 -32.666 -31.846  1.00 39.41           O  
ANISOU 4056  OD1 ASP B  78     4829   5310   4835   -566   -445   2392       O  
ATOM   4057  OD2 ASP B  78     -17.887 -34.220 -30.459  1.00 43.95           O1-
ANISOU 4057  OD2 ASP B  78     5337   5946   5418   -849   -602   2954       O1-
ATOM   4058  N   GLN B  79     -14.317 -30.598 -31.180  1.00 38.84           N  
ANISOU 4058  N   GLN B  79     4904   5329   4524   -402   -590   2128       N  
ATOM   4059  CA  GLN B  79     -13.803 -29.931 -32.394  1.00 37.37           C  
ANISOU 4059  CA  GLN B  79     4706   4998   4493   -257   -525   1859       C  
ATOM   4060  C   GLN B  79     -14.647 -30.354 -33.600  1.00 36.59           C  
ANISOU 4060  C   GLN B  79     4551   4778   4575   -197   -421   1761       C  
ATOM   4061  O   GLN B  79     -14.985 -29.452 -34.407  1.00 35.49           O  
ANISOU 4061  O   GLN B  79     4429   4672   4386   -114   -284   1551       O  
ATOM   4062  CB  GLN B  79     -12.328 -30.248 -32.616  1.00 37.82           C  
ANISOU 4062  CB  GLN B  79     4713   4883   4775   -206   -686   1868       C  
ATOM   4063  CG  GLN B  79     -11.427 -29.576 -31.597  1.00 39.30           C  
ANISOU 4063  CG  GLN B  79     4951   5200   4782   -246   -785   1900       C  
ATOM   4064  CD  GLN B  79      -9.992 -30.025 -31.721  1.00 40.70           C  
ANISOU 4064  CD  GLN B  79     5049   5212   5202   -204   -965   1938       C  
ATOM   4065  NE2 GLN B  79      -9.208 -29.800 -30.680  1.00 42.47           N  
ANISOU 4065  NE2 GLN B  79     5298   5537   5302   -261  -1111   2036       N  
ATOM   4066  OE1 GLN B  79      -9.564 -30.544 -32.747  1.00 41.69           O  
ANISOU 4066  OE1 GLN B  79     5078   5145   5619   -116   -977   1855       O  
ATOM   4067  N   GLY B  80     -14.972 -31.647 -33.724  1.00 37.30           N  
ANISOU 4067  N   GLY B  80     4570   4724   4880   -242   -501   1909       N  
ATOM   4068  CA  GLY B  80     -15.851 -32.160 -34.801  1.00 36.50           C  
ANISOU 4068  CA  GLY B  80     4399   4515   4956   -199   -425   1803       C  
ATOM   4069  C   GLY B  80     -17.092 -31.287 -34.983  1.00 35.27           C  
ANISOU 4069  C   GLY B  80     4283   4549   4568   -194   -230   1685       C  
ATOM   4070  O   GLY B  80     -17.260 -30.697 -36.071  1.00 34.06           O  
ANISOU 4070  O   GLY B  80     4119   4385   4437    -87   -134   1469       O  
ATOM   4071  N   THR B  81     -17.901 -31.163 -33.924  1.00 35.91           N  
ANISOU 4071  N   THR B  81     4396   4828   4419   -307   -179   1826       N  
ATOM   4072  CA  THR B  81     -19.164 -30.378 -33.883  1.00 35.12           C  
ANISOU 4072  CA  THR B  81     4306   4936   4103   -305      0   1714       C  
ATOM   4073  C   THR B  81     -18.866 -28.920 -34.233  1.00 33.48           C  
ANISOU 4073  C   THR B  81     4163   4790   3768   -182     82   1471       C  
ATOM   4074  O   THR B  81     -19.582 -28.336 -35.056  1.00 31.98           O  
ANISOU 4074  O   THR B  81     3956   4607   3588    -98    187   1305       O  
ATOM   4075  CB  THR B  81     -19.831 -30.472 -32.502  1.00 37.08           C  
ANISOU 4075  CB  THR B  81     4553   5448   4086   -455     36   1899       C  
ATOM   4076  CG2 THR B  81     -21.220 -29.889 -32.483  1.00 37.01           C  
ANISOU 4076  CG2 THR B  81     4504   5652   3904   -452    219   1776       C  
ATOM   4077  OG1 THR B  81     -19.914 -31.839 -32.112  1.00 38.43           O  
ANISOU 4077  OG1 THR B  81     4664   5533   4405   -597    -79   2199       O  
ATOM   4078  N   LEU B  82     -17.834 -28.351 -33.622  1.00 34.30           N  
ANISOU 4078  N   LEU B  82     4330   4924   3778   -179     14   1466       N  
ATOM   4079  CA  LEU B  82     -17.436 -26.941 -33.858  1.00 33.45           C  
ANISOU 4079  CA  LEU B  82     4278   4837   3596    -84     57   1257       C  
ATOM   4080  C   LEU B  82     -17.180 -26.733 -35.349  1.00 31.46           C  
ANISOU 4080  C   LEU B  82     3997   4412   3546     21     80   1143       C  
ATOM   4081  O   LEU B  82     -17.689 -25.782 -35.914  1.00 30.74           O  
ANISOU 4081  O   LEU B  82     3914   4338   3426     94    163   1005       O  
ATOM   4082  CB  LEU B  82     -16.180 -26.626 -33.050  1.00 34.11           C  
ANISOU 4082  CB  LEU B  82     4410   4936   3616   -115    -62   1290       C  
ATOM   4083  CG  LEU B  82     -15.668 -25.207 -33.192  1.00 33.77           C  
ANISOU 4083  CG  LEU B  82     4411   4878   3541    -43    -50   1092       C  
ATOM   4084  CD1 LEU B  82     -16.786 -24.219 -32.915  1.00 34.80           C  
ANISOU 4084  CD1 LEU B  82     4558   5147   3518     -4     66    919       C  
ATOM   4085  CD2 LEU B  82     -14.524 -24.964 -32.231  1.00 34.70           C  
ANISOU 4085  CD2 LEU B  82     4563   5041   3580    -93   -181   1118       C  
ATOM   4086  N   PHE B  83     -16.434 -27.618 -35.974  1.00 31.63           N  
ANISOU 4086  N   PHE B  83     3967   4287   3764     31      1   1199       N  
ATOM   4087  CA  PHE B  83     -16.201 -27.573 -37.439  1.00 31.71           C  
ANISOU 4087  CA  PHE B  83     3919   4203   3925    121     32   1083       C  
ATOM   4088  C   PHE B  83     -17.537 -27.592 -38.182  1.00 30.97           C  
ANISOU 4088  C   PHE B  83     3794   4153   3821    155    134   1012       C  
ATOM   4089  O   PHE B  83     -17.788 -26.698 -38.983  1.00 28.84           O  
ANISOU 4089  O   PHE B  83     3527   3916   3513    222    200    911       O  
ATOM   4090  CB  PHE B  83     -15.315 -28.739 -37.852  1.00 32.97           C  
ANISOU 4090  CB  PHE B  83     3994   4228   4305    129    -71   1115       C  
ATOM   4091  CG  PHE B  83     -14.994 -28.781 -39.315  1.00 33.25           C  
ANISOU 4091  CG  PHE B  83     3942   4236   4456    218    -33    965       C  
ATOM   4092  CD1 PHE B  83     -14.005 -27.967 -39.824  1.00 33.24           C  
ANISOU 4092  CD1 PHE B  83     3927   4269   4435    254    -17    904       C  
ATOM   4093  CD2 PHE B  83     -15.644 -29.657 -40.175  1.00 34.53           C  
ANISOU 4093  CD2 PHE B  83     4019   4363   4740    252    -20    884       C  
ATOM   4094  CE1 PHE B  83     -13.678 -28.020 -41.173  1.00 33.93           C  
ANISOU 4094  CE1 PHE B  83     3912   4402   4580    318     30    780       C  
ATOM   4095  CE2 PHE B  83     -15.288 -29.734 -41.513  1.00 34.48           C  
ANISOU 4095  CE2 PHE B  83     3913   4391   4797    333     12    719       C  
ATOM   4096  CZ  PHE B  83     -14.313 -28.907 -42.015  1.00 33.92           C  
ANISOU 4096  CZ  PHE B  83     3824   4402   4661    363     47    675       C  
ATOM   4097  N   GLU B  84     -18.379 -28.577 -37.891  1.00 33.17           N  
ANISOU 4097  N   GLU B  84     4032   4430   4142     99    130   1086       N  
ATOM   4098  CA  GLU B  84     -19.719 -28.745 -38.517  1.00 34.71           C  
ANISOU 4098  CA  GLU B  84     4172   4668   4346    117    211   1023       C  
ATOM   4099  C   GLU B  84     -20.533 -27.457 -38.368  1.00 23.10           C  
ATOM   4100  O   GLU B  84     -21.295 -27.117 -39.303  1.00 29.97           O  
ANISOU 4100  O   GLU B  84     3574   4229   3584    227    370    844       O  
ATOM   4101  CB  GLU B  84     -20.442 -29.938 -37.896  1.00 39.77           C  
ANISOU 4101  CB  GLU B  84     4760   5291   5061      8    179   1162       C  
ATOM   4102  CG  GLU B  84     -19.929 -31.296 -38.357  1.00 44.37           C  
ANISOU 4102  CG  GLU B  84     5263   5673   5921     -8     53   1198       C  
ATOM   4103  CD  GLU B  84     -19.641 -31.401 -39.856  1.00 49.26           C  
ANISOU 4103  CD  GLU B  84     5813   6224   6678    110     49    984       C  
ATOM   4104  OE1 GLU B  84     -20.381 -30.728 -40.662  1.00 49.82           O  
ANISOU 4104  OE1 GLU B  84     5875   6408   6648    172    146    854       O  
ATOM   4105  OE2 GLU B  84     -18.634 -32.114 -40.225  1.00 55.88           O1-
ANISOU 4105  OE2 GLU B  84     6594   6922   7714    146    -55    938       O1-
ATOM   4106  N   LEU B  85     -20.348 -26.761 -37.251  1.00 31.22           N  
ANISOU 4106  N   LEU B  85     3840   4450   3573    128    327    963       N  
ATOM   4107  CA  LEU B  85     -20.989 -25.456 -36.976  1.00 31.28           C  
ANISOU 4107  CA  LEU B  85     3875   4560   3449    187    403    837       C  
ATOM   4108  C   LEU B  85     -20.402 -24.378 -37.876  1.00 30.03           C  
ANISOU 4108  C   LEU B  85     3748   4301   3359    282    381    748       C  
ATOM   4109  O   LEU B  85     -21.158 -23.538 -38.339  1.00 29.73           O  
ANISOU 4109  O   LEU B  85     3694   4275   3326    358    423    656       O  
ATOM   4110  CB  LEU B  85     -20.787 -25.085 -35.505  1.00 32.63           C  
ANISOU 4110  CB  LEU B  85     4092   4867   3438    127    400    844       C  
ATOM   4111  CG  LEU B  85     -21.769 -25.733 -34.542  1.00 34.23           C  
ANISOU 4111  CG  LEU B  85     4242   5271   3494     29    465    922       C  
ATOM   4112  CD1 LEU B  85     -21.260 -25.688 -33.124  1.00 36.20           C  
ANISOU 4112  CD1 LEU B  85     4530   5690   3533    -61    432    984       C  
ATOM   4113  CD2 LEU B  85     -23.111 -25.041 -34.618  1.00 34.41           C  
ANISOU 4113  CD2 LEU B  85     4198   5425   3452     95    586    760       C  
ATOM   4114  N   ILE B  86     -19.097 -24.376 -38.098  1.00 30.27           N  
ANISOU 4114  N   ILE B  86     3809   4239   3453    271    308    790       N  
ATOM   4115  CA  ILE B  86     -18.473 -23.354 -38.982  1.00 29.94           C  
ANISOU 4115  CA  ILE B  86     3779   4119   3478    328    288    753       C  
ATOM   4116  C   ILE B  86     -18.999 -23.597 -40.398  1.00 29.03           C  
ANISOU 4116  C   ILE B  86     3597   4014   3420    379    324    749       C  
ATOM   4117  O   ILE B  86     -19.439 -22.634 -41.029  1.00 29.11           O  
ANISOU 4117  O   ILE B  86     3605   4019   3438    435    336    727       O  
ATOM   4118  CB  ILE B  86     -16.945 -23.402 -38.900  1.00 30.58           C  
ANISOU 4118  CB  ILE B  86     3873   4135   3613    287    213    805       C  
ATOM   4119  CG1 ILE B  86     -16.473 -22.940 -37.526  1.00 31.88           C  
ANISOU 4119  CG1 ILE B  86     4102   4310   3700    242    159    788       C  
ATOM   4120  CG2 ILE B  86     -16.323 -22.570 -40.000  1.00 31.01           C  
ANISOU 4120  CG2 ILE B  86     3903   4140   3739    315    207    814       C  
ATOM   4121  CD1 ILE B  86     -15.083 -23.371 -37.183  1.00 32.25           C  
ANISOU 4121  CD1 ILE B  86     4144   4314   3795    189     67    856       C  
ATOM   4122  N   LEU B  87     -19.019 -24.848 -40.848  1.00 27.57           N  
ANISOU 4122  N   LEU B  87     3351   3841   3284    362    323    763       N  
ATOM   4123  CA  LEU B  87     -19.501 -25.169 -42.207  1.00 27.55           C  
ANISOU 4123  CA  LEU B  87     3269   3887   3313    410    346    717       C  
ATOM   4124  C   LEU B  87     -20.926 -24.658 -42.377  1.00 28.37           C  
ANISOU 4124  C   LEU B  87     3362   4047   3371    455    391    681       C  
ATOM   4125  O   LEU B  87     -21.205 -23.983 -43.405  1.00 29.08           O  
ANISOU 4125  O   LEU B  87     3425   4180   3444    511    391    676       O  
ATOM   4126  CB  LEU B  87     -19.431 -26.678 -42.412  1.00 27.92           C  
ANISOU 4126  CB  LEU B  87     3241   3909   3460    386    318    687       C  
ATOM   4127  CG  LEU B  87     -18.016 -27.253 -42.569  1.00 28.38           C  
ANISOU 4127  CG  LEU B  87     3262   3911   3609    377    261    681       C  
ATOM   4128  CD1 LEU B  87     -18.057 -28.619 -43.223  1.00 29.31           C  
ANISOU 4128  CD1 LEU B  87     3267   3996   3874    395    220    581       C  
ATOM   4129  CD2 LEU B  87     -17.068 -26.365 -43.358  1.00 27.93           C  
ANISOU 4129  CD2 LEU B  87     3192   3921   3500    404    279    673       C  
ATOM   4130  N   ALA B  88     -21.785 -24.941 -41.390  1.00 28.67           N  
ANISOU 4130  N   ALA B  88     3405   4105   3384    426    422    673       N  
ATOM   4131  CA  ALA B  88     -23.225 -24.612 -41.437  1.00 28.01           C  
ANISOU 4131  CA  ALA B  88     3275   4094   3275    469    472    616       C  
ATOM   4132  C   ALA B  88     -23.422 -23.105 -41.389  1.00 26.82           C  
ANISOU 4132  C   ALA B  88     3160   3925   3105    548    470    574       C  
ATOM   4133  O   ALA B  88     -24.286 -22.614 -42.138  1.00 26.87           O  
ANISOU 4133  O   ALA B  88     3114   3955   3140    622    467    542       O  
ATOM   4134  CB  ALA B  88     -23.934 -25.280 -40.304  1.00 30.20           C  
ANISOU 4134  CB  ALA B  88     3526   4435   3514    395    519    631       C  
ATOM   4135  N   ALA B  89     -22.654 -22.413 -40.552  1.00 26.05           N  
ANISOU 4135  N   ALA B  89     3138   3775   2986    534    449    570       N  
ATOM   4136  CA  ALA B  89     -22.726 -20.943 -40.401  1.00 27.66           C  
ANISOU 4136  CA  ALA B  89     3371   3906   3233    607    415    505       C  
ATOM   4137  C   ALA B  89     -22.455 -20.307 -41.771  1.00 27.75           C  
ANISOU 4137  C   ALA B  89     3372   3841   3332    651    354    594       C  
ATOM   4138  O   ALA B  89     -23.187 -19.398 -42.209  1.00 27.96           O  
ANISOU 4138  O   ALA B  89     3367   3821   3434    733    318    577       O  
ATOM   4139  CB  ALA B  89     -21.734 -20.457 -39.367  1.00 27.82           C  
ANISOU 4139  CB  ALA B  89     3466   3873   3231    567    379    475       C  
ATOM   4140  N   ASN B  90     -21.427 -20.805 -42.431  1.00 26.98           N  
ANISOU 4140  N   ASN B  90     3282   3748   3220    593    338    693       N  
ATOM   4141  CA  ASN B  90     -20.991 -20.277 -43.732  1.00 27.87           C  
ANISOU 4141  CA  ASN B  90     3369   3860   3360    600    294    810       C  
ATOM   4142  C   ASN B  90     -22.041 -20.608 -44.789  1.00 28.76           C  
ANISOU 4142  C   ASN B  90     3404   4088   3434    652    303    814       C  
ATOM   4143  O   ASN B  90     -22.348 -19.711 -45.611  1.00 29.45           O  
ANISOU 4143  O   ASN B  90     3470   4170   3551    691    245    909       O  
ATOM   4144  CB  ASN B  90     -19.642 -20.864 -44.129  1.00 27.56           C  
ANISOU 4144  CB  ASN B  90     3320   3863   3288    526    299    873       C  
ATOM   4145  CG  ASN B  90     -19.067 -20.137 -45.300  1.00 27.67           C  
ANISOU 4145  CG  ASN B  90     3297   3918   3297    505    265   1015       C  
ATOM   4146  ND2 ASN B  90     -18.903 -20.837 -46.413  1.00 27.27           N  
ANISOU 4146  ND2 ASN B  90     3163   4047   3149    495    298   1031       N  
ATOM   4147  OD1 ASN B  90     -18.839 -18.939 -45.173  1.00 29.49           O  
ANISOU 4147  OD1 ASN B  90     3562   4025   3616    495    204   1104       O  
ATOM   4148  N   TYR B  91     -22.548 -21.845 -44.781  1.00 28.69           N  
ANISOU 4148  N   TYR B  91     3349   4172   3380    642    353    730       N  
ATOM   4149  CA  TYR B  91     -23.589 -22.324 -45.727  1.00 29.55           C  
ANISOU 4149  CA  TYR B  91     3369   4401   3457    684    353    694       C  
ATOM   4150  C   TYR B  91     -24.861 -21.478 -45.568  1.00 30.67           C  
ANISOU 4150  C   TYR B  91     3487   4517   3651    765    332    673       C  
ATOM   4151  O   TYR B  91     -25.507 -21.153 -46.555  1.00 32.03           O  
ANISOU 4151  O   TYR B  91     3598   4759   3813    818    281    713       O  
ATOM   4152  CB  TYR B  91     -23.885 -23.808 -45.500  1.00 29.52           C  
ANISOU 4152  CB  TYR B  91     3314   4441   3460    643    392    594       C  
ATOM   4153  CG  TYR B  91     -24.874 -24.410 -46.473  1.00 30.13           C  
ANISOU 4153  CG  TYR B  91     3286   4638   3526    674    376    522       C  
ATOM   4154  CD1 TYR B  91     -24.502 -24.741 -47.766  1.00 30.22           C  
ANISOU 4154  CD1 TYR B  91     3234   4781   3467    684    344    498       C  
ATOM   4155  CD2 TYR B  91     -26.190 -24.648 -46.110  1.00 30.31           C  
ANISOU 4155  CD2 TYR B  91     3249   4673   3593    690    393    462       C  
ATOM   4156  CE1 TYR B  91     -25.390 -25.327 -48.655  1.00 31.12           C  
ANISOU 4156  CE1 TYR B  91     3241   5024   3558    711    313    398       C  
ATOM   4157  CE2 TYR B  91     -27.095 -25.231 -46.988  1.00 30.71           C  
ANISOU 4157  CE2 TYR B  91     3189   4829   3649    710    363    383       C  
ATOM   4158  CZ  TYR B  91     -26.704 -25.547 -48.278  1.00 31.78           C  
ANISOU 4158  CZ  TYR B  91     3274   5085   3714    725    313    346       C  
ATOM   4159  OH  TYR B  91     -27.560 -26.138 -49.168  1.00 33.18           O  
ANISOU 4159  OH  TYR B  91     3335   5389   3884    745    266    236       O  
ATOM   4160  N   LEU B  92     -25.227 -21.128 -44.346  1.00 30.25           N  
ANISOU 4160  N   LEU B  92     3463   4387   3645    781    364    599       N  
ATOM   4161  CA  LEU B  92     -26.467 -20.362 -44.099  1.00 31.10           C  
ANISOU 4161  CA  LEU B  92     3513   4479   3823    877    351    522       C  
ATOM   4162  C   LEU B  92     -26.175 -18.867 -44.123  1.00 32.07           C  
ANISOU 4162  C   LEU B  92     3677   4445   4064    945    260    565       C  
ATOM   4163  O   LEU B  92     -27.151 -18.077 -44.075  1.00 32.94           O  
ANISOU 4163  O   LEU B  92     3724   4505   4288   1053    215    497       O  
ATOM   4164  CB  LEU B  92     -27.042 -20.787 -42.751  1.00 31.28           C  
ANISOU 4164  CB  LEU B  92     3513   4553   3817    856    445    388       C  
ATOM   4165  CG  LEU B  92     -27.370 -22.271 -42.674  1.00 31.06           C  
ANISOU 4165  CG  LEU B  92     3434   4640   3727    765    512    389       C  
ATOM   4166  CD1 LEU B  92     -27.630 -22.670 -41.246  1.00 31.52           C  
ANISOU 4166  CD1 LEU B  92     3482   4771   3721    699    601    334       C  
ATOM   4167  CD2 LEU B  92     -28.528 -22.648 -43.589  1.00 31.05           C  
ANISOU 4167  CD2 LEU B  92     3311   4724   3762    806    497    360       C  
ATOM   4168  N   ASP B  93     -24.903 -18.487 -44.197  1.00 31.39           N  
ANISOU 4168  N   ASP B  93     3672   4268   3985    886    221    670       N  
ATOM   4169  CA  ASP B  93     -24.497 -17.058 -44.168  1.00 32.75           C  
ANISOU 4169  CA  ASP B  93     3880   4244   4318    924    113    730       C  
ATOM   4170  C   ASP B  93     -25.119 -16.410 -42.920  1.00 19.96           C  
ATOM   4171  O   ASP B  93     -26.024 -15.557 -43.058  1.00 34.57           O  
ANISOU 4171  O   ASP B  93     4033   4284   4817   1127     40    451       O  
ATOM   4172  CB  ASP B  93     -24.874 -16.370 -45.483  1.00 33.99           C  
ANISOU 4172  CB  ASP B  93     3987   4377   4551    967      0    914       C  
ATOM   4173  CG  ASP B  93     -24.326 -14.960 -45.601  1.00 36.36           C  
ANISOU 4173  CG  ASP B  93     4315   4440   5058    972   -142   1049       C  
ATOM   4174  OD1 ASP B  93     -23.489 -14.595 -44.734  1.00 36.47           O  
ANISOU 4174  OD1 ASP B  93     4393   4320   5145    930   -144    981       O  
ATOM   4175  OD2 ASP B  93     -24.741 -14.226 -46.550  1.00 38.68           O1-
ANISOU 4175  OD2 ASP B  93     4562   4679   5457   1011   -268   1233       O1-
ATOM   4176  N   ILE B  94     -24.658 -16.856 -41.749  1.00 33.02           N  
ANISOU 4176  N   ILE B  94     3951   4232   4364    954    194    383       N  
ATOM   4177  CA  ILE B  94     -24.937 -16.244 -40.416  1.00 34.24           C  
ANISOU 4177  CA  ILE B  94     4097   4353   4558   1011    206    142       C  
ATOM   4178  C   ILE B  94     -23.641 -15.651 -39.859  1.00 33.58           C  
ANISOU 4178  C   ILE B  94     4102   4130   4526    952    136    136       C  
ATOM   4179  O   ILE B  94     -22.891 -16.375 -39.166  1.00 31.87           O  
ANISOU 4179  O   ILE B  94     3941   4018   4150    854    194    135       O  
ATOM   4180  CB  ILE B  94     -25.559 -17.304 -39.485  1.00 34.28           C  
ANISOU 4180  CB  ILE B  94     4062   4602   4359    973    352     19       C  
ATOM   4181  CG1 ILE B  94     -26.797 -17.940 -40.119  1.00 34.47           C  
ANISOU 4181  CG1 ILE B  94     3982   4752   4362   1009    410     40       C  
ATOM   4182  CG2 ILE B  94     -25.884 -16.707 -38.128  1.00 35.86           C  
ANISOU 4182  CG2 ILE B  94     4229   4862   4534   1027    383   -248       C  
ATOM   4183  CD1 ILE B  94     -27.280 -19.164 -39.391  1.00 34.24           C  
ANISOU 4183  CD1 ILE B  94     3908   4950   4151    922    544      9       C  
ATOM   4184  N   LYS B  95     -23.381 -14.379 -40.152  1.00 35.46           N  
ANISOU 4184  N   LYS B  95     4343   4125   5005   1004     -3    147       N  
ATOM   4185  CA  LYS B  95     -22.064 -13.761 -39.837  1.00 36.60           C  
ANISOU 4185  CA  LYS B  95     4558   4103   5247    928    -96    180       C  
ATOM   4186  C   LYS B  95     -21.725 -13.972 -38.354  1.00 36.98           C  
ANISOU 4186  C   LYS B  95     4637   4255   5160    903    -46    -64       C  
ATOM   4187  O   LYS B  95     -20.615 -14.449 -38.072  1.00 36.66           O  
ANISOU 4187  O   LYS B  95     4659   4258   5013    788    -39     19       O  
ATOM   4188  CB  LYS B  95     -21.995 -12.281 -40.208  1.00 38.74           C  
ANISOU 4188  CB  LYS B  95     4806   4057   5857    987   -277    202       C  
ATOM   4189  CG  LYS B  95     -20.621 -11.691 -39.942  1.00 40.12           C  
ANISOU 4189  CG  LYS B  95     5035   4053   6154    882   -378    255       C  
ATOM   4190  CD  LYS B  95     -20.367 -10.334 -40.589  1.00 43.51           C  
ANISOU 4190  CD  LYS B  95     5438   4139   6954    886   -579    400       C  
ATOM   4191  CE  LYS B  95     -19.586  -9.343 -39.723  1.00 46.16           C  
ANISOU 4191  CE  LYS B  95     5785   4217   7536    864   -721    223       C  
ATOM   4192  NZ  LYS B  95     -18.125  -9.640 -39.672  1.00 45.55           N1+
ANISOU 4192  NZ  LYS B  95     5760   4174   7375    687   -714    373       N1+
ATOM   4193  N   GLY B  96     -22.635 -13.640 -37.438  1.00 37.96           N  
ANISOU 4193  N   GLY B  96     4701   4450   5272   1008    -15   -357       N  
ATOM   4194  CA  GLY B  96     -22.341 -13.638 -35.993  1.00 38.54           C  
ANISOU 4194  CA  GLY B  96     4786   4662   5195    989     15   -616       C  
ATOM   4195  C   GLY B  96     -21.919 -15.007 -35.501  1.00 36.51           C  
ANISOU 4195  C   GLY B  96     4578   4677   4616    856    133   -495       C  
ATOM   4196  O   GLY B  96     -20.999 -15.096 -34.668  1.00 36.90           O  
ANISOU 4196  O   GLY B  96     4681   4783   4558    777    102   -541       O  
ATOM   4197  N   LEU B  97     -22.575 -16.044 -35.996  1.00 34.81           N  
ANISOU 4197  N   LEU B  97     4337   4612   4279    832    243   -344       N  
ATOM   4198  CA  LEU B  97     -22.288 -17.432 -35.599  1.00 34.46           C  
ANISOU 4198  CA  LEU B  97     4321   4782   3990    706    333   -201       C  
ATOM   4199  C   LEU B  97     -20.938 -17.830 -36.178  1.00 33.31           C  
ANISOU 4199  C   LEU B  97     4255   4511   3892    612    264     21       C  
ATOM   4200  O   LEU B  97     -20.144 -18.513 -35.497  1.00 33.41           O  
ANISOU 4200  O   LEU B  97     4310   4615   3770    515    259     83       O  
ATOM   4201  CB  LEU B  97     -23.375 -18.374 -36.119  1.00 33.72           C  
ANISOU 4201  CB  LEU B  97     4158   4820   3832    707    441   -107       C  
ATOM   4202  CG  LEU B  97     -23.077 -19.853 -35.852  1.00 32.76           C  
ANISOU 4202  CG  LEU B  97     4057   4849   3543    570    499     76       C  
ATOM   4203  CD1 LEU B  97     -22.924 -20.093 -34.354  1.00 34.36           C  
ANISOU 4203  CD1 LEU B  97     4265   5270   3519    493    534      4       C  
ATOM   4204  CD2 LEU B  97     -24.136 -20.762 -36.443  1.00 32.14           C  
ANISOU 4204  CD2 LEU B  97     3897   4857   3458    561    580    159       C  
ATOM   4205  N   LEU B  98     -20.735 -17.498 -37.434  1.00 33.01           N  
ANISOU 4205  N   LEU B  98     4216   4301   4025    637    216    153       N  
ATOM   4206  CA  LEU B  98     -19.450 -17.777 -38.090  1.00 32.89           C  
ANISOU 4206  CA  LEU B  98     4241   4200   4057    553    164    342       C  
ATOM   4207  C   LEU B  98     -18.351 -17.053 -37.305  1.00 33.54           C  
ANISOU 4207  C   LEU B  98     4368   4184   4190    509     68    272       C  
ATOM   4208  O   LEU B  98     -17.287 -17.672 -37.084  1.00 33.05           O  
ANISOU 4208  O   LEU B  98     4331   4158   4069    421     49    363       O  
ATOM   4209  CB  LEU B  98     -19.553 -17.298 -39.538  1.00 33.54           C  
ANISOU 4209  CB  LEU B  98     4292   4168   4284    586    131    483       C  
ATOM   4210  CG  LEU B  98     -18.338 -17.581 -40.403  1.00 32.79           C  
ANISOU 4210  CG  LEU B  98     4197   4050   4211    501    107    674       C  
ATOM   4211  CD1 LEU B  98     -18.173 -19.064 -40.599  1.00 31.59           C  
ANISOU 4211  CD1 LEU B  98     4025   4053   3924    459    184    724       C  
ATOM   4212  CD2 LEU B  98     -18.475 -16.879 -41.738  1.00 34.11           C  
ANISOU 4212  CD2 LEU B  98     4324   4149   4487    518     64    828       C  
ATOM   4213  N   ASP B  99     -18.617 -15.820 -36.860  1.00 34.50           N  
ANISOU 4213  N   ASP B  99     4484   4184   4439    576     -4     91       N  
ATOM   4214  CA  ASP B  99     -17.614 -14.986 -36.159  1.00 35.91           C  
ANISOU 4214  CA  ASP B  99     4693   4238   4715    537   -123    -16       C  
ATOM   4215  C   ASP B  99     -17.238 -15.613 -34.819  1.00 20.85           C  
ATOM   4216  O   ASP B  99     -16.028 -15.640 -34.531  1.00 37.68           O  
ANISOU 4216  O   ASP B  99     4972   4632   4711    396   -184    -81       O  
ATOM   4217  CB  ASP B  99     -18.118 -13.577 -35.923  1.00 38.66           C  
ANISOU 4217  CB  ASP B  99     5009   4392   5287    638   -221   -238       C  
ATOM   4218  CG  ASP B  99     -18.107 -12.697 -37.147  1.00 39.77           C  
ANISOU 4218  CG  ASP B  99     5125   4258   5727    659   -316    -68       C  
ATOM   4219  OD1 ASP B  99     -17.318 -12.993 -38.080  1.00 39.03           O  
ANISOU 4219  OD1 ASP B  99     5042   4133   5653    561   -319    215       O  
ATOM   4220  OD2 ASP B  99     -18.866 -11.702 -37.123  1.00 42.37           O1-
ANISOU 4220  OD2 ASP B  99     5410   4417   6270    772   -394   -225       O1-
ATOM   4221  N   VAL B 100     -18.203 -16.082 -34.020  1.00 37.41           N  
ANISOU 4221  N   VAL B 100     4889   4870   4454    517     -8   -268       N  
ATOM   4222  CA  VAL B 100     -17.912 -16.650 -32.661  1.00 38.57           C  
ANISOU 4222  CA  VAL B 100     5054   5276   4326    447      3   -350       C  
ATOM   4223  C   VAL B 100     -17.156 -17.961 -32.852  1.00 36.68           C  
ANISOU 4223  C   VAL B 100     4848   5099   3990    334     13    -63       C  
ATOM   4224  O   VAL B 100     -16.134 -18.160 -32.185  1.00 37.42           O  
ANISOU 4224  O   VAL B 100     4972   5237   4010    257    -73    -33       O  
ATOM   4225  CB  VAL B 100     -19.151 -16.882 -31.758  1.00 40.27           C  
ANISOU 4225  CB  VAL B 100     5212   5789   4300    485    121   -528       C  
ATOM   4226  CG1 VAL B 100     -19.812 -15.599 -31.302  1.00 43.06           C  
ANISOU 4226  CG1 VAL B 100     5503   6120   4736    613     99   -897       C  
ATOM   4227  CG2 VAL B 100     -20.196 -17.792 -32.387  1.00 39.07           C  
ANISOU 4227  CG2 VAL B 100     5018   5726   4101    490    255   -367       C  
ATOM   4228  N   THR B 101     -17.647 -18.817 -33.743  1.00 35.03           N  
ANISOU 4228  N   THR B 101     4620   4884   3806    334     96    119       N  
ATOM   4229  CA  THR B 101     -17.065 -20.152 -33.982  1.00 34.77           C  
ANISOU 4229  CA  THR B 101     4594   4885   3734    249     97    355       C  
ATOM   4230  C   THR B 101     -15.601 -19.968 -34.388  1.00 34.86           C  
ANISOU 4230  C   THR B 101     4622   4736   3889    211    -10    437       C  
ATOM   4231  O   THR B 101     -14.738 -20.756 -33.919  1.00 35.37           O  
ANISOU 4231  O   THR B 101     4691   4846   3901    138    -72    547       O  
ATOM   4232  CB  THR B 101     -17.898 -20.911 -35.009  1.00 33.36           C  
ANISOU 4232  CB  THR B 101     4373   4693   3610    276    188    466       C  
ATOM   4233  CG2 THR B 101     -19.204 -21.408 -34.445  1.00 33.33           C  
ANISOU 4233  CG2 THR B 101     4330   4882   3453    272    288    432       C  
ATOM   4234  OG1 THR B 101     -18.146 -20.004 -36.075  1.00 33.92           O  
ANISOU 4234  OG1 THR B 101     4429   4614   3844    358    191    420       O  
ATOM   4235  N   CYS B 102     -15.317 -18.938 -35.183  1.00 34.12           N  
ANISOU 4235  N   CYS B 102     4521   4464   3980    250    -42    401       N  
ATOM   4236  CA  CYS B 102     -13.954 -18.691 -35.709  1.00 33.91           C  
ANISOU 4236  CA  CYS B 102     4478   4303   4101    197   -125    497       C  
ATOM   4237  C   CYS B 102     -13.065 -18.224 -34.571  1.00 35.26           C  
ANISOU 4237  C   CYS B 102     4674   4476   4246    145   -243    396       C  
ATOM   4238  O   CYS B 102     -11.991 -18.851 -34.387  1.00 36.10           O  
ANISOU 4238  O   CYS B 102     4763   4606   4349     79   -304    496       O  
ATOM   4239  CB  CYS B 102     -13.977 -17.720 -36.875  1.00 33.76           C  
ANISOU 4239  CB  CYS B 102     4432   4119   4275    224   -130    540       C  
ATOM   4240  SG  CYS B 102     -14.480 -18.565 -38.395  1.00 32.60           S  
ANISOU 4240  SG  CYS B 102     4232   4030   4123    252    -19    705       S  
ATOM   4241  N   LYS B 103     -13.513 -17.209 -33.830  1.00 36.62           N  
ANISOU 4241  N   LYS B 103     4870   4636   4409    182   -283    180       N  
ATOM   4242  CA  LYS B 103     -12.783 -16.680 -32.652  1.00 38.84           C  
ANISOU 4242  CA  LYS B 103     5166   4951   4642    140   -408     16       C  
ATOM   4243  C   LYS B 103     -12.543 -17.823 -31.654  1.00 38.46           C  
ANISOU 4243  C   LYS B 103     5135   5154   4325     79   -414     83       C  
ATOM   4244  O   LYS B 103     -11.503 -17.800 -30.981  1.00 38.39           O  
ANISOU 4244  O   LYS B 103     5126   5174   4287     14   -539     71       O  
ATOM   4245  CB  LYS B 103     -13.547 -15.494 -32.065  1.00 41.96           C  
ANISOU 4245  CB  LYS B 103     5560   5315   5066    218   -435   -287       C  
ATOM   4246  CG  LYS B 103     -13.023 -14.925 -30.748  1.00 46.16           C  
ANISOU 4246  CG  LYS B 103     6096   5937   5505    193   -560   -545       C  
ATOM   4247  CD  LYS B 103     -11.623 -14.289 -30.775  1.00 48.12           C  
ANISOU 4247  CD  LYS B 103     6330   5985   5968    115   -729   -542       C  
ATOM   4248  CE  LYS B 103     -11.330 -13.403 -29.568  1.00 51.78           C  
ANISOU 4248  CE  LYS B 103     6781   6490   6402    118   -874   -891       C  
ATOM   4249  NZ  LYS B 103     -11.221 -11.950 -29.885  1.00 53.58           N1+
ANISOU 4249  NZ  LYS B 103     6973   6380   7006    154   -998  -1087       N1+
ATOM   4250  N   THR B 104     -13.442 -18.809 -31.574  1.00 37.99           N  
ANISOU 4250  N   THR B 104     5079   5261   4093     88   -303    179       N  
ATOM   4251  CA  THR B 104     -13.309 -19.964 -30.641  1.00 39.22           C  
ANISOU 4251  CA  THR B 104     5243   5646   4011     10   -324    312       C  
ATOM   4252  C   THR B 104     -12.111 -20.822 -31.051  1.00 37.97           C  
ANISOU 4252  C   THR B 104     5066   5380   3981    -45   -412    537       C  
ATOM   4253  O   THR B 104     -11.369 -21.231 -30.167  1.00 41.18           O  
ANISOU 4253  O   THR B 104     5475   5893   4279   -112   -530    602       O  
ATOM   4254  CB  THR B 104     -14.591 -20.804 -30.522  1.00 39.60           C  
ANISOU 4254  CB  THR B 104     5280   5871   3894      9   -190    393       C  
ATOM   4255  CG2 THR B 104     -14.504 -21.876 -29.452  1.00 40.90           C  
ANISOU 4255  CG2 THR B 104     5446   6280   3814    -97   -231    566       C  
ATOM   4256  OG1 THR B 104     -15.682 -19.926 -30.231  1.00 40.64           O  
ANISOU 4256  OG1 THR B 104     5399   6103   3940     79   -101    147       O  
ATOM   4257  N   VAL B 105     -11.925 -21.092 -32.336  1.00 35.44           N  
ANISOU 4257  N   VAL B 105     4711   4882   3875    -12   -365    640       N  
ATOM   4258  CA  VAL B 105     -10.752 -21.873 -32.823  1.00 34.11           C  
ANISOU 4258  CA  VAL B 105     4486   4618   3857    -42   -440    798       C  
ATOM   4259  C   VAL B 105      -9.488 -21.027 -32.638  1.00 34.62           C  
ANISOU 4259  C   VAL B 105     4526   4602   4024    -76   -561    730       C  
ATOM   4260  O   VAL B 105      -8.478 -21.559 -32.168  1.00 35.57           O  
ANISOU 4260  O   VAL B 105     4610   4743   4163   -121   -683    811       O  
ATOM   4261  CB  VAL B 105     -10.901 -22.275 -34.292  1.00 32.89           C  
ANISOU 4261  CB  VAL B 105     4274   4349   3873      7   -344    865       C  
ATOM   4262  CG1 VAL B 105      -9.644 -22.988 -34.771  1.00 32.41           C  
ANISOU 4262  CG1 VAL B 105     4122   4219   3974     -6   -416    960       C  
ATOM   4263  CG2 VAL B 105     -12.117 -23.145 -34.528  1.00 32.75           C  
ANISOU 4263  CG2 VAL B 105     4263   4390   3791     35   -245    918       C  
ATOM   4264  N   ALA B 106      -9.535 -19.750 -32.994  1.00 34.33           N  
ANISOU 4264  N   ALA B 106     4498   4462   4086    -61   -548    598       N  
ATOM   4265  CA  ALA B 106      -8.417 -18.808 -32.764  1.00 35.82           C  
ANISOU 4265  CA  ALA B 106     4655   4551   4403   -112   -675    520       C  
ATOM   4266  C   ALA B 106      -7.948 -18.937 -31.305  1.00 37.84           C  
ANISOU 4266  C   ALA B 106     4936   4953   4487   -160   -816    444       C  
ATOM   4267  O   ALA B 106      -6.724 -18.979 -31.043  1.00 38.55           O  
ANISOU 4267  O   ALA B 106     4971   5019   4658   -217   -949    479       O  
ATOM   4268  CB  ALA B 106      -8.832 -17.396 -33.099  1.00 35.99           C  
ANISOU 4268  CB  ALA B 106     4692   4425   4556    -91   -666    377       C  
ATOM   4269  N   ASN B 107      -8.900 -19.006 -30.374  1.00 38.55           N  
ANISOU 4269  N   ASN B 107     5092   5227   4329   -141   -788    344       N  
ATOM   4270  CA  ASN B 107      -8.598 -19.047 -28.922  1.00 40.71           C  
ANISOU 4270  CA  ASN B 107     5387   5720   4362   -193   -916    257       C  
ATOM   4271  C   ASN B 107      -7.931 -20.388 -28.608  1.00 40.74           C  
ANISOU 4271  C   ASN B 107     5365   5817   4297   -249   -999    518       C  
ATOM   4272  O   ASN B 107      -7.046 -20.411 -27.767  1.00 42.29           O  
ANISOU 4272  O   ASN B 107     5543   6106   4418   -306  -1166    517       O  
ATOM   4273  CB  ASN B 107      -9.838 -18.703 -28.101  1.00 41.58           C  
ANISOU 4273  CB  ASN B 107     5542   6052   4204   -161   -838     64       C  
ATOM   4274  CG  ASN B 107     -10.137 -17.214 -28.138  1.00 41.77           C  
ANISOU 4274  CG  ASN B 107     5565   5952   4355   -100   -845   -261       C  
ATOM   4275  ND2 ASN B 107     -11.360 -16.815 -27.825  1.00 42.51           N  
ANISOU 4275  ND2 ASN B 107     5668   6170   4315    -31   -741   -461       N  
ATOM   4276  OD1 ASN B 107      -9.258 -16.416 -28.417  1.00 41.10           O  
ANISOU 4276  OD1 ASN B 107     5454   5654   4510   -118   -957   -337       O  
ATOM   4277  N   MET B 108      -8.278 -21.444 -29.327  1.00 39.49           N  
ANISOU 4277  N   MET B 108     5191   5605   4208   -227   -911    726       N  
ATOM   4278  CA  MET B 108      -7.610 -22.761 -29.169  1.00 41.28           C  
ANISOU 4278  CA  MET B 108     5371   5841   4471   -263  -1016    976       C  
ATOM   4279  C   MET B 108      -6.189 -22.738 -29.740  1.00 40.60           C  
ANISOU 4279  C   MET B 108     5190   5581   4656   -259  -1122   1003       C  
ATOM   4280  O   MET B 108      -5.436 -23.661 -29.434  1.00 40.50           O  
ANISOU 4280  O   MET B 108     5118   5568   4700   -279  -1259   1165       O  
ATOM   4281  CB  MET B 108      -8.409 -23.867 -29.848  1.00 41.49           C  
ANISOU 4281  CB  MET B 108     5389   5817   4559   -233   -904   1142       C  
ATOM   4282  CG  MET B 108      -9.731 -24.035 -29.199  1.00 44.29           C  
ANISOU 4282  CG  MET B 108     5806   6371   4650   -261   -811   1157       C  
ATOM   4283  SD  MET B 108     -10.742 -25.168 -30.117  1.00 47.39           S  
ANISOU 4283  SD  MET B 108     6174   6668   5165   -232   -680   1313       S  
ATOM   4284  CE  MET B 108     -10.154 -26.737 -29.472  1.00 49.71           C  
ANISOU 4284  CE  MET B 108     6422   6958   5509   -311   -867   1639       C  
ATOM   4285  N   ILE B 109      -5.824 -21.729 -30.529  1.00 39.99           N  
ANISOU 4285  N   ILE B 109     5079   5362   4752   -242  -1072    865       N  
ATOM   4286  CA  ILE B 109      -4.452 -21.608 -31.108  1.00 40.10           C  
ANISOU 4286  CA  ILE B 109     4970   5248   5017   -258  -1152    888       C  
ATOM   4287  C   ILE B 109      -3.582 -20.655 -30.279  1.00 40.94           C  
ANISOU 4287  C   ILE B 109     5063   5374   5120   -326  -1314    761       C  
ATOM   4288  O   ILE B 109      -2.394 -20.978 -30.141  1.00 41.88           O  
ANISOU 4288  O   ILE B 109     5077   5476   5360   -355  -1453    823       O  
ATOM   4289  CB  ILE B 109      -4.511 -21.167 -32.579  1.00 39.68           C  
ANISOU 4289  CB  ILE B 109     4859   5059   5160   -228   -997    871       C  
ATOM   4290  CG1 ILE B 109      -5.216 -22.216 -33.445  1.00 38.12           C  
ANISOU 4290  CG1 ILE B 109     4646   4858   4980   -158   -863    968       C  
ATOM   4291  CG2 ILE B 109      -3.110 -20.867 -33.088  1.00 41.12           C  
ANISOU 4291  CG2 ILE B 109     4892   5166   5566   -271  -1063    884       C  
ATOM   4292  CD1 ILE B 109      -5.719 -21.697 -34.772  1.00 36.25           C  
ANISOU 4292  CD1 ILE B 109     4390   4563   4822   -128   -696    940       C  
ATOM   4293  N   LYS B 110      -4.113 -19.526 -29.792  1.00 40.96           N  
ANISOU 4293  N   LYS B 110     5143   5396   5022   -341  -1311    565       N  
ATOM   4294  CA  LYS B 110      -3.299 -18.451 -29.159  1.00 42.92           C  
ANISOU 4294  CA  LYS B 110     5362   5616   5330   -405  -1472    387       C  
ATOM   4295  C   LYS B 110      -2.487 -19.010 -27.976  1.00 44.44           C  
ANISOU 4295  C   LYS B 110     5529   5985   5373   -453  -1679    422       C  
ATOM   4296  O   LYS B 110      -2.948 -19.916 -27.275  1.00 44.42           O  
ANISOU 4296  O   LYS B 110     5580   6175   5121   -444  -1698    533       O  
ATOM   4297  CB  LYS B 110      -4.150 -17.233 -28.768  1.00 44.54           C  
ANISOU 4297  CB  LYS B 110     5648   5806   5469   -389  -1448    123       C  
ATOM   4298  CG  LYS B 110      -5.273 -17.490 -27.781  1.00 46.39           C  
ANISOU 4298  CG  LYS B 110     5981   6291   5354   -350  -1407     20       C  
ATOM   4299  CD  LYS B 110      -5.948 -16.259 -27.184  1.00 48.94           C  
ANISOU 4299  CD  LYS B 110     6345   6638   5614   -319  -1421   -326       C  
ATOM   4300  CE  LYS B 110      -6.965 -16.661 -26.121  1.00 50.53           C  
ANISOU 4300  CE  LYS B 110     6605   7185   5408   -293  -1367   -424       C  
ATOM   4301  NZ  LYS B 110      -7.831 -15.545 -25.656  1.00 52.36           N1+
ANISOU 4301  NZ  LYS B 110     6852   7462   5580   -227  -1339   -804       N1+
ATOM   4302  N   GLY B 111      -1.276 -18.498 -27.815  1.00 46.08           N  
ANISOU 4302  N   GLY B 111     5639   6123   5747   -515  -1840    361       N  
ATOM   4303  CA  GLY B 111      -0.409 -18.714 -26.643  1.00 48.67           C  
ANISOU 4303  CA  GLY B 111     5928   6613   5950   -569  -2080    344       C  
ATOM   4304  C   GLY B 111       0.111 -20.131 -26.554  1.00 48.61           C  
ANISOU 4304  C   GLY B 111     5860   6678   5933   -553  -2158    618       C  
ATOM   4305  O   GLY B 111       0.303 -20.597 -25.452  1.00 50.38           O  
ANISOU 4305  O   GLY B 111     6103   7106   5933   -583  -2329    676       O  
ATOM   4306  N   LYS B 112       0.335 -20.807 -27.669  1.00 47.73           N  
ANISOU 4306  N   LYS B 112     5665   6412   6059   -505  -2050    778       N  
ATOM   4307  CA  LYS B 112       0.861 -22.190 -27.661  1.00 48.70           C  
ANISOU 4307  CA  LYS B 112     5702   6546   6258   -467  -2145   1009       C  
ATOM   4308  C   LYS B 112       2.059 -22.292 -28.598  1.00 48.87           C  
ANISOU 4308  C   LYS B 112     5522   6412   6634   -450  -2159   1026       C  
ATOM   4309  O   LYS B 112       2.054 -21.619 -29.624  1.00 47.76           O  
ANISOU 4309  O   LYS B 112     5335   6163   6648   -455  -1994    941       O  
ATOM   4310  CB  LYS B 112      -0.203 -23.181 -28.114  1.00 47.21           C  
ANISOU 4310  CB  LYS B 112     5583   6342   6013   -399  -1992   1158       C  
ATOM   4311  CG  LYS B 112      -1.398 -23.309 -27.197  1.00 48.30           C  
ANISOU 4311  CG  LYS B 112     5884   6671   5798   -425  -1966   1191       C  
ATOM   4312  CD  LYS B 112      -2.280 -24.471 -27.585  1.00 48.29           C  
ANISOU 4312  CD  LYS B 112     5915   6638   5795   -380  -1861   1385       C  
ATOM   4313  CE  LYS B 112      -3.708 -24.310 -27.090  1.00 49.02           C  
ANISOU 4313  CE  LYS B 112     6150   6904   5570   -406  -1730   1365       C  
ATOM   4314  NZ  LYS B 112      -4.583 -25.427 -27.531  1.00 47.88           N1+
ANISOU 4314  NZ  LYS B 112     6021   6707   5465   -378  -1630   1556       N1+
ATOM   4315  N   THR B 113       3.020 -23.134 -28.236  1.00 50.65           N  
ANISOU 4315  N   THR B 113     5619   6651   6977   -432  -2355   1147       N  
ATOM   4316  CA  THR B 113       4.138 -23.564 -29.103  1.00 51.90           C  
ANISOU 4316  CA  THR B 113     5544   6697   7481   -387  -2369   1169       C  
ATOM   4317  C   THR B 113       3.582 -24.369 -30.280  1.00 51.50           C  
ANISOU 4317  C   THR B 113     5458   6553   7555   -286  -2162   1216       C  
ATOM   4318  O   THR B 113       2.554 -25.048 -30.162  1.00 51.93           O  
ANISOU 4318  O   THR B 113     5645   6609   7479   -243  -2107   1308       O  
ATOM   4319  CB  THR B 113       5.125 -24.439 -28.331  1.00 54.28           C  
ANISOU 4319  CB  THR B 113     5718   7026   7881   -362  -2654   1295       C  
ATOM   4320  CG2 THR B 113       5.443 -23.892 -26.957  1.00 56.73           C  
ANISOU 4320  CG2 THR B 113     6096   7488   7972   -456  -2892   1277       C  
ATOM   4321  OG1 THR B 113       4.537 -25.739 -28.237  1.00 54.30           O  
ANISOU 4321  OG1 THR B 113     5767   6993   7873   -281  -2682   1481       O  
ATOM   4322  N   PRO B 114       4.261 -24.353 -31.446  1.00 51.20           N  
ANISOU 4322  N   PRO B 114     5223   6459   7773   -252  -2046   1147       N  
ATOM   4323  CA  PRO B 114       3.802 -25.123 -32.601  1.00 50.37           C  
ANISOU 4323  CA  PRO B 114     5058   6305   7775   -151  -1860   1140       C  
ATOM   4324  C   PRO B 114       3.473 -26.569 -32.200  1.00 51.40           C  
ANISOU 4324  C   PRO B 114     5205   6366   7959    -50  -1985   1262       C  
ATOM   4325  O   PRO B 114       2.423 -27.047 -32.523  1.00 49.63           O  
ANISOU 4325  O   PRO B 114     5089   6108   7660     -8  -1868   1293       O  
ATOM   4326  CB  PRO B 114       4.990 -25.058 -33.574  1.00 51.17           C  
ANISOU 4326  CB  PRO B 114     4874   6426   8141   -133  -1803   1046       C  
ATOM   4327  CG  PRO B 114       5.732 -23.795 -33.185  1.00 51.86           C  
ANISOU 4327  CG  PRO B 114     4927   6554   8222   -271  -1869   1010       C  
ATOM   4328  CD  PRO B 114       5.503 -23.616 -31.699  1.00 52.26           C  
ANISOU 4328  CD  PRO B 114     5161   6606   8090   -320  -2091   1063       C  
ATOM   4329  N   GLU B 115       4.375 -27.213 -31.466  1.00 55.10           N  
ANISOU 4329  N   GLU B 115     5559   6803   8573    -24  -2242   1347       N  
ATOM   4330  CA  GLU B 115       4.198 -28.608 -30.985  1.00 57.88           C  
ANISOU 4330  CA  GLU B 115     5904   7048   9039     58  -2426   1516       C  
ATOM   4331  C   GLU B 115       2.883 -28.699 -30.199  1.00 27.69           C  
ATOM   4332  O   GLU B 115       2.122 -29.631 -30.477  1.00 54.60           O  
ANISOU 4332  O   GLU B 115     5789   6580   8377     47  -2382   1762       O  
ATOM   4333  CB  GLU B 115       5.396 -29.047 -30.140  1.00 63.89           C  
ANISOU 4333  CB  GLU B 115     6516   7786   9972     73  -2746   1617       C  
ATOM   4334  CG  GLU B 115       6.751 -28.758 -30.779  1.00 68.23           C  
ANISOU 4334  CG  GLU B 115     6783   8338  10801    115  -2753   1442       C  
ATOM   4335  CD  GLU B 115       7.433 -27.444 -30.374  1.00 71.23           C  
ANISOU 4335  CD  GLU B 115     7153   8855  11055    -15  -2778   1364       C  
ATOM   4336  OE1 GLU B 115       7.259 -26.431 -31.119  1.00 69.74           O  
ANISOU 4336  OE1 GLU B 115     6982   8726  10791    -82  -2538   1224       O  
ATOM   4337  OE2 GLU B 115       8.158 -27.431 -29.322  1.00 74.76           O1-
ANISOU 4337  OE2 GLU B 115     7565   9343  11499    -56  -3057   1452       O1-
ATOM   4338  N   GLU B 116       2.610 -27.760 -29.282  1.00 54.40           N  
ANISOU 4338  N   GLU B 116     5890   6818   7960   -125  -2444   1690       N  
ATOM   4339  CA  GLU B 116       1.388 -27.774 -28.430  1.00 54.05           C  
ANISOU 4339  CA  GLU B 116     6071   6896   7570   -198  -2427   1819       C  
ATOM   4340  C   GLU B 116       0.160 -27.719 -29.341  1.00 25.60           C  
ATOM   4341  O   GLU B 116      -0.782 -28.506 -29.139  1.00 50.52           O  
ANISOU 4341  O   GLU B 116     5802   6393   7001   -169  -2130   1895       O  
ATOM   4342  CB  GLU B 116       1.394 -26.614 -27.434  1.00 54.91           C  
ANISOU 4342  CB  GLU B 116     6295   7214   7354   -307  -2479   1738       C  
ATOM   4343  CG  GLU B 116       2.245 -26.891 -26.225  1.00 58.69           C  
ANISOU 4343  CG  GLU B 116     6728   7807   7763   -358  -2792   1880       C  
ATOM   4344  CD  GLU B 116       2.476 -25.719 -25.292  1.00 60.78           C  
ANISOU 4344  CD  GLU B 116     7063   8287   7744   -457  -2875   1730       C  
ATOM   4345  OE1 GLU B 116       2.150 -24.577 -25.672  1.00 59.22           O  
ANISOU 4345  OE1 GLU B 116     6921   8092   7486   -478  -2698   1485       O  
ATOM   4346  OE2 GLU B 116       2.960 -25.973 -24.146  1.00 64.58           O1-
ANISOU 4346  OE2 GLU B 116     7535   8936   8066   -514  -3139   1863       O1-
ATOM   4347  N   ILE B 117       0.205 -26.844 -30.342  1.00 49.79           N  
ANISOU 4347  N   ILE B 117     5593   6285   7040   -148  -1944   1534       N  
ATOM   4348  CA  ILE B 117      -0.892 -26.677 -31.338  1.00 47.76           C  
ANISOU 4348  CA  ILE B 117     5406   5997   6743   -114  -1682   1449       C  
ATOM   4349  C   ILE B 117      -1.106 -27.999 -32.094  1.00 48.28           C  
ANISOU 4349  C   ILE B 117     5377   5928   7038    -15  -1660   1504       C  
ATOM   4350  O   ILE B 117      -2.272 -28.407 -32.279  1.00 47.91           O  
ANISOU 4350  O   ILE B 117     5428   5868   6908     -6  -1554   1548       O  
ATOM   4351  CB  ILE B 117      -0.562 -25.533 -32.311  1.00 46.17           C  
ANISOU 4351  CB  ILE B 117     5146   5794   6600   -123  -1517   1268       C  
ATOM   4352  CG1 ILE B 117      -0.400 -24.196 -31.590  1.00 46.72           C  
ANISOU 4352  CG1 ILE B 117     5302   5939   6510   -220  -1561   1188       C  
ATOM   4353  CG2 ILE B 117      -1.619 -25.455 -33.397  1.00 43.90           C  
ANISOU 4353  CG2 ILE B 117     4910   5489   6282    -82  -1279   1209       C  
ATOM   4354  CD1 ILE B 117       0.060 -23.076 -32.484  1.00 46.82           C  
ANISOU 4354  CD1 ILE B 117     5236   5913   6642   -257  -1447   1067       C  
ATOM   4355  N   ARG B 118      -0.023 -28.627 -32.566  1.00 49.09           N  
ANISOU 4355  N   ARG B 118     5274   5934   7446     63  -1755   1468       N  
ATOM   4356  CA  ARG B 118      -0.089 -29.892 -33.346  1.00 48.80           C  
ANISOU 4356  CA  ARG B 118     5104   5746   7693    180  -1757   1447       C  
ATOM   4357  C   ARG B 118      -0.856 -30.927 -32.529  1.00 49.37           C  
ANISOU 4357  C   ARG B 118     5277   5723   7757    162  -1905   1677       C  
ATOM   4358  O   ARG B 118      -1.706 -31.606 -33.131  1.00 48.10           O  
ANISOU 4358  O   ARG B 118     5126   5468   7681    208  -1816   1659       O  
ATOM   4359  CB  ARG B 118       1.300 -30.427 -33.702  1.00 50.11           C  
ANISOU 4359  CB  ARG B 118     5007   5833   8201    275  -1889   1360       C  
ATOM   4360  CG  ARG B 118       1.985 -29.671 -34.824  1.00 49.21           C  
ANISOU 4360  CG  ARG B 118     4731   5828   8138    298  -1702   1132       C  
ATOM   4361  CD  ARG B 118       3.062 -30.460 -35.553  1.00 50.93           C  
ANISOU 4361  CD  ARG B 118     4642   5993   8715    431  -1755    972       C  
ATOM   4362  NE  ARG B 118       4.428 -30.282 -35.075  1.00 52.75           N  
ANISOU 4362  NE  ARG B 118     4699   6244   9100    426  -1927    975       N  
ATOM   4363  CZ  ARG B 118       5.130 -29.165 -35.170  1.00 52.68           C  
ANISOU 4363  CZ  ARG B 118     4631   6385   9000    333  -1855    924       C  
ATOM   4364  NH1 ARG B 118       4.631 -28.128 -35.806  1.00 51.48           N1+
ANISOU 4364  NH1 ARG B 118     4572   6364   8627    243  -1614    874       N1+
ATOM   4365  NH2 ARG B 118       6.353 -29.098 -34.685  1.00 54.71           N  
ANISOU 4365  NH2 ARG B 118     4715   6650   9421    328  -2035    928       N  
ATOM   4366  N   LYS B 119      -0.577 -31.015 -31.219  1.00 51.00           N  
ANISOU 4366  N   LYS B 119     5548   5976   7855     84  -2125   1893       N  
ATOM   4367  CA  LYS B 119      -1.169 -32.057 -30.340  1.00 53.44           C  
ANISOU 4367  CA  LYS B 119     5927   6217   8160     36  -2303   2190       C  
ATOM   4368  C   LYS B 119      -2.665 -31.758 -30.182  1.00 51.26           C  
ANISOU 4368  C   LYS B 119     5845   6067   7563    -52  -2113   2241       C  
ATOM   4369  O   LYS B 119      -3.462 -32.722 -30.148  1.00 53.30           O  
