CNRS Nantes University UFIP UFIP
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***  3BLH_A_VS_3BLR_A  ***

elNémo ID: 22051215411050811

Job options:

ID        	=	 22051215411050811
JOBID     	=	 3BLH_A_VS_3BLR_A
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3BLH_A_VS_3BLR_A

CRYST1  172.920  172.920   95.760  90.00  90.00 120.00 H 3           9
ATOM      1  N   VAL A   8      36.703  -3.391 -38.181  1.00115.79      A    N  
ANISOU    1  N   VAL A   8    14060  17400  12535    844    -90   -925  A    N  
ATOM      2  CA  VAL A   8      36.086  -2.950 -36.930  1.00115.57      A    C  
ANISOU    2  CA  VAL A   8    13961  17258  12693    858   -142   -800  A    C  
ATOM      3  C   VAL A   8      37.119  -2.302 -36.005  1.00108.34      A    C  
ANISOU    3  C   VAL A   8    13069  16187  11909    844      1   -676  A    C  
ATOM      4  O   VAL A   8      38.105  -2.937 -35.624  1.00107.78      A    O  
ANISOU    4  O   VAL A   8    12963  16025  11965    790     99   -761  A    O  
ATOM      5  CB  VAL A   8      35.337  -4.117 -36.223  1.00 71.68      A    C  
ANISOU    5  CB  VAL A   8     8268  11640   7328    803   -248   -934  A    C  
ATOM      6  CG1 VAL A   8      35.287  -3.922 -34.718  1.00 60.19      A    C  
ANISOU    6  CG1 VAL A   8     6740  10019   6111    788   -226   -838  A    C  
ATOM      7  CG2 VAL A   8      33.935  -4.257 -36.792  1.00 75.83      A    C  
ANISOU    7  CG2 VAL A   8     8749  12321   7743    824   -423   -967  A    C  
ATOM      8  N   GLU A   9      36.886  -1.037 -35.657  1.00101.15      A    N  
ANISOU    8  N   GLU A   9    12222  15247  10963    896      6   -479  A    N  
ATOM      9  CA  GLU A   9      37.821  -0.269 -34.833  1.00 98.88      A    C  
ANISOU    9  CA  GLU A   9    11979  14818  10774    872    129   -349  A    C  
ATOM     10  C   GLU A   9      37.994  -0.833 -33.423  1.00 89.71      A    C  
ANISOU   10  C   GLU A   9    10709  13491   9885    825    142   -383  A    C  
ATOM     11  O   GLU A   9      37.062  -1.393 -32.846  1.00 91.86      A    O  
ANISOU   11  O   GLU A   9    10886  13744  10271    831     40   -432  A    O  
ATOM     12  CB  GLU A   9      37.388   1.193 -34.753  1.00109.84      A    C  
ANISOU   12  CB  GLU A   9    13482  16191  12063    944    109   -138  A    C  
ATOM     13  CG  GLU A   9      37.752   2.018 -35.969  1.00124.01      A    C  
ANISOU   13  CG  GLU A   9    15433  18089  13596    963    154    -50  A    C  
ATOM     14  CD  GLU A   9      37.561   3.498 -35.721  1.00138.02      A    C  
ANISOU   14  CD  GLU A   9    17351  19787  15302   1025    153    170  A    C  
ATOM     15  OE1 GLU A   9      37.551   3.894 -34.535  1.00140.54      A    O  
ANISOU   15  OE1 GLU A   9    17654  19953  15793   1028    166    244  A    O  
ATOM     16  OE2 GLU A   9      37.420   4.261 -36.703  1.00144.03      A    O1-
ANISOU   16  OE2 GLU A   9    18255  20635  15833   1070    137    268  A    O1-
ATOM     17  N   CYS A  10      39.189  -0.675 -32.864  1.00 80.19      A    N  
ANISOU   17  N   CYS A  10     9514  12178   8776    771    267   -350  A    N  
ATOM     18  CA  CYS A  10      39.487  -1.268 -31.566  1.00 75.50      A    C  
ANISOU   18  CA  CYS A  10     8827  11433   8428    724    279   -386  A    C  
ATOM     19  C   CYS A  10      40.580  -0.551 -30.764  1.00 74.72      A    C  
ANISOU   19  C   CYS A  10     8762  11213   8417    679    391   -272  A    C  
ATOM     20  O   CYS A  10      41.575  -1.155 -30.381  1.00 78.98      A    O  
ANISOU   20  O   CYS A  10     9240  11693   9075    627    461   -342  A    O  
ATOM     21  CB  CYS A  10      39.849  -2.738 -31.738  1.00 66.58      A    C  
ANISOU   21  CB  CYS A  10     7609  10303   7387    687    277   -586  A    C  
ATOM     22  SG  CYS A  10      39.750  -3.615 -30.196  1.00 83.94      A    S  
ANISOU   22  SG  CYS A  10     9702  12321   9870    641    235   -630  A    S  
ATOM     23  N   PRO A  11      40.357   0.735 -30.473  1.00 71.68      A    N  
ANISOU   23  N   PRO A  11     8474  10785   7974    704    396    -99  A    N  
ATOM     24  CA  PRO A  11      41.294   1.663 -29.831  1.00 62.50      A    C  
ANISOU   24  CA  PRO A  11     7382   9514   6852    651    491     30  A    C  
ATOM     25  C   PRO A  11      41.883   1.167 -28.520  1.00 62.86      A    C  
ANISOU   25  C   PRO A  11     7339   9420   7126    592    514      1  A    C  
ATOM     26  O   PRO A  11      42.995   1.553 -28.171  1.00 70.13      A    O  
ANISOU   26  O   PRO A  11     8275  10284   8087    520    605     52  A    O  
ATOM     27  CB  PRO A  11      40.415   2.884 -29.527  1.00 67.75      A    C  
ANISOU   27  CB  PRO A  11     8161  10127   7453    719    435    189  A    C  
ATOM     28  CG  PRO A  11      39.287   2.801 -30.484  1.00 69.50      A    C  
ANISOU   28  CG  PRO A  11     8394  10487   7527    813    337    162  A    C  
ATOM     29  CD  PRO A  11      39.040   1.354 -30.718  1.00 70.23      A    C  
ANISOU   29  CD  PRO A  11     8342  10655   7687    796    291    -23  A    C  
ATOM     30  N   PHE A  12      41.137   0.351 -27.788  1.00 61.40      A    N  
ANISOU   30  N   PHE A  12     7062   9186   7081    613    430    -72  A    N  
ATOM     31  CA  PHE A  12      41.465   0.089 -26.391  1.00 55.29      A    C  
ANISOU   31  CA  PHE A  12     6235   8266   6507    567    433    -60  A    C  
ATOM     32  C   PHE A  12      41.829  -1.363 -26.166  1.00 53.85      A    C  
ANISOU   32  C   PHE A  12     5935   8061   6465    535    419   -214  A    C  
ATOM     33  O   PHE A  12      41.944  -1.824 -25.030  1.00 51.23      A    O  
ANISOU   33  O   PHE A  12     5552   7612   6301    503    397   -221  A    O  
ATOM     34  CB  PHE A  12      40.302   0.496 -25.476  1.00 58.58      A    C  
ANISOU   34  CB  PHE A  12     6664   8617   6975    612    355     15  A    C  
ATOM     35  CG  PHE A  12      39.894   1.926 -25.625  1.00 62.39      A    C  
ANISOU   35  CG  PHE A  12     7278   9098   7328    671    359    163  A    C  
ATOM     36  CD1 PHE A  12      40.845   2.936 -25.598  1.00 69.97      A    C  
ANISOU   36  CD1 PHE A  12     8352   9996   8238    627    442    270  A    C  
ATOM     37  CD2 PHE A  12      38.571   2.268 -25.798  1.00 64.29      A    C  
ANISOU   37  CD2 PHE A  12     7532   9400   7497    770    276    195  A    C  
ATOM     38  CE1 PHE A  12      40.479   4.264 -25.733  1.00 71.51      A    C  
ANISOU   38  CE1 PHE A  12     8699  10160   8312    681    439    409  A    C  
ATOM     39  CE2 PHE A  12      38.198   3.596 -25.934  1.00 71.60      A    C  
ANISOU   39  CE2 PHE A  12     8593  10309   8304    849    273    332  A    C  
ATOM     40  CZ  PHE A  12      39.152   4.594 -25.901  1.00 70.18      A    C  
ANISOU   40  CZ  PHE A  12     8554  10038   8074    804    353    439  A    C  
ATOM     41  N   CYS A  13      42.004  -2.089 -27.261  1.00 53.55      A    N  
ANISOU   41  N   CYS A  13     5868   8128   6351    548    428   -339  A    N  
ATOM     42  CA  CYS A  13      42.498  -3.444 -27.166  1.00 59.28      A    C  
ANISOU   42  CA  CYS A  13     6506   8820   7199    531    423   -494  A    C  
ATOM     43  C   CYS A  13      43.594  -3.614 -28.202  1.00 61.56      A    C  
ANISOU   43  C   CYS A  13     6789   9207   7393    537    521   -571  A    C  
ATOM     44  O   CYS A  13      43.307  -3.719 -29.394  1.00 63.29      A    O  
ANISOU   44  O   CYS A  13     7039   9555   7453    567    522   -638  A    O  
ATOM     45  CB  CYS A  13      41.363  -4.425 -27.414  1.00 62.45      A    C  
ANISOU   45  CB  CYS A  13     6873   9243   7612    548    313   -608  A    C  
ATOM     46  SG  CYS A  13      41.751  -6.105 -26.968  1.00 60.87      A    S  
ANISOU   46  SG  CYS A  13     6599   8931   7598    521    278   -780  A    S  
ATOM     47  N   ASP A  14      44.848  -3.615 -27.752  1.00 57.62      A    N  
ANISOU   47  N   ASP A  14     6246   8662   6984    507    605   -562  A    N  
ATOM     48  CA  ASP A  14      45.993  -3.722 -28.666  1.00 56.52      A    C  
ANISOU   48  CA  ASP A  14     6077   8638   6760    511    718   -631  A    C  
ATOM     49  C   ASP A  14      46.230  -5.164 -29.100  1.00 53.38      A    C  
ANISOU   49  C   ASP A  14     5612   8253   6417    565    706   -837  A    C  
ATOM     50  O   ASP A  14      45.923  -6.107 -28.357  1.00 54.86      A    O  
ANISOU   50  O   ASP A  14     5763   8314   6767    579    622   -909  A    O  
ATOM     51  CB  ASP A  14      47.265  -3.164 -28.017  1.00 60.34      A    C  
ANISOU   51  CB  ASP A  14     6515   9090   7322    455    811   -545  A    C  
ATOM     52  CG  ASP A  14      47.284  -1.645 -27.957  1.00 74.14      A    C  
ANISOU   52  CG  ASP A  14     8359  10849   8963    391    855   -356  A    C  
ATOM     53  OD1 ASP A  14      46.476  -0.988 -28.662  1.00 78.47      A    O  
ANISOU   53  OD1 ASP A  14     9012  11457   9346    407    835   -295  A    O  
ATOM     54  OD2 ASP A  14      48.123  -1.110 -27.198  1.00 79.61      A    O1-
ANISOU   54  OD2 ASP A  14     9028  11486   9735    323    902   -268  A    O1-
ATOM     55  N   GLU A  15      46.773  -5.334 -30.300  1.00 62.03      A    N  
ANISOU   55  N   GLU A  15     6704   9496   7369    595    790   -932  A    N  
ATOM     56  CA  GLU A  15      47.176  -6.660 -30.768  1.00 66.86      A    C  
ANISOU   56  CA  GLU A  15     7262  10119   8022    662    797  -1142  A    C  
ATOM     57  C   GLU A  15      48.419  -7.149 -30.029  1.00 60.94      A    C  
ANISOU   57  C   GLU A  15     6403   9301   7449    685    853  -1181  A    C  
ATOM     58  O   GLU A  15      49.369  -6.387 -29.826  1.00 57.50      A    O  
ANISOU   58  O   GLU A  15     5917   8921   7011    646    953  -1082  A    O  
ATOM     59  CB  GLU A  15      47.430  -6.643 -32.269  1.00 69.37      A    C  
ANISOU   59  CB  GLU A  15     7613  10631   8115    694    884  -1235  A    C  
ATOM     60  CG  GLU A  15      46.328  -5.980 -33.066  1.00 82.84      A    C  
ANISOU   60  CG  GLU A  15     9427  12430   9618    675    831  -1172  A    C  
ATOM     61  CD  GLU A  15      46.575  -6.052 -34.561  1.00103.19      A    C  
ANISOU   61  CD  GLU A  15    12048  15200  11958    705    910  -1273  A    C  
ATOM     62  OE1 GLU A  15      47.154  -7.062 -35.029  1.00107.36      A    O  
ANISOU   62  OE1 GLU A  15    12533  15763  12497    763    955  -1463  A    O  
ATOM     63  OE2 GLU A  15      46.183  -5.098 -35.268  1.00112.30      A    O1-
ANISOU   63  OE2 GLU A  15    13290  16469  12910    678    924  -1163  A    O1-
ATOM     64  N   VAL A  16      48.404  -8.423 -29.641  1.00 56.98      A    N  
ANISOU   64  N   VAL A  16     5872   8680   7100    743    783  -1322  A    N  
ATOM     65  CA  VAL A  16      49.479  -9.024 -28.848  1.00 57.10      A    C  
ANISOU   65  CA  VAL A  16     5786   8607   7302    789    805  -1365  A    C  
ATOM     66  C   VAL A  16      50.826  -9.037 -29.607  1.00 54.43      A    C  
ANISOU   66  C   VAL A  16     5352   8432   6896    849    955  -1446  A    C  
ATOM     67  O   VAL A  16      51.895  -9.220 -29.019  1.00 56.59      A    O  
ANISOU   67  O   VAL A  16     5514   8689   7299    882    998  -1448  A    O  
ATOM     68  CB  VAL A  16      49.087 -10.455 -28.373  1.00 54.27      A    C  
ANISOU   68  CB  VAL A  16     5447   8069   7104    848    686  -1504  A    C  
ATOM     69  CG1 VAL A  16      49.251 -11.453 -29.493  1.00 51.28      A    C  
ANISOU   69  CG1 VAL A  16     5088   7748   6650    944    710  -1725  A    C  
ATOM     70  CG2 VAL A  16      49.909 -10.889 -27.176  1.00 52.71      A    C  
ANISOU   70  CG2 VAL A  16     5172   7733   7122    878    662  -1480  A    C  
ATOM     71  N   SER A  17      50.768  -8.817 -30.915  1.00 52.35      A    N  
ANISOU   71  N   SER A  17     5127   8343   6422    861   1036  -1510  A    N  
ATOM     72  CA  SER A  17      51.973  -8.702 -31.744  1.00 59.79      A    C  
ANISOU   72  CA  SER A  17     5978   9479   7262    903   1200  -1577  A    C  
ATOM     73  C   SER A  17      52.936  -7.617 -31.256  1.00 62.89      A    C  
ANISOU   73  C   SER A  17     6276   9948   7672    816   1301  -1408  A    C  
ATOM     74  O   SER A  17      54.094  -7.617 -31.635  1.00 74.13      A    O  
ANISOU   74  O   SER A  17     7578  11520   9069    845   1432  -1457  A    O  
ATOM     75  CB  SER A  17      51.594  -8.416 -33.201  1.00 64.98      A    C  
ANISOU   75  CB  SER A  17     6720  10317   7651    898   1268  -1630  A    C  
ATOM     76  OG  SER A  17      51.072  -7.096 -33.360  1.00 71.17      A    O  
ANISOU   76  OG  SER A  17     7587  11161   8293    783   1277  -1435  A    O  
ATOM     77  N   LYS A  18      52.458  -6.688 -30.434  1.00 55.14      A    N  
ANISOU   77  N   LYS A  18     5348   8873   6729    709   1240  -1214  A    N  
ATOM     78  CA  LYS A  18      53.330  -5.668 -29.855  1.00 58.00      A    C  
ANISOU   78  CA  LYS A  18     5639   9276   7123    607   1314  -1054  A    C  
ATOM     79  C   LYS A  18      54.406  -6.320 -28.980  1.00 67.73      A    C  
ANISOU   79  C   LYS A  18     6707  10462   8564    660   1315  -1108  A    C  
ATOM     80  O   LYS A  18      55.493  -5.759 -28.753  1.00 61.61      A    O  
ANISOU   80  O   LYS A  18     5814   9786   7808    600   1406  -1039  A    O  
ATOM     81  CB  LYS A  18      52.516  -4.667 -29.015  1.00 46.88      A    C  
ANISOU   81  CB  LYS A  18     4341   7736   5734    501   1227   -858  A    C  
ATOM     82  CG  LYS A  18      51.909  -5.265 -27.759  1.00 54.66      A    C  
ANISOU   82  CG  LYS A  18     5340   8506   6923    530   1079   -855  A    C  
ATOM     83  CD  LYS A  18      50.879  -4.330 -27.114  1.00 60.00      A    C  
ANISOU   83  CD  LYS A  18     6141   9073   7582    450    998   -688  A    C  
ATOM     84  CE  LYS A  18      51.533  -3.105 -26.499  1.00 54.76      A    C  
ANISOU   84  CE  LYS A  18     5477   8407   6921    336   1049   -515  A    C  