ANISOU 4369  O   LYS B 119     6123   6218   7909    -68  -2143   2407       O  
ATOM   4370  CB  LYS B 119      -0.440 -32.168 -29.002  1.00 57.04           C  
ANISOU 4370  CB  LYS B 119     6388   6753   8533    -39  -2592   2427       C  
ATOM   4371  CG  LYS B 119       0.912 -32.867 -29.075  1.00 60.62           C  
ANISOU 4371  CG  LYS B 119     6619   7023   9389     63  -2843   2447       C  
ATOM   4372  CD  LYS B 119       1.597 -33.025 -27.706  1.00 64.88           C  
ANISOU 4372  CD  LYS B 119     7162   7653   9836    -16  -3165   2721       C  
ATOM   4373  CE  LYS B 119       3.111 -32.817 -27.692  1.00 66.86           C  
ANISOU 4373  CE  LYS B 119     7217   7874  10310     54  -3342   2612       C  
ATOM   4374  NZ  LYS B 119       3.527 -31.490 -27.145  1.00 66.37           N1+
ANISOU 4374  NZ  LYS B 119     7225   8077   9916    -42  -3309   2494       N1+
ATOM   4375  N   THR B 120      -3.037 -30.480 -30.130  1.00 47.60           N  
ANISOU 4375  N   THR B 120     5499   5802   6783   -104  -1932   2092       N  
ATOM   4376  CA  THR B 120      -4.446 -30.026 -30.016  1.00 45.68           C  
ANISOU 4376  CA  THR B 120     5417   5700   6239   -168  -1736   2082       C  
ATOM   4377  C   THR B 120      -5.286 -30.549 -31.194  1.00 43.90           C  
ANISOU 4377  C   THR B 120     5163   5332   6185    -97  -1565   1999       C  
ATOM   4378  O   THR B 120      -6.412 -31.038 -30.955  1.00 44.70           O  
ANISOU 4378  O   THR B 120     5337   5457   6191   -150  -1518   2128       O  
ATOM   4379  CB  THR B 120      -4.521 -28.502 -29.947  1.00 44.24           C  
ANISOU 4379  CB  THR B 120     5322   5688   5799   -197  -1595   1872       C  
ATOM   4380  CG2 THR B 120      -5.920 -27.988 -29.671  1.00 42.86           C  
ANISOU 4380  CG2 THR B 120     5290   5673   5320   -249  -1422   1839       C  
ATOM   4381  OG1 THR B 120      -3.587 -28.092 -28.942  1.00 46.70           O  
ANISOU 4381  OG1 THR B 120     5628   6111   6005   -253  -1783   1907       O  
ATOM   4382  N   PHE B 121      -4.782 -30.457 -32.420  1.00 42.18           N  
ANISOU 4382  N   PHE B 121     4828   5004   6195      9  -1475   1788       N  
ATOM   4383  CA  PHE B 121      -5.594 -30.687 -33.644  1.00 41.09           C  
ANISOU 4383  CA  PHE B 121     4665   4800   6148     76  -1287   1644       C  
ATOM   4384  C   PHE B 121      -5.157 -31.968 -34.386  1.00 41.01           C  
ANISOU 4384  C   PHE B 121     4477   4577   6530    183  -1382   1598       C  
ATOM   4385  O   PHE B 121      -5.815 -32.329 -35.406  1.00 38.75           O  
ANISOU 4385  O   PHE B 121     4147   4239   6338    244  -1254   1457       O  
ATOM   4386  CB  PHE B 121      -5.533 -29.432 -34.523  1.00 40.09           C  
ANISOU 4386  CB  PHE B 121     4546   4781   5906    100  -1084   1427       C  
ATOM   4387  CG  PHE B 121      -6.069 -28.163 -33.890  1.00 39.36           C  
ANISOU 4387  CG  PHE B 121     4612   4844   5500     18  -1002   1423       C  
ATOM   4388  CD1 PHE B 121      -7.416 -28.006 -33.604  1.00 38.43           C  
ANISOU 4388  CD1 PHE B 121     4622   4804   5176    -20   -898   1456       C  
ATOM   4389  CD2 PHE B 121      -5.226 -27.098 -33.606  1.00 39.27           C  
ANISOU 4389  CD2 PHE B 121     4601   4895   5427    -16  -1032   1355       C  
ATOM   4390  CE1 PHE B 121      -7.889 -26.818 -33.059  1.00 37.80           C  
ANISOU 4390  CE1 PHE B 121     4657   4861   4844    -69   -828   1392       C  
ATOM   4391  CE2 PHE B 121      -5.705 -25.922 -33.046  1.00 38.32           C  
ANISOU 4391  CE2 PHE B 121     4606   4882   5070    -75   -979   1300       C  
ATOM   4392  CZ  PHE B 121      -7.034 -25.777 -32.776  1.00 37.36           C  
ANISOU 4392  CZ  PHE B 121     4604   4838   4753    -91   -876   1303       C  
ATOM   4393  N   ASN B 122      -4.136 -32.669 -33.872  1.00 42.44           N  
ANISOU 4393  N   ASN B 122     4546   4633   6944    210  -1616   1699       N  
ATOM   4394  CA  ASN B 122      -3.631 -33.943 -34.453  1.00 44.17           C  
ANISOU 4394  CA  ASN B 122     4568   4611   7605    331  -1755   1633       C  
ATOM   4395  C   ASN B 122      -3.046 -33.631 -35.837  1.00 44.04           C  
ANISOU 4395  C   ASN B 122     4385   4646   7704    454  -1592   1288       C  
ATOM   4396  O   ASN B 122      -3.618 -34.075 -36.878  1.00 44.07           O  
ANISOU 4396  O   ASN B 122     4323   4608   7815    529  -1474   1099       O  
ATOM   4397  CB  ASN B 122      -4.730 -35.006 -34.535  1.00 44.45           C  
ANISOU 4397  CB  ASN B 122     4629   4474   7787    320  -1792   1733       C  
ATOM   4398  CG  ASN B 122      -4.260 -36.385 -34.956  1.00 46.14           C  
ANISOU 4398  CG  ASN B 122     4639   4381   8513    441  -1992   1673       C  
ATOM   4399  ND2 ASN B 122      -5.190 -37.143 -35.520  1.00 45.42           N  
ANISOU 4399  ND2 ASN B 122     4527   4142   8588    461  -1961   1613       N  
ATOM   4400  OD1 ASN B 122      -3.099 -36.768 -34.754  1.00 46.91           O  
ANISOU 4400  OD1 ASN B 122     4586   4362   8875    518  -2187   1669       O  
ATOM   4401  N   ILE B 123      -1.951 -32.875 -35.846  1.00 43.92           N  
ANISOU 4401  N   ILE B 123     4292   4747   7649    460  -1584   1210       N  
ATOM   4402  CA  ILE B 123      -1.250 -32.435 -37.081  1.00 43.38           C  
ANISOU 4402  CA  ILE B 123     4042   4802   7639    541  -1419    924       C  
ATOM   4403  C   ILE B 123       0.171 -32.988 -37.021  1.00 45.84           C  
ANISOU 4403  C   ILE B 123     4108   5031   8278    636  -1598    847       C  
ATOM   4404  O   ILE B 123       0.800 -32.956 -35.936  1.00 46.72           O  
ANISOU 4404  O   ILE B 123     4241   5089   8421    589  -1805   1035       O  
ATOM   4405  CB  ILE B 123      -1.286 -30.897 -37.180  1.00 42.03           C  
ANISOU 4405  CB  ILE B 123     3983   4855   7130    435  -1234    922       C  
ATOM   4406  CG1 ILE B 123      -2.718 -30.360 -36.991  1.00 39.61           C  
ANISOU 4406  CG1 ILE B 123     3921   4600   6529    351  -1105   1016       C  
ATOM   4407  CG2 ILE B 123      -0.646 -30.439 -38.480  1.00 42.14           C  
ANISOU 4407  CG2 ILE B 123     3806   5033   7173    482  -1053    692       C  
ATOM   4408  CD1 ILE B 123      -2.837 -28.870 -36.930  1.00 37.88           C  
ANISOU 4408  CD1 ILE B 123     3821   4536   6037    254   -974   1026       C  
ATOM   4409  N   LYS B 124       0.657 -33.490 -38.149  1.00 47.50           N  
ANISOU 4409  N   LYS B 124     4074   5256   8720    771  -1528    562       N  
ATOM   4410  CA  LYS B 124       2.038 -34.031 -38.277  1.00 50.44           C  
ANISOU 4410  CA  LYS B 124     4151   5575   9439    893  -1673    413       C  
ATOM   4411  C   LYS B 124       2.923 -32.889 -38.773  1.00 49.79           C  
ANISOU 4411  C   LYS B 124     3954   5778   9188    841  -1500    302       C  
ATOM   4412  O   LYS B 124       2.477 -32.171 -39.699  1.00 48.30           O  
ANISOU 4412  O   LYS B 124     3793   5808   8750    794  -1236    195       O  
ATOM   4413  CB  LYS B 124       2.091 -35.255 -39.212  1.00 52.57           C  
ANISOU 4413  CB  LYS B 124     4180   5719  10077   1081  -1699    112       C  
ATOM   4414  CG  LYS B 124       3.319 -36.166 -39.041  1.00 55.96           C  
ANISOU 4414  CG  LYS B 124     4313   5971  10979   1238  -1946     -9       C  
ATOM   4415  CD  LYS B 124       4.277 -36.378 -40.249  1.00 57.39           C  
ANISOU 4415  CD  LYS B 124     4119   6326  11362   1402  -1826   -449       C  
ATOM   4416  CE  LYS B 124       5.519 -37.198 -39.928  1.00 60.26           C  
ANISOU 4416  CE  LYS B 124     4181   6503  12213   1563  -2094   -559       C  
ATOM   4417  NZ  LYS B 124       6.228 -36.749 -38.702  0.69 60.07           N1+
ANISOU 4417  NZ  LYS B 124     4230   6423  12170   1464  -2297   -231       N1+
ATOM   4418  N   ASN B 125       4.075 -32.683 -38.133  1.00 50.95           N  
ANISOU 4418  N   ASN B 125     3985   5921   9455    828  -1655    366       N  
ATOM   4419  CA  ASN B 125       5.103 -31.719 -38.592  1.00 51.35           C  
ANISOU 4419  CA  ASN B 125     3861   6220   9430    774  -1524    261       C  
ATOM   4420  C   ASN B 125       5.623 -32.197 -39.944  1.00 53.53           C  
ANISOU 4420  C   ASN B 125     3809   6652   9878    911  -1368    -82       C  
ATOM   4421  O   ASN B 125       6.339 -33.192 -39.950  1.00 56.27           O  
ANISOU 4421  O   ASN B 125     3910   6876  10593   1071  -1531   -241       O  
ATOM   4422  CB  ASN B 125       6.246 -31.609 -37.587  1.00 52.34           C  
ANISOU 4422  CB  ASN B 125     3893   6282   9711    749  -1767    379       C  
ATOM   4423  CG  ASN B 125       7.281 -30.584 -37.978  1.00 52.31           C  
ANISOU 4423  CG  ASN B 125     3706   6519   9648    664  -1646    299       C  
ATOM   4424  ND2 ASN B 125       8.417 -30.622 -37.317  1.00 54.63           N  
ANISOU 4424  ND2 ASN B 125     3836   6779  10142    672  -1854    331       N  
ATOM   4425  OD1 ASN B 125       7.079 -29.794 -38.888  1.00 50.98           O  
ANISOU 4425  OD1 ASN B 125     3525   6569   9275    586  -1380    224       O  
ATOM   4426  N   ASP B 126       5.277 -31.519 -41.036  1.00 53.82           N  
ANISOU 4426  N   ASP B 126     3829   6964   9658    855  -1076   -195       N  
ATOM   4427  CA  ASP B 126       5.729 -31.912 -42.398  1.00 57.89           C  
ANISOU 4427  CA  ASP B 126     4016   7728  10250    971   -894   -543       C  
ATOM   4428  C   ASP B 126       6.851 -30.956 -42.846  1.00 28.80           C  
ATOM   4429  O   ASP B 126       6.989 -30.726 -44.062  1.00 64.03           O  
ANISOU 4429  O   ASP B 126     4369   9174  10785    864   -498   -755       O  
ATOM   4430  CB  ASP B 126       4.563 -31.984 -43.390  1.00 55.85           C  
ANISOU 4430  CB  ASP B 126     3855   7598   9766    984   -686   -656       C  
ATOM   4431  CG  ASP B 126       3.807 -30.677 -43.525  1.00 53.75           C  
ANISOU 4431  CG  ASP B 126     3848   7487   9089    787   -505   -418       C  
ATOM   4432  OD1 ASP B 126       4.305 -29.662 -42.982  1.00 53.21           O  
ANISOU 4432  OD1 ASP B 126     3842   7450   8925    641   -517   -209       O  
ATOM   4433  OD2 ASP B 126       2.694 -30.685 -44.119  1.00 53.50           O1-
ANISOU 4433  OD2 ASP B 126     3952   7510   8863    785   -379   -443       O1-
ATOM   4434  N   PHE B 127       7.638 -30.409 -41.919  1.00 64.79           N  
ANISOU 4434  N   PHE B 127     4670   8848  11100    774   -894   -383       N  
ATOM   4435  CA  PHE B 127       8.784 -29.532 -42.251  1.00 68.41           C  
ANISOU 4435  CA  PHE B 127     4884   9580  11527    659   -785   -389       C  
ATOM   4436  C   PHE B 127      10.052 -30.365 -42.185  1.00 73.65           C  
ANISOU 4436  C   PHE B 127     5171  10243  12571    817   -926   -613       C  
ATOM   4437  O   PHE B 127      10.187 -31.163 -41.241  1.00 72.85           O  
ANISOU 4437  O   PHE B 127     5110   9825  12746    932  -1215   -578       O  
ATOM   4438  CB  PHE B 127       8.906 -28.352 -41.285  1.00 68.11           C  
ANISOU 4438  CB  PHE B 127     5061   9455  11362    452   -876    -82       C  
ATOM   4439  CG  PHE B 127       7.873 -27.271 -41.474  1.00 66.22           C  
ANISOU 4439  CG  PHE B 127     5121   9262  10780    283   -718    112       C  
ATOM   4440  CD1 PHE B 127       7.867 -26.482 -42.612  1.00 67.50           C  
ANISOU 4440  CD1 PHE B 127     5180   9727  10741    166   -452    114       C  
ATOM   4441  CD2 PHE B 127       6.909 -27.038 -40.511  1.00 64.75           C  
ANISOU 4441  CD2 PHE B 127     5299   8829  10473    238   -841    300       C  
ATOM   4442  CE1 PHE B 127       6.919 -25.486 -42.781  1.00 65.71           C  
ANISOU 4442  CE1 PHE B 127     5216   9504  10247     21   -341    311       C  
ATOM   4443  CE2 PHE B 127       5.964 -26.039 -40.680  1.00 63.23           C  
ANISOU 4443  CE2 PHE B 127     5355   8662  10008    105   -710    447       C  
ATOM   4444  CZ  PHE B 127       5.971 -25.267 -41.814  1.00 63.48           C  
ANISOU 4444  CZ  PHE B 127     5286   8943   9889      2   -474    457       C  
ATOM   4445  N   THR B 128      10.961 -30.157 -43.136  1.00 79.28           N  
ANISOU 4445  N   THR B 128     5514  11313  13295    812   -735   -816       N  
ATOM   4446  CA  THR B 128      12.340 -30.700 -43.057  1.00 86.94           C  
ANISOU 4446  CA  THR B 128     6072  12336  14625    936   -851  -1027       C  
ATOM   4447  C   THR B 128      12.934 -30.103 -41.779  1.00 87.07           C  
ANISOU 4447  C   THR B 128     6197  12153  14735    810  -1095   -745       C  
ATOM   4448  O   THR B 128      12.389 -29.095 -41.333  1.00 85.67           O  
ANISOU 4448  O   THR B 128     6332  11929  14291    608  -1072   -459       O  
ATOM   4449  CB  THR B 128      13.123 -30.409 -44.343  1.00 92.66           C  
ANISOU 4449  CB  THR B 128     6381  13565  15260    909   -551  -1272       C  
ATOM   4450  CG2 THR B 128      14.567 -30.870 -44.279  1.00 92.98           C  
ANISOU 4450  CG2 THR B 128     6420  13885  15023    943   -270  -1456       C  
ATOM   4451  OG1 THR B 128      12.443 -31.046 -45.423  1.00 95.76           O  
ANISOU 4451  OG1 THR B 128     6770  14148  15465    642   -452  -1009       O  
ATOM   4452  N   GLU B 129      13.944 -30.716 -41.167  1.00 90.23           N  
ANISOU 4452  N   GLU B 129     6357  12420  15506    934  -1345   -830       N  
ATOM   4453  CA  GLU B 129      14.624 -30.116 -39.989  1.00 91.94           C  
ANISOU 4453  CA  GLU B 129     6632  12503  15797    808  -1586   -586       C  
ATOM   4454  C   GLU B 129      15.302 -28.811 -40.443  1.00 45.19           C  
ATOM   4455  O   GLU B 129      15.451 -27.888 -39.610  1.00 90.51           O  
ANISOU 4455  O   GLU B 129     6469  12565  15355    383  -1495   -278       O  
ATOM   4456  CB  GLU B 129      15.662 -31.068 -39.392  1.00 97.55           C  
ANISOU 4456  CB  GLU B 129     7052  13048  16965   1001  -1897   -708       C  
ATOM   4457  CG  GLU B 129      15.141 -32.441 -38.996  1.00 99.09           C  
ANISOU 4457  CG  GLU B 129     7331  12891  17430   1236  -2142   -759       C  
ATOM   4458  CD  GLU B 129      16.210 -33.334 -38.373  1.00105.14           C  
ANISOU 4458  CD  GLU B 129     7797  13462  18691   1425  -2491   -840       C  
ATOM   4459  OE1 GLU B 129      16.115 -33.577 -37.151  1.00107.28           O  
ANISOU 4459  OE1 GLU B 129     8275  13442  19046   1415  -2829   -561       O  
ATOM   4460  OE2 GLU B 129      17.150 -33.774 -39.097  1.00107.69           O1-
ANISOU 4460  OE2 GLU B 129     7664  13945  19307   1581  -2432  -1179       O1-
ATOM   4461  N   GLU B 130      15.706 -28.752 -41.724  1.00 93.65           N  
ANISOU 4461  N   GLU B 130     6364  13426  15792    575  -1077   -741       N  
ATOM   4462  CA  GLU B 130      16.334 -27.567 -42.381  1.00 93.58           C  
ANISOU 4462  CA  GLU B 130     6156  13789  15612    329   -833   -659       C  
ATOM   4463  C   GLU B 130      15.288 -26.449 -42.413  1.00 89.69           C  
ANISOU 4463  C   GLU B 130     6067  13262  14750     98   -708   -357       C  
ATOM   4464  O   GLU B 130      15.447 -25.503 -41.667  1.00 88.22           O  
ANISOU 4464  O   GLU B 130     6034  12945  14541    -93   -826   -118       O  
ATOM   4465  CB  GLU B 130      16.865 -27.910 -43.786  1.00 95.46           C  
ANISOU 4465  CB  GLU B 130     5947  14494  15832    399   -530   -966       C  
ATOM   4466  CG  GLU B 130      17.176 -26.685 -44.664  1.00 95.97           C  
ANISOU 4466  CG  GLU B 130     5860  14990  15615    108   -222   -810       C  
ATOM   4467  CD  GLU B 130      18.318 -26.760 -45.685  1.00 99.38           C  
ANISOU 4467  CD  GLU B 130     5718  15950  16092     97     17  -1048       C  
ATOM   4468  OE1 GLU B 130      19.428 -27.208 -45.315  1.00101.06           O  
ANISOU 4468  OE1 GLU B 130     5585  16165  16646    205   -125  -1229       O  
ATOM   4469  OE2 GLU B 130      18.118 -26.328 -46.850  1.00 98.51           O1-
ANISOU 4469  OE2 GLU B 130     5486  16283  15661    -32    345  -1037       O1-
ATOM   4470  N   GLU B 131      14.234 -26.622 -43.204  1.00 89.08           N  
ANISOU 4470  N   GLU B 131     6142  13285  14420    131   -499   -394       N  
ATOM   4471  CA  GLU B 131      13.130 -25.642 -43.371  1.00 88.09           C  
ANISOU 4471  CA  GLU B 131     6388  13124  13957    -49   -376   -134       C  
ATOM   4472  C   GLU B 131      12.663 -25.083 -42.033  1.00 42.71           C  
ATOM   4473  O   GLU B 131      12.287 -23.921 -41.991  1.00 81.31           O  
ANISOU 4473  O   GLU B 131     6099  11859  12938   -351   -573    340       O  
ATOM   4474  CB  GLU B 131      11.895 -26.403 -43.837  1.00 90.18           C  
ANISOU 4474  CB  GLU B 131     6822  13389  14053    105   -260   -260       C  
ATOM   4475  CG  GLU B 131      11.052 -25.683 -44.859  1.00 91.04           C  
ANISOU 4475  CG  GLU B 131     7091  13700  13799    -54    -12    -99       C  
ATOM   4476  CD  GLU B 131      10.494 -26.677 -45.854  1.00 94.76           C  
ANISOU 4476  CD  GLU B 131     7495  14393  14116    101    175   -339       C  
ATOM   4477  OE1 GLU B 131       9.991 -26.239 -46.894  1.00 95.08           O  
ANISOU 4477  OE1 GLU B 131     7398  14361  14366    346     91   -650       O  
ATOM   4478  OE2 GLU B 131      10.588 -27.887 -45.584  1.00 98.40           O1-
ANISOU 4478  OE2 GLU B 131     8030  15093  14265    -23    385   -219       O1-
ATOM   4479  N   GLU B 132      12.662 -25.923 -41.008  1.00 78.95           N  
ANISOU 4479  N   GLU B 132     5715  11286  12998     24   -902     59       N  
ATOM   4480  CA  GLU B 132      12.128 -25.592 -39.662  1.00 75.62           C  
ANISOU 4480  CA  GLU B 132     5660  10541  12533    -29  -1149    257       C  
ATOM   4481  C   GLU B 132      13.092 -24.653 -38.932  1.00 37.00           C  
ATOM   4482  O   GLU B 132      12.651 -23.597 -38.462  1.00 76.16           O  
ANISOU 4482  O   GLU B 132     5895  10495  12549   -378  -1327    539       O  
ATOM   4483  CB  GLU B 132      11.898 -26.868 -38.861  1.00 76.04           C  
ANISOU 4483  CB  GLU B 132     5797  10344  12752    184  -1397    198       C  
ATOM   4484  CG  GLU B 132      11.109 -26.608 -37.593  1.00 74.48           C  
ANISOU 4484  CG  GLU B 132     5991   9895  12411    126  -1600    405       C  
ATOM   4485  CD  GLU B 132      10.683 -27.838 -36.828  1.00 74.18           C  
ANISOU 4485  CD  GLU B 132     6072   9627  12487    297  -1831    429       C  
ATOM   4486  OE1 GLU B 132      10.159 -27.644 -35.722  1.00 71.06           O  
ANISOU 4486  OE1 GLU B 132     5958   9090  11953    236  -2004    607       O  
ATOM   4487  OE2 GLU B 132      10.924 -28.969 -37.325  1.00 77.47           O1-
ANISOU 4487  OE2 GLU B 132     6277  10015  13142    483  -1848    266       O1-
ATOM   4488  N   ALA B 133      14.362 -25.036 -38.832  1.00 78.03           N  
ANISOU 4488  N   ALA B 133     5532  10909  13208   -155  -1408    258       N  
ATOM   4489  CA  ALA B 133      15.453 -24.202 -38.271  1.00 79.89           C  
ANISOU 4489  CA  ALA B 133     5604  11167  13582   -324  -1547    331       C  
ATOM   4490  C   ALA B 133      15.391 -22.785 -38.870  1.00 79.61           C  
ANISOU 4490  C   ALA B 133     5586  11269  13392   -596  -1340    478       C  
ATOM   4491  O   ALA B 133      15.573 -21.800 -38.120  1.00 80.58           O  
ANISOU 4491  O   ALA B 133     5826  11261  13530   -776  -1488    608       O  
ATOM   4492  CB  ALA B 133      16.785 -24.858 -38.551  1.00 83.10           C  
ANISOU 4492  CB  ALA B 133     5541  11737  14296   -220  -1589    147       C  
ATOM   4493  N   GLN B 134      15.137 -22.697 -40.184  1.00 79.22           N  
ANISOU 4493  N   GLN B 134     5416  11477  13209   -628  -1023    459       N  
ATOM   4494  CA  GLN B 134      15.116 -21.447 -40.990  1.00 78.92           C  
ANISOU 4494  CA  GLN B 134     5334  11616  13036   -892   -804    642       C  
ATOM   4495  C   GLN B 134      14.010 -20.549 -40.434  1.00 74.95           C  
ANISOU 4495  C   GLN B 134     5272  10835  12369  -1005   -876    834       C  
ATOM   4496  O   GLN B 134      14.298 -19.390 -40.127  1.00 75.51           O  
ANISOU 4496  O   GLN B 134     5368  10816  12506  -1229   -947    989       O  
ATOM   4497  CB  GLN B 134      14.934 -21.803 -42.474  1.00 80.41           C  
ANISOU 4497  CB  GLN B 134     5319  12175  13057   -856   -470    569       C  
ATOM   4498  CG  GLN B 134      14.905 -20.624 -43.439  1.00 81.84           C  
ANISOU 4498  CG  GLN B 134     5425  12597  13074  -1133   -234    806       C  
ATOM   4499  CD  GLN B 134      16.140 -19.770 -43.345  1.00 85.86           C  
ANISOU 4499  CD  GLN B 134     5635  13206  13781  -1375   -270    931       C  
ATOM   4500  NE2 GLN B 134      15.986 -18.497 -43.674  1.00 87.86           N  
ANISOU 4500  NE2 GLN B 134     5950  13460  13972  -1660   -200   1230       N  
ATOM   4501  OE1 GLN B 134      17.216 -20.234 -42.973  1.00 88.48           O  
ANISOU 4501  OE1 GLN B 134     5675  13596  14348  -1312   -377    772       O  
ATOM   4502  N   VAL B 135      12.817 -21.108 -40.221  1.00 70.82           N  
ANISOU 4502  N   VAL B 135     5069  10161  11679   -845   -887    799       N  
ATOM   4503  CA  VAL B 135      11.625 -20.337 -39.767  1.00 66.76           C  
ANISOU 4503  CA  VAL B 135     4960   9413  10991   -918   -927    939       C  
ATOM   4504  C   VAL B 135      11.829 -19.970 -38.295  1.00 65.95           C  
ANISOU 4504  C   VAL B 135     5020   9050  10988   -954  -1232    944       C  
ATOM   4505  O   VAL B 135      11.598 -18.802 -37.958  1.00 65.72           O  
ANISOU 4505  O   VAL B 135     5139   8883  10950  -1124  -1289   1048       O  
ATOM   4506  CB  VAL B 135      10.314 -21.103 -40.009  1.00 63.47           C  
ANISOU 4506  CB  VAL B 135     4793   8953  10369   -740   -836    888       C  
ATOM   4507  CG1 VAL B 135       9.105 -20.328 -39.515  1.00 61.18           C  
ANISOU 4507  CG1 VAL B 135     4885   8445   9917   -801   -876   1005       C  
ATOM   4508  CG2 VAL B 135      10.143 -21.459 -41.481  1.00 64.00           C  
ANISOU 4508  CG2 VAL B 135     4681   9317  10318   -705   -548    847       C  
ATOM   4509  N   ARG B 136      12.274 -20.926 -37.471  1.00 66.14           N  
ANISOU 4509  N   ARG B 136     4998   9017  11116   -801  -1435    830       N  
ATOM   4510  CA  ARG B 136      12.538 -20.742 -36.017  1.00 67.12           C  
ANISOU 4510  CA  ARG B 136     5250   8959  11294   -820  -1750    825       C  
ATOM   4511  C   ARG B 136      13.400 -19.490 -35.824  1.00 68.45           C  
ANISOU 4511  C   ARG B 136     5282   9115  11611  -1052  -1831    871       C  
ATOM   4512  O   ARG B 136      13.006 -18.618 -35.012  1.00 67.04           O  
ANISOU 4512  O   ARG B 136     5331   8768  11374  -1155  -1974    891       O  
ATOM   4513  CB  ARG B 136      13.234 -21.972 -35.417  1.00 69.85           C  
ANISOU 4513  CB  ARG B 136     5442   9306  11792   -644  -1955    737       C  
ATOM   4514  CG  ARG B 136      12.325 -23.176 -35.220  1.00 69.84           C  
ANISOU 4514  CG  ARG B 136     5628   9222  11687   -435  -1978    723       C  
ATOM   4515  CD  ARG B 136      12.674 -24.108 -34.063  1.00 71.78           C  
ANISOU 4515  CD  ARG B 136     5882   9361  12031   -309  -2298    733       C  
ATOM   4516  NE  ARG B 136      11.487 -24.898 -33.725  1.00 70.95           N  
ANISOU 4516  NE  ARG B 136     6055   9143  11760   -190  -2318    796       N  
ATOM   4517  CZ  ARG B 136      10.440 -24.461 -33.006  1.00 69.73           C  
ANISOU 4517  CZ  ARG B 136     6242   8921  11330   -253  -2349    886       C  
ATOM   4518  NH1 ARG B 136       9.397 -25.245 -32.777  1.00 68.37           N1+
ANISOU 4518  NH1 ARG B 136     6277   8674  11025   -154  -2348    954       N1+
ATOM   4519  NH2 ARG B 136      10.434 -23.242 -32.503  1.00 70.29           N  
ANISOU 4519  NH2 ARG B 136     6429   9002  11277   -415  -2385    892       N  
ATOM   4520  N   LYS B 137      14.522 -19.422 -36.557  1.00 70.87           N  
ANISOU 4520  N   LYS B 137     5211   9604  12113  -1131  -1740    867       N  
ATOM   4521  CA  LYS B 137      15.471 -18.271 -36.620  1.00 73.19           C  
ANISOU 4521  CA  LYS B 137     5291   9919  12600  -1383  -1780    938       C  
ATOM   4522  C   LYS B 137      14.697 -17.002 -37.007  1.00 71.75           C  
ANISOU 4522  C   LYS B 137     5309   9622  12332  -1576  -1667   1090       C  
ATOM   4523  O   LYS B 137      14.769 -16.007 -36.250  1.00 72.42           O  
ANISOU 4523  O   LYS B 137     5501   9503  12514  -1725  -1859   1105       O  
ATOM   4524  CB  LYS B 137      16.605 -18.574 -37.610  1.00 76.23           C  
ANISOU 4524  CB  LYS B 137     5215  10596  13152  -1420  -1614    922       C  
ATOM   4525  CG  LYS B 137      17.574 -17.428 -37.915  1.00 79.54           C  
ANISOU 4525  CG  LYS B 137     5361  11088  13774  -1711  -1598   1041       C  
ATOM   4526  CD  LYS B 137      18.531 -17.720 -39.081  1.00 82.27           C  
ANISOU 4526  CD  LYS B 137     5238  11810  14212  -1761  -1356   1041       C  
ATOM   4527  CE  LYS B 137      19.736 -16.790 -39.163  1.00 85.73           C  
ANISOU 4527  CE  LYS B 137     5330  12335  14908  -2043  -1395   1146       C  
ATOM   4528  NZ  LYS B 137      20.945 -17.454 -39.717  1.00 87.88           N1+
ANISOU 4528  NZ  LYS B 137     5099  12959  15332  -2002  -1289   1028       N1+
ATOM   4529  N   GLU B 138      13.968 -17.052 -38.130  1.00 70.10           N  
ANISOU 4529  N   GLU B 138     5142   9533  11960  -1564  -1389   1185       N  
ATOM   4530  CA  GLU B 138      13.236 -15.898 -38.728  1.00 69.10           C  
ANISOU 4530  CA  GLU B 138     5164   9320  11772  -1743  -1266   1376       C  
ATOM   4531  C   GLU B 138      12.250 -15.290 -37.718  1.00 26.80           C  
ATOM   4532  O   GLU B 138      12.014 -14.078 -37.811  1.00 67.68           O  
ANISOU 4532  O   GLU B 138     5443   8639  11633  -1911  -1480   1458       O  
ATOM   4533  CB  GLU B 138      12.498 -16.330 -39.999  1.00 67.40           C  
ANISOU 4533  CB  GLU B 138     4955   9321  11332  -1673   -965   1454       C  
ATOM   4534  CG  GLU B 138      13.365 -16.266 -41.250  1.00 69.97           C  
ANISOU 4534  CG  GLU B 138     4888  10005  11692  -1811   -735   1567       C  
ATOM   4535  CD  GLU B 138      12.800 -16.888 -42.522  1.00 69.20           C  
ANISOU 4535  CD  GLU B 138     4735  10219  11338  -1718   -441   1581       C  
ATOM   4536  OE1 GLU B 138      11.659 -17.387 -42.497  1.00 66.93           O  
ANISOU 4536  OE1 GLU B 138     4727   9841  10861  -1543   -412   1512       O  
ATOM   4537  OE2 GLU B 138      13.513 -16.889 -43.540  1.00 70.89           O1-
ANISOU 4537  OE2 GLU B 138     4606  10797  11530  -1824   -239   1647       O1-
ATOM   4538  N   ASN B 139      11.700 -16.109 -36.808  1.00 64.81           N  
ANISOU 4538  N   ASN B 139     5225   8374  11026  -1519  -1574   1178       N  
ATOM   4539  CA  ASN B 139      10.550 -15.786 -35.923  1.00 62.56           C  
ANISOU 4539  CA  ASN B 139     5309   7870  10591  -1456  -1692   1109       C  
ATOM   4540  C   ASN B 139      11.005 -15.558 -34.472  1.00 64.90           C  
ANISOU 4540  C   ASN B 139     5662   8041  10954  -1471  -2004    960       C  
ATOM   4541  O   ASN B 139      10.149 -15.152 -33.652  1.00 63.59           O  
ANISOU 4541  O   ASN B 139     5770   7731  10662  -1440  -2113    865       O  
ATOM   4542  CB  ASN B 139       9.498 -16.892 -36.010  1.00 58.72           C  
ANISOU 4542  CB  ASN B 139     5016   7446   9850  -1234  -1580   1069       C  
ATOM   4543  CG  ASN B 139       8.680 -16.806 -37.282  1.00 56.48           C  
ANISOU 4543  CG  ASN B 139     4770   7237   9452  -1232  -1309   1187       C  
ATOM   4544  ND2 ASN B 139       7.549 -17.493 -37.321  1.00 53.42           N  
ANISOU 4544  ND2 ASN B 139     4593   6850   8854  -1070  -1226   1151       N  
ATOM   4545  OD1 ASN B 139       9.043 -16.091 -38.211  1.00 56.42           O  
ANISOU 4545  OD1 ASN B 139     4601   7296   9541  -1390  -1184   1329       O  
ATOM   4546  N   GLN B 140      12.296 -15.756 -34.165  1.00 68.69           N  
ANISOU 4546  N   GLN B 140     5881   8600  11620  -1522  -2145    924       N  
ATOM   4547  CA  GLN B 140      12.803 -15.809 -32.762  1.00 70.73           C  
ANISOU 4547  CA  GLN B 140     6168   8806  11899  -1506  -2464    778       C  
ATOM   4548  C   GLN B 140      12.644 -14.431 -32.111  1.00 70.29           C  
ANISOU 4548  C   GLN B 140     6235   8545  11927  -1667  -2629    688       C  
ATOM   4549  O   GLN B 140      12.677 -14.358 -30.874  1.00 71.59           O  
ANISOU 4549  O   GLN B 140     6510   8678  12014  -1641  -2882    526       O  
ATOM   4550  CB  GLN B 140      14.242 -16.334 -32.692  1.00 75.51           C  
ANISOU 4550  CB  GLN B 140     6430   9545  12715  -1518  -2580    766       C  
ATOM   4551  CG  GLN B 140      14.407 -17.499 -31.705  1.00 78.42           C  
ANISOU 4551  CG  GLN B 140     6837   9981  12977  -1332  -2790    693       C  
ATOM   4552  CD  GLN B 140      15.075 -18.736 -32.285  1.00 81.32           C  
ANISOU 4552  CD  GLN B 140     6940  10499  13458  -1188  -2721    723       C  
ATOM   4553  NE2 GLN B 140      14.265 -19.722 -32.665  1.00 78.82           N  
ANISOU 4553  NE2 GLN B 140     6749  10209  12991  -1007  -2579    753       N  
ATOM   4554  OE1 GLN B 140      16.307 -18.826 -32.377  1.00 85.30           O  
ANISOU 4554  OE1 GLN B 140     7114  11088  14207  -1230  -2806    699       O  
ATOM   4555  N   TRP B 141      12.443 -13.384 -32.906  1.00 68.97           N  
ANISOU 4555  N   TRP B 141     6045   8247  11912  -1826  -2505    788       N  
ATOM   4556  CA  TRP B 141      12.264 -12.001 -32.397  1.00 69.97           C  
ANISOU 4556  CA  TRP B 141     6268   8115  12204  -1981  -2674    692       C  
ATOM   4557  C   TRP B 141      11.073 -11.911 -31.425  1.00 68.49           C  
ANISOU 4557  C   TRP B 141     6420   7836  11766  -1844  -2770    488       C  
ATOM   4558  O   TRP B 141      11.122 -11.038 -30.553  1.00 71.12           O  
ANISOU 4558  O   TRP B 141     6811   8013  12199  -1917  -2998    285       O  
ATOM   4559  CB  TRP B 141      12.135 -11.017 -33.559  1.00 70.03           C  
ANISOU 4559  CB  TRP B 141     6196   7984  12430  -2163  -2512    904       C  
ATOM   4560  CG  TRP B 141      10.959 -11.315 -34.428  1.00 66.86           C  
ANISOU 4560  CG  TRP B 141     5968   7621  11814  -2054  -2250   1039       C  
ATOM   4561  CD1 TRP B 141      10.943 -12.080 -35.553  1.00 65.30           C  
ANISOU 4561  CD1 TRP B 141     5660   7655  11495  -2005  -1984   1223       C  
ATOM   4562  CD2 TRP B 141       9.603 -10.888 -34.213  1.00 65.40           C  
ANISOU 4562  CD2 TRP B 141     6086   7261  11504  -1966  -2239    964       C  
ATOM   4563  CE2 TRP B 141       8.830 -11.426 -35.267  1.00 62.73           C  
ANISOU 4563  CE2 TRP B 141     5808   7051  10977  -1877  -1967   1140       C  
ATOM   4564  CE3 TRP B 141       8.974 -10.094 -33.245  1.00 65.89           C  
ANISOU 4564  CE3 TRP B 141     6350   7087  11599  -1949  -2435    737       C  
ATOM   4565  NE1 TRP B 141       9.673 -12.158 -36.062  1.00 62.67           N  
ANISOU 4565  NE1 TRP B 141     5549   7298  10966  -1902  -1818   1284       N  
ATOM   4566  CZ2 TRP B 141       7.460 -11.190 -35.373  1.00 60.95           C  
ANISOU 4566  CZ2 TRP B 141     5837   6709  10611  -1778  -1893   1124       C  
ATOM   4567  CZ3 TRP B 141       7.624  -9.854 -33.361  1.00 64.10           C  
ANISOU 4567  CZ3 TRP B 141     6364   6752  11240  -1842  -2348    704       C  
ATOM   4568  CH2 TRP B 141       6.879 -10.398 -34.410  1.00 61.53           C  
ANISOU 4568  CH2 TRP B 141     6095   6543  10742  -1760  -2083    909       C  
ATOM   4569  N   CYS B 142      10.041 -12.751 -31.531  1.00 65.59           N  
ANISOU 4569  N   CYS B 142     6254   7575  11094  -1657  -2612    513       N  
ATOM   4570  CA  CYS B 142       8.846 -12.632 -30.648  1.00 64.85           C  
ANISOU 4570  CA  CYS B 142     6459   7435  10746  -1541  -2673    326       C  
ATOM   4571  C   CYS B 142       9.015 -13.445 -29.342  1.00 67.12           C  
ANISOU 4571  C   CYS B 142     6812   7909  10782  -1434  -2869    181       C  
ATOM   4572  O   CYS B 142       8.031 -13.518 -28.585  1.00 66.98           O  
ANISOU 4572  O   CYS B 142     7020   7938  10489  -1336  -2897     43       O  
ATOM   4573  CB  CYS B 142       7.540 -12.961 -31.367  1.00 61.11           C  
ANISOU 4573  CB  CYS B 142     6168   6968  10084  -1422  -2419    427       C  
ATOM   4574  SG  CYS B 142       7.561 -14.469 -32.361  1.00 57.14           S  
ANISOU 4574  SG  CYS B 142     5580   6687   9444  -1297  -2174    649       S  
ATOM   4575  N   GLU B 143      10.206 -13.996 -29.042  1.00 70.54           N  
ANISOU 4575  N   GLU B 143     7044   8459  11299  -1458  -3015    214       N  
ATOM   4576  CA  GLU B 143      10.598 -14.573 -27.713  1.00 72.63           C  
ANISOU 4576  CA  GLU B 143     7329   8891  11374  -1401  -3279     99       C  
ATOM   4577  C   GLU B 143      11.898 -13.914 -27.224  1.00 75.17           C  
ANISOU 4577  C   GLU B 143     7432   9177  11951  -1550  -3541    -15       C  
ATOM   4578  O   GLU B 143      11.953 -13.072 -26.337  1.00 75.96           O  
ANISOU 4578  O   GLU B 143     7582   9231  12048  -1625  -3756   -249       O  
ATOM   4579  CB  GLU B 143      10.808 -16.089 -27.805  1.00 72.84           C  
ANISOU 4579  CB  GLU B 143     7300   9093  11283  -1259  -3243    279       C  
ATOM   4580  CG  GLU B 143       9.756 -16.906 -27.074  1.00 73.85           C  
ANISOU 4580  CG  GLU B 143     7675   9354  11030  -1119  -3248    296       C  
ATOM   4581  CD  GLU B 143       8.561 -17.373 -27.910  1.00 73.42           C  
ANISOU 4581  CD  GLU B 143     7774   9268  10856  -1018  -2954    410       C  
ATOM   4582  OE1 GLU B 143       8.795 -17.908 -29.022  1.00 73.74           O  
ANISOU 4582  OE1 GLU B 143     7680   9274  11061   -979  -2776    551       O  
ATOM   4583  OE2 GLU B 143       7.383 -17.227 -27.447  1.00 73.52           O1-
ANISOU 4583  OE2 GLU B 143     8021   9314  10598   -974  -2902    339       O1-
TER   
HETATM 4584  C1  GOL B 201     -21.413 -16.703 -47.255  1.00 60.62           C  
ANISOU 4584  C1  GOL B 201     7418   7925   7691    655      7   1391       C  
HETATM 4585  O1  GOL B 201     -20.951 -17.341 -46.059  1.00 53.44           O  
ANISOU 4585  O1  GOL B 201     6562   6969   6774    637     85   1205       O  
HETATM 4586  C2  GOL B 201     -21.557 -17.663 -48.437  1.00 63.37           C  
ANISOU 4586  C2  GOL B 201     7689   8564   7824    635     62   1429       C  
HETATM 4587  O2  GOL B 201     -22.827 -17.507 -49.076  1.00 66.42           O  
ANISOU 4587  O2  GOL B 201     8021   9015   8199    718      4   1451       O  
HETATM 4588  C3  GOL B 201     -20.482 -17.514 -49.507  1.00 64.67           C  
ANISOU 4588  C3  GOL B 201     7804   8900   7866    529     60   1638       C  
HETATM 4589  O3  GOL B 201     -19.531 -18.576 -49.434  1.00 60.49           O  
ANISOU 4589  O3  GOL B 201     7251   8508   7222    474    166   1519       O  
HETATM 4590  O   HOH B 301     -27.539 -34.022 -48.080  1.00 33.85           O  
HETATM 4591  O   HOH B 302     -30.209 -25.349 -49.383  1.00 33.01           O  
HETATM 4592  O   HOH B 303     -33.137 -31.146 -46.750  1.00 27.66           O  
HETATM 4593  O   HOH B 304      10.699 -19.346 -44.017  1.00 49.67           O  
HETATM 4594  O   HOH B 305      12.276 -15.270 -45.415  1.00 33.64           O  
HETATM 4595  O   HOH B 306     -35.373 -22.167 -30.695  1.00 29.79           O  
HETATM 4596  O   HOH B 307     -41.072 -24.091 -52.913  1.00 46.91           O  
HETATM 4597  O   HOH B 308     -22.813 -27.621 -42.716  1.00 32.36           O  
HETATM 4598  O   HOH B 309     -43.247 -19.582 -51.521  1.00 53.04           O  
HETATM 4599  O   HOH B 310       0.257 -19.501 -30.539  1.00 29.04           O  
HETATM 4600  O   HOH B 311     -40.290 -14.977 -46.998  1.00 28.27           O  
HETATM 4601  O   HOH B 312     -16.069 -23.032 -25.353  1.00 38.70           O  
HETATM 4602  O   HOH B 313      -0.706 -35.444 -33.252  1.00 36.11           O  
HETATM 4603  O   HOH B 314       1.610 -35.345 -34.003  1.00 20.67           O  
HETATM 4604  O   HOH B 315     -17.640 -13.035 -41.313  1.00 44.87           O  
HETATM 4605  O   HOH B 316     -36.945 -33.594 -32.309  1.00 28.80           O  
HETATM 4606  O   HOH B 317     -24.476 -14.033 -23.504  1.00 45.99           O  
HETATM 4607  O   HOH B 318     -30.155 -17.642 -21.564  1.00 37.27           O  
HETATM 4608  O   HOH B 319     -14.435 -15.057 -38.993  1.00 50.94           O  
HETATM 4609  O   HOH B 320       4.991 -31.942 -30.753  1.00 35.06           O  
ATOM   4610  N   LEU C  31       5.564  39.644 -14.001  1.00 26.09           N  
ANISOU 4610  N   LEU C  31     3243   3409   3260    440     14   -493       N  
ATOM   4611  CA  LEU C  31       6.016  38.395 -14.784  1.00 26.65           C  
ANISOU 4611  CA  LEU C  31     3321   3461   3346    464     15   -515       C  
ATOM   4612  C   LEU C  31       5.082  37.208 -14.527  1.00 27.42           C  
ANISOU 4612  C   LEU C  31     3416   3548   3457    457    -30   -530       C  
ATOM   4613  O   LEU C  31       4.384  37.183 -13.490  1.00 31.93           O  
ANISOU 4613  O   LEU C  31     3972   4116   4042    427    -49   -520       O  
ATOM   4614  CB  LEU C  31       7.455  38.037 -14.432  1.00 26.51           C  
ANISOU 4614  CB  LEU C  31     3262   3417   3394    463     35   -501       C  
ATOM   4615  CG  LEU C  31       7.855  38.139 -12.971  1.00 26.05           C  
ANISOU 4615  CG  LEU C  31     3177   3346   3376    424    -14   -464       C  
ATOM   4616  CD1 LEU C  31       7.368  36.936 -12.221  1.00 26.32           C  
ANISOU 4616  CD1 LEU C  31     3217   3362   3423    400    -68   -464       C  
ATOM   4617  CD2 LEU C  31       9.357  38.250 -12.818  1.00 26.53           C  
ANISOU 4617  CD2 LEU C  31     3186   3362   3531    425    -13   -441       C  
ATOM   4618  N   ASP C  32       5.012  36.262 -15.447  1.00 27.14           N  
ANISOU 4618  N   ASP C  32     3404   3494   3413    478    -36   -555       N  
ATOM   4619  CA  ASP C  32       3.917  35.240 -15.568  1.00 26.18           C  
ANISOU 4619  CA  ASP C  32     3289   3359   3299    479    -88   -574       C  
ATOM   4620  C   ASP C  32       2.498  35.787 -15.417  1.00 14.29           C  
ATOM   4621  O   ASP C  32       1.897  35.619 -14.382  1.00 24.75           O  
ANISOU 4621  O   ASP C  32     3060   3166   3177    444   -128   -567       O  
ATOM   4622  CB  ASP C  32       4.074  34.076 -14.600  1.00 25.92           C  
ANISOU 4622  CB  ASP C  32     3218   3316   3314    463   -104   -570       C  
ATOM   4623  CG  ASP C  32       3.514  32.826 -15.248  1.00 26.54           C  
ANISOU 4623  CG  ASP C  32     3313   3375   3397    478   -136   -598       C  
ATOM   4624  OD1 ASP C  32       2.721  33.002 -16.240  1.00 27.06           O1-
ANISOU 4624  OD1 ASP C  32     3423   3429   3430    490   -166   -613       O1-
ATOM   4625  OD2 ASP C  32       3.905  31.695 -14.818  1.00 15.04           O1-
HETATM 4626  N   SEP C  33       1.928  36.328 -16.497  1.00 25.26           N  
ANISOU 4626  N   SEP C  33     3208   3220   3170    481   -168   -578       N  
HETATM 4627  CA  SEP C  33       0.538  36.760 -16.536  1.00 25.12           C  
ANISOU 4627  CA  SEP C  33     3162   3168   3213    475   -231   -576       C  
HETATM 4628  C   SEP C  33      -0.387  35.563 -16.743  1.00 25.94           C  
ANISOU 4628  C   SEP C  33     3255   3230   3371    476   -298   -592       C  
HETATM 4629  O   SEP C  33      -1.592  35.743 -16.834  1.00 26.93           O  
ANISOU 4629  O   SEP C  33     3341   3304   3588    472   -363   -591       O  
HETATM 4630  CB  SEP C  33       0.284  37.765 -17.663  1.00 24.79           C  
ANISOU 4630  CB  SEP C  33     3182   3101   3135    481   -287   -567       C  
HETATM 4631  OG  SEP C  33       1.152  38.891 -17.501  1.00 23.77           O  
ANISOU 4631  OG  SEP C  33     3062   3011   2959    481   -219   -553       O  
HETATM 4632  P   SEP C  33       1.535  39.785 -18.775  1.00 23.44           P  
ANISOU 4632  P   SEP C  33     3129   2953   2826    485   -239   -547       P  
HETATM 4633  O1P SEP C  33       2.139  38.804 -19.764  1.00 23.38           O  
ANISOU 4633  O1P SEP C  33     3231   2921   2731    488   -227   -570       O  
HETATM 4634  O2P SEP C  33       0.218  40.416 -19.169  1.00 23.74           O1-
ANISOU 4634  O2P SEP C  33     3161   2934   2926    477   -356   -532       O1-
HETATM 4635  O3P SEP C  33       2.517  40.812 -18.266  1.00 22.44           O  
ANISOU 4635  O3P SEP C  33     2977   2873   2677    485   -146   -533       O  
ATOM   4636  N   GLY C  34       0.153  34.359 -16.938  1.00 26.09           N  
ANISOU 4636  N   GLY C  34     3304   3257   3351    484   -292   -607       N  
ATOM   4637  CA  GLY C  34      -0.699  33.260 -17.345  1.00 26.52           C  
ANISOU 4637  CA  GLY C  34     3364   3267   3444    487   -367   -623       C  
ATOM   4638  C   GLY C  34      -1.362  32.618 -16.153  1.00 26.58           C  
ANISOU 4638  C   GLY C  34     3282   3268   3550    472   -346   -626       C  
ATOM   4639  O   GLY C  34      -2.288  31.869 -16.356  1.00 26.99           O  
ANISOU 4639  O   GLY C  34     3313   3274   3669    473   -409   -637       O  
ATOM   4640  N   ILE C  35      -0.851  32.834 -14.944  1.00 26.77           N  
ANISOU 4640  N   ILE C  35     3273   3324   3575    452   -263   -617       N  
ATOM   4641  CA  ILE C  35      -1.437  32.223 -13.714  1.00 27.40           C  
ANISOU 4641  CA  ILE C  35     3308   3379   3723    422   -222   -622       C  
ATOM   4642  C   ILE C  35      -1.344  33.195 -12.540  1.00 27.97           C  
ANISOU 4642  C   ILE C  35     3375   3452   3799    384   -137   -609       C  
ATOM   4643  O   ILE C  35      -0.475  34.124 -12.528  1.00 27.45           O  
ANISOU 4643  O   ILE C  35     3336   3425   3670    385   -116   -591       O  
ATOM   4644  CB  ILE C  35      -0.767  30.893 -13.352  1.00 26.91           C  
ANISOU 4644  CB  ILE C  35     3266   3332   3628    417   -223   -626       C  
ATOM   4645  CG1 ILE C  35       0.679  31.145 -12.951  1.00 26.60           C  
ANISOU 4645  CG1 ILE C  35     3256   3330   3521    411   -193   -606       C  
ATOM   4646  CG2 ILE C  35      -0.869  29.875 -14.484  1.00 27.23           C  
ANISOU 4646  CG2 ILE C  35     3323   3363   3661    450   -291   -644       C  
ATOM   4647  CD1 ILE C  35       1.163  30.245 -11.879  1.00 26.67           C  
ANISOU 4647  CD1 ILE C  35     3276   3325   3531    378   -190   -595       C  
ATOM   4648  N   HIS C  36      -2.237  32.966 -11.589  1.00 29.30           N  
ANISOU 4648  N   HIS C  36     3522   3568   4042    346    -80   -620       N  
ATOM   4649  CA  HIS C  36      -2.309  33.697 -10.310  1.00 30.45           C  
ANISOU 4649  CA  HIS C  36     3698   3686   4185    290     26   -616       C  
ATOM   4650  C   HIS C  36      -2.572  32.724  -9.176  1.00 29.95           C  
ANISOU 4650  C   HIS C  36     3682   3575   4123    236     84   -626       C  
ATOM   4651  O   HIS C  36      -3.211  31.697  -9.381  1.00 29.85           O  
ANISOU 4651  O   HIS C  36     3635   3533   4174    246     63   -644       O  
ATOM   4652  CB  HIS C  36      -3.326  34.810 -10.477  1.00 32.74           C  
ANISOU 4652  CB  HIS C  36     3924   3927   4587    291     70   -627       C  
ATOM   4653  CG  HIS C  36      -2.739  35.865 -11.336  1.00 34.64           C  
ANISOU 4653  CG  HIS C  36     4162   4220   4779    327     16   -608       C  
ATOM   4654  CD2 HIS C  36      -1.888  36.874 -11.046  1.00 35.78           C  
ANISOU 4654  CD2 HIS C  36     4348   4405   4841    317     49   -589       C  
ATOM   4655  ND1 HIS C  36      -2.900  35.854 -12.710  1.00 36.40           N  
ANISOU 4655  ND1 HIS C  36     4359   4453   5019    377    -94   -606       N  
ATOM   4656  CE1 HIS C  36      -2.237  36.864 -13.240  1.00 36.28           C  
ANISOU 4656  CE1 HIS C  36     4370   4479   4935    393   -111   -588       C  
ATOM   4657  NE2 HIS C  36      -1.595  37.491 -12.240  1.00 36.61           N  
ANISOU 4657  NE2 HIS C  36     4440   4546   4925    362    -24   -578       N  
HETATM 4658  N   SEP C  37      -1.995  33.035  -8.014  1.00 29.50           N  
ANISOU 4658  N   SEP C  37     3724   3503   3982    175    144   -611       N  
HETATM 4659  CA  SEP C  37      -2.294  32.318  -6.793  1.00 29.83           C  
ANISOU 4659  CA  SEP C  37     3858   3475   4002    101    215   -619       C  
HETATM 4660  C   SEP C  37      -3.388  33.089  -6.075  1.00 32.13           C  
ANISOU 4660  C   SEP C  37     4164   3676   4368     47    375   -648       C  
HETATM 4661  O   SEP C  37      -3.897  34.049  -6.643  1.00 32.46           O  
ANISOU 4661  O   SEP C  37     4115   3718   4502     81    402   -659       O  
HETATM 4662  CB  SEP C  37      -1.052  32.188  -5.981  1.00 28.16           C  
ANISOU 4662  CB  SEP C  37     3773   3272   3655     52    165   -582       C  
HETATM 4663  OG  SEP C  37      -1.140  30.955  -5.318  1.00 27.42           O  
ANISOU 4663  OG  SEP C  37     3752   3130   3538      7    155   -582       O  
HETATM 4664  P   SEP C  37       0.097  30.447  -4.489  1.00 27.09           P  
ANISOU 4664  P   SEP C  37     3842   3069   3384    -48     54   -537       P  
HETATM 4665  O1P SEP C  37       1.083  30.008  -5.568  1.00 26.28           O  
ANISOU 4665  O1P SEP C  37     3624   3045   3315     36    -79   -518       O  
HETATM 4666  O2P SEP C  37       0.568  31.549  -3.583  1.00 27.29           O1-
ANISOU 4666  O2P SEP C  37     3998   3054   3317   -120     83   -513       O1-
HETATM 4667  O3P SEP C  37      -0.420  29.332  -3.649  1.00 27.81           O  
ANISOU 4667  O3P SEP C  37     4033   3082   3453   -115     83   -546       O  
ATOM   4668  N   GLY C  38      -3.704  32.717  -4.831  1.00 34.76           N  
ANISOU 4668  N   GLY C  38     4623   3920   4664    -42    487   -661       N  
ATOM   4669  CA  GLY C  38      -4.489  33.591  -3.973  1.00 37.63           C  
ANISOU 4669  CA  GLY C  38     5044   4180   5072   -112    677   -691       C  
ATOM   4670  C   GLY C  38      -3.736  34.062  -2.737  1.00 40.62           C  
ANISOU 4670  C   GLY C  38     5642   4518   5273   -211    728   -671       C  
ATOM   4671  O   GLY C  38      -4.255  34.957  -2.059  1.00 41.78           O  
ANISOU 4671  O   GLY C  38     5859   4579   5436   -274    896   -696       O  
ATOM   4672  N   ALA C  39      -2.557  33.486  -2.461  1.00 44.92           N  
ANISOU 4672  N   ALA C  39     6295   5105   5667   -230    583   -625       N  
ATOM   4673  CA  ALA C  39      -1.906  33.346  -1.120  1.00 49.88           C  
ANISOU 4673  CA  ALA C  39     7178   5654   6120   -348    582   -598       C  
ATOM   4674  C   ALA C  39      -2.819  33.843   0.002  1.00 49.26           C  
ANISOU 4674  C   ALA C  39     7266   5432   6018   -461    816   -640       C  
ATOM   4675  O   ALA C  39      -3.242  32.960   0.751  1.00 51.32           O  
ANISOU 4675  O   ALA C  39     7662   5598   6239   -538    889   -656       O  
ATOM   4676  CB  ALA C  39      -0.569  34.070  -1.016  1.00 53.71           C  
ANISOU 4676  CB  ALA C  39     7728   6185   6494   -354    444   -544       C  
ATOM   4677  OXT ALA C  39      -3.069  35.051   0.152  1.00 45.49           O1-
ANISOU 4677  OXT ALA C  39     6798   4929   5559   -479    932   -657       O1-
TER   
HETATM 4678  O   HOH C 101      -6.034  35.085  -8.004  1.00 28.23           O  
ATOM   4679  N   LEU D   2      63.262  52.390 -64.803  1.00155.15           N  
ANISOU 4679  N   LEU D   2    23058  19768  16123 -16054   1239  -2830       N  
ATOM   4680  CA  LEU D   2      63.734  51.682 -63.575  1.00154.62           C  
ANISOU 4680  CA  LEU D   2    22462  20232  16054 -15985   1010  -2997       C  
ATOM   4681  C   LEU D   2      62.810  50.489 -63.319  1.00148.35           C  
ANISOU 4681  C   LEU D   2    21429  19511  15426 -15125    926  -2932       C  
ATOM   4682  O   LEU D   2      61.623  50.580 -63.677  1.00144.98           O  
ANISOU 4682  O   LEU D   2    21463  18549  15073 -14659   1004  -2830       O  
ATOM   4683  CB  LEU D   2      63.794  52.664 -62.392  1.00158.31           C  
ANISOU 4683  CB  LEU D   2    23382  20405  16363 -16403    882  -3215       C  
ATOM   4684  CG  LEU D   2      62.549  52.820 -61.511  1.00155.47           C  
ANISOU 4684  CG  LEU D   2    23545  19509  16019 -15915    788  -3289       C  
ATOM   4685  CD1 LEU D   2      62.903  53.581 -60.249  1.00159.38           C  
ANISOU 4685  CD1 LEU D   2    24295  19920  16342 -16376    635  -3534       C  
ATOM   4686  CD2 LEU D   2      61.424  53.535 -62.237  1.00154.31           C  
ANISOU 4686  CD2 LEU D   2    24148  18581  15902 -15676    958  -3165       C  
ATOM   4687  N   GLN D   3      63.368  49.402 -62.772  1.00147.07           N  
ANISOU 4687  N   GLN D   3    20559  20007  15315 -14936    777  -2980       N  
ATOM   4688  CA  GLN D   3      62.640  48.158 -62.385  1.00141.59           C  
ANISOU 4688  CA  GLN D   3    19563  19469  14766 -14162    671  -2934       C  
ATOM   4689  C   GLN D   3      62.944  47.827 -60.898  1.00142.77           C  
ANISOU 4689  C   GLN D   3    19458  19937  14851 -14160    422  -3116       C  
ATOM   4690  O   GLN D   3      63.361  48.777 -60.146  1.00146.93           O  
ANISOU 4690  O   GLN D   3    20259  20350  15216 -14700    345  -3285       O  
ATOM   4691  CB  GLN D   3      62.913  47.033 -63.399  1.00138.20           C  
ANISOU 4691  CB  GLN D   3    18547  19487  14476 -13833    761  -2768       C  
ATOM   4692  CG  GLN D   3      63.864  47.375 -64.542  1.00141.02           C  
ANISOU 4692  CG  GLN D   3    18715  20075  14794 -14334    937  -2691       C  
ATOM   4693  CD  GLN D   3      64.527  46.142 -65.100  1.00139.14           C  
ANISOU 4693  CD  GLN D   3    17704  20506  14656 -14095    955  -2608       C  
ATOM   4694  NE2 GLN D   3      65.762  46.306 -65.546  1.00142.73           N  
ANISOU 4694  NE2 GLN D   3    17763  21429  15038 -14628   1020  -2625       N  
ATOM   4695  OE1 GLN D   3      63.951  45.055 -65.133  1.00134.10           O  
ANISOU 4695  OE1 GLN D   3    16827  19971  14154 -13447    915  -2533       O  
ATOM   4696  N   ARG D   4      62.685  46.577 -60.464  1.00139.05           N  
ANISOU 4696  N   ARG D   4    18540  19805  14487 -13580    301  -3085       N  
ATOM   4697  CA  ARG D   4      62.717  46.133 -59.037  1.00138.72           C  
ANISOU 4697  CA  ARG D   4    18309  20005  14393 -13429     61  -3228       C  
ATOM   4698  C   ARG D   4      62.983  44.623 -58.927  1.00135.48           C  
ANISOU 4698  C   ARG D   4    17184  20194  14100 -12943    -43  -3155       C  
ATOM   4699  O   ARG D   4      62.588  43.904 -59.852  1.00131.48           O  
ANISOU 4699  O   ARG D   4    16525  19692  13741 -12520     77  -2992       O  
ATOM   4700  CB  ARG D   4      61.389  46.458 -58.340  1.00136.28           C  
ANISOU 4700  CB  ARG D   4    18610  19092  14079 -13060     28  -3273       C  
ATOM   4701  CG  ARG D   4      60.964  47.926 -58.335  1.00139.11           C  
ANISOU 4701  CG  ARG D   4    19746  18786  14323 -13439    121  -3352       C  
ATOM   4702  CD  ARG D   4      61.744  48.895 -57.449  1.00144.38           C  
ANISOU 4702  CD  ARG D   4    20586  19482  14790 -14117     12  -3565       C  
ATOM   4703  NE  ARG D   4      61.054  50.175 -57.357  1.00146.27           N  
ANISOU 4703  NE  ARG D   4    21649  18990  14939 -14312     99  -3637       N  
ATOM   4704  CZ  ARG D   4      61.569  51.308 -56.884  1.00151.52           C  
ANISOU 4704  CZ  ARG D   4    22675  19469  15425 -14955     71  -3806       C  
ATOM   4705  NH1 ARG D   4      62.822  51.369 -56.462  1.00155.52           N1+
ANISOU 4705  NH1 ARG D   4    22777  20496  15817 -15519    -45  -3925       N1+
ATOM   4706  NH2 ARG D   4      60.818  52.394 -56.843  1.00152.97           N  
ANISOU 4706  NH2 ARG D   4    23639  18940  15541 -15032    160  -3857       N  
ATOM   4707  N   ASP D   5      63.642  44.187 -57.845  1.00137.53           N  
ANISOU 4707  N   ASP D   5    17041  20932  14284 -13013   -261  -3274       N  
ATOM   4708  CA  ASP D   5      63.984  42.765 -57.584  1.00135.94           C  
ANISOU 4708  CA  ASP D   5    16163  21318  14171 -12567   -390  -3218       C  
ATOM   4709  C   ASP D   5      62.770  42.041 -57.000  1.00133.05           C  
ANISOU 4709  C   ASP D   5    15978  20689  13887 -11883   -461  -3172       C  
ATOM   4710  O   ASP D   5      62.575  40.887 -57.388  1.00130.60           O  
ANISOU 4710  O   ASP D   5    15309  20597  13715 -11372   -450  -3044       O  
ATOM   4711  CB  ASP D   5      65.212  42.616 -56.681  1.00139.25           C  
ANISOU 4711  CB  ASP D   5    16075  22372  14462 -12926   -602  -3353       C  
ATOM   4712  CG  ASP D   5      65.490  41.186 -56.230  1.00136.69           C  
ANISOU 4712  CG  ASP D   5    15120  22606  14209 -12428   -765  -3301       C  
ATOM   4713  OD1 ASP D   5      64.760  40.711 -55.351  1.00133.72           O  
ANISOU 4713  OD1 ASP D   5    14871  22098  13837 -12008   -895  -3315       O  
ATOM   4714  OD2 ASP D   5      66.422  40.553 -56.775  1.00137.69           O1-
ANISOU 4714  OD2 ASP D   5    14643  23287  14384 -12453   -754  -3244       O1-
ATOM   4715  N   PHE D   6      62.000  42.680 -56.118  1.00134.73           N  
ANISOU 4715  N   PHE D   6    16721  20460  14012 -11879   -524  -3277       N  
ATOM   4716  CA  PHE D   6      60.803  42.093 -55.445  1.00131.60           C  
ANISOU 4716  CA  PHE D   6    16533  19801  13667 -11269   -589  -3251       C  
ATOM   4717  C   PHE D   6      61.200  41.198 -54.256  1.00130.78           C  
ANISOU 4717  C   PHE D   6    15993  20188  13508 -11081   -832  -3313       C  
ATOM   4718  O   PHE D   6      60.918  41.607 -53.112  1.00132.65           O  
ANISOU 4718  O   PHE D   6    16506  20282  13612 -11156   -961  -3450       O  
ATOM   4719  CB  PHE D   6      59.872  41.394 -56.446  1.00128.91           C  
ANISOU 4719  CB  PHE D   6    16229  19234  13518 -10703   -430  -3061       C  
ATOM   4720  CG  PHE D   6      59.190  42.348 -57.393  1.00131.02           C  
ANISOU 4720  CG  PHE D   6    17056  18912  13815 -10808   -217  -3006       C  
ATOM   4721  CD1 PHE D   6      59.840  42.833 -58.520  1.00134.21           C  
ANISOU 4721  CD1 PHE D   6    17414  19351  14230 -11187    -64  -2948       C  
ATOM   4722  CD2 PHE D   6      57.900  42.786 -57.143  1.00130.03           C  
ANISOU 4722  CD2 PHE D   6    17509  18202  13693 -10528   -168  -3012       C  
ATOM   4723  CE1 PHE D   6      59.215  43.732 -59.369  1.00134.43           C  
ANISOU 4723  CE1 PHE D   6    17983  18823  14269 -11283    123  -2888       C  
ATOM   4724  CE2 PHE D   6      57.273  43.685 -57.996  1.00130.36           C  
ANISOU 4724  CE2 PHE D   6    18077  17699  13754 -10604     17  -2956       C  
ATOM   4725  CZ  PHE D   6      57.933  44.159 -59.107  1.00132.36           C  
ANISOU 4725  CZ  PHE D   6    18300  17977  14015 -10982    158  -2890       C  
ATOM   4726  N   ILE D   7      61.852  40.052 -54.476  1.00128.58           N  
ANISOU 4726  N   ILE D   7    15075  20466  13312 -10854   -897  -3223       N  
ATOM   4727  CA  ILE D   7      62.118  39.054 -53.399  1.00127.36           C  
ANISOU 4727  CA  ILE D   7    14514  20757  13119 -10568  -1128  -3246       C  
ATOM   4728  C   ILE D   7      63.189  39.590 -52.446  1.00131.63           C  
ANISOU 4728  C   ILE D   7    14879  21673  13463 -11107  -1320  -3420       C  
ATOM   4729  O   ILE D   7      63.202  39.149 -51.290  1.00131.93           O  
ANISOU 4729  O   ILE D   7    14799  21919  13408 -10953  -1526  -3482       O  
ATOM   4730  CB  ILE D   7      62.505  37.687 -53.991  1.00125.38           C  
ANISOU 4730  CB  ILE D   7    13659  20963  13017 -10150  -1130  -3093       C  
ATOM   4731  CG1 ILE D   7      61.390  37.163 -54.900  1.00121.08           C  
ANISOU 4731  CG1 ILE D   7    13318  20031  12654  -9631   -948  -2932       C  
ATOM   4732  CG2 ILE D   7      62.838  36.677 -52.898  1.00125.30           C  
ANISOU 4732  CG2 ILE D   7    13242  21409  12958  -9863  -1373  -3105       C  
ATOM   4733  CD1 ILE D   7      60.001  37.127 -54.249  1.00117.82           C  
ANISOU 4733  CD1 ILE D   7    13388  19133  12247  -9240   -962  -2929       C  
ATOM   4734  N   THR D   8      64.039  40.499 -52.913  1.00134.82           N  
ANISOU 4734  N   THR D   8    15270  22160  13796 -11723  -1256  -3494       N  
ATOM   4735  CA  THR D   8      65.032  41.195 -52.068  1.00140.07           C  
ANISOU 4735  CA  THR D   8    15832  23132  14257 -12329  -1423  -3678       C  
ATOM   4736  C   THR D   8      64.399  42.467 -51.499  1.00141.46           C  
ANISOU 4736  C   THR D   8    16735  22717  14296 -12651  -1402  -3828       C  
ATOM   4737  O   THR D   8      64.598  42.733 -50.287  1.00145.49           O  
ANISOU 4737  O   THR D   8    17312  23336  14633 -12844  -1597  -3985       O  
ATOM   4738  CB  THR D   8      66.299  41.519 -52.861  1.00144.09           C  
ANISOU 4738  CB  THR D   8    15941  24056  14750 -12861  -1360  -3685       C  
ATOM   4739  CG2 THR D   8      67.286  42.352 -52.071  1.00149.46           C  
ANISOU 4739  CG2 THR D   8    16556  25016  15214 -13551  -1517  -3881       C  
ATOM   4740  OG1 THR D   8      66.853  40.254 -53.221  1.00142.90           O  
ANISOU 4740  OG1 THR D   8    15105  24475  14715 -12490  -1403  -3561       O  
ATOM   4741  N   ALA D   9      63.670  43.212 -52.334  1.00138.91           N  
ANISOU 4741  N   ALA D   9    16941  21797  14040 -12694  -1177  -3783       N  
ATOM   4742  CA  ALA D   9      63.174  44.570 -52.023  1.00139.83           C  
ANISOU 4742  CA  ALA D   9    17780  21317  14031 -13063  -1117  -3922       C  
ATOM   4743  C   ALA D   9      62.177  44.503 -50.864  1.00136.91           C  
ANISOU 4743  C   ALA D   9    17779  20647  13595 -12703  -1225  -4004       C  
ATOM   4744  O   ALA D   9      62.162  45.443 -50.055  1.00140.20           O  
ANISOU 4744  O   ALA D   9    18607  20829  13835 -13071  -1292  -4188       O  
ATOM   4745  CB  ALA D   9      62.556  45.191 -53.249  1.00138.46           C  
ANISOU 4745  CB  ALA D   9    18045  20598  13965 -13066   -855  -3816       C  
ATOM   4746  N   LEU D  10      61.383  43.436 -50.786  1.00130.61           N  
ANISOU 4746  N   LEU D  10    16846  19858  12923 -12025  -1237  -3877       N  
ATOM   4747  CA  LEU D  10      60.311  43.338 -49.769  1.00127.63           C  
ANISOU 4747  CA  LEU D  10    16834  19170  12490 -11641  -1307  -3936       C  
ATOM   4748  C   LEU D  10      60.925  43.082 -48.398  1.00129.19           C  
ANISOU 4748  C   LEU D  10    16779  19800  12506 -11781  -1569  -4077       C  
ATOM   4749  O   LEU D  10      60.608  43.796 -47.460  1.00131.10           O  
ANISOU 4749  O   LEU D  10    17442  19787  12582 -11956  -1637  -4245       O  
ATOM   4750  CB  LEU D  10      59.314  42.259 -50.176  1.00122.48           C  
ANISOU 4750  CB  LEU D  10    16091  18418  12026 -10914  -1230  -3748       C  
ATOM   4751  CG  LEU D  10      58.462  42.637 -51.383  1.00120.37           C  
ANISOU 4751  CG  LEU D  10    16199  17629  11909 -10743   -981  -3629       C  
ATOM   4752  CD1 LEU D  10      57.828  41.405 -52.011  1.00115.47           C  
ANISOU 4752  CD1 LEU D  10    15305  17083  11487 -10107   -916  -3427       C  
ATOM   4753  CD2 LEU D  10      57.403  43.663 -51.013  1.00120.73           C  
ANISOU 4753  CD2 LEU D  10    16978  17015  11879 -10737   -898  -3729       C  
ATOM   4754  N   PRO D  11      61.805  42.076 -48.215  1.00128.51           N  
ANISOU 4754  N   PRO D  11    16019  20375  12434 -11700  -1728  -4019       N  
ATOM   4755  CA  PRO D  11      62.525  41.923 -46.949  1.00131.20           C  
ANISOU 4755  CA  PRO D  11    16103  21167  12580 -11901  -1992  -4155       C  
ATOM   4756  C   PRO D  11      63.234  43.199 -46.480  1.00136.30           C  
ANISOU 4756  C   PRO D  11    16989  21785  13015 -12644  -2056  -4376       C  
ATOM   4757  O   PRO D  11      63.265  43.450 -45.301  1.00138.18           O  
ANISOU 4757  O   PRO D  11    17368  22074  13060 -12780  -2227  -4531       O  
ATOM   4758  CB  PRO D  11      63.556  40.843 -47.272  1.00131.34           C  
ANISOU 4758  CB  PRO D  11    15341  21888  12676 -11799  -2096  -4038       C  
ATOM   4759  CG  PRO D  11      62.869  40.005 -48.317  1.00126.47           C  
ANISOU 4759  CG  PRO D  11    14637  21113  12303 -11237  -1918  -3823       C  
ATOM   4760  CD  PRO D  11      62.104  40.997 -49.166  1.00125.71           C  
ANISOU 4760  CD  PRO D  11    15129  20362  12274 -11368  -1669  -3821       C  
ATOM   4761  N   GLU D  12      63.777  43.975 -47.416  1.00138.73           N  
ANISOU 4761  N   GLU D  12    17353  22007  13352 -13119  -1915  -4386       N  
ATOM   4762  CA  GLU D  12      64.481  45.250 -47.118  1.00144.25           C  
ANISOU 4762  CA  GLU D  12    18307  22644  13856 -13888  -1950  -4590       C  
ATOM   4763  C   GLU D  12      63.487  46.260 -46.549  1.00144.54           C  
ANISOU 4763  C   GLU D  12    19153  21981  13783 -13945  -1889  -4733       C  
ATOM   4764  O   GLU D  12      63.903  47.159 -45.813  1.00148.41           O  
ANISOU 4764  O   GLU D  12    19901  22425  14063 -14476  -1987  -4943       O  
ATOM   4765  CB  GLU D  12      65.150  45.778 -48.382  1.00146.19           C  
ANISOU 4765  CB  GLU D  12    18462  22904  14181 -14323  -1774  -4532       C  
ATOM   4766  CG  GLU D  12      66.352  44.934 -48.764  1.00147.37           C  
ANISOU 4766  CG  GLU D  12    17783  23827  14383 -14395  -1861  -4447       C  
ATOM   4767  CD  GLU D  12      67.348  45.556 -49.724  1.00151.16           C  
ANISOU 4767  CD  GLU D  12    18082  24490  14863 -15006  -1742  -4448       C  
ATOM   4768  OE1 GLU D  12      67.890  44.825 -50.566  1.00150.46           O  
ANISOU 4768  OE1 GLU D  12    17445  24814  14908 -14866  -1681  -4303       O  
ATOM   4769  OE2 GLU D  12      67.630  46.762 -49.586  1.00155.00           O1-
ANISOU 4769  OE2 GLU D  12    18962  24732  15201 -15642  -1716  -4601       O1-
ATOM   4770  N   GLN D  13      62.218  46.088 -46.902  1.00140.68           N  
ANISOU 4770  N   GLN D  13    19037  20983  13432 -13401  -1730  -4625       N  
ATOM   4771  CA  GLN D  13      61.068  46.901 -46.442  1.00140.61           C  
ANISOU 4771  CA  GLN D  13    19789  20283  13353 -13291  -1644  -4731       C  
ATOM   4772  C   GLN D  13      60.492  46.315 -45.146  1.00139.76           C  
ANISOU 4772  C   GLN D  13    19695  20263  13145 -12891  -1809  -4797       C  
ATOM   4773  O   GLN D  13      59.475  46.849 -44.655  1.00139.60           O  
ANISOU 4773  O   GLN D  13    20260  19719  13062 -12717  -1746  -4886       O  
ATOM   4774  CB  GLN D  13      60.024  46.914 -47.561  1.00136.30           C  
ANISOU 4774  CB  GLN D  13    19553  19219  13015 -12876  -1392  -4559       C  
ATOM   4775  CG  GLN D  13      60.447  47.747 -48.760  1.00138.16           C  
ANISOU 4775  CG  GLN D  13    19954  19233  13306 -13314  -1212  -4516       C  
ATOM   4776  CD  GLN D  13      60.376  49.228 -48.484  1.00142.01           C  
ANISOU 4776  CD  GLN D  13    21128  19201  13627 -13832  -1157  -4707       C  
ATOM   4777  NE2 GLN D  13      60.381  50.006 -49.550  1.00143.01           N  
ANISOU 4777  NE2 GLN D  13    21567  18958  13813 -14094   -964  -4647       N  
ATOM   4778  OE1 GLN D  13      60.335  49.668 -47.337  1.00143.94           O  
ANISOU 4778  OE1 GLN D  13    21631  19375  13686 -14001  -1287  -4905       O  
ATOM   4779  N   GLY D  14      61.095  45.245 -44.615  1.00139.58           N  
ANISOU 4779  N   GLY D  14    19056  20873  13103 -12728  -2009  -4749       N  
ATOM   4780  CA  GLY D  14      60.561  44.497 -43.458  1.00137.40           C  
ANISOU 4780  CA  GLY D  14    18728  20734  12745 -12292  -2165  -4768       C  
ATOM   4781  C   GLY D  14      59.365  43.626 -43.822  1.00131.34           C  
ANISOU 4781  C   GLY D  14    18003  19731  12170 -11555  -2040  -4578       C  
ATOM   4782  O   GLY D  14      58.679  43.147 -42.895  1.00129.41           O  
ANISOU 4782  O   GLY D  14    17852  19462  11854 -11179  -2122  -4595       O  
ATOM   4783  N   LEU D  15      59.146  43.379 -45.114  1.00128.43           N  
ANISOU 4783  N   LEU D  15    17544  19228  12027 -11360  -1854  -4400       N  
ATOM   4784  CA  LEU D  15      57.922  42.709 -45.617  1.00122.87           C  
ANISOU 4784  CA  LEU D  15    16954  18220  11511 -10706  -1704  -4226       C  
ATOM   4785  C   LEU D  15      58.288  41.329 -46.137  1.00119.12           C  
ANISOU 4785  C   LEU D  15    15834  18223  11201 -10342  -1746  -4023       C  
ATOM   4786  O   LEU D  15      57.745  40.926 -47.162  1.00115.34           O  
ANISOU 4786  O   LEU D  15    15335  17567  10922 -10011  -1580  -3858       O  
ATOM   4787  CB  LEU D  15      57.290  43.574 -46.705  1.00122.95           C  
ANISOU 4787  CB  LEU D  15    17434  17646  11634 -10757  -1453  -4189       C  
ATOM   4788  CG  LEU D  15      56.829  44.960 -46.256  1.00126.57           C  
ANISOU 4788  CG  LEU D  15    18595  17557  11940 -11064  -1390  -4384       C  
ATOM   4789  CD1 LEU D  15      56.115  45.682 -47.395  1.00125.81           C  
ANISOU 4789  CD1 LEU D  15    18950  16880  11973 -11013  -1142  -4308       C  
ATOM   4790  CD2 LEU D  15      55.928  44.852 -45.033  1.00125.73           C  
ANISOU 4790  CD2 LEU D  15    18775  17285  11712 -10740  -1462  -4484       C  
ATOM   4791  N   ASP D  16      59.135  40.625 -45.396  1.00120.17           N  
ANISOU 4791  N   ASP D  16    15483  18933  11242 -10381  -1969  -4040       N  
ATOM   4792  CA  ASP D  16      59.539  39.224 -45.674  1.00118.09           C  
ANISOU 4792  CA  ASP D  16    14594  19167  11108 -10001  -2047  -3860       C  
ATOM   4793  C   ASP D  16      58.310  38.379 -46.038  1.00113.29           C  
ANISOU 4793  C   ASP D  16    14090  18280  10673  -9340  -1923  -3689       C  
ATOM   4794  O   ASP D  16      58.342  37.699 -47.079  1.00111.10           O  
ANISOU 4794  O   ASP D  16    13534  18089  10590  -9094  -1819  -3522       O  
ATOM   4795  CB  ASP D  16      60.251  38.622 -44.465  1.00119.61           C  
ANISOU 4795  CB  ASP D  16    14414  19900  11134 -10020  -2326  -3917       C  
ATOM   4796  CG  ASP D  16      61.583  39.275 -44.139  1.00124.47           C  
ANISOU 4796  CG  ASP D  16    14802  20909  11582 -10658  -2476  -4070       C  
ATOM   4797  OD1 ASP D  16      61.592  40.480 -43.852  1.00127.13           O  
ANISOU 4797  OD1 ASP D  16    15562  20961  11780 -11123  -2451  -4249       O  
ATOM   4798  OD2 ASP D  16      62.604  38.571 -44.181  1.00125.36           O1-
ANISOU 4798  OD2 ASP D  16    14315  21613  11703 -10685  -2616  -4012       O1-
ATOM   4799  N   HIS D  17      57.272  38.403 -45.202  1.00112.31           N  
ANISOU 4799  N   HIS D  17    14345  17854  10473  -9070  -1932  -3734       N  
ATOM   4800  CA  HIS D  17      56.106  37.489 -45.315  1.00108.58           C  
ANISOU 4800  CA  HIS D  17    13932  17191  10135  -8442  -1849  -3580       C  
ATOM   4801  C   HIS D  17      55.472  37.622 -46.706  1.00105.98           C  
ANISOU 4801  C   HIS D  17    13758  16490  10019  -8276  -1604  -3458       C  
ATOM   4802  O   HIS D  17      55.016  36.596 -47.238  1.00102.26           O  
ANISOU 4802  O   HIS D  17    13077  16066   9711  -7821  -1547  -3285       O  
ATOM   4803  CB  HIS D  17      55.090  37.743 -44.193  1.00108.70           C  
ANISOU 4803  CB  HIS D  17    14387  16907  10006  -8267  -1873  -3679       C  
ATOM   4804  CG  HIS D  17      54.468  39.098 -44.232  1.00110.52           C  
ANISOU 4804  CG  HIS D  17    15228  16592  10172  -8503  -1731  -3825       C  
ATOM   4805  CD2 HIS D  17      53.292  39.526 -44.741  1.00108.62           C  
ANISOU 4805  CD2 HIS D  17    15426  15820  10025  -8269  -1527  -3797       C  
ATOM   4806  ND1 HIS D  17      55.087  40.209 -43.682  1.00115.32           N  
ANISOU 4806  ND1 HIS D  17    16064  17163  10589  -9042  -1802  -4033       N  
ATOM   4807  CE1 HIS D  17      54.322  41.269 -43.857  1.00115.96           C  
ANISOU 4807  CE1 HIS D  17    16721  16688  10652  -9124  -1642  -4127       C  
ATOM   4808  NE2 HIS D  17      53.210  40.875 -44.506  1.00111.99           N  
ANISOU 4808  NE2 HIS D  17    16348  15880  10322  -8641  -1473  -3982       N  
ATOM   4809  N   ILE D  18      55.444  38.838 -47.259  1.00107.44           N  
ANISOU 4809  N   ILE D  18    14315  16314  10194  -8635  -1469  -3544       N  
ATOM   4810  CA  ILE D  18      54.842  39.127 -48.591  1.00104.83           C  
ANISOU 4810  CA  ILE D  18    14192  15598  10041  -8520  -1236  -3435       C  
ATOM   4811  C   ILE D  18      55.613  38.336 -49.646  1.00103.40           C  
ANISOU 4811  C   ILE D  18    13484  15786  10018  -8479  -1210  -3281       C  
ATOM   4812  O   ILE D  18      54.979  37.569 -50.392  1.00 99.43           O  
ANISOU 4812  O   ILE D  18    12889  15205   9685  -8048  -1105  -3120       O  
ATOM   4813  CB  ILE D  18      54.852  40.642 -48.859  1.00107.73           C  
ANISOU 4813  CB  ILE D  18    15060  15543  10329  -8980  -1127  -3567       C  
ATOM   4814  CG1 ILE D  18      53.906  41.334 -47.874  1.00108.18           C  
ANISOU 4814  CG1 ILE D  18    15669  15186  10248  -8911  -1126  -3711       C  
ATOM   4815  CG2 ILE D  18      54.501  40.961 -50.306  1.00106.27           C  
ANISOU 4815  CG2 ILE D  18    15027  15039  10310  -8938   -908  -3444       C  
ATOM   4816  CD1 ILE D  18      53.779  42.822 -48.043  1.00111.25           C  
ANISOU 4816  CD1 ILE D  18    16628  15093  10551  -9305  -1017  -3849       C  
ATOM   4817  N   ALA D  19      56.929  38.528 -49.685  1.00106.21           N  
ANISOU 4817  N   ALA D  19    13507  16540  10309  -8919  -1302  -3339       N  
ATOM   4818  CA  ALA D  19      57.848  37.835 -50.609  1.00106.14           C  
ANISOU 4818  CA  ALA D  19    12953  16955  10422  -8935  -1287  -3220       C  
ATOM   4819  C   ALA D  19      57.627  36.329 -50.494  1.00102.73           C  
ANISOU 4819  C   ALA D  19    12127  16812  10096  -8371  -1360  -3075       C  
ATOM   4820  O   ALA D  19      57.621  35.667 -51.524  1.00100.18           O  
ANISOU 4820  O   ALA D  19    11568  16557   9937  -8133  -1253  -2931       O  
ATOM   4821  CB  ALA D  19      59.277  38.214 -50.300  1.00111.01           C  
ANISOU 4821  CB  ALA D  19    13243  18026  10909  -9477  -1422  -3333       C  
ATOM   4822  N   GLU D  20      57.446  35.827 -49.275  1.00102.89           N  
ANISOU 4822  N   GLU D  20    12104  16979  10011  -8177  -1536  -3114       N  
ATOM   4823  CA  GLU D  20      57.171  34.395 -49.004  1.00100.43           C  
ANISOU 4823  CA  GLU D  20    11477  16905   9775  -7638  -1620  -2978       C  
ATOM   4824  C   GLU D  20      55.875  33.997 -49.706  1.00 96.47           C  
ANISOU 4824  C   GLU D  20    11229  15987   9439  -7182  -1437  -2847       C  
ATOM   4825  O   GLU D  20      55.891  32.979 -50.383  1.00 93.81           O  
ANISOU 4825  O   GLU D  20    10584  15810   9250  -6852  -1398  -2700       O  
ATOM   4826  CB  GLU D  20      57.083  34.133 -47.499  1.00101.19           C  
ANISOU 4826  CB  GLU D  20    11599  17152   9696  -7558  -1827  -3054       C  
ATOM   4827  CG  GLU D  20      58.423  34.241 -46.786  1.00105.41           C  
ANISOU 4827  CG  GLU D  20    11776  18205  10071  -7934  -2045  -3157       C  
ATOM   4828  CD  GLU D  20      58.364  34.233 -45.268  1.00106.98           C  
ANISOU 4828  CD  GLU D  20    12072  18520  10055  -7948  -2253  -3261       C  
ATOM   4829  OE1 GLU D  20      57.667  33.366 -44.717  1.00104.66           O  
ANISOU 4829  OE1 GLU D  20    11798  18203   9766  -7500  -2302  -3173       O  
ATOM   4830  OE2 GLU D  20      59.009  35.102 -44.647  1.00110.41           O1-
ANISOU 4830  OE2 GLU D  20    12577  19067  10310  -8423  -2361  -3430       O1-
ATOM   4831  N   ASN D  21      54.800  34.775 -49.538  1.00 96.55           N  
ANISOU 4831  N   ASN D  21    11776  15492   9417  -7162  -1332  -2905       N  
ATOM   4832  CA  ASN D  21      53.480  34.533 -50.187  1.00 93.46           C  
ANISOU 4832  CA  ASN D  21    11658  14685   9167  -6751  -1156  -2794       C  
ATOM   4833  C   ASN D  21      53.692  34.429 -51.695  1.00 93.10           C  
ANISOU 4833  C   ASN D  21    11465  14615   9295  -6748   -997  -2678       C  
ATOM   4834  O   ASN D  21      53.175  33.471 -52.305  1.00 89.18           O  
ANISOU 4834  O   ASN D  21    10825  14116   8945  -6336   -930  -2532       O  
ATOM   4835  CB  ASN D  21      52.468  35.637 -49.867  1.00 93.55           C  
ANISOU 4835  CB  ASN D  21    12269  14172   9103  -6815  -1059  -2898       C  
ATOM   4836  CG  ASN D  21      51.978  35.523 -48.446  1.00 94.01           C  
ANISOU 4836  CG  ASN D  21    12486  14225   9009  -6686  -1184  -2986       C  
ATOM   4837  ND2 ASN D  21      52.123  36.570 -47.639  1.00 97.13           N  
ANISOU 4837  ND2 ASN D  21    13191  14489   9225  -7030  -1236  -3167       N  
ATOM   4838  OD1 ASN D  21      51.469  34.463 -48.091  1.00 91.82           O  
ANISOU 4838  OD1 ASN D  21    12055  14062   8771  -6276  -1229  -2888       O  
ATOM   4839  N   ILE D  22      54.436  35.375 -52.264  1.00 96.52           N  
ANISOU 4839  N   ILE D  22    11940  15033   9700  -7206   -939  -2744       N  
ATOM   4840  CA  ILE D  22      54.731  35.348 -53.719  1.00 96.50           C  
ANISOU 4840  CA  ILE D  22    11798  15029   9839  -7253   -781  -2639       C  
ATOM   4841  C   ILE D  22      55.329  33.983 -54.048  1.00 96.43           C  
ANISOU 4841  C   ILE D  22    11219  15486   9933  -6981   -840  -2520       C  
ATOM   4842  O   ILE D  22      54.766  33.302 -54.878  1.00 94.53           O  
ANISOU 4842  O   ILE D  22    10931  15150   9837  -6629   -730  -2389       O  
ATOM   4843  CB  ILE D  22      55.629  36.511 -54.128  1.00100.00           C  
ANISOU 4843  CB  ILE D  22    12317  15472  10207  -7842   -733  -2732       C  
ATOM   4844  CG1 ILE D  22      54.817  37.807 -54.155  1.00100.72           C  
ANISOU 4844  CG1 ILE D  22    13046  14984  10239  -8016   -619  -2809       C  
ATOM   4845  CG2 ILE D  22      56.297  36.225 -55.456  1.00100.36           C  
ANISOU 4845  CG2 ILE D  22    12041  15720  10370  -7916   -616  -2626       C  
ATOM   4846  CD1 ILE D  22      55.663  39.067 -54.218  1.00105.58           C  
ANISOU 4846  CD1 ILE D  22    13828  15553  10734  -8649   -604  -2936       C  
ATOM   4847  N   LEU D  23      56.388  33.575 -53.367  1.00 99.88           N  
ANISOU 4847  N   LEU D  23    11253  16408  10291  -7116  -1016  -2568       N  
ATOM   4848  CA  LEU D  23      57.117  32.318 -53.689  1.00100.79           C  
ANISOU 4848  CA  LEU D  23    10801  16999  10494  -6874  -1079  -2464       C  
ATOM   4849  C   LEU D  23      56.216  31.104 -53.427  1.00 98.39           C  
ANISOU 4849  C   LEU D  23    10476  16632  10275  -6287  -1107  -2348       C  
ATOM   4850  O   LEU D  23      56.396  30.073 -54.088  1.00 95.87           O  
ANISOU 4850  O   LEU D  23     9835  16509  10080  -5988  -1076  -2230       O  
ATOM   4851  CB  LEU D  23      58.379  32.240 -52.835  1.00104.73           C  
ANISOU 4851  CB  LEU D  23    10910  18020  10862  -7141  -1287  -2553       C  
ATOM   4852  CG  LEU D  23      59.370  33.390 -52.991  1.00108.98           C  
ANISOU 4852  CG  LEU D  23    11424  18686  11299  -7766  -1280  -2679       C  
ATOM   4853  CD1 LEU D  23      60.469  33.286 -51.950  1.00112.62           C  
ANISOU 4853  CD1 LEU D  23    11522  19659  11607  -8000  -1517  -2776       C  
ATOM   4854  CD2 LEU D  23      59.968  33.425 -54.384  1.00109.52           C  
ANISOU 4854  CD2 LEU D  23    11258  18874  11479  -7905  -1115  -2611       C  
ATOM   4855  N   SER D  24      55.261  31.226 -52.509  1.00 99.78           N  
ANISOU 4855  N   SER D  24    10997  16534  10380  -6134  -1155  -2382       N  
ATOM   4856  CA  SER D  24      54.335  30.141 -52.105  1.00 97.85           C  
ANISOU 4856  CA  SER D  24    10776  16213  10190  -5618  -1186  -2280       C  
ATOM   4857  C   SER D  24      53.475  29.672 -53.282  1.00 96.49           C  
ANISOU 4857  C   SER D  24    10693  15773  10198  -5293   -999  -2149       C  
ATOM   4858  O   SER D  24      52.864  28.604 -53.144  1.00 94.67           O  
ANISOU 4858  O   SER D  24    10398  15540  10032  -4872  -1018  -2047       O  
ATOM   4859  CB  SER D  24      53.456  30.585 -50.996  1.00 97.26           C  
ANISOU 4859  CB  SER D  24    11095  15869   9992  -5586  -1237  -2359       C  
ATOM   4860  OG  SER D  24      52.467  29.595 -50.770  1.00 95.09           O  
ANISOU 4860  OG  SER D  24    10868  15483   9778  -5109  -1228  -2250       O  
ATOM   4861  N   TYR D  25      53.398  30.458 -54.362  1.00 99.21           N  
ANISOU 4861  N   TYR D  25    11204  15887  10605  -5492   -830  -2151       N  
ATOM   4862  CA  TYR D  25      52.581  30.169 -55.572  1.00 98.37           C  
ANISOU 4862  CA  TYR D  25    11212  15511  10653  -5230   -646  -2035       C  
ATOM   4863  C   TYR D  25      53.354  29.288 -56.554  1.00 97.12           C  
ANISOU 4863  C   TYR D  25    10618  15673  10609  -5125   -608  -1940       C  
ATOM   4864  O   TYR D  25      52.738  28.731 -57.466  1.00 92.42           O  
ANISOU 4864  O   TYR D  25    10044  14933  10140  -4841   -487  -1835       O  
ATOM   4865  CB  TYR D  25      52.172  31.449 -56.303  1.00101.03           C  
ANISOU 4865  CB  TYR D  25    11944  15455  10989  -5491   -485  -2073       C  
ATOM   4866  CG  TYR D  25      51.180  32.296 -55.554  1.00102.97           C  
ANISOU 4866  CG  TYR D  25    12677  15302  11146  -5508   -479  -2153       C  
ATOM   4867  CD1 TYR D  25      49.967  31.784 -55.111  1.00102.33           C  
ANISOU 4867  CD1 TYR D  25    12775  15017  11090  -5111   -475  -2108       C  
ATOM   4868  CD2 TYR D  25      51.478  33.611 -55.254  1.00106.04           C  
ANISOU 4868  CD2 TYR D  25    13345  15528  11416  -5931   -474  -2283       C  
ATOM   4869  CE1 TYR D  25      49.073  32.565 -54.398  1.00103.09           C  
ANISOU 4869  CE1 TYR D  25    13301  14773  11097  -5113   -462  -2191       C  
ATOM   4870  CE2 TYR D  25      50.587  34.418 -54.564  1.00107.63           C  
ANISOU 4870  CE2 TYR D  25    14010  15355  11530  -5935   -461  -2369       C  
ATOM   4871  CZ  TYR D  25      49.385  33.887 -54.126  1.00106.44           C  
ANISOU 4871  CZ  TYR D  25    14012  15024  11406  -5513   -454  -2325       C  
ATOM   4872  OH  TYR D  25      48.503  34.658 -53.428  1.00107.93           O  
ANISOU 4872  OH  TYR D  25    14638  14868  11503  -5493   -433  -2417       O  
ATOM   4873  N   LEU D  26      54.671  29.184 -56.401  1.00100.77           N  
ANISOU 4873  N   LEU D  26    10694  16569  11026  -5350   -705  -1983       N  
ATOM   4874  CA  LEU D  26      55.548  28.413 -57.325  1.00102.28           C  
ANISOU 4874  CA  LEU D  26    10439  17111  11313  -5274   -664  -1911       C  
ATOM   4875  C   LEU D  26      55.346  26.909 -57.116  1.00101.37           C  
ANISOU 4875  C   LEU D  26    10077  17165  11275  -4774   -739  -1809       C  
ATOM   4876  O   LEU D  26      55.118  26.484 -55.978  1.00101.18           O  
ANISOU 4876  O   LEU D  26    10068  17193  11184  -4613   -893  -1818       O  
ATOM   4877  CB  LEU D  26      57.011  28.796 -57.098  1.00106.40           C  
ANISOU 4877  CB  LEU D  26    10607  18075  11745  -5670   -756  -1998       C  
ATOM   4878  CG  LEU D  26      57.310  30.288 -57.209  1.00109.70           C  
ANISOU 4878  CG  LEU D  26    11271  18342  12068  -6217   -696  -2107       C  
ATOM   4879  CD1 LEU D  26      58.774  30.565 -56.912  1.00114.49           C  
ANISOU 4879  CD1 LEU D  26    11483  19438  12579  -6614   -803  -2195       C  
ATOM   4880  CD2 LEU D  26      56.928  30.834 -58.575  1.00109.06           C  
ANISOU 4880  CD2 LEU D  26    11410  17957  12072  -6308   -467  -2054       C  
ATOM   4881  N   ASP D  27      55.428  26.144 -58.204  1.00102.44           N  
ANISOU 4881  N   ASP D  27    10015  17371  11538  -4546   -629  -1717       N  
ATOM   4882  CA  ASP D  27      55.540  24.661 -58.211  1.00101.00           C  
ANISOU 4882  CA  ASP D  27     9529  17411  11434  -4104   -689  -1623       C  
ATOM   4883  C   ASP D  27      56.964  24.293 -57.776  1.00101.77           C  
ANISOU 4883  C   ASP D  27     9144  18048  11477  -4194   -835  -1660       C  
ATOM   4884  O   ASP D  27      57.866  25.123 -57.940  1.00102.85           O  
ANISOU 4884  O   ASP D  27     9136  18388  11552  -4599   -827  -1741       O  
ATOM   4885  CB  ASP D  27      55.206  24.115 -59.601  1.00100.29           C  
ANISOU 4885  CB  ASP D  27     9415  17205  11484  -3884   -508  -1535       C  
ATOM   4886  CG  ASP D  27      56.192  24.568 -60.666  1.00102.93           C  
ANISOU 4886  CG  ASP D  27     9515  17756  11838  -4164   -389  -1562       C  
ATOM   4887  OD1 ASP D  27      56.618  25.738 -60.620  1.00103.50           O  
ANISOU 4887  OD1 ASP D  27     9669  17827  11828  -4601   -371  -1643       O  
ATOM   4888  OD2 ASP D  27      56.537  23.745 -61.526  1.00106.25           O1-
ANISOU 4888  OD2 ASP D  27     9679  18346  12346  -3951   -313  -1505       O1-
ATOM   4889  N   ALA D  28      57.152  23.084 -57.259  1.00100.34           N  
ANISOU 4889  N   ALA D  28     8721  18091  11314  -3827   -963  -1597       N  
ATOM   4890  CA  ALA D  28      58.453  22.572 -56.781  1.00105.46           C  
ANISOU 4890  CA  ALA D  28     8889  19272  11910  -3822  -1124  -1615       C  
ATOM   4891  C   ALA D  28      59.585  22.982 -57.738  1.00111.17           C  
ANISOU 4891  C   ALA D  28     9274  20311  12655  -4103  -1027  -1661       C  
ATOM   4892  O   ALA D  28      60.583  23.575 -57.264  1.00114.34           O  
ANISOU 4892  O   ALA D  28     9441  21052  12952  -4447  -1131  -1749       O  
ATOM   4893  CB  ALA D  28      58.370  21.078 -56.618  1.00103.39           C  
ANISOU 4893  CB  ALA D  28     8447  19122  11713  -3304  -1199  -1507       C  
ATOM   4894  N   ARG D  29      59.455  22.668 -59.030  1.00112.15           N  
ANISOU 4894  N   ARG D  29     9364  20348  12901  -3973   -836  -1608       N  
ATOM   4895  CA  ARG D  29      60.560  22.837 -60.015  1.00115.82           C  
ANISOU 4895  CA  ARG D  29     9458  21157  13389  -4173   -728  -1637       C  
ATOM   4896  C   ARG D  29      61.009  24.306 -60.069  1.00118.21           C  
ANISOU 4896  C   ARG D  29     9845  21473  13597  -4769   -684  -1739       C  
ATOM   4897  O   ARG D  29      62.230  24.554 -60.138  1.00118.73           O  
ANISOU 4897  O   ARG D  29     9518  21985  13608  -5038   -715  -1799       O  
ATOM   4898  CB  ARG D  29      60.141  22.368 -61.409  1.00114.31           C  
ANISOU 4898  CB  ARG D  29     9318  20787  13328  -3954   -511  -1566       C  
ATOM   4899  CG  ARG D  29      61.330  22.134 -62.331  1.00118.06           C  
ANISOU 4899  CG  ARG D  29     9332  21694  13831  -4016   -416  -1582       C  
ATOM   4900  CD  ARG D  29      61.009  22.130 -63.814  1.00116.79           C  
ANISOU 4900  CD  ARG D  29     9270  21348  13757  -3983   -170  -1542       C  
ATOM   4901  NE  ARG D  29      60.722  20.806 -64.356  1.00115.15           N  
ANISOU 4901  NE  ARG D  29     8971  21125  13657  -3471   -120  -1467       N  
ATOM   4902  CZ  ARG D  29      59.521  20.367 -64.727  1.00110.35           C  
ANISOU 4902  CZ  ARG D  29     8714  20091  13124  -3191    -47  -1398       C  
ATOM   4903  NH1 ARG D  29      58.452  21.136 -64.614  1.00107.97           N1+
ANISOU 4903  NH1 ARG D  29     8868  19349  12807  -3341    -14  -1389       N1+
ATOM   4904  NH2 ARG D  29      59.389  19.150 -65.220  1.00109.12           N  
ANISOU 4904  NH2 ARG D  29     8450  19955  13055  -2756     -6  -1341       N  
ATOM   4905  N   SER D  30      60.059  25.240 -60.059  1.00116.20           N  
ANISOU 4905  N   SER D  30    10084  20748  13319  -4967   -611  -1759       N  
ATOM   4906  CA  SER D  30      60.319  26.705 -60.109  1.00116.64           C  
ANISOU 4906  CA  SER D  30    10329  20708  13280  -5534   -558  -1853       C  
ATOM   4907  C   SER D  30      60.918  27.178 -58.783  1.00117.22           C  
ANISOU 4907  C   SER D  30    10314  21014  13208  -5810   -770  -1956       C  
ATOM   4908  O   SER D  30      61.836  27.997 -58.832  1.00118.60           O  
ANISOU 4908  O   SER D  30    10336  21427  13300  -6277   -772  -2042       O  
ATOM   4909  CB  SER D  30      59.071  27.469 -60.459  1.00114.04           C  
ANISOU 4909  CB  SER D  30    10569  19791  12971  -5589   -426  -1836       C  
ATOM   4910  OG  SER D  30      58.559  27.022 -61.707  1.00111.31           O  
ANISOU 4910  OG  SER D  30    10282  19264  12745  -5346   -241  -1742       O  
ATOM   4911  N   LEU D  31      60.423  26.667 -57.649  1.00114.79           N  
ANISOU 4911  N   LEU D  31    10099  20652  12863  -5543   -941  -1947       N  
ATOM   4912  CA  LEU D  31      60.965  26.959 -56.292  1.00117.04           C  
ANISOU 4912  CA  LEU D  31    10289  21186  12996  -5747  -1169  -2039       C  
ATOM   4913  C   LEU D  31      62.465  26.625 -56.262  1.00121.34           C  
ANISOU 4913  C   LEU D  31    10233  22371  13501  -5873  -1273  -2071       C  
ATOM   4914  O   LEU D  31      63.241  27.424 -55.684  1.00124.58           O  
ANISOU 4914  O   LEU D  31    10535  23024  13777  -6317  -1380  -2183       O  
ATOM   4915  CB  LEU D  31      60.181  26.147 -55.256  1.00114.08           C  
ANISOU 4915  CB  LEU D  31    10056  20686  12605  -5328  -1315  -1987       C  
ATOM   4916  CG  LEU D  31      60.612  26.286 -53.794  1.00115.77           C  
ANISOU 4916  CG  LEU D  31    10195  21142  12652  -5458  -1562  -2066       C  
ATOM   4917  CD1 LEU D  31      60.526  27.736 -53.340  1.00117.70           C  
ANISOU 4917  CD1 LEU D  31    10774  21184  12764  -5976  -1563  -2205       C  
ATOM   4918  CD2 LEU D  31      59.783  25.378 -52.886  1.00112.61           C  
ANISOU 4918  CD2 LEU D  31     9943  20605  12240  -5009  -1681  -1990       C  
ATOM   4919  N   CYS D  32      62.861  25.487 -56.840  1.00120.63           N  
ANISOU 4919  N   CYS D  32     9766  22552  13516  -5495  -1249  -1982       N  
ATOM   4920  CA  CYS D  32      64.275  25.045 -56.930  1.00124.46           C  
ANISOU 4920  CA  CYS D  32     9637  23672  13979  -5534  -1330  -2001       C  
ATOM   4921  C   CYS D  32      65.088  26.062 -57.731  1.00127.94           C  
ANISOU 4921  C   CYS D  32     9935  24287  14389  -6072  -1194  -2081       C  
ATOM   4922  O   CYS D  32      66.225  26.340 -57.339  1.00131.05           O  
ANISOU 4922  O   CYS D  32     9942  25168  14683  -6373  -1310  -2160       O  
ATOM   4923  CB  CYS D  32      64.371  23.684 -57.594  1.00123.00           C  
ANISOU 4923  CB  CYS D  32     9164  23640  13929  -4998  -1277  -1890       C  
ATOM   4924  SG  CYS D  32      63.150  22.525 -56.936  1.00117.93           S  
ANISOU 4924  SG  CYS D  32     8816  22644  13346  -4381  -1367  -1774       S  
ATOM   4925  N   ALA D  33      64.524  26.547 -58.839  1.00127.36           N  
ANISOU 4925  N   ALA D  33    10151  23845  14394  -6177   -955  -2055       N  
ATOM   4926  CA  ALA D  33      65.134  27.574 -59.717  1.00129.80           C  
ANISOU 4926  CA  ALA D  33    10420  24225  14674  -6701   -789  -2113       C  
ATOM   4927  C   ALA D  33      65.350  28.855 -58.902  1.00131.85           C  
ANISOU 4927  C   ALA D  33    10887  24431  14777  -7268   -886  -2237       C  
ATOM   4928  O   ALA D  33      66.447  29.446 -58.956  1.00136.43           O  
ANISOU 4928  O   ALA D  33    11166  25400  15270  -7728   -901  -2319       O  
ATOM   4929  CB  ALA D  33      64.250  27.817 -60.917  1.00126.23           C  
ANISOU 4929  CB  ALA D  33    10343  23297  14322  -6643   -538  -2043       C  
ATOM   4930  N   ALA D  34      64.324  29.257 -58.159  1.00127.71           N  
ANISOU 4930  N   ALA D  34    10865  23446  14216  -7236   -947  -2254       N  
ATOM   4931  CA  ALA D  34      64.334  30.484 -57.333  1.00127.38           C  
ANISOU 4931  CA  ALA D  34    11123  23252  14021  -7735  -1033  -2380       C  
ATOM   4932  C   ALA D  34      65.495  30.413 -56.331  1.00129.70           C  
ANISOU 4932  C   ALA D  34    10975  24124  14183  -7950  -1269  -2473       C  
ATOM   4933  O   ALA D  34      66.179  31.439 -56.173  1.00132.13           O  
ANISOU 4933  O   ALA D  34    11269  24565  14370  -8525  -1288  -2588       O  
ATOM   4934  CB  ALA D  34      62.997  30.665 -56.663  1.00124.20           C  
ANISOU 4934  CB  ALA D  34    11280  22300  13609  -7532  -1065  -2375       C  
ATOM   4935  N   GLU D  35      65.746  29.249 -55.717  1.00128.51           N  
ANISOU 4935  N   GLU D  35    10467  24315  14045  -7517  -1443  -2422       N  
ATOM   4936  CA  GLU D  35      66.870  29.067 -54.754  1.00131.96           C  
ANISOU 4936  CA  GLU D  35    10438  25349  14351  -7661  -1690  -2495       C  
ATOM   4937  C   GLU D  35      68.173  29.546 -55.399  1.00136.47           C  
ANISOU 4937  C   GLU D  35    10563  26403  14887  -8120  -1631  -2560       C  
ATOM   4938  O   GLU D  35      68.990  30.152 -54.694  1.00141.03           O  
ANISOU 4938  O   GLU D  35    10957  27317  15311  -8558  -1784  -2676       O  
ATOM   4939  CB  GLU D  35      67.042  27.607 -54.323  1.00130.47           C  
ANISOU 4939  CB  GLU D  35     9875  25486  14212  -7064  -1845  -2397       C  
ATOM   4940  CG  GLU D  35      65.988  27.111 -53.345  1.00127.09           C  
ANISOU 4940  CG  GLU D  35     9802  24721  13764  -6676  -1971  -2349       C  
ATOM   4941  CD  GLU D  35      65.811  25.602 -53.313  1.00124.71           C  
ANISOU 4941  CD  GLU D  35     9280  24540  13564  -6013  -2032  -2209       C  
ATOM   4942  OE1 GLU D  35      65.172  25.112 -52.370  1.00122.31           O  
ANISOU 4942  OE1 GLU D  35     9174  24083  13216  -5719  -2173  -2168       O  
ATOM   4943  OE2 GLU D  35      66.324  24.914 -54.222  1.00125.48           O1-
ANISOU 4943  OE2 GLU D  35     9016  24884  13777  -5794  -1936  -2143       O1-
ATOM   4944  N   LEU D  36      68.343  29.287 -56.697  1.00136.25           N  
ANISOU 4944  N   LEU D  36    10373  26411  14986  -8033  -1412  -2490       N  
ATOM   4945  CA  LEU D  36      69.635  29.442 -57.424  1.00140.95           C  
ANISOU 4945  CA  LEU D  36    10435  27553  15566  -8354  -1337  -2526       C  
ATOM   4946  C   LEU D  36      69.793  30.851 -57.996  1.00143.16           C  
ANISOU 4946  C   LEU D  36    10975  27639  15779  -9034  -1172  -2607       C  
ATOM   4947  O   LEU D  36      70.894  31.141 -58.511  1.00149.68           O  
ANISOU 4947  O   LEU D  36    11381  28927  16564  -9403  -1111  -2652       O  
ATOM   4948  CB  LEU D  36      69.697  28.409 -58.547  1.00139.59           C  
ANISOU 4948  CB  LEU D  36     9981  27502  15555  -7891  -1172  -2410       C  
ATOM   4949  CG  LEU D  36      69.960  26.978 -58.082  1.00139.92           C  
ANISOU 4949  CG  LEU D  36     9612  27904  15649  -7278  -1337  -2339       C  
ATOM   4950  CD1 LEU D  36      69.456  25.977 -59.119  1.00136.61           C  
ANISOU 4950  CD1 LEU D  36     9192  27310  15403  -6736  -1156  -2217       C  
ATOM   4951  CD2 LEU D  36      71.432  26.758 -57.733  1.00145.09           C  
ANISOU 4951  CD2 LEU D  36     9573  29338  16215  -7423  -1490  -2400       C  
ATOM   4952  N   VAL D  37      68.762  31.691 -57.893  1.00139.69           N  
ANISOU 4952  N   VAL D  37    11192  26560  15322  -9194  -1102  -2625       N  
ATOM   4953  CA  VAL D  37      68.758  33.065 -58.475  1.00139.91           C  
ANISOU 4953  CA  VAL D  37    11577  26291  15290  -9810   -930  -2688       C  
ATOM   4954  C   VAL D  37      69.811  33.931 -57.774  1.00144.27           C  
ANISOU 4954  C   VAL D  37    11932  27222  15663 -10458  -1070  -2838       C  
ATOM   4955  O   VAL D  37      70.488  34.687 -58.474  1.00147.90           O  
ANISOU 4955  O   VAL D  37    12303  27815  16078 -10975   -932  -2879       O  
ATOM   4956  CB  VAL D  37      67.359  33.699 -58.392  1.00135.52           C  
ANISOU 4956  CB  VAL D  37    11780  24959  14752  -9758   -852  -2673       C  
ATOM   4957  CG1 VAL D  37      67.389  35.171 -58.774  1.00137.86           C  
ANISOU 4957  CG1 VAL D  37    12484  24937  14959 -10405   -716  -2748       C  
ATOM   4958  CG2 VAL D  37      66.372  32.930 -59.251  1.00129.84           C  
ANISOU 4958  CG2 VAL D  37    11235  23893  14205  -9192   -691  -2526       C  
ATOM   4959  N   CYS D  38      69.931  33.838 -56.451  1.00144.18           N  
ANISOU 4959  N   CYS D  38    11867  27373  15541 -10448  -1331  -2919       N  
ATOM   4960  CA  CYS D  38      71.002  34.508 -55.664  1.00149.01           C  
ANISOU 4960  CA  CYS D  38    12217  28434  15968 -11028  -1508  -3069       C  
ATOM   4961  C   CYS D  38      70.831  34.163 -54.186  1.00147.93           C  
ANISOU 4961  C   CYS D  38    12093  28387  15726 -10830  -1801  -3125       C  
ATOM   4962  O   CYS D  38      69.778  33.613 -53.835  1.00143.85           O  
ANISOU 4962  O   CYS D  38    11894  27485  15278 -10320  -1828  -3053       O  
ATOM   4963  CB  CYS D  38      70.968  36.023 -55.824  1.00151.45           C  
ANISOU 4963  CB  CYS D  38    12989  28387  16168 -11736  -1399  -3178       C  
ATOM   4964  SG  CYS D  38      69.444  36.755 -55.178  1.00147.68           S  
ANISOU 4964  SG  CYS D  38    13418  27034  15659 -11671  -1397  -3214       S  
ATOM   4965  N   LYS D  39      71.829  34.490 -53.371  1.00151.21           N  
ANISOU 4965  N   LYS D  39    12177  29302  15973 -11237  -2008  -3250       N  
ATOM   4966  CA  LYS D  39      71.917  34.054 -51.955  1.00151.19           C  
ANISOU 4966  CA  LYS D  39    12054  29543  15846 -11059  -2317  -3301       C  
ATOM   4967  C   LYS D  39      70.695  34.576 -51.191  1.00147.10           C  
ANISOU 4967  C   LYS D  39    12261  28359  15272 -11016  -2347  -3347       C  
ATOM   4968  O   LYS D  39      70.167  33.828 -50.341  1.00145.09           O  
ANISOU 4968  O   LYS D  39    12058  28063  15005 -10545  -2508  -3302       O  
ATOM   4969  CB  LYS D  39      73.246  34.518 -51.353  1.00158.32           C  
ANISOU 4969  CB  LYS D  39    12498  31095  16563 -11618  -2512  -3442       C  
ATOM   4970  CG  LYS D  39      74.455  33.644 -51.681  1.00161.95           C  
ANISOU 4970  CG  LYS D  39    12124  32353  17056 -11467  -2582  -3391       C  
ATOM   4971  CD  LYS D  39      74.625  32.457 -50.743  1.00162.37           C  
ANISOU 4971  CD  LYS D  39    11806  32804  17085 -10905  -2855  -3332       C  
ATOM   4972  CE  LYS D  39      75.301  32.812 -49.428  1.00167.05           C  
ANISOU 4972  CE  LYS D  39    12215  33813  17442 -11255  -3169  -3469       C  
ATOM   4973  NZ  LYS D  39      74.972  31.831 -48.364  1.00165.84           N1+
ANISOU 4973  NZ  LYS D  39    12010  33752  17248 -10683  -3420  -3402       N1+
ATOM   4974  N   GLU D  40      70.242  35.794 -51.501  1.00145.76           N  
ANISOU 4974  N   GLU D  40    12639  27677  15066 -11470  -2189  -3426       N  
ATOM   4975  CA  GLU D  40      69.120  36.443 -50.774  1.00142.74           C  
ANISOU 4975  CA  GLU D  40    12965  26657  14611 -11481  -2206  -3495       C  
ATOM   4976  C   GLU D  40      67.824  35.658 -51.016  1.00135.34           C  
ANISOU 4976  C   GLU D  40    12327  25258  13840 -10784  -2103  -3346       C  
ATOM   4977  O   GLU D  40      67.092  35.431 -50.055  1.00134.12           O  
ANISOU 4977  O   GLU D  40    12442  24891  13628 -10507  -2229  -3361       O  
ATOM   4978  CB  GLU D  40      68.960  37.905 -51.192  1.00144.91           C  
ANISOU 4978  CB  GLU D  40    13757  26479  14824 -12097  -2038  -3601       C  
ATOM   4979  CG  GLU D  40      67.879  38.632 -50.413  1.00143.92           C  
ANISOU 4979  CG  GLU D  40    14351  25723  14609 -12122  -2056  -3692       C  
ATOM   4980  CD  GLU D  40      68.100  38.733 -48.907  1.00146.72           C  
ANISOU 4980  CD  GLU D  40    14706  26286  14756 -12253  -2337  -3836       C  
ATOM   4981  OE1 GLU D  40      69.201  38.377 -48.426  1.00150.60           O  
ANISOU 4981  OE1 GLU D  40    14634  27436  15149 -12418  -2538  -3881       O  
ATOM   4982  OE2 GLU D  40      67.164  39.176 -48.211  1.00145.72           O1-
ANISOU 4982  OE2 GLU D  40    15141  25668  14556 -12184  -2355  -3905       O1-
ATOM   4983  N   TRP D  41      67.560  35.252 -52.254  1.00130.66           N  
ANISOU 4983  N   TRP D  41    11680  24533  13434 -10524  -1883  -3210       N  
ATOM   4984  CA  TRP D  41      66.398  34.401 -52.610  1.00123.98           C  
ANISOU 4984  CA  TRP D  41    11046  23306  12754  -9860  -1781  -3060       C  
ATOM   4985  C   TRP D  41      66.502  33.076 -51.857  1.00121.95           C  
ANISOU 4985  C   TRP D  41    10406  23421  12509  -9327  -1987  -2988       C  
ATOM   4986  O   TRP D  41      65.530  32.702 -51.230  1.00117.93           O  
ANISOU 4986  O   TRP D  41    10205  22597  12004  -8952  -2041  -2951       O  
ATOM   4987  CB  TRP D  41      66.324  34.178 -54.119  1.00122.19           C  
ANISOU 4987  CB  TRP D  41    10740  22981  12705  -9733  -1525  -2938       C  
ATOM   4988  CG  TRP D  41      65.793  35.359 -54.871  1.00121.88           C  
ANISOU 4988  CG  TRP D  41    11234  22400  12676 -10093  -1304  -2964       C  
ATOM   4989  CD1 TRP D  41      66.140  36.666 -54.693  1.00125.31           C  
ANISOU 4989  CD1 TRP D  41    11933  22708  12971 -10737  -1291  -3100       C  
ATOM   4990  CD2 TRP D  41      64.839  35.339 -55.946  1.00118.22           C  
ANISOU 4990  CD2 TRP D  41    11109  21449  12361  -9831  -1069  -2847       C  
ATOM   4991  CE2 TRP D  41      64.667  36.676 -56.366  1.00119.75           C  
ANISOU 4991  CE2 TRP D  41    11766  21238  12494 -10328   -925  -2911       C  
ATOM   4992  CE3 TRP D  41      64.116  34.325 -56.593  1.00113.96           C  
ANISOU 4992  CE3 TRP D  41    10535  20774  11990  -9234   -970  -2696       C  
ATOM   4993  NE1 TRP D  41      65.469  37.461 -55.583  1.00123.99           N  
ANISOU 4993  NE1 TRP D  41    12260  21994  12859 -10878  -1061  -3067       N  
ATOM   4994  CZ2 TRP D  41      63.795  37.022 -57.396  1.00117.20           C  
ANISOU 4994  CZ2 TRP D  41    11861  20397  12274 -10222   -695  -2820       C  
ATOM   4995  CZ3 TRP D  41      63.249  34.670 -57.608  1.00111.33           C  
ANISOU 4995  CZ3 TRP D  41    10603  19940  11756  -9149   -745  -2616       C  
ATOM   4996  CH2 TRP D  41      63.095  36.000 -58.002  1.00112.98           C  
ANISOU 4996  CH2 TRP D  41    11257  19768  11901  -9627   -613  -2673       C  
ATOM   4997  N   GLN D  42      67.650  32.407 -51.916  1.00124.60           N  
ANISOU 4997  N   GLN D  42    10093  24408  12842  -9299  -2095  -2966       N  
ATOM   4998  CA  GLN D  42      67.894  31.154 -51.155  1.00124.77           C  
ANISOU 4998  CA  GLN D  42     9722  24832  12855  -8807  -2314  -2896       C  
ATOM   4999  C   GLN D  42      67.573  31.423 -49.683  1.00126.33           C  
ANISOU 4999  C   GLN D  42    10178  24950  12871  -8873  -2542  -2988       C  
ATOM   5000  O   GLN D  42      66.843  30.593 -49.089  1.00123.84           O  
ANISOU 5000  O   GLN D  42     9984  24492  12576  -8366  -2628  -2903       O  
ATOM   5001  CB  GLN D  42      69.329  30.650 -51.356  1.00128.43           C  
ANISOU 5001  CB  GLN D  42     9444  26049  13302  -8878  -2412  -2894       C  
ATOM   5002  CG  GLN D  42      69.745  29.509 -50.426  1.00129.04           C  
ANISOU 5002  CG  GLN D  42     9108  26591  13329  -8445  -2679  -2840       C  
ATOM   5003  CD  GLN D  42      70.610  29.981 -49.276  1.00133.95           C  
ANISOU 5003  CD  GLN D  42     9507  27661  13726  -8848  -2950  -2975       C  
ATOM   5004  NE2 GLN D  42      70.127  29.784 -48.055  1.00133.06           N  
ANISOU 5004  NE2 GLN D  42     9618  27446  13494  -8674  -3154  -2988       N  
ATOM   5005  OE1 GLN D  42      71.708  30.513 -49.474  1.00138.28           O  