ATOM     85  NZ  LYS A  18      50.544  -2.308 -25.721  1.00 58.05      A    N1+
ANISOU   85  NZ  LYS A  18     6020   8690   7345    286    963   -373  A    N1+
ATOM     86  N   TYR A  19      54.066  -7.501 -28.469  1.00 66.69      A    N  
ANISOU   86  N   TYR A  19     6576  10176   8587    766   1203  -1226  A    N  
ATOM     87  CA  TYR A  19      54.966  -8.304 -27.663  1.00 58.72      A    C  
ANISOU   87  CA  TYR A  19     5432   9098   7779    851   1177  -1292  A    C  
ATOM     88  C   TYR A  19      55.522  -9.403 -28.546  1.00 62.90      A    C  
ANISOU   88  C   TYR A  19     5892   9716   8292   1009   1240  -1513  A    C  
ATOM     89  O   TYR A  19      54.851  -9.889 -29.451  1.00 69.74      A    O  
ANISOU   89  O   TYR A  19     6857  10598   9046   1061   1236  -1634  A    O  
ATOM     90  CB  TYR A  19      54.235  -8.890 -26.451  1.00 61.73      A    C  
ANISOU   90  CB  TYR A  19     5883   9229   8343    862   1007  -1264  A    C  
ATOM     91  CG  TYR A  19      53.668  -7.830 -25.536  1.00 62.50      A    C  
ANISOU   91  CG  TYR A  19     6053   9241   8454    721    950  -1060  A    C  
ATOM     92  CD1 TYR A  19      54.488  -7.140 -24.651  1.00 64.91      A    C  
ANISOU   92  CD1 TYR A  19     6276   9550   8838    646    965   -933  A    C  
ATOM     93  CD2 TYR A  19      52.317  -7.499 -25.573  1.00 60.76      A    C  
ANISOU   93  CD2 TYR A  19     5981   8946   8160    666    880   -999  A    C  
ATOM     94  CE1 TYR A  19      53.980  -6.154 -23.821  1.00 59.18      A    C  
ANISOU   94  CE1 TYR A  19     5634   8736   8113    523    916   -758  A    C  
ATOM     95  CE2 TYR A  19      51.792  -6.507 -24.749  1.00 54.59      A    C  
ANISOU   95  CE2 TYR A  19     5268   8089   7384    559    836   -822  A    C  
ATOM     96  CZ  TYR A  19      52.630  -5.840 -23.873  1.00 63.27      A    C  
ANISOU   96  CZ  TYR A  19     6306   9176   8559    489    856   -705  A    C  
ATOM     97  OH  TYR A  19      52.123  -4.855 -23.042  1.00 61.84      A    O  
ANISOU   97  OH  TYR A  19     6211   8908   8377    388    812   -543  A    O  
ATOM     98  N   GLU A  20      56.768  -9.774 -28.302  1.00 70.95      A    N  
ANISOU   98  N   GLU A  20     6739  10804   9414   1091   1297  -1572  A    N  
ATOM     99  CA  GLU A  20      57.395 -10.806 -29.093  1.00 69.65      A    C  
ANISOU   99  CA  GLU A  20     6497  10727   9240   1268   1366  -1791  A    C  
ATOM    100  C   GLU A  20      57.539 -12.058 -28.242  1.00 65.13      A    C  
ANISOU  100  C   GLU A  20     5907   9947   8893   1417   1237  -1892  A    C  
ATOM    101  O   GLU A  20      58.200 -12.045 -27.206  1.00 62.60      A    O  
ANISOU  101  O   GLU A  20     5478   9571   8736   1425   1190  -1817  A    O  
ATOM    102  CB  GLU A  20      58.742 -10.308 -29.577  1.00 79.76      A    C  
ANISOU  102  CB  GLU A  20     7577  12275  10453   1269   1544  -1794  A    C  
ATOM    103  CG  GLU A  20      59.445 -11.221 -30.546  1.00 96.78      A    C  
ANISOU  103  CG  GLU A  20     9639  14575  12559   1456   1653  -2025  A    C  
ATOM    104  CD  GLU A  20      60.890 -10.808 -30.736  1.00113.93      A    C  
ANISOU  104  CD  GLU A  20    11562  17010  14716   1465   1817  -2019  A    C  
ATOM    105  OE1 GLU A  20      61.266  -9.719 -30.234  1.00113.97      A    O  
ANISOU  105  OE1 GLU A  20    11492  17090  14721   1292   1849  -1827  A    O  
ATOM    106  OE2 GLU A  20      61.642 -11.571 -31.378  1.00119.96      A    O1-
ANISOU  106  OE2 GLU A  20    12206  17909  15465   1642   1915  -2209  A    O1-
ATOM    107  N   LYS A  21      56.887 -13.134 -28.663  1.00 62.35      A    N  
ANISOU  107  N   LYS A  21     5679   9469   8544   1525   1169  -2058  A    N  
ATOM    108  CA  LYS A  21      56.909 -14.371 -27.887  1.00 70.81      A    C  
ANISOU  108  CA  LYS A  21     6779  10305   9821   1660   1034  -2151  A    C  
ATOM    109  C   LYS A  21      58.307 -14.983 -27.835  1.00 78.68      A    C  
ANISOU  109  C   LYS A  21     7592  11381  10923   1850   1095  -2267  A    C  
ATOM    110  O   LYS A  21      58.889 -15.308 -28.869  1.00 84.88      A    O  
ANISOU  110  O   LYS A  21     8309  12333  11610   1974   1220  -2432  A    O  
ATOM    111  CB  LYS A  21      55.915 -15.382 -28.462  1.00 67.62      A    C  
ANISOU  111  CB  LYS A  21     6560   9751   9380   1719    952  -2315  A    C  
ATOM    112  CG  LYS A  21      54.504 -15.220 -27.964  1.00 57.97      A    C  
ANISOU  112  CG  LYS A  21     5506   8355   8164   1566    817  -2205  A    C  
ATOM    113  CD  LYS A  21      53.541 -15.949 -28.872  1.00 63.07      A    C  
ANISOU  113  CD  LYS A  21     6313   8944   8707   1583    771  -2365  A    C  
ATOM    114  CE  LYS A  21      52.095 -15.680 -28.464  1.00 70.46      A    C  
ANISOU  114  CE  LYS A  21     7385   9758   9629   1417    648  -2251  A    C  
ATOM    115  NZ  LYS A  21      51.131 -15.890 -29.593  1.00 73.41      A    N1+
ANISOU  115  NZ  LYS A  21     7881  10183   9829   1384    635  -2365  A    N1+
ATOM    116  N   LEU A  22      58.839 -15.146 -26.630  1.00 77.96      A    N  
ANISOU  116  N   LEU A  22     7417  11179  11026   1881   1007  -2183  A    N  
ATOM    117  CA  LEU A  22      60.170 -15.721 -26.463  1.00 83.37      A    C  
ANISOU  117  CA  LEU A  22     7910  11938  11829   2075   1043  -2279  A    C  
ATOM    118  C   LEU A  22      60.154 -17.216 -26.146  1.00 91.57      A    C  
ANISOU  118  C   LEU A  22     9034  12732  13027   2289    916  -2438  A    C  
ATOM    119  O   LEU A  22      60.927 -17.982 -26.717  1.00100.69      A    O  
ANISOU  119  O   LEU A  22    10105  13955  14198   2507    978  -2626  A    O  
ATOM    120  CB  LEU A  22      60.934 -14.983 -25.366  1.00 82.46      A    C  
ANISOU  120  CB  LEU A  22     7628  11878  11825   1993   1020  -2094  A    C  
ATOM    121  CG  LEU A  22      61.269 -13.529 -25.657  1.00 81.60      A    C  
ANISOU  121  CG  LEU A  22     7407  12023  11576   1797   1158  -1949  A    C  
ATOM    122  CD1 LEU A  22      62.033 -12.929 -24.493  1.00 82.18      A    C  
ANISOU  122  CD1 LEU A  22     7328  12123  11775   1717   1109  -1784  A    C  
ATOM    123  CD2 LEU A  22      62.071 -13.453 -26.932  1.00 83.29      A    C  
ANISOU  123  CD2 LEU A  22     7472  12528  11647   1875   1355  -2083  A    C  
ATOM    124  N   ALA A  23      59.275 -17.630 -25.235  1.00 93.20      A    N  
ANISOU  124  N   ALA A  23     9416  12653  13345   2228    741  -2362  A    N  
ATOM    125  CA  ALA A  23      59.308 -18.992 -24.713  1.00 89.95      A    C  
ANISOU  125  CA  ALA A  23     9100  11975  13103   2407    599  -2470  A    C  
ATOM    126  C   ALA A  23      58.058 -19.348 -23.908  1.00 96.69      A    C  
ANISOU  126  C   ALA A  23    10183  12528  14026   2277    425  -2379  A    C  
ATOM    127  O   ALA A  23      57.650 -18.591 -23.028  1.00 99.47      A    O  
ANISOU  127  O   ALA A  23    10543  12850  14400   2099    372  -2177  A    O  
ATOM    128  CB  ALA A  23      60.551 -19.170 -23.846  1.00 80.63      A    C  
ANISOU  128  CB  ALA A  23     7731  10816  12090   2550    564  -2431  A    C  
ATOM    129  N   LYS A  24      57.460 -20.503 -24.202  1.00 98.45      A    N  
ANISOU  129  N   LYS A  24    10595  12533  14278   2361    340  -2530  A    N  
ATOM    130  CA  LYS A  24      56.392 -21.041 -23.362  1.00 95.64      A    C  
ANISOU  130  CA  LYS A  24    10449  11879  14012   2251    169  -2455  A    C  
ATOM    131  C   LYS A  24      56.935 -21.266 -21.963  1.00 94.42      A    C  
ANISOU  131  C   LYS A  24    10256  11575  14045   2295     51  -2323  A    C  
ATOM    132  O   LYS A  24      58.084 -21.658 -21.798  1.00 97.58      A    O  
ANISOU  132  O   LYS A  24    10531  12003  14542   2497     57  -2382  A    O  
ATOM    133  CB  LYS A  24      55.871 -22.375 -23.900  1.00 99.58      A    C  
ANISOU  133  CB  LYS A  24    11151  12155  14529   2350     92  -2658  A    C  
ATOM    134  CG  LYS A  24      54.915 -22.271 -25.076  1.00109.15      A    C  
ANISOU  134  CG  LYS A  24    12471  13443  15558   2247    148  -2766  A    C  
ATOM    135  CD  LYS A  24      54.378 -23.650 -25.465  1.00116.78      A    C  
ANISOU  135  CD  LYS A  24    13662  14152  16558   2323     46  -2963  A    C  
ATOM    136  CE  LYS A  24      53.926 -23.697 -26.926  1.00117.14      A    C  
ANISOU  136  CE  LYS A  24    13769  14330  16408   2316    132  -3150  A    C  
ATOM    137  NZ  LYS A  24      53.382 -25.032 -27.324  1.00113.63      A    N1+
ANISOU  137  NZ  LYS A  24    13559  13627  15988   2372     25  -3352  A    N1+
ATOM    138  N   ILE A  25      56.108 -21.011 -20.958  1.00 95.62      A    N  
ANISOU  138  N   ILE A  25    10510  11580  14240   2111    -56  -2145  A    N  
ATOM    139  CA  ILE A  25      56.484 -21.291 -19.579  1.00 99.21      A    C  
ANISOU  139  CA  ILE A  25    10969  11868  14857   2135   -185  -2013  A    C  
ATOM    140  C   ILE A  25      55.309 -21.919 -18.845  1.00109.45      A    C  
ANISOU  140  C   ILE A  25    12501  12876  16210   2003   -333  -1945  A    C  
ATOM    141  O   ILE A  25      55.189 -21.803 -17.622  1.00104.23      A    O  
ANISOU  141  O   ILE A  25    11873  12099  15632   1918   -431  -1776  A    O  
ATOM    142  CB  ILE A  25      56.979 -20.030 -18.843  1.00 87.85      A    C  
ANISOU  142  CB  ILE A  25     9358  10611  13410   2024   -145  -1816  A    C  
ATOM    143  CG1 ILE A  25      55.868 -18.984 -18.750  1.00 82.93      A    C  
ANISOU  143  CG1 ILE A  25     8795  10048  12668   1767   -112  -1674  A    C  
ATOM    144  CG2 ILE A  25      58.193 -19.451 -19.549  1.00 85.66      A    C  
ANISOU  144  CG2 ILE A  25     8839  10626  13083   2136      2  -1880  A    C  
ATOM    145  CD1 ILE A  25      56.329 -17.647 -18.193  1.00 77.11      A    C  
ANISOU  145  CD1 ILE A  25     7910   9494  11897   1652    -56  -1500  A    C  
ATOM    146  N   GLY A  26      54.446 -22.585 -19.610  1.00118.30      A    N  
ANISOU  146  N   GLY A  26    13783  13890  17277   1976   -347  -2080  A    N  
ATOM    147  CA  GLY A  26      53.313 -23.306 -19.060  1.00120.13      A    C  
ANISOU  147  CA  GLY A  26    14238  13851  17555   1842   -481  -2041  A    C  
ATOM    148  C   GLY A  26      52.086 -23.337 -19.960  1.00121.06      A    C  
ANISOU  148  C   GLY A  26    14468  13986  17544   1694   -456  -2125  A    C  
ATOM    149  O   GLY A  26      52.136 -22.943 -21.130  1.00111.77      A    O  
ANISOU  149  O   GLY A  26    13222  13010  16237   1726   -342  -2241  A    O  
ATOM    150  N   GLN A  27      50.984 -23.835 -19.404  1.00129.16      A    N  
ANISOU  150  N   GLN A  27    15667  14805  18603   1528   -570  -2063  A    N  
ATOM    151  CA  GLN A  27      49.676 -23.796 -20.057  1.00128.92      A    C  
ANISOU  151  CA  GLN A  27    15726  14799  18457   1347   -568  -2107  A    C  
ATOM    152  C   GLN A  27      48.569 -23.612 -19.025  1.00125.74      A    C  
ANISOU  152  C   GLN A  27    15398  14300  18078   1111   -649  -1923  A    C  
ATOM    153  O   GLN A  27      48.190 -24.563 -18.334  1.00127.76      A    O  
ANISOU  153  O   GLN A  27    15814  14294  18434   1056   -771  -1902  A    O  
ATOM    154  CB  GLN A  27      49.408 -25.064 -20.869  1.00126.18      A    C  
ANISOU  154  CB  GLN A  27    15554  14273  18116   1409   -629  -2329  A    C  
ATOM    155  CG  GLN A  27      47.937 -25.222 -21.226  1.00125.53      A    C  
ANISOU  155  CG  GLN A  27    15589  14157  17948   1181   -678  -2348  A    C  
ATOM    156  CD  GLN A  27      47.729 -25.714 -22.639  1.00133.20      A    C  
ANISOU  156  CD  GLN A  27    16630  15168  18811   1232   -652  -2585  A    C  
ATOM    157  NE2 GLN A  27      46.612 -25.319 -23.241  1.00127.11      A    N  
ANISOU  157  NE2 GLN A  27    15864  14525  17907   1053   -644  -2593  A    N  
ATOM    158  OE1 GLN A  27      48.562 -26.439 -23.188  1.00143.06      A    O  
ANISOU  158  OE1 GLN A  27    17926  16339  20090   1441   -642  -2764  A    O  
ATOM    159  N   GLY A  28      48.052 -22.390 -18.939  1.00116.33      A    N  
ANISOU  159  N   GLY A  28    14094  13320  16786    977   -576  -1791  A    N  
ATOM    160  CA  GLY A  28      47.046 -22.033 -17.953  1.00116.04      A    C  
ANISOU  160  CA  GLY A  28    14094  13243  16755    770   -626  -1611  A    C  
ATOM    161  C   GLY A  28      45.671 -22.659 -18.140  1.00117.75      A    C  
ANISOU  161  C   GLY A  28    14440  13359  16941    590   -700  -1650  A    C  
ATOM    162  O   GLY A  28      45.509 -23.647 -18.864  1.00122.46      A    O  
ANISOU  162  O   GLY A  28    15150  13837  17545    617   -749  -1820  A    O  
ATOM    163  N   THR A  29      44.676 -22.068 -17.480  1.00112.67      A    N  
ANISOU  163  N   THR A  29    13776  12773  16261    401   -705  -1496  A    N  
ATOM    164  CA  THR A  29      43.317 -22.609 -17.450  1.00111.22      A    C  
ANISOU  164  CA  THR A  29    13687  12514  16057    200   -777  -1502  A    C  
ATOM    165  C   THR A  29      42.583 -22.487 -18.786  1.00108.03      A    C  
ANISOU  165  C   THR A  29    13257  12267  15521    156   -749  -1640  A    C  
ATOM    166  O   THR A  29      41.714 -23.300 -19.101  1.00105.12      A    O  
ANISOU  166  O   THR A  29    12989  11803  15147     30   -827  -1724  A    O  
ATOM    167  CB  THR A  29      42.462 -21.933 -16.350  1.00103.98      A    C  
ANISOU  167  CB  THR A  29    12729  11651  15129     23   -776  -1297  A    C  
ATOM    168  CG2 THR A  29      41.084 -22.589 -16.251  1.00 98.19      A    C  
ANISOU  168  CG2 THR A  29    12078  10846  14384   -199   -850  -1299  A    C  
ATOM    169  OG1 THR A  29      43.129 -22.044 -15.088  1.00107.58      A    O  
ANISOU  169  OG1 THR A  29    13222  11965  15691     55   -809  -1165  A    O  
ATOM    170  N   PHE A  30      42.940 -21.476 -19.572  1.00104.42      A    N  
ANISOU  170  N   PHE A  30    12671  12050  14953    252   -644  -1662  A    N  
ATOM    171  CA  PHE A  30      42.194 -21.159 -20.783  1.00 98.79      A    C  
ANISOU  171  CA  PHE A  30    11921  11522  14091    208   -617  -1761  A    C  
ATOM    172  C   PHE A  30      43.054 -21.195 -22.033  1.00 97.86      A    C  
ANISOU  172  C   PHE A  30    11789  11496  13899    383   -551  -1934  A    C  
ATOM    173  O   PHE A  30      42.588 -20.808 -23.105  1.00101.93      A    O  
ANISOU  173  O   PHE A  30    12271  12191  14269    368   -516  -2011  A    O  
ATOM    174  CB  PHE A  30      41.561 -19.772 -20.648  1.00 99.05      A    C  
ANISOU  174  CB  PHE A  30    11824  11791  14020    135   -549  -1609  A    C  
ATOM    175  CG  PHE A  30      40.629 -19.647 -19.476  1.00100.12      A    C  
ANISOU  175  CG  PHE A  30    11958  11879  14205    -32   -596  -1449  A    C  
ATOM    176  CD1 PHE A  30      39.367 -20.239 -19.514  1.00 92.42      A    C  
ANISOU  176  CD1 PHE A  30    11025  10873  13217   -209   -676  -1475  A    C  
ATOM    177  CD2 PHE A  30      41.014 -18.953 -18.334  1.00 96.37      A    C  
ANISOU  177  CD2 PHE A  30    11437  11398  13783    -22   -559  -1276  A    C  
ATOM    178  CE1 PHE A  30      38.513 -20.136 -18.441  1.00 93.16      A    C  
ANISOU  178  CE1 PHE A  30    11103  10945  13349   -366   -705  -1328  A    C  
ATOM    179  CE2 PHE A  30      40.160 -18.846 -17.253  1.00 92.72      A    C  
ANISOU  179  CE2 PHE A  30    10976  10902  13352   -171   -590  -1134  A    C  
ATOM    180  CZ  PHE A  30      38.906 -19.437 -17.308  1.00 93.25      A    C  
ANISOU  180  CZ  PHE A  30    11073  10952  13404   -341   -658  -1159  A    C  
ATOM    181  N   GLY A  31      44.300 -21.657 -21.885  1.00 92.43      A    N  
ANISOU  181  N   GLY A  31    11121  10695  13304    552   -533  -1991  A    N  
ATOM    182  CA  GLY A  31      45.296 -21.602 -22.946  1.00 98.32      A    C  
ANISOU  182  CA  GLY A  31    11822  11551  13984    739   -444  -2139  A    C  
ATOM    183  C   GLY A  31      46.736 -21.577 -22.430  1.00110.46      A    C  
ANISOU  183  C   GLY A  31    13294  13048  15627    917   -397  -2112  A    C  
ATOM    184  O   GLY A  31      46.981 -21.813 -21.247  1.00122.00      A    O  
ANISOU  184  O   GLY A  31    14777  14352  17226    907   -457  -1997  A    O  
ATOM    185  N   GLU A  32      47.690 -21.276 -23.312  1.00 99.83      A    N  
ANISOU  185  N   GLU A  32    11859  11861  14209   1078   -287  -2216  A    N  
ATOM    186  CA  GLU A  32      49.108 -21.352 -22.971  1.00 91.49      A    C  
ANISOU  186  CA  GLU A  32    10719  10794  13250   1263   -241  -2221  A    C  
ATOM    187  C   GLU A  32      49.693 -20.091 -22.318  1.00 82.56      A    C  
ANISOU  187  C   GLU A  32     9424   9827  12118   1244   -164  -2029  A    C  
ATOM    188  O   GLU A  32      49.146 -18.998 -22.446  1.00 83.07      A    O  
ANISOU  188  O   GLU A  32     9434  10059  12071   1122   -108  -1918  A    O  
ATOM    189  CB  GLU A  32      49.923 -21.729 -24.207  1.00101.75      A    C  
ANISOU  189  CB  GLU A  32    11991  12191  14478   1450   -154  -2437  A    C  
ATOM    190  CG  GLU A  32      49.652 -23.142 -24.699  1.00110.67      A    C  
ANISOU  190  CG  GLU A  32    13301  13106  15643   1515   -242  -2648  A    C  
ATOM    191  CD  GLU A  32      50.772 -23.688 -25.569  1.00114.80      A    C  
ANISOU  191  CD  GLU A  32    13796  13673  16150   1762   -164  -2860  A    C  
ATOM    192  OE1 GLU A  32      50.980 -23.153 -26.680  1.00114.27      A    O  
ANISOU  192  OE1 GLU A  32    13650  13848  15918   1802    -38  -2950  A    O  
ATOM    193  OE2 GLU A  32      51.433 -24.662 -25.145  1.00114.49      A    O1-
ANISOU  193  OE2 GLU A  32    13819  13426  16256   1921   -228  -2938  A    O1-
ATOM    194  N   VAL A  33      50.807 -20.261 -21.612  1.00 74.59      A    N  
ANISOU  194  N   VAL A  33     8347   8760  11235   1369   -169  -1993  A    N  
ATOM    195  CA  VAL A  33      51.502 -19.148 -20.973  1.00 77.98      A    C  
ANISOU  195  CA  VAL A  33     8622   9334  11673   1352   -105  -1828  A    C  
ATOM    196  C   VAL A  33      52.874 -18.905 -21.611  1.00 82.68      A    C  
ANISOU  196  C   VAL A  33     9056  10113  12247   1522     12  -1913  A    C  
ATOM    197  O   VAL A  33      53.699 -19.818 -21.677  1.00 87.21      A    O  
ANISOU  197  O   VAL A  33     9618  10604  12915   1705    -10  -2037  A    O  
ATOM    198  CB  VAL A  33      51.696 -19.404 -19.472  1.00 74.74      A    C  
ANISOU  198  CB  VAL A  33     8240   8738  11421   1330   -216  -1685  A    C  
ATOM    199  CG1 VAL A  33      52.134 -18.123 -18.768  1.00 69.05      A    C  
ANISOU  199  CG1 VAL A  33     7386   8166  10683   1258   -163  -1499  A    C  
ATOM    200  CG2 VAL A  33      50.418 -19.923 -18.868  1.00 75.87      A    C  
ANISOU  200  CG2 VAL A  33     8550   8681  11596   1179   -332  -1628  A    C  
ATOM    201  N   PHE A  34      53.115 -17.672 -22.063  1.00 75.25      A    N  
ANISOU  201  N   PHE A  34     7992   9420  11179   1463    137  -1841  A    N  
ATOM    202  CA  PHE A  34      54.366 -17.304 -22.736  1.00 67.52      A    C  
ANISOU  202  CA  PHE A  34     6843   8659  10155   1586    270  -1908  A    C  
ATOM    203  C   PHE A  34      55.151 -16.221 -22.011  1.00 67.86      A    C  
ANISOU  203  C   PHE A  34     6731   8832  10222   1528    318  -1736  A    C  
ATOM    204  O   PHE A  34      54.569 -15.261 -21.493  1.00 66.15      A    O  
ANISOU  204  O   PHE A  34     6539   8634   9962   1360    310  -1567  A    O  
ATOM    205  CB  PHE A  34      54.074 -16.763 -24.132  1.00 66.88      A    C  
ANISOU  205  CB  PHE A  34     6753   8789   9870   1555    398  -1989  A    C  
ATOM    206  CG  PHE A  34      53.468 -17.760 -25.054  1.00 78.75      A    C  
ANISOU  206  CG  PHE A  34     8390  10214  11318   1619    371  -2187  A    C  
ATOM    207  CD1 PHE A  34      54.270 -18.653 -25.750  1.00 86.35      A    C  
ANISOU  207  CD1 PHE A  34     9326  11188  12295   1819    415  -2394  A    C  
ATOM    208  CD2 PHE A  34      52.098 -17.803 -25.239  1.00 78.31      A    C  
ANISOU  208  CD2 PHE A  34     8482  10082  11192   1483    300  -2174  A    C  
ATOM    209  CE1 PHE A  34      53.716 -19.577 -26.609  1.00 87.51      A    C  
ANISOU  209  CE1 PHE A  34     9616  11252  12383   1875    386  -2589  A    C  
ATOM    210  CE2 PHE A  34      51.534 -18.723 -26.098  1.00 88.89      A    C  
ANISOU  210  CE2 PHE A  34     9948  11351  12475   1524    265  -2363  A    C  
ATOM    211  CZ  PHE A  34      52.348 -19.615 -26.785  1.00 90.51      A    C  
ANISOU  211  CZ  PHE A  34    10149  11549  12691   1718    306  -2573  A    C  
ATOM    212  N   LYS A  35      56.475 -16.355 -21.999  1.00 68.92      A    N  
ANISOU  212  N   LYS A  35     6702   9065  10422   1668    369  -1784  A    N  
ATOM    213  CA  LYS A  35      57.328 -15.226 -21.663  1.00 65.96      A    C  
ANISOU  213  CA  LYS A  35     6153   8881  10029   1599    447  -1650  A    C  
ATOM    214  C   LYS A  35      57.518 -14.419 -22.941  1.00 67.86      A    C  
ANISOU  214  C   LYS A  35     6317   9385  10080   1559    621  -1693  A    C  
ATOM    215  O   LYS A  35      57.718 -14.991 -24.012  1.00 72.85      A    O  
ANISOU  215  O   LYS A  35     6937  10097  10645   1683    696  -1869  A    O  
ATOM    216  CB  LYS A  35      58.681 -15.679 -21.127  1.00 67.73      A    C  
ANISOU  216  CB  LYS A  35     6207   9131  10397   1758    426  -1680  A    C  
ATOM    217  CG  LYS A  35      59.567 -14.513 -20.698  1.00 69.20      A    C  
ANISOU  217  CG  LYS A  35     6206   9515  10571   1658    491  -1536  A    C  
ATOM    218  CD  LYS A  35      60.968 -14.961 -20.337  1.00 72.59      A    C  
ANISOU  218  CD  LYS A  35     6427  10024  11129   1827    480  -1584  A    C  
ATOM    219  CE  LYS A  35      61.796 -13.790 -19.815  1.00 82.49      A    C  
ANISOU  219  CE  LYS A  35     7499  11469  12375   1692    526  -1431  A    C  
ATOM    220  NZ  LYS A  35      63.182 -14.184 -19.406  1.00 84.89      A    N1+
ANISOU  220  NZ  LYS A  35     7569  11877  12808   1847    502  -1469  A    N1+
ATOM    221  N   ALA A  36      57.431 -13.097 -22.847  1.00 57.10      A    N  
ANISOU  221  N   ALA A  36     4923   8151   8623   1386    685  -1533  A    N  
ATOM    222  CA  ALA A  36      57.589 -12.280 -24.043  1.00 59.33      A    C  
ANISOU  222  CA  ALA A  36     5155   8674   8713   1330    846  -1551  A    C  
ATOM    223  C   ALA A  36      58.231 -10.928 -23.792  1.00 62.36      A    C  
ANISOU  223  C   ALA A  36     5426   9226   9043   1182    931  -1386  A    C  
ATOM    224  O   ALA A  36      58.432 -10.499 -22.650  1.00 59.24      A    O  
ANISOU  224  O   ALA A  36     5003   8755   8748   1102    855  -1247  A    O  
ATOM    225  CB  ALA A  36      56.261 -12.114 -24.773  1.00 56.87      A    C  
ANISOU  225  CB  ALA A  36     5025   8330   8254   1253    844  -1564  A    C  
ATOM    226  N   ARG A  37      58.522 -10.254 -24.894  1.00 66.49      A    N  
ANISOU  226  N   ARG A  37     5897   9973   9393   1137   1085  -1403  A    N  
ATOM    227  CA  ARG A  37      59.349  -9.065 -24.892  1.00 65.31      A    C  
ANISOU  227  CA  ARG A  37     5622  10016   9178   1001   1193  -1275  A    C  
ATOM    228  C   ARG A  37      58.636  -7.975 -25.660  1.00 63.33      A    C  
ANISOU  228  C   ARG A  37     5498   9845   8719    849   1273  -1182  A    C  
ATOM    229  O   ARG A  37      58.258  -8.171 -26.815  1.00 60.50      A    O  
ANISOU  229  O   ARG A  37     5199   9574   8215    894   1346  -1283  A    O  
ATOM    230  CB  ARG A  37      60.677  -9.393 -25.582  1.00 63.26      A    C  
ANISOU  230  CB  ARG A  37     5138   9991   8905   1112   1329  -1401  A    C  
ATOM    231  CG  ARG A  37      61.663  -8.264 -25.630  1.00 60.01      A    C  
ANISOU  231  CG  ARG A  37     4564   9805   8430    962   1451  -1283  A    C  
ATOM    232  CD  ARG A  37      62.888  -8.649 -26.456  1.00 56.73      A    C  
ANISOU  232  CD  ARG A  37     3916   9657   7982   1079   1605  -1424  A    C  
ATOM    233  NE  ARG A  37      63.831  -7.542 -26.480  1.00 67.41      A    N  
ANISOU  233  NE  ARG A  37     5102  11236   9273    903   1723  -1301  A    N  
ATOM    234  CZ  ARG A  37      63.750  -6.513 -27.313  1.00 68.35      A    C  
ANISOU  234  CZ  ARG A  37     5271  11511   9190    731   1860  -1218  A    C  
ATOM    235  NH1 ARG A  37      62.776  -6.462 -28.216  1.00 59.96      A    N1+
ANISOU  235  NH1 ARG A  37     4407  10413   7960    730   1894  -1250  A    N1+
ATOM    236  NH2 ARG A  37      64.655  -5.545 -27.251  1.00 74.43      A    N  
ANISOU  236  NH2 ARG A  37     5891  12472   9916    553   1960  -1101  A    N  
ATOM    237  N   HIS A  38      58.437  -6.832 -25.020  1.00 58.50      A    N  
ANISOU  237  N   HIS A  38     4942   9198   8088    674   1250   -993  A    N  
ATOM    238  CA  HIS A  38      57.880  -5.695 -25.720  1.00 57.48      A    C  
ANISOU  238  CA  HIS A  38     4934   9143   7761    534   1326   -888  A    C  
ATOM    239  C   HIS A  38      58.810  -5.321 -26.868  1.00 64.55      A    C  
ANISOU  239  C   HIS A  38     5711  10307   8506    508   1509   -927  A    C  
ATOM    240  O   HIS A  38      60.017  -5.198 -26.668  1.00 66.91      A    O  
ANISOU  240  O   HIS A  38     5818  10742   8862    485   1579   -922  A    O  
ATOM    241  CB  HIS A  38      57.707  -4.517 -24.773  1.00 61.91      A    C  
ANISOU  241  CB  HIS A  38     5569   9615   8339    361   1276   -684  A    C  
ATOM    242  CG  HIS A  38      56.980  -3.373 -25.394  1.00 68.71      A    C  
ANISOU  242  CG  HIS A  38     6594  10502   9009    239   1325   -567  A    C  
ATOM    243  CD2 HIS A  38      55.721  -2.909 -25.211  1.00 55.77      A    C  
ANISOU  243  CD2 HIS A  38     5151   8724   7317    206   1246   -483  A    C  
ATOM    244  ND1 HIS A  38      57.545  -2.581 -26.372  1.00 77.72      A    N  
ANISOU  244  ND1 HIS A  38     7711  11840   9978    147   1475   -527  A    N  
ATOM    245  CE1 HIS A  38      56.668  -1.669 -26.753  1.00 77.58      A    C  
ANISOU  245  CE1 HIS A  38     7883  11785   9810     64   1475   -416  A    C  
ATOM    246  NE2 HIS A  38      55.553  -1.847 -26.063  1.00 61.03      A    N  
ANISOU  246  NE2 HIS A  38     5913   9489   7785    108   1336   -392  A    N  
ATOM    247  N   ARG A  39      58.263  -5.138 -28.069  1.00 62.30      A    N  
ANISOU  247  N   ARG A  39     5530  10116   8026    508   1587   -965  A    N  
ATOM    248  CA  ARG A  39      59.113  -4.984 -29.246  1.00 56.86      A    C  
ANISOU  248  CA  ARG A  39     4730   9693   7179    504   1770  -1030  A    C  
ATOM    249  C   ARG A  39      59.891  -3.671 -29.294  1.00 64.42      A    C  
ANISOU  249  C   ARG A  39     5630  10802   8045    302   1886   -863  A    C  
ATOM    250  O   ARG A  39      60.855  -3.548 -30.058  1.00 63.22      A    O  
ANISOU  250  O   ARG A  39     5332  10893   7795    279   2047   -906  A    O  
ATOM    251  CB  ARG A  39      58.333  -5.198 -30.542  1.00 63.98      A    C  
ANISOU  251  CB  ARG A  39     5768  10660   7880    561   1817  -1123  A    C  
ATOM    252  CG  ARG A  39      58.000  -6.665 -30.814  1.00 82.79      A    C  
ANISOU  252  CG  ARG A  39     8153  12973  10330    767   1756  -1346  A    C  
ATOM    253  CD  ARG A  39      57.470  -6.909 -32.241  1.00 87.87      A    C  
ANISOU  253  CD  ARG A  39     8902  13734  10750    820   1826  -1465  A    C  
ATOM    254  NE  ARG A  39      56.613  -8.097 -32.308  1.00 86.40      A    N  
ANISOU  254  NE  ARG A  39     8813  13390  10624    963   1702  -1629  A    N  
ATOM    255  CZ  ARG A  39      57.018  -9.313 -32.679  1.00 92.85      A    C  
ANISOU  255  CZ  ARG A  39     9565  14223  11490   1136   1720  -1850  A    C  
ATOM    256  NH1 ARG A  39      58.281  -9.523 -33.043  1.00 88.28      A    N1+
ANISOU  256  NH1 ARG A  39     8803  13833  10905   1214   1867  -1942  A    N1+
ATOM    257  NH2 ARG A  39      56.152 -10.323 -32.688  1.00 90.56      A    N  
ANISOU  257  NH2 ARG A  39     9395  13760  11254   1234   1592  -1983  A    N  