ANISOU 5005  OE1 GLN D  42     9680  28660  14200  -9321  -2977  -3067       O  
ATOM   5006  N   ARG D  43      68.071  32.540 -49.130  1.00130.83           N  
ANISOU 5006  N   ARG D  43    10852  25596  13263  -9484  -2627  -3155       N  
ATOM   5007  CA  ARG D  43      67.913  32.870 -47.686  1.00132.48           C  
ANISOU 5007  CA  ARG D  43    11278  25793  13264  -9615  -2858  -3269       C  
ATOM   5008  C   ARG D  43      66.415  32.958 -47.364  1.00128.36           C  
ANISOU 5008  C   ARG D  43    11409  24590  12771  -9315  -2773  -3242       C  
ATOM   5009  O   ARG D  43      65.991  32.361 -46.359  1.00126.88           O  
ANISOU 5009  O   ARG D  43    11285  24416  12507  -8982  -2939  -3217       O  
ATOM   5010  CB  ARG D  43      68.626  34.175 -47.313  1.00137.37           C  
ANISOU 5010  CB  ARG D  43    11972  26527  13694 -10373  -2923  -3467       C  
ATOM   5011  CG  ARG D  43      68.584  34.480 -45.822  1.00139.45           C  
ANISOU 5011  CG  ARG D  43    12413  26846  13724 -10525  -3175  -3597       C  
ATOM   5012  CD  ARG D  43      68.845  35.940 -45.458  1.00143.15           C  
ANISOU 5012  CD  ARG D  43    13216  27163  14010 -11259  -3187  -3809       C  
ATOM   5013  NE  ARG D  43      67.849  36.877 -45.960  1.00140.92           N  
ANISOU 5013  NE  ARG D  43    13613  26145  13785 -11406  -2944  -3848       N  
ATOM   5014  CZ  ARG D  43      66.590  36.975 -45.519  1.00137.36           C  
ANISOU 5014  CZ  ARG D  43    13730  25128  13334 -11117  -2892  -3846       C  
ATOM   5015  NH1 ARG D  43      66.127  36.169 -44.578  1.00135.48           N1+
ANISOU 5015  NH1 ARG D  43    13481  24953  13043 -10667  -3053  -3801       N1+
ATOM   5016  NH2 ARG D  43      65.770  37.862 -46.053  1.00135.71           N  
ANISOU 5016  NH2 ARG D  43    14100  24286  13178 -11258  -2671  -3881       N  
ATOM   5017  N   VAL D  44      65.650  33.667 -48.200  1.00126.55           N  
ANISOU 5017  N   VAL D  44    11636  23804  12643  -9424  -2521  -3242       N  
ATOM   5018  CA  VAL D  44      64.197  33.921 -47.987  1.00122.99           C  
ANISOU 5018  CA  VAL D  44    11827  22685  12218  -9186  -2413  -3231       C  
ATOM   5019  C   VAL D  44      63.448  32.588 -48.032  1.00119.40           C  
ANISOU 5019  C   VAL D  44    11295  22171  11902  -8477  -2407  -3055       C  
ATOM   5020  O   VAL D  44      62.634  32.342 -47.133  1.00118.04           O  
ANISOU 5020  O   VAL D  44    11402  21785  11662  -8213  -2489  -3054       O  
ATOM   5021  CB  VAL D  44      63.643  34.908 -49.032  1.00121.56           C  
ANISOU 5021  CB  VAL D  44    12087  21972  12129  -9429  -2143  -3247       C  
ATOM   5022  CG1 VAL D  44      62.123  34.906 -49.064  1.00117.10           C  
ANISOU 5022  CG1 VAL D  44    12076  20775  11642  -9047  -2008  -3191       C  
ATOM   5023  CG2 VAL D  44      64.162  36.315 -48.807  1.00125.78           C  
ANISOU 5023  CG2 VAL D  44    12851  22436  12502 -10131  -2150  -3432       C  
ATOM   5024  N   ILE D  45      63.698  31.777 -49.059  1.00118.49           N  
ANISOU 5024  N   ILE D  45    10831  22226  11966  -8194  -2302  -2916       N  
ATOM   5025  CA  ILE D  45      63.072  30.435 -49.222  1.00114.77           C  
ANISOU 5025  CA  ILE D  45    10257  21715  11635  -7529  -2287  -2744       C  
ATOM   5026  C   ILE D  45      63.383  29.613 -47.975  1.00115.11           C  
ANISOU 5026  C   ILE D  45    10053  22129  11556  -7285  -2559  -2728       C  
ATOM   5027  O   ILE D  45      62.434  29.001 -47.420  1.00111.92           O  
ANISOU 5027  O   ILE D  45     9889  21478  11158  -6873  -2591  -2655       O  
ATOM   5028  CB  ILE D  45      63.565  29.746 -50.508  1.00115.21           C  
ANISOU 5028  CB  ILE D  45     9913  21988  11875  -7338  -2151  -2627       C  
ATOM   5029  CG1 ILE D  45      62.953  30.399 -51.753  1.00113.71           C  
ANISOU 5029  CG1 ILE D  45    10053  21338  11813  -7458  -1869  -2606       C  
ATOM   5030  CG2 ILE D  45      63.284  28.246 -50.478  1.00112.78           C  
ANISOU 5030  CG2 ILE D  45     9379  21799  11674  -6692  -2204  -2469       C  
ATOM   5031  CD1 ILE D  45      63.774  30.212 -53.018  1.00115.08           C  
ANISOU 5031  CD1 ILE D  45     9831  21791  12101  -7539  -1730  -2555       C  
ATOM   5032  N   SER D  46      64.654  29.608 -47.559  1.00118.32           N  
ANISOU 5032  N   SER D  46     9995  23113  11847  -7536  -2746  -2791       N  
ATOM   5033  CA  SER D  46      65.129  28.791 -46.419  1.00119.59           C  
ANISOU 5033  CA  SER D  46     9849  23710  11880  -7308  -3028  -2765       C  
ATOM   5034  C   SER D  46      64.408  29.238 -45.143  1.00119.82           C  
ANISOU 5034  C   SER D  46    10326  23475  11726  -7379  -3149  -2851       C  
ATOM   5035  O   SER D  46      63.724  28.385 -44.521  1.00118.47           O  
ANISOU 5035  O   SER D  46    10267  23199  11545  -6919  -3225  -2751       O  
ATOM   5036  CB  SER D  46      66.617  28.855 -46.263  1.00123.94           C  
ANISOU 5036  CB  SER D  46     9828  24930  12332  -7613  -3199  -2830       C  
ATOM   5037  OG  SER D  46      67.036  27.985 -45.228  1.00124.68           O  
ANISOU 5037  OG  SER D  46     9622  25440  12309  -7329  -3472  -2782       O  
ATOM   5038  N   GLU D  47      64.512  30.523 -44.778  1.00121.93           N  
ANISOU 5038  N   GLU D  47    10869  23611  11847  -7930  -3156  -3030       N  
ATOM   5039  CA  GLU D  47      64.026  31.018 -43.460  1.00122.25           C  
ANISOU 5039  CA  GLU D  47    11292  23486  11673  -8059  -3298  -3146       C  
ATOM   5040  C   GLU D  47      62.507  31.194 -43.495  1.00117.87           C  
ANISOU 5040  C   GLU D  47    11343  22259  11182  -7811  -3115  -3119       C  
ATOM   5041  O   GLU D  47      61.885  31.025 -42.453  1.00117.31           O  
ANISOU 5041  O   GLU D  47    11522  22068  10982  -7640  -3219  -3136       O  
ATOM   5042  CB  GLU D  47      64.744  32.299 -43.060  1.00126.38           C  
ANISOU 5042  CB  GLU D  47    11882  24128  12008  -8743  -3376  -3358       C  
ATOM   5043  CG  GLU D  47      66.207  32.051 -42.775  1.00130.69           C  
ANISOU 5043  CG  GLU D  47    11807  25400  12451  -8967  -3603  -3390       C  
ATOM   5044  CD  GLU D  47      66.956  33.287 -42.350  1.00135.49           C  
ANISOU 5044  CD  GLU D  47    12460  26161  12860  -9677  -3694  -3605       C  
ATOM   5045  OE1 GLU D  47      66.298  34.295 -42.079  1.00135.48           O  
ANISOU 5045  OE1 GLU D  47    13016  25684  12775  -9963  -3609  -3736       O  
ATOM   5046  OE2 GLU D  47      68.194  33.246 -42.306  1.00139.49           O1-
ANISOU 5046  OE2 GLU D  47    12445  27261  13294  -9946  -3846  -3645       O1-
ATOM   5047  N   GLY D  48      61.932  31.514 -44.653  1.00115.34           N  
ANISOU 5047  N   GLY D  48    11240  21536  11047  -7788  -2853  -3077       N  
ATOM   5048  CA  GLY D  48      60.473  31.630 -44.860  1.00111.64           C  
ANISOU 5048  CA  GLY D  48    11302  20450  10668  -7515  -2663  -3035       C  
ATOM   5049  C   GLY D  48      59.765  30.284 -44.769  1.00108.43           C  
ANISOU 5049  C   GLY D  48    10820  20016  10364  -6882  -2670  -2854       C  
ATOM   5050  O   GLY D  48      58.520  30.287 -44.757  1.00104.55           O  
ANISOU 5050  O   GLY D  48    10742  19061   9920  -6634  -2541  -2819       O  
ATOM   5051  N   MET D  49      60.508  29.168 -44.714  1.00109.95           N  
ANISOU 5051  N   MET D  49    10509  20680  10586  -6623  -2813  -2742       N  
ATOM   5052  CA  MET D  49      59.945  27.816 -44.458  1.00108.17           C  
ANISOU 5052  CA  MET D  49    10207  20467  10426  -6035  -2858  -2570       C  
ATOM   5053  C   MET D  49      59.029  27.474 -45.647  1.00105.21           C  
ANISOU 5053  C   MET D  49    10000  19688  10285  -5732  -2602  -2453       C  
ATOM   5054  O   MET D  49      57.885  27.015 -45.438  1.00102.20           O  
ANISOU 5054  O   MET D  49     9914  18975   9942  -5385  -2536  -2375       O  
ATOM   5055  CB  MET D  49      59.189  27.829 -43.119  1.00107.85           C  
ANISOU 5055  CB  MET D  49    10508  20267  10203  -5937  -2974  -2608       C  
ATOM   5056  CG  MET D  49      59.378  26.606 -42.196  1.00108.32           C  
ANISOU 5056  CG  MET D  49    10326  20657  10174  -5557  -3193  -2490       C  
ATOM   5057  SD  MET D  49      61.066  25.935 -41.900  1.00112.81           S  
ANISOU 5057  SD  MET D  49    10209  21989  10665  -5584  -3471  -2456       S  
ATOM   5058  CE  MET D  49      62.063  27.343 -41.414  1.00117.49           C  
ANISOU 5058  CE  MET D  49    10745  22844  11052  -6288  -3596  -2693       C  
ATOM   5059  N   LEU D  50      59.520  27.722 -46.866  1.00106.89           N  
ANISOU 5059  N   LEU D  50    10032  19941  10642  -5882  -2458  -2444       N  
ATOM   5060  CA  LEU D  50      58.690  27.732 -48.102  1.00104.81           C  
ANISOU 5060  CA  LEU D  50     9982  19265  10578  -5720  -2198  -2368       C  
ATOM   5061  C   LEU D  50      58.297  26.309 -48.515  1.00102.78           C  
ANISOU 5061  C   LEU D  50     9552  19027  10471  -5158  -2166  -2187       C  
ATOM   5062  O   LEU D  50      57.228  26.175 -49.161  1.00 98.90           O  
ANISOU 5062  O   LEU D  50     9346  18125  10109  -4933  -1985  -2118       O  
ATOM   5063  CB  LEU D  50      59.437  28.446 -49.231  1.00107.05           C  
ANISOU 5063  CB  LEU D  50    10112  19625  10938  -6085  -2066  -2417       C  
ATOM   5064  CG  LEU D  50      59.064  29.914 -49.462  1.00107.77           C  
ANISOU 5064  CG  LEU D  50    10641  19325  10981  -6527  -1931  -2545       C  
ATOM   5065  CD1 LEU D  50      57.607  30.097 -49.905  1.00103.30           C  
ANISOU 5065  CD1 LEU D  50    10568  18168  10514  -6293  -1737  -2495       C  
ATOM   5066  CD2 LEU D  50      59.358  30.748 -48.231  1.00111.50           C  
ANISOU 5066  CD2 LEU D  50    11269  19866  11231  -6899  -2097  -2708       C  
ATOM   5067  N   TRP D  51      59.097  25.290 -48.180  1.00105.03           N  
ANISOU 5067  N   TRP D  51     9406  19759  10741  -4933  -2335  -2113       N  
ATOM   5068  CA  TRP D  51      58.768  23.871 -48.497  1.00102.80           C  
ANISOU 5068  CA  TRP D  51     8977  19492  10589  -4387  -2320  -1942       C  
ATOM   5069  C   TRP D  51      57.587  23.420 -47.626  1.00100.09           C  
ANISOU 5069  C   TRP D  51     8992  18845  10191  -4092  -2356  -1883       C  
ATOM   5070  O   TRP D  51      56.620  22.890 -48.165  1.00 95.06           O  
ANISOU 5070  O   TRP D  51     8550  17884   9684  -3787  -2211  -1786       O  
ATOM   5071  CB  TRP D  51      60.001  22.962 -48.349  1.00105.63           C  
ANISOU 5071  CB  TRP D  51     8788  20413  10935  -4227  -2496  -1884       C  
ATOM   5072  CG  TRP D  51      60.990  23.134 -49.463  1.00107.57           C  
ANISOU 5072  CG  TRP D  51     8660  20931  11282  -4399  -2404  -1907       C  
ATOM   5073  CD1 TRP D  51      62.136  23.878 -49.444  1.00111.17           C  
ANISOU 5073  CD1 TRP D  51     8824  21764  11651  -4828  -2475  -2021       C  
ATOM   5074  CD2 TRP D  51      60.891  22.600 -50.799  1.00105.52           C  
ANISOU 5074  CD2 TRP D  51     8292  20580  11219  -4174  -2207  -1822       C  
ATOM   5075  CE2 TRP D  51      62.030  23.040 -51.505  1.00108.07           C  
ANISOU 5075  CE2 TRP D  51     8245  21256  11561  -4472  -2167  -1886       C  
ATOM   5076  CE3 TRP D  51      59.987  21.748 -51.449  1.00102.14           C  
ANISOU 5076  CE3 TRP D  51     8028  19838  10945  -3751  -2067  -1699       C  
ATOM   5077  NE1 TRP D  51      62.758  23.833 -50.661  1.00111.44           N  
ANISOU 5077  NE1 TRP D  51     8567  21959  11815  -4880  -2330  -2007       N  
ATOM   5078  CZ2 TRP D  51      62.274  22.672 -52.827  1.00107.41           C  
ANISOU 5078  CZ2 TRP D  51     7963  21211  11638  -4351  -1986  -1833       C  
ATOM   5079  CZ3 TRP D  51      60.220  21.403 -52.763  1.00101.23           C  
ANISOU 5079  CZ3 TRP D  51     7729  19745  10987  -3641  -1895  -1653       C  
ATOM   5080  CH2 TRP D  51      61.359  21.845 -53.437  1.00103.70           C  
ANISOU 5080  CH2 TRP D  51     7679  20412  11311  -3926  -1854  -1719       C  
ATOM   5081  N   LYS D  52      57.652  23.665 -46.319  1.00102.49           N  
ANISOU 5081  N   LYS D  52     9387  19258  10297  -4205  -2539  -1946       N  
ATOM   5082  CA  LYS D  52      56.500  23.425 -45.422  1.00100.73           C  
ANISOU 5082  CA  LYS D  52     9541  18740   9991  -3993  -2558  -1912       C  
ATOM   5083  C   LYS D  52      55.290  24.152 -46.010  1.00 97.78           C  
ANISOU 5083  C   LYS D  52     9612  17835   9704  -4053  -2320  -1951       C  
ATOM   5084  O   LYS D  52      54.239  23.519 -46.139  1.00 95.19           O  
ANISOU 5084  O   LYS D  52     9483  17228   9456  -3718  -2224  -1848       O  
ATOM   5085  CB  LYS D  52      56.833  23.905 -44.012  1.00104.40           C  
ANISOU 5085  CB  LYS D  52    10065  19395  10205  -4221  -2769  -2017       C  
ATOM   5086  CG  LYS D  52      55.722  23.766 -42.978  1.00103.82           C  
ANISOU 5086  CG  LYS D  52    10380  19059  10009  -4053  -2792  -2003       C  
ATOM   5087  CD  LYS D  52      56.140  24.312 -41.610  1.00107.56           C  
ANISOU 5087  CD  LYS D  52    10908  19745  10214  -4315  -3002  -2124       C  
ATOM   5088  CE  LYS D  52      55.268  23.839 -40.461  1.00106.62           C  
ANISOU 5088  CE  LYS D  52    11061  19502   9946  -4078  -3072  -2074       C  
ATOM   5089  NZ  LYS D  52      54.007  24.621 -40.340  1.00104.72           N1+
ANISOU 5089  NZ  LYS D  52    11321  18784   9684  -4151  -2891  -2160       N1+
ATOM   5090  N   LYS D  53      55.448  25.423 -46.384  1.00 98.71           N  
ANISOU 5090  N   LYS D  53     9875  17823   9806  -4465  -2230  -2089       N  
ATOM   5091  CA  LYS D  53      54.335  26.277 -46.880  1.00 96.91           C  
ANISOU 5091  CA  LYS D  53    10098  17087   9638  -4545  -2017  -2139       C  
ATOM   5092  C   LYS D  53      53.744  25.674 -48.155  1.00 95.10           C  
ANISOU 5092  C   LYS D  53     9857  16646   9630  -4251  -1826  -2009       C  
ATOM   5093  O   LYS D  53      52.507  25.722 -48.327  1.00 93.57           O  
ANISOU 5093  O   LYS D  53    10002  16060   9491  -4072  -1689  -1976       O  
ATOM   5094  CB  LYS D  53      54.792  27.708 -47.163  1.00 98.24           C  
ANISOU 5094  CB  LYS D  53    10397  17178   9754  -5049  -1961  -2298       C  
ATOM   5095  CG  LYS D  53      54.874  28.634 -45.958  1.00100.76           C  
ANISOU 5095  CG  LYS D  53    10949  17486   9847  -5371  -2082  -2462       C  
ATOM   5096  CD  LYS D  53      54.675  30.112 -46.314  1.00101.20           C  
ANISOU 5096  CD  LYS D  53    11368  17208   9876  -5777  -1947  -2609       C  
ATOM   5097  CE  LYS D  53      55.283  31.073 -45.315  1.00104.16           C  
ANISOU 5097  CE  LYS D  53    11847  17701  10027  -6218  -2090  -2794       C  
ATOM   5098  NZ  LYS D  53      55.110  30.591 -43.927  1.00104.38           N1+
ANISOU 5098  NZ  LYS D  53    11895  17885   9880  -6065  -2274  -2811       N1+
ATOM   5099  N   LEU D  54      54.592  25.144 -49.030  1.00 96.09           N  
ANISOU 5099  N   LEU D  54     9604  17032   9873  -4205  -1814  -1943       N  
ATOM   5100  CA  LEU D  54      54.132  24.577 -50.323  1.00 93.63           C  
ANISOU 5100  CA  LEU D  54     9264  16545   9764  -3949  -1631  -1831       C  
ATOM   5101  C   LEU D  54      53.308  23.330 -50.012  1.00 90.72           C  
ANISOU 5101  C   LEU D  54     8942  16085   9442  -3477  -1652  -1696       C  
ATOM   5102  O   LEU D  54      52.183  23.204 -50.508  1.00 87.74           O  
ANISOU 5102  O   LEU D  54     8826  15352   9158  -3290  -1501  -1641       O  
ATOM   5103  CB  LEU D  54      55.352  24.243 -51.184  1.00 96.08           C  
ANISOU 5103  CB  LEU D  54     9127  17218  10159  -4007  -1632  -1805       C  
ATOM   5104  CG  LEU D  54      55.146  23.242 -52.329  1.00 93.92           C  
ANISOU 5104  CG  LEU D  54     8707  16905  10073  -3657  -1504  -1674       C  
ATOM   5105  CD1 LEU D  54      54.101  23.719 -53.329  1.00 90.53           C  
ANISOU 5105  CD1 LEU D  54     8614  16029   9755  -3653  -1278  -1658       C  
ATOM   5106  CD2 LEU D  54      56.466  22.981 -53.038  1.00 96.65           C  
ANISOU 5106  CD2 LEU D  54     8588  17663  10472  -3735  -1516  -1671       C  
ATOM   5107  N   ILE D  55      53.888  22.439 -49.221  1.00 91.43           N  
ANISOU 5107  N   ILE D  55     8778  16501   9461  -3300  -1839  -1642       N  
ATOM   5108  CA  ILE D  55      53.237  21.172 -48.801  1.00 88.44           C  
ANISOU 5108  CA  ILE D  55     8432  16070   9103  -2864  -1884  -1504       C  
ATOM   5109  C   ILE D  55      51.886  21.512 -48.178  1.00 86.85           C  
ANISOU 5109  C   ILE D  55     8672  15493   8835  -2825  -1822  -1521       C  
ATOM   5110  O   ILE D  55      50.934  20.839 -48.508  1.00 83.64           O  
ANISOU 5110  O   ILE D  55     8408  14850   8522  -2538  -1721  -1422       O  
ATOM   5111  CB  ILE D  55      54.159  20.382 -47.864  1.00 90.33           C  
ANISOU 5111  CB  ILE D  55     8365  16727   9231  -2740  -2123  -1459       C  
ATOM   5112  CG1 ILE D  55      55.388  19.883 -48.629  1.00 91.85           C  
ANISOU 5112  CG1 ILE D  55     8098  17284   9516  -2692  -2156  -1426       C  
ATOM   5113  CG2 ILE D  55      53.399  19.244 -47.227  1.00 88.42           C  
ANISOU 5113  CG2 ILE D  55     8247  16382   8967  -2347  -2177  -1325       C  
ATOM   5114  CD1 ILE D  55      56.376  19.116 -47.803  1.00 94.32           C  
ANISOU 5114  CD1 ILE D  55     8072  18038   9726  -2548  -2395  -1377       C  
ATOM   5115  N   GLU D  56      51.794  22.539 -47.340  1.00 89.55           N  
ANISOU 5115  N   GLU D  56     9225  15781   9020  -3111  -1873  -1649       N  
ATOM   5116  CA  GLU D  56      50.489  22.970 -46.780  1.00 89.59           C  
ANISOU 5116  CA  GLU D  56     9657  15426   8957  -3078  -1792  -1683       C  
ATOM   5117  C   GLU D  56      49.566  23.359 -47.933  1.00 88.56           C  
ANISOU 5117  C   GLU D  56     9745  14918   8987  -3039  -1558  -1672       C  
ATOM   5118  O   GLU D  56      48.411  22.915 -47.920  1.00 88.66           O  
ANISOU 5118  O   GLU D  56     9962  14684   9040  -2785  -1468  -1601       O  
ATOM   5119  CB  GLU D  56      50.648  24.125 -45.799  1.00 92.33           C  
ANISOU 5119  CB  GLU D  56    10198  15775   9107  -3420  -1871  -1847       C  
ATOM   5120  CG  GLU D  56      51.148  23.674 -44.450  1.00 95.49           C  
ANISOU 5120  CG  GLU D  56    10486  16480   9315  -3396  -2098  -1847       C  
ATOM   5121  CD  GLU D  56      51.738  24.798 -43.617  1.00 99.31           C  
ANISOU 5121  CD  GLU D  56    11051  17080   9601  -3800  -2211  -2025       C  
ATOM   5122  OE1 GLU D  56      52.002  25.872 -44.188  1.00100.46           O  
ANISOU 5122  OE1 GLU D  56    11275  17118   9778  -4122  -2125  -2143       O  
ATOM   5123  OE2 GLU D  56      51.902  24.602 -42.392  1.00101.13           O1-
ANISOU 5123  OE2 GLU D  56    11289  17495   9639  -3799  -2384  -2046       O1-
ATOM   5124  N   ARG D  57      50.049  24.141 -48.897  1.00 89.01           N  
ANISOU 5124  N   ARG D  57     9755  14941   9124  -3282  -1465  -1733       N  
ATOM   5125  CA  ARG D  57      49.209  24.591 -50.037  1.00 87.67           C  
ANISOU 5125  CA  ARG D  57     9803  14415   9094  -3258  -1249  -1719       C  
ATOM   5126  C   ARG D  57      48.800  23.375 -50.879  1.00 83.47           C  
ANISOU 5126  C   ARG D  57     9133  13855   8726  -2894  -1173  -1566       C  
ATOM   5127  O   ARG D  57      47.686  23.368 -51.416  1.00 79.56           O  
ANISOU 5127  O   ARG D  57     8863  13051   8313  -2740  -1028  -1523       O  
ATOM   5128  CB  ARG D  57      49.932  25.638 -50.881  1.00 91.70           C  
ANISOU 5128  CB  ARG D  57    10281  14923   9639  -3612  -1176  -1805       C  
ATOM   5129  CG  ARG D  57      49.017  26.318 -51.897  1.00 90.83           C  
ANISOU 5129  CG  ARG D  57    10467  14414   9630  -3621   -969  -1803       C  
ATOM   5130  CD  ARG D  57      49.723  27.177 -52.936  1.00 93.28           C  
ANISOU 5130  CD  ARG D  57    10733  14716   9993  -3935   -876  -1849       C  
ATOM   5131  NE  ARG D  57      50.880  26.513 -53.546  1.00 94.97           N  
ANISOU 5131  NE  ARG D  57    10514  15294  10278  -3951   -917  -1797       N  
ATOM   5132  CZ  ARG D  57      51.238  26.559 -54.831  1.00 94.69           C  
ANISOU 5132  CZ  ARG D  57    10352  15269  10357  -4007   -793  -1755       C  
ATOM   5133  NH1 ARG D  57      50.540  27.252 -55.718  1.00 93.76           N1+
ANISOU 5133  NH1 ARG D  57    10515  14808  10300  -4062   -623  -1749       N1+
ATOM   5134  NH2 ARG D  57      52.313  25.895 -55.226  1.00 95.93           N  
ANISOU 5134  NH2 ARG D  57    10094  15796  10559  -3996   -840  -1718       N  
ATOM   5135  N   MET D  58      49.663  22.375 -51.007  1.00 83.83           N  
ANISOU 5135  N   MET D  58     8823  14214   8815  -2754  -1267  -1488       N  
ATOM   5136  CA  MET D  58      49.327  21.115 -51.718  1.00 82.52           C  
ANISOU 5136  CA  MET D  58     8536  14027   8791  -2393  -1209  -1348       C  
ATOM   5137  C   MET D  58      48.195  20.426 -50.962  1.00 80.71           C  
ANISOU 5137  C   MET D  58     8520  13624   8522  -2123  -1224  -1275       C  
ATOM   5138  O   MET D  58      47.233  20.007 -51.604  1.00 78.01           O  
ANISOU 5138  O   MET D  58     8312  13043   8285  -1925  -1094  -1204       O  
ATOM   5139  CB  MET D  58      50.539  20.179 -51.841  1.00 84.76           C  
ANISOU 5139  CB  MET D  58     8405  14694   9106  -2278  -1325  -1289       C  
ATOM   5140  CG  MET D  58      51.533  20.649 -52.864  1.00 86.88           C  
ANISOU 5140  CG  MET D  58     8433  15131   9448  -2488  -1264  -1337       C  
ATOM   5141  SD  MET D  58      50.651  21.042 -54.404  1.00 85.80           S  
ANISOU 5141  SD  MET D  58     8509  14622   9468  -2484  -1006  -1318       S  
ATOM   5142  CE  MET D  58      50.408  22.817 -54.299  1.00 86.45           C  
ANISOU 5142  CE  MET D  58     8901  14481   9466  -2915   -938  -1456       C  
ATOM   5143  N   VAL D  59      48.293  20.348 -49.643  1.00 83.47           N  
ANISOU 5143  N   VAL D  59     8903  14097   8713  -2134  -1374  -1294       N  
ATOM   5144  CA  VAL D  59      47.292  19.628 -48.809  1.00 83.94           C  
ANISOU 5144  CA  VAL D  59     9150  14033   8711  -1889  -1397  -1216       C  
ATOM   5145  C   VAL D  59      45.956  20.363 -48.927  1.00 83.17           C  
ANISOU 5145  C   VAL D  59     9411  13571   8619  -1924  -1236  -1264       C  
ATOM   5146  O   VAL D  59      44.926  19.687 -49.072  1.00 81.08           O  
ANISOU 5146  O   VAL D  59     9268  13128   8410  -1686  -1153  -1174       O  
ATOM   5147  CB  VAL D  59      47.771  19.485 -47.353  1.00 86.20           C  
ANISOU 5147  CB  VAL D  59     9398  14554   8801  -1925  -1598  -1234       C  
ATOM   5148  CG1 VAL D  59      46.640  19.155 -46.394  1.00 84.92           C  
ANISOU 5148  CG1 VAL D  59     9506  14228   8533  -1774  -1595  -1192       C  
ATOM   5149  CG2 VAL D  59      48.900  18.470 -47.247  1.00 88.00           C  
ANISOU 5149  CG2 VAL D  59     9271  15130   9034  -1779  -1759  -1146       C  
ATOM   5150  N   ARG D  60      45.981  21.696 -48.909  1.00 86.13           N  
ANISOU 5150  N   ARG D  60     9945  13840   8940  -2208  -1191  -1399       N  
ATOM   5151  CA  ARG D  60      44.743  22.523 -48.889  1.00 86.50           C  
ANISOU 5151  CA  ARG D  60    10350  13547   8968  -2236  -1050  -1460       C  
ATOM   5152  C   ARG D  60      44.057  22.413 -50.259  1.00 82.38           C  
ANISOU 5152  C   ARG D  60     9872  12800   8629  -2107   -873  -1396       C  
ATOM   5153  O   ARG D  60      42.838  22.620 -50.303  1.00 79.34           O  
ANISOU 5153  O   ARG D  60     9732  12160   8255  -1998   -759  -1392       O  
ATOM   5154  CB  ARG D  60      45.010  23.977 -48.464  1.00 90.86           C  
ANISOU 5154  CB  ARG D  60    11089  14031   9402  -2569  -1057  -1627       C  
ATOM   5155  CG  ARG D  60      45.272  24.951 -49.613  1.00 93.94           C  
ANISOU 5155  CG  ARG D  60    11526  14276   9892  -2781   -940  -1687       C  
ATOM   5156  CD  ARG D  60      45.349  26.421 -49.259  1.00 97.58           C  
ANISOU 5156  CD  ARG D  60    12248  14587  10242  -3099   -921  -1848       C  
ATOM   5157  NE  ARG D  60      46.293  26.725 -48.185  1.00102.62           N  
ANISOU 5157  NE  ARG D  60    12808  15471  10711  -3338  -1091  -1948       N  
ATOM   5158  CZ  ARG D  60      46.689  27.948 -47.827  1.00104.76           C  
ANISOU 5158  CZ  ARG D  60    13254  15681  10868  -3679  -1111  -2102       C  
ATOM   5159  NH1 ARG D  60      46.247  29.024 -48.457  1.00105.18           N1+
ANISOU 5159  NH1 ARG D  60    13589  15415  10958  -3818   -967  -2171       N1+
ATOM   5160  NH2 ARG D  60      47.537  28.093 -46.825  1.00107.21           N  
ANISOU 5160  NH2 ARG D  60    13469  16250  11018  -3883  -1282  -2187       N  
ATOM   5161  N   THR D  61      44.789  22.099 -51.332  1.00 80.85           N  
ANISOU 5161  N   THR D  61     9445  12710   8564  -2114   -850  -1350       N  
ATOM   5162  CA  THR D  61      44.225  22.087 -52.710  1.00 78.24           C  
ANISOU 5162  CA  THR D  61     9158  12177   8392  -2025   -685  -1298       C  
ATOM   5163  C   THR D  61      44.022  20.634 -53.169  1.00 76.56           C  
ANISOU 5163  C   THR D  61     8778  12026   8286  -1720   -679  -1161       C  
ATOM   5164  O   THR D  61      42.874  20.297 -53.498  1.00 77.38           O  
ANISOU 5164  O   THR D  61     9033  11921   8445  -1539   -579  -1103       O  
ATOM   5165  CB  THR D  61      45.042  22.989 -53.647  1.00 79.00           C  
ANISOU 5165  CB  THR D  61     9188  12288   8538  -2288   -630  -1362       C  
ATOM   5166  CG2 THR D  61      45.275  24.370 -53.072  1.00 80.62           C  
ANISOU 5166  CG2 THR D  61     9586  12424   8623  -2606   -649  -1501       C  
ATOM   5167  OG1 THR D  61      46.306  22.393 -53.920  1.00 80.05           O  
ANISOU 5167  OG1 THR D  61     8972  12736   8706  -2317   -713  -1333       O  
ATOM   5168  N   ASP D  62      45.054  19.788 -53.140  1.00 75.83           N  
ANISOU 5168  N   ASP D  62     8393  12208   8212  -1655   -786  -1112       N  
ATOM   5169  CA  ASP D  62      44.995  18.398 -53.675  1.00 71.73           C  
ANISOU 5169  CA  ASP D  62     7719  11737   7798  -1365   -777   -988       C  
ATOM   5170  C   ASP D  62      44.589  17.439 -52.557  1.00 70.53           C  
ANISOU 5170  C   ASP D  62     7609  11626   7565  -1160   -881   -912       C  
ATOM   5171  O   ASP D  62      45.341  17.236 -51.597  1.00 73.33           O  
ANISOU 5171  O   ASP D  62     7844  12205   7813  -1182  -1037   -917       O  
ATOM   5172  CB  ASP D  62      46.335  17.983 -54.284  1.00 72.18           C  
ANISOU 5172  CB  ASP D  62     7442  12066   7917  -1374   -826   -976       C  
ATOM   5173  CG  ASP D  62      46.252  16.804 -55.238  1.00 69.77           C  
ANISOU 5173  CG  ASP D  62     7017  11747   7746  -1108   -763   -876       C  
ATOM   5174  OD1 ASP D  62      45.248  16.052 -55.164  1.00 65.67           O  
ANISOU 5174  OD1 ASP D  62     6649  11051   7253   -895   -727   -799       O  
ATOM   5175  OD2 ASP D  62      47.194  16.626 -56.037  1.00 70.22           O1-
ANISOU 5175  OD2 ASP D  62     6831  11977   7873  -1120   -748   -880       O1-
ATOM   5176  N   PRO D  63      43.413  16.787 -52.659  1.00 66.94           N  
ANISOU 5176  N   PRO D  63     7316  10969   7150   -960   -802   -834       N  
ATOM   5177  CA  PRO D  63      42.984  15.808 -51.661  1.00 67.23           C  
ANISOU 5177  CA  PRO D  63     7408  11028   7108   -773   -885   -747       C  
ATOM   5178  C   PRO D  63      43.917  14.593 -51.558  1.00 67.83           C  
ANISOU 5178  C   PRO D  63     7250  11321   7202   -591  -1008   -654       C  
ATOM   5179  O   PRO D  63      43.932  13.934 -50.531  1.00 68.70           O  
ANISOU 5179  O   PRO D  63     7380  11514   7210   -481  -1123   -590       O  
ATOM   5180  CB  PRO D  63      41.609  15.357 -52.178  1.00 65.67           C  
ANISOU 5180  CB  PRO D  63     7391  10575   6986   -623   -745   -684       C  
ATOM   5181  CG  PRO D  63      41.159  16.465 -53.117  1.00 64.14           C  
ANISOU 5181  CG  PRO D  63     7298  10209   6862   -766   -603   -766       C  
ATOM   5182  CD  PRO D  63      42.443  16.930 -53.752  1.00 65.22           C  
ANISOU 5182  CD  PRO D  63     7231  10503   7047   -912   -632   -821       C  
ATOM   5183  N   LEU D  64      44.638  14.302 -52.640  1.00 67.76           N  
ANISOU 5183  N   LEU D  64     7037  11390   7319   -547   -974   -645       N  
ATOM   5184  CA  LEU D  64      45.743  13.306 -52.672  1.00 68.62           C  
ANISOU 5184  CA  LEU D  64     6881  11738   7452   -377  -1087   -581       C  
ATOM   5185  C   LEU D  64      46.736  13.641 -51.556  1.00 71.72           C  
ANISOU 5185  C   LEU D  64     7133  12413   7703   -486  -1270   -619       C  
ATOM   5186  O   LEU D  64      47.041  12.746 -50.728  1.00 71.85           O  
ANISOU 5186  O   LEU D  64     7094  12561   7645   -306  -1410   -534       O  
ATOM   5187  CB  LEU D  64      46.403  13.374 -54.049  1.00 67.53           C  
ANISOU 5187  CB  LEU D  64     6548  11659   7453   -393   -996   -612       C  
ATOM   5188  CG  LEU D  64      47.738  12.658 -54.238  1.00 69.41           C  
ANISOU 5188  CG  LEU D  64     6461  12191   7720   -261  -1093   -584       C  
ATOM   5189  CD1 LEU D  64      47.710  11.244 -53.683  1.00 70.09           C  
ANISOU 5189  CD1 LEU D  64     6545  12298   7790     58  -1192   -460       C  
ATOM   5190  CD2 LEU D  64      48.117  12.643 -55.711  1.00 68.53           C  
ANISOU 5190  CD2 LEU D  64     6205  12086   7749   -253   -958   -610       C  
ATOM   5191  N   TRP D  65      47.218  14.886 -51.555  1.00 74.69           N  
ANISOU 5191  N   TRP D  65     7465  12876   8038   -778  -1270   -741       N  
ATOM   5192  CA  TRP D  65      48.244  15.356 -50.590  1.00 80.41           C  
ANISOU 5192  CA  TRP D  65     8036  13895   8623   -942  -1444   -802       C  
ATOM   5193  C   TRP D  65      47.639  15.308 -49.193  1.00 82.27           C  
ANISOU 5193  C   TRP D  65     8480  14087   8693   -924  -1542   -783       C  
ATOM   5194  O   TRP D  65      48.307  14.773 -48.274  1.00 84.29           O  
ANISOU 5194  O   TRP D  65     8606  14582   8837   -841  -1722   -738       O  
ATOM   5195  CB  TRP D  65      48.796  16.742 -50.953  1.00 81.89           C  
ANISOU 5195  CB  TRP D  65     8172  14143   8800  -1295  -1404   -943       C  
ATOM   5196  CG  TRP D  65      49.779  16.673 -52.084  1.00 82.67           C  
ANISOU 5196  CG  TRP D  65     7976  14416   9017  -1322  -1360   -955       C  
ATOM   5197  CD1 TRP D  65      49.466  16.439 -53.390  1.00 81.33           C  
ANISOU 5197  CD1 TRP D  65     7806  14092   9002  -1232  -1195   -925       C  
ATOM   5198  CD2 TRP D  65      51.214  16.805 -52.036  1.00 84.99           C  
ANISOU 5198  CD2 TRP D  65     7923  15090   9279  -1443  -1474  -1000       C  
ATOM   5199  CE2 TRP D  65      51.686  16.637 -53.353  1.00 85.07           C  
ANISOU 5199  CE2 TRP D  65     7740  15153   9431  -1412  -1356   -994       C  
ATOM   5200  CE3 TRP D  65      52.150  17.048 -51.031  1.00 88.46           C  
ANISOU 5200  CE3 TRP D  65     8184  15850   9576  -1578  -1665  -1046       C  
ATOM   5201  NE1 TRP D  65      50.601  16.407 -54.151  1.00 83.43           N  
ANISOU 5201  NE1 TRP D  65     7760  14608   9331  -1282  -1190   -948       N  
ATOM   5202  CZ2 TRP D  65      53.037  16.665 -53.686  1.00 87.17           C  
ANISOU 5202  CZ2 TRP D  65     7631  15784   9706  -1497  -1412  -1030       C  
ATOM   5203  CZ3 TRP D  65      53.490  17.109 -51.364  1.00 91.44           C  
ANISOU 5203  CZ3 TRP D  65     8185  16595   9965  -1675  -1732  -1083       C  
ATOM   5204  CH2 TRP D  65      53.925  16.932 -52.679  1.00 90.48           C  
ANISOU 5204  CH2 TRP D  65     7865  16522   9990  -1638  -1600  -1076       C  
ATOM   5205  N   LYS D  66      46.403  15.796 -49.071  1.00 81.66           N  
ANISOU 5205  N   LYS D  66     8709  13722   8598   -978  -1424   -810       N  
ATOM   5206  CA  LYS D  66      45.590  15.692 -47.833  1.00 82.80           C  
ANISOU 5206  CA  LYS D  66     9086  13785   8589   -938  -1473   -787       C  
ATOM   5207  C   LYS D  66      45.604  14.235 -47.351  1.00 80.61           C  
ANISOU 5207  C   LYS D  66     8756  13583   8288   -645  -1571   -631       C  
ATOM   5208  O   LYS D  66      46.088  13.982 -46.232  1.00 81.78           O  
ANISOU 5208  O   LYS D  66     8865  13926   8280   -627  -1740   -604       O  
ATOM   5209  CB  LYS D  66      44.180  16.198 -48.133  1.00 83.71           C  
ANISOU 5209  CB  LYS D  66     9492  13571   8741   -964  -1291   -816       C  
ATOM   5210  CG  LYS D  66      43.289  16.484 -46.940  1.00 85.47           C  
ANISOU 5210  CG  LYS D  66     9972  13703   8799   -993  -1299   -839       C  
ATOM   5211  CD  LYS D  66      42.181  17.476 -47.333  1.00 85.80           C  
ANISOU 5211  CD  LYS D  66    10258  13469   8873  -1094  -1121   -927       C  
ATOM   5212  CE  LYS D  66      40.883  17.309 -46.569  1.00 86.12           C  
ANISOU 5212  CE  LYS D  66    10543  13359   8818   -999  -1056   -901       C  
ATOM   5213  NZ  LYS D  66      41.139  17.109 -45.123  1.00 88.05           N1+
ANISOU 5213  NZ  LYS D  66    10827  13770   8857  -1016  -1201   -896       N1+
ATOM   5214  N   GLY D  67      45.146  13.314 -48.203  1.00 75.80           N  
ANISOU 5214  N   GLY D  67     8152  12827   7823   -428  -1473   -532       N  
ATOM   5215  CA  GLY D  67      45.063  11.878 -47.890  1.00 73.82           C  
ANISOU 5215  CA  GLY D  67     7897  12584   7566   -141  -1541   -377       C  
ATOM   5216  C   GLY D  67      46.371  11.372 -47.330  1.00 75.33           C  
ANISOU 5216  C   GLY D  67     7846  13091   7684    -50  -1744   -334       C  
ATOM   5217  O   GLY D  67      46.419  11.023 -46.133  1.00 75.63           O  
ANISOU 5217  O   GLY D  67     7948  13229   7560      4  -1885   -274       O  
ATOM   5218  N   LEU D  68      47.412  11.392 -48.153  1.00 76.51           N  
ANISOU 5218  N   LEU D  68     7718  13414   7940    -43  -1761   -367       N  
ATOM   5219  CA  LEU D  68      48.764  10.922 -47.778  1.00 80.75           C  
ANISOU 5219  CA  LEU D  68     7962  14295   8426     63  -1951   -333       C  
ATOM   5220  C   LEU D  68      49.235  11.561 -46.461  1.00 83.63           C  
ANISOU 5220  C   LEU D  68     8306  14888   8583   -115  -2129   -385       C  
ATOM   5221  O   LEU D  68      49.887  10.848 -45.647  1.00 84.74           O  
ANISOU 5221  O   LEU D  68     8332  15250   8615     50  -2318   -298       O  
ATOM   5222  CB  LEU D  68      49.710  11.260 -48.927  1.00 82.03           C  
ANISOU 5222  CB  LEU D  68     7830  14613   8723     -2  -1899   -408       C  
ATOM   5223  CG  LEU D  68      49.764  10.231 -50.051  1.00 82.25           C  
ANISOU 5223  CG  LEU D  68     7773  14556   8922    271  -1804   -332       C  
ATOM   5224  CD1 LEU D  68      50.803  10.657 -51.078  1.00 84.50           C  
ANISOU 5224  CD1 LEU D  68     7744  15052   9310    181  -1759   -417       C  
ATOM   5225  CD2 LEU D  68      50.088   8.838 -49.512  1.00 84.23           C  
ANISOU 5225  CD2 LEU D  68     7981  14887   9136    623  -1942   -186       C  
ATOM   5226  N   SER D  69      48.952  12.853 -46.253  1.00 83.70           N  
ANISOU 5226  N   SER D  69     8426  14848   8530   -432  -2078   -523       N  
ATOM   5227  CA  SER D  69      49.398  13.585 -45.038  1.00 86.17           C  
ANISOU 5227  CA  SER D  69     8738  15369   8635   -644  -2239   -601       C  
ATOM   5228  C   SER D  69      48.876  12.843 -43.805  1.00 86.56           C  
ANISOU 5228  C   SER D  69     8974  15395   8519   -476  -2347   -489       C  
ATOM   5229  O   SER D  69      49.642  12.705 -42.826  1.00 89.67           O  
ANISOU 5229  O   SER D  69     9251  16071   8749   -474  -2555   -470       O  
ATOM   5230  CB  SER D  69      48.982  15.047 -45.058  1.00 85.40           C  
ANISOU 5230  CB  SER D  69     8806  15140   8502   -992  -2137   -767       C  
ATOM   5231  OG  SER D  69      47.638  15.231 -44.636  1.00 83.05           O  
ANISOU 5231  OG  SER D  69     8858  14546   8152   -990  -2028   -765       O  
ATOM   5232  N   GLU D  70      47.639  12.348 -43.897  1.00 83.87           N  
ANISOU 5232  N   GLU D  70     8900  14747   8220   -341  -2211   -411       N  
ATOM   5233  CA  GLU D  70      46.931  11.641 -42.805  1.00 84.77           C  
ANISOU 5233  CA  GLU D  70     9239  14787   8181   -200  -2270   -296       C  
ATOM   5234  C   GLU D  70      47.451  10.209 -42.699  1.00 88.24           C  
ANISOU 5234  C   GLU D  70     9563  15332   8631    124  -2394   -119       C  
ATOM   5235  O   GLU D  70      47.931   9.829 -41.615  1.00 92.51           O  
ANISOU 5235  O   GLU D  70    10082  16075   8994    195  -2586    -50       O  
ATOM   5236  CB  GLU D  70      45.428  11.657 -43.057  1.00 79.88           C  
ANISOU 5236  CB  GLU D  70     8919  13817   7613   -194  -2063   -284       C  
ATOM   5237  CG  GLU D  70      44.843  13.050 -42.971  1.00 78.07           C  
ANISOU 5237  CG  GLU D  70     8845  13476   7342   -475  -1953   -450       C  
ATOM   5238  CD  GLU D  70      43.519  13.217 -43.705  1.00 74.60           C  
ANISOU 5238  CD  GLU D  70     8609  12712   7025   -466  -1723   -462       C  
ATOM   5239  OE1 GLU D  70      43.099  12.282 -44.389  1.00 73.77           O  
ANISOU 5239  OE1 GLU D  70     8506  12473   7049   -272  -1645   -351       O  
ATOM   5240  OE2 GLU D  70      42.901  14.281 -43.594  1.00 72.97           O1-
ANISOU 5240  OE2 GLU D  70     8562  12385   6777   -649  -1624   -585       O1-
ATOM   5241  N   ARG D  71      47.364   9.440 -43.778  1.00 88.68           N  
ANISOU 5241  N   ARG D  71     9561  15253   8881    321  -2293    -48       N  
ATOM   5242  CA  ARG D  71      47.672   7.991 -43.720  1.00 91.00           C  
ANISOU 5242  CA  ARG D  71     9817  15568   9192    661  -2384    128       C  
ATOM   5243  C   ARG D  71      49.140   7.786 -43.336  1.00 93.83           C  
ANISOU 5243  C   ARG D  71     9864  16305   9481    757  -2609    147       C  
ATOM   5244  O   ARG D  71      49.416   6.809 -42.614  1.00 97.28           O  
ANISOU 5244  O   ARG D  71    10323  16824   9816    997  -2761    293       O  
ATOM   5245  CB  ARG D  71      47.256   7.336 -45.033  1.00 90.42           C  
ANISOU 5245  CB  ARG D  71     9760  15256   9340    820  -2213    168       C  
ATOM   5246  CG  ARG D  71      45.742   7.196 -45.120  1.00 89.91           C  
ANISOU 5246  CG  ARG D  71    10021  14844   9296    787  -2037    201       C  
ATOM   5247  CD  ARG D  71      45.159   7.660 -46.444  1.00 89.12           C  
ANISOU 5247  CD  ARG D  71     9934  14541   9387    691  -1825    111       C  
ATOM   5248  NE  ARG D  71      43.714   7.880 -46.411  1.00 87.12           N  
ANISOU 5248  NE  ARG D  71     9959  14017   9127    593  -1667    105       N  
ATOM   5249  CZ  ARG D  71      42.878   7.690 -47.435  1.00 83.64           C  
ANISOU 5249  CZ  ARG D  71     9609  13338   8834    615  -1491    105       C  
ATOM   5250  NH1 ARG D  71      43.325   7.222 -48.590  1.00 82.15           N1+
ANISOU 5250  NH1 ARG D  71     9280  13124   8810    737  -1443    111       N1+
ATOM   5251  NH2 ARG D  71      41.587   7.942 -47.282  1.00 81.24           N  
ANISOU 5251  NH2 ARG D  71     9531  12834   8501    522  -1365     96       N  
ATOM   5252  N   ARG D  72      50.032   8.678 -43.774  1.00 93.16           N  
ANISOU 5252  N   ARG D  72     9506  16450   9442    571  -2633      9       N  
ATOM   5253  CA  ARG D  72      51.484   8.618 -43.444  1.00 96.40           C  
ANISOU 5253  CA  ARG D  72     9566  17277   9783    623  -2847      4       C  
ATOM   5254  C   ARG D  72      51.749   9.314 -42.102  1.00 96.98           C  
ANISOU 5254  C   ARG D  72     9663  17572   9614    413  -3025    -48       C  
ATOM   5255  O   ARG D  72      52.773   9.020 -41.470  1.00 98.39           O  
ANISOU 5255  O   ARG D  72     9616  18093   9676    507  -3246     -5       O  
ATOM   5256  CB  ARG D  72      52.314   9.265 -44.559  1.00 97.53           C  
ANISOU 5256  CB  ARG D  72     9396  17582  10078    487  -2778   -124       C  
ATOM   5257  CG  ARG D  72      52.864   8.333 -45.635  1.00 97.77           C  
ANISOU 5257  CG  ARG D  72     9213  17645  10290    783  -2730    -57       C  
ATOM   5258  CD  ARG D  72      52.202   6.971 -45.684  1.00 96.70           C  
ANISOU 5258  CD  ARG D  72     9294  17246  10202   1142  -2697    112       C  
ATOM   5259  NE  ARG D  72      52.120   6.403 -47.009  1.00 94.91           N  
ANISOU 5259  NE  ARG D  72     9022  16857  10183   1315  -2533    124       N  
ATOM   5260  CZ  ARG D  72      51.551   5.241 -47.299  1.00 93.87           C  
ANISOU 5260  CZ  ARG D  72     9079  16464  10121   1605  -2472    249       C  
ATOM   5261  NH1 ARG D  72      50.985   4.512 -46.347  1.00 94.18           N1+
ANISOU 5261  NH1 ARG D  72     9375  16368  10040   1748  -2557    385       N1+
ATOM   5262  NH2 ARG D  72      51.541   4.816 -48.551  1.00 92.61           N  
ANISOU 5262  NH2 ARG D  72     8866  16176  10143   1735  -2322    236       N  
ATOM   5263  N   GLY D  73      50.871  10.239 -41.727  1.00 94.91           N  
ANISOU 5263  N   GLY D  73     9656  17130   9276    139  -2928   -146       N  
ATOM   5264  CA  GLY D  73      50.969  11.003 -40.471  1.00 96.28           C  
ANISOU 5264  CA  GLY D  73     9909  17466   9209    -92  -3067   -222       C  
ATOM   5265  C   GLY D  73      52.117  12.000 -40.495  1.00 98.33           C  
ANISOU 5265  C   GLY D  73     9874  18058   9428   -363  -3175   -377       C  
ATOM   5266  O   GLY D  73      52.733  12.205 -39.438  1.00101.51           O  
ANISOU 5266  O   GLY D  73    10200  18745   9622   -451  -3384   -396       O  
ATOM   5267  N   TRP D  74      52.410  12.617 -41.641  1.00 97.51           N  
ANISOU 5267  N   TRP D  74     9614  17933   9503   -513  -3042   -485       N  
ATOM   5268  CA  TRP D  74      53.295  13.814 -41.669  1.00 98.93           C  
ANISOU 5268  CA  TRP D  74     9587  18368   9635   -871  -3102   -660       C  
ATOM   5269  C   TRP D  74      52.437  15.083 -41.623  1.00 98.09           C  
ANISOU 5269  C   TRP D  74     9782  17992   9496  -1209  -2950   -814       C  
ATOM   5270  O   TRP D  74      53.020  16.178 -41.529  1.00 98.25           O  
ANISOU 5270  O   TRP D  74     9716  18163   9450  -1549  -2990   -970       O  
ATOM   5271  CB  TRP D  74      54.305  13.813 -42.829  1.00 98.39           C  
ANISOU 5271  CB  TRP D  74     9141  18500   9742   -871  -3070   -692       C  
ATOM   5272  CG  TRP D  74      53.832  13.376 -44.185  1.00 94.85           C  
ANISOU 5272  CG  TRP D  74     8716  17787   9538   -703  -2850   -645       C  
ATOM   5273  CD1 TRP D  74      54.090  12.176 -44.785  1.00 94.80           C  
ANISOU 5273  CD1 TRP D  74     8556  17805   9658   -339  -2843   -514       C  
ATOM   5274  CD2 TRP D  74      53.116  14.150 -45.163  1.00 91.30           C  
ANISOU 5274  CD2 TRP D  74     8434  17029   9228   -893  -2611   -737       C  
ATOM   5275  CE2 TRP D  74      52.942  13.333 -46.303  1.00 88.97           C  
ANISOU 5275  CE2 TRP D  74     8078  16594   9132   -634  -2475   -651       C  
ATOM   5276  CE3 TRP D  74      52.583  15.440 -45.182  1.00 89.98           C  
ANISOU 5276  CE3 TRP D  74     8481  16677   9029  -1241  -2501   -879       C  
ATOM   5277  NE1 TRP D  74      53.542  12.132 -46.041  1.00 91.45           N  
ANISOU 5277  NE1 TRP D  74     8203  17108   9435   -300  -2616   -521       N  
ATOM   5278  CZ2 TRP D  74      52.269  13.768 -47.442  1.00 85.21           C  
ANISOU 5278  CZ2 TRP D  74     7732  15827   8816   -723  -2244   -700       C  
ATOM   5279  CZ3 TRP D  74      51.914  15.869 -46.311  1.00 86.71           C  
ANISOU 5279  CZ3 TRP D  74     8201  15964   8780  -1310  -2272   -920       C  
ATOM   5280  CH2 TRP D  74      51.766  15.045 -47.424  1.00 84.15           C  
ANISOU 5280  CH2 TRP D  74     7798  15531   8645  -1058  -2150   -829       C  
ATOM   5281  N   ASP D  75      51.107  14.931 -41.623  1.00 96.70           N  
ANISOU 5281  N   ASP D  75     9952  17442   9349  -1117  -2791   -771       N  
ATOM   5282  CA  ASP D  75      50.146  16.027 -41.327  1.00 96.74           C  
ANISOU 5282  CA  ASP D  75    10288  17185   9284  -1372  -2662   -901       C  
ATOM   5283  C   ASP D  75      50.466  16.640 -39.962  1.00101.52           C  
ANISOU 5283  C   ASP D  75    10962  17987   9622  -1582  -2838   -991       C  
ATOM   5284  O   ASP D  75      50.219  17.842 -39.790  1.00102.33           O  
ANISOU 5284  O   ASP D  75    11235  17989   9658  -1885  -2775  -1156       O  
ATOM   5285  CB  ASP D  75      48.685  15.562 -41.360  1.00 93.70           C  
ANISOU 5285  CB  ASP D  75    10226  16434   8942  -1188  -2494   -817       C  
ATOM   5286  CG  ASP D  75      48.323  14.425 -40.418  1.00 94.20           C  
ANISOU 5286  CG  ASP D  75    10390  16522   8878   -925  -2596   -655       C  
ATOM   5287  OD1 ASP D  75      49.238  13.841 -39.816  1.00 96.92           O  
ANISOU 5287  OD1 ASP D  75    10543  17163   9119   -823  -2806   -582       O  
ATOM   5288  OD2 ASP D  75      47.118  14.124 -40.310  1.00 92.21           O1-
ANISOU 5288  OD2 ASP D  75    10406  15998   8630   -823  -2463   -598       O1-
ATOM   5289  N   GLN D  76      51.013  15.857 -39.031  1.00105.53           N  
ANISOU 5289  N   GLN D  76    11356  18765   9976  -1427  -3054   -888       N  
ATOM   5290  CA  GLN D  76      51.206  16.332 -37.637  1.00108.96           C  
ANISOU 5290  CA  GLN D  76    11891  19382  10127  -1603  -3228   -960       C  
ATOM   5291  C   GLN D  76      52.360  17.341 -37.596  1.00112.03           C  
ANISOU 5291  C   GLN D  76    12049  20068  10450  -1947  -3351  -1128       C  
ATOM   5292  O   GLN D  76      52.493  18.008 -36.553  1.00115.60           O  
ANISOU 5292  O   GLN D  76    12612  20641  10669  -2175  -3471  -1237       O  
ATOM   5293  CB  GLN D  76      51.377  15.143 -36.681  1.00111.33           C  
ANISOU 5293  CB  GLN D  76    12161  19865  10274  -1316  -3420   -780       C  
ATOM   5294  CG  GLN D  76      50.254  14.110 -36.799  1.00108.20           C  
ANISOU 5294  CG  GLN D  76    11995  19165   9952  -1002  -3286   -608       C  
ATOM   5295  CD  GLN D  76      49.748  13.572 -35.483  1.00107.99           C  
ANISOU 5295  CD  GLN D  76    12198  19151   9681   -891  -3388   -506       C  
ATOM   5296  NE2 GLN D  76      48.461  13.269 -35.460  1.00103.77           N  
ANISOU 5296  NE2 GLN D  76    11967  18292   9169   -793  -3209   -444       N  
ATOM   5297  OE1 GLN D  76      50.490  13.433 -34.508  1.00109.83           O  
ANISOU 5297  OE1 GLN D  76    12336  19693   9704   -900  -3623   -481       O  
ATOM   5298  N   TYR D  77      53.121  17.485 -38.694  1.00112.93           N  
ANISOU 5298  N   TYR D  77    11871  20286  10751  -2004  -3311  -1158       N  
ATOM   5299  CA  TYR D  77      54.302  18.397 -38.808  1.00117.11           C  
ANISOU 5299  CA  TYR D  77    12134  21124  11239  -2351  -3416  -1310       C  
ATOM   5300  C   TYR D  77      53.943  19.604 -39.683  1.00114.06           C  
ANISOU 5300  C   TYR D  77    11900  20464  10975  -2662  -3199  -1469       C  
ATOM   5301  O   TYR D  77      54.863  20.354 -40.070  1.00113.49           O  
ANISOU 5301  O   TYR D  77    11611  20591  10917  -2962  -3234  -1587       O  
ATOM   5302  CB  TYR D  77      55.538  17.589 -39.236  1.00120.51           C  
ANISOU 5302  CB  TYR D  77    12092  21946  11749  -2174  -3560  -1214       C  
ATOM   5303  CG  TYR D  77      55.512  16.259 -38.519  1.00123.91           C  
ANISOU 5303  CG  TYR D  77    12490  22494  12096  -1771  -3715  -1020       C  
ATOM   5304  CD1 TYR D  77      55.376  16.205 -37.134  1.00125.89           C  
ANISOU 5304  CD1 TYR D  77    12897  22849  12084  -1785  -3890  -1005       C  
ATOM   5305  CD2 TYR D  77      55.410  15.067 -39.218  1.00123.41           C  
ANISOU 5305  CD2 TYR D  77    12326  22355  12210  -1374  -3655   -848       C  
ATOM   5306  CE1 TYR D  77      55.227  15.004 -36.460  1.00125.99           C  
ANISOU 5306  CE1 TYR D  77    12945  22917  12009  -1421  -4016   -814       C  
ATOM   5307  CE2 TYR D  77      55.273  13.854 -38.559  1.00123.91           C  
ANISOU 5307  CE2 TYR D  77    12428  22458  12194  -1006  -3780   -662       C  
ATOM   5308  CZ  TYR D  77      55.177  13.823 -37.177  1.00125.42           C  
ANISOU 5308  CZ  TYR D  77    12769  22765  12121  -1030  -3961   -638       C  
ATOM   5309  OH  TYR D  77      55.035  12.637 -36.522  1.00126.04           O  
ANISOU 5309  OH  TYR D  77    12910  22870  12108   -676  -4083   -443       O  
ATOM   5310  N   LEU D  78      52.655  19.766 -39.994  1.00109.90           N  
ANISOU 5310  N   LEU D  78    11725  19504  10530  -2590  -2985  -1464       N  
ATOM   5311  CA  LEU D  78      52.129  20.892 -40.800  1.00108.24           C  
ANISOU 5311  CA  LEU D  78    11722  18976  10429  -2837  -2768  -1598       C  
ATOM   5312  C   LEU D  78      51.242  21.788 -39.928  1.00107.97           C  
ANISOU 5312  C   LEU D  78    12100  18700  10223  -3014  -2720  -1724       C  
ATOM   5313  O   LEU D  78      50.712  21.303 -38.904  1.00106.68           O  
ANISOU 5313  O   LEU D  78    12092  18535   9905  -2858  -2791  -1669       O  
ATOM   5314  CB  LEU D  78      51.333  20.313 -41.977  1.00104.49           C  
ANISOU 5314  CB  LEU D  78    11301  18204  10198  -2572  -2554  -1485       C  
ATOM   5315  CG  LEU D  78      52.127  19.460 -42.959  1.00103.78           C  
ANISOU 5315  CG  LEU D  78    10838  18308  10287  -2385  -2566  -1375       C  
ATOM   5316  CD1 LEU D  78      51.227  18.946 -44.066  1.00100.25           C  