ATOM    258  N   LYS A  40      59.495  -2.699 -28.474  1.00 66.18      A    N  
ANISOU  258  N   LYS A  40     5966  10885   8296    151   1807   -678  A    N  
ATOM    259  CA  LYS A  40      60.135  -1.380 -28.509  1.00 57.70      A    C  
ANISOU  259  CA  LYS A  40     4880   9918   7125    -66   1903   -509  A    C  
ATOM    260  C   LYS A  40      61.063  -1.113 -27.330  1.00 57.24      A    C  
ANISOU  260  C   LYS A  40     4672   9840   7239   -158   1864   -434  A    C  
ATOM    261  O   LYS A  40      62.093  -0.464 -27.482  1.00 62.91      A    O  
ANISOU  261  O   LYS A  40     5259  10732   7911   -304   1976   -369  A    O  
ATOM    262  CB  LYS A  40      59.089  -0.276 -28.592  1.00 60.25      A    C  
ANISOU  262  CB  LYS A  40     5466  10113   7314   -187   1859   -344  A    C  
ATOM    263  CG  LYS A  40      58.443  -0.116 -29.960  1.00 60.52      A    C  
ANISOU  263  CG  LYS A  40     5639  10243   7115   -163   1935   -367  A    C  
ATOM    264  CD  LYS A  40      57.130   0.659 -29.831  1.00 62.25      A    C  
ANISOU  264  CD  LYS A  40     6119  10279   7253   -202   1831   -234  A    C  
ATOM    265  CE  LYS A  40      56.593   1.061 -31.188  1.00 70.53      A    C  
ANISOU  265  CE  LYS A  40     7313  11438   8045   -209   1904   -217  A    C  
ATOM    266  NZ  LYS A  40      57.629   1.764 -32.000  1.00 77.24      A    N1+
ANISOU  266  NZ  LYS A  40     8110  12506   8730   -355   2085   -152  A    N1+
ATOM    267  N   THR A  41      60.695  -1.624 -26.163  1.00 56.83      A    N  
ANISOU  267  N   THR A  41     4636   9582   7377    -83   1703   -443  A    N  
ATOM    268  CA  THR A  41      61.375  -1.299 -24.914  1.00 59.34      A    C  
ANISOU  268  CA  THR A  41     4857   9842   7848   -178   1630   -354  A    C  
ATOM    269  C   THR A  41      62.111  -2.496 -24.330  1.00 64.95      A    C  
ANISOU  269  C   THR A  41     5349  10573   8756    -16   1572   -487  A    C  
ATOM    270  O   THR A  41      62.987  -2.334 -23.482  1.00 67.06      A    O  
ANISOU  270  O   THR A  41     5467  10871   9139    -81   1536   -439  A    O  
ATOM    271  CB  THR A  41      60.354  -0.881 -23.855  1.00 58.16      A    C  
ANISOU  271  CB  THR A  41     4915   9422   7761   -224   1474   -242  A    C  
ATOM    272  CG2 THR A  41      59.354   0.133 -24.440  1.00 42.40      A    C  
ANISOU  272  CG2 THR A  41     3167   7365   5579   -320   1502   -131  A    C  
ATOM    273  OG1 THR A  41      59.661  -2.054 -23.397  1.00 54.30      A    O  
ANISOU  273  OG1 THR A  41     4453   8778   7400    -37   1351   -350  A    O  
ATOM    274  N   GLY A  42      61.729  -3.697 -24.759  1.00 63.28      A    N  
ANISOU  274  N   GLY A  42     5133  10332   8579    198   1552   -652  A    N  
ATOM    275  CA  GLY A  42      62.356  -4.918 -24.291  1.00 55.56      A    C  
ANISOU  275  CA  GLY A  42     3979   9349   7782    385   1492   -787  A    C  
ATOM    276  C   GLY A  42      61.751  -5.407 -22.991  1.00 58.04      A    C  
ANISOU  276  C   GLY A  42     4390   9394   8268    439   1296   -755  A    C  
ATOM    277  O   GLY A  42      62.148  -6.451 -22.468  1.00 58.07      A    O  
ANISOU  277  O   GLY A  42     4290   9344   8431    598   1216   -850  A    O  
ATOM    278  N   GLN A  43      60.782  -4.663 -22.464  1.00 59.41      A    N  
ANISOU  278  N   GLN A  43     4771   9399   8406    311   1222   -619  A    N  
ATOM    279  CA  GLN A  43      60.151  -5.033 -21.195  1.00 63.14      A    C  
ANISOU  279  CA  GLN A  43     5344   9626   9019    339   1048   -574  A    C  
ATOM    280  C   GLN A  43      59.600  -6.447 -21.260  1.00 64.88      A    C  
ANISOU  280  C   GLN A  43     5602   9722   9328    541    970   -721  A    C  
ATOM    281  O   GLN A  43      58.813  -6.759 -22.152  1.00 62.02      A    O  
ANISOU  281  O   GLN A  43     5344   9351   8870    598   1005   -800  A    O  
ATOM    282  CB  GLN A  43      59.036  -4.054 -20.836  1.00 58.21      A    C  
ANISOU  282  CB  GLN A  43     4948   8858   8313    199   1003   -431  A    C  
ATOM    283  CG  GLN A  43      58.187  -4.482 -19.649  1.00 67.60      A    C  
ANISOU  283  CG  GLN A  43     6259   9806   9619    233    842   -395  A    C  
ATOM    284  CD  GLN A  43      56.804  -3.845 -19.668  1.00 79.33      A    C  
ANISOU  284  CD  GLN A  43     7969  11170  11004    168    817   -314  A    C  
ATOM    285  NE2 GLN A  43      56.184  -3.739 -18.499  1.00 80.63      A    N  
ANISOU  285  NE2 GLN A  43     8239  11158  11240    133    702   -234  A    N  
ATOM    286  OE1 GLN A  43      56.297  -3.459 -20.728  1.00 82.30      A    O  
ANISOU  286  OE1 GLN A  43     8418  11621  11232    158    899   -324  A    O  
ATOM    287  N   LYS A  44      60.028  -7.302 -20.331  1.00 67.15      A    N  
ANISOU  287  N   LYS A  44     5811   9910   9792    645    857   -757  A    N  
ATOM    288  CA  LYS A  44      59.567  -8.689 -20.301  1.00 62.06      A    C  
ANISOU  288  CA  LYS A  44     5218   9117   9245    830    770   -891  A    C  
ATOM    289  C   LYS A  44      58.210  -8.790 -19.616  1.00 67.84      A    C  
ANISOU  289  C   LYS A  44     6169   9611   9996    781    648   -824  A    C  
ATOM    290  O   LYS A  44      57.971  -8.152 -18.589  1.00 71.23      A    O  
ANISOU  290  O   LYS A  44     6660   9948  10455    663    576   -682  A    O  
ATOM    291  CB  LYS A  44      60.560  -9.587 -19.576  1.00 58.94      A    C  
ANISOU  291  CB  LYS A  44     4670   8698   9028    970    689   -948  A    C  
ATOM    292  CG  LYS A  44      61.988  -9.566 -20.124  1.00 60.60      A    C  
ANISOU  292  CG  LYS A  44     4620   9164   9242   1038    802  -1020  A    C  
ATOM    293  CD  LYS A  44      62.048  -9.950 -21.585  1.00 63.52      A    C  
ANISOU  293  CD  LYS A  44     4953   9682   9499   1144    947  -1180  A    C  
ATOM    294  CE  LYS A  44      63.483  -9.871 -22.100  1.00 67.03      A    C  
ANISOU  294  CE  LYS A  44     5120  10411   9938   1203   1076  -1247  A    C  
ATOM    295  NZ  LYS A  44      64.155  -8.597 -21.718  1.00 63.66      A    N1+
ANISOU  295  NZ  LYS A  44     4574  10139   9473    988   1126  -1086  A    N1+
ATOM    296  N   VAL A  45      57.327  -9.598 -20.192  1.00 65.74      A    N  
ANISOU  296  N   VAL A  45     6017   9256   9707    869    627   -932  A    N  
ATOM    297  CA  VAL A  45      55.976  -9.771 -19.674  1.00 62.79      A    C  
ANISOU  297  CA  VAL A  45     5832   8685   9343    820    523   -883  A    C  
ATOM    298  C   VAL A  45      55.566 -11.244 -19.776  1.00 66.60      A    C  
ANISOU  298  C   VAL A  45     6375   9018   9913    961    440  -1027  A    C  
ATOM    299  O   VAL A  45      56.230 -12.033 -20.445  1.00 62.33      A    O  
ANISOU  299  O   VAL A  45     5752   8534   9399   1106    478  -1177  A    O  
ATOM    300  CB  VAL A  45      54.961  -8.927 -20.476  1.00 63.21      A    C  
ANISOU  300  CB  VAL A  45     6000   8798   9219    721    590   -842  A    C  
ATOM    301  CG1 VAL A  45      55.370  -7.449 -20.487  1.00 60.37      A    C  
ANISOU  301  CG1 VAL A  45     5610   8569   8758    581    676   -701  A    C  
ATOM    302  CG2 VAL A  45      54.829  -9.463 -21.902  1.00 60.38      A    C  
ANISOU  302  CG2 VAL A  45     5640   8544   8757    813    669  -1002  A    C  
ATOM    303  N   ALA A  46      54.473 -11.615 -19.112  1.00 66.68      A    N  
ANISOU  303  N   ALA A  46     6532   8836   9968    917    329   -986  A    N  
ATOM    304  CA  ALA A  46      53.890 -12.943 -19.288  1.00 61.16      A    C  
ANISOU  304  CA  ALA A  46     5926   7981   9331   1010    250  -1114  A    C  
ATOM    305  C   ALA A  46      52.558 -12.811 -20.004  1.00 61.21      A    C  
ANISOU  305  C   ALA A  46     6055   7988   9213    937    261  -1138  A    C  
ATOM    306  O   ALA A  46      51.719 -11.992 -19.623  1.00 61.10      A    O  
ANISOU  306  O   ALA A  46     6106   7969   9139    809    250  -1011  A    O  
ATOM    307  CB  ALA A  46      53.705 -13.648 -17.951  1.00 56.04      A    C  
ANISOU  307  CB  ALA A  46     5348   7108   8835   1010    104  -1052  A    C  
ATOM    308  N   LEU A  47      52.377 -13.615 -21.046  1.00 63.90      A    N  
ANISOU  308  N   LEU A  47     6426   8341   9511   1025    280  -1307  A    N  
ATOM    309  CA  LEU A  47      51.126 -13.643 -21.783  1.00 56.27      A    C  
ANISOU  309  CA  LEU A  47     5570   7381   8430    962    272  -1352  A    C  
ATOM    310  C   LEU A  47      50.373 -14.923 -21.444  1.00 61.29      A    C  
ANISOU  310  C   LEU A  47     6325   7800   9164    975    145  -1432  A    C  
ATOM    311  O   LEU A  47      50.867 -16.025 -21.678  1.00 71.65      A    O  
ANISOU  311  O   LEU A  47     7650   9021  10552   1098    114  -1576  A    O  
ATOM    312  CB  LEU A  47      51.393 -13.572 -23.288  1.00 56.35      A    C  
ANISOU  312  CB  LEU A  47     5547   7574   8291   1029    384  -1487  A    C  
ATOM    313  CG  LEU A  47      52.267 -12.425 -23.792  1.00 58.76      A    C  
ANISOU  313  CG  LEU A  47     5735   8105   8487   1015    525  -1425  A    C  
ATOM    314  CD1 LEU A  47      52.442 -12.493 -25.306  1.00 52.71      A    C  
ANISOU  314  CD1 LEU A  47     4955   7515   7558   1079    634  -1569  A    C  
ATOM    315  CD2 LEU A  47      51.689 -11.078 -23.373  1.00 52.49      A    C  
ANISOU  315  CD2 LEU A  47     4973   7354   7616    865    536  -1231  A    C  
ATOM    316  N   LYS A  48      49.185 -14.778 -20.875  1.00 58.96      A    N  
ANISOU  316  N   LYS A  48     6117   7419   8865    848     71  -1338  A    N  
ATOM    317  CA  LYS A  48      48.346 -15.926 -20.566  1.00 59.05      A    C  
ANISOU  317  CA  LYS A  48     6247   7235   8955    816    -46  -1399  A    C  
ATOM    318  C   LYS A  48      47.135 -15.918 -21.475  1.00 56.51      A    C  
ANISOU  318  C   LYS A  48     5986   6980   8505    740    -52  -1463  A    C  
ATOM    319  O   LYS A  48      46.313 -15.008 -21.411  1.00 66.32      A    O  
ANISOU  319  O   LYS A  48     7221   8320   9659    637    -36  -1353  A    O  
ATOM    320  CB  LYS A  48      47.919 -15.899 -19.101  1.00 58.57      A    C  
ANISOU  320  CB  LYS A  48     6228   7026   8999    717   -132  -1242  A    C  
ATOM    321  CG  LYS A  48      49.093 -15.909 -18.145  1.00 76.38      A    C  
ANISOU  321  CG  LYS A  48     8428   9218  11376    787   -146  -1172  A    C  
ATOM    322  CD  LYS A  48      48.669 -16.348 -16.757  1.00 95.97      A    C  
ANISOU  322  CD  LYS A  48    10992  11503  13968    708   -258  -1059  A    C  
ATOM    323  CE  LYS A  48      49.842 -16.311 -15.772  1.00101.67      A    C  
ANISOU  323  CE  LYS A  48    11659  12171  14800    778   -287   -980  A    C  
ATOM    324  NZ  LYS A  48      49.359 -16.486 -14.365  1.00103.23      A    N1+
ANISOU  324  NZ  LYS A  48    11944  12209  15070    676   -384   -839  A    N1+
ATOM    325  N   LYS A  49      47.033 -16.927 -22.335  1.00 55.76      A    N  
ANISOU  325  N   LYS A  49     5953   6837   8396    798    -79  -1647  A    N  
ATOM    326  CA  LYS A  49      45.962 -16.980 -23.319  1.00 65.46      A    C  
ANISOU  326  CA  LYS A  49     7235   8148   9490    730    -93  -1729  A    C  
ATOM    327  C   LYS A  49      44.653 -17.409 -22.659  1.00 67.66      A    C  
ANISOU  327  C   LYS A  49     7592   8298   9817    578   -209  -1675  A    C  
ATOM    328  O   LYS A  49      44.679 -18.180 -21.705  1.00 63.13      A    O  
ANISOU  328  O   LYS A  49     7079   7522   9389    552   -289  -1649  A    O  
ATOM    329  CB  LYS A  49      46.330 -17.951 -24.431  1.00 73.25      A    C  
ANISOU  329  CB  LYS A  49     8274   9117  10440    838    -88  -1956  A    C  
ATOM    330  CG  LYS A  49      45.572 -17.744 -25.733  1.00 83.16      A    C  
ANISOU  330  CG  LYS A  49     9555  10533  11508    801    -67  -2054  A    C  
ATOM    331  CD  LYS A  49      45.831 -18.903 -26.686  1.00 95.55      A    C  
ANISOU  331  CD  LYS A  49    11212  12040  13054    896    -85  -2296  A    C  
ATOM    332  CE  LYS A  49      45.154 -18.689 -28.031  1.00107.41      A    C  
ANISOU  332  CE  LYS A  49    12742  13718  14349    862    -67  -2401  A    C  
ATOM    333  NZ  LYS A  49      45.802 -17.608 -28.829  1.00111.80      A    N1+
ANISOU  333  NZ  LYS A  49    13204  14528  14746    932     78  -2370  A    N1+
ATOM    334  N   VAL A  50      43.528 -16.874 -23.144  1.00 68.78      A    N  
ANISOU  334  N   VAL A  50     7728   8571   9833    478   -217  -1648  A    N  
ATOM    335  CA  VAL A  50      42.182 -17.355 -22.782  1.00 72.15      A    C  
ANISOU  335  CA  VAL A  50     8209   8923  10282    325   -322  -1630  A    C  
ATOM    336  C   VAL A  50      41.601 -18.130 -23.975  1.00 65.18      A    C  
ANISOU  336  C   VAL A  50     7391   8062   9311    304   -373  -1819  A    C  
ATOM    337  O   VAL A  50      42.261 -18.247 -24.995  1.00 77.24      A    O  
ANISOU  337  O   VAL A  50     8929   9659  10762    417   -321  -1954  A    O  
ATOM    338  CB  VAL A  50      41.258 -16.199 -22.393  1.00 66.23      A    C  
ANISOU  338  CB  VAL A  50     7389   8317   9458    232   -305  -1464  A    C  
ATOM    339  CG1 VAL A  50      39.929 -16.731 -21.864  1.00 58.84      A    C  
ANISOU  339  CG1 VAL A  50     6481   7316   8561     71   -405  -1436  A    C  
ATOM    340  CG2 VAL A  50      41.938 -15.328 -21.365  1.00 58.13      A    C  
ANISOU  340  CG2 VAL A  50     6312   7282   8491    264   -244  -1297  A    C  
ATOM    341  N   GLU A  55      34.116 -21.087 -23.620  1.00114.74      A    N  
ANISOU  341  N   GLU A  55    13735  14303  15558   -763   -959  -1909  A    N  
ATOM    342  CA  GLU A  55      33.765 -22.295 -24.366  1.00107.99      A    C  
ANISOU  342  CA  GLU A  55    12999  13340  14693   -871  -1068  -2102  A    C  
ATOM    343  C   GLU A  55      32.331 -22.361 -24.906  1.00 94.71      A    C  
ANISOU  343  C   GLU A  55    11233  11839  12912  -1062  -1161  -2141  A    C  