ANISOU 5316  CD1 LEU D  78    10498  17537  10056  -2146  -2350  -1280       C  
ATOM   5317  CD2 LEU D  78      53.281  20.267 -43.519  1.00105.92           C  
ANISOU 5317  CD2 LEU D  78    10844  18813  10589  -2706  -2595  -1492       C  
ATOM   5318  N   PHE D  79      51.054  23.036 -40.367  1.00107.82           N  
ANISOU 5318  N   PHE D  79    12265  18467  10233  -3316  -2588  -1883       N  
ATOM   5319  CA  PHE D  79      50.193  24.060 -39.731  1.00107.22           C  
ANISOU 5319  CA  PHE D  79    12608  18111  10020  -3494  -2504  -2031       C  
ATOM   5320  C   PHE D  79      50.772  24.312 -38.336  1.00113.57           C  
ANISOU 5320  C   PHE D  79    13418  19190  10542  -3679  -2726  -2123       C  
ATOM   5321  O   PHE D  79      51.726  25.123 -38.262  1.00117.78           O  
ANISOU 5321  O   PHE D  79    13843  19908  11000  -4033  -2824  -2261       O  
ATOM   5322  CB  PHE D  79      48.735  23.597 -39.827  1.00101.67           C  
ANISOU 5322  CB  PHE D  79    12177  17066   9387  -3185  -2327  -1938       C  
ATOM   5323  CG  PHE D  79      48.302  23.243 -41.234  1.00 95.77           C  
ANISOU 5323  CG  PHE D  79    11370  16109   8910  -3006  -2141  -1839       C  
ATOM   5324  CD1 PHE D  79      48.596  22.013 -41.803  1.00 92.82           C  
ANISOU 5324  CD1 PHE D  79    10716  15873   8678  -2730  -2170  -1665       C  
ATOM   5325  CD2 PHE D  79      47.533  24.128 -41.983  1.00 92.55           C  
ANISOU 5325  CD2 PHE D  79    11212  15345   8606  -3093  -1932  -1919       C  
ATOM   5326  CE1 PHE D  79      48.185  21.698 -43.092  1.00 89.72           C  
ANISOU 5326  CE1 PHE D  79    10285  15288   8518  -2576  -1999  -1585       C  
ATOM   5327  CE2 PHE D  79      47.104  23.804 -43.264  1.00 89.84           C  
ANISOU 5327  CE2 PHE D  79    10823  14818   8494  -2929  -1769  -1826       C  
ATOM   5328  CZ  PHE D  79      47.424  22.586 -43.815  1.00 88.19           C  
ANISOU 5328  CZ  PHE D  79    10329  14762   8417  -2679  -1801  -1663       C  
ATOM   5329  N   LYS D  80      50.311  23.579 -37.308  1.00115.33           N  
ANISOU 5329  N   LYS D  80    13732  19476  10613  -3458  -2813  -2040       N  
ATOM   5330  CA  LYS D  80      50.937  23.565 -35.951  1.00117.32           C  
ANISOU 5330  CA  LYS D  80    13942  20051  10583  -3577  -3058  -2089       C  
ATOM   5331  C   LYS D  80      52.430  23.227 -36.063  1.00118.35           C  
ANISOU 5331  C   LYS D  80    13621  20635  10711  -3666  -3277  -2056       C  
ATOM   5332  O   LYS D  80      53.182  23.760 -35.237  1.00121.33           O  
ANISOU 5332  O   LYS D  80    13945  21278  10876  -3940  -3463  -2177       O  
ATOM   5333  CB  LYS D  80      50.258  22.535 -35.046  1.00117.26           C  
ANISOU 5333  CB  LYS D  80    14042  20060  10450  -3254  -3110  -1942       C  
ATOM   5334  CG  LYS D  80      48.806  22.836 -34.697  1.00116.28           C  
ANISOU 5334  CG  LYS D  80    14344  19563  10275  -3174  -2916  -1981       C  
ATOM   5335  CD  LYS D  80      48.655  23.799 -33.530  1.00119.09           C  
ANISOU 5335  CD  LYS D  80    14983  19917  10348  -3433  -2970  -2172       C  
ATOM   5336  CE  LYS D  80      47.446  23.487 -32.676  1.00118.43           C  
ANISOU 5336  CE  LYS D  80    15212  19666  10119  -3240  -2883  -2134       C  
ATOM   5337  NZ  LYS D  80      47.614  22.206 -31.953  1.00119.20           N1+
ANISOU 5337  NZ  LYS D  80    15171  20016  10102  -2989  -3045  -1939       N1+
ATOM   5338  N   PRO D  87      61.843  21.039 -36.224  1.00119.05           N  
ANISOU 5338  N   PRO D  87    10418  24188  10629  -3974  -4727  -1891       N  
ATOM   5339  CA  PRO D  87      61.144  20.951 -37.522  1.00114.68           C  
ANISOU 5339  CA  PRO D  87     9994  23216  10363  -3836  -4422  -1844       C  
ATOM   5340  C   PRO D  87      61.769  21.808 -38.621  1.00115.48           C  
ANISOU 5340  C   PRO D  87     9890  23378  10610  -4197  -4288  -1972       C  
ATOM   5341  O   PRO D  87      61.073  22.631 -39.198  1.00112.72           O  
ANISOU 5341  O   PRO D  87     9859  22618  10353  -4415  -4062  -2066       O  
ATOM   5342  CB  PRO D  87      59.739  21.511 -37.246  1.00111.08           C  
ANISOU 5342  CB  PRO D  87    10124  22206   9877  -3907  -4241  -1903       C  
ATOM   5343  CG  PRO D  87      59.566  21.385 -35.748  1.00113.12           C  
ANISOU 5343  CG  PRO D  87    10555  22578   9847  -3886  -4453  -1904       C  
ATOM   5344  CD  PRO D  87      60.955  21.506 -35.157  1.00118.17           C  
ANISOU 5344  CD  PRO D  87    10779  23811  10308  -4092  -4744  -1962       C  
ATOM   5345  N   PRO D  88      63.072  21.655 -38.952  1.00119.43           N  
ANISOU 5345  N   PRO D  88     9862  24386  11129  -4269  -4416  -1977       N  
ATOM   5346  CA  PRO D  88      63.788  22.672 -39.729  1.00122.35           C  
ANISOU 5346  CA  PRO D  88    10042  24886  11561  -4737  -4328  -2131       C  
ATOM   5347  C   PRO D  88      63.387  22.629 -41.218  1.00121.58           C  
ANISOU 5347  C   PRO D  88     9980  24468  11748  -4638  -4027  -2086       C  
ATOM   5348  O   PRO D  88      62.757  21.648 -41.606  1.00119.85           O  
ANISOU 5348  O   PRO D  88     9832  24032  11672  -4172  -3932  -1928       O  
ATOM   5349  CB  PRO D  88      65.260  22.300 -39.502  1.00125.81           C  
ANISOU 5349  CB  PRO D  88     9871  26016  11914  -4760  -4577  -2121       C  
ATOM   5350  CG  PRO D  88      65.232  20.795 -39.331  1.00124.69           C  
ANISOU 5350  CG  PRO D  88     9554  25999  11822  -4131  -4679  -1902       C  
ATOM   5351  CD  PRO D  88      63.913  20.490 -38.640  1.00121.40           C  
ANISOU 5351  CD  PRO D  88     9671  25110  11346  -3895  -4640  -1829       C  
ATOM   5352  N   ASN D  89      63.715  23.670 -42.006  1.00123.76           N  
ANISOU 5352  N   ASN D  89    10233  24700  12088  -5078  -3882  -2221       N  
ATOM   5353  CA  ASN D  89      63.327  23.725 -43.447  1.00120.99           C  
ANISOU 5353  CA  ASN D  89     9941  24039  11989  -5021  -3591  -2184       C  
ATOM   5354  C   ASN D  89      63.940  22.517 -44.167  1.00121.16           C  
ANISOU 5354  C   ASN D  89     9501  24367  12168  -4601  -3596  -2033       C  
ATOM   5355  O   ASN D  89      63.206  21.814 -44.894  1.00117.77           O  
ANISOU 5355  O   ASN D  89     9205  23623  11918  -4224  -3425  -1911       O  
ATOM   5356  CB  ASN D  89      63.717  25.030 -44.147  1.00122.26           C  
ANISOU 5356  CB  ASN D  89    10127  24155  12172  -5581  -3454  -2344       C  
ATOM   5357  CG  ASN D  89      63.187  25.111 -45.565  1.00119.20           C  
ANISOU 5357  CG  ASN D  89     9868  23405  12019  -5511  -3156  -2297       C  
ATOM   5358  ND2 ASN D  89      64.092  25.094 -46.520  1.00121.06           N  
ANISOU 5358  ND2 ASN D  89     9704  23937  12358  -5621  -3088  -2295       N  
ATOM   5359  OD1 ASN D  89      61.981  25.207 -45.808  1.00115.80           O  
ANISOU 5359  OD1 ASN D  89     9884  22448  11668  -5368  -2987  -2264       O  
ATOM   5360  N   SER D  90      65.239  22.290 -43.946  1.00125.43           N  
ANISOU 5360  N   SER D  90     9518  25508  12632  -4663  -3790  -2047       N  
ATOM   5361  CA  SER D  90      66.045  21.154 -44.479  1.00126.71           C  
ANISOU 5361  CA  SER D  90     9168  26069  12906  -4264  -3838  -1921       C  
ATOM   5362  C   SER D  90      65.188  19.883 -44.579  1.00124.33           C  
ANISOU 5362  C   SER D  90     9046  25470  12723  -3645  -3785  -1735       C  
ATOM   5363  O   SER D  90      65.344  19.144 -45.563  1.00123.35           O  
ANISOU 5363  O   SER D  90     8716  25368  12782  -3335  -3660  -1644       O  
ATOM   5364  CB  SER D  90      67.258  20.903 -43.614  1.00131.03           C  
ANISOU 5364  CB  SER D  90     9241  27268  13278  -4294  -4144  -1935       C  
ATOM   5365  OG  SER D  90      66.881  20.344 -42.362  1.00130.66           O  
ANISOU 5365  OG  SER D  90     9364  27210  13069  -4035  -4359  -1860       O  
ATOM   5366  N   PHE D  91      64.347  19.628 -43.569  1.00124.26           N  
ANISOU 5366  N   PHE D  91     9404  25209  12600  -3482  -3881  -1683       N  
ATOM   5367  CA  PHE D  91      63.529  18.395 -43.433  1.00121.91           C  
ANISOU 5367  CA  PHE D  91     9300  24648  12371  -2922  -3867  -1502       C  
ATOM   5368  C   PHE D  91      62.433  18.322 -44.500  1.00117.11           C  
ANISOU 5368  C   PHE D  91     9025  23494  11977  -2794  -3565  -1461       C  
ATOM   5369  O   PHE D  91      62.249  17.231 -45.099  1.00114.55           O  
ANISOU 5369  O   PHE D  91     8631  23090  11803  -2351  -3492  -1322       O  
ATOM   5370  CB  PHE D  91      62.843  18.290 -42.069  1.00122.31           C  
ANISOU 5370  CB  PHE D  91     9694  24553  12225  -2855  -4023  -1471       C  
ATOM   5371  CG  PHE D  91      62.024  17.027 -41.981  1.00119.96           C  
ANISOU 5371  CG  PHE D  91     9594  23986  11998  -2314  -3995  -1280       C  
ATOM   5372  CD1 PHE D  91      62.662  15.796 -41.937  1.00121.52           C  
ANISOU 5372  CD1 PHE D  91     9468  24484  12220  -1872  -4136  -1130       C  
ATOM   5373  CD2 PHE D  91      60.634  17.054 -42.038  1.00115.80           C  
ANISOU 5373  CD2 PHE D  91     9566  22908  11526  -2241  -3815  -1249       C  
ATOM   5374  CE1 PHE D  91      61.932  14.621 -41.887  1.00119.31           C  
ANISOU 5374  CE1 PHE D  91     9391  23937  12005  -1390  -4106   -952       C  
ATOM   5375  CE2 PHE D  91      59.904  15.875 -41.993  1.00113.41           C  
ANISOU 5375  CE2 PHE D  91     9434  22370  11287  -1773  -3785  -1073       C  
ATOM   5376  CZ  PHE D  91      60.555  14.662 -41.914  1.00115.57           C  
ANISOU 5376  CZ  PHE D  91     9412  22922  11576  -1359  -3930   -925       C  
ATOM   5377  N   TYR D  92      61.700  19.427 -44.681  1.00115.42           N  
ANISOU 5377  N   TYR D  92     9182  22909  11765  -3156  -3405  -1577       N  
ATOM   5378  CA  TYR D  92      60.583  19.577 -45.645  1.00111.78           C  
ANISOU 5378  CA  TYR D  92     9074  21915  11481  -3099  -3124  -1558       C  
ATOM   5379  C   TYR D  92      61.121  19.508 -47.071  1.00112.14           C  
ANISOU 5379  C   TYR D  92     8838  22050  11720  -3099  -2954  -1554       C  
ATOM   5380  O   TYR D  92      60.405  18.999 -47.951  1.00109.98           O  
ANISOU 5380  O   TYR D  92     8712  21459  11617  -2839  -2765  -1471       O  
ATOM   5381  CB  TYR D  92      59.823  20.879 -45.395  1.00110.90           C  
ANISOU 5381  CB  TYR D  92     9396  21447  11295  -3505  -3025  -1695       C  
ATOM   5382  CG  TYR D  92      59.175  20.924 -44.036  1.00111.11           C  
ANISOU 5382  CG  TYR D  92     9734  21352  11131  -3480  -3161  -1703       C  
ATOM   5383  CD1 TYR D  92      57.992  20.248 -43.781  1.00107.87           C  
ANISOU 5383  CD1 TYR D  92     9650  20587  10749  -3136  -3096  -1592       C  
ATOM   5384  CD2 TYR D  92      59.777  21.583 -42.980  1.00114.65           C  
ANISOU 5384  CD2 TYR D  92    10134  22072  11357  -3798  -3361  -1819       C  
ATOM   5385  CE1 TYR D  92      57.392  20.273 -42.531  1.00108.26           C  
ANISOU 5385  CE1 TYR D  92     9981  20540  10612  -3114  -3208  -1597       C  
ATOM   5386  CE2 TYR D  92      59.185  21.622 -41.726  1.00114.88           C  
ANISOU 5386  CE2 TYR D  92    10456  21999  11194  -3776  -3480  -1831       C  
ATOM   5387  CZ  TYR D  92      58.002  20.945 -41.490  1.00111.49           C  
ANISOU 5387  CZ  TYR D  92    10349  21217  10795  -3423  -3402  -1715       C  
ATOM   5388  OH  TYR D  92      57.420  20.965 -40.255  1.00111.81           O  
ANISOU 5388  OH  TYR D  92    10673  21175  10637  -3401  -3508  -1724       O  
ATOM   5389  N   ARG D  93      62.332  20.014 -47.297  1.00116.35           N  
ANISOU 5389  N   ARG D  93     8979  23011  12219  -3396  -3015  -1645       N  
ATOM   5390  CA  ARG D  93      63.039  19.859 -48.594  1.00117.46           C  
ANISOU 5390  CA  ARG D  93     8769  23341  12519  -3384  -2872  -1638       C  
ATOM   5391  C   ARG D  93      63.221  18.359 -48.885  1.00116.44           C  
ANISOU 5391  C   ARG D  93     8394  23351  12496  -2807  -2903  -1482       C  
ATOM   5392  O   ARG D  93      62.979  17.966 -50.039  1.00113.65           O  
ANISOU 5392  O   ARG D  93     8035  22827  12320  -2623  -2701  -1434       O  
ATOM   5393  CB  ARG D  93      64.361  20.634 -48.566  1.00123.37           C  
ANISOU 5393  CB  ARG D  93     9111  24591  13174  -3820  -2966  -1764       C  
ATOM   5394  CG  ARG D  93      65.292  20.455 -49.761  1.00125.48           C  
ANISOU 5394  CG  ARG D  93     8932  25176  13571  -3826  -2847  -1765       C  
ATOM   5395  CD  ARG D  93      66.600  21.171 -49.446  1.00131.20           C  
ANISOU 5395  CD  ARG D  93     9238  26450  14161  -4265  -2988  -1887       C  
ATOM   5396  NE  ARG D  93      67.471  21.487 -50.567  1.00133.66           N  
ANISOU 5396  NE  ARG D  93     9180  27044  14558  -4485  -2842  -1937       N  
ATOM   5397  CZ  ARG D  93      67.134  22.252 -51.602  1.00132.34           C  
ANISOU 5397  CZ  ARG D  93     9219  26579  14486  -4773  -2588  -1987       C  
ATOM   5398  NH1 ARG D  93      65.919  22.771 -51.693  1.00128.43           N1+
ANISOU 5398  NH1 ARG D  93     9291  25484  14023  -4848  -2453  -1991       N1+
ATOM   5399  NH2 ARG D  93      68.007  22.492 -52.563  1.00134.56           N  
ANISOU 5399  NH2 ARG D  93     9133  27170  14824  -4976  -2466  -2027       N  
ATOM   5400  N   SER D  94      63.616  17.562 -47.880  1.00117.78           N  
ANISOU 5400  N   SER D  94     8392  23803  12555  -2530  -3146  -1407       N  
ATOM   5401  CA  SER D  94      63.941  16.113 -48.021  1.00117.65           C  
ANISOU 5401  CA  SER D  94     8124  23964  12615  -1968  -3213  -1258       C  
ATOM   5402  C   SER D  94      62.656  15.304 -48.226  1.00113.81           C  
ANISOU 5402  C   SER D  94     8056  22952  12236  -1586  -3087  -1133       C  
ATOM   5403  O   SER D  94      62.706  14.231 -48.873  1.00114.12           O  
ANISOU 5403  O   SER D  94     7977  22976  12406  -1164  -3024  -1028       O  
ATOM   5404  CB  SER D  94      64.690  15.600 -46.823  1.00120.68           C  
ANISOU 5404  CB  SER D  94     8249  24779  12827  -1810  -3521  -1211       C  
ATOM   5405  OG  SER D  94      65.882  16.340 -46.622  1.00124.96           O  
ANISOU 5405  OG  SER D  94     8381  25836  13261  -2180  -3648  -1331       O  
ATOM   5406  N   LEU D  95      61.556  15.799 -47.660  1.00110.80           N  
ANISOU 5406  N   LEU D  95     8143  22167  11789  -1731  -3055  -1151       N  
ATOM   5407  CA  LEU D  95      60.259  15.090 -47.589  1.00106.43           C  
ANISOU 5407  CA  LEU D  95     8008  21137  11295  -1413  -2967  -1036       C  
ATOM   5408  C   LEU D  95      59.589  15.095 -48.974  1.00102.79           C  
ANISOU 5408  C   LEU D  95     7701  20315  11041  -1370  -2683  -1033       C  
ATOM   5409  O   LEU D  95      59.105  14.028 -49.422  1.00102.07           O  
ANISOU 5409  O   LEU D  95     7691  20028  11064   -972  -2609   -914       O  
ATOM   5410  CB  LEU D  95      59.419  15.803 -46.526  1.00105.65           C  
ANISOU 5410  CB  LEU D  95     8307  20796  11038  -1646  -3022  -1085       C  
ATOM   5411  CG  LEU D  95      57.975  15.322 -46.386  1.00102.34           C  
ANISOU 5411  CG  LEU D  95     8346  19880  10657  -1416  -2913   -992       C  
ATOM   5412  CD1 LEU D  95      57.935  13.859 -45.992  1.00103.03           C  
ANISOU 5412  CD1 LEU D  95     8393  20010  10744   -924  -3026   -817       C  
ATOM   5413  CD2 LEU D  95      57.195  16.165 -45.398  1.00101.53           C  
ANISOU 5413  CD2 LEU D  95     8614  19568  10395  -1678  -2943  -1066       C  
ATOM   5414  N   TYR D  96      59.553  16.256 -49.634  1.00100.87           N  
ANISOU 5414  N   TYR D  96     7515  19977  10835  -1774  -2532  -1157       N  
ATOM   5415  CA  TYR D  96      58.794  16.452 -50.893  1.00 96.69           C  
ANISOU 5415  CA  TYR D  96     7193  19070  10475  -1788  -2263  -1161       C  
ATOM   5416  C   TYR D  96      59.042  15.278 -51.839  1.00 96.29           C  
ANISOU 5416  C   TYR D  96     6932  19076  10579  -1384  -2182  -1063       C  
ATOM   5417  O   TYR D  96      58.103  14.611 -52.245  1.00 92.13           O  
ANISOU 5417  O   TYR D  96     6657  18200  10150  -1113  -2069   -979       O  
ATOM   5418  CB  TYR D  96      59.140  17.795 -51.531  1.00 97.33           C  
ANISOU 5418  CB  TYR D  96     7244  19175  10563  -2272  -2143  -1300       C  
ATOM   5419  CG  TYR D  96      58.143  18.230 -52.561  1.00 94.27           C  
ANISOU 5419  CG  TYR D  96     7182  18336  10301  -2340  -1892  -1308       C  
ATOM   5420  CD1 TYR D  96      58.148  17.689 -53.833  1.00 93.39           C  
ANISOU 5420  CD1 TYR D  96     6965  18169  10350  -2148  -1723  -1258       C  
ATOM   5421  CD2 TYR D  96      57.138  19.124 -52.239  1.00 93.73           C  
ANISOU 5421  CD2 TYR D  96     7541  17889  10182  -2561  -1828  -1361       C  
ATOM   5422  CE1 TYR D  96      57.209  18.068 -54.780  1.00 91.65           C  
ANISOU 5422  CE1 TYR D  96     7046  17544  10232  -2200  -1505  -1258       C  
ATOM   5423  CE2 TYR D  96      56.186  19.510 -53.174  1.00 91.70           C  
ANISOU 5423  CE2 TYR D  96     7584  17224  10036  -2594  -1609  -1360       C  
ATOM   5424  CZ  TYR D  96      56.213  18.972 -54.451  1.00 90.65           C  
ANISOU 5424  CZ  TYR D  96     7333  17051  10057  -2415  -1452  -1304       C  
ATOM   5425  OH  TYR D  96      55.289  19.342 -55.392  1.00 87.58           O  
ANISOU 5425  OH  TYR D  96     7230  16281   9765  -2445  -1248  -1297       O  
ATOM   5426  N   PRO D  97      60.299  14.954 -52.217  1.00 99.81           N  
ANISOU 5426  N   PRO D  97     6909  19966  11047  -1320  -2235  -1074       N  
ATOM   5427  CA  PRO D  97      60.534  13.838 -53.140  1.00 99.51           C  
ANISOU 5427  CA  PRO D  97     6687  19969  11152   -917  -2145   -993       C  
ATOM   5428  C   PRO D  97      60.080  12.460 -52.611  1.00 98.59           C  
ANISOU 5428  C   PRO D  97     6694  19721  11043   -411  -2243   -847       C  
ATOM   5429  O   PRO D  97      59.756  11.588 -53.426  1.00 96.92           O  
ANISOU 5429  O   PRO D  97     6534  19329  10963    -92  -2118   -780       O  
ATOM   5430  CB  PRO D  97      62.054  13.882 -53.391  1.00103.40           C  
ANISOU 5430  CB  PRO D  97     6626  21032  11627   -977  -2216  -1048       C  
ATOM   5431  CG  PRO D  97      62.624  14.667 -52.221  1.00106.22           C  
ANISOU 5431  CG  PRO D  97     6867  21687  11804  -1304  -2429  -1118       C  
ATOM   5432  CD  PRO D  97      61.539  15.638 -51.811  1.00103.64           C  
ANISOU 5432  CD  PRO D  97     7019  20939  11420  -1630  -2375  -1170       C  
ATOM   5433  N   LYS D  98      60.063  12.277 -51.282  1.00 99.07           N  
ANISOU 5433  N   LYS D  98     6818  19867  10958   -354  -2462   -801       N  
ATOM   5434  CA  LYS D  98      59.593  11.027 -50.628  1.00 97.66           C  
ANISOU 5434  CA  LYS D  98     6804  19545  10757     91  -2571   -651       C  
ATOM   5435  C   LYS D  98      58.075  10.898 -50.768  1.00 93.58           C  
ANISOU 5435  C   LYS D  98     6787  18472  10296    134  -2421   -602       C  
ATOM   5436  O   LYS D  98      57.569   9.747 -50.871  1.00 92.77           O  
ANISOU 5436  O   LYS D  98     6836  18159  10255    517  -2400   -481       O  
ATOM   5437  CB  LYS D  98      59.985  11.018 -49.151  1.00 99.92           C  
ANISOU 5437  CB  LYS D  98     7033  20086  10845     81  -2844   -620       C  
ATOM   5438  CG  LYS D  98      61.474  10.824 -48.873  1.00104.71           C  
ANISOU 5438  CG  LYS D  98     7125  21277  11384    155  -3037   -632       C  
ATOM   5439  CD  LYS D  98      61.824   9.672 -47.908  1.00107.15           C  
ANISOU 5439  CD  LYS D  98     7353  21766  11592    584  -3276   -487       C  
ATOM   5440  CE  LYS D  98      62.230  10.096 -46.507  1.00109.74           C  
ANISOU 5440  CE  LYS D  98     7619  22384  11693    412  -3541   -498       C  
ATOM   5441  NZ  LYS D  98      62.217   8.952 -45.566  1.00110.82           N1+
ANISOU 5441  NZ  LYS D  98     7824  22555  11728    840  -3745   -330       N1+
ATOM   5442  N   ILE D  99      57.372  12.030 -50.750  1.00 91.69           N  
ANISOU 5442  N   ILE D  99     6801  18007  10031   -244  -2324   -693       N  
ATOM   5443  CA  ILE D  99      55.911  12.081 -51.017  1.00 88.35           C  
ANISOU 5443  CA  ILE D  99     6823  17077   9668   -244  -2157   -667       C  
ATOM   5444  C   ILE D  99      55.695  11.719 -52.487  1.00 87.62           C  
ANISOU 5444  C   ILE D  99     6717  16811   9763   -116  -1941   -659       C  
ATOM   5445  O   ILE D  99      54.807  10.906 -52.778  1.00 85.01           O  
ANISOU 5445  O   ILE D  99     6624  16169   9507    139  -1857   -571       O  
ATOM   5446  CB  ILE D  99      55.332  13.462 -50.670  1.00 87.51           C  
ANISOU 5446  CB  ILE D  99     6958  16809   9484   -669  -2109   -779       C  
ATOM   5447  CG1 ILE D  99      55.440  13.723 -49.164  1.00 89.21           C  
ANISOU 5447  CG1 ILE D  99     7232  17167   9498   -770  -2321   -787       C  
ATOM   5448  CG2 ILE D  99      53.901  13.605 -51.195  1.00 83.99           C  
ANISOU 5448  CG2 ILE D  99     6911  15879   9123   -671  -1910   -765       C  
ATOM   5449  CD1 ILE D  99      55.032  15.121 -48.742  1.00 88.97           C  
ANISOU 5449  CD1 ILE D  99     7420  17016   9370  -1194  -2290   -917       C  
ATOM   5450  N   ILE D 100      56.488  12.292 -53.385  1.00 89.67           N  
ANISOU 5450  N   ILE D 100     6708  17277  10087   -299  -1854   -748       N  
ATOM   5451  CA  ILE D 100      56.338  12.030 -54.844  1.00 88.78           C  
ANISOU 5451  CA  ILE D 100     6574  17022  10136   -206  -1640   -752       C  
ATOM   5452  C   ILE D 100      56.568  10.532 -55.097  1.00 89.77           C  
ANISOU 5452  C   ILE D 100     6588  17188  10334    274  -1666   -646       C  
ATOM   5453  O   ILE D 100      55.749   9.899 -55.803  1.00 86.21           O  
ANISOU 5453  O   ILE D 100     6357  16414   9986    471  -1527   -595       O  
ATOM   5454  CB  ILE D 100      57.274  12.938 -55.660  1.00 90.54           C  
ANISOU 5454  CB  ILE D 100     6503  17512  10387   -512  -1554   -865       C  
ATOM   5455  CG1 ILE D 100      56.890  14.420 -55.505  1.00 89.75           C  
ANISOU 5455  CG1 ILE D 100     6600  17277  10223   -987  -1503   -965       C  
ATOM   5456  CG2 ILE D 100      57.302  12.473 -57.109  1.00 90.20           C  
ANISOU 5456  CG2 ILE D 100     6383  17396  10491   -357  -1355   -859       C  
ATOM   5457  CD1 ILE D 100      56.557  15.175 -56.782  1.00 87.78           C  
ANISOU 5457  CD1 ILE D 100     6457  16828  10067  -1213  -1272  -1024       C  
ATOM   5458  N   GLN D 101      57.622   9.971 -54.514  1.00 94.60           N  
ANISOU 5458  N   GLN D 101     6882  18175  10886    464  -1844   -614       N  
ATOM   5459  CA  GLN D 101      57.886   8.513 -54.593  1.00 97.29           C  
ANISOU 5459  CA  GLN D 101     7138  18552  11276    957  -1896   -505       C  
ATOM   5460  C   GLN D 101      56.650   7.749 -54.094  1.00 95.71           C  
ANISOU 5460  C   GLN D 101     7368  17929  11070   1169  -1904   -391       C  
ATOM   5461  O   GLN D 101      56.129   6.881 -54.821  1.00 95.40           O  
ANISOU 5461  O   GLN D 101     7482  17630  11137   1429  -1784   -337       O  
ATOM   5462  CB  GLN D 101      59.116   8.122 -53.785  1.00102.38           C  
ANISOU 5462  CB  GLN D 101     7413  19662  11826   1124  -2124   -477       C  
ATOM   5463  CG  GLN D 101      59.524   6.692 -54.108  1.00104.04           C  
ANISOU 5463  CG  GLN D 101     7503  19922  12105   1642  -2147   -381       C  
ATOM   5464  CD  GLN D 101      59.940   5.930 -52.880  1.00106.91           C  
ANISOU 5464  CD  GLN D 101     7805  20466  12349   1931  -2403   -270       C  
ATOM   5465  NE2 GLN D 101      59.183   4.891 -52.554  1.00105.86           N  
ANISOU 5465  NE2 GLN D 101     7997  20004  12222   2252  -2426   -140       N  
ATOM   5466  OE1 GLN D 101      60.927   6.277 -52.237  1.00109.32           O  
ANISOU 5466  OE1 GLN D 101     7779  21206  12550   1854  -2579   -297       O  
ATOM   5467  N   ASP D 102      56.188   8.067 -52.892  1.00 96.38           N  
ANISOU 5467  N   ASP D 102     7644  17952  11022   1046  -2037   -361       N  
ATOM   5468  CA  ASP D 102      54.923   7.520 -52.334  1.00 94.32           C  
ANISOU 5468  CA  ASP D 102     7807  17297  10734   1170  -2033   -260       C  
ATOM   5469  C   ASP D 102      53.867   7.524 -53.441  1.00 87.17           C  
ANISOU 5469  C   ASP D 102     7158  15999   9965   1135  -1795   -278       C  
ATOM   5470  O   ASP D 102      53.377   6.439 -53.826  1.00 84.61           O  
ANISOU 5470  O   ASP D 102     6989  15445   9714   1432  -1736   -191       O  
ATOM   5471  CB  ASP D 102      54.440   8.342 -51.137  1.00 97.50           C  
ANISOU 5471  CB  ASP D 102     8396  17668  10981    895  -2136   -280       C  
ATOM   5472  CG  ASP D 102      53.820   7.514 -50.032  1.00100.71           C  
ANISOU 5472  CG  ASP D 102     9060  17925  11281   1110  -2260   -146       C  
ATOM   5473  OD1 ASP D 102      54.367   6.418 -49.754  1.00105.62           O  
ANISOU 5473  OD1 ASP D 102     9574  18670  11887   1458  -2382    -38       O  
ATOM   5474  OD2 ASP D 102      52.865   8.012 -49.385  1.00100.07           O1-
ANISOU 5474  OD2 ASP D 102     9275  17632  11117    925  -2243   -152       O1-
ATOM   5475  N   ILE D 103      53.576   8.704 -53.972  1.00 83.45           N  
ANISOU 5475  N   ILE D 103     6725  15460   9521    785  -1666   -389       N  
ATOM   5476  CA  ILE D 103      52.518   8.908 -55.002  1.00 80.32           C  
ANISOU 5476  CA  ILE D 103     6578  14703   9237    707  -1447   -413       C  
ATOM   5477  C   ILE D 103      52.759   7.955 -56.179  1.00 82.48           C  
ANISOU 5477  C   ILE D 103     6751  14942   9645    985  -1334   -387       C  
ATOM   5478  O   ILE D 103      51.810   7.329 -56.633  1.00 82.55           O  
ANISOU 5478  O   ILE D 103     7014  14630   9720   1125  -1231   -335       O  
ATOM   5479  CB  ILE D 103      52.461  10.373 -55.466  1.00 77.58           C  
ANISOU 5479  CB  ILE D 103     6228  14356   8894    300  -1340   -537       C  
ATOM   5480  CG1 ILE D 103      51.898  11.284 -54.381  1.00 76.09           C  
ANISOU 5480  CG1 ILE D 103     6246  14085   8578     43  -1414   -569       C  
ATOM   5481  CG2 ILE D 103      51.683  10.503 -56.762  1.00 74.15           C  
ANISOU 5481  CG2 ILE D 103     5955  13635   8583    265  -1121   -560       C  
ATOM   5482  CD1 ILE D 103      52.039  12.754 -54.675  1.00 75.96           C  
ANISOU 5482  CD1 ILE D 103     6219  14099   8543   -359  -1342   -695       C  
ATOM   5483  N   GLU D 104      53.977   7.859 -56.694  1.00 86.17           N  
ANISOU 5483  N   GLU D 104     6858  15734  10147   1053  -1345   -429       N  
ATOM   5484  CA  GLU D 104      54.234   7.043 -57.911  1.00 86.68           C  
ANISOU 5484  CA  GLU D 104     6825  15773  10336   1303  -1214   -426       C  
ATOM   5485  C   GLU D 104      54.053   5.547 -57.615  1.00 84.14           C  
ANISOU 5485  C   GLU D 104     6620  15321  10030   1736  -1283   -309       C  
ATOM   5486  O   GLU D 104      53.667   4.824 -58.545  1.00 84.56           O  
ANISOU 5486  O   GLU D 104     6787  15161  10180   1924  -1149   -297       O  
ATOM   5487  CB  GLU D 104      55.588   7.405 -58.525  1.00 92.66           C  
ANISOU 5487  CB  GLU D 104     7152  16939  11116   1245  -1194   -511       C  
ATOM   5488  CG  GLU D 104      55.449   8.508 -59.579  1.00 93.41           C  
ANISOU 5488  CG  GLU D 104     7240  16990  11261    898  -1005   -615       C  
ATOM   5489  CD  GLU D 104      56.465   9.645 -59.549  1.00 97.15           C  
ANISOU 5489  CD  GLU D 104     7401  17831  11681    560  -1030   -712       C  
ATOM   5490  OE1 GLU D 104      56.027  10.818 -59.649  1.00 96.28           O  
ANISOU 5490  OE1 GLU D 104     7436  17601  11547    185   -961   -771       O  
ATOM   5491  OE2 GLU D 104      57.685   9.357 -59.430  1.00100.01           O1-
ANISOU 5491  OE2 GLU D 104     7378  18598  12023    671  -1117   -727       O1-
ATOM   5492  N   THR D 105      54.296   5.071 -56.395  1.00 82.00           N  
ANISOU 5492  N   THR D 105     6345  15151   9660   1891  -1481   -224       N  
ATOM   5493  CA  THR D 105      54.061   3.637 -56.051  1.00 81.24           C  
ANISOU 5493  CA  THR D 105     6415  14886   9565   2299  -1551    -96       C  
ATOM   5494  C   THR D 105      52.544   3.372 -56.057  1.00 76.96           C  
ANISOU 5494  C   THR D 105     6321  13879   9041   2256  -1455    -41       C  
ATOM   5495  O   THR D 105      52.101   2.292 -56.476  1.00 75.71           O  
ANISOU 5495  O   THR D 105     6349  13472   8944   2517  -1395     24       O  
ATOM   5496  CB  THR D 105      54.735   3.219 -54.737  1.00 83.74           C  
ANISOU 5496  CB  THR D 105     6619  15443   9757   2476  -1796     -7       C  
ATOM   5497  CG2 THR D 105      56.209   3.544 -54.655  1.00 87.41           C  
ANISOU 5497  CG2 THR D 105     6615  16408  10190   2493  -1907    -64       C  
ATOM   5498  OG1 THR D 105      54.049   3.875 -53.679  1.00 82.13           O  
ANISOU 5498  OG1 THR D 105     6620  15151   9435   2222  -1878     14       O  
ATOM   5499  N   ILE D 106      51.754   4.354 -55.650  1.00 74.86           N  
ANISOU 5499  N   ILE D 106     6222  13499   8723   1926  -1431    -75       N  
ATOM   5500  CA  ILE D 106      50.271   4.278 -55.767  1.00 72.19           C  
ANISOU 5500  CA  ILE D 106     6269  12754   8405   1842  -1316    -42       C  
ATOM   5501  C   ILE D 106      49.908   4.128 -57.254  1.00 70.61           C  
ANISOU 5501  C   ILE D 106     6111  12374   8344   1857  -1113    -98       C  
ATOM   5502  O   ILE D 106      49.193   3.186 -57.604  1.00 69.38           O  
ANISOU 5502  O   ILE D 106     6182  11944   8237   2035  -1048    -37       O  
ATOM   5503  CB  ILE D 106      49.620   5.505 -55.099  1.00 70.93           C  
ANISOU 5503  CB  ILE D 106     6232  12556   8160   1488  -1323    -90       C  
ATOM   5504  CG1 ILE D 106      49.895   5.553 -53.587  1.00 71.73           C  
ANISOU 5504  CG1 ILE D 106     6332  12817   8105   1484  -1525    -33       C  
ATOM   5505  CG2 ILE D 106      48.133   5.552 -55.435  1.00 68.67           C  
ANISOU 5505  CG2 ILE D 106     6285  11896   7911   1393  -1178    -78       C  
ATOM   5506  CD1 ILE D 106      49.431   6.827 -52.893  1.00 70.24           C  
ANISOU 5506  CD1 ILE D 106     6238  12631   7817   1138  -1538   -102       C  
ATOM   5507  N   GLU D 107      50.374   5.028 -58.110  1.00 70.95           N  
ANISOU 5507  N   GLU D 107     5955  12564   8439   1661  -1014   -209       N  
ATOM   5508  CA  GLU D 107      50.134   4.983 -59.582  1.00 70.42           C  
ANISOU 5508  CA  GLU D 107     5903  12367   8488   1657   -820   -268       C  
ATOM   5509  C   GLU D 107      50.503   3.596 -60.126  1.00 30.05           C  
ATOM   5510  O   GLU D 107      49.779   3.074 -60.985  1.00 68.16           O  
ANISOU 5510  O   GLU D 107     5784  11779   8337   2106   -670   -225       O  
ATOM   5511  CB  GLU D 107      50.983   6.028 -60.318  1.00 73.21           C  
ANISOU 5511  CB  GLU D 107     5972  12979   8867   1435   -747   -381       C  
ATOM   5512  CG  GLU D 107      50.738   7.451 -59.873  1.00 74.25           C  
ANISOU 5512  CG  GLU D 107     6135  13144   8935   1055   -757   -437       C  
ATOM   5513  CD  GLU D 107      49.488   8.094 -60.451  1.00 74.08           C  
ANISOU 5513  CD  GLU D 107     6395  12807   8944    852   -612   -462       C  
ATOM   5514  OE1 GLU D 107      48.494   7.377 -60.776  1.00 73.17           O  
ANISOU 5514  OE1 GLU D 107     6523  12406   8872    992   -544   -410       O  
ATOM   5515  OE2 GLU D 107      49.512   9.320 -60.579  1.00 77.08           O1-
ANISOU 5515  OE2 GLU D 107     6756  13231   9301    552   -569   -532       O1-
ATOM   5516  N   SER D 108      51.620   3.032 -59.658  1.00 71.40           N  
ANISOU 5516  N   SER D 108     5763  12717   8650   2271   -930   -195       N  
ATOM   5517  CA  SER D 108      52.099   1.703 -60.094  1.00 72.23           C  
ANISOU 5517  CA  SER D 108     5833  12804   8809   2672   -925   -156       C  
ATOM   5518  C   SER D 108      51.043   0.657 -59.720  1.00 70.35           C  
ANISOU 5518  C   SER D 108     5985  12181   8562   2846   -941    -47       C  
ATOM   5519  O   SER D 108      50.790  -0.251 -60.529  1.00 69.72           O  
ANISOU 5519  O   SER D 108     6041  11894   8554   3051   -841    -45       O  
ATOM   5520  CB  SER D 108      53.425   1.386 -59.501  1.00 76.18           C  
ANISOU 5520  CB  SER D 108     6011  13669   9265   2894  -1082   -134       C  
ATOM   5521  OG  SER D 108      53.967   0.227 -60.120  1.00 78.90           O  
ANISOU 5521  OG  SER D 108     6293  14013   9672   3284  -1047   -121       O  
ATOM   5522  N   ASN D 109      50.427   0.810 -58.544  1.00 69.17           N  
ANISOU 5522  N   ASN D 109     6018  11940   8321   2743  -1055     33       N  
ATOM   5523  CA  ASN D 109      49.374  -0.113 -58.035  1.00 67.66           C  
ANISOU 5523  CA  ASN D 109     6207  11400   8101   2857  -1076    147       C  
ATOM   5524  C   ASN D 109      48.165  -0.090 -58.978  1.00 64.96           C  
ANISOU 5524  C   ASN D 109     6117  10733   7832   2711   -891    108       C  
ATOM   5525  O   ASN D 109      47.638  -1.178 -59.304  1.00 64.07           O  
ANISOU 5525  O   ASN D 109     6241  10349   7754   2895   -844    161       O  
ATOM   5526  CB  ASN D 109      48.940   0.230 -56.614  1.00 67.13           C  
ANISOU 5526  CB  ASN D 109     6264  11337   7907   2724  -1215    227       C  
ATOM   5527  CG  ASN D 109      50.047   0.075 -55.594  1.00 69.65           C  
ANISOU 5527  CG  ASN D 109     6370  11962   8132   2887  -1420    284       C  
ATOM   5528  ND2 ASN D 109      49.862   0.665 -54.428  1.00 68.98           N  
ANISOU 5528  ND2 ASN D 109     6323  11963   7924   2714  -1539    319       N  
ATOM   5529  OD1 ASN D 109      51.037  -0.596 -55.845  1.00 72.15           O  
ANISOU 5529  OD1 ASN D 109     6497  12438   8481   3178  -1471    297       O  
ATOM   5530  N   TRP D 110      47.748   1.108 -59.395  1.00 63.72           N  
ANISOU 5530  N   TRP D 110     5918  10601   7691   2390   -797     19       N  
ATOM   5531  CA  TRP D 110      46.652   1.292 -60.384  1.00 61.94           C  
ANISOU 5531  CA  TRP D 110     5888  10116   7531   2235   -625    -28       C  
ATOM   5532  C   TRP D 110      47.031   0.598 -61.697  1.00 64.52           C  
ANISOU 5532  C   TRP D 110     6162  10399   7953   2421   -508    -81       C  
ATOM   5533  O   TRP D 110      46.190  -0.159 -62.232  1.00 63.55           O  
ANISOU 5533  O   TRP D 110     6288   9992   7867   2488   -425    -62       O  
ATOM   5534  CB  TRP D 110      46.352   2.776 -60.608  1.00 58.79           C  
ANISOU 5534  CB  TRP D 110     5419   9792   7126   1890   -558   -113       C  
ATOM   5535  CG  TRP D 110      45.591   3.457 -59.510  1.00 56.92           C  
ANISOU 5535  CG  TRP D 110     5325   9501   6800   1688   -624    -78       C  
ATOM   5536  CD1 TRP D 110      46.103   4.022 -58.381  1.00 57.28           C  
ANISOU 5536  CD1 TRP D 110     5264   9747   6753   1608   -759    -67       C  
ATOM   5537  CD2 TRP D 110      44.169   3.681 -59.453  1.00 53.98           C  
ANISOU 5537  CD2 TRP D 110     5222   8873   6414   1534   -550    -61       C  
ATOM   5538  CE2 TRP D 110      43.911   4.385 -58.262  1.00 53.35           C  
ANISOU 5538  CE2 TRP D 110     5185   8851   6232   1381   -638    -42       C  
ATOM   5539  CE3 TRP D 110      43.089   3.341 -60.279  1.00 51.86           C  
ANISOU 5539  CE3 TRP D 110     5153   8350   6202   1513   -422    -62       C  
ATOM   5540  NE1 TRP D 110      45.108   4.569 -57.630  1.00 55.50           N  
ANISOU 5540  NE1 TRP D 110     5236   9395   6455   1425   -768    -47       N  
ATOM   5541  CZ2 TRP D 110      42.627   4.766 -57.888  1.00 51.37           C  
ANISOU 5541  CZ2 TRP D 110     5160   8417   5939   1226   -591    -27       C  
ATOM   5542  CZ3 TRP D 110      41.819   3.729 -59.917  1.00 49.27           C  
ANISOU 5542  CZ3 TRP D 110     5031   7856   5834   1349   -384    -43       C  
ATOM   5543  CH2 TRP D 110      41.595   4.423 -58.735  1.00 49.13           C  
ANISOU 5543  CH2 TRP D 110     5045   7903   5719   1217   -463    -25       C  
ATOM   5544  N   ARG D 111      48.252   0.846 -62.181  1.00 69.22           N  
ANISOU 5544  N   ARG D 111     6443  11279   8580   2493   -501   -150       N  
ATOM   5545  CA  ARG D 111      48.775   0.360 -63.487  1.00 73.05           C  
ANISOU 5545  CA  ARG D 111     6823  11788   9145   2654   -374   -224       C  
ATOM   5546  C   ARG D 111      48.797  -1.172 -63.505  1.00 74.24           C  
ANISOU 5546  C   ARG D 111     7138  11754   9315   3020   -398   -162       C  
ATOM   5547  O   ARG D 111      48.356  -1.760 -64.529  1.00 74.19           O  
ANISOU 5547  O   ARG D 111     7287  11537   9363   3093   -268   -203       O  
ATOM   5548  CB  ARG D 111      50.196   0.874 -63.736  1.00 79.11           C  
ANISOU 5548  CB  ARG D 111     7186  12952   9919   2678   -386   -295       C  
ATOM   5549  CG  ARG D 111      50.315   1.996 -64.751  1.00 81.29           C  
ANISOU 5549  CG  ARG D 111     7313  13348  10226   2398   -243   -404       C  
ATOM   5550  CD  ARG D 111      51.611   2.749 -64.483  1.00 87.05           C  
ANISOU 5550  CD  ARG D 111     7653  14496  10926   2319   -304   -451       C  
ATOM   5551  NE  ARG D 111      51.432   4.191 -64.637  1.00 88.89           N  
ANISOU 5551  NE  ARG D 111     7836  14801  11137   1921   -251   -509       N  
ATOM   5552  CZ  ARG D 111      52.136   5.140 -64.010  1.00 91.68           C  
ANISOU 5552  CZ  ARG D 111     7963  15435  11436   1716   -337   -535       C  
ATOM   5553  NH1 ARG D 111      53.088   4.826 -63.137  1.00 93.21           N1+
ANISOU 5553  NH1 ARG D 111     7927  15902  11586   1867   -493   -506       N1+
ATOM   5554  NH2 ARG D 111      51.858   6.411 -64.262  1.00 90.87           N  
ANISOU 5554  NH2 ARG D 111     7881  15330  11316   1356   -269   -588       N  
ATOM   5555  N   CYS D 112      49.286  -1.779 -62.419  1.00 75.30           N  
ANISOU 5555  N   CYS D 112     7256  11958   9398   3236   -560    -68       N  
ATOM   5556  CA  CYS D 112      49.457  -3.246 -62.260  1.00 76.97           C  
ANISOU 5556  CA  CYS D 112     7628  12004   9614   3618   -610      8       C  
ATOM   5557  C   CYS D 112      48.196  -3.881 -61.669  1.00 75.32           C  
ANISOU 5557  C   CYS D 112     7833  11420   9367   3582   -636    113       C  
ATOM   5558  O   CYS D 112      48.151  -5.109 -61.580  1.00 76.95           O  
ANISOU 5558  O   CYS D 112     8248  11418   9574   3859   -663    182       O  
ATOM   5559  CB  CYS D 112      50.647  -3.528 -61.362  1.00 80.14           C  
ANISOU 5559  CB  CYS D 112     7795  12689   9966   3873   -784     68       C  
ATOM   5560  SG  CYS D 112      52.112  -2.651 -61.952  1.00 83.67           S  
ANISOU 5560  SG  CYS D 112     7712  13635  10444   3851   -757    -58       S  
ATOM   5561  N   GLY D 113      47.248  -3.054 -61.231  1.00 72.93           N  
ANISOU 5561  N   GLY D 113     7639  11048   9024   3255   -631    127       N  
ATOM   5562  CA  GLY D 113      45.957  -3.489 -60.674  1.00 72.33           C  
ANISOU 5562  CA  GLY D 113     7925  10654   8903   3159   -638    218       C  
ATOM   5563  C   GLY D 113      46.124  -4.350 -59.449  1.00 74.57           C  
ANISOU 5563  C   GLY D 113     8347  10882   9103   3368   -796    361       C  
ATOM   5564  O   GLY D 113      45.308  -5.285 -59.296  1.00 73.35           O  
ANISOU 5564  O   GLY D 113     8525  10414   8931   3426   -781    442       O  
ATOM   5565  N   ARG D 114      47.134  -4.048 -58.618  1.00 77.66           N  
ANISOU 5565  N   ARG D 114     8501  11570   9438   3466   -944    394       N  
ATOM   5566  CA  ARG D 114      47.228  -4.618 -57.246  1.00 79.95           C  
ANISOU 5566  CA  ARG D 114     8915  11846   9615   3609  -1119    543       C  
ATOM   5567  C   ARG D 114      46.402  -3.712 -56.324  1.00 78.30           C  
ANISOU 5567  C   ARG D 114     8787  11651   9314   3279  -1154    571       C  
ATOM   5568  O   ARG D 114      46.543  -2.450 -56.391  1.00 76.82           O  
ANISOU 5568  O   ARG D 114     8382  11680   9128   3029  -1133    474       O  
ATOM   5569  CB  ARG D 114      48.673  -4.857 -56.801  1.00 84.37           C  
ANISOU 5569  CB  ARG D 114     9196  12715  10145   3903  -1272    572       C  
ATOM   5570  CG  ARG D 114      49.589  -3.653 -56.954  1.00 86.10           C  
ANISOU 5570  CG  ARG D 114     8994  13343  10376   3758  -1292    459       C  
ATOM   5571  CD  ARG D 114      50.942  -3.872 -56.285  1.00 91.32           C  
ANISOU 5571  CD  ARG D 114     9371  14345  10981   4025  -1474    503       C  
ATOM   5572  NE  ARG D 114      52.034  -4.215 -57.197  1.00 94.58           N  
ANISOU 5572  NE  ARG D 114     9506  14950  11481   4288  -1431    428       N  
ATOM   5573  CZ  ARG D 114      52.698  -3.357 -57.981  1.00 94.67           C  
ANISOU 5573  CZ  ARG D 114     9173  15245  11553   4152  -1349    290       C  
ATOM   5574  NH1 ARG D 114      53.671  -3.801 -58.760  1.00 97.15           N1+
ANISOU 5574  NH1 ARG D 114     9247  15732  11935   4425  -1305    231       N1+
ATOM   5575  NH2 ARG D 114      52.378  -2.068 -57.998  1.00 91.65           N  
ANISOU 5575  NH2 ARG D 114     8700  14965  11159   3748  -1301    212       N  
ATOM   5576  N   HIS D 115      45.508  -4.330 -55.548  1.00 78.11           N  
ANISOU 5576  N   HIS D 115     9086  11382   9209   3265  -1188    692       N  
ATOM   5577  CA  HIS D 115      44.519  -3.632 -54.687  1.00 75.20           C  
ANISOU 5577  CA  HIS D 115     8852  10976   8745   2966  -1194    723       C  
ATOM   5578  C   HIS D 115      44.051  -4.562 -53.563  1.00 76.08           C  
ANISOU 5578  C   HIS D 115     9262  10910   8734   3064  -1291    893       C  
ATOM   5579  O   HIS D 115      44.094  -5.790 -53.760  1.00 77.20           O  
ANISOU 5579  O   HIS D 115     9597  10840   8897   3306  -1296    975       O  
ATOM   5580  CB  HIS D 115      43.309  -3.178 -55.507  1.00 72.10           C  
ANISOU 5580  CB  HIS D 115     8585  10391   8420   2700  -1013    643       C  
ATOM   5581  CG  HIS D 115      42.622  -4.312 -56.197  1.00 71.76           C  
ANISOU 5581  CG  HIS D 115     8812  10020   8435   2797   -916    679       C  
ATOM   5582  CD2 HIS D 115      42.711  -4.740 -57.472  1.00 71.76           C  
ANISOU 5582  CD2 HIS D 115     8809   9908   8549   2888   -804    603       C  
ATOM   5583  ND1 HIS D 115      41.774  -5.199 -55.555  1.00 72.67           N  
ANISOU 5583  ND1 HIS D 115     9255   9881   8475   2804   -931    805       N  
ATOM   5584  CE1 HIS D 115      41.330  -6.089 -56.423  1.00 73.07           C  
ANISOU 5584  CE1 HIS D 115     9498   9668   8597   2873   -832    799       C  
ATOM   5585  NE2 HIS D 115      41.899  -5.834 -57.606  1.00 72.36           N  
ANISOU 5585  NE2 HIS D 115     9212   9660   8623   2935   -755    673       N  
ATOM   5586  N   ASN D 116      43.628  -3.984 -52.438  1.00 74.73           N  
ANISOU 5586  N   ASN D 116     9141  10819   8433   2880  -1361    941       N  
ATOM   5587  CA  ASN D 116      42.866  -4.670 -51.358  1.00 74.68           C  
ANISOU 5587  CA  ASN D 116     9453  10630   8291   2872  -1414   1097       C  
ATOM   5588  C   ASN D 116      41.382  -4.533 -51.707  1.00 70.84           C  
ANISOU 5588  C   ASN D 116     9185   9904   7827   2605  -1246   1071       C  
ATOM   5589  O   ASN D 116      40.933  -3.404 -51.989  1.00 69.55           O  
ANISOU 5589  O   ASN D 116     8899   9834   7692   2355  -1160    955       O  
ATOM   5590  CB  ASN D 116      43.141  -4.094 -49.958  1.00 75.86           C  
ANISOU 5590  CB  ASN D 116     9543  11008   8271   2800  -1567   1154       C  
ATOM   5591  CG  ASN D 116      44.615  -4.052 -49.588  1.00 78.39           C  
ANISOU 5591  CG  ASN D 116     9595  11631   8559   3026  -1746   1165       C  
ATOM   5592  ND2 ASN D 116      45.074  -2.930 -49.047  1.00 77.66           N  
ANISOU 5592  ND2 ASN D 116     9271  11839   8399   2868  -1825   1091       N  
ATOM   5593  OD1 ASN D 116      45.335  -5.029 -49.788  1.00 79.90           O  
ANISOU 5593  OD1 ASN D 116     9788  11787   8782   3344  -1815   1236       O  
ATOM   5594  N   LEU D 117      40.647  -5.637 -51.729  1.00 69.59           N  
ANISOU 5594  N   LEU D 117     9339   9447   7656   2654  -1198   1173       N  
ATOM   5595  CA  LEU D 117      39.195  -5.611 -52.027  1.00 67.10           C  
ANISOU 5595  CA  LEU D 117     9227   8919   7350   2396  -1044   1158       C  
ATOM   5596  C   LEU D 117      38.425  -5.852 -50.728  1.00 67.61           C  
ANISOU 5596  C   LEU D 117     9526   8920   7243   2278  -1084   1294       C  
ATOM   5597  O   LEU D 117      38.790  -6.799 -50.027  1.00 71.35           O  
ANISOU 5597  O   LEU D 117    10172   9309   7628   2464  -1192   1440       O  
ATOM   5598  CB  LEU D 117      38.870  -6.680 -53.070  1.00 67.01           C  
ANISOU 5598  CB  LEU D 117     9401   8618   7442   2491   -946   1161       C  
ATOM   5599  CG  LEU D 117      37.441  -6.628 -53.608  1.00 65.16           C  
ANISOU 5599  CG  LEU D 117     9323   8198   7237   2221   -785   1120       C  
ATOM   5600  CD1 LEU D 117      37.282  -5.496 -54.600  1.00 62.29           C  
ANISOU 5600  CD1 LEU D 117     8718   7968   6982   2065   -681    951       C  
ATOM   5601  CD2 LEU D 117      37.021  -7.948 -54.236  1.00 66.70           C  
ANISOU 5601  CD2 LEU D 117     9800   8067   7475   2299   -722   1169       C  
ATOM   5602  N   GLN D 118      37.415  -5.027 -50.427  1.00 65.37           N  
ANISOU 5602  N   GLN D 118     9252   8679   6908   1994   -999   1249       N  
ATOM   5603  CA  GLN D 118      36.347  -5.361 -49.440  1.00 64.90           C  
ANISOU 5603  CA  GLN D 118     9450   8512   6698   1835   -974   1365       C  
ATOM   5604  C   GLN D 118      34.983  -5.380 -50.127  1.00 61.63           C  
ANISOU 5604  C   GLN D 118     9148   7929   6341   1607   -794   1316       C  
ATOM   5605  O   GLN D 118      34.699  -4.487 -50.948  1.00 59.60           O  
ANISOU 5605  O   GLN D 118     8712   7748   6186   1486   -700   1172       O  
ATOM   5606  CB  GLN D 118      36.310  -4.392 -48.260  1.00 65.37           C  
ANISOU 5606  CB  GLN D 118     9426   8803   6608   1706  -1036   1362       C  
ATOM   5607  CG  GLN D 118      37.576  -4.406 -47.423  1.00 68.03           C  
ANISOU 5607  CG  GLN D 118     9666   9330   6854   1904  -1230   1424       C  
ATOM   5608  CD  GLN D 118      38.218  -3.067 -47.647  1.00 67.86           C  
ANISOU 5608  CD  GLN D 118     9325   9577   6883   1840  -1254   1264       C  
ATOM   5609  NE2 GLN D 118      39.148  -2.994 -48.600  1.00 68.98           N  
ANISOU 5609  NE2 GLN D 118     9257   9783   7171   1984  -1273   1182       N  
ATOM   5610  OE1 GLN D 118      37.792  -2.095 -47.027  1.00 66.42           O  
ANISOU 5610  OE1 GLN D 118     9101   9527   6609   1643  -1236   1207       O  
ATOM   5611  N   ARG D 119      34.172  -6.369 -49.778  1.00 61.40           N  
ANISOU 5611  N   ARG D 119     9409   7683   6236   1546   -754   1439       N  
ATOM   5612  CA  ARG D 119      32.853  -6.632 -50.386  1.00 60.22           C  
ANISOU 5612  CA  ARG D 119     9393   7364   6125   1328   -595   1415       C  
ATOM   5613  C   ARG D 119      31.803  -6.420 -49.309  1.00 60.57           C  
ANISOU 5613  C   ARG D 119     9554   7455   6006   1102   -548   1486       C  
ATOM   5614  O   ARG D 119      31.873  -7.116 -48.284  1.00 65.64           O  
ANISOU 5614  O   ARG D 119    10401   8037   6503   1143   -620   1640       O  
ATOM   5615  CB  ARG D 119      32.824  -8.063 -50.928  1.00 62.05           C  
ANISOU 5615  CB  ARG D 119     9881   7293   6401   1432   -581   1497       C  
ATOM   5616  CG  ARG D 119      31.502  -8.477 -51.566  1.00 61.78           C  
ANISOU 5616  CG  ARG D 119     9999   7076   6396   1195   -430   1477       C  
ATOM   5617  CD  ARG D 119      31.555  -9.805 -52.303  1.00 64.02           C  
ANISOU 5617  CD  ARG D 119    10530   7052   6744   1292   -411   1520       C  
ATOM   5618  NE  ARG D 119      32.227  -9.703 -53.607  1.00 64.24           N  
ANISOU 5618  NE  ARG D 119    10403   7066   6939   1445   -396   1385       N  
ATOM   5619  CZ  ARG D 119      33.409 -10.249 -53.933  1.00 65.95           C  
ANISOU 5619  CZ  ARG D 119    10625   7216   7218   1749   -479   1392       C  
ATOM   5620  NH1 ARG D 119      34.099 -10.970 -53.061  1.00 68.69           N1+
ANISOU 5620  NH1 ARG D 119    11129   7492   7478   1959   -600   1535       N1+
ATOM   5621  NH2 ARG D 119      33.902 -10.063 -55.144  1.00 64.61           N  
ANISOU 5621  NH2 ARG D 119    10298   7062   7189   1853   -441   1257       N  
ATOM   5622  N   ILE D 120      30.886  -5.486 -49.518  1.00 58.22           N  
ANISOU 5622  N   ILE D 120     9130   7268   5721    886   -433   1381       N  
ATOM   5623  CA  ILE D 120      29.656  -5.368 -48.690  1.00 58.89           C  
ANISOU 5623  CA  ILE D 120     9326   7386   5663    651   -345   1433       C  
ATOM   5624  C   ILE D 120      28.544  -6.141 -49.385  1.00 59.41           C  
ANISOU 5624  C   ILE D 120     9542   7258   5772    489   -217   1451       C  
ATOM   5625  O   ILE D 120      28.190  -5.766 -50.507  1.00 58.50           O  
ANISOU 5625  O   ILE D 120     9294   7140   5792    433   -136   1328       O  
ATOM   5626  CB  ILE D 120      29.261  -3.900 -48.475  1.00 57.11           C  
ANISOU 5626  CB  ILE D 120     8880   7401   5417    527   -291   1305       C  
ATOM   5627  CG1 ILE D 120      30.419  -3.078 -47.905  1.00 57.35           C  
ANISOU 5627  CG1 ILE D 120     8754   7622   5414    664   -421   1264       C  
ATOM   5628  CG2 ILE D 120      28.027  -3.809 -47.598  1.00 57.83           C  
ANISOU 5628  CG2 ILE D 120     9074   7547   5352    312   -194   1354       C  
ATOM   5629  CD1 ILE D 120      30.118  -1.600 -47.809  1.00 55.68           C  
ANISOU 5629  CD1 ILE D 120     8348   7613   5196    551   -367   1121       C  
ATOM   5630  N   GLN D 121      28.019  -7.179 -48.745  1.00 62.62           N  
ANISOU 5630  N   GLN D 121    10221   7513   6059    404   -202   1600       N  
ATOM   5631  CA  GLN D 121      26.718  -7.747 -49.156  1.00 63.98           C  
ANISOU 5631  CA  GLN D 121    10524   7559   6228    163    -64   1615       C  
ATOM   5632  C   GLN D 121      25.658  -6.857 -48.512  1.00 64.01           C  
ANISOU 5632  C   GLN D 121    10412   7782   6125    -58     37   1578       C  
ATOM   5633  O   GLN D 121      25.643  -6.773 -47.282  1.00 65.78           O  
ANISOU 5633  O   GLN D 121    10712   8099   6183    -84      7   1669       O  
ATOM   5634  CB  GLN D 121      26.597  -9.213 -48.770  1.00 67.29           C  
ANISOU 5634  CB  GLN D 121    11296   7713   6560    141    -81   1788       C  
ATOM   5635  CG  GLN D 121      25.845 -10.019 -49.816  1.00 68.48           C  
ANISOU 5635  CG  GLN D 121    11574   7647   6797     -5     18   1763       C  
ATOM   5636  CD  GLN D 121      26.753 -10.496 -50.929  1.00 69.41           C  
ANISOU 5636  CD  GLN D 121    11708   7587   7077    218    -40   1704       C  
ATOM   5637  NE2 GLN D 121      26.181 -10.686 -52.114  1.00 68.48           N  
ANISOU 5637  NE2 GLN D 121    11572   7375   7071    103     49   1604       N  
ATOM   5638  OE1 GLN D 121      27.946 -10.741 -50.731  1.00 70.73           O  
ANISOU 5638  OE1 GLN D 121    11908   7704   7260    493   -163   1749       O  
ATOM   5639  N   CYS D 122      24.844  -6.176 -49.314  1.00 63.36           N  
ANISOU 5639  N   CYS D 122    10147   7796   6131   -191    148   1447       N  
ATOM   5640  CA  CYS D 122      23.734  -5.316 -48.828  1.00 63.99           C  
ANISOU 5640  CA  CYS D 122    10100   8090   6121   -384    261   1396       C  
ATOM   5641  C   CYS D 122      22.520  -6.167 -48.423  1.00 67.87           C  
ANISOU 5641  C   CYS D 122    10771   8523   6493   -635    368   1500       C  
ATOM   5642  O   CYS D 122      21.498  -5.569 -48.050  1.00 67.61           O  
ANISOU 5642  O   CYS D 122    10629   8678   6381   -802    478   1462       O  
ATOM   5643  CB  CYS D 122      23.318  -4.313 -49.892  1.00 61.20           C  
ANISOU 5643  CB  CYS D 122     9491   7855   5907   -408    332   1226       C  
ATOM   5644  SG  CYS D 122      24.725  -3.438 -50.612  1.00 58.63           S  
ANISOU 5644  SG  CYS D 122     8973   7565   5737   -154    223   1106       S  
ATOM   5645  N   ARG D 123      22.621  -7.502 -48.509  1.00 73.07           N  
ANISOU 5645  N   ARG D 123    11695   8931   7137   -662    343   1622       N  
ATOM   5646  CA  ARG D 123      21.576  -8.448 -48.027  1.00 76.98           C  
ANISOU 5646  CA  ARG D 123    12411   9340   7499   -922    436   1745       C  
ATOM   5647  C   ARG D 123      20.189  -7.851 -48.315  1.00 77.77           C  
ANISOU 5647  C   ARG D 123    12315   9644   7592  -1169    590   1650       C  
ATOM   5648  O   ARG D 123      19.449  -7.624 -47.366  1.00 78.86           O  
ANISOU 5648  O   ARG D 123    12446   9946   7572  -1322    669   1697       O  
ATOM   5649  CB  ARG D 123      21.728  -8.718 -46.520  1.00 79.41           C  
ANISOU 5649  CB  ARG D 123    12900   9677   7595   -933    400   1902       C  
ATOM   5650  CG  ARG D 123      23.142  -9.017 -46.032  1.00 81.49           C  
ANISOU 5650  CG  ARG D 123    13292   9830   7841   -653    230   1989       C  
ATOM   5651  CD  ARG D 123      23.285 -10.204 -45.071  1.00 85.77           C  
ANISOU 5651  CD  ARG D 123    14195  10182   8213   -676    181   2205       C  
ATOM   5652  NE  ARG D 123      24.614 -10.810 -45.221  1.00 87.98           N  
ANISOU 5652  NE  ARG D 123    14609  10265   8554   -378     19   2271       N  
ATOM   5653  CZ  ARG D 123      25.011 -11.605 -46.238  1.00 89.01           C  
ANISOU 5653  CZ  ARG D 123    14852  10137   8832   -272    -11   2260       C  
ATOM   5654  NH1 ARG D 123      24.182 -11.952 -47.219  1.00 88.57           N1+
ANISOU 5654  NH1 ARG D 123    14812   9968   8871   -460    103   2191       N1+
ATOM   5655  NH2 ARG D 123      26.255 -12.058 -46.266  1.00 88.84           N  
ANISOU 5655  NH2 ARG D 123    14923   9980   8852     32   -158   2316       N  
ATOM   5656  N   SER D 124      19.872  -7.520 -49.570  1.00 78.22           N  
ANISOU 5656  N   SER D 124    12197   9718   7805  -1187    629   1516       N  
ATOM   5657  CA  SER D 124      18.575  -6.891 -49.937  1.00 78.97           C  
ANISOU 5657  CA  SER D 124    12072  10031   7901  -1387    762   1419       C  
ATOM   5658  C   SER D 124      17.499  -7.977 -49.904  1.00 80.74           C  
ANISOU 5658  C   SER D 124    12463  10175   8040  -1691    858   1507       C  
ATOM   5659  O   SER D 124      17.848  -9.135 -50.142  1.00 79.32           O  
ANISOU 5659  O   SER D 124    12547   9718   7873  -1716    813   1593       O  
ATOM   5660  CB  SER D 124      18.632  -6.190 -51.264  1.00 78.47           C  
ANISOU 5660  CB  SER D 124    11782  10015   8018  -1297    758   1260       C  
ATOM   5661  OG  SER D 124      17.785  -6.856 -52.185  1.00 84.75           O  
ANISOU 5661  OG  SER D 124    12600  10741   8861  -1495    824   1238       O  
ATOM   5662  N   GLU D 125      16.246  -7.573 -49.658  1.00 84.31           N  
ANISOU 5662  N   GLU D 125    12756  10867   8409  -1908    986   1477       N  
ATOM   5663  CA  GLU D 125      15.081  -8.454 -49.341  1.00 87.36           C  
ANISOU 5663  CA  GLU D 125    13262  11264   8669  -2248   1100   1566       C  
ATOM   5664  C   GLU D 125      14.622  -9.167 -50.625  1.00 48.70           C  
ATOM   5665  O   GLU D 125      15.149 -10.255 -50.925  1.00 88.55           O  
ANISOU 5665  O   GLU D 125    13724  10961   8958  -2410   1055   1590       O  
ATOM   5666  CB  GLU D 125      13.958  -7.626 -48.692  1.00 87.82           C  
ANISOU 5666  CB  GLU D 125    13081  11679   8608  -2389   1234   1527       C  
ATOM   5667  CG  GLU D 125      14.389  -6.818 -47.464  1.00 86.69           C  
ANISOU 5667  CG  GLU D 125    12904  11686   8349  -2233   1223   1548       C  
ATOM   5668  CD  GLU D 125      14.142  -7.456 -46.100  1.00 86.52           C  
ANISOU 5668  CD  GLU D 125    13103  11669   8103  -2393   1274   1710       C  
ATOM   5669  OE1 GLU D 125      12.972  -7.814 -45.825  1.00 89.03           O  
ANISOU 5669  OE1 GLU D 125    13400  12123   8306  -2681   1411   1749       O  
ATOM   5670  OE2 GLU D 125      15.108  -7.565 -45.288  1.00 82.74           O1-
ANISOU 5670  OE2 GLU D 125    12804  11080   7552  -2234   1177   1798       O1-
ATOM   5671  N   ASN D 126      13.680  -8.566 -51.346  1.00 85.30           N  
ANISOU 5671  N   ASN D 126    12750  11091   8571  -2514   1193   1397       N  
ATOM   5672  CA  ASN D 126      13.054  -9.125 -52.561  1.00 87.19           C  
ANISOU 5672  CA  ASN D 126    12969  11268   8892  -2699   1216   1335       C  
ATOM   5673  C   ASN D 126      13.876  -8.669 -53.764  1.00 85.01           C  
ANISOU 5673  C   ASN D 126    12600  10896   8804  -2445   1120   1213       C  
ATOM   5674  O   ASN D 126      14.822  -9.370 -54.158  1.00 88.14           O  
ANISOU 5674  O   ASN D 126    13223  10995   9271  -2326   1032   1240       O  
ATOM   5675  CB  ASN D 126      11.623  -8.614 -52.701  1.00 89.67           C  
ANISOU 5675  CB  ASN D 126    12991  11925   9155  -2925   1338   1266       C  
ATOM   5676  CG  ASN D 126      10.582  -9.693 -52.563  1.00 93.35           C  
ANISOU 5676  CG  ASN D 126    13582  12381   9506  -3321   1428   1344       C  
ATOM   5677  ND2 ASN D 126      10.436 -10.222 -51.356  1.00 94.14           N  
ANISOU 5677  ND2 ASN D 126    13872  12455   9443  -3463   1483   1484       N  
ATOM   5678  OD1 ASN D 126       9.930 -10.027 -53.554  1.00 94.96           O  
ANISOU 5678  OD1 ASN D 126    13714  12606   9762  -3504   1446   1277       O  
ATOM   5679  N   SER D 127      13.546  -7.500 -54.302  1.00 81.51           N  
ANISOU 5679  N   SER D 127    11835  10702   8432  -2350   1138   1085       N  
ATOM   5680  CA  SER D 127      14.374  -6.807 -55.319  1.00 79.43           C  
ANISOU 5680  CA  SER D 127    11456  10394   8332  -2087   1055    972       C  
ATOM   5681  C   SER D 127      15.838  -6.810 -54.841  1.00 76.61           C  
ANISOU 5681  C   SER D 127    11258   9844   8007  -1819    953   1020       C  
ATOM   5682  O   SER D 127      16.053  -6.497 -53.664  1.00 76.85           O  
ANISOU 5682  O   SER D 127    11312   9948   7941  -1762    956   1086       O  
ATOM   5683  CB  SER D 127      13.841  -5.418 -55.565  1.00 78.54           C  
ANISOU 5683  CB  SER D 127    11006  10586   8251  -2003   1095    860       C  
ATOM   5684  OG  SER D 127      12.808  -5.435 -56.554  1.00 78.19           O  
ANISOU 5684  OG  SER D 127    10800  10673   8236  -2171   1141    785       O  
ATOM   5685  N   LYS D 128      16.796  -7.178 -55.706  1.00 73.38           N  
ANISOU 5685  N   LYS D 128    10951   9213   7719  -1664    869    987       N  
ATOM   5686  CA  LYS D 128      18.264  -7.135 -55.433  1.00 71.67           C  
ANISOU 5686  CA  LYS D 128    10838   8843   7553  -1381    764   1015       C  
ATOM   5687  C   LYS D 128      18.926  -6.080 -56.335  1.00 67.42           C  
ANISOU 5687  C   LYS D 128    10079   8385   7153  -1163    719    883       C  
ATOM   5688  O   LYS D 128      18.512  -5.967 -57.513  1.00 68.85           O  
ANISOU 5688  O   LYS D 128    10158   8587   7417  -1216    743    789       O  
ATOM   5689  CB  LYS D 128      18.905  -8.506 -55.668  1.00 73.68           C  
ANISOU 5689  CB  LYS D 128    11405   8767   7825  -1361    708   1089       C  
ATOM   5690  CG  LYS D 128      18.168  -9.673 -55.027  1.00 79.61           C  
ANISOU 5690  CG  LYS D 128    12415   9388   8446  -1619    760   1216       C  
ATOM   5691  CD  LYS D 128      18.871 -10.329 -53.867  1.00 83.79           C  
ANISOU 5691  CD  LYS D 128    13206   9754   8876  -1530    703   1371       C  
ATOM   5692  CE  LYS D 128      19.997 -11.210 -54.368  1.00 86.36           C  
ANISOU 5692  CE  LYS D 128    13770   9761   9283  -1327    609   1396       C  
ATOM   5693  NZ  LYS D 128      20.912 -11.594 -53.271  1.00 88.86           N1+
ANISOU 5693  NZ  LYS D 128    14282   9961   9520  -1146    524   1536       N1+
ATOM   5694  N   GLY D 129      19.907  -5.335 -55.806  1.00 60.89           N  
ANISOU 5694  N   GLY D 129     9187   7607   6340   -943    655    878       N  
ATOM   5695  CA  GLY D 129      20.807  -4.469 -56.589  1.00 56.59           C  
ANISOU 5695  CA  GLY D 129     8485   7095   5923   -730    601    773       C  
ATOM   5696  C   GLY D 129      21.004  -3.106 -55.966  1.00 53.17           C  
ANISOU 5696  C   GLY D 129     7865   6870   5467   -630    596    728       C  
ATOM   5697  O   GLY D 129      20.130  -2.713 -55.185  1.00 56.28           O  
ANISOU 5697  O   GLY D 129     8204   7420   5758   -745    660    747       O  
ATOM   5698  N   VAL D 130      22.087  -2.407 -56.328  1.00 48.26           N  
ANISOU 5698  N   VAL D 130     7150   6255   4934   -435    530    664       N  
ATOM   5699  CA  VAL D 130      22.464  -1.072 -55.781  1.00 46.87           C  
ANISOU 5699  CA  VAL D 130     6820   6248   4741   -335    512    609       C  
ATOM   5700  C   VAL D 130      22.710  -0.090 -56.919  1.00 46.08           C  
ANISOU 5700  C   VAL D 130     6545   6203   4761   -255    517    488       C  
ATOM   5701  O   VAL D 130      23.790  -0.131 -57.539  1.00 48.31           O  
ANISOU 5701  O   VAL D 130     6819   6404   5134   -124    455    458       O  
ATOM   5702  CB  VAL D 130      23.708  -1.162 -54.901  1.00 46.95           C  
ANISOU 5702  CB  VAL D 130     6904   6220   4715   -190    411    665       C  
ATOM   5703  CG1 VAL D 130      24.073   0.197 -54.328  1.00 45.96           C  
ANISOU 5703  CG1 VAL D 130     6639   6263   4562   -121    392    599       C  
ATOM   5704  CG2 VAL D 130      23.530  -2.184 -53.802  1.00 49.65           C  
ANISOU 5704  CG2 VAL D 130     7447   6489   4929   -255    397    801       C  
ATOM   5705  N   TYR D 131      21.752   0.790 -57.157  1.00 45.31           N  
ANISOU 5705  N   TYR D 131     6311   6248   4655   -323    590    423       N  
ATOM   5706  CA  TYR D 131      21.685   1.602 -58.391  1.00 43.33           C  
ANISOU 5706  CA  TYR D 131     5918   6038   4507   -278    608    322       C  
ATOM   5707  C   TYR D 131      22.637   2.797 -58.321  1.00 41.58           C  
ANISOU 5707  C   TYR D 131     5610   5866   4324   -140    566    258       C  
ATOM   5708  O   TYR D 131      23.091   3.232 -59.376  1.00 41.06           O  
ANISOU 5708  O   TYR D 131     5474   5775   4352    -77    554    195       O  
ATOM   5709  CB  TYR D 131      20.250   2.049 -58.619  1.00 44.43           C  
ANISOU 5709  CB  TYR D 131     5951   6318   4611   -388    695    289       C  
ATOM   5710  CG  TYR D 131      19.366   1.072 -59.345  1.00 45.85           C  
ANISOU 5710  CG  TYR D 131     6161   6463   4798   -535    732    309       C  
ATOM   5711  CD1 TYR D 131      19.650   0.685 -60.636  1.00 45.76           C  
ANISOU 5711  CD1 TYR D 131     6159   6350   4879   -522    709    270       C  
ATOM   5712  CD2 TYR D 131      18.176   0.635 -58.793  1.00 48.09           C  
ANISOU 5712  CD2 TYR D 131     6447   6839   4986   -700    799    354       C  
ATOM   5713  CE1 TYR D 131      18.802  -0.147 -61.346  1.00 47.30           C  
ANISOU 5713  CE1 TYR D 131     6381   6520   5070   -674    739    272       C  
ATOM   5714  CE2 TYR D 131      17.318  -0.205 -59.489  1.00 49.38           C  
ANISOU 5714  CE2 TYR D 131     6624   6990   5149   -866    832    362       C  
ATOM   5715  CZ  TYR D 131      17.631  -0.602 -60.775  1.00 48.30           C  
ANISOU 5715  CZ  TYR D 131     6511   6737   5104   -855    797    318       C  
ATOM   5716  OH  TYR D 131      16.814  -1.448 -61.475  1.00 50.72           O  
ANISOU 5716  OH  TYR D 131     6846   7026   5401  -1033    822    317       O  
ATOM   5717  N   CYS D 132      22.921   3.309 -57.127  1.00 41.55           N  
ANISOU 5717  N   CYS D 132     5617   5931   4238   -110    545    273       N  
ATOM   5718  CA  CYS D 132      23.698   4.559 -56.912  1.00 39.64           C  
ANISOU 5718  CA  CYS D 132     5301   5751   4010    -17    511    203       C  
ATOM   5719  C   CYS D 132      24.464   4.531 -55.583  1.00 39.87           C  
ANISOU 5719  C   CYS D 132     5396   5804   3947     18    443    246       C  
ATOM   5720  O   CYS D 132      24.129   3.753 -54.689  1.00 39.94           O  
ANISOU 5720  O   CYS D 132     5505   5809   3860    -34    443    330       O  
ATOM   5721  CB  CYS D 132      22.775   5.768 -56.929  1.00 39.18           C  
ANISOU 5721  CB  CYS D 132     5152   5808   3925    -35    586    131       C  
ATOM   5722  SG  CYS D 132      21.399   5.632 -55.766  1.00 38.74           S  
ANISOU 5722  SG  CYS D 132     5120   5875   3724   -133    669    171       S  
ATOM   5723  N   LEU D 133      25.451   5.407 -55.454  1.00 39.33           N  
ANISOU 5723  N   LEU D 133     5276   5769   3899     90    386    188       N  
ATOM   5724  CA  LEU D 133      26.232   5.555 -54.205  1.00 40.48           C  
ANISOU 5724  CA  LEU D 133     5466   5968   3948    119    308    212       C  
ATOM   5725  C   LEU D 133      27.006   6.876 -54.223  1.00 38.77           C  
ANISOU 5725  C   LEU D 133     5168   5813   3752    152    275    113       C  
ATOM   5726  O   LEU D 133      27.209   7.447 -55.314  1.00 36.91           O  
ANISOU 5726  O   LEU D 133     4853   5549   3623    169    296     46       O  
ATOM   5727  CB  LEU D 133      27.178   4.361 -54.054  1.00 42.36           C  
ANISOU 5727  CB  LEU D 133     5769   6130   4197    185    214    302       C  
ATOM   5728  CG  LEU D 133      28.388   4.365 -54.989  1.00 42.69           C  
ANISOU 5728  CG  LEU D 133     5727   6132   4361    282    152    265       C  
ATOM   5729  CD1 LEU D 133      29.548   5.148 -54.409  1.00 43.11           C  
ANISOU 5729  CD1 LEU D 133     5708   6286   4386    328     62    223       C  
ATOM   5730  CD2 LEU D 133      28.828   2.936 -55.292  1.00 44.45           C  
ANISOU 5730  CD2 LEU D 133     6029   6236   4623    357    107    352       C  
ATOM   5731  N   GLN D 134      27.422   7.311 -53.033  1.00 38.70           N  
ANISOU 5731  N   GLN D 134     5191   5882   3630    146    222    106       N  
ATOM   5732  CA  GLN D 134      28.416   8.385 -52.817  1.00 38.91           C  
ANISOU 5732  CA  GLN D 134     5165   5967   3652    156    159     22       C  
ATOM   5733  C   GLN D 134      29.140   8.078 -51.504  1.00 40.66           C  
ANISOU 5733  C   GLN D 134     5438   6264   3747    164     54     70       C  
ATOM   5734  O   GLN D 134      28.492   7.490 -50.605  1.00 42.08           O  
ANISOU 5734  O   GLN D 134     5714   6461   3811    143     70    142       O  
ATOM   5735  CB  GLN D 134      27.689   9.728 -52.824  1.00 38.53           C  
ANISOU 5735  CB  GLN D 134     5115   5944   3580    112    244    -82       C  
ATOM   5736  CG  GLN D 134      28.569  10.945 -52.546  1.00 38.71           C  
ANISOU 5736  CG  GLN D 134     5120   6007   3581     88    194   -181       C  
ATOM   5737  CD  GLN D 134      27.748  12.216 -52.573  1.00 38.12           C  
ANISOU 5737  CD  GLN D 134     5084   5921   3480     65    288   -280       C  
ATOM   5738  NE2 GLN D 134      28.082  13.135 -51.684  1.00 38.73           N  
ANISOU 5738  NE2 GLN D 134     5218   6041   3456     25    261   -357       N  
ATOM   5739  OE1 GLN D 134      26.813  12.372 -53.370  1.00 36.51           O  
ANISOU 5739  OE1 GLN D 134     4864   5670   3338     89    380   -289       O  
ATOM   5740  N   TYR D 135      30.415   8.445 -51.378  1.00 41.40           N  
ANISOU 5740  N   TYR D 135     5466   6416   3850    186    -51     35       N  
ATOM   5741  CA  TYR D 135      31.195   8.210 -50.132  1.00 43.36           C  
ANISOU 5741  CA  TYR D 135     5746   6763   3967    199   -174     78       C  
ATOM   5742  C   TYR D 135      32.029   9.428 -49.747  1.00 43.28           C  
ANISOU 5742  C   TYR D 135     5677   6855   3913    141   -237    -32       C  
ATOM   5743  O   TYR D 135      32.119  10.384 -50.539  1.00 41.99           O  
ANISOU 5743  O   TYR D 135     5454   6665   3837     95   -188   -132       O  
ATOM   5744  CB  TYR D 135      32.080   6.967 -50.262  1.00 44.44           C  
ANISOU 5744  CB  TYR D 135     5857   6885   4143    309   -276    184       C  
ATOM   5745  CG  TYR D 135      33.282   7.095 -51.161  1.00 44.58           C  
ANISOU 5745  CG  TYR D 135     5722   6928   4286    367   -337    141       C  
ATOM   5746  CD1 TYR D 135      34.429   7.732 -50.719  1.00 45.75           C  
ANISOU 5746  CD1 TYR D 135     5771   7218   4395    353   -446     88       C  
ATOM   5747  CD2 TYR D 135      33.293   6.542 -52.433  1.00 43.41           C  
ANISOU 5747  CD2 TYR D 135     5527   6681   4287    429   -286    153       C  
ATOM   5748  CE1 TYR D 135      35.545   7.851 -51.529  1.00 45.59           C  
ANISOU 5748  CE1 TYR D 135     5588   7252   4482    393   -494     48       C  
ATOM   5749  CE2 TYR D 135      34.409   6.636 -53.241  1.00 43.82           C  
ANISOU 5749  CE2 TYR D 135     5432   6776   4443    485   -330    112       C  
ATOM   5750  CZ  TYR D 135      35.545   7.285 -52.789  1.00 44.87           C  
ANISOU 5750  CZ  TYR D 135     5448   7064   4537    468   -432     63       C  
ATOM   5751  OH  TYR D 135      36.657   7.398 -53.577  1.00 44.95           O  
ANISOU 5751  OH  TYR D 135     5290   7146   4642    509   -467     21       O  
ATOM   5752  N   ASP D 136      32.580   9.355 -48.534  1.00 45.18           N  
ANISOU 5752  N   ASP D 136     5953   7206   4009    132   -345     -7       N  
ATOM   5753  CA  ASP D 136      33.593  10.277 -47.953  1.00 47.57           C  
ANISOU 5753  CA  ASP D 136     6201   7636   4237     66   -448    -96       C  
ATOM   5754  C   ASP D 136      34.481   9.488 -46.986  1.00 24.46           C  
ATOM   5755  O   ASP D 136      34.309   8.251 -46.903  1.00 50.21           O  
ANISOU 5755  O   ASP D 136     6572   8047   4458    231   -629    130       O  
ATOM   5756  CB  ASP D 136      32.944  11.469 -47.242  1.00 47.57           C  
ANISOU 5756  CB  ASP D 136     6305   7652   4119    -44   -385   -207       C  
ATOM   5757  CG  ASP D 136      31.878  11.080 -46.240  1.00 47.66           C  
ANISOU 5757  CG  ASP D 136     6461   7666   3981    -41   -329   -152       C  
ATOM   5758  OD1 ASP D 136      32.135  10.170 -45.432  1.00 48.16           O  
ANISOU 5758  OD1 ASP D 136     6565   7793   3940      0   -416    -43       O  
ATOM   5759  OD2 ASP D 136      30.799  11.683 -46.295  1.00 47.00           O1-
ANISOU 5759  OD2 ASP D 136     6448   7528   3884    -73   -196   -214       O1-
ATOM   5760  N   ASP D 137      35.379  10.182 -46.277  1.00 53.71           N  
ANISOU 5760  N   ASP D 137     6919   8684   4803     58   -724    -72       N  
ATOM   5761  CA  ASP D 137      36.271   9.584 -45.254  1.00 57.41           C  
ANISOU 5761  CA  ASP D 137     7369   9308   5138    112   -898      7       C  
ATOM   5762  C   ASP D 137      35.449   8.727 -44.284  1.00 27.47           C  
ATOM   5763  O   ASP D 137      35.963   7.680 -43.887  1.00 58.41           O  
ANISOU 5763  O   ASP D 137     7677   9445   5072    277  -1001    261       O  
ATOM   5764  CB  ASP D 137      37.074  10.668 -44.524  1.00 61.42           C  
ANISOU 5764  CB  ASP D 137     7827   9982   5526    -19  -1002   -110       C  
ATOM   5765  CG  ASP D 137      38.340  11.095 -45.257  1.00 64.59           C  
ANISOU 5765  CG  ASP D 137     8015  10486   6038    -49  -1082   -179       C  
ATOM   5766  OD1 ASP D 137      38.324  11.044 -46.534  1.00 63.50           O  
ANISOU 5766  OD1 ASP D 137     7791  10248   6088    -15   -993   -190       O  
ATOM   5767  OD2 ASP D 137      39.347  11.464 -44.538  1.00 69.11           O1-
ANISOU 5767  OD2 ASP D 137     8503  11257   6500   -116  -1234   -220       O1-
ATOM   5768  N   GLU D 138      34.213   9.126 -43.950  1.00 57.28           N  
ANISOU 5768  N   GLU D 138     7671   9188   4906     82   -752     94       N  
ATOM   5769  CA  GLU D 138      33.437   8.568 -42.805  1.00 57.93           C  
ANISOU 5769  CA  GLU D 138     7926   9284   4801     78   -734    187       C  
ATOM   5770  C   GLU D 138      32.324   7.599 -43.223  1.00 55.70           C  
ANISOU 5770  C   GLU D 138     7732   8855   4577    123   -607    297       C  
ATOM   5771  O   GLU D 138      32.014   6.691 -42.432  1.00 56.85           O  
ANISOU 5771  O   GLU D 138     8004   9003   4593    149   -629    429       O  
ATOM   5772  CB  GLU D 138      32.819   9.706 -42.010  1.00 58.52           C  
ANISOU 5772  CB  GLU D 138     8094   9414   4727    -47   -663     61       C  
ATOM   5773  CG  GLU D 138      33.862  10.561 -41.340  1.00 60.50           C  
ANISOU 5773  CG  GLU D 138     8303   9816   4868   -120   -801    -40       C  
ATOM   5774  CD  GLU D 138      33.221  11.297 -40.184  1.00 62.97           C  
ANISOU 5774  CD  GLU D 138     8770  10190   4965   -219   -752   -123       C  
ATOM   5775  OE1 GLU D 138      33.605  11.043 -39.018  1.00 66.13           O  
ANISOU 5775  OE1 GLU D 138     9239  10725   5162   -234   -868    -77       O  
ATOM   5776  OE2 GLU D 138      32.264  12.054 -40.461  1.00 63.55           O1-
ANISOU 5776  OE2 GLU D 138     8901  10176   5068   -265   -590   -225       O1-
ATOM   5777  N   LYS D 139      31.702   7.770 -44.380  1.00 52.30           N  
ANISOU 5777  N   LYS D 139     7250   8304   4318    117   -477    250       N  
ATOM   5778  CA  LYS D 139      30.560   6.890 -44.714  1.00 50.91           C  
ANISOU 5778  CA  LYS D 139     7157   8009   4177    126   -355    343       C  
ATOM   5779  C   LYS D 139      30.425   6.698 -46.220  1.00 48.69           C  
ANISOU 5779  C   LYS D 139     6782   7602   4117    165   -287    325       C  
ATOM   5780  O   LYS D 139      30.976   7.506 -47.007  1.00 46.87           O  
ANISOU 5780  O   LYS D 139     6428   7375   4004    166   -295    218       O  
ATOM   5781  CB  LYS D 139      29.267   7.492 -44.165  1.00 50.85           C  
ANISOU 5781  CB  LYS D 139     7234   8028   4058     29   -211    287       C  
ATOM   5782  CG  LYS D 139      28.844   8.780 -44.860  1.00 49.46           C  
ANISOU 5782  CG  LYS D 139     6982   7835   3975    -11   -107    126       C  
ATOM   5783  CD  LYS D 139      27.796   9.576 -44.138  1.00 49.82           C  
ANISOU 5783  CD  LYS D 139     7104   7939   3886    -75     13     45       C  
ATOM   5784  CE  LYS D 139      27.606  10.945 -44.762  1.00 49.30           C  
ANISOU 5784  CE  LYS D 139     6985   7845   3904    -87     86   -118       C  
ATOM   5785  NZ  LYS D 139      28.697  11.891 -44.420  1.00 50.16           N1+
ANISOU 5785  NZ  LYS D 139     7088   7999   3973   -120    -20   -224       N1+
ATOM   5786  N   ILE D 140      29.675   5.651 -46.561  1.00 48.12           N  
ANISOU 5786  N   ILE D 140     6780   7421   4080    178   -219    427       N  
ATOM   5787  CA  ILE D 140      29.133   5.358 -47.917  1.00 45.90           C  
ANISOU 5787  CA  ILE D 140     6448   7016   3975    185   -122    416       C  
ATOM   5788  C   ILE D 140      27.609   5.372 -47.806  1.00 44.81           C  
ANISOU 5788  C   ILE D 140     6374   6865   3786     88     29    418       C  
ATOM   5789  O   ILE D 140      27.061   4.592 -46.980  1.00 44.92           O  
ANISOU 5789  O   ILE D 140     6513   6882   3672     44     48    524       O  
ATOM   5790  CB  ILE D 140      29.621   3.985 -48.414  1.00 46.42           C  
ANISOU 5790  CB  ILE D 140     6553   6966   4118    279   -183    534       C  
ATOM   5791  CG1 ILE D 140      31.140   3.818 -48.290  1.00 47.04           C  
ANISOU 5791  CG1 ILE D 140     6565   7095   4214    402   -343    553       C  
ATOM   5792  CG2 ILE D 140      29.106   3.712 -49.820  1.00 45.11           C  
ANISOU 5792  CG2 ILE D 140     6341   6679   4120    275    -89    507       C  
ATOM   5793  CD1 ILE D 140      31.579   2.374 -48.184  1.00 48.16           C  
ANISOU 5793  CD1 ILE D 140     6809   7139   4350    520   -423    700       C  
ATOM   5794  N   ILE D 141      26.960   6.203 -48.616  1.00 42.88           N  
ANISOU 5794  N   ILE D 141     6044   6615   3633     56    132    313       N  
ATOM   5795  CA  ILE D 141      25.478   6.199 -48.757  1.00 43.07           C  
ANISOU 5795  CA  ILE D 141     6082   6645   3637    -20    280    308       C  
ATOM   5796  C   ILE D 141      25.138   5.584 -50.104  1.00 41.27           C  
ANISOU 5796  C   ILE D 141     5805   6308   3567    -15    322    329       C  
ATOM   5797  O   ILE D 141      25.830   5.918 -51.069  1.00 40.47           O  
ANISOU 5797  O   ILE D 141     5620   6157   3600     45    284    272       O  
ATOM   5798  CB  ILE D 141      24.895   7.616 -48.615  1.00 42.80           C  
ANISOU 5798  CB  ILE D 141     5995   6697   3569    -37    364    175       C  
ATOM   5799  CG1 ILE D 141      25.443   8.279 -47.348  1.00 44.09           C  
ANISOU 5799  CG1 ILE D 141     6219   6955   3577    -42    304    134       C  
ATOM   5800  CG2 ILE D 141      23.373   7.575 -48.672  1.00 42.54           C  
ANISOU 5800  CG2 ILE D 141     5952   6710   3502    -95    511    175       C  
ATOM   5801  CD1 ILE D 141      24.775   9.569 -46.956  1.00 44.22           C  
ANISOU 5801  CD1 ILE D 141     6235   7047   3521    -57    397      6       C  
ATOM   5802  N   SER D 142      24.093   4.756 -50.139  1.00 41.24           N  
ANISOU 5802  N   SER D 142     5853   6282   3535    -93    403    401       N  
ATOM   5803  CA  SER D 142      23.737   3.897 -51.293  1.00 40.93           C  
ANISOU 5803  CA  SER D 142     5804   6132   3617   -116    434    437       C  
ATOM   5804  C   SER D 142      22.220   3.884 -51.484  1.00 41.40           C  
ANISOU 5804  C   SER D 142     5829   6254   3649   -228    567    429       C  
ATOM   5805  O   SER D 142      21.510   3.949 -50.485  1.00 43.18           O  
ANISOU 5805  O   SER D 142     6091   6582   3734   -299    628    454       O  
ATOM   5806  CB  SER D 142      24.288   2.512 -51.098  1.00 41.41           C  
ANISOU 5806  CB  SER D 142     6000   6070   3665   -103    360    563       C  
ATOM   5807  OG  SER D 142      23.787   1.950 -49.914  1.00 41.36           O  
ANISOU 5807  OG  SER D 142     6121   6098   3496   -184    380    661       O  
ATOM   5808  N   GLY D 143      21.762   3.803 -52.737  1.00 40.56           N  
ANISOU 5808  N   GLY D 143     5644   6104   3663   -244    610    392       N  
ATOM   5809  CA  GLY D 143      20.346   3.620 -53.110  1.00 40.70           C  
ANISOU 5809  CA  GLY D 143     5606   6191   3668   -358    721    390       C  
ATOM   5810  C   GLY D 143      20.116   2.262 -53.750  1.00 41.38           C  
ANISOU 5810  C   GLY D 143     5769   6154   3798   -451    719    467       C  
ATOM   5811  O   GLY D 143      20.920   1.853 -54.617  1.00 40.88           O  
ANISOU 5811  O   GLY D 143     5733   5952   3847   -386    652    464       O  
ATOM   5812  N   LEU D 144      19.049   1.576 -53.345  1.00 42.60           N  
ANISOU 5812  N   LEU D 144     5963   6360   3862   -608    795    530       N  
ATOM   5813  CA  LEU D 144      18.861   0.140 -53.640  1.00 43.95           C  
ANISOU 5813  CA  LEU D 144     6272   6390   4037   -732    791    623       C  
ATOM   5814  C   LEU D 144      17.530  -0.079 -54.338  1.00 44.58           C  
ANISOU 5814  C   LEU D 144     6257   6555   4125   -894    885    599       C  
ATOM   5815  O   LEU D 144      16.646   0.791 -54.256  1.00 42.48           O  
ANISOU 5815  O   LEU D 144     5826   6489   3825   -912    962    536       O  
ATOM   5816  CB  LEU D 144      18.923  -0.643 -52.334  1.00 46.94           C  
ANISOU 5816  CB  LEU D 144     6830   6737   4270   -807    785    746       C  
ATOM   5817  CG  LEU D 144      20.315  -0.735 -51.712  1.00 47.76           C  
ANISOU 5817  CG  LEU D 144     7049   6737   4360   -650    667    793       C  
ATOM   5818  CD1 LEU D 144      20.645   0.535 -50.975  1.00 47.16           C  
ANISOU 5818  CD1 LEU D 144     6873   6816   4231   -550    654    725       C  
ATOM   5819  CD2 LEU D 144      20.428  -1.921 -50.760  1.00 50.57           C  
ANISOU 5819  CD2 LEU D 144     7636   6987   4593   -724    641    945       C  
ATOM   5820  N   ARG D 145      17.426  -1.229 -55.000  1.00 47.55           N  
ANISOU 5820  N   ARG D 145     6742   6783   4542  -1002    873    645       N  
ATOM   5821  CA  ARG D 145      16.259  -1.625 -55.817  1.00 50.16           C  
ANISOU 5821  CA  ARG D 145     6997   7175   4885  -1183    942    621       C  
ATOM   5822  C   ARG D 145      15.056  -1.894 -54.908  1.00 52.80           C  
ANISOU 5822  C   ARG D 145     7313   7674   5073  -1388   1044    679       C  
ATOM   5823  O   ARG D 145      13.900  -1.725 -55.373  1.00 52.63           O  
ANISOU 5823  O   ARG D 145     7128   7827   5040  -1517   1118    634       O  
ATOM   5824  CB  ARG D 145      16.615  -2.868 -56.618  1.00 52.46           C  
ANISOU 5824  CB  ARG D 145     7462   7230   5240  -1251    896    656       C  
ATOM   5825  CG  ARG D 145      15.591  -3.165 -57.694  1.00 55.39           C  
ANISOU 5825  CG  ARG D 145     7744   7659   5643  -1421    942    604       C  
ATOM   5826  CD  ARG D 145      16.073  -4.419 -58.368  1.00 58.34           C  
ANISOU 5826  CD  ARG D 145     8335   7765   6066  -1476    894    633       C  
ATOM   5827  NE  ARG D 145      15.249  -4.766 -59.501  1.00 61.71           N  
ANISOU 5827  NE  ARG D 145     8702   8220   6524  -1639    921    573       N  
ATOM   5828  CZ  ARG D 145      15.574  -4.543 -60.767  1.00 63.87           C  
ANISOU 5828  CZ  ARG D 145     8915   8450   6903  -1550    881    483       C  
ATOM   5829  NH1 ARG D 145      16.724  -3.959 -61.085  1.00 63.26           N1+
ANISOU 5829  NH1 ARG D 145     8820   8298   6915  -1302    821    442       N1+
ATOM   5830  NH2 ARG D 145      14.739  -4.925 -61.717  1.00 66.32           N  
ANISOU 5830  NH2 ARG D 145     9180   8802   7217  -1726    902    433       N  
ATOM   5831  N   ASP D 146      15.323  -2.270 -53.651  1.00 54.06           N  
ANISOU 5831  N   ASP D 146     7624   7801   5116  -1415   1047    775       N  
ATOM   5832  CA  ASP D 146      14.295  -2.531 -52.616  1.00 55.89           C  
ANISOU 5832  CA  ASP D 146     7861   8193   5184  -1611   1152    842       C  
ATOM   5833  C   ASP D 146      13.746  -1.200 -52.081  1.00 25.98           C  
ATOM   5834  O   ASP D 146      13.041  -1.235 -51.067  1.00 53.31           O  
ANISOU 5834  O   ASP D 146     7306   8299   4649  -1644   1316    807       O  
ATOM   5835  CB  ASP D 146      14.859  -3.466 -51.543  1.00 59.70           C  
ANISOU 5835  CB  ASP D 146     8615   8515   5555  -1661   1120    983       C  
ATOM   5836  CG  ASP D 146      15.794  -2.807 -50.539  1.00 60.93           C  
ANISOU 5836  CG  ASP D 146     8813   8684   5655  -1465   1061    996       C  
ATOM   5837  OD1 ASP D 146      16.020  -1.576 -50.680  1.00 60.25           O  
ANISOU 5837  OD1 ASP D 146     8550   8722   5622  -1298   1051    886       O  
ATOM   5838  OD2 ASP D 146      16.274  -3.528 -49.600  1.00 63.00           O1-
ANISOU 5838  OD2 ASP D 146     9295   8831   5809  -1488   1023   1120       O1-
ATOM   5839  N   ASN D 147      14.040  -0.069 -52.729  1.00 51.24           N  
ANISOU 5839  N   ASN D 147     6891   7933   4644  -1332   1193    647       N  
ATOM   5840  CA  ASN D 147      13.401   1.242 -52.423  1.00 51.63           C  
ANISOU 5840  CA  ASN D 147     6733   8230   4653  -1237   1269    554       C  
ATOM   5841  C   ASN D 147      14.044   1.918 -51.201  1.00 50.67           C  
ANISOU 5841  C   ASN D 147     6682   8132   4440  -1110   1258    552       C  
ATOM   5842  O   ASN D 147      13.586   3.028 -50.849  1.00 50.06           O  
ANISOU 5842  O   ASN D 147     6468   8235   4317  -1016   1323    468       O  
ATOM   5843  CB  ASN D 147      11.896   1.110 -52.149  1.00 54.18           C  
ANISOU 5843  CB  ASN D 147     6912   8805   4870  -1420   1404    559       C  
ATOM   5844  CG  ASN D 147      11.109   0.526 -53.306  1.00 55.46           C  
ANISOU 5844  CG  ASN D 147     6972   8998   5101  -1571   1418    549       C  
ATOM   5845  ND2 ASN D 147       9.803   0.439 -53.130  1.00 58.15           N  
ANISOU 5845  ND2 ASN D 147     7153   9589   5353  -1735   1530    548       N  
ATOM   5846  OD1 ASN D 147      11.657   0.176 -54.354  1.00 54.10           O  
ANISOU 5846  OD1 ASN D 147     6855   8646   5055  -1544   1332    536       O  
ATOM   5847  N   SER D 148      15.041   1.294 -50.567  1.00 50.34           N  
ANISOU 5847  N   SER D 148     6846   7920   4359  -1099   1177    638       N  
ATOM   5848  CA  SER D 148      15.683   1.799 -49.328  1.00 50.54           C  
ANISOU 5848  CA  SER D 148     6957   7973   4272  -1005   1151    648       C  
ATOM   5849  C   SER D 148      16.961   2.561 -49.687  1.00 48.28           C  
ANISOU 5849  C   SER D 148     6672   7576   4096   -797   1033    577       C  
ATOM   5850  O   SER D 148      17.549   2.312 -50.746  1.00 47.00           O  
ANISOU 5850  O   SER D 148     6507   7268   4081   -742    959    565       O  
ATOM   5851  CB  SER D 148      15.964   0.676 -48.349  1.00 52.99           C  
ANISOU 5851  CB  SER D 148     7488   8194   4451  -1119   1128    794       C  
ATOM   5852  OG  SER D 148      17.199   0.028 -48.637  1.00 53.40           O  
ANISOU 5852  OG  SER D 148     7695   8011   4585  -1034    990    854       O  
ATOM   5853  N   ILE D 149      17.361   3.480 -48.815  1.00 47.59           N  
ANISOU 5853  N   ILE D 149     6588   7567   3927   -697   1023    526       N  
ATOM   5854  CA  ILE D 149      18.733   4.053 -48.764  1.00 46.32           C  
ANISOU 5854  CA  ILE D 149     6471   7310   3820   -542    898    485       C  
ATOM   5855  C   ILE D 149      19.457   3.382 -47.607  1.00 48.05           C  
ANISOU 5855  C   ILE D 149     6866   7483   3907   -561    823    592       C  
ATOM   5856  O   ILE D 149      18.886   3.361 -46.523  1.00 50.46           O  
ANISOU 5856  O   ILE D 149     7222   7907   4042   -637    891    626       O  
ATOM   5857  CB  ILE D 149      18.692   5.573 -48.555  1.00 45.01           C  
ANISOU 5857  CB  ILE D 149     6207   7256   3639   -433    930    347       C  
ATOM   5858  CG1 ILE D 149      18.002   6.273 -49.728  1.00 43.77           C  
ANISOU 5858  CG1 ILE D 149     5888   7136   3608   -387    994    252       C  
ATOM   5859  CG2 ILE D 149      20.095   6.105 -48.271  1.00 44.32           C  
ANISOU 5859  CG2 ILE D 149     6180   7093   3568   -323    804    312       C  
ATOM   5860  CD1 ILE D 149      17.389   7.600 -49.398  1.00 44.08           C  
ANISOU 5860  CD1 ILE D 149     5842   7314   3591   -306   1080    134       C  
ATOM   5861  N   LYS D 150      20.677   2.909 -47.811  1.00 48.35           N  
ANISOU 5861  N   LYS D 150     6986   7372   4013   -480    689    639       N  
ATOM   5862  CA  LYS D 150      21.477   2.300 -46.730  1.00 50.51           C  
ANISOU 5862  CA  LYS D 150     7425   7607   4161   -464    593    747       C  
ATOM   5863  C   LYS D 150      22.769   3.105 -46.558  1.00 49.08           C  
ANISOU 5863  C   LYS D 150     7209   7433   4007   -319    468    678       C  
ATOM   5864  O   LYS D 150      23.393   3.477 -47.557  1.00 47.70           O  
ANISOU 5864  O   LYS D 150     6938   7194   3994   -231    418    606       O  
ATOM   5865  CB  LYS D 150      21.677   0.814 -47.024  1.00 53.66           C  
ANISOU 5865  CB  LYS D 150     7968   7829   4590   -505    547    888       C  
ATOM   5866  CG  LYS D 150      20.510  -0.073 -46.599  1.00 57.67           C  
ANISOU 5866  CG  LYS D 150     8578   8349   4983   -695    657    990       C  
ATOM   5867  CD  LYS D 150      20.710  -1.561 -46.842  1.00 60.51           C  
ANISOU 5867  CD  LYS D 150     9129   8500   5361   -747    612   1132       C  
ATOM   5868  CE  LYS D 150      19.602  -2.388 -46.223  1.00 63.50           C  
ANISOU 5868  CE  LYS D 150     9634   8899   5592   -968    721   1243       C  
ATOM   5869  NZ  LYS D 150      19.315  -3.604 -47.027  1.00 65.51           N1+
ANISOU 5869  NZ  LYS D 150    10009   8957   5924  -1075    733   1316       N1+
ATOM   5870  N   ILE D 151      23.126   3.404 -45.311  1.00 49.87           N  
ANISOU 5870  N   ILE D 151     7383   7626   3941   -311    424    694       N  
ATOM   5871  CA  ILE D 151      24.368   4.141 -44.949  1.00 48.50           C  
ANISOU 5871  CA  ILE D 151     7185   7488   3756   -204    294    632       C  
ATOM   5872  C   ILE D 151      25.290   3.148 -44.255  1.00 49.26           C  
ANISOU 5872  C   ILE D 151     7416   7533   3767   -158    154    773       C  
ATOM   5873  O   ILE D 151      24.829   2.483 -43.285  1.00 50.31           O  
ANISOU 5873  O   ILE D 151     7695   7692   3729   -231    178    887       O  
ATOM   5874  CB  ILE D 151      24.071   5.359 -44.060  1.00 49.09           C  
ANISOU 5874  CB  ILE D 151     7240   7719   3693   -228    343    520       C  
ATOM   5875  CG1 ILE D 151      23.073   6.290 -44.763  1.00 48.16           C  
ANISOU 5875  CG1 ILE D 151     7001   7641   3657   -244    486    391       C  
ATOM   5876  CG2 ILE D 151      25.366   6.058 -43.661  1.00 49.00           C  
ANISOU 5876  CG2 ILE D 151     7215   7746   3657   -153    200    457       C  
ATOM   5877  CD1 ILE D 151      22.658   7.517 -43.996  1.00 48.57           C  
ANISOU 5877  CD1 ILE D 151     7046   7825   3583   -247    557    266       C  
ATOM   5878  N   TRP D 152      26.527   3.065 -44.760  1.00 47.75           N  
ANISOU 5878  N   TRP D 152     7174   7281   3687    -37     19    769       N  
ATOM   5879  CA  TRP D 152      27.570   2.125 -44.292  1.00 48.42           C  
ANISOU 5879  CA  TRP D 152     7360   7316   3723     60   -135    899       C  
ATOM   5880  C   TRP D 152      28.680   2.909 -43.596  1.00 49.31           C  
ANISOU 5880  C   TRP D 152     7412   7565   3758    127   -271    841       C  
ATOM   5881  O   TRP D 152      29.059   4.003 -44.106  1.00 47.77           O  
ANISOU 5881  O   TRP D 152     7066   7429   3657    137   -274    694       O  
ATOM   5882  CB  TRP D 152      28.094   1.327 -45.478  1.00 46.92           C  
ANISOU 5882  CB  TRP D 152     7142   6964   3722    159   -176    936       C  
ATOM   5883  CG  TRP D 152      26.997   0.687 -46.264  1.00 45.70           C  
ANISOU 5883  CG  TRP D 152     7033   6682   3647     68    -44    963       C  
ATOM   5884  CD1 TRP D 152      26.344   1.201 -47.345  1.00 43.77           C  
ANISOU 5884  CD1 TRP D 152     6666   6424   3540     17     64    855       C  
ATOM   5885  CD2 TRP D 152      26.394  -0.587 -45.996  1.00 46.69           C  
ANISOU 5885  CD2 TRP D 152     7352   6685   3703      1     -8   1112       C  
ATOM   5886  CE2 TRP D 152      25.397  -0.784 -46.971  1.00 45.51           C  
ANISOU 5886  CE2 TRP D 152     7170   6462   3660   -104    120   1075       C  
ATOM   5887  CE3 TRP D 152      26.593  -1.573 -45.025  1.00 49.02           C  
ANISOU 5887  CE3 TRP D 152     7854   6923   3849     11    -75   1276       C  
ATOM   5888  NE1 TRP D 152      25.385   0.326 -47.772  1.00 43.72           N  
ANISOU 5888  NE1 TRP D 152     6744   6313   3556    -81    158    920       N  
ATOM   5889  CZ2 TRP D 152      24.605  -1.932 -47.003  1.00 46.79           C  
ANISOU 5889  CZ2 TRP D 152     7496   6497   3785   -220    187   1187       C  
ATOM   5890  CZ3 TRP D 152      25.810  -2.708 -45.055  1.00 50.26           C  
ANISOU 5890  CZ3 TRP D 152     8194   6934   3970    -96     -4   1396       C  
ATOM   5891  CH2 TRP D 152      24.829  -2.882 -46.034  1.00 49.24           C  
ANISOU 5891  CH2 TRP D 152     8025   6735   3950   -221    127   1347       C  
ATOM   5892  N   ASP D 153      29.180   2.377 -42.477  1.00 52.02           N  
ANISOU 5892  N   ASP D 153     7876   7958   3929    162   -384    955       N  
ATOM   5893  CA  ASP D 153      30.429   2.890 -41.866  1.00 53.73           C  
ANISOU 5893  CA  ASP D 153     8029   8310   4074    240   -553    921       C  
ATOM   5894  C   ASP D 153      31.558   2.605 -42.859  1.00 21.41           C  
ATOM   5895  O   ASP D 153      31.652   1.462 -43.358  1.00 53.83           O  
ANISOU 5895  O   ASP D 153     7978   8121   4354    477   -675   1030       O  
ATOM   5896  CB  ASP D 153      30.679   2.309 -40.480  1.00 56.66           C  
ANISOU 5896  CB  ASP D 153     8564   8756   4209    254   -657   1058       C  
ATOM   5897  CG  ASP D 153      31.873   2.949 -39.811  1.00 58.33           C  
ANISOU 5897  CG  ASP D 153     8693   9142   4327    309   -832   1006       C  
ATOM   5898  OD1 ASP D 153      31.775   4.125 -39.401  1.00 57.89           O  
ANISOU 5898  OD1 ASP D 153     8583   9217   4197    213   -806    863       O  
ATOM   5899  OD2 ASP D 153      32.887   2.239 -39.709  1.00 60.73           O1-
ANISOU 5899  OD2 ASP D 153     8994   9451   4629    452   -995   1109       O1-
ATOM   5900  N   LYS D 154      32.330   3.640 -43.183  1.00 53.45           N  
ANISOU 5900  N   LYS D 154     7687   8326   4297    395   -713    776       N  
ATOM   5901  CA  LYS D 154      33.399   3.595 -44.205  1.00 53.43           C  
ANISOU 5901  CA  LYS D 154     7517   8309   4476    511   -790    739       C  
ATOM   5902  C   LYS D 154      34.484   2.616 -43.755  1.00 55.22           C  
ANISOU 5902  C   LYS D 154     7762   8568   4650    679   -968    873       C  
ATOM   5903  O   LYS D 154      35.042   1.939 -44.607  1.00 54.73           O  
ANISOU 5903  O   LYS D 154     7641   8423   4730    816  -1000    911       O  
ATOM   5904  CB  LYS D 154      33.960   4.999 -44.434  1.00 53.45           C  
ANISOU 5904  CB  LYS D 154     7347   8442   4520    442   -808    565       C  
ATOM   5905  CG  LYS D 154      35.042   5.107 -45.502  1.00 53.27           C  
ANISOU 5905  CG  LYS D 154     7129   8435   4674    528   -868    511       C  
ATOM   5906  CD  LYS D 154      34.508   5.189 -46.913  1.00 51.20           C  
ANISOU 5906  CD  LYS D 154     6815   8030   4609    515   -727    453       C  
ATOM   5907  CE  LYS D 154      35.621   5.369 -47.922  1.00 50.94           C  
ANISOU 5907  CE  LYS D 154     6586   8037   4730    588   -778    393       C  
ATOM   5908  NZ  LYS D 154      36.651   4.307 -47.794  1.00 52.61           N1+
ANISOU 5908  NZ  LYS D 154     6757   8287   4944    770   -916    501       N1+
ATOM   5909  N   THR D 155      34.761   2.535 -42.460  1.00 57.57           N  
ANISOU 5909  N   THR D 155     8146   8986   4740    681  -1081    943       N  
ATOM   5910  CA  THR D 155      35.879   1.729 -41.915  1.00 60.66           C  
ANISOU 5910  CA  THR D 155     8543   9449   5058    859  -1277   1070       C  
ATOM   5911  C   THR D 155      35.353   0.316 -41.593  1.00 61.47           C  
ANISOU 5911  C   THR D 155     8889   9373   5093    940  -1266   1268       C  
ATOM   5912  O   THR D 155      35.883  -0.632 -42.170  1.00 62.27           O  
ANISOU 5912  O   THR D 155     8998   9361   5299   1118  -1320   1355       O  
ATOM   5913  CB  THR D 155      36.553   2.535 -40.796  1.00 62.62           C  
ANISOU 5913  CB  THR D 155     8729   9943   5121    808  -1417   1020       C  
ATOM   5914  CG2 THR D 155      37.260   3.796 -41.253  1.00 61.76           C  
ANISOU 5914  CG2 THR D 155     8384   9986   5098    733  -1443    833       C  
ATOM   5915  OG1 THR D 155      35.491   2.961 -39.954  1.00 64.09           O  
ANISOU 5915  OG1 THR D 155     9074  10134   5142    640  -1317   1003       O  
ATOM   5916  N   SER D 156      34.309   0.171 -40.781  1.00 61.66           N  
ANISOU 5916  N   SER D 156     9112   9358   4957    809  -1182   1333       N  
ATOM   5917  CA  SER D 156      33.811  -1.133 -40.264  1.00 63.80           C  
ANISOU 5917  CA  SER D 156     9647   9473   5119    846  -1177   1535       C  
ATOM   5918  C   SER D 156      32.915  -1.846 -41.281  1.00 63.06           C  
ANISOU 5918  C   SER D 156     9644   9135   5182    808  -1017   1563       C  
ATOM   5919  O   SER D 156      32.686  -3.055 -41.103  1.00 64.22           O  
ANISOU 5919  O   SER D 156    10010   9109   5280    859  -1024   1730       O  
ATOM   5920  CB  SER D 156      33.062  -0.947 -38.977  1.00 65.29           C  
ANISOU 5920  CB  SER D 156    10001   9747   5058    696  -1140   1586       C  
ATOM   5921  OG  SER D 156      31.759  -0.442 -39.222  1.00 63.94           O  
ANISOU 5921  OG  SER D 156     9845   9539   4909    498   -932   1497       O  
ATOM   5922  N   LEU D 157      32.365  -1.104 -42.249  1.00 62.05           N  
ANISOU 5922  N   LEU D 157     9372   8992   5214    703   -877   1407       N  
ATOM   5923  CA  LEU D 157      31.414  -1.582 -43.298  1.00 60.97           C  
ANISOU 5923  CA  LEU D 157     9283   8659   5224    631   -717   1399       C  
ATOM   5924  C   LEU D 157      30.074  -1.998 -42.685  1.00 61.97           C  
ANISOU 5924  C   LEU D 157     9610   8724   5212    450   -586   1483       C  
ATOM   5925  O   LEU D 157      29.285  -2.623 -43.394  1.00 60.82           O  
ANISOU 5925  O   LEU D 157     9541   8415   5155    379   -472   1510       O  
ATOM   5926  CB  LEU D 157      32.033  -2.756 -44.063  1.00 61.86           C  
ANISOU 5926  CB  LEU D 157     9460   8581   5463    811   -779   1490       C  
ATOM   5927  CG  LEU D 157      33.422  -2.514 -44.649  1.00 61.97           C  
ANISOU 5927  CG  LEU D 157     9272   8669   5603   1012   -908   1424       C  
ATOM   5928  CD1 LEU D 157      33.819  -3.678 -45.545  1.00 62.65           C  
ANISOU 5928  CD1 LEU D 157     9433   8545   5825   1186   -926   1493       C  
ATOM   5929  CD2 LEU D 157      33.470  -1.203 -45.420  1.00 59.62           C  
ANISOU 5929  CD2 LEU D 157     8721   8497   5435    929   -843   1225       C  
ATOM   5930  N   GLU D 158      29.814  -1.667 -41.421  1.00 64.83           N  
ANISOU 5930  N   GLU D 158    10050   9225   5357    367   -598   1519       N  
ATOM   5931  CA  GLU D 158      28.501  -1.936 -40.774  1.00 66.10           C  
ANISOU 5931  CA  GLU D 158    10374   9374   5367    174   -454   1587       C  
ATOM   5932  C   GLU D 158      27.454  -0.978 -41.356  1.00 27.08           C  
ATOM   5933  O   GLU D 158      27.819   0.114 -41.833  1.00 59.99           O  
ANISOU 5933  O   GLU D 158     9251   8762   4779     62   -284   1261       O  
ATOM   5934  CB  GLU D 158      28.591  -1.794 -39.255  1.00 70.43           C  
ANISOU 5934  CB  GLU D 158    11041  10073   5645    138   -517   1662       C  
ATOM   5935  CG  GLU D 158      29.480  -2.839 -38.601  1.00 74.80           C  
ANISOU 5935  CG  GLU D 158    11775  10557   6087    286   -693   1853       C  
ATOM   5936  CD  GLU D 158      29.278  -3.002 -37.099  1.00 79.76           C  
ANISOU 5936  CD  GLU D 158    12593  11294   6418    215   -727   1975       C  
ATOM   5937  OE1 GLU D 158      30.296  -3.259 -36.420  1.00 83.62           O  
ANISOU 5937  OE1 GLU D 158    13136  11840   6795    363   -916   2066       O  
ATOM   5938  OE2 GLU D 158      28.110  -2.878 -36.598  1.00 81.82           O1-
ANISOU 5938  OE2 GLU D 158    12939  11598   6549     14   -565   1979       O1-
ATOM   5939  N   CYS D 159      26.191  -1.401 -41.332  1.00 62.31           N  
ANISOU 5939  N   CYS D 159     9838   8914   4923   -141   -119   1469       N  
ATOM   5940  CA  CYS D 159      25.025  -0.588 -41.759  1.00 59.98           C  
ANISOU 5940  CA  CYS D 159     9408   8707   4676   -281     60   1334       C  
ATOM   5941  C   CYS D 159      24.537   0.236 -40.575  1.00 60.19           C  
ANISOU 5941  C   CYS D 159     9437   8939   4492   -367    120   1287       C  