ATOM    344  O   GLU A  55      32.042 -21.887 -26.008  1.00 91.60      A    O  
ANISOU  344  O   GLU A  55    10781  11659  12366  -1010  -1171  -2219  A    O  
ATOM    345  CB  GLU A  55      34.023 -23.494 -23.452  1.00112.24      A    C  
ANISOU  345  CB  GLU A  55    13690  13554  15402   -970  -1125  -2106  A    C  
ATOM    346  CG  GLU A  55      35.184 -23.259 -22.456  1.00111.05      A    C  
ANISOU  346  CG  GLU A  55    13569  13256  15370   -819  -1044  -1987  A    C  
ATOM    347  CD  GLU A  55      34.889 -22.212 -21.364  1.00 97.45      A    C  
ANISOU  347  CD  GLU A  55    11706  11657  13666   -844   -974  -1759  A    C  
ATOM    348  OE1 GLU A  55      33.717 -21.822 -21.167  1.00 96.90      A    O  
ANISOU  348  OE1 GLU A  55    11522  11749  13545   -993   -993  -1680  A    O  
ATOM    349  OE2 GLU A  55      35.842 -21.784 -20.686  1.00 88.45      A    O1-
ANISOU  349  OE2 GLU A  55    10567  10452  12590   -710   -903  -1663  A    O1-
ATOM    350  N   LYS A  56      31.439 -22.963 -24.124  1.00 86.51      A    N  
ANISOU  350  N   LYS A  56    10189  10724  11958  -1290  -1235  -2084  A    N  
ATOM    351  CA  LYS A  56      30.062 -23.189 -24.560  1.00 88.06      A    C  
ANISOU  351  CA  LYS A  56    10297  11084  12080  -1502  -1337  -2129  A    C  
ATOM    352  C   LYS A  56      29.134 -22.010 -24.250  1.00 71.63      A    C  
ANISOU  352  C   LYS A  56     7980   9308   9929  -1521  -1297  -1968  A    C  
ATOM    353  O   LYS A  56      27.986 -21.970 -24.680  1.00 73.81      A    O  
ANISOU  353  O   LYS A  56     8134   9787  10125  -1660  -1374  -1993  A    O  
ATOM    354  CB  LYS A  56      29.511 -24.470 -23.921  1.00 96.37      A    C  
ANISOU  354  CB  LYS A  56    11455  11912  13250  -1767  -1436  -2153  A    C  
ATOM    355  CG  LYS A  56      30.123 -25.770 -24.451  1.00100.23      A    C  
ANISOU  355  CG  LYS A  56    12192  12105  13785  -1782  -1514  -2351  A    C  
ATOM    356  CD  LYS A  56      29.288 -26.970 -24.020  1.00104.59      A    C  
ANISOU  356  CD  LYS A  56    12842  12479  14419  -2092  -1635  -2382  A    C  
ATOM    357  CE  LYS A  56      29.479 -28.147 -24.957  1.00108.68      A    C  
ANISOU  357  CE  LYS A  56    13581  12791  14921  -2143  -1746  -2623  A    C  
ATOM    358  NZ  LYS A  56      28.243 -28.978 -25.044  1.00108.31      A    N1+
ANISOU  358  NZ  LYS A  56    13552  12732  14870  -2486  -1884  -2680  A    N1+
ATOM    359  N   GLU A  57      29.634 -21.050 -23.497  1.00 59.49      A    N  
ANISOU  359  N   GLU A  57     6378   7805   8421  -1375  -1183  -1807  A    N  
ATOM    360  CA  GLU A  57      28.812 -19.939 -23.075  1.00 56.26      A    C  
ANISOU  360  CA  GLU A  57     5767   7650   7957  -1370  -1138  -1652  A    C  
ATOM    361  C   GLU A  57      29.533 -18.629 -23.354  1.00 53.32      A    C  
ANISOU  361  C   GLU A  57     5354   7401   7505  -1114  -1032  -1582  A    C  
ATOM    362  O   GLU A  57      29.631 -17.772 -22.482  1.00 51.92      A    O  
ANISOU  362  O   GLU A  57     5108   7261   7356  -1042   -947  -1423  A    O  
ATOM    363  CB  GLU A  57      28.491 -20.082 -21.587  1.00 47.59      A    C  
ANISOU  363  CB  GLU A  57     4637   6461   6984  -1498  -1105  -1498  A    C  
ATOM    364  CG  GLU A  57      27.602 -21.273 -21.273  1.00 61.14      A    C  
ANISOU  364  CG  GLU A  57     6375   8093   8765  -1788  -1206  -1540  A    C  
ATOM    365  CD  GLU A  57      26.191 -21.118 -21.845  1.00 73.72      A    C  
ANISOU  365  CD  GLU A  57     7777   9974  10257  -1932  -1281  -1571  A    C  
ATOM    366  OE1 GLU A  57      25.652 -19.986 -21.824  1.00 68.01      A    O  
ANISOU  366  OE1 GLU A  57     6866   9521   9455  -1836  -1232  -1475  A    O  
ATOM    367  OE2 GLU A  57      25.622 -22.130 -22.315  1.00 81.92      A    O1-
ANISOU  367  OE2 GLU A  57     8858  10969  11297  -2140  -1396  -1693  A    O1-
ATOM    368  N   GLY A  58      30.050 -18.483 -24.570  1.00 52.24      A    N  
ANISOU  368  N   GLY A  58     5271   7318   7260   -984  -1036  -1700  A    N  
ATOM    369  CA  GLY A  58      30.834 -17.309 -24.913  1.00 50.78      A    C  
ANISOU  369  CA  GLY A  58     5072   7230   6992   -759   -934  -1638  A    C  
ATOM    370  C   GLY A  58      32.080 -17.146 -24.053  1.00 52.06      A    C  
ANISOU  370  C   GLY A  58     5315   7199   7267   -652   -831  -1558  A    C  
ATOM    371  O   GLY A  58      32.664 -18.130 -23.582  1.00 54.13      A    O  
ANISOU  371  O   GLY A  58     5689   7223   7654   -700   -848  -1610  A    O  
ATOM    372  N   PHE A  59      32.479 -15.895 -23.840  1.00 49.72      A    N  
ANISOU  372  N   PHE A  59     4964   7001   6925   -507   -735  -1430  A    N  
ATOM    373  CA  PHE A  59      33.654 -15.589 -23.041  1.00 45.22      A    C  
ANISOU  373  CA  PHE A  59     4451   6282   6448   -408   -641  -1346  A    C  
ATOM    374  C   PHE A  59      33.524 -16.123 -21.615  1.00 51.33      A    C  
ANISOU  374  C   PHE A  59     5242   6886   7378   -523   -652  -1257  A    C  
ATOM    375  O   PHE A  59      32.583 -15.793 -20.918  1.00 58.91      A    O  
ANISOU  375  O   PHE A  59     6112   7928   8344   -611   -659  -1153  A    O  
ATOM    376  CB  PHE A  59      33.931 -14.083 -23.022  1.00 45.03      A    C  
ANISOU  376  CB  PHE A  59     4369   6401   6338   -266   -547  -1214  A    C  
ATOM    377  CG  PHE A  59      35.305 -13.745 -22.530  1.00 54.50      A    C  
ANISOU  377  CG  PHE A  59     5630   7474   7602   -158   -454  -1160  A    C  
ATOM    378  CD1 PHE A  59      36.374 -13.660 -23.416  1.00 55.58      A    C  
ANISOU  378  CD1 PHE A  59     5819   7615   7684    -42   -403  -1241  A    C  
ATOM    379  CD2 PHE A  59      35.545 -13.554 -21.182  1.00 52.36      A    C  
ANISOU  379  CD2 PHE A  59     5359   7090   7445   -182   -420  -1032  A    C  
ATOM    380  CE1 PHE A  59      37.660 -13.377 -22.971  1.00 49.41      A    C  
ANISOU  380  CE1 PHE A  59     5071   6737   6967     48   -321  -1195  A    C  
ATOM    381  CE2 PHE A  59      36.828 -13.268 -20.728  1.00 54.07      A    C  
ANISOU  381  CE2 PHE A  59     5623   7200   7723    -91   -349   -986  A    C  
ATOM    382  CZ  PHE A  59      37.890 -13.183 -21.629  1.00 45.80      A    C  
ANISOU  382  CZ  PHE A  59     4609   6166   6626     21   -301  -1068  A    C  
ATOM    383  N   PRO A  60      34.482 -16.948 -21.178  1.00 60.98      A    N  
ANISOU  383  N   PRO A  60     6576   7873   8718   -514   -652  -1297  A    N  
ATOM    384  CA  PRO A  60      34.430 -17.633 -19.878  1.00 56.85      A    C  
ANISOU  384  CA  PRO A  60     6103   7158   8339   -630   -678  -1222  A    C  
ATOM    385  C   PRO A  60      34.186 -16.686 -18.699  1.00 55.85      A    C  
ANISOU  385  C   PRO A  60     5900   7092   8228   -634   -614  -1032  A    C  
ATOM    386  O   PRO A  60      34.965 -15.754 -18.421  1.00 51.46      A    O  
ANISOU  386  O   PRO A  60     5333   6559   7660   -500   -532   -950  A    O  
ATOM    387  CB  PRO A  60      35.823 -18.275 -19.761  1.00 52.29      A    C  
ANISOU  387  CB  PRO A  60     5652   6356   7860   -528   -668  -1282  A    C  
ATOM    388  CG  PRO A  60      36.281 -18.405 -21.164  1.00 54.87      A    C  
ANISOU  388  CG  PRO A  60     6004   6743   8100   -421   -666  -1446  A    C  
ATOM    389  CD  PRO A  60      35.749 -17.203 -21.880  1.00 56.89      A    C  
ANISOU  389  CD  PRO A  60     6145   7271   8201   -372   -619  -1407  A    C  
ATOM    390  N   ILE A  61      33.100 -16.961 -17.990  1.00 52.19      A    N  
ANISOU  390  N   ILE A  61     5387   6651   7790   -800   -649   -968  A    N  
ATOM    391  CA  ILE A  61      32.691 -16.166 -16.843  1.00 41.47      A    C  
ANISOU  391  CA  ILE A  61     3958   5362   6438   -819   -589   -802  A    C  
ATOM    392  C   ILE A  61      33.777 -16.173 -15.774  1.00 50.16      A    C  
ANISOU  392  C   ILE A  61     5154   6270   7635   -767   -548   -715  A    C  
ATOM    393  O   ILE A  61      33.941 -15.216 -15.015  1.00 59.40      A    O  
ANISOU  393  O   ILE A  61     6291   7490   8789   -705   -477   -591  A    O  
ATOM    394  CB  ILE A  61      31.312 -16.635 -16.308  1.00 57.85      A    C  
ANISOU  394  CB  ILE A  61     5954   7505   8521  -1027   -631   -765  A    C  
ATOM    395  CG1 ILE A  61      30.830 -15.755 -15.157  1.00 52.46      A    C  
ANISOU  395  CG1 ILE A  61     5186   6921   7824  -1032   -554   -603  A    C  
ATOM    396  CG2 ILE A  61      31.307 -18.158 -15.954  1.00 37.73      A    C  
ANISOU  396  CG2 ILE A  61     3527   4728   6083  -1210   -714   -818  A    C  
ATOM    397  CD1 ILE A  61      29.377 -15.994 -14.839  1.00 46.73      A    C  
ANISOU  397  CD1 ILE A  61     4332   6347   7076  -1212   -577   -574  A    C  
ATOM    398  N   THR A  62      34.547 -17.246 -15.747  1.00 56.85      A    N  
ANISOU  398  N   THR A  62     6127   6895   8577   -782   -600   -785  A    N  
ATOM    399  CA  THR A  62      35.650 -17.375 -14.804  1.00 54.91      A    C  
ANISOU  399  CA  THR A  62     5972   6463   8427   -721   -583   -713  A    C  
ATOM    400  C   THR A  62      36.777 -16.409 -15.139  1.00 55.21      A    C  
ANISOU  400  C   THR A  62     5989   6556   8433   -524   -511   -705  A    C  
ATOM    401  O   THR A  62      37.384 -15.810 -14.241  1.00 54.86      A    O  
ANISOU  401  O   THR A  62     5952   6478   8415   -473   -466   -592  A    O  
ATOM    402  CB  THR A  62      36.153 -18.832 -14.757  1.00 62.32      A    C  
ANISOU  402  CB  THR A  62     7056   7143   9478   -768   -671   -799  A    C  
ATOM    403  CG2 THR A  62      37.620 -18.896 -14.493  1.00 75.29      A    C  
ANISOU  403  CG2 THR A  62     8772   8639  11197   -610   -658   -797  A    C  
ATOM    404  OG1 THR A  62      35.484 -19.506 -13.688  1.00 66.43      A    O  
ANISOU  404  OG1 THR A  62     7631   7550  10060   -953   -715   -711  A    O  
ATOM    405  N   ALA A  63      37.049 -16.246 -16.430  1.00 48.05      A    N  
ANISOU  405  N   ALA A  63     5059   5742   7458   -428   -498   -823  A    N  
ATOM    406  CA  ALA A  63      38.052 -15.276 -16.862  1.00 50.48      A    C  
ANISOU  406  CA  ALA A  63     5337   6130   7715   -263   -420   -812  A    C  
ATOM    407  C   ALA A  63      37.580 -13.830 -16.627  1.00 56.20      A    C  
ANISOU  407  C   ALA A  63     5979   7034   8342   -238   -349   -689  A    C  
ATOM    408  O   ALA A  63      38.368 -12.977 -16.224  1.00 52.10      A    O  
ANISOU  408  O   ALA A  63     5458   6519   7818   -156   -287   -607  A    O  
ATOM    409  CB  ALA A  63      38.438 -15.502 -18.324  1.00 48.29      A    C  
ANISOU  409  CB  ALA A  63     5064   5914   7372   -176   -418   -970  A    C  
ATOM    410  N   LEU A  64      36.295 -13.559 -16.861  1.00 57.96      A    N  
ANISOU  410  N   LEU A  64     6133   7402   8488   -307   -363   -676  A    N  
ATOM    411  CA  LEU A  64      35.753 -12.232 -16.572  1.00 51.64      A    C  
ANISOU  411  CA  LEU A  64     5263   6757   7600   -268   -303   -560  A    C  
ATOM    412  C   LEU A  64      35.960 -11.898 -15.117  1.00 49.79      A    C  
ANISOU  412  C   LEU A  64     5054   6434   7428   -294   -269   -428  A    C  
ATOM    413  O   LEU A  64      36.343 -10.788 -14.781  1.00 55.28      A    O  
ANISOU  413  O   LEU A  64     5751   7171   8082   -212   -205   -341  A    O  
ATOM    414  CB  LEU A  64      34.261 -12.140 -16.883  1.00 47.26      A    C  
ANISOU  414  CB  LEU A  64     4614   6371   6971   -339   -334   -566  A    C  
ATOM    415  CG  LEU A  64      33.915 -12.194 -18.367  1.00 51.66      A    C  
ANISOU  415  CG  LEU A  64     5137   7065   7429   -301   -372   -683  A    C  
ATOM    416  CD1 LEU A  64      32.426 -12.351 -18.540  1.00 56.11      A    C  
ANISOU  416  CD1 LEU A  64     5594   7784   7943   -400   -428   -695  A    C  
ATOM    417  CD2 LEU A  64      34.443 -10.974 -19.119  1.00 39.16      A    C  
ANISOU  417  CD2 LEU A  64     3554   5593   5733   -143   -308   -656  A    C  
ATOM    418  N   ARG A  65      35.705 -12.864 -14.248  1.00 46.53      A    N  
ANISOU  418  N   ARG A  65     4676   5893   7109   -417   -315   -412  A    N  
ATOM    419  CA  ARG A  65      35.837 -12.623 -12.816  1.00 48.63      A    C  
ANISOU  419  CA  ARG A  65     4978   6080   7422   -456   -289   -284  A    C  
ATOM    420  C   ARG A  65      37.277 -12.264 -12.454  1.00 51.38      A    C  
ANISOU  420  C   ARG A  65     5392   6317   7813   -356   -263   -248  A    C  
ATOM    421  O   ARG A  65      37.518 -11.294 -11.729  1.00 53.32      A    O  
ANISOU  421  O   ARG A  65     5644   6586   8028   -316   -210   -147  A    O  
ATOM    422  CB  ARG A  65      35.359 -13.836 -12.032  1.00 46.57      A    C  
ANISOU  422  CB  ARG A  65     4759   5690   7244   -618   -349   -272  A    C  
ATOM    423  CG  ARG A  65      35.267 -13.647 -10.549  1.00 58.98      A    C  
ANISOU  423  CG  ARG A  65     6365   7204   8840   -682   -323   -137  A    C  
ATOM    424  CD  ARG A  65      34.942 -14.984  -9.932  1.00 66.42      A    C  
ANISOU  424  CD  ARG A  65     7378   7996   9865   -849   -391   -131  A    C  
ATOM    425  NE  ARG A  65      35.845 -15.997 -10.470  1.00 85.64      A    N  
ANISOU  425  NE  ARG A  65     9906  10247  12389   -818   -466   -228  A    N  
ATOM    426  CZ  ARG A  65      35.918 -17.253 -10.045  1.00 93.20      A    C  
ANISOU  426  CZ  ARG A  65    10971  11006  13434   -927   -543   -236  A    C  
ATOM    427  NH1 ARG A  65      35.123 -17.673  -9.064  1.00 92.09      A    N1+
ANISOU  427  NH1 ARG A  65    10856  10832  13301  -1099   -552   -143  A    N1+
ATOM    428  NH2 ARG A  65      36.790 -18.087 -10.603  1.00 93.92      A    N  
ANISOU  428  NH2 ARG A  65    11150  10932  13601   -860   -607   -336  A    N  
ATOM    429  N   GLU A  66      38.229 -13.030 -12.986  1.00 47.74      A    N  
ANISOU  429  N   GLU A  66     4978   5744   7418   -311   -301   -339  A    N  
ATOM    430  CA  GLU A  66      39.642 -12.803 -12.704  1.00 49.78      A    C  