ATOM   5942  O   CYS D 159      24.102  -0.367 -39.595  1.00 63.62           O  
ANISOU 5942  O   CYS D 159    10043   9399   4730   -460    150   1412       O  
ATOM   5943  CB  CYS D 159      23.874  -1.445 -42.261  1.00 59.61           C  
ANISOU 5943  CB  CYS D 159     9438   8549   4663   -431    200   1402       C  
ATOM   5944  SG  CYS D 159      22.576  -0.404 -42.963  1.00 57.97           S  
ANISOU 5944  SG  CYS D 159     9012   8473   4541   -552    392   1227       S  
ATOM   5945  N   LEU D 160      24.584   1.561 -40.675  1.00 58.06           N  
ANISOU 5945  N   LEU D 160     9002   8800   4257   -342    145   1111       N  
ATOM   5946  CA  LEU D 160      24.277   2.481 -39.549  1.00 57.94           C  
ANISOU 5946  CA  LEU D 160     8996   8978   4042   -396    190   1035       C  
ATOM   5947  C   LEU D 160      22.803   2.892 -39.577  1.00 56.93           C  
ANISOU 5947  C   LEU D 160     8813   8941   3878   -524    403    966       C  
ATOM   5948  O   LEU D 160      22.210   2.980 -38.495  1.00 58.53           O  
ANISOU 5948  O   LEU D 160     9101   9275   3865   -612    480    989       O  
ATOM   5949  CB  LEU D 160      25.204   3.692 -39.667  1.00 56.67           C  
ANISOU 5949  CB  LEU D 160     8706   8886   3939   -297     94    877       C  
ATOM   5950  CG  LEU D 160      26.689   3.354 -39.735  1.00 56.29           C  
ANISOU 5950  CG  LEU D 160     8659   8789   3941   -168   -116    930       C  
ATOM   5951  CD1 LEU D 160      27.521   4.581 -40.033  1.00 54.76           C  
ANISOU 5951  CD1 LEU D 160     8313   8666   3826   -110   -190    761       C  
ATOM   5952  CD2 LEU D 160      27.134   2.699 -38.444  1.00 58.98           C  
ANISOU 5952  CD2 LEU D 160     9172   9187   4050   -161   -228   1074       C  
ATOM   5953  N   LYS D 161      22.257   3.162 -40.763  1.00 55.05           N  
ANISOU 5953  N   LYS D 161     8430   8653   3835   -525    491    881       N  
ATOM   5954  CA  LYS D 161      20.842   3.567 -40.949  1.00 55.26           C  
ANISOU 5954  CA  LYS D 161     8363   8783   3851   -623    687    809       C  
ATOM   5955  C   LYS D 161      20.277   2.883 -42.191  1.00 53.28           C  
ANISOU 5955  C   LYS D 161     8043   8418   3782   -671    743    844       C  
ATOM   5956  O   LYS D 161      21.061   2.467 -43.082  1.00 51.60           O  
ANISOU 5956  O   LYS D 161     7823   8045   3738   -594    637    868       O  
ATOM   5957  CB  LYS D 161      20.687   5.086 -41.107  1.00 55.44           C  
ANISOU 5957  CB  LYS D 161     8243   8912   3910   -549    741    610       C  
ATOM   5958  CG  LYS D 161      20.796   5.910 -39.827  1.00 58.40           C  
ANISOU 5958  CG  LYS D 161     8684   9435   4072   -542    749    539       C  
ATOM   5959  CD  LYS D 161      19.472   6.223 -39.108  1.00 60.60           C  
ANISOU 5959  CD  LYS D 161     8953   9891   4180   -625    941    499       C  
ATOM   5960  CE  LYS D 161      19.594   6.147 -37.593  1.00 63.21           C  
ANISOU 5960  CE  LYS D 161     9442  10343   4233   -679    934    545       C  
ATOM   5961  NZ  LYS D 161      18.496   6.878 -36.915  1.00 64.89           N1+
ANISOU 5961  NZ  LYS D 161     9621  10748   4285   -713   1120    441       N1+
ATOM   5962  N   VAL D 162      18.951   2.814 -42.239  1.00 53.05           N  
ANISOU 5962  N   VAL D 162     7955   8491   3713   -794    909    837       N  
ATOM   5963  CA  VAL D 162      18.186   2.373 -43.432  1.00 52.84           C  
ANISOU 5963  CA  VAL D 162     7825   8410   3843   -863    984    837       C  
ATOM   5964  C   VAL D 162      17.019   3.333 -43.631  1.00 52.55           C  
ANISOU 5964  C   VAL D 162     7600   8563   3805   -879   1140    706       C  
ATOM   5965  O   VAL D 162      16.033   3.186 -42.921  1.00 55.24           O  
ANISOU 5965  O   VAL D 162     7937   9061   3990  -1000   1271    735       O  
ATOM   5966  CB  VAL D 162      17.694   0.926 -43.255  1.00 54.77           C  
ANISOU 5966  CB  VAL D 162     8214   8580   4018  -1040   1019   1006       C  
ATOM   5967  CG1 VAL D 162      16.805   0.503 -44.427  1.00 54.55           C  
ANISOU 5967  CG1 VAL D 162     8076   8523   4128  -1144   1103    993       C  
ATOM   5968  CG2 VAL D 162      18.856  -0.046 -43.047  1.00 55.28           C  
ANISOU 5968  CG2 VAL D 162     8486   8438   4079   -989    861   1143       C  
ATOM   5969  N   LEU D 163      17.119   4.266 -44.570  1.00 50.96           N  
ANISOU 5969  N   LEU D 163     7248   8352   3763   -756   1130    574       N  
ATOM   5970  CA  LEU D 163      16.056   5.272 -44.820  1.00 50.80           C  
ANISOU 5970  CA  LEU D 163     7049   8504   3750   -724   1267    445       C  
ATOM   5971  C   LEU D 163      15.013   4.666 -45.765  1.00 50.78           C  
ANISOU 5971  C   LEU D 163     6923   8535   3835   -833   1350    475       C  
ATOM   5972  O   LEU D 163      15.396   4.127 -46.815  1.00 49.07           O  
ANISOU 5972  O   LEU D 163     6706   8164   3777   -837   1273    506       O  
ATOM   5973  CB  LEU D 163      16.686   6.552 -45.372  1.00 49.05           C  
ANISOU 5973  CB  LEU D 163     6754   8235   3646   -543   1209    301       C  
ATOM   5974  CG  LEU D 163      17.381   7.417 -44.323  1.00 49.90           C  
ANISOU 5974  CG  LEU D 163     6953   8376   3630   -462   1167    231       C  
ATOM   5975  CD1 LEU D 163      18.346   6.583 -43.505  1.00 51.01           C  
ANISOU 5975  CD1 LEU D 163     7266   8442   3673   -512   1048    350       C  
ATOM   5976  CD2 LEU D 163      18.131   8.571 -44.949  1.00 48.12           C  
ANISOU 5976  CD2 LEU D 163     6686   8067   3532   -317   1096    102       C  
ATOM   5977  N   THR D 164      13.737   4.718 -45.376  1.00 52.34           N  
ANISOU 5977  N   THR D 164     7019   8944   3922   -928   1504    464       N  
ATOM   5978  CA  THR D 164      12.605   4.225 -46.198  1.00 52.70           C  
ANISOU 5978  CA  THR D 164     6914   9083   4029  -1052   1594    480       C  
ATOM   5979  C   THR D 164      11.591   5.345 -46.390  1.00 53.55           C  
ANISOU 5979  C   THR D 164     6796   9418   4133   -953   1714    348       C  
ATOM   5980  O   THR D 164      11.523   6.256 -45.549  1.00 53.93           O  
ANISOU 5980  O   THR D 164     6841   9579   4071   -844   1772    269       O  
ATOM   5981  CB  THR D 164      11.983   2.979 -45.583  1.00 54.57           C  
ANISOU 5981  CB  THR D 164     7235   9371   4128  -1300   1665    619       C  
ATOM   5982  CG2 THR D 164      13.054   2.018 -45.116  1.00 55.08           C  
ANISOU 5982  CG2 THR D 164     7561   9208   4157  -1350   1545    751       C  
ATOM   5983  OG1 THR D 164      11.116   3.395 -44.527  1.00 56.05           O  
ANISOU 5983  OG1 THR D 164     7357   9813   4126  -1344   1813    593       O  
ATOM   5984  N   GLY D 165      10.869   5.298 -47.504  1.00 54.32           N  
ANISOU 5984  N   GLY D 165     6718   9573   4347   -973   1742    320       N  
ATOM   5985  CA  GLY D 165       9.974   6.388 -47.940  1.00 55.26           C  
ANISOU 5985  CA  GLY D 165     6611   9890   4497   -833   1830    196       C  
ATOM   5986  C   GLY D 165       9.601   6.233 -49.397  1.00 55.01           C  
ANISOU 5986  C   GLY D 165     6433   9841   4628   -839   1792    183       C  
ATOM   5987  O   GLY D 165       8.412   6.290 -49.708  1.00 57.15           O  
ANISOU 5987  O   GLY D 165     6495  10341   4878   -882   1888    158       O  
ATOM   5988  N   HIS D 166      10.587   6.050 -50.265  1.00 53.97           N  
ANISOU 5988  N   HIS D 166     6397   9464   4645   -794   1656    196       N  
ATOM   5989  CA  HIS D 166      10.331   5.896 -51.716  1.00 53.76           C  
ANISOU 5989  CA  HIS D 166     6254   9405   4769   -798   1610    181       C  
ATOM   5990  C   HIS D 166       9.478   4.639 -51.868  1.00 55.78           C  
ANISOU 5990  C   HIS D 166     6462   9751   4981  -1062   1659    267       C  
ATOM   5991  O   HIS D 166       9.682   3.697 -51.058  1.00 56.16           O  
ANISOU 5991  O   HIS D 166     6668   9737   4935  -1230   1670    364       O  
ATOM   5992  CB  HIS D 166      11.638   5.876 -52.520  1.00 51.53           C  
ANISOU 5992  CB  HIS D 166     6102   8843   4635   -711   1466    180       C  
ATOM   5993  CG  HIS D 166      12.208   7.225 -52.806  1.00 50.14           C  
ANISOU 5993  CG  HIS D 166     5910   8613   4529   -475   1426     79       C  
ATOM   5994  CD2 HIS D 166      13.364   7.805 -52.411  1.00 49.05           C  
ANISOU 5994  CD2 HIS D 166     5907   8325   4406   -359   1356     49       C  
ATOM   5995  ND1 HIS D 166      11.577   8.132 -53.636  1.00 50.61           N  
ANISOU 5995  ND1 HIS D 166     5806   8771   4651   -344   1453     -2       N  
ATOM   5996  CE1 HIS D 166      12.324   9.214 -53.730  1.00 49.79           C  
ANISOU 5996  CE1 HIS D 166     5762   8558   4597   -161   1408    -74       C  
ATOM   5997  NE2 HIS D 166      13.429   9.036 -52.983  1.00 48.04           N  
ANISOU 5997  NE2 HIS D 166     5715   8189   4347   -179   1349    -49       N  
ATOM   5998  N   THR D 167       8.545   4.661 -52.825  1.00 57.41           N  
ANISOU 5998  N   THR D 167     6465  10108   5240  -1100   1687    233       N  
ATOM   5999  CA  THR D 167       7.645   3.525 -53.173  1.00 59.12           C  
ANISOU 5999  CA  THR D 167     6608  10430   5424  -1375   1728    296       C  
ATOM   6000  C   THR D 167       8.229   2.815 -54.397  1.00 58.33           C  
ANISOU 6000  C   THR D 167     6601  10098   5462  -1437   1609    319       C  
ATOM   6001  O   THR D 167       7.543   1.949 -54.966  1.00 61.54           O  
ANISOU 6001  O   THR D 167     6951  10565   5867  -1655   1622    350       O  
ATOM   6002  CB  THR D 167       6.215   4.025 -53.417  1.00 61.00           C  
ANISOU 6002  CB  THR D 167     6539  11022   5618  -1378   1831    236       C  
ATOM   6003  CG2 THR D 167       5.640   4.780 -52.244  1.00 62.26           C  
ANISOU 6003  CG2 THR D 167     6600  11417   5638  -1285   1960    198       C  
ATOM   6004  OG1 THR D 167       6.190   4.932 -54.520  1.00 61.06           O  
ANISOU 6004  OG1 THR D 167     6410  11045   5746  -1164   1771    151       O  
ATOM   6005  N   GLY D 168       9.445   3.188 -54.801  1.00 55.14           N  
ANISOU 6005  N   GLY D 168     6330   9451   5168  -1258   1503    296       N  
ATOM   6006  CA  GLY D 168      10.167   2.551 -55.915  1.00 53.32           C  
ANISOU 6006  CA  GLY D 168     6209   8987   5065  -1285   1394    310       C  
ATOM   6007  C   GLY D 168      11.664   2.622 -55.702  1.00 50.65           C  
ANISOU 6007  C   GLY D 168     6077   8382   4786  -1145   1301    325       C  
ATOM   6008  O   GLY D 168      12.090   3.388 -54.830  1.00 49.89           O  
ANISOU 6008  O   GLY D 168     6009   8303   4644  -1009   1311    306       O  
ATOM   6009  N   SER D 169      12.421   1.839 -56.464  1.00 49.21           N  
ANISOU 6009  N   SER D 169     6030   7973   4694  -1180   1215    353       N  
ATOM   6010  CA  SER D 169      13.910   1.842 -56.482  1.00 47.41           C  
ANISOU 6010  CA  SER D 169     5970   7504   4541  -1036   1116    362       C  
ATOM   6011  C   SER D 169      14.469   3.268 -56.370  1.00 44.31           C  
ANISOU 6011  C   SER D 169     5504   7147   4185   -807   1095    283       C  
ATOM   6012  O   SER D 169      13.912   4.204 -56.989  1.00 43.18           O  
ANISOU 6012  O   SER D 169     5197   7131   4078   -721   1123    207       O  
ATOM   6013  CB  SER D 169      14.408   1.139 -57.719  1.00 46.99           C  
ANISOU 6013  CB  SER D 169     5986   7267   4601  -1058   1044    358       C  
ATOM   6014  OG  SER D 169      13.657  -0.052 -57.923  1.00 49.13           O  
ANISOU 6014  OG  SER D 169     6310   7526   4831  -1291   1075    410       O  
ATOM   6015  N   VAL D 170      15.541   3.420 -55.597  1.00 42.93           N  
ANISOU 6015  N   VAL D 170     5456   6863   3993   -715   1044    304       N  
ATOM   6016  CA  VAL D 170      16.324   4.685 -55.500  1.00 41.50           C  
ANISOU 6016  CA  VAL D 170     5249   6670   3851   -522   1006    229       C  
ATOM   6017  C   VAL D 170      17.414   4.618 -56.562  1.00 39.67           C  
ANISOU 6017  C   VAL D 170     5056   6263   3755   -440    914    208       C  
ATOM   6018  O   VAL D 170      18.321   3.785 -56.416  1.00 39.04           O  
ANISOU 6018  O   VAL D 170     5107   6033   3692   -450    847    266       O  
ATOM   6019  CB  VAL D 170      16.934   4.885 -54.103  1.00 41.83           C  
ANISOU 6019  CB  VAL D 170     5396   6709   3789   -485    992    254       C  
ATOM   6020  CG1 VAL D 170      17.767   6.150 -54.040  1.00 40.10           C  
ANISOU 6020  CG1 VAL D 170     5163   6469   3606   -321    948    169       C  
ATOM   6021  CG2 VAL D 170      15.870   4.881 -53.014  1.00 43.22           C  
ANISOU 6021  CG2 VAL D 170     5545   7067   3812   -576   1096    277       C  
ATOM   6022  N   LEU D 171      17.304   5.470 -57.574  1.00 39.02           N  
ANISOU 6022  N   LEU D 171     4865   6205   3755   -352    914    132       N  
ATOM   6023  CA  LEU D 171      18.045   5.340 -58.850  1.00 38.60           C  
ANISOU 6023  CA  LEU D 171     4821   6020   3827   -305    851    108       C  
ATOM   6024  C   LEU D 171      19.276   6.245 -58.832  1.00 38.00           C  
ANISOU 6024  C   LEU D 171     4770   5868   3801   -167    794     62       C  
ATOM   6025  O   LEU D 171      20.312   5.869 -59.446  1.00 38.32           O  
ANISOU 6025  O   LEU D 171     4860   5781   3921   -133    731     66       O  
ATOM   6026  CB  LEU D 171      17.096   5.728 -59.983  1.00 38.35           C  
ANISOU 6026  CB  LEU D 171     4655   6080   3834   -310    886     62       C  
ATOM   6027  CG  LEU D 171      15.902   4.799 -60.155  1.00 39.43           C  
ANISOU 6027  CG  LEU D 171     4746   6310   3926   -475    933     99       C  
ATOM   6028  CD1 LEU D 171      15.032   5.263 -61.304  1.00 39.65           C  
ANISOU 6028  CD1 LEU D 171     4624   6453   3987   -463    950     50       C  
ATOM   6029  CD2 LEU D 171      16.347   3.368 -60.376  1.00 39.86           C  
ANISOU 6029  CD2 LEU D 171     4938   6205   4000   -595    894    158       C  
ATOM   6030  N   CYS D 172      19.146   7.398 -58.193  1.00 36.95           N  
ANISOU 6030  N   CYS D 172     4603   5817   3619    -94    822     13       N  
ATOM   6031  CA  CYS D 172      20.223   8.390 -58.107  1.00 36.78           C  
ANISOU 6031  CA  CYS D 172     4608   5735   3630      7    775    -41       C  
ATOM   6032  C   CYS D 172      20.187   8.990 -56.718  1.00 37.80           C  
ANISOU 6032  C   CYS D 172     4778   5934   3648     26    795    -59       C  
ATOM   6033  O   CYS D 172      19.106   9.003 -56.128  1.00 39.37           O  
ANISOU 6033  O   CYS D 172     4947   6250   3761     -4    869    -53       O  
ATOM   6034  CB  CYS D 172      20.021   9.470 -59.150  1.00 37.28           C  
ANISOU 6034  CB  CYS D 172     4603   5802   3760     86    794   -109       C  
ATOM   6035  SG  CYS D 172      18.318  10.079 -59.240  1.00 39.35           S  
ANISOU 6035  SG  CYS D 172     4757   6226   3968    114    889   -138       S  
ATOM   6036  N   LEU D 173      21.327   9.453 -56.224  1.00 37.53           N  
ANISOU 6036  N   LEU D 173     4805   5845   3610     66    732    -83       N  
ATOM   6037  CA  LEU D 173      21.398  10.226 -54.967  1.00 38.20           C  
ANISOU 6037  CA  LEU D 173     4940   5990   3583     86    743   -124       C  
ATOM   6038  C   LEU D 173      22.622  11.120 -55.019  1.00 36.97           C  
ANISOU 6038  C   LEU D 173     4817   5766   3463    130    675   -188       C  
ATOM   6039  O   LEU D 173      23.525  10.840 -55.791  1.00 36.49           O  
ANISOU 6039  O   LEU D 173     4739   5628   3499    133    612   -175       O  
ATOM   6040  CB  LEU D 173      21.415   9.289 -53.747  1.00 40.17           C  
ANISOU 6040  CB  LEU D 173     5262   6282   3719     19    728    -47       C  
ATOM   6041  CG  LEU D 173      22.676   8.448 -53.490  1.00 40.89           C  
ANISOU 6041  CG  LEU D 173     5420   6293   3825      7    617     19       C  
ATOM   6042  CD1 LEU D 173      23.746   9.207 -52.709  1.00 41.36           C  
ANISOU 6042  CD1 LEU D 173     5520   6362   3831     41    543    -30       C  
ATOM   6043  CD2 LEU D 173      22.325   7.212 -52.701  1.00 42.09           C  
ANISOU 6043  CD2 LEU D 173     5647   6460   3884    -66    620    127       C  
ATOM   6044  N   GLN D 174      22.602  12.167 -54.212  1.00 37.74           N  
ANISOU 6044  N   GLN D 174     4962   5898   3478    156    695   -260       N  
ATOM   6045  CA  GLN D 174      23.770  13.025 -53.921  1.00 38.06           C  
ANISOU 6045  CA  GLN D 174     5056   5891   3513    158    626   -326       C  
ATOM   6046  C   GLN D 174      23.550  13.544 -52.507  1.00 39.10           C  
ANISOU 6046  C   GLN D 174     5270   6095   3492    150    646   -372       C  
ATOM   6047  O   GLN D 174      22.369  13.739 -52.150  1.00 40.02           O  
ANISOU 6047  O   GLN D 174     5386   6279   3538    181    743   -388       O  
ATOM   6048  CB  GLN D 174      23.860  14.129 -54.975  1.00 37.33           C  
ANISOU 6048  CB  GLN D 174     4952   5721   3512    201    649   -399       C  
ATOM   6049  CG  GLN D 174      25.159  14.918 -54.958  1.00 37.79           C  
ANISOU 6049  CG  GLN D 174     5053   5717   3587    166    578   -460       C  
ATOM   6050  CD  GLN D 174      24.994  16.280 -55.575  1.00 37.82           C  
ANISOU 6050  CD  GLN D 174     5107   5639   3623    200    625   -544       C  
ATOM   6051  NE2 GLN D 174      25.593  17.278 -54.941  1.00 38.01           N  
ANISOU 6051  NE2 GLN D 174     5226   5629   3585    161    602   -628       N  
ATOM   6052  OE1 GLN D 174      24.309  16.444 -56.587  1.00 37.87           O  
ANISOU 6052  OE1 GLN D 174     5081   5611   3699    258    679   -534       O  
ATOM   6053  N   TYR D 175      24.613  13.739 -51.734  1.00 39.28           N  
ANISOU 6053  N   TYR D 175     5350   6122   3454    110    560   -395       N  
ATOM   6054  CA  TYR D 175      24.493  14.297 -50.367  1.00 41.26           C  
ANISOU 6054  CA  TYR D 175     5696   6441   3541     93    571   -452       C  
ATOM   6055  C   TYR D 175      25.565  15.358 -50.145  1.00 42.04           C  
ANISOU 6055  C   TYR D 175     5855   6496   3623     57    501   -551       C  
ATOM   6056  O   TYR D 175      26.542  15.377 -50.893  1.00 41.46           O  
ANISOU 6056  O   TYR D 175     5730   6367   3654     30    428   -547       O  
ATOM   6057  CB  TYR D 175      24.533  13.163 -49.340  1.00 41.87           C  
ANISOU 6057  CB  TYR D 175     5798   6605   3507     50    532   -355       C  
ATOM   6058  CG  TYR D 175      25.862  12.460 -49.152  1.00 41.98           C  
ANISOU 6058  CG  TYR D 175     5805   6614   3533     17    389   -291       C  
ATOM   6059  CD1 TYR D 175      26.840  12.990 -48.325  1.00 42.62           C  
ANISOU 6059  CD1 TYR D 175     5934   6736   3523    -19    295   -344       C  
ATOM   6060  CD2 TYR D 175      26.121  11.226 -49.734  1.00 41.18           C  
ANISOU 6060  CD2 TYR D 175     5651   6477   3519     29    346   -178       C  
ATOM   6061  CE1 TYR D 175      28.046  12.342 -48.116  1.00 42.90           C  
ANISOU 6061  CE1 TYR D 175     5940   6800   3561    -33    157   -282       C  
ATOM   6062  CE2 TYR D 175      27.316  10.556 -49.516  1.00 41.44           C  
ANISOU 6062  CE2 TYR D 175     5675   6515   3556     33    216   -117       C  
ATOM   6063  CZ  TYR D 175      28.289  11.118 -48.709  1.00 42.47           C  
ANISOU 6063  CZ  TYR D 175     5827   6711   3600      8    118   -166       C  
ATOM   6064  OH  TYR D 175      29.476  10.480 -48.469  1.00 43.67           O  
ANISOU 6064  OH  TYR D 175     5946   6898   3747     28    -19   -105       O  
ATOM   6065  N   ASP D 176      25.354  16.224 -49.157  1.00 44.15           N  
ANISOU 6065  N   ASP D 176     6229   6792   3754     50    531   -644       N  
ATOM   6066  CA  ASP D 176      26.381  17.159 -48.644  1.00 46.42           C  
ANISOU 6066  CA  ASP D 176     6601   7056   3981    -21    454   -745       C  
ATOM   6067  C   ASP D 176      26.326  17.155 -47.115  1.00 25.83           C  
ATOM   6068  O   ASP D 176      25.757  16.226 -46.540  1.00 49.19           O  
ANISOU 6068  O   ASP D 176     7031   7602   4056    -39    461   -686       O  
ATOM   6069  CB  ASP D 176      26.190  18.547 -49.257  1.00 46.94           C  
ANISOU 6069  CB  ASP D 176     6742   6997   4096      3    519   -863       C  
ATOM   6070  CG  ASP D 176      24.887  19.227 -48.904  1.00 48.36           C  
ANISOU 6070  CG  ASP D 176     7008   7167   4198    103    653   -933       C  
ATOM   6071  OD1 ASP D 176      24.146  18.690 -48.058  1.00 48.95           O  
ANISOU 6071  OD1 ASP D 176     7082   7356   4163    133    703   -903       O  
ATOM   6072  OD2 ASP D 176      24.610  20.270 -49.515  1.00 50.10           O1-
ANISOU 6072  OD2 ASP D 176     7297   7271   4470    157    711  -1011       O1-
ATOM   6073  N   GLU D 177      26.932  18.155 -46.487  1.00 52.17           N  
ANISOU 6073  N   GLU D 177     7533   7875   4415   -123    396   -892       N  
ATOM   6074  CA  GLU D 177      27.006  18.269 -45.007  1.00 54.18           C  
ANISOU 6074  CA  GLU D 177     7896   8232   4456   -171    367   -939       C  
ATOM   6075  C   GLU D 177      25.582  18.345 -44.437  1.00 27.16           C  
ATOM   6076  O   GLU D 177      25.418  17.873 -43.326  1.00 55.12           O  
ANISOU 6076  O   GLU D 177     8125   8514   4304   -109    511   -932       O  
ATOM   6077  CB  GLU D 177      27.904  19.440 -44.602  1.00 56.72           C  
ANISOU 6077  CB  GLU D 177     8330   8513   4708   -274    298  -1083       C  
ATOM   6078  CG  GLU D 177      27.770  20.657 -45.504  1.00 58.94           C  
ANISOU 6078  CG  GLU D 177     8678   8624   5095   -261    368  -1191       C  
ATOM   6079  CD  GLU D 177      28.855  20.829 -46.563  1.00 60.60           C  
ANISOU 6079  CD  GLU D 177     8803   8761   5461   -343    283  -1179       C  
ATOM   6080  OE1 GLU D 177      28.561  20.626 -47.789  1.00 57.81           O  
ANISOU 6080  OE1 GLU D 177     8360   8330   5274   -275    333  -1117       O  
ATOM   6081  OE2 GLU D 177      30.004  21.197 -46.157  1.00 65.04           O1-
ANISOU 6081  OE2 GLU D 177     9386   9358   5967   -486    168  -1237       O1-
ATOM   6082  N   ARG D 178      24.583  18.839 -45.178  1.00 53.98           N  
ANISOU 6082  N   ARG D 178     7925   8177   4410     19    648   -997       N  
ATOM   6083  CA  ARG D 178      23.217  19.129 -44.644  1.00 54.61           C  
ANISOU 6083  CA  ARG D 178     8051   8316   4381    119    804  -1045       C  
ATOM   6084  C   ARG D 178      22.209  18.040 -45.084  1.00 52.08           C  
ANISOU 6084  C   ARG D 178     7584   8081   4122    173    881   -914       C  
ATOM   6085  O   ARG D 178      21.387  17.661 -44.234  1.00 53.01           O  
ANISOU 6085  O   ARG D 178     7710   8332   4102    187    966   -895       O  
ATOM   6086  CB  ARG D 178      22.665  20.504 -45.078  1.00 57.57           C  
ANISOU 6086  CB  ARG D 178     8518   8569   4787    225    905  -1185       C  
ATOM   6087  CG  ARG D 178      23.496  21.775 -44.899  1.00 60.83           C  
ANISOU 6087  CG  ARG D 178     9105   8844   5165    170    855  -1331       C  
ATOM   6088  CD  ARG D 178      23.644  22.667 -46.164  1.00 63.73           C  
ANISOU 6088  CD  ARG D 178     9501   9018   5696    215    866  -1375       C  
ATOM   6089  NE  ARG D 178      22.430  23.017 -46.961  1.00 67.00           N  
ANISOU 6089  NE  ARG D 178     9883   9382   6191    398    996  -1375       N  
ATOM   6090  CZ  ARG D 178      22.109  22.598 -48.225  1.00 65.47           C  
ANISOU 6090  CZ  ARG D 178     9546   9164   6166    457   1007  -1276       C  
ATOM   6091  NH1 ARG D 178      20.987  23.002 -48.814  1.00 64.58           N1+
ANISOU 6091  NH1 ARG D 178     9410   9030   6097    630   1116  -1287       N1+
ATOM   6092  NH2 ARG D 178      22.896  21.779 -48.903  1.00 62.97           N  
ANISOU 6092  NH2 ARG D 178     9107   8853   5964    355    907  -1170       N  
ATOM   6093  N   VAL D 179      22.207  17.561 -46.341  1.00 48.95           N  
ANISOU 6093  N   VAL D 179     7065   7624   3911    193    864   -832       N  
ATOM   6094  CA  VAL D 179      21.084  16.726 -46.882  1.00 47.44           C  
ANISOU 6094  CA  VAL D 179     6742   7504   3778    240    953   -736       C  
ATOM   6095  C   VAL D 179      21.558  15.604 -47.806  1.00 45.91           C  
ANISOU 6095  C   VAL D 179     6441   7272   3730    187    871   -606       C  
ATOM   6096  O   VAL D 179      22.636  15.714 -48.408  1.00 45.74           O  
ANISOU 6096  O   VAL D 179     6419   7150   3811    157    768   -606       O  
ATOM   6097  CB  VAL D 179      20.049  17.543 -47.678  1.00 46.48           C  
ANISOU 6097  CB  VAL D 179     6578   7355   3728    374   1069   -803       C  
ATOM   6098  CG1 VAL D 179      19.221  18.452 -46.801  1.00 48.25           C  
ANISOU 6098  CG1 VAL D 179     6884   7643   3804    468   1188   -920       C  
ATOM   6099  CG2 VAL D 179      20.696  18.326 -48.799  1.00 45.53           C  
ANISOU 6099  CG2 VAL D 179     6478   7065   3757    405   1015   -848       C  
ATOM   6100  N   ILE D 180      20.679  14.610 -47.961  1.00 45.46           N  
ANISOU 6100  N   ILE D 180     6295   7297   3680    176    931   -508       N  
ATOM   6101  CA  ILE D 180      20.666  13.580 -49.040  1.00 44.12           C  
ANISOU 6101  CA  ILE D 180     6022   7087   3654    147    900   -399       C  
ATOM   6102  C   ILE D 180      19.511  13.916 -49.963  1.00 44.12           C  
ANISOU 6102  C   ILE D 180     5920   7112   3732    222   1003   -425       C  
ATOM   6103  O   ILE D 180      18.446  14.214 -49.438  1.00 47.31           O  
ANISOU 6103  O   ILE D 180     6302   7634   4040    264   1114   -460       O  
ATOM   6104  CB  ILE D 180      20.450  12.160 -48.499  1.00 44.20           C  
ANISOU 6104  CB  ILE D 180     6029   7168   3598     56    892   -269       C  
ATOM   6105  CG1 ILE D 180      21.395  11.823 -47.349  1.00 45.57           C  
ANISOU 6105  CG1 ILE D 180     6311   7354   3648      0    798   -234       C  
ATOM   6106  CG2 ILE D 180      20.543  11.152 -49.621  1.00 42.64           C  
ANISOU 6106  CG2 ILE D 180     5758   6898   3547     24    854   -175       C  
ATOM   6107  CD1 ILE D 180      21.014  10.579 -46.572  1.00 46.37           C  
ANISOU 6107  CD1 ILE D 180     6453   7530   3637    -83    811   -107       C  
ATOM   6108  N   VAL D 181      19.706  13.803 -51.266  1.00 42.90           N  
ANISOU 6108  N   VAL D 181     5697   6870   3734    240    968   -402       N  
ATOM   6109  CA  VAL D 181      18.650  14.035 -52.285  1.00 43.30           C  
ANISOU 6109  CA  VAL D 181     5638   6951   3862    311   1045   -412       C  
ATOM   6110  C   VAL D 181      18.598  12.808 -53.192  1.00 43.24           C  
ANISOU 6110  C   VAL D 181     5547   6930   3953    235   1010   -310       C  
ATOM   6111  O   VAL D 181      19.651  12.417 -53.689  1.00 43.35           O  
ANISOU 6111  O   VAL D 181     5590   6831   4052    199    917   -278       O  
ATOM   6112  CB  VAL D 181      18.942  15.295 -53.115  1.00 42.55           C  
ANISOU 6112  CB  VAL D 181     5571   6744   3852    415   1035   -498       C  
ATOM   6113  CG1 VAL D 181      17.794  15.604 -54.059  1.00 42.30           C  
ANISOU 6113  CG1 VAL D 181     5433   6764   3876    514   1108   -506       C  
ATOM   6114  CG2 VAL D 181      19.266  16.482 -52.237  1.00 43.31           C  
ANISOU 6114  CG2 VAL D 181     5798   6803   3856    467   1049   -606       C  
ATOM   6115  N   THR D 182      17.417  12.266 -53.447  1.00 44.24           N  
ANISOU 6115  N   THR D 182     5568   7171   4068    212   1084   -271       N  
ATOM   6116  CA  THR D 182      17.242  10.998 -54.183  1.00 44.42           C  
ANISOU 6116  CA  THR D 182     5533   7186   4159    110   1060   -178       C  
ATOM   6117  C   THR D 182      16.104  11.117 -55.193  1.00 45.60           C  
ANISOU 6117  C   THR D 182     5540   7426   4361    142   1118   -190       C  
ATOM   6118  O   THR D 182      15.088  11.757 -54.871  1.00 48.56           O  
ANISOU 6118  O   THR D 182     5839   7944   4668    212   1207   -236       O  
ATOM   6119  CB  THR D 182      16.953   9.868 -53.200  1.00 45.67           C  
ANISOU 6119  CB  THR D 182     5726   7416   4210    -19   1083    -94       C  
ATOM   6120  CG2 THR D 182      18.124   9.614 -52.280  1.00 45.79           C  
ANISOU 6120  CG2 THR D 182     5879   7347   4171    -44   1003    -65       C  
ATOM   6121  OG1 THR D 182      15.788  10.236 -52.458  1.00 47.67           O  
ANISOU 6121  OG1 THR D 182     5916   7851   4344     -9   1198   -124       O  
ATOM   6122  N   GLY D 183      16.270  10.478 -56.351  1.00 44.05           N  
ANISOU 6122  N   GLY D 183     5307   7159   4270     96   1069   -150       N  
ATOM   6123  CA  GLY D 183      15.207  10.245 -57.342  1.00 42.77           C  
ANISOU 6123  CA  GLY D 183     5007   7096   4147     80   1104   -141       C  
ATOM   6124  C   GLY D 183      14.883   8.774 -57.391  1.00 42.34           C  
ANISOU 6124  C   GLY D 183     4943   7065   4080    -98   1103    -58       C  
ATOM   6125  O   GLY D 183      15.802   7.956 -57.243  1.00 41.51           O  
ANISOU 6125  O   GLY D 183     4954   6820   3997   -170   1041     -8       O  
ATOM   6126  N   SER D 184      13.616   8.437 -57.568  1.00 42.94           N  
ANISOU 6126  N   SER D 184     4886   7314   4114   -169   1168    -45       N  
ATOM   6127  CA  SER D 184      13.158   7.033 -57.524  1.00 43.97           C  
ANISOU 6127  CA  SER D 184     5018   7476   4213   -375   1181     31       C  
ATOM   6128  C   SER D 184      12.415   6.681 -58.815  1.00 44.25           C  
ANISOU 6128  C   SER D 184     4929   7579   4306   -438   1172     27       C  
ATOM   6129  O   SER D 184      11.972   7.598 -59.524  1.00 43.79           O  
ANISOU 6129  O   SER D 184     4748   7608   4282   -309   1176    -29       O  
ATOM   6130  CB  SER D 184      12.317   6.820 -56.293  1.00 45.16           C  
ANISOU 6130  CB  SER D 184     5133   7801   4224   -462   1276     57       C  
ATOM   6131  OG  SER D 184      11.604   5.594 -56.357  1.00 46.00           O  
ANISOU 6131  OG  SER D 184     5213   7974   4290   -681   1307    125       O  
ATOM   6132  N   SER D 185      12.287   5.387 -59.095  1.00 45.46           N  
ANISOU 6132  N   SER D 185     5127   7685   4460   -631   1156     85       N  
ATOM   6133  CA  SER D 185      11.267   4.816 -60.010  1.00 47.15           C  
ANISOU 6133  CA  SER D 185     5213   8024   4678   -769   1168     86       C  
ATOM   6134  C   SER D 185       9.873   5.380 -59.672  1.00 48.65           C  
ANISOU 6134  C   SER D 185     5182   8521   4783   -764   1257     60       C  
ATOM   6135  O   SER D 185       9.044   5.478 -60.582  1.00 50.18           O  
ANISOU 6135  O   SER D 185     5210   8866   4991   -781   1253     33       O  
ATOM   6136  CB  SER D 185      11.258   3.308 -59.923  1.00 48.91           C  
ANISOU 6136  CB  SER D 185     5555   8153   4875  -1010   1161    156       C  
ATOM   6137  OG  SER D 185      12.548   2.755 -60.157  1.00 48.52           O  
ANISOU 6137  OG  SER D 185     5710   7826   4898   -985   1084    180       O  
ATOM   6138  N   ASP D 186       9.606   5.748 -58.419  1.00 48.46           N  
ANISOU 6138  N   ASP D 186     5144   8604   4665   -732   1336     64       N  
ATOM   6139  CA  ASP D 186       8.276   6.269 -58.006  1.00 51.32           C  
ANISOU 6139  CA  ASP D 186     5285   9281   4935   -712   1438     34       C  
ATOM   6140  C   ASP D 186       8.033   7.694 -58.542  1.00 25.81           C  
ATOM   6141  O   ASP D 186       6.969   8.242 -58.234  1.00 52.04           O  
ANISOU 6141  O   ASP D 186     5056   9720   4996   -370   1516    -81       O  
ATOM   6142  CB  ASP D 186       8.110   6.208 -56.481  1.00 53.49           C  
ANISOU 6142  CB  ASP D 186     5604   9639   5082   -759   1533     59       C  
ATOM   6143  CG  ASP D 186       8.957   7.214 -55.709  1.00 53.75           C  
ANISOU 6143  CG  ASP D 186     5758   9559   5105   -548   1530     16       C  
ATOM   6144  OD1 ASP D 186       9.406   8.230 -56.312  1.00 53.24           O  
ANISOU 6144  OD1 ASP D 186     5696   9410   5125   -338   1479    -48       O  
ATOM   6145  OD2 ASP D 186       9.185   6.969 -54.500  1.00 55.35           O1-
ANISOU 6145  OD2 ASP D 186     6069   9754   5209   -607   1575     48       O1-
ATOM   6146  N   SER D 187       8.990   8.307 -59.235  1.00 47.58           N  
ANISOU 6146  N   SER D 187     4788   8685   4604   -286   1349    -76       N  
ATOM   6147  CA  SER D 187       8.858   9.611 -59.951  1.00 47.51           C  
ANISOU 6147  CA  SER D 187     4701   8704   4644    -38   1329   -139       C  
ATOM   6148  C   SER D 187       9.115  10.806 -59.042  1.00 47.34           C  
ANISOU 6148  C   SER D 187     4742   8660   4584    168   1378   -194       C  
ATOM   6149  O   SER D 187       9.042  11.941 -59.547  1.00 45.49           O  
ANISOU 6149  O   SER D 187     4483   8417   4384    383   1366   -244       O  
ATOM   6150  CB  SER D 187       7.521   9.758 -60.604  1.00 49.09           C  
ANISOU 6150  CB  SER D 187     4654   9179   4818    -16   1355   -154       C  
ATOM   6151  OG  SER D 187       7.287   8.669 -61.476  1.00 49.73           O  
ANISOU 6151  OG  SER D 187     4690   9280   4927   -226   1303   -114       O  
ATOM   6152  N   THR D 188       9.366  10.566 -57.754  1.00 49.63           N  
ANISOU 6152  N   THR D 188     5123   8940   4795    103   1432   -184       N  
ATOM   6153  CA  THR D 188       9.541  11.634 -56.735  1.00 50.18           C  
ANISOU 6153  CA  THR D 188     5262   9005   4800    273   1489   -246       C  
ATOM   6154  C   THR D 188      11.022  11.884 -56.553  1.00 48.94           C  
ANISOU 6154  C   THR D 188     5331   8570   4695    299   1410   -253       C  
ATOM   6155  O   THR D 188      11.816  10.961 -56.798  1.00 48.06           O  
ANISOU 6155  O   THR D 188     5311   8313   4635    155   1338   -194       O  
ATOM   6156  CB  THR D 188       8.919  11.284 -55.381  1.00 51.20           C  
ANISOU 6156  CB  THR D 188     5354   9313   4785    187   1599   -238       C  
ATOM   6157  CG2 THR D 188       7.452  10.964 -55.524  1.00 53.61           C  
ANISOU 6157  CG2 THR D 188     5410   9929   5031    131   1684   -230       C  
ATOM   6158  OG1 THR D 188       9.615  10.188 -54.780  1.00 49.65           O  
ANISOU 6158  OG1 THR D 188     5302   9002   4562    -20   1569   -163       O  
ATOM   6159  N   VAL D 189      11.345  13.097 -56.126  1.00 50.10           N  
ANISOU 6159  N   VAL D 189     5559   8654   4822    478   1427   -328       N  
ATOM   6160  CA  VAL D 189      12.658  13.417 -55.509  1.00 50.41           C  
ANISOU 6160  CA  VAL D 189     5804   8486   4863    482   1375   -349       C  
ATOM   6161  C   VAL D 189      12.398  13.650 -54.033  1.00 50.52           C  
ANISOU 6161  C   VAL D 189     5862   8600   4733    491   1459   -385       C  
ATOM   6162  O   VAL D 189      11.386  14.293 -53.728  1.00 51.44           O  
ANISOU 6162  O   VAL D 189     5882   8884   4780    612   1557   -440       O  
ATOM   6163  CB  VAL D 189      13.329  14.626 -56.178  1.00 51.18           C  
ANISOU 6163  CB  VAL D 189     5993   8412   5040    642   1324   -413       C  
ATOM   6164  CG1 VAL D 189      14.620  15.032 -55.478  1.00 51.09           C  
ANISOU 6164  CG1 VAL D 189     6172   8224   5016    628   1274   -447       C  
ATOM   6165  CG2 VAL D 189      13.586  14.328 -57.640  1.00 49.86           C  
ANISOU 6165  CG2 VAL D 189     5785   8161   4999    619   1248   -371       C  
ATOM   6166  N   ARG D 190      13.264  13.107 -53.183  1.00 49.36           N  
ANISOU 6166  N   ARG D 190     5849   8367   4538    374   1420   -351       N  
ATOM   6167  CA  ARG D 190      13.158  13.265 -51.720  1.00 50.85           C  
ANISOU 6167  CA  ARG D 190     6108   8642   4571    363   1488   -380       C  
ATOM   6168  C   ARG D 190      14.452  13.867 -51.191  1.00 49.05           C  
ANISOU 6168  C   ARG D 190     6069   8234   4332    395   1412   -427       C  
ATOM   6169  O   ARG D 190      15.525  13.408 -51.564  1.00 46.23           O  
ANISOU 6169  O   ARG D 190     5785   7725   4056    322   1302   -380       O  
ATOM   6170  CB  ARG D 190      12.821  11.946 -51.036  1.00 52.53           C  
ANISOU 6170  CB  ARG D 190     6300   8965   4694    169   1520   -281       C  
ATOM   6171  CG  ARG D 190      11.322  11.705 -50.933  1.00 55.10           C  
ANISOU 6171  CG  ARG D 190     6440   9551   4946    142   1648   -274       C  
ATOM   6172  CD  ARG D 190      10.960  10.280 -50.565  1.00 57.08           C  
ANISOU 6172  CD  ARG D 190     6669   9887   5132    -92   1673   -160       C  
ATOM   6173  NE  ARG D 190       9.756   9.864 -51.288  1.00 59.26           N  
ANISOU 6173  NE  ARG D 190     6735  10348   5432   -156   1735   -138       N  
ATOM   6174  CZ  ARG D 190       8.562   9.626 -50.785  1.00 60.97           C  
ANISOU 6174  CZ  ARG D 190     6802  10830   5535   -229   1862   -131       C  
ATOM   6175  NH1 ARG D 190       8.332   9.794 -49.493  1.00 62.79           N1+
ANISOU 6175  NH1 ARG D 190     7074  11179   5605   -237   1959   -147       N1+
ATOM   6176  NH2 ARG D 190       7.607   9.218 -51.610  1.00 61.64           N  
ANISOU 6176  NH2 ARG D 190     6688  11073   5661   -303   1889   -111       N  
ATOM   6177  N   VAL D 191      14.292  14.877 -50.343  1.00 50.44           N  
ANISOU 6177  N   VAL D 191     6313   8447   4404    503   1475   -526       N  
ATOM   6178  CA  VAL D 191      15.371  15.510 -49.544  1.00 49.90           C  
ANISOU 6178  CA  VAL D 191     6431   8253   4276    510   1419   -589       C  
ATOM   6179  C   VAL D 191      15.319  14.906 -48.150  1.00 49.50           C  
ANISOU 6179  C   VAL D 191     6436   8318   4054    406   1454   -559       C  
ATOM   6180  O   VAL D 191      14.257  14.996 -47.527  1.00 52.37           O  
ANISOU 6180  O   VAL D 191     6738   8861   4300    440   1581   -586       O  
ATOM   6181  CB  VAL D 191      15.181  17.032 -49.502  1.00 51.37           C  
ANISOU 6181  CB  VAL D 191     6687   8389   4441    692   1472   -727       C  
ATOM   6182  CG1 VAL D 191      16.362  17.707 -48.809  1.00 51.31           C  
ANISOU 6182  CG1 VAL D 191     6878   8236   4381    669   1401   -802       C  
ATOM   6183  CG2 VAL D 191      14.979  17.574 -50.919  1.00 50.99           C  
ANISOU 6183  CG2 VAL D 191     6574   8253   4547    806   1454   -737       C  
ATOM   6184  N   TRP D 192      16.418  14.307 -47.703  1.00 47.11           N  
ANISOU 6184  N   TRP D 192     6239   7928   3731    290   1346   -501       N  
ATOM   6185  CA  TRP D 192      16.518  13.738 -46.343  1.00 48.26           C  
ANISOU 6185  CA  TRP D 192     6470   8168   3700    190   1358   -460       C  
ATOM   6186  C   TRP D 192      17.527  14.551 -45.529  1.00 48.93           C  
ANISOU 6186  C   TRP D 192     6717   8175   3698    211   1289   -548       C  
ATOM   6187  O   TRP D 192      18.480  15.100 -46.125  1.00 48.38           O  
ANISOU 6187  O   TRP D 192     6693   7952   3739    240   1190   -592       O  
ATOM   6188  CB  TRP D 192      16.888  12.255 -46.395  1.00 46.84           C  
ANISOU 6188  CB  TRP D 192     6288   7968   3541     40   1284   -304       C  
ATOM   6189  CG  TRP D 192      16.208  11.475 -47.469  1.00 45.30           C  
ANISOU 6189  CG  TRP D 192     5957   7786   3469     -2   1312   -227       C  
ATOM   6190  CD1 TRP D 192      16.412  11.611 -48.804  1.00 43.86           C  
ANISOU 6190  CD1 TRP D 192     5703   7496   3465     48   1261   -236       C  
ATOM   6191  CD2 TRP D 192      15.256  10.404 -47.319  1.00 45.57           C  
ANISOU 6191  CD2 TRP D 192     5922   7948   3447   -125   1390   -129       C  
ATOM   6192  CE2 TRP D 192      14.929   9.957 -48.617  1.00 44.75           C  
ANISOU 6192  CE2 TRP D 192     5703   7803   3497   -144   1376    -92       C  
ATOM   6193  CE3 TRP D 192      14.656   9.772 -46.233  1.00 47.06           C  
ANISOU 6193  CE3 TRP D 192     6139   8281   3461   -237   1472    -67       C  
ATOM   6194  NE1 TRP D 192      15.653  10.713 -49.498  1.00 43.72           N  
ANISOU 6194  NE1 TRP D 192     5575   7530   3505    -28   1297   -158       N  
ATOM   6195  CZ2 TRP D 192      14.031   8.919 -48.859  1.00 44.95           C  
ANISOU 6195  CZ2 TRP D 192     5643   7923   3512   -280   1436     -5       C  
ATOM   6196  CZ3 TRP D 192      13.765   8.753 -46.468  1.00 47.73           C  
ANISOU 6196  CZ3 TRP D 192     6139   8459   3537   -376   1539     27       C  
ATOM   6197  CH2 TRP D 192      13.451   8.340 -47.764  1.00 46.93           C  
ANISOU 6197  CH2 TRP D 192     5924   8314   3595   -401   1519     53       C  
ATOM   6198  N   ASP D 193      17.317  14.624 -44.213  1.00 50.34           N  
ANISOU 6198  N   ASP D 193     6981   8469   3678    183   1343   -576       N  
ATOM   6199  CA  ASP D 193      18.330  15.146 -43.266  1.00 50.26           C  
ANISOU 6199  CA  ASP D 193     7136   8411   3549    158   1259   -642       C  
ATOM   6200  C   ASP D 193      19.457  14.134 -43.235  1.00 20.66           C  
ATOM   6201  O   ASP D 193      19.180  12.989 -42.893  1.00 48.49           O  
ANISOU 6201  O   ASP D 193     6928   8197   3300    -40   1108   -387       O  
ATOM   6202  CB  ASP D 193      17.800  15.325 -41.851  1.00 52.53           C  
ANISOU 6202  CB  ASP D 193     7509   8854   3595    145   1356   -691       C  
ATOM   6203  CG  ASP D 193      18.811  16.034 -40.965  1.00 54.00           C  
ANISOU 6203  CG  ASP D 193     7870   8991   3658    123   1266   -787       C  
ATOM   6204  OD1 ASP D 193      19.084  17.217 -41.251  1.00 54.72           O  
ANISOU 6204  OD1 ASP D 193     8022   8975   3795    204   1261   -927       O  
ATOM   6205  OD2 ASP D 193      19.375  15.374 -40.048  1.00 55.06           O1-
ANISOU 6205  OD2 ASP D 193     8084   9183   3654     18   1188   -714       O1-
ATOM   6206  N   VAL D 194      20.669  14.547 -43.587  1.00 47.08           N  
ANISOU 6206  N   VAL D 194     6810   7816   3263     43    966   -554       N  
ATOM   6207  CA  VAL D 194      21.810  13.602 -43.743  1.00 46.15           C  
ANISOU 6207  CA  VAL D 194     6691   7640   3204    -30    808   -437       C  
ATOM   6208  C   VAL D 194      22.148  12.969 -42.384  1.00 47.05           C  
ANISOU 6208  C   VAL D 194     6909   7854   3115   -106    753   -368       C  
ATOM   6209  O   VAL D 194      22.865  11.942 -42.402  1.00 46.94           O  
ANISOU 6209  O   VAL D 194     6896   7814   3127   -149    638   -240       O  
ATOM   6210  CB  VAL D 194      23.029  14.306 -44.368  1.00 45.01           C  
ANISOU 6210  CB  VAL D 194     6551   7373   3179    -18    687   -507       C  
ATOM   6211  CG1 VAL D 194      23.702  15.252 -43.386  1.00 46.69           C  
ANISOU 6211  CG1 VAL D 194     6887   7607   3247    -48    633   -625       C  
ATOM   6212  CG2 VAL D 194      24.026  13.313 -44.908  1.00 43.65           C  
ANISOU 6212  CG2 VAL D 194     6321   7146   3117    -53    551   -389       C  
ATOM   6213  N   ASN D 195      21.669  13.542 -41.265  1.00 48.01           N  
ANISOU 6213  N   ASN D 195     7122   8084   3038   -111    830   -448       N  
ATOM   6214  CA  ASN D 195      21.967  13.061 -39.886  1.00 49.54           C  
ANISOU 6214  CA  ASN D 195     7433   8386   3003   -186    782   -392       C  
ATOM   6215  C   ASN D 195      20.786  12.287 -39.299  1.00 50.31           C  
ANISOU 6215  C   ASN D 195     7533   8612   2969   -228    920   -301       C  
ATOM   6216  O   ASN D 195      20.957  11.092 -39.047  1.00 50.81           O  
ANISOU 6216  O   ASN D 195     7624   8688   2993   -299    864   -139       O  
ATOM   6217  CB  ASN D 195      22.368  14.212 -38.966  1.00 50.75           C  
ANISOU 6217  CB  ASN D 195     7708   8579   2995   -185    763   -550       C  
ATOM   6218  CG  ASN D 195      23.500  15.027 -39.564  1.00 49.85           C  
ANISOU 6218  CG  ASN D 195     7591   8343   3007   -176    636   -646       C  
ATOM   6219  ND2 ASN D 195      23.263  16.312 -39.772  1.00 49.76           N  
ANISOU 6219  ND2 ASN D 195     7620   8271   3016   -126    708   -815       N  
ATOM   6220  OD1 ASN D 195      24.575  14.507 -39.860  1.00 48.37           O  
ANISOU 6220  OD1 ASN D 195     7366   8114   2898   -211    480   -568       O  
ATOM   6221  N   THR D 196      19.641  12.941 -39.083  1.00 51.00           N  
ANISOU 6221  N   THR D 196     7598   8794   2985   -186   1095   -400       N  
ATOM   6222  CA  THR D 196      18.415  12.334 -38.479  1.00 51.74           C  
ANISOU 6222  CA  THR D 196     7671   9052   2935   -238   1255   -333       C  
ATOM   6223  C   THR D 196      17.807  11.297 -39.435  1.00 50.31           C  
ANISOU 6223  C   THR D 196     7360   8849   2907   -283   1293   -199       C  
ATOM   6224  O   THR D 196      17.116  10.385 -38.967  1.00 51.32           O  
ANISOU 6224  O   THR D 196     7489   9082   2926   -385   1373    -85       O  
ATOM   6225  CB  THR D 196      17.368  13.386 -38.077  1.00 52.74           C  
ANISOU 6225  CB  THR D 196     7780   9303   2956   -153   1438   -492       C  
ATOM   6226  CG2 THR D 196      17.944  14.466 -37.195  1.00 54.05           C  
ANISOU 6226  CG2 THR D 196     8098   9467   2972   -111   1406   -646       C  
ATOM   6227  OG1 THR D 196      16.746  13.989 -39.210  1.00 51.10           O  
ANISOU 6227  OG1 THR D 196     7433   9048   2936    -39   1515   -569       O  
ATOM   6228  N   GLY D 197      18.061  11.432 -40.730  1.00 48.27           N  
ANISOU 6228  N   GLY D 197     7002   8456   2883   -224   1240   -213       N  
ATOM   6229  CA  GLY D 197      17.491  10.540 -41.756  1.00 47.59           C  
ANISOU 6229  CA  GLY D 197     6793   8339   2949   -266   1272   -109       C  
ATOM   6230  C   GLY D 197      16.022  10.835 -42.005  1.00 48.10           C  
ANISOU 6230  C   GLY D 197     6718   8552   3006   -241   1457   -161       C  
ATOM   6231  O   GLY D 197      15.382  10.040 -42.708  1.00 46.90           O  
ANISOU 6231  O   GLY D 197     6460   8418   2941   -308   1498    -75       O  
ATOM   6232  N   GLU D 198      15.501  11.938 -41.466  1.00 49.83           N  
ANISOU 6232  N   GLU D 198     6935   8877   3122   -144   1563   -303       N  
ATOM   6233  CA  GLU D 198      14.082  12.321 -41.680  1.00 51.72           C  
ANISOU 6233  CA  GLU D 198     7018   9286   3347    -81   1744   -365       C  
ATOM   6234  C   GLU D 198      13.917  12.852 -43.112  1.00 18.92           C  
ATOM   6235  O   GLU D 198      14.786  13.598 -43.568  1.00 48.55           O  
ANISOU 6235  O   GLU D 198     6553   8621   3272    128   1627   -491       O  
ATOM   6236  CB  GLU D 198      13.578  13.347 -40.656  1.00 53.91           C  
ANISOU 6236  CB  GLU D 198     7343   9703   3438     17   1871   -508       C  
ATOM   6237  CG  GLU D 198      12.063  13.461 -40.701  1.00 55.80           C  
ANISOU 6237  CG  GLU D 198     7402  10172   3630     65   2067   -542       C  
ATOM   6238  CD  GLU D 198      11.401  14.637 -39.996  1.00 58.74           C  
ANISOU 6238  CD  GLU D 198     7781  10679   3859    229   2215   -711       C  
ATOM   6239  OE1 GLU D 198      12.128  15.430 -39.328  1.00 59.72           O  
ANISOU 6239  OE1 GLU D 198     8088  10708   3894    292   2171   -816       O  
ATOM   6240  OE2 GLU D 198      10.149  14.763 -40.136  1.00 60.20           O1-
ANISOU 6240  OE2 GLU D 198     7784  11070   4020    297   2375   -743       O1-
ATOM   6241  N   VAL D 199      12.821  12.488 -43.779  1.00 51.37           N  
ANISOU 6241  N   VAL D 199     6660   9268   3589     28   1821   -384       N  
ATOM   6242  CA  VAL D 199      12.391  13.133 -45.044  1.00 50.99           C  
ANISOU 6242  CA  VAL D 199     6472   9189   3715    168   1832   -448       C  
ATOM   6243  C   VAL D 199      12.012  14.578 -44.739  1.00 52.01           C  
ANISOU 6243  C   VAL D 199     6613   9362   3787    376   1920   -613       C  
ATOM   6244  O   VAL D 199      11.131  14.776 -43.940  1.00 52.86           O  
ANISOU 6244  O   VAL D 199     6673   9669   3742    409   2062   -659       O  
ATOM   6245  CB  VAL D 199      11.236  12.363 -45.694  1.00 51.93           C  
ANISOU 6245  CB  VAL D 199     6381   9470   3878     92   1913   -374       C  
ATOM   6246  CG1 VAL D 199      10.602  13.128 -46.846  1.00 51.92           C  
ANISOU 6246  CG1 VAL D 199     6220   9495   4014    260   1940   -447       C  
ATOM   6247  CG2 VAL D 199      11.736  11.014 -46.176  1.00 50.68           C  
ANISOU 6247  CG2 VAL D 199     6252   9203   3802   -100   1810   -226       C  
ATOM   6248  N   LEU D 200      12.647  15.532 -45.410  1.00 51.61           N  
ANISOU 6248  N   LEU D 200     6630   9125   3856    511   1843   -695       N  
ATOM   6249  CA  LEU D 200      12.411  16.978 -45.175  1.00 53.54           C  
ANISOU 6249  CA  LEU D 200     6939   9349   4054    719   1913   -857       C  
ATOM   6250  C   LEU D 200      11.546  17.580 -46.276  1.00 53.61           C  
ANISOU 6250  C   LEU D 200     6796   9389   4184    900   1968   -897       C  
ATOM   6251  O   LEU D 200      10.905  18.596 -46.015  1.00 57.33           O  
ANISOU 6251  O   LEU D 200     7272   9918   4591   1094   2072  -1016       O  
ATOM   6252  CB  LEU D 200      13.755  17.704 -45.126  1.00 52.94           C  
ANISOU 6252  CB  LEU D 200     7073   9027   4013    731   1788   -923       C  
ATOM   6253  CG  LEU D 200      14.746  17.227 -44.073  1.00 53.28           C  
ANISOU 6253  CG  LEU D 200     7269   9039   3937    572   1705   -892       C  
ATOM   6254  CD1 LEU D 200      15.948  18.167 -44.067  1.00 53.07           C  
ANISOU 6254  CD1 LEU D 200     7423   8801   3939    596   1594   -988       C  
ATOM   6255  CD2 LEU D 200      14.112  17.121 -42.694  1.00 54.99           C  