ANISOU  430  CA  GLU A  66     5273   5914   7726   -218   -284   -317  A    C  
ATOM    431  C   GLU A  66      40.084 -11.424 -13.187  1.00 52.31      A    C  
ANISOU  431  C   GLU A  66     5549   6374   7954   -117   -203   -286  A    C  
ATOM    432  O   GLU A  66      40.716 -10.665 -12.448  1.00 50.64      A    O  
ANISOU  432  O   GLU A  66     5354   6143   7744    -91   -169   -194  A    O  
ATOM    433  CB  GLU A  66      40.497 -13.880 -13.360  1.00 53.94      A    C  
ANISOU  433  CB  GLU A  66     5837   6327   8332   -164   -333   -441  A    C  
ATOM    434  CG  GLU A  66      41.991 -13.708 -13.132  1.00 62.82      A    C  
ANISOU  434  CG  GLU A  66     6970   7385   9513    -57   -318   -429  A    C  
ATOM    435  CD  GLU A  66      42.812 -14.797 -13.806  1.00 74.95      A    C  
ANISOU  435  CD  GLU A  66     8532   8819  11126     22   -362   -565  A    C  
ATOM    436  OE1 GLU A  66      42.210 -15.669 -14.469  1.00 79.36      A    O  
ANISOU  436  OE1 GLU A  66     9124   9342  11688    -12   -405   -672  A    O  
ATOM    437  OE2 GLU A  66      44.059 -14.783 -13.682  1.00 73.52      A    O1-
ANISOU  437  OE2 GLU A  66     8335   8597  10999    122   -354   -570  A    O1-
ATOM    438  N   ILE A  67      39.742 -11.109 -14.433  1.00 45.00      A    N  
ANISOU  438  N   ILE A  67     4577   5580   6938    -71   -177   -361  A    N  
ATOM    439  CA  ILE A  67      40.029  -9.805 -14.999  1.00 49.40      A    C  
ANISOU  439  CA  ILE A  67     5109   6268   7391     13   -104   -326  A    C  
ATOM    440  C   ILE A  67      39.453  -8.690 -14.122  1.00 51.53      A    C  
ANISOU  440  C   ILE A  67     5385   6584   7608     -2    -66   -194  A    C  
ATOM    441  O   ILE A  67      40.138  -7.711 -13.812  1.00 44.36      A    O  
ANISOU  441  O   ILE A  67     4505   5677   6673     40    -16   -122  A    O  
ATOM    442  CB  ILE A  67      39.470  -9.692 -16.434  1.00 48.60      A    C  
ANISOU  442  CB  ILE A  67     4971   6312   7184     51    -97   -415  A    C  
ATOM    443  CG1 ILE A  67      40.218 -10.650 -17.357  1.00 48.48      A    C  
ANISOU  443  CG1 ILE A  67     4963   6256   7201     87   -118   -555  A    C  
ATOM    444  CG2 ILE A  67      39.568  -8.259 -16.948  1.00 38.49      A    C  
ANISOU  444  CG2 ILE A  67     3685   5162   5779    126    -26   -351  A    C  
ATOM    445  CD1 ILE A  67      39.615 -10.752 -18.748  1.00 51.87      A    C  
ANISOU  445  CD1 ILE A  67     5369   6819   7520    109   -126   -660  A    C  
ATOM    446  N   LYS A  68      38.198  -8.842 -13.705  1.00 45.10      A    N  
ANISOU  446  N   LYS A  68     4546   5811   6779    -66    -87   -168  A    N  
ATOM    447  CA  LYS A  68      37.558  -7.812 -12.885  1.00 47.95      A    C  
ANISOU  447  CA  LYS A  68     4909   6227   7083    -63    -45    -58  A    C  
ATOM    448  C   LYS A  68      38.370  -7.609 -11.607  1.00 47.11      A    C  
ANISOU  448  C   LYS A  68     4871   5993   7036    -85    -32     28  A    C  
ATOM    449  O   LYS A  68      38.651  -6.483 -11.215  1.00 46.91      A    O  
ANISOU  449  O   LYS A  68     4884   5982   6957    -38     16    102  A    O  
ATOM    450  CB  LYS A  68      36.104  -8.178 -12.560  1.00 41.00      A    C  
ANISOU  450  CB  LYS A  68     3966   5423   6187   -136    -66    -50  A    C  
ATOM    451  CG  LYS A  68      35.467  -7.332 -11.466  1.00 49.59      A    C  
ANISOU  451  CG  LYS A  68     5057   6552   7234   -136    -18     56  A    C  
ATOM    452  CD  LYS A  68      34.210  -7.989 -10.880  1.00 58.74      A    C  
ANISOU  452  CD  LYS A  68     6145   7767   8406   -244    -35     66  A    C  
ATOM    453  CE  LYS A  68      34.563  -9.250 -10.084  1.00 62.07      A    C  
ANISOU  453  CE  LYS A  68     6618   8028   8937   -379    -82     68  A    C  
ATOM    454  NZ  LYS A  68      33.399  -9.853  -9.375  1.00 60.85      A    N1+
ANISOU  454  NZ  LYS A  68     6408   7922   8790   -513    -87     97  A    N1+
ATOM    455  N   ILE A  69      38.773  -8.713 -10.986  1.00 43.83      A    N  
ANISOU  455  N   ILE A  69     4483   5444   6727   -155    -85     16  A    N  
ATOM    456  CA  ILE A  69      39.580  -8.673  -9.768  1.00 41.50      A    C  
ANISOU  456  CA  ILE A  69     4254   5025   6488   -179    -94     94  A    C  
ATOM    457  C   ILE A  69      41.002  -8.106  -9.964  1.00 46.43      A    C  
ANISOU  457  C   ILE A  69     4899   5619   7125   -108    -77     98  A    C  
ATOM    458  O   ILE A  69      41.456  -7.270  -9.176  1.00 45.94      A    O  
ANISOU  458  O   ILE A  69     4880   5533   7041   -105    -53    181  A    O  
ATOM    459  CB  ILE A  69      39.586 -10.035  -9.070  1.00 46.05      A    C  
ANISOU  459  CB  ILE A  69     4866   5462   7168   -270   -166     89  A    C  
ATOM    460  CG1 ILE A  69      38.166 -10.325  -8.532  1.00 37.54      A    C  
ANISOU  460  CG1 ILE A  69     3771   4431   6061   -375   -164    125  A    C  
ATOM    461  CG2 ILE A  69      40.592 -10.034  -7.934  1.00 39.58      A    C  
ANISOU  461  CG2 ILE A  69     4117   4517   6405   -278   -193    165  A    C  
ATOM    462  CD1 ILE A  69      37.857 -11.775  -8.292  1.00 35.40      A    C  
ANISOU  462  CD1 ILE A  69     3530   4047   5874   -487   -237     96  A    C  
ATOM    463  N   LEU A  70      41.694  -8.541 -11.015  1.00 50.83      A    N  
ANISOU  463  N   LEU A  70     5420   6182   7710    -55    -85      7  A    N  
ATOM    464  CA  LEU A  70      43.002  -7.973 -11.365  1.00 43.34      A    C  
ANISOU  464  CA  LEU A  70     4461   5245   6762      8    -54      3  A    C  
ATOM    465  C   LEU A  70      42.909  -6.457 -11.623  1.00 48.27      A    C  
ANISOU  465  C   LEU A  70     5100   5972   7269     35     19     65  A    C  
ATOM    466  O   LEU A  70      43.796  -5.702 -11.251  1.00 46.36      A    O  
ANISOU  466  O   LEU A  70     4881   5713   7019     36     44    121  A    O  
ATOM    467  CB  LEU A  70      43.572  -8.672 -12.600  1.00 48.09      A    C  
ANISOU  467  CB  LEU A  70     5012   5872   7387     67    -57   -120  A    C  
ATOM    468  CG  LEU A  70      44.556  -9.851 -12.465  1.00 58.22      A    C  
ANISOU  468  CG  LEU A  70     6285   7040   8796     96   -116   -185  A    C  
ATOM    469  CD1 LEU A  70      44.696 -10.357 -11.049  1.00 52.26      A    C  
ANISOU  469  CD1 LEU A  70     5583   6141   8132     45   -186   -109  A    C  
ATOM    470  CD2 LEU A  70      44.165 -10.990 -13.411  1.00 41.61      A    C  
ANISOU  470  CD2 LEU A  70     4173   4922   6715    119   -148   -319  A    C  
ATOM    471  N   GLN A  71      41.832  -6.003 -12.254  1.00 48.62      A    N  
ANISOU  471  N   GLN A  71     5136   6117   7220     55     49     58  A    N  
ATOM    472  CA  GLN A  71      41.688  -4.574 -12.502  1.00 48.55      A    C  
ANISOU  472  CA  GLN A  71     5165   6185   7098     95    111    121  A    C  
ATOM    473  C   GLN A  71      41.443  -3.761 -11.230  1.00 49.83      A    C  
ANISOU  473  C   GLN A  71     5398   6294   7239     70    123    225  A    C  
ATOM    474  O   GLN A  71      41.787  -2.585 -11.170  1.00 45.04      A    O  
ANISOU  474  O   GLN A  71     4854   5693   6565     91    165    284  A    O  
ATOM    475  CB  GLN A  71      40.566  -4.321 -13.491  1.00 37.08      A    C  
ANISOU  475  CB  GLN A  71     3684   4857   5548    143    124     89  A    C  
ATOM    476  CG  GLN A  71      40.944  -4.645 -14.923  1.00 44.83      A    C  
ANISOU  476  CG  GLN A  71     4625   5913   6496    182    132     -3  A    C  
ATOM    477  CD  GLN A  71      39.715  -4.768 -15.794  1.00 55.74      A    C  
ANISOU  477  CD  GLN A  71     5967   7413   7799    212    112    -51  A    C  
ATOM    478  NE2 GLN A  71      38.545  -4.900 -15.164  1.00 61.29      A    N  
ANISOU  478  NE2 GLN A  71     6646   8133   8507    188     84    -24  A    N  
ATOM    479  OE1 GLN A  71      39.811  -4.757 -17.013  1.00 59.41      A    O  
ANISOU  479  OE1 GLN A  71     6416   7965   8192    254    123   -111  A    O  
ATOM    480  N   LEU A  72      40.838  -4.396 -10.229  1.00 43.14      A    N  
ANISOU  480  N   LEU A  72     4553   5395   6444     18     88    243  A    N  
ATOM    481  CA  LEU A  72      40.563  -3.755  -8.956  1.00 39.36      A    C  
ANISOU  481  CA  LEU A  72     4145   4871   5939     -7    103    331  A    C  
ATOM    482  C   LEU A  72      41.820  -3.646  -8.099  1.00 45.91      A    C  
ANISOU  482  C   LEU A  72     5031   5592   6822    -51     80    375  A    C  
ATOM    483  O   LEU A  72      42.066  -2.599  -7.498  1.00 46.17      A    O  
ANISOU  483  O   LEU A  72     5144   5600   6798    -52    107    439  A    O  
ATOM    484  CB  LEU A  72      39.495  -4.543  -8.184  1.00 44.70      A    C  
ANISOU  484  CB  LEU A  72     4797   5544   6641    -64     80    338  A    C  
ATOM    485  CG  LEU A  72      39.226  -4.030  -6.760  1.00 48.83      A    C  
ANISOU  485  CG  LEU A  72     5397   6025   7133    -98    100    422  A    C  
ATOM    486  CD1 LEU A  72      38.560  -2.632  -6.776  1.00 35.55      A    C  
ANISOU  486  CD1 LEU A  72     3756   4420   5333    -14    168    459  A    C  
ATOM    487  CD2 LEU A  72      38.378  -5.017  -5.978  1.00 42.13      A    C  
ANISOU  487  CD2 LEU A  72     4521   5169   6319   -182     78    434  A    C  
ATOM    488  N   LEU A  73      42.607  -4.728  -8.052  1.00 39.18      A    N  
ANISOU  488  N   LEU A  73     4141   4674   6074    -81     23    337  A    N  
ATOM    489  CA  LEU A  73      43.738  -4.838  -7.136  1.00 45.22      A    C  
ANISOU  489  CA  LEU A  73     4939   5342   6900   -121    -22    379  A    C  
ATOM    490  C   LEU A  73      45.033  -4.192  -7.659  1.00 50.58      A    C  
ANISOU  490  C   LEU A  73     5597   6042   7579   -100     -4    374  A    C  
ATOM    491  O   LEU A  73      45.681  -4.728  -8.554  1.00 52.54      A    O  
ANISOU  491  O   LEU A  73     5766   6320   7876    -64     -8    305  A    O  
ATOM    492  CB  LEU A  73      43.982  -6.309  -6.798  1.00 46.94      A    C  
ANISOU  492  CB  LEU A  73     5130   5472   7233   -146    -99    349  A    C  
ATOM    493  CG  LEU A  73      42.774  -7.015  -6.183  1.00 47.59      A    C  
ANISOU  493  CG  LEU A  73     5239   5526   7317   -203   -119    368  A    C  
ATOM    494  CD1 LEU A  73      43.086  -8.486  -5.810  1.00 37.98      A    C  
ANISOU  494  CD1 LEU A  73     4029   4189   6214   -238   -206    348  A    C  
ATOM    495  CD2 LEU A  73      42.286  -6.222  -4.972  1.00 36.28      A    C  
ANISOU  495  CD2 LEU A  73     3885   4088   5810   -246    -92    460  A    C  
ATOM    496  N   LYS A  74      45.406  -3.045  -7.101  1.00 44.35      A    N  
ANISOU  496  N   LYS A  74     4880   5242   6731   -129     18    442  A    N  
ATOM    497  CA  LYS A  74      46.672  -2.395  -7.469  1.00 47.45      A    C  
ANISOU  497  CA  LYS A  74     5252   5656   7120   -144     33    449  A    C  
ATOM    498  C   LYS A  74      47.553  -2.150  -6.251  1.00 47.99      A    C  
ANISOU  498  C   LYS A  74     5363   5652   7219   -214    -24    510  A    C  
ATOM    499  O   LYS A  74      47.307  -1.236  -5.473  1.00 55.50      A    O  
ANISOU  499  O   LYS A  74     6424   6565   8098   -255    -14    571  A    O  
ATOM    500  CB  LYS A  74      46.426  -1.089  -8.215  1.00 39.49      A    C  
ANISOU  500  CB  LYS A  74     4298   4709   5997   -130    111    470  A    C  
ATOM    501  CG  LYS A  74      45.575  -1.277  -9.455  1.00 52.29      A    C  
ANISOU  501  CG  LYS A  74     5877   6416   7573    -57    155    414  A    C  
ATOM    502  CD  LYS A  74      46.144  -2.401 -10.310  1.00 59.82      A    C  
ANISOU  502  CD  LYS A  74     6711   7413   8606    -30    139    326  A    C  
ATOM    503  CE  LYS A  74      45.296  -2.661 -11.540  1.00 60.82      A    C  
ANISOU  503  CE  LYS A  74     6802   7628   8681     33    171    260  A    C  
ATOM    504  NZ  LYS A  74      46.100  -3.368 -12.567  1.00 54.71      A    N1+
ANISOU  504  NZ  LYS A  74     5933   6910   7944     63    181    172  A    N1+
ATOM    505  N   HIS A  75      48.591  -2.964  -6.096  1.00 43.97      A    N  
ANISOU  505  N   HIS A  75     4769   5126   6812   -219    -87    487  A    N  
ATOM    506  CA  HIS A  75      49.368  -2.946  -4.872  1.00 44.06      A    C  
ANISOU  506  CA  HIS A  75     4809   5073   6859   -279   -166    544  A    C  
ATOM    507  C   HIS A  75      50.752  -3.577  -5.092  1.00 55.62      A    C  
ANISOU  507  C   HIS A  75     6141   6564   8427   -262   -221    510  A    C  
ATOM    508  O   HIS A  75      50.889  -4.505  -5.897  1.00 58.25      A    O  
ANISOU  508  O   HIS A  75     6377   6924   8829   -185   -219    436  A    O  
ATOM    509  CB  HIS A  75      48.578  -3.675  -3.787  1.00 37.47      A    C  
ANISOU  509  CB  HIS A  75     4048   4148   6040   -290   -222    578  A    C  
ATOM    510  CG  HIS A  75      49.241  -3.669  -2.451  1.00 52.09      A    C  
ANISOU  510  CG  HIS A  75     5954   5931   7905   -352   -311    643  A    C  
ATOM    511  CD2 HIS A  75      49.117  -2.826  -1.398  1.00 50.92      A    C  
ANISOU  511  CD2 HIS A  75     5927   5746   7673   -421   -321    709  A    C  
ATOM    512  ND1 HIS A  75      50.165  -4.622  -2.078  1.00 54.19      A    N  
ANISOU  512  ND1 HIS A  75     6154   6161   8277   -337   -412    642  A    N  
ATOM    513  CE1 HIS A  75      50.583  -4.364  -0.851  1.00 58.09      A    C  
ANISOU  513  CE1 HIS A  75     6720   6604   8747   -402   -486    710  A    C  
ATOM    514  NE2 HIS A  75      49.963  -3.281  -0.415  1.00 60.83      A    N  
ANISOU  514  NE2 HIS A  75     7184   6950   8977   -460   -430    748  A    N  
ATOM    515  N   GLU A  76      51.776  -3.067  -4.398  1.00 46.98      A    N  
ANISOU  515  N   GLU A  76     5040   5470   7339   -328   -271    557  A    N  
ATOM    516  CA  GLU A  76      53.142  -3.546  -4.609  1.00 52.69      A    C  
ANISOU  516  CA  GLU A  76     5611   6252   8158   -307   -321    527  A    C  
ATOM    517  C   GLU A  76      53.288  -5.065  -4.451  1.00 49.95      A    C  
ANISOU  517  C   GLU A  76     5199   5850   7931   -209   -404    485  A    C  
ATOM    518  O   GLU A  76      54.129  -5.676  -5.097  1.00 52.62      A    O  
ANISOU  518  O   GLU A  76     5395   6247   8350   -133   -414    420  A    O  
ATOM    519  CB  GLU A  76      54.133  -2.824  -3.686  1.00 65.71      A    C  
ANISOU  519  CB  GLU A  76     7263   7908   9795   -408   -387    592  A    C  
ATOM    520  CG  GLU A  76      54.954  -1.748  -4.375  1.00 91.01      A    C  
ANISOU  520  CG  GLU A  76    10402  11223  12955   -485   -320    592  A    C  
ATOM    521  CD  GLU A  76      56.305  -2.252  -4.867  1.00108.04      A    C  
ANISOU  521  CD  GLU A  76    12345  13498  15207   -453   -343    546  A    C  
ATOM    522  OE1 GLU A  76      57.115  -2.702  -4.027  1.00114.20      A    O  
ANISOU  522  OE1 GLU A  76    13056  14274  16060   -456   -457    566  A    O  
ATOM    523  OE2 GLU A  76      56.567  -2.182  -6.091  1.00111.39      A    O1-
ANISOU  523  OE2 GLU A  76    12666  14031  15627   -422   -247    490  A    O1-
ATOM    524  N   ASN A  77      52.468  -5.662  -3.592  1.00 41.34      A    N  
ANISOU  524  N   ASN A  77     4219   4644   6845   -210   -462    521  A    N  
ATOM    525  CA  ASN A  77      52.544  -7.099  -3.330  1.00 46.58      A    C  
ANISOU  525  CA  ASN A  77     4861   5221   7616   -131   -554    496  A    C  
ATOM    526  C   ASN A  77      51.428  -7.914  -3.981  1.00 51.56      A    C  
ANISOU  526  C   ASN A  77     5529   5804   8257    -82   -513    439  A    C  
ATOM    527  O   ASN A  77      51.126  -9.026  -3.561  1.00 54.71      A    O  
ANISOU  527  O   ASN A  77     5974   6092   8721    -54   -587    439  A    O  
ATOM    528  CB  ASN A  77      52.625  -7.365  -1.823  1.00 47.47      A    C  
ANISOU  528  CB  ASN A  77     5072   5231   7735   -182   -670    589  A    C  
ATOM    529  CG  ASN A  77      53.757  -6.582  -1.167  1.00 55.30      A    C  
ANISOU  529  CG  ASN A  77     6024   6275   8711   -240   -727    641  A    C  
ATOM    530  ND2 ASN A  77      54.979  -6.821  -1.623  1.00 53.37      A    N  
ANISOU  530  ND2 ASN A  77     5618   6108   8552   -179   -763    598  A    N  
ATOM    531  OD1 ASN A  77      53.528  -5.744  -0.300  1.00 56.39      A    O  
ANISOU  531  OD1 ASN A  77     6271   6396   8759   -340   -735    710  A    O  
ATOM    532  N   VAL A  78      50.823  -7.351  -5.019  1.00 47.60      A    N  
ANISOU  532  N   VAL A  78     5011   5385   7690    -81   -403    391  A    N  
ATOM    533  CA  VAL A  78      49.857  -8.081  -5.813  1.00 40.84      A    C  
ANISOU  533  CA  VAL A  78     4165   4513   6841    -38   -368    320  A    C  
ATOM    534  C   VAL A  78      50.263  -7.994  -7.265  1.00 44.15      A    C  
ANISOU  534  C   VAL A  78     4475   5042   7258     32   -294    222  A    C  
ATOM    535  O   VAL A  78      50.682  -6.937  -7.742  1.00 47.28      A    O  
ANISOU  535  O   VAL A  78     4832   5546   7587     11   -222    232  A    O  
ATOM    536  CB  VAL A  78      48.440  -7.526  -5.626  1.00 43.01      A    C  
ANISOU  536  CB  VAL A  78     4537   4792   7014   -102   -311    361  A    C  
ATOM    537  CG1 VAL A  78      47.473  -8.230  -6.560  1.00 40.06      A    C  
ANISOU  537  CG1 VAL A  78     4149   4429   6643    -69   -280    281  A    C  
ATOM    538  CG2 VAL A  78      48.009  -7.705  -4.173  1.00 44.69      A    C  
ANISOU  538  CG2 VAL A  78     4856   4904   7219   -173   -374    454  A    C  
ATOM    539  N   VAL A  79      50.179  -9.120  -7.959  1.00 47.67      A    N  
ANISOU  539  N   VAL A  79     4885   5457   7769    111   -311    126  A    N  
ATOM    540  CA  VAL A  79      50.597  -9.184  -9.351  1.00 48.67      A    C  
ANISOU  540  CA  VAL A  79     4914   5691   7889    189   -241     17  A    C  
ATOM    541  C   VAL A  79      49.831  -8.133 -10.129  1.00 51.65      A    C  
ANISOU  541  C   VAL A  79     5311   6177   8135    145   -137     23  A    C  
ATOM    542  O   VAL A  79      48.679  -7.812  -9.812  1.00 52.53      A    O  
ANISOU  542  O   VAL A  79     5510   6262   8185     88   -129     72  A    O  
ATOM    543  CB  VAL A  79      50.382 -10.597  -9.947  1.00 55.66      A    C  
ANISOU  543  CB  VAL A  79     5796   6502   8850    277   -281    -98  A    C  
ATOM    544  CG1 VAL A  79      48.924 -10.824 -10.294  1.00 48.79      A    C  
ANISOU  544  CG1 VAL A  79     5009   5605   7923    228   -264   -119  A    C  
ATOM    545  CG2 VAL A  79      51.259 -10.806 -11.151  1.00 62.55      A    C  
ANISOU  545  CG2 VAL A  79     6551   7479   9736    382   -226   -216  A    C  
ATOM    546  N   ASN A  80      50.497  -7.572 -11.125  1.00 47.38      A    N  
ANISOU  546  N   ASN A  80     4688   5766   7547    173    -59    -19  A    N  
ATOM    547  CA  ASN A  80      49.943  -6.485 -11.902  1.00 43.64      A    C  
ANISOU  547  CA  ASN A  80     4244   5395   6941    138     35     -0  A    C  
ATOM    548  C   ASN A  80      49.588  -6.855 -13.333  1.00 48.73      A    C  
ANISOU  548  C   ASN A  80     4854   6126   7536    203     92   -110  A    C  
ATOM    549  O   ASN A  80      50.456  -7.148 -14.155  1.00 55.83      A    O  
ANISOU  549  O   ASN A  80     5660   7105   8447    261    133   -191  A    O  
ATOM    550  CB  ASN A  80      50.907  -5.308 -11.927  1.00 44.08      A    C  
ANISOU  550  CB  ASN A  80     4264   5538   6948     85     91     62  A    C  
ATOM    551  CG  ASN A  80      50.377  -4.150 -12.750  1.00 49.67      A    C  
ANISOU  551  CG  ASN A  80     5026   6333   7513     51    184     92  A    C  
ATOM    552  ND2 ASN A  80      51.119  -3.767 -13.781  1.00 44.81      A    N  
ANISOU  552  ND2 ASN A  80     4339   5842   6845     56    263     59  A    N  
ATOM    553  OD1 ASN A  80      49.304  -3.615 -12.468  1.00 55.62      A    O  
ANISOU  553  OD1 ASN A  80     5887   7048   8200     26    184    146  A    O  
ATOM    554  N   LEU A  81      48.298  -6.820 -13.623  1.00 50.47      A    N  
ANISOU  554  N   LEU A  81     5143   6343   7690    191     97   -114  A    N  
ATOM    555  CA  LEU A  81      47.805  -6.996 -14.972  1.00 52.67      A    C  
ANISOU  555  CA  LEU A  81     5406   6715   7891    238    144   -205  A    C  
ATOM    556  C   LEU A  81      48.065  -5.700 -15.723  1.00 56.04      A    C  
ANISOU  556  C   LEU A  81     5834   7270   8188    222    238   -160  A    C  
ATOM    557  O   LEU A  81      47.574  -4.643 -15.335  1.00 55.45      A    O  
ANISOU  557  O   LEU A  81     5831   7194   8042    173    255    -58  A    O  
ATOM    558  CB  LEU A  81      46.308  -7.317 -14.945  1.00 42.11      A    C  
ANISOU  558  CB  LEU A  81     4131   5345   6524    218    105   -212  A    C  
ATOM    559  CG  LEU A  81      45.605  -7.477 -16.289  1.00 46.28      A    C  
ANISOU  559  CG  LEU A  81     4651   5975   6958    254    133   -302  A    C  
ATOM    560  CD1 LEU A  81      46.058  -8.769 -17.010  1.00 40.03      A    C  
ANISOU  560  CD1 LEU A  81     3816   5164   6228    314    111   -452  A    C  
ATOM    561  CD2 LEU A  81      44.079  -7.465 -16.085  1.00 39.20      A    C  
ANISOU  561  CD2 LEU A  81     3798   5076   6019    216     96   -276  A    C  
ATOM    562  N   ILE A  82      48.859  -5.769 -16.783  1.00 55.75      A    N  
ANISOU  562  N   ILE A  82     5726   7341   8115    262    302   -233  A    N  
ATOM    563  CA  ILE A  82      49.193  -4.569 -17.530  1.00 51.19      A    C  
ANISOU  563  CA  ILE A  82     5158   6885   7408    231    395   -181  A    C  
ATOM    564  C   ILE A  82      48.060  -4.180 -18.461  1.00 52.54      A    C  
ANISOU  564  C   ILE A  82     5399   7122   7441    250    419   -188  A    C  
ATOM    565  O   ILE A  82      47.648  -3.030 -18.500  1.00 54.10      A    O  
ANISOU  565  O   ILE A  82     5676   7342   7536    213    449    -90  A    O  
ATOM    566  CB  ILE A  82      50.482  -4.741 -18.339  1.00 50.86      A    C  
ANISOU  566  CB  ILE A  82     5005   6960   7361    259    469   -253  A    C  
ATOM    567  CG1 ILE A  82      51.674  -4.877 -17.393  1.00 49.09      A    C  
ANISOU  567  CG1 ILE A  82     4695   6698   7261    236    444   -224  A    C  
ATOM    568  CG2 ILE A  82      50.674  -3.559 -19.271  1.00 36.69      A    C  
ANISOU  568  CG2 ILE A  82     3237   5296   5407    212    572   -198  A    C  
ATOM    569  CD1 ILE A  82      52.836  -5.609 -18.007  1.00 53.32      A    C  
ANISOU  569  CD1 ILE A  82     5084   7328   7847    310    486   -335  A    C  
ATOM    570  N   GLU A  83      47.557  -5.151 -19.209  1.00 57.52      A    N  
ANISOU  570  N   GLU A  83     6007   7780   8067    310    397   -308  A    N  
ATOM    571  CA  GLU A  83      46.512  -4.897 -20.188  1.00 45.51      A    C  
ANISOU  571  CA  GLU A  83     4537   6343   6412    333    406   -329  A    C  
ATOM    572  C   GLU A  83      46.021  -6.223 -20.726  1.00 52.97      A    C  
ANISOU  572  C   GLU A  83     5454   7281   7390    380    354   -475  A    C  
ATOM    573  O   GLU A  83      46.581  -7.284 -20.415  1.00 55.53      A    O  
ANISOU  573  O   GLU A  83     5732   7529   7837    405    322   -560  A    O  
ATOM    574  CB  GLU A  83      47.054  -4.068 -21.354  1.00 44.59      A    C  
ANISOU  574  CB  GLU A  83     4427   6371   6145    337    505   -318  A    C  
ATOM    575  CG  GLU A  83      48.045  -4.842 -22.245  1.00 52.77      A    C  
ANISOU  575  CG  GLU A  83     5373   7494   7183    382    561   -449  A    C  
ATOM    576  CD  GLU A  83      48.576  -4.006 -23.411  1.00 62.71      A    C  
ANISOU  576  CD  GLU A  83     6640   8913   8274    371    671   -430  A    C  
ATOM    577  OE1 GLU A  83      47.839  -3.135 -23.912  1.00 71.99      A    O  
ANISOU  577  OE1 GLU A  83     7908  10138   9308    354    682   -354  A    O  
ATOM    578  OE2 GLU A  83      49.732  -4.226 -23.835  1.00 60.71      A    O1-
ANISOU  578  OE2 GLU A  83     6298   8743   8025    380    749   -489  A    O1-
ATOM    579  N   ILE A  84      44.978  -6.153 -21.545  1.00 57.51      A    N  
ANISOU  579  N   ILE A  84     6065   7932   7852    395    338   -507  A    N  
ATOM    580  CA  ILE A  84      44.470  -7.317 -22.260  1.00 53.09      A    C  
ANISOU  580  CA  ILE A  84     5493   7387   7293    426    288   -655  A    C  
ATOM    581  C   ILE A  84      44.657  -7.144 -23.765  1.00 52.46      A    C  
ANISOU  581  C   ILE A  84     5416   7463   7055    470    349   -733  A    C  
ATOM    582  O   ILE A  84      44.355  -6.090 -24.319  1.00 58.16      A    O  
ANISOU  582  O   ILE A  84     6177   8290   7632    467    389   -654  A    O  
ATOM    583  CB  ILE A  84      42.998  -7.578 -21.894  1.00 49.67      A    C  
ANISOU  583  CB  ILE A  84     5084   6919   6868    388    197   -641  A    C  
ATOM    584  CG1 ILE A  84      42.945  -8.131 -20.474  1.00 45.42      A    C  
ANISOU  584  CG1 ILE A  84     4542   6220   6495    340    140   -599  A    C  
ATOM    585  CG2 ILE A  84      42.349  -8.537 -22.890  1.00 48.63      A    C  
ANISOU  585  CG2 ILE A  84     4952   6837   6689    400    146   -790  A    C  
ATOM    586  CD1 ILE A  84      41.912  -7.487 -19.627  1.00 51.80      A    C  
ANISOU  586  CD1 ILE A  84     5372   7015   7296    294    111   -481  A    C  
ATOM    587  N   CYS A  85      45.179  -8.175 -24.421  1.00 52.43      A    N  
ANISOU  587  N   CYS A  85     5383   7469   7070    517    357   -890  A    N  
ATOM    588  CA  CYS A  85      45.506  -8.063 -25.831  1.00 50.48      A    C  
ANISOU  588  CA  CYS A  85     5139   7377   6663    562    429   -976  A    C  
ATOM    589  C   CYS A  85      44.740  -9.071 -26.666  1.00 57.17      A    C  
ANISOU  589  C   CYS A  85     6015   8244   7460    586    362  -1136  A    C  
ATOM    590  O   CYS A  85      44.404 -10.163 -26.202  1.00 62.14      A    O  
ANISOU  590  O   CYS A  85     6650   8745   8216    579    277  -1222  A    O  
ATOM    591  CB  CYS A  85      47.020  -8.199 -26.046  1.00 64.22      A    C  
ANISOU  591  CB  CYS A  85     6810   9158   8432    608    530  -1028  A    C  
ATOM    592  SG  CYS A  85      47.980  -6.697 -25.589  1.00 61.02      A    S  
ANISOU  592  SG  CYS A  85     6376   8810   7998    551    635   -840  A    S  
ATOM    593  N   ARG A  86      44.451  -8.682 -27.901  1.00 58.33      A    N  
ANISOU  593  N   ARG A  86     6197   8551   7417    605    395  -1172  A    N  
ATOM    594  CA  ARG A  86      43.722  -9.527 -28.834  1.00 56.67      A    C  
ANISOU  594  CA  ARG A  86     6023   8385   7124    618    330  -1328  A    C  
ATOM    595  C   ARG A  86      44.662 -10.084 -29.894  1.00 66.52      A    C  
ANISOU  595  C   ARG A  86     7268   9716   8291    691    413  -1491  A    C  
ATOM    596  O   ARG A  86      45.875  -9.878 -29.852  1.00 57.89      A    O  
ANISOU  596  O   ARG A  86     6125   8649   7223    731    521  -1482  A    O  
ATOM    597  CB  ARG A  86      42.636  -8.714 -29.542  1.00 49.23      A    C  
ANISOU  597  CB  ARG A  86     5124   7583   5998    597    293  -1260  A    C  
ATOM    598  CG  ARG A  86      43.209  -7.569 -30.361  1.00 55.98      A    C  
ANISOU  598  CG  ARG A  86     6007   8594   6670    623    404  -1177  A    C  
ATOM    599  CD  ARG A  86      42.151  -6.718 -31.031  1.00 68.52      A    C  
ANISOU  599  CD  ARG A  86     7652  10309   8074    620    356  -1094  A    C  
ATOM    600  NE  ARG A  86      42.669  -5.379 -31.317  1.00 81.50      A    N  
ANISOU  600  NE  ARG A  86     9342  12036   9591    624    454   -941  A    N  
ATOM    601  CZ  ARG A  86      42.936  -4.903 -32.532  1.00 87.75      A    C  
ANISOU  601  CZ  ARG A  86    10190  12983  10168    644    518   -945  A    C  
ATOM    602  NH1 ARG A  86      42.727  -5.656 -33.603  1.00 89.14      A    N1+
ANISOU  602  NH1 ARG A  86    10382  13262  10225    671    496  -1104  A    N1+
ATOM    603  NH2 ARG A  86      43.404  -3.666 -32.676  1.00 87.75      A    N  