ANISOU 6255  CD2 LEU D 200     7520   9453   3921    548   1826   -922       C  
ATOM   6256  N   ASN D 201      11.552  17.001 -47.467  1.00 51.97           N  
ANISOU 6256  N   ASN D 201     6469   9138   4138    850   1896   -805       N  
ATOM   6257  CA  ASN D 201      10.822  17.522 -48.651  1.00 52.35           C  
ANISOU 6257  CA  ASN D 201     6374   9208   4307   1015   1918   -826       C  
ATOM   6258  C   ASN D 201      10.639  16.354 -49.629  1.00 51.71           C  
ANISOU 6258  C   ASN D 201     6134   9173   4342    866   1860   -696       C  
ATOM   6259  O   ASN D 201      11.433  15.401 -49.600  1.00 49.80           O  
ANISOU 6259  O   ASN D 201     5956   8838   4129    675   1770   -606       O  
ATOM   6260  CB  ASN D 201      11.564  18.710 -49.278  1.00 51.71           C  
ANISOU 6260  CB  ASN D 201     6446   8876   4323   1165   1845   -907       C  
ATOM   6261  CG  ASN D 201      10.694  19.642 -50.100  1.00 52.48           C  
ANISOU 6261  CG  ASN D 201     6456   9004   4479   1410   1900   -965       C  
ATOM   6262  ND2 ASN D 201      11.163  20.861 -50.324  1.00 52.79           N  
ANISOU 6262  ND2 ASN D 201     6672   8836   4551   1566   1875  -1056       N  
ATOM   6263  OD1 ASN D 201       9.615  19.276 -50.556  1.00 52.64           O  
ANISOU 6263  OD1 ASN D 201     6256   9230   4513   1457   1959   -925       O  
ATOM   6264  N   THR D 202       9.596  16.427 -50.441  1.00 53.27           N  
ANISOU 6264  N   THR D 202     6132   9517   4591    960   1909   -690       N  
ATOM   6265  CA  THR D 202       9.279  15.477 -51.523  1.00 54.18           C  
ANISOU 6265  CA  THR D 202     6087   9685   4814    839   1856   -589       C  
ATOM   6266  C   THR D 202       8.812  16.295 -52.715  1.00 55.67           C  
ANISOU 6266  C   THR D 202     6178   9867   5106   1042   1838   -626       C  
ATOM   6267  O   THR D 202       7.768  16.953 -52.596  1.00 60.10           O  
ANISOU 6267  O   THR D 202     6610  10615   5610   1224   1938   -687       O  
ATOM   6268  CB  THR D 202       8.182  14.489 -51.127  1.00 56.47           C  
ANISOU 6268  CB  THR D 202     6182  10260   5012    692   1953   -528       C  
ATOM   6269  CG2 THR D 202       7.891  13.475 -52.209  1.00 55.72           C  
ANISOU 6269  CG2 THR D 202     5948  10207   5018    537   1893   -433       C  
ATOM   6270  OG1 THR D 202       8.621  13.842 -49.937  1.00 58.18           O  
ANISOU 6270  OG1 THR D 202     6523  10471   5112    524   1975   -491       O  
ATOM   6271  N   LEU D 203       9.568  16.270 -53.808  1.00 55.60           N  
ANISOU 6271  N   LEU D 203     6232   9658   5236   1023   1718   -590       N  
ATOM   6272  CA  LEU D 203       9.216  16.989 -55.055  1.00 55.80           C  
ANISOU 6272  CA  LEU D 203     6187   9657   5358   1201   1683   -606       C  
ATOM   6273  C   LEU D 203       8.417  16.034 -55.930  1.00 56.89           C  
ANISOU 6273  C   LEU D 203     6100   9978   5539   1092   1667   -528       C  
ATOM   6274  O   LEU D 203       8.990  15.028 -56.396  1.00 56.17           O  
ANISOU 6274  O   LEU D 203     6032   9798   5511    888   1589   -453       O  
ATOM   6275  CB  LEU D 203      10.490  17.460 -55.750  1.00 52.97           C  
ANISOU 6275  CB  LEU D 203     6023   8994   5108   1213   1570   -609       C  
ATOM   6276  CG  LEU D 203      11.375  18.369 -54.907  1.00 52.72           C  
ANISOU 6276  CG  LEU D 203     6224   8775   5033   1276   1573   -690       C  
ATOM   6277  CD1 LEU D 203      12.586  18.798 -55.706  1.00 52.04           C  
ANISOU 6277  CD1 LEU D 203     6299   8417   5056   1261   1464   -686       C  
ATOM   6278  CD2 LEU D 203      10.618  19.591 -54.444  1.00 54.06           C  
ANISOU 6278  CD2 LEU D 203     6415   9002   5123   1525   1671   -792       C  
ATOM   6279  N   ILE D 204       7.129  16.334 -56.087  1.00 59.69           N  
ANISOU 6279  N   ILE D 204     6241  10589   5848   1225   1743   -550       N  
ATOM   6280  CA  ILE D 204       6.244  15.732 -57.123  1.00 62.22           C  
ANISOU 6280  CA  ILE D 204     6324  11107   6209   1171   1716   -495       C  
ATOM   6281  C   ILE D 204       6.318  16.640 -58.351  1.00 60.21           C  
ANISOU 6281  C   ILE D 204     6087  10744   6046   1384   1638   -508       C  
ATOM   6282  O   ILE D 204       6.129  17.876 -58.181  1.00 62.19           O  
ANISOU 6282  O   ILE D 204     6393  10963   6274   1655   1677   -577       O  
ATOM   6283  CB  ILE D 204       4.801  15.563 -56.604  1.00 66.82           C  
ANISOU 6283  CB  ILE D 204     6639  12068   6683   1195   1837   -510       C  
ATOM   6284  CG1 ILE D 204       4.775  14.662 -55.366  1.00 69.14           C  
ANISOU 6284  CG1 ILE D 204     6945  12455   6872    964   1921   -487       C  
ATOM   6285  CG2 ILE D 204       3.883  15.036 -57.704  1.00 68.09           C  
ANISOU 6285  CG2 ILE D 204     6541  12451   6878   1140   1798   -462       C  
ATOM   6286  CD1 ILE D 204       4.809  15.394 -54.020  1.00 72.46           C  
ANISOU 6286  CD1 ILE D 204     7467  12889   7176   1094   2031   -566       C  
ATOM   6287  N   HIS D 205       6.625  16.063 -59.513  1.00 56.72           N  
ANISOU 6287  N   HIS D 205     5627  10229   5695   1267   1534   -446       N  
ATOM   6288  CA  HIS D 205       6.810  16.820 -60.776  1.00 54.65           C  
ANISOU 6288  CA  HIS D 205     5405   9845   5514   1435   1449   -442       C  
ATOM   6289  C   HIS D 205       6.935  15.855 -61.950  1.00 52.46           C  
ANISOU 6289  C   HIS D 205     5060   9567   5305   1248   1353   -372       C  
ATOM   6290  O   HIS D 205       6.022  15.774 -62.765  1.00 53.12           O  
ANISOU 6290  O   HIS D 205     4949   9852   5383   1292   1328   -352       O  
ATOM   6291  CB  HIS D 205       8.017  17.752 -60.710  1.00 52.88           C  
ANISOU 6291  CB  HIS D 205     5463   9292   5337   1538   1414   -477       C  
ATOM   6292  CG  HIS D 205       8.139  18.480 -61.992  1.00 53.36           C  
ANISOU 6292  CG  HIS D 205     5569   9241   5465   1689   1337   -460       C  
ATOM   6293  CD2 HIS D 205       7.244  19.244 -62.659  1.00 55.00           C  
ANISOU 6293  CD2 HIS D 205     5672   9567   5659   1927   1334   -463       C  
ATOM   6294  ND1 HIS D 205       9.230  18.327 -62.813  1.00 51.17           N  
ANISOU 6294  ND1 HIS D 205     5441   8730   5273   1584   1247   -424       N  
ATOM   6295  CE1 HIS D 205       9.033  19.008 -63.919  1.00 52.18           C  
ANISOU 6295  CE1 HIS D 205     5573   8821   5431   1740   1195   -405       C  
ATOM   6296  NE2 HIS D 205       7.816  19.575 -63.856  1.00 54.07           N  
ANISOU 6296  NE2 HIS D 205     5662   9269   5611   1957   1240   -423       N  
ATOM   6297  N   HIS D 206       8.038  15.140 -62.034  1.00 50.11           N  
ANISOU 6297  N   HIS D 206     4918   9058   5064   1051   1298   -341       N  
ATOM   6298  CA  HIS D 206       8.214  14.113 -63.085  1.00 50.25           C  
ANISOU 6298  CA  HIS D 206     4896   9057   5139    860   1216   -285       C  
ATOM   6299  C   HIS D 206       7.030  13.169 -62.966  1.00 52.26           C  
ANISOU 6299  C   HIS D 206     4919   9608   5331    708   1255   -262       C  
ATOM   6300  O   HIS D 206       6.683  12.866 -61.838  1.00 53.51           O  
ANISOU 6300  O   HIS D 206     5036   9876   5418    638   1339   -269       O  
ATOM   6301  CB  HIS D 206       9.584  13.436 -62.976  1.00 47.97           C  
ANISOU 6301  CB  HIS D 206     4810   8508   4910    689   1170   -262       C  
ATOM   6302  CG  HIS D 206      10.686  14.405 -63.194  1.00 46.99           C  
ANISOU 6302  CG  HIS D 206     4879   8133   4842    821   1132   -288       C  
ATOM   6303  CD2 HIS D 206      11.543  14.990 -62.336  1.00 47.35           C  
ANISOU 6303  CD2 HIS D 206     5091   8018   4884    869   1151   -323       C  
ATOM   6304  ND1 HIS D 206      10.953  14.940 -64.435  1.00 47.00           N  
ANISOU 6304  ND1 HIS D 206     4916   8040   4901    911   1067   -280       N  
ATOM   6305  CE1 HIS D 206      11.955  15.794 -64.338  1.00 47.16           C  
ANISOU 6305  CE1 HIS D 206     5120   7842   4955    995   1054   -306       C  
ATOM   6306  NE2 HIS D 206      12.339  15.838 -63.065  1.00 47.78           N  
ANISOU 6306  NE2 HIS D 206     5277   7878   4998    967   1100   -336       N  
ATOM   6307  N   ASN D 207       6.421  12.792 -64.090  1.00 55.01           N  
ANISOU 6307  N   ASN D 207     5120  10088   5693    658   1197   -238       N  
ATOM   6308  CA  ASN D 207       5.281  11.833 -64.141  1.00 58.33           C  
ANISOU 6308  CA  ASN D 207     5307  10804   6052    470   1220   -217       C  
ATOM   6309  C   ASN D 207       5.825  10.426 -64.410  1.00 56.26           C  
ANISOU 6309  C   ASN D 207     5142  10415   5820    160   1176   -177       C  
ATOM   6310  O   ASN D 207       5.009   9.499 -64.493  1.00 58.19           O  
ANISOU 6310  O   ASN D 207     5236  10858   6016    -51   1189   -159       O  
ATOM   6311  CB  ASN D 207       4.219  12.262 -65.160  1.00 62.09           C  
ANISOU 6311  CB  ASN D 207     5553  11532   6508    596   1176   -221       C  
ATOM   6312  CG  ASN D 207       4.844  12.785 -66.433  1.00 63.59           C  
ANISOU 6312  CG  ASN D 207     5858  11535   6769    717   1069   -211       C  
ATOM   6313  ND2 ASN D 207       4.597  14.047 -66.746  1.00 65.53           N  
ANISOU 6313  ND2 ASN D 207     6085  11803   7012   1018   1057   -226       N  
ATOM   6314  OD1 ASN D 207       5.587  12.064 -67.098  1.00 65.96           O  
ANISOU 6314  OD1 ASN D 207     6283  11659   7120    546   1003   -190       O  
ATOM   6315  N   GLU D 208       7.147  10.284 -64.558  1.00 54.00           N  
ANISOU 6315  N   GLU D 208     5096   9812   5607    136   1127   -168       N  
ATOM   6316  CA  GLU D 208       7.844   8.988 -64.782  1.00 51.47           C  
ANISOU 6316  CA  GLU D 208     4911   9322   5323   -114   1086   -134       C  
ATOM   6317  C   GLU D 208       9.128   8.971 -63.950  1.00 26.90           C  
ATOM   6318  O   GLU D 208       9.512  10.023 -63.430  1.00 45.34           O  
ANISOU 6318  O   GLU D 208     4420   8221   4585     87   1118   -154       O  
ATOM   6319  CB  GLU D 208       8.125   8.790 -66.276  1.00 50.90           C  
ANISOU 6319  CB  GLU D 208     4862   9168   5310   -135    991   -135       C  
ATOM   6320  CG  GLU D 208       7.299   7.711 -66.965  1.00 52.37           C  
ANISOU 6320  CG  GLU D 208     4925   9512   5459   -365    963   -124       C  
ATOM   6321  CD  GLU D 208       7.206   7.875 -68.476  1.00 53.71           C  
ANISOU 6321  CD  GLU D 208     5052   9700   5653   -327    872   -138       C  
ATOM   6322  OE1 GLU D 208       6.922   9.003 -68.941  1.00 54.60           O  
ANISOU 6322  OE1 GLU D 208     5081   9899   5765    -99    850   -149       O  
ATOM   6323  OE2 GLU D 208       7.419   6.881 -69.196  1.00 55.03           O1-
ANISOU 6323  OE2 GLU D 208     5288   9790   5833   -519    825   -138       O1-
ATOM   6324  N   ALA D 209       9.742   7.798 -63.828  1.00 45.89           N  
ANISOU 6324  N   ALA D 209     4564   8202   4668   -299   1074    -91       N  
ATOM   6325  CA  ALA D 209      10.958   7.542 -63.023  1.00 44.93           C  
ANISOU 6325  CA  ALA D 209     4649   7852   4571   -311   1069    -71       C  
ATOM   6326  C   ALA D 209      11.956   8.702 -63.168  1.00 43.57           C  
ANISOU 6326  C   ALA D 209     4572   7524   4460    -99   1036   -107       C  
ATOM   6327  O   ALA D 209      12.236   9.167 -64.291  1.00 41.51           O  
ANISOU 6327  O   ALA D 209     4311   7202   4260    -14    985   -128       O  
ATOM   6328  CB  ALA D 209      11.590   6.244 -63.460  1.00 44.79           C  
ANISOU 6328  CB  ALA D 209     4762   7662   4593   -489   1019    -35       C  
ATOM   6329  N   VAL D 210      12.488   9.158 -62.042  1.00 43.74           N  
ANISOU 6329  N   VAL D 210     4682   7485   4454    -33   1066   -115       N  
ATOM   6330  CA  VAL D 210      13.554  10.194 -61.995  1.00 41.72           C  
ANISOU 6330  CA  VAL D 210     4540   7066   4244    125   1036   -151       C  
ATOM   6331  C   VAL D 210      14.895   9.482 -61.977  1.00 41.09           C  
ANISOU 6331  C   VAL D 210     4612   6781   4219     46    976   -125       C  
ATOM   6332  O   VAL D 210      15.166   8.788 -60.985  1.00 40.44           O  
ANISOU 6332  O   VAL D 210     4599   6674   4094    -42    986    -90       O  
ATOM   6333  CB  VAL D 210      13.394  11.044 -60.736  1.00 42.22           C  
ANISOU 6333  CB  VAL D 210     4621   7187   4233    226   1097   -185       C  
ATOM   6334  CG1 VAL D 210      14.534  12.028 -60.603  1.00 41.31           C  
ANISOU 6334  CG1 VAL D 210     4644   6897   4157    343   1063   -227       C  
ATOM   6335  CG2 VAL D 210      12.053  11.736 -60.713  1.00 43.45           C  
ANISOU 6335  CG2 VAL D 210     4617   7560   4331    333   1165   -217       C  
ATOM   6336  N   LEU D 211      15.691   9.657 -63.035  1.00 41.61           N  
ANISOU 6336  N   LEU D 211     4725   6716   4369     87    918   -137       N  
ATOM   6337  CA  LEU D 211      16.823   8.750 -63.376  1.00 40.72           C  
ANISOU 6337  CA  LEU D 211     4718   6438   4317     10    862   -112       C  
ATOM   6338  C   LEU D 211      18.129   9.351 -62.881  1.00 39.46           C  
ANISOU 6338  C   LEU D 211     4657   6151   4184     86    832   -131       C  
ATOM   6339  O   LEU D 211      19.063   8.571 -62.593  1.00 39.07           O  
ANISOU 6339  O   LEU D 211     4689   6000   4157     37    793   -104       O  
ATOM   6340  CB  LEU D 211      16.890   8.552 -64.892  1.00 40.01           C  
ANISOU 6340  CB  LEU D 211     4605   6308   4291      1    827   -122       C  
ATOM   6341  CG  LEU D 211      15.670   7.881 -65.513  1.00 40.93           C  
ANISOU 6341  CG  LEU D 211     4620   6554   4376    -99    840   -110       C  
ATOM   6342  CD1 LEU D 211      15.853   7.733 -67.014  1.00 42.13           C  
ANISOU 6342  CD1 LEU D 211     4770   6660   4579   -104    797   -127       C  
ATOM   6343  CD2 LEU D 211      15.414   6.528 -64.883  1.00 41.80           C  
ANISOU 6343  CD2 LEU D 211     4771   6663   4450   -267    853    -67       C  
ATOM   6344  N   HIS D 212      18.208  10.674 -62.865  1.00 38.22           N  
ANISOU 6344  N   HIS D 212     4498   5997   4026    201    844   -178       N  
ATOM   6345  CA  HIS D 212      19.425  11.361 -62.402  1.00 37.97           C  
ANISOU 6345  CA  HIS D 212     4557   5858   4012    248    814   -206       C  
ATOM   6346  C   HIS D 212      19.049  12.703 -61.803  1.00 37.69           C  
ANISOU 6346  C   HIS D 212     4537   5858   3925    349    854   -257       C  
ATOM   6347  O   HIS D 212      17.956  13.200 -62.073  1.00 37.25           O  
ANISOU 6347  O   HIS D 212     4415   5894   3843    418    899   -271       O  
ATOM   6348  CB  HIS D 212      20.443  11.489 -63.536  1.00 38.59           C  
ANISOU 6348  CB  HIS D 212     4664   5824   4176    258    770   -217       C  
ATOM   6349  CG  HIS D 212      21.839  11.363 -63.041  1.00 38.99           C  
ANISOU 6349  CG  HIS D 212     4778   5786   4249    237    724   -220       C  
ATOM   6350  CD2 HIS D 212      22.741  12.288 -62.638  1.00 40.18           C  
ANISOU 6350  CD2 HIS D 212     4979   5888   4399    263    705   -260       C  
ATOM   6351  ND1 HIS D 212      22.429  10.138 -62.885  1.00 39.26           N  
ANISOU 6351  ND1 HIS D 212     4829   5785   4302    181    687   -180       N  
ATOM   6352  CE1 HIS D 212      23.645  10.307 -62.394  1.00 40.75           C  
ANISOU 6352  CE1 HIS D 212     5054   5927   4502    190    642   -191       C  
ATOM   6353  NE2 HIS D 212      23.863  11.617 -62.219  1.00 40.76           N  
ANISOU 6353  NE2 HIS D 212     5071   5926   4489    224    652   -242       N  
ATOM   6354  N   LEU D 213      19.958  13.211 -60.989  1.00 38.07           N  
ANISOU 6354  N   LEU D 213     4673   5839   3954    356    834   -287       N  
ATOM   6355  CA  LEU D 213      19.915  14.572 -60.437  1.00 39.81           C  
ANISOU 6355  CA  LEU D 213     4957   6041   4128    443    863   -352       C  
ATOM   6356  C   LEU D 213      21.317  14.980 -59.997  1.00 39.33           C  
ANISOU 6356  C   LEU D 213     4993   5876   4077    404    810   -384       C  
ATOM   6357  O   LEU D 213      22.175  14.096 -59.732  1.00 38.63           O  
ANISOU 6357  O   LEU D 213     4901   5772   4004    325    756   -349       O  
ATOM   6358  CB  LEU D 213      18.938  14.613 -59.254  1.00 41.70           C  
ANISOU 6358  CB  LEU D 213     5179   6403   4263    470    926   -366       C  
ATOM   6359  CG  LEU D 213      19.296  13.754 -58.044  1.00 41.46           C  
ANISOU 6359  CG  LEU D 213     5178   6410   4166    376    910   -335       C  
ATOM   6360  CD1 LEU D 213      20.029  14.581 -56.998  1.00 41.68           C  
ANISOU 6360  CD1 LEU D 213     5317   6392   4130    392    896   -396       C  
ATOM   6361  CD2 LEU D 213      18.045  13.142 -57.427  1.00 43.24           C  
ANISOU 6361  CD2 LEU D 213     5328   6793   4310    351    980   -304       C  
ATOM   6362  N   ARG D 214      21.500  16.285 -59.900  1.00 40.01           N  
ANISOU 6362  N   ARG D 214     5163   5894   4144    461    825   -449       N  
ATOM   6363  CA  ARG D 214      22.694  16.899 -59.305  1.00 41.73           C  
ANISOU 6363  CA  ARG D 214     5479   6032   4345    408    783   -498       C  
ATOM   6364  C   ARG D 214      22.260  18.231 -58.717  1.00 42.12           C  
ANISOU 6364  C   ARG D 214     5640   6042   4323    484    832   -579       C  
ATOM   6365  O   ARG D 214      21.333  18.842 -59.280  1.00 42.34           O  
ANISOU 6365  O   ARG D 214     5672   6060   4356    596    886   -589       O  
ATOM   6366  CB  ARG D 214      23.765  17.058 -60.383  1.00 43.35           C  
ANISOU 6366  CB  ARG D 214     5686   6144   4640    356    738   -492       C  
ATOM   6367  CG  ARG D 214      24.966  17.862 -59.922  1.00 46.18           C  
ANISOU 6367  CG  ARG D 214     6133   6431   4981    283    697   -551       C  
ATOM   6368  CD  ARG D 214      26.121  17.890 -60.907  1.00 48.82           C  
ANISOU 6368  CD  ARG D 214     6442   6710   5397    207    658   -541       C  
ATOM   6369  NE  ARG D 214      27.110  18.904 -60.554  1.00 50.91           N  
ANISOU 6369  NE  ARG D 214     6797   6911   5637    120    633   -607       N  
ATOM   6370  CZ  ARG D 214      27.974  18.786 -59.547  1.00 52.72           C  
ANISOU 6370  CZ  ARG D 214     7022   7189   5819     38    573   -636       C  
ATOM   6371  NH1 ARG D 214      28.010  17.689 -58.793  1.00 51.69           N1+
ANISOU 6371  NH1 ARG D 214     6815   7162   5662     47    532   -596       N1+
ATOM   6372  NH2 ARG D 214      28.795  19.788 -59.295  1.00 54.09           N  
ANISOU 6372  NH2 ARG D 214     7281   7308   5964    -61    552   -705       N  
ATOM   6373  N   PHE D 215      22.881  18.638 -57.615  1.00 42.65           N  
ANISOU 6373  N   PHE D 215     5797   6092   4317    434    810   -635       N  
ATOM   6374  CA  PHE D 215      22.647  19.970 -57.010  1.00 44.18           C  
ANISOU 6374  CA  PHE D 215     6136   6217   4434    494    854   -731       C  
ATOM   6375  C   PHE D 215      23.991  20.547 -56.574  1.00 44.85           C  
ANISOU 6375  C   PHE D 215     6327   6215   4499    371    790   -790       C  
ATOM   6376  O   PHE D 215      24.873  19.774 -56.153  1.00 43.11           O  
ANISOU 6376  O   PHE D 215     6047   6056   4276    264    717   -760       O  
ATOM   6377  CB  PHE D 215      21.660  19.885 -55.844  1.00 44.11           C  
ANISOU 6377  CB  PHE D 215     6131   6320   4311    564    916   -759       C  
ATOM   6378  CG  PHE D 215      22.164  19.107 -54.661  1.00 43.29           C  
ANISOU 6378  CG  PHE D 215     6016   6306   4128    461    873   -746       C  
ATOM   6379  CD1 PHE D 215      21.972  17.740 -54.574  1.00 42.19           C  
ANISOU 6379  CD1 PHE D 215     5755   6277   3997    416    855   -651       C  
ATOM   6380  CD2 PHE D 215      22.815  19.746 -53.620  1.00 43.98           C  
ANISOU 6380  CD2 PHE D 215     6229   6363   4119    407    847   -827       C  
ATOM   6381  CE1 PHE D 215      22.419  17.031 -53.464  1.00 42.46           C  
ANISOU 6381  CE1 PHE D 215     5801   6386   3947    334    811   -626       C  
ATOM   6382  CE2 PHE D 215      23.269  19.030 -52.517  1.00 44.02           C  
ANISOU 6382  CE2 PHE D 215     6227   6464   4035    321    797   -807       C  
ATOM   6383  CZ  PHE D 215      23.071  17.673 -52.435  1.00 42.83           C  
ANISOU 6383  CZ  PHE D 215     5961   6420   3894    292    778   -701       C  
ATOM   6384  N   SER D 216      24.115  21.874 -56.674  1.00 46.47           N  
ANISOU 6384  N   SER D 216     6690   6283   4685    390    814   -870       N  
ATOM   6385  CA  SER D 216      25.274  22.662 -56.190  1.00 48.38           C  
ANISOU 6385  CA  SER D 216     7062   6435   4887    255    764   -949       C  
ATOM   6386  C   SER D 216      24.882  24.142 -56.173  1.00 49.24           C  
ANISOU 6386  C   SER D 216     7384   6376   4949    324    826  -1042       C  
ATOM   6387  O   SER D 216      24.030  24.495 -57.009  1.00 49.09           O  
ANISOU 6387  O   SER D 216     7382   6296   4975    466    885  -1015       O  
ATOM   6388  CB  SER D 216      26.473  22.378 -57.073  1.00 49.26           C  
ANISOU 6388  CB  SER D 216     7100   6524   5094    122    696   -905       C  
ATOM   6389  OG  SER D 216      27.325  23.509 -57.220  1.00 52.52           O  
ANISOU 6389  OG  SER D 216     7655   6802   5497      7    680   -976       O  
ATOM   6390  N   ASN D 217      25.464  24.947 -55.271  1.00 50.15           N  
ANISOU 6390  N   ASN D 217     7662   6421   4973    232    808  -1146       N  
ATOM   6391  CA  ASN D 217      25.309  26.431 -55.202  1.00 52.73           C  
ANISOU 6391  CA  ASN D 217     8243   6544   5246    267    859  -1251       C  
ATOM   6392  C   ASN D 217      23.835  26.823 -55.373  1.00 52.16           C  
ANISOU 6392  C   ASN D 217     8220   6439   5159    521    961  -1255       C  
ATOM   6393  O   ASN D 217      23.560  27.754 -56.152  1.00 51.12           O  
ANISOU 6393  O   ASN D 217     8231   6132   5060    608   1001  -1265       O  
ATOM   6394  CB  ASN D 217      26.138  27.179 -56.258  1.00 55.33           C  
ANISOU 6394  CB  ASN D 217     8673   6701   5650    151    836  -1246       C  
ATOM   6395  CG  ASN D 217      27.600  26.788 -56.270  1.00 57.37           C  
ANISOU 6395  CG  ASN D 217     8840   7022   5936    -93    741  -1235       C  
ATOM   6396  ND2 ASN D 217      28.193  26.658 -57.452  1.00 58.26           N  
ANISOU 6396  ND2 ASN D 217     8878   7106   6150   -170    723  -1166       N  
ATOM   6397  OD1 ASN D 217      28.189  26.610 -55.209  1.00 61.18           O  
ANISOU 6397  OD1 ASN D 217     9315   7593   6340   -207    685  -1291       O  
ATOM   6398  N   GLY D 218      22.920  26.125 -54.687  1.00 51.70           N  
ANISOU 6398  N   GLY D 218     8044   6553   5048    636   1002  -1241       N  
ATOM   6399  CA  GLY D 218      21.496  26.511 -54.584  1.00 52.53           C  
ANISOU 6399  CA  GLY D 218     8172   6676   5110    880   1105  -1266       C  
ATOM   6400  C   GLY D 218      20.747  26.262 -55.879  1.00 51.07           C  
ANISOU 6400  C   GLY D 218     7862   6512   5031   1017   1128  -1166       C  
ATOM   6401  O   GLY D 218      19.678  26.877 -56.091  1.00 52.38           O  
ANISOU 6401  O   GLY D 218     8072   6652   5177   1236   1203  -1187       O  
ATOM   6402  N   LEU D 219      21.277  25.353 -56.690  1.00 48.95           N  
ANISOU 6402  N   LEU D 219     7434   6304   4863    900   1063  -1065       N  
ATOM   6403  CA  LEU D 219      20.663  24.902 -57.954  1.00 47.77           C  
ANISOU 6403  CA  LEU D 219     7141   6202   4807    990   1067   -964       C  
ATOM   6404  C   LEU D 219      20.644  23.374 -57.959  1.00 44.60           C  
ANISOU 6404  C   LEU D 219     6506   5997   4443    903   1032   -878       C  
ATOM   6405  O   LEU D 219      21.681  22.758 -57.655  1.00 42.36           O  
ANISOU 6405  O   LEU D 219     6190   5732   4173    731    967   -864       O  
ATOM   6406  CB  LEU D 219      21.506  25.446 -59.109  1.00 49.83           C  
ANISOU 6406  CB  LEU D 219     7496   6289   5149    911   1025   -935       C  
ATOM   6407  CG  LEU D 219      20.768  25.870 -60.381  1.00 51.43           C  
ANISOU 6407  CG  LEU D 219     7706   6431   5403   1070   1050   -876       C  
ATOM   6408  CD1 LEU D 219      21.751  26.015 -61.545  1.00 51.31           C  
ANISOU 6408  CD1 LEU D 219     7735   6295   5466    936   1001   -823       C  
ATOM   6409  CD2 LEU D 219      19.687  24.883 -60.746  1.00 51.76           C  
ANISOU 6409  CD2 LEU D 219     7515   6681   5470   1178   1064   -802       C  
ATOM   6410  N   MET D 220      19.498  22.797 -58.301  1.00 43.80           N  
ANISOU 6410  N   MET D 220     6251   6038   4354   1019   1072   -823       N  
ATOM   6411  CA  MET D 220      19.356  21.347 -58.546  1.00 43.10           C  
ANISOU 6411  CA  MET D 220     5959   6108   4308    935   1043   -734       C  
ATOM   6412  C   MET D 220      18.774  21.140 -59.947  1.00 42.65           C  
ANISOU 6412  C   MET D 220     5799   6074   4331   1005   1040   -664       C  
ATOM   6413  O   MET D 220      17.915  21.927 -60.387  1.00 43.95           O  
ANISOU 6413  O   MET D 220     5988   6226   4484   1175   1082   -677       O  
ATOM   6414  CB  MET D 220      18.426  20.717 -57.517  1.00 44.49           C  
ANISOU 6414  CB  MET D 220     6035   6470   4398    968   1099   -737       C  
ATOM   6415  CG  MET D 220      18.108  19.267 -57.804  1.00 44.53           C  
ANISOU 6415  CG  MET D 220     5857   6623   4439    882   1080   -643       C  
ATOM   6416  SD  MET D 220      17.387  18.368 -56.395  1.00 46.85           S  
ANISOU 6416  SD  MET D 220     6067   7118   4617    836   1136   -633       S  
ATOM   6417  CE  MET D 220      15.797  19.167 -56.231  1.00 47.87           C  
ANISOU 6417  CE  MET D 220     6137   7378   4675   1046   1253   -687       C  
ATOM   6418  N   VAL D 221      19.220  20.091 -60.617  1.00 40.78           N  
ANISOU 6418  N   VAL D 221     5455   5874   4164    887    988   -593       N  
ATOM   6419  CA  VAL D 221      18.661  19.671 -61.927  1.00 39.32           C  
ANISOU 6419  CA  VAL D 221     5158   5739   4042    924    977   -526       C  
ATOM   6420  C   VAL D 221      18.256  18.217 -61.796  1.00 36.84           C  
ANISOU 6420  C   VAL D 221     4681   5582   3733    837    969   -471       C  
ATOM   6421  O   VAL D 221      19.056  17.437 -61.310  1.00 36.59           O  
ANISOU 6421  O   VAL D 221     4651   5541   3710    708    934   -457       O  
ATOM   6422  CB  VAL D 221      19.699  19.840 -63.045  1.00 39.21           C  
ANISOU 6422  CB  VAL D 221     5204   5588   4106    850    925   -501       C  
ATOM   6423  CG1 VAL D 221      19.123  19.442 -64.398  1.00 39.02           C  
ANISOU 6423  CG1 VAL D 221     5081   5617   4128    888    912   -438       C  
ATOM   6424  CG2 VAL D 221      20.267  21.248 -63.055  1.00 39.92           C  
ANISOU 6424  CG2 VAL D 221     5486   5500   4183    887    933   -554       C  
ATOM   6425  N   THR D 222      17.066  17.891 -62.234  1.00 36.04           N  
ANISOU 6425  N   THR D 222     4452   5620   3622    904    997   -441       N  
ATOM   6426  CA  THR D 222      16.556  16.506 -62.237  1.00 35.52           C  
ANISOU 6426  CA  THR D 222     4240   5700   3556    799    994   -387       C  
ATOM   6427  C   THR D 222      16.285  16.146 -63.690  1.00 33.49           C  
ANISOU 6427  C   THR D 222     3905   5463   3359    792    958   -342       C  
ATOM   6428  O   THR D 222      16.054  17.071 -64.477  1.00 33.53           O  
ANISOU 6428  O   THR D 222     3937   5427   3376    914    955   -350       O  
ATOM   6429  CB  THR D 222      15.306  16.410 -61.347  1.00 38.08           C  
ANISOU 6429  CB  THR D 222     4463   6211   3793    853   1066   -400       C  
ATOM   6430  CG2 THR D 222      15.575  16.854 -59.922  1.00 38.62           C  
ANISOU 6430  CG2 THR D 222     4628   6262   3785    868   1107   -454       C  
ATOM   6431  OG1 THR D 222      14.261  17.218 -61.912  1.00 39.39           O  
ANISOU 6431  OG1 THR D 222     4561   6461   3943   1026   1099   -415       O  
ATOM   6432  N   CYS D 223      16.314  14.874 -64.028  1.00 31.61           N  
ANISOU 6432  N   CYS D 223     3592   5273   3147    658    931   -298       N  
ATOM   6433  CA  CYS D 223      15.976  14.417 -65.382  1.00 31.23           C  
ANISOU 6433  CA  CYS D 223     3468   5260   3138    633    897   -264       C  
ATOM   6434  C   CYS D 223      15.285  13.072 -65.263  1.00 31.49           C  
ANISOU 6434  C   CYS D 223     3388   5426   3149    501    903   -230       C  
ATOM   6435  O   CYS D 223      15.595  12.353 -64.329  1.00 31.48           O  
ANISOU 6435  O   CYS D 223     3416   5413   3131    404    914   -219       O  
ATOM   6436  CB  CYS D 223      17.226  14.386 -66.248  1.00 30.18           C  
ANISOU 6436  CB  CYS D 223     3429   4963   3075    585    848   -258       C  
ATOM   6437  SG  CYS D 223      18.358  13.030 -65.885  1.00 29.11           S  
ANISOU 6437  SG  CYS D 223     3333   4748   2980    422    816   -239       S  
ATOM   6438  N   SER D 224      14.365  12.773 -66.168  1.00 32.57           N  
ANISOU 6438  N   SER D 224     3408   5689   3279    493    891   -213       N  
ATOM   6439  CA  SER D 224      13.423  11.642 -65.995  1.00 34.16           C  
ANISOU 6439  CA  SER D 224     3485   6054   3439    357    908   -188       C  
ATOM   6440  C   SER D 224      13.225  10.861 -67.299  1.00 34.28           C  
ANISOU 6440  C   SER D 224     3453   6092   3479    257    857   -171       C  
ATOM   6441  O   SER D 224      13.605  11.343 -68.362  1.00 32.14           O  
ANISOU 6441  O   SER D 224     3218   5750   3243    326    815   -176       O  
ATOM   6442  CB  SER D 224      12.127  12.146 -65.427  1.00 35.70           C  
ANISOU 6442  CB  SER D 224     3537   6466   3561    444    964   -200       C  
ATOM   6443  OG  SER D 224      11.080  11.198 -65.565  1.00 36.65           O  
ANISOU 6443  OG  SER D 224     3503   6782   3639    308    976   -178       O  
ATOM   6444  N   LYS D 225      12.672   9.658 -67.147  1.00 36.22           N  
ANISOU 6444  N   LYS D 225     3638   6427   3697     82    864   -151       N  
ATOM   6445  CA  LYS D 225      12.143   8.780 -68.215  1.00 37.79           C  
ANISOU 6445  CA  LYS D 225     3771   6699   3890    -52    824   -144       C  
ATOM   6446  C   LYS D 225      11.099   9.563 -69.021  1.00 39.77           C  
ANISOU 6446  C   LYS D 225     3862   7146   4104     59    805   -153       C  
ATOM   6447  O   LYS D 225      10.935   9.282 -70.217  1.00 40.78           O  
ANISOU 6447  O   LYS D 225     3962   7300   4233     14    750   -156       O  
ATOM   6448  CB  LYS D 225      11.579   7.509 -67.566  1.00 39.03           C  
ANISOU 6448  CB  LYS D 225     3897   6931   4002   -265    854   -122       C  
ATOM   6449  CG  LYS D 225      10.943   6.510 -68.522  1.00 40.66           C  
ANISOU 6449  CG  LYS D 225     4045   7218   4188   -447    818   -124       C  
ATOM   6450  CD  LYS D 225      10.518   5.181 -67.930  1.00 41.62           C  
ANISOU 6450  CD  LYS D 225     4185   7363   4265   -692    848    -99       C  
ATOM   6451  CE  LYS D 225      10.085   4.218 -69.021  1.00 42.04           C  
ANISOU 6451  CE  LYS D 225     4226   7445   4302   -881    802   -116       C  
ATOM   6452  NZ  LYS D 225       8.843   3.492 -68.670  1.00 44.00           N1+
ANISOU 6452  NZ  LYS D 225     4344   7905   4468  -1100    834   -103       N1+
ATOM   6453  N   ASP D 226      10.430  10.531 -68.401  1.00 41.48           N  
ANISOU 6453  N   ASP D 226     3982   7496   4283    215    847   -160       N  
ATOM   6454  CA  ASP D 226       9.416  11.382 -69.069  1.00 43.51           C  
ANISOU 6454  CA  ASP D 226     4083   7948   4500    372    827   -163       C  
ATOM   6455  C   ASP D 226      10.069  12.271 -70.143  1.00 25.80           C  
ATOM   6456  O   ASP D 226       9.329  13.031 -70.785  1.00 46.27           O  
ANISOU 6456  O   ASP D 226     4442   8285   4855    679    742   -152       O  
ATOM   6457  CB  ASP D 226       8.636  12.191 -68.032  1.00 44.95           C  
ANISOU 6457  CB  ASP D 226     4160   8287   4632    528    898   -177       C  
ATOM   6458  CG  ASP D 226       9.410  13.281 -67.316  1.00 44.36           C  
ANISOU 6458  CG  ASP D 226     4243   8030   4581    707    935   -199       C  
ATOM   6459  OD1 ASP D 226      10.524  13.617 -67.752  1.00 42.03           O  
ANISOU 6459  OD1 ASP D 226     4122   7501   4345    734    898   -199       O  
ATOM   6460  OD2 ASP D 226       8.860  13.797 -66.318  1.00 46.66           O1-
ANISOU 6460  OD2 ASP D 226     4476   8429   4825    811   1005   -222       O1-
ATOM   6461  N   ARG D 227      11.396  12.222 -70.319  1.00 43.02           N  
ANISOU 6461  N   ARG D 227     4318   7488   4540    492    757   -163       N  
ATOM   6462  CA  ARG D 227      12.134  12.894 -71.432  1.00 42.73           C  
ANISOU 6462  CA  ARG D 227     4395   7305   4534    582    710   -156       C  
ATOM   6463  C   ARG D 227      12.438  14.356 -71.081  1.00 41.74           C  
ANISOU 6463  C   ARG D 227     4363   7081   4416    793    735   -159       C  
ATOM   6464  O   ARG D 227      12.993  15.085 -71.949  1.00 41.35           O  
ANISOU 6464  O   ARG D 227     4420   6909   4380    875    704   -145       O  
ATOM   6465  CB  ARG D 227      11.366  12.848 -72.757  1.00 44.76           C  
ANISOU 6465  CB  ARG D 227     4551   7708   4749    594    647   -138       C  
ATOM   6466  CG  ARG D 227      10.984  11.442 -73.186  1.00 46.82           C  
ANISOU 6466  CG  ARG D 227     4732   8068   4990    371    619   -146       C  
ATOM   6467  CD  ARG D 227      10.173  11.316 -74.461  1.00 50.31           C  
ANISOU 6467  CD  ARG D 227     5062   8682   5372    355    546   -137       C  
ATOM   6468  NE  ARG D 227       9.826   9.899 -74.597  1.00 52.68           N  
ANISOU 6468  NE  ARG D 227     5306   9058   5651    106    533   -158       N  
ATOM   6469  CZ  ARG D 227       9.397   9.294 -75.703  1.00 54.54           C  
ANISOU 6469  CZ  ARG D 227     5490   9394   5838    -12    468   -170       C  
ATOM   6470  NH1 ARG D 227       9.159   7.993 -75.672  1.00 56.54           N1+
ANISOU 6470  NH1 ARG D 227     5730   9677   6074   -256    467   -196       N1+
ATOM   6471  NH2 ARG D 227       9.211   9.975 -76.820  1.00 55.03           N  
ANISOU 6471  NH2 ARG D 227     5531   9518   5858    106    404   -155       N  
ATOM   6472  N   SER D 228      12.120  14.768 -69.859  1.00 41.93           N  
ANISOU 6472  N   SER D 228     4366   7144   4421    866    791   -179       N  
ATOM   6473  CA  SER D 228      12.273  16.170 -69.390  1.00 42.02           C  
ANISOU 6473  CA  SER D 228     4478   7062   4425   1070    823   -196       C  
ATOM   6474  C   SER D 228      13.472  16.280 -68.452  1.00 39.82           C  
ANISOU 6474  C   SER D 228     4360   6585   4183   1009    854   -225       C  
ATOM   6475  O   SER D 228      13.852  15.286 -67.829  1.00 37.33           O  
ANISOU 6475  O   SER D 228     4034   6266   3882    850    865   -229       O  
ATOM   6476  CB  SER D 228      11.005  16.693 -68.730  1.00 43.84           C  
ANISOU 6476  CB  SER D 228     4573   7491   4593   1229    868   -211       C  
ATOM   6477  OG  SER D 228      10.960  16.408 -67.344  1.00 43.12           O  
ANISOU 6477  OG  SER D 228     4467   7436   4481   1176    936   -244       O  
ATOM   6478  N   ILE D 229      14.029  17.484 -68.409  1.00 40.13           N  
ANISOU 6478  N   ILE D 229     4552   6464   4231   1134    863   -242       N  
ATOM   6479  CA  ILE D 229      14.968  17.991 -67.374  1.00 39.98           C  
ANISOU 6479  CA  ILE D 229     4684   6282   4223   1121    896   -284       C  
ATOM   6480  C   ILE D 229      14.232  19.085 -66.621  1.00 41.14           C  
ANISOU 6480  C   ILE D 229     4858   6460   4314   1316    948   -322       C  
ATOM   6481  O   ILE D 229      13.592  19.911 -67.286  1.00 41.83           O  
ANISOU 6481  O   ILE D 229     4950   6563   4381   1491    941   -308       O  
ATOM   6482  CB  ILE D 229      16.248  18.553 -68.016  1.00 39.91           C  
ANISOU 6482  CB  ILE D 229     4846   6056   4261   1085    867   -281       C  
ATOM   6483  CG1 ILE D 229      16.953  17.486 -68.847  1.00 38.14           C  
ANISOU 6483  CG1 ILE D 229     4588   5815   4087    920    824   -251       C  
ATOM   6484  CG2 ILE D 229      17.165  19.141 -66.956  1.00 40.61           C  
ANISOU 6484  CG2 ILE D 229     5079   6000   4351   1060    892   -331       C  
ATOM   6485  CD1 ILE D 229      17.808  18.064 -69.917  1.00 38.08           C  
ANISOU 6485  CD1 ILE D 229     4697   5664   4108    913    801   -234       C  
ATOM   6486  N   ALA D 230      14.338  19.080 -65.300  1.00 40.79           N  
ANISOU 6486  N   ALA D 230     4841   6420   4238   1295    996   -368       N  
ATOM   6487  CA  ALA D 230      13.790  20.143 -64.434  1.00 42.00           C  
ANISOU 6487  CA  ALA D 230     5053   6577   4330   1477   1058   -425       C  
ATOM   6488  C   ALA D 230      14.965  20.877 -63.806  1.00 41.20           C  
ANISOU 6488  C   ALA D 230     5173   6248   4232   1442   1062   -476       C  
ATOM   6489  O   ALA D 230      15.947  20.211 -63.435  1.00 41.00           O  
ANISOU 6489  O   ALA D 230     5178   6166   4235   1258   1036   -475       O  
ATOM   6490  CB  ALA D 230      12.870  19.543 -63.409  1.00 42.76           C  
ANISOU 6490  CB  ALA D 230     4993   6891   4362   1472   1118   -444       C  
ATOM   6491  N   VAL D 231      14.889  22.200 -63.769  1.00 42.06           N  
ANISOU 6491  N   VAL D 231     5438   6228   4315   1610   1087   -517       N  
ATOM   6492  CA  VAL D 231      15.903  23.066 -63.102  1.00 43.39           C  
ANISOU 6492  CA  VAL D 231     5838   6177   4471   1575   1097   -583       C  
ATOM   6493  C   VAL D 231      15.231  23.736 -61.903  1.00 46.10           C  
ANISOU 6493  C   VAL D 231     6235   6555   4727   1726   1174   -665       C  
ATOM   6494  O   VAL D 231      14.154  24.347 -62.102  1.00 48.93           O  
ANISOU 6494  O   VAL D 231     6564   6977   5050   1955   1214   -672       O  
ATOM   6495  CB  VAL D 231      16.460  24.116 -64.075  1.00 43.45           C  
ANISOU 6495  CB  VAL D 231     6037   5962   4509   1624   1069   -568       C  
ATOM   6496  CG1 VAL D 231      17.613  24.903 -63.480  1.00 43.42           C  
ANISOU 6496  CG1 VAL D 231     6266   5737   4495   1526   1071   -634       C  
ATOM   6497  CG2 VAL D 231      16.870  23.481 -65.391  1.00 43.08           C  
ANISOU 6497  CG2 VAL D 231     5915   5921   4531   1515   1008   -485       C  
ATOM   6498  N   TRP D 232      15.833  23.614 -60.719  1.00 45.94           N  
ANISOU 6498  N   TRP D 232     6283   6507   4665   1612   1191   -726       N  
ATOM   6499  CA  TRP D 232      15.262  24.127 -59.452  1.00 48.37           C  
ANISOU 6499  CA  TRP D 232     6643   6863   4871   1728   1271   -815       C  
ATOM   6500  C   TRP D 232      16.207  25.138 -58.813  1.00 51.20           C  
ANISOU 6500  C   TRP D 232     7270   6989   5192   1692   1271   -905       C  
ATOM   6501  O   TRP D 232      17.410  24.846 -58.775  1.00 50.17           O  
ANISOU 6501  O   TRP D 232     7199   6766   5097   1482   1209   -897       O  
ATOM   6502  CB  TRP D 232      15.019  22.973 -58.494  1.00 47.15           C  
ANISOU 6502  CB  TRP D 232     6326   6919   4670   1608   1294   -807       C  
ATOM   6503  CG  TRP D 232      14.350  21.791 -59.113  1.00 45.50           C  
ANISOU 6503  CG  TRP D 232     5873   6915   4502   1556   1279   -716       C  
ATOM   6504  CD1 TRP D 232      14.930  20.830 -59.888  1.00 43.70           C  
ANISOU 6504  CD1 TRP D 232     5570   6679   4355   1386   1205   -637       C  
ATOM   6505  CD2 TRP D 232      12.971  21.416 -58.949  1.00 45.54           C  
ANISOU 6505  CD2 TRP D 232     5675   7170   4457   1660   1345   -704       C  
ATOM   6506  CE2 TRP D 232      12.790  20.217 -59.666  1.00 44.05           C  
ANISOU 6506  CE2 TRP D 232     5308   7106   4324   1522   1300   -615       C  
ATOM   6507  CE3 TRP D 232      11.876  21.978 -58.282  1.00 46.85           C  
ANISOU 6507  CE3 TRP D 232     5789   7478   4533   1855   1442   -764       C  
ATOM   6508  NE1 TRP D 232      13.999  19.887 -60.227  1.00 43.10           N  
ANISOU 6508  NE1 TRP D 232     5281   6812   4283   1368   1217   -579       N  
ATOM   6509  CZ2 TRP D 232      11.556  19.574 -59.739  1.00 44.24           C  
ANISOU 6509  CZ2 TRP D 232     5102   7392   4315   1545   1342   -583       C  
ATOM   6510  CZ3 TRP D 232      10.660  21.343 -58.349  1.00 47.16           C  
ANISOU 6510  CZ3 TRP D 232     5579   7798   4542   1894   1488   -729       C  
ATOM   6511  CH2 TRP D 232      10.505  20.155 -59.069  1.00 46.19           C  
ANISOU 6511  CH2 TRP D 232     5278   7796   4474   1727   1436   -638       C  
ATOM   6512  N   ASP D 233      15.653  26.237 -58.285  1.00 55.28           N  
ANISOU 6512  N   ASP D 233     7934   7434   5634   1888   1341   -992       N  
ATOM   6513  CA  ASP D 233      16.300  27.090 -57.255  1.00 57.14           C  
ANISOU 6513  CA  ASP D 233     8418   7501   5793   1852   1365  -1109       C  
ATOM   6514  C   ASP D 233      16.178  26.319 -55.937  1.00 30.85           C  
ATOM   6515  O   ASP D 233      15.050  25.910 -55.591  1.00 58.40           O  
ANISOU 6515  O   ASP D 233     8304   8067   5817   1891   1469  -1142       O  
ATOM   6516  CB  ASP D 233      15.666  28.484 -57.198  1.00 60.72           C  
ANISOU 6516  CB  ASP D 233     9079   7802   6191   2115   1435  -1191       C  
ATOM   6517  CG  ASP D 233      15.617  29.205 -58.542  1.00 62.13           C  
ANISOU 6517  CG  ASP D 233     9359   7806   6442   2233   1403  -1130       C  
ATOM   6518  OD1 ASP D 233      16.677  29.242 -59.212  1.00 60.75           O  
ANISOU 6518  OD1 ASP D 233     9274   7473   6333   2044   1332  -1087       O  
ATOM   6519  OD2 ASP D 233      14.510  29.720 -58.921  1.00 64.84           O1-
ANISOU 6519  OD2 ASP D 233     9682   8185   6769   2519   1451  -1123       O1-
ATOM   6520  N   MET D 234      17.297  26.073 -55.262  1.00 57.29           N  
ANISOU 6520  N   MET D 234     8414   7653   5701   1544   1346  -1177       N  
ATOM   6521  CA  MET D 234      17.358  25.227 -54.046  1.00 58.18           C  
ANISOU 6521  CA  MET D 234     8440   7939   5726   1427   1356  -1192       C  
ATOM   6522  C   MET D 234      17.895  26.073 -52.873  1.00 59.95           C  
ANISOU 6522  C   MET D 234     8899   8049   5830   1391   1374  -1326       C  
ATOM   6523  O   MET D 234      19.085  25.913 -52.469  1.00 59.12           O  
ANISOU 6523  O   MET D 234     8868   7881   5713   1180   1292  -1340       O  
ATOM   6524  CB  MET D 234      18.235  23.999 -54.304  1.00 57.07           C  
ANISOU 6524  CB  MET D 234     8166   7862   5657   1199   1260  -1093       C  
ATOM   6525  CG  MET D 234      17.930  22.845 -53.352  1.00 58.90           C  
ANISOU 6525  CG  MET D 234     8254   8310   5814   1119   1276  -1056       C  
ATOM   6526  SD  MET D 234      19.021  21.364 -53.427  1.00 59.19           S  
ANISOU 6526  SD  MET D 234     8176   8401   5913    873   1160   -944       S  
ATOM   6527  CE  MET D 234      20.390  21.943 -52.422  1.00 62.54           C  
ANISOU 6527  CE  MET D 234     8794   8711   6256    736   1090  -1033       C  
ATOM   6528  N   ALA D 235      17.039  26.956 -52.347  1.00 60.99           N  
ANISOU 6528  N   ALA D 235     9141   8163   5870   1598   1476  -1426       N  
ATOM   6529  CA  ALA D 235      17.382  27.928 -51.280  1.00 62.28           C  
ANISOU 6529  CA  ALA D 235     9564   8195   5904   1601   1510  -1577       C  
ATOM   6530  C   ALA D 235      17.776  27.166 -50.018  1.00 61.79           C  
ANISOU 6530  C   ALA D 235     9456   8292   5729   1428   1493  -1598       C  
ATOM   6531  O   ALA D 235      18.742  27.569 -49.356  1.00 63.42           O  
ANISOU 6531  O   ALA D 235     9843   8388   5868   1276   1440  -1678       O  
ATOM   6532  CB  ALA D 235      16.217  28.850 -51.006  1.00 64.25           C  
ANISOU 6532  CB  ALA D 235     9906   8430   6076   1896   1638  -1673       C  
ATOM   6533  N   SER D 236      17.020  26.108 -49.713  1.00 60.54           N  
ANISOU 6533  N   SER D 236     9068   8390   5545   1446   1535  -1524       N  
ATOM   6534  CA  SER D 236      17.144  25.237 -48.516  1.00 58.00           C  
ANISOU 6534  CA  SER D 236     8681   8254   5100   1309   1536  -1516       C  
ATOM   6535  C   SER D 236      16.569  23.872 -48.875  1.00 55.01           C  
ANISOU 6535  C   SER D 236     8027   8094   4779   1270   1538  -1370       C  
ATOM   6536  O   SER D 236      16.026  23.728 -49.963  1.00 52.64           O  
ANISOU 6536  O   SER D 236     7596   7808   4598   1360   1547  -1300       O  
ATOM   6537  CB  SER D 236      16.411  25.812 -47.351  1.00 59.37           C  
ANISOU 6537  CB  SER D 236     8955   8504   5098   1439   1658  -1643       C  
ATOM   6538  OG  SER D 236      15.009  25.758 -47.585  1.00 59.93           O  
ANISOU 6538  OG  SER D 236     8869   8736   5167   1656   1782  -1628       O  
ATOM   6539  N   ALA D 237      16.646  22.933 -47.953  1.00 55.12           N  
ANISOU 6539  N   ALA D 237     7974   8272   4697   1139   1534  -1328       N  
ATOM   6540  CA  ALA D 237      15.979  21.619 -48.039  1.00 55.43           C  
ANISOU 6540  CA  ALA D 237     7786   8526   4751   1085   1559  -1200       C  
ATOM   6541  C   ALA D 237      14.468  21.758 -48.320  1.00 56.17           C  
ANISOU 6541  C   ALA D 237     7727   8779   4835   1277   1694  -1208       C  
ATOM   6542  O   ALA D 237      13.893  20.868 -48.965  1.00 53.68           O  
ANISOU 6542  O   ALA D 237     7209   8594   4593   1247   1699  -1100       O  
ATOM   6543  CB  ALA D 237      16.231  20.872 -46.742  1.00 56.26           C  
ANISOU 6543  CB  ALA D 237     7912   8761   4703    940   1555  -1180       C  
ATOM   6544  N   THR D 238      13.831  22.821 -47.818  1.00 58.97           N  
ANISOU 6544  N   THR D 238     8174   9138   5092   1468   1802  -1336       N  
ATOM   6545  CA  THR D 238      12.347  22.989 -47.788  1.00 61.42           C  
ANISOU 6545  CA  THR D 238     8329   9655   5353   1673   1949  -1363       C  
ATOM   6546  C   THR D 238      11.894  24.053 -48.789  1.00 63.71           C  
ANISOU 6546  C   THR D 238     8644   9824   5738   1920   1969  -1411       C  
ATOM   6547  O   THR D 238      10.679  24.085 -49.081  1.00 66.00           O  
ANISOU 6547  O   THR D 238     8752  10301   6025   2100   2063  -1405       O  
ATOM   6548  CB  THR D 238      11.854  23.382 -46.395  1.00 62.86           C  
ANISOU 6548  CB  THR D 238     8589   9963   5332   1746   2078  -1479       C  
ATOM   6549  CG2 THR D 238      11.650  22.174 -45.512  1.00 62.98           C  
ANISOU 6549  CG2 THR D 238     8484  10212   5235   1559   2111  -1402       C  
ATOM   6550  OG1 THR D 238      12.814  24.268 -45.815  1.00 62.25           O  
ANISOU 6550  OG1 THR D 238     8798   9662   5191   1725   2033  -1595       O  
ATOM   6551  N   ASP D 239      12.826  24.884 -49.270  1.00 63.36           N  
ANISOU 6551  N   ASP D 239     8815   9492   5766   1924   1884  -1453       N  
ATOM   6552  CA  ASP D 239      12.546  25.994 -50.211  1.00 63.89           C  
ANISOU 6552  CA  ASP D 239     8972   9390   5915   2152   1891  -1494       C  
ATOM   6553  C   ASP D 239      13.162  25.637 -51.558  1.00 30.42           C  
ATOM   6554  O   ASP D 239      14.307  26.092 -51.848  1.00 60.60           O  
ANISOU 6554  O   ASP D 239     8698   8606   5722   1935   1677  -1392       O  
ATOM   6555  CB  ASP D 239      13.091  27.311 -49.666  1.00 65.96           C  
ANISOU 6555  CB  ASP D 239     9560   9397   6103   2230   1908  -1643       C  
ATOM   6556  CG  ASP D 239      12.696  28.523 -50.481  1.00 67.77           C  
ANISOU 6556  CG  ASP D 239     9924   9436   6388   2493   1934  -1690       C  
ATOM   6557  OD1 ASP D 239      11.847  28.371 -51.400  1.00 67.44           O  
ANISOU 6557  OD1 ASP D 239     9695   9504   6427   2655   1949  -1611       O  
ATOM   6558  OD2 ASP D 239      13.231  29.618 -50.164  1.00 69.83           O1-
ANISOU 6558  OD2 ASP D 239    10490   9442   6602   2533   1937  -1806       O1-
ATOM   6559  N   ILE D 240      12.436  24.830 -52.335  1.00 61.57           N  
ANISOU 6559  N   ILE D 240     8368   9160   5866   2064   1765  -1267       N  
ATOM   6560  CA  ILE D 240      12.921  24.294 -53.642  1.00 59.49           C  
ANISOU 6560  CA  ILE D 240     8023   8826   5754   1953   1653  -1150       C  
ATOM   6561  C   ILE D 240      11.851  24.498 -54.715  1.00 60.91           C  
ANISOU 6561  C   ILE D 240     8048   9100   5995   2161   1677  -1104       C  
ATOM   6562  O   ILE D 240      10.904  23.694 -54.764  1.00 60.62           O  
ANISOU 6562  O   ILE D 240     7759   9329   5945   2168   1718  -1050       O  
ATOM   6563  CB  ILE D 240      13.314  22.821 -53.518  1.00 57.44           C  
ANISOU 6563  CB  ILE D 240     7610   8695   5519   1695   1597  -1050       C  
ATOM   6564  CG1 ILE D 240      14.415  22.632 -52.472  1.00 57.49           C  
ANISOU 6564  CG1 ILE D 240     7768   8618   5459   1508   1557  -1085       C  
ATOM   6565  CG2 ILE D 240      13.730  22.300 -54.875  1.00 56.17           C  
ANISOU 6565  CG2 ILE D 240     7371   8468   5503   1608   1498   -945       C  
ATOM   6566  CD1 ILE D 240      14.814  21.195 -52.215  1.00 55.43           C  
ANISOU 6566  CD1 ILE D 240     7387   8470   5204   1282   1502   -985       C  
ATOM   6567  N   THR D 241      12.041  25.524 -55.556  1.00 62.46           N  
ANISOU 6567  N   THR D 241     8397   9084   6251   2308   1645  -1119       N  
ATOM   6568  CA  THR D 241      11.070  26.029 -56.563  1.00 62.62           C