ANISOU  603  NH2 ARG A  86    10245  13031  10064    627    605   -787  A    N  
ATOM    604  N   THR A  87      44.058 -10.762 -30.861  1.00 79.84      A    N  
ANISOU  604  N   THR A  87     9005  11458   9873    704    360  -1640  A    N  
ATOM    605  CA  THR A  87      44.739 -11.357 -31.986  1.00 84.69      A    C  
ANISOU  605  CA  THR A  87     9638  12161  10380    778    428  -1821  A    C  
ATOM    606  C   THR A  87      43.634 -12.063 -32.726  1.00 96.49      A    C  
ANISOU  606  C   THR A  87    11205  13675  11782    752    313  -1955  A    C  
ATOM    607  O   THR A  87      43.373 -11.805 -33.899  1.00109.37      A    O  
ANISOU  607  O   THR A  87    12882  15472  13200    764    330  -2009  A    O  
ATOM    608  CB  THR A  87      45.678 -12.441 -31.526  1.00 89.76      A    C  
ANISOU  608  CB  THR A  87    10246  12661  11196    847    447  -1950  A    C  
ATOM    609  CG2 THR A  87      44.893 -13.713 -31.249  1.00 73.33      A    C  
ANISOU  609  CG2 THR A  87     8226  10408   9226    824    305  -2080  A    C  
ATOM    610  OG1 THR A  87      46.647 -12.691 -32.550  1.00109.33      A    O  
ANISOU  610  OG1 THR A  87    12714  15264  13562    941    565  -2092  A    O  
ATOM    611  N   SER A  98      41.602 -14.845 -30.447  1.00 92.62      A    N  
ANISOU  611  N   SER A  98    10772  12648  11772    563    -59  -2085  A    N  
ATOM    612  CA  SER A  98      41.965 -15.105 -29.053  1.00 90.12      A    C  
ANISOU  612  CA  SER A  98    10428  12139  11676    547    -70  -1996  A    C  
ATOM    613  C   SER A  98      42.165 -13.853 -28.192  1.00 81.23      A    C  
ANISOU  613  C   SER A  98     9227  11055  10581    537     -8  -1771  A    C  
ATOM    614  O   SER A  98      42.045 -12.722 -28.664  1.00 88.42      A    O  
ANISOU  614  O   SER A  98    10113  12135  11347    547     50  -1675  A    O  
ATOM    615  CB  SER A  98      43.222 -15.968 -28.984  1.00 93.03      A    C  
ANISOU  615  CB  SER A  98    10817  12378  12150    655    -22  -2122  A    C  
ATOM    616  OG  SER A  98      42.958 -17.267 -29.474  1.00106.12      A    O  
ANISOU  616  OG  SER A  98    12572  13925  13825    655   -103  -2326  A    O  
ATOM    617  N   ILE A  99      42.479 -14.086 -26.922  1.00 63.07      A    N  
ANISOU  617  N   ILE A  99     6910   8589   8465    518    -25  -1691  A    N  
ATOM    618  CA  ILE A  99      42.683 -13.028 -25.945  1.00 57.43      A    C  
ANISOU  618  CA  ILE A  99     6141   7881   7800    501     20  -1491  A    C  
ATOM    619  C   ILE A  99      43.812 -13.412 -24.986  1.00 57.43      A    C  
ANISOU  619  C   ILE A  99     6121   7730   7972    546     46  -1471  A    C  
ATOM    620  O   ILE A  99      43.984 -14.585 -24.647  1.00 62.21      A    O  
ANISOU  620  O   ILE A  99     6765   8170   8702    558    -16  -1568  A    O  
ATOM    621  CB  ILE A  99      41.379 -12.753 -25.160  1.00 59.27      A    C  
ANISOU  621  CB  ILE A  99     6368   8089   8063    392    -63  -1374  A    C  
ATOM    622  CG1 ILE A  99      40.415 -11.950 -26.027  1.00 63.90      A    C  
ANISOU  622  CG1 ILE A  99     6944   8868   8467    375    -71  -1343  A    C  
ATOM    623  CG2 ILE A  99      41.653 -12.024 -23.851  1.00 48.82      A    C  
ANISOU  623  CG2 ILE A  99     5014   6698   6838    372    -34  -1195  A    C  
ATOM    624  CD1 ILE A  99      41.012 -10.678 -26.579  1.00 59.60      A    C  
ANISOU  624  CD1 ILE A  99     6389   8469   7788    444     34  -1256  A    C  
ATOM    625  N   TYR A 100      44.586 -12.422 -24.556  1.00 52.35      A    N  
ANISOU  625  N   TYR A 100     5423   7139   7330    570    130  -1342  A    N  
ATOM    626  CA  TYR A 100      45.704 -12.673 -23.664  1.00 54.85      A    C  
ANISOU  626  CA  TYR A 100     5701   7343   7797    615    149  -1313  A    C  
ATOM    627  C   TYR A 100      45.659 -11.706 -22.502  1.00 56.19      A    C  
ANISOU  627  C   TYR A 100     5848   7486   8015    550    153  -1117  A    C  
ATOM    628  O   TYR A 100      45.439 -10.501 -22.690  1.00 55.90      A    O  
ANISOU  628  O   TYR A 100     5803   7570   7866    520    208  -1010  A    O  
ATOM    629  CB  TYR A 100      47.047 -12.454 -24.381  1.00 59.98      A    C  
ANISOU  629  CB  TYR A 100     6286   8105   8399    717    264  -1375  A    C  
ATOM    630  CG  TYR A 100      47.384 -13.412 -25.496  1.00 60.35      A    C  
ANISOU  630  CG  TYR A 100     6349   8181   8399    811    282  -1584  A    C  
ATOM    631  CD1 TYR A 100      48.253 -14.472 -25.283  1.00 65.33      A    C  
ANISOU  631  CD1 TYR A 100     6965   8696   9161    915    268  -1702  A    C  
ATOM    632  CD2 TYR A 100      46.859 -13.239 -26.767  1.00 64.40      A    C  
ANISOU  632  CD2 TYR A 100     6898   8841   8731    810    313  -1666  A    C  
ATOM    633  CE1 TYR A 100      48.581 -15.343 -26.297  1.00 64.26      A    C  
ANISOU  633  CE1 TYR A 100     6855   8581   8979   1019    292  -1907  A    C  
ATOM    634  CE2 TYR A 100      47.184 -14.110 -27.796  1.00 70.73      A    C  
ANISOU  634  CE2 TYR A 100     7726   9674   9475    898    335  -1870  A    C  
ATOM    635  CZ  TYR A 100      48.047 -15.160 -27.556  1.00 69.65      A    C  
ANISOU  635  CZ  TYR A 100     7579   9412   9473   1006    328  -1995  A    C  
ATOM    636  OH  TYR A 100      48.373 -16.035 -28.575  1.00 78.56      A    O  
ANISOU  636  OH  TYR A 100     8746  10561  10541   1111    353  -2211  A    O  
ATOM    637  N   LEU A 101      45.895 -12.224 -21.303  1.00 50.06      A    N  
ANISOU  637  N   LEU A 101     5078   6546   7397    535     94  -1073  A    N  
ATOM    638  CA  LEU A 101      46.138 -11.357 -20.170  1.00 48.30      A    C  
ANISOU  638  CA  LEU A 101     4835   6296   7222    487    105   -905  A    C  
ATOM    639  C   LEU A 101      47.630 -11.070 -20.148  1.00 56.25      A    C  
ANISOU  639  C   LEU A 101     5765   7345   8262    555    176   -900  A    C  
ATOM    640  O   LEU A 101      48.439 -11.995 -20.208  1.00 47.71      A    O  
ANISOU  640  O   LEU A 101     4653   6202   7271    638    162  -1003  A    O  
ATOM    641  CB  LEU A 101      45.683 -12.020 -18.866  1.00 55.71      A    C  
ANISOU  641  CB  LEU A 101     5819   7051   8297    428      6   -850  A    C  
ATOM    642  CG  LEU A 101      44.189 -11.871 -18.538  1.00 51.17      A    C  
ANISOU  642  CG  LEU A 101     5290   6471   7683    327    -44   -789  A    C  
ATOM    643  CD1 LEU A 101      43.358 -12.531 -19.597  1.00 42.49      A    C  
ANISOU  643  CD1 LEU A 101     4213   5414   6518    318    -76   -918  A    C  
ATOM    644  CD2 LEU A 101      43.878 -12.464 -17.184  1.00 49.45      A    C  
ANISOU  644  CD2 LEU A 101     5115   6084   7589    257   -123   -719  A    C  
ATOM    645  N   VAL A 102      47.998  -9.792 -20.093  1.00 54.64      A    N  
ANISOU  645  N   VAL A 102     5531   7247   7983    521    251   -784  A    N  
ATOM    646  CA  VAL A 102      49.408  -9.427 -20.033  1.00 52.92      A    C  
ANISOU  646  CA  VAL A 102     5224   7091   7794    556    319   -767  A    C  
ATOM    647  C   VAL A 102      49.849  -9.016 -18.625  1.00 54.16      A    C  
ANISOU  647  C   VAL A 102     5368   7157   8053    502    279   -634  A    C  
ATOM    648  O   VAL A 102      49.340  -8.039 -18.087  1.00 59.43      A    O  
ANISOU  648  O   VAL A 102     6087   7820   8671    419    280   -507  A    O  
ATOM    649  CB  VAL A 102      49.741  -8.294 -21.022  1.00 49.09      A    C  
ANISOU  649  CB  VAL A 102     4712   6794   7147    536    438   -736  A    C  
ATOM    650  CG1 VAL A 102      51.250  -8.115 -21.113  1.00 44.64      A    C  
ANISOU  650  CG1 VAL A 102     4030   6319   6614    566    516   -747  A    C  
ATOM    651  CG2 VAL A 102      49.160  -8.608 -22.384  1.00 45.02      A    C  
ANISOU  651  CG2 VAL A 102     4229   6375   6503    579    468   -852  A    C  
ATOM    652  N   PHE A 103      50.802  -9.750 -18.044  1.00 50.73      A    N  
ANISOU  652  N   PHE A 103     4871   6651   7753    560    239   -669  A    N  
ATOM    653  CA  PHE A 103      51.371  -9.391 -16.738  1.00 53.71      A    C  
ANISOU  653  CA  PHE A 103     5228   6958   8221    513    194   -549  A    C  
ATOM    654  C   PHE A 103      52.856  -9.013 -16.788  1.00 59.19      A    C  
ANISOU  654  C   PHE A 103     5786   7763   8940    540    250   -545  A    C  
ATOM    655  O   PHE A 103      53.628  -9.578 -17.570  1.00 58.16      A    O  
ANISOU  655  O   PHE A 103     5558   7715   8825    641    296   -663  A    O  
ATOM    656  CB  PHE A 103      51.255 -10.552 -15.753  1.00 56.13      A    C  
ANISOU  656  CB  PHE A 103     5575   7077   8674    547     71   -565  A    C  
ATOM    657  CG  PHE A 103      49.871 -11.121 -15.615  1.00 53.03      A    C  
ANISOU  657  CG  PHE A 103     5300   6572   8277    507      9   -575  A    C  
ATOM    658  CD1 PHE A 103      49.054 -10.734 -14.566  1.00 48.09      A    C  
ANISOU  658  CD1 PHE A 103     4754   5867   7652    406    -39   -453  A    C  
ATOM    659  CD2 PHE A 103      49.406 -12.076 -16.505  1.00 54.23      A    C  
ANISOU  659  CD2 PHE A 103     5482   6701   8423    562     -4   -715  A    C  
ATOM    660  CE1 PHE A 103      47.786 -11.278 -14.415  1.00 54.71      A    C  
ANISOU  660  CE1 PHE A 103     5678   6622   8488    356    -92   -461  A    C  
ATOM    661  CE2 PHE A 103      48.133 -12.620 -16.362  1.00 63.76      A    C  
ANISOU  661  CE2 PHE A 103     6786   7812   9629    500    -68   -725  A    C  
ATOM    662  CZ  PHE A 103      47.326 -12.226 -15.313  1.00 58.20      A    C  
ANISOU  662  CZ  PHE A 103     6139   7045   8929    394   -108   -594  A    C  
ATOM    663  N   ASP A 104      53.260  -8.082 -15.925  1.00 63.65      A    N  
ANISOU  663  N   ASP A 104     6341   8334   9510    449    244   -413  A    N  
ATOM    664  CA  ASP A 104      54.679  -7.872 -15.625  1.00 63.46      A    C  
ANISOU  664  CA  ASP A 104     6176   8391   9545    455    259   -395  A    C  
ATOM    665  C   ASP A 104      55.309  -9.237 -15.324  1.00 63.50      A    C  
ANISOU  665  C   ASP A 104     6106   8322   9698    594    179   -491  A    C  
ATOM    666  O   ASP A 104      54.771 -10.007 -14.531  1.00 70.33      A    O  
ANISOU  666  O   ASP A 104     7059   9013  10648    618     69   -482  A    O  
ATOM    667  CB  ASP A 104      54.837  -6.941 -14.414  1.00 73.14      A    C  
ANISOU  667  CB  ASP A 104     7438   9571  10780    331    214   -243  A    C  
ATOM    668  CG  ASP A 104      54.731  -5.445 -14.777  1.00 85.78      A    C  
ANISOU  668  CG  ASP A 104     9083  11270  12241    204    307   -151  A    C  
ATOM    669  OD1 ASP A 104      55.308  -5.026 -15.805  1.00 90.93      A    O  
ANISOU  669  OD1 ASP A 104     9654  12079  12817    196    413   -186  A    O  
ATOM    670  OD2 ASP A 104      54.091  -4.680 -14.014  1.00 81.50      A    O1-
ANISOU  670  OD2 ASP A 104     8664  10643  11661    110    275    -44  A    O1-
ATOM    671  N   PHE A 105      56.435  -9.551 -15.958  1.00 64.40      A    N  
ANISOU  671  N   PHE A 105     6062   8567   9841    691    235   -584  A    N  
ATOM    672  CA  PHE A 105      57.072 -10.865 -15.786  1.00 64.85      A    C  
ANISOU  672  CA  PHE A 105     6048   8556  10036    858    163   -691  A    C  
ATOM    673  C   PHE A 105      57.771 -11.034 -14.430  1.00 72.43      A    C  
ANISOU  673  C   PHE A 105     6959   9435  11125    864     43   -605  A    C  
ATOM    674  O   PHE A 105      58.377 -10.093 -13.919  1.00 74.07      A    O  
ANISOU  674  O   PHE A 105     7090   9735  11316    761     53   -501  A    O  
ATOM    675  CB  PHE A 105      58.063 -11.123 -16.921  1.00 57.19      A    C  
ANISOU  675  CB  PHE A 105     4908   7773   9047    980    273   -827  A    C  
ATOM    676  CG  PHE A 105      58.783 -12.439 -16.822  1.00 54.80      A    C  
ANISOU  676  CG  PHE A 105     4527   7409   8884   1184    205   -950  A    C  
ATOM    677  CD1 PHE A 105      58.161 -13.613 -17.196  1.00 55.60      A    C  
ANISOU  677  CD1 PHE A 105     4745   7359   9023   1305    157  -1075  A    C  
ATOM    678  CD2 PHE A 105      60.106 -12.494 -16.382  1.00 60.60      A    C  
ANISOU  678  CD2 PHE A 105     5069   8243   9712   1260    187   -944  A    C  
ATOM    679  CE1 PHE A 105      58.842 -14.833 -17.122  1.00 63.98      A    C  
ANISOU  679  CE1 PHE A 105     5755   8341  10212   1511     92  -1194  A    C  
ATOM    680  CE2 PHE A 105      60.800 -13.710 -16.306  1.00 55.59      A    C  
ANISOU  680  CE2 PHE A 105     4358   7554   9210   1479    120  -1061  A    C  
ATOM    681  CZ  PHE A 105      60.168 -14.877 -16.673  1.00 57.43      A    C  
ANISOU  681  CZ  PHE A 105     4732   7610   9479   1612     72  -1186  A    C  
ATOM    682  N   CYS A 106      57.668 -12.232 -13.852  1.00 72.07      A    N  
ANISOU  682  N   CYS A 106     6972   9210  11202    978    -80   -645  A    N  
ATOM    683  CA  CYS A 106      58.306 -12.541 -12.571  1.00 70.32      A    C  
ANISOU  683  CA  CYS A 106     6719   8898  11099   1005   -214   -565  A    C  
ATOM    684  C   CYS A 106      59.064 -13.854 -12.702  1.00 79.32      A    C  
ANISOU  684  C   CYS A 106     7785   9985  12369   1227   -279   -687  A    C  
ATOM    685  O   CYS A 106      58.490 -14.888 -13.064  1.00 72.26      A    O  
ANISOU  685  O   CYS A 106     7004   8942  11508   1326   -312   -786  A    O  
ATOM    686  CB  CYS A 106      57.290 -12.623 -11.417  1.00 70.90      A    C  
ANISOU  686  CB  CYS A 106     6989   8764  11186    900   -326   -447  A    C  
ATOM    687  SG  CYS A 106      56.147 -11.159 -11.186  1.00 97.97      A    S  
ANISOU  687  SG  CYS A 106    10543  12219  14461    666   -257   -314  A    S  
ATOM    688  N   GLU A 107      60.360 -13.798 -12.406  1.00 85.91      A    N  
ANISOU  688  N   GLU A 107     8428  10939  13274   1306   -303   -683  A    N  
ATOM    689  CA  GLU A 107      61.261 -14.917 -12.631  1.00 80.86      A    C  
ANISOU  689  CA  GLU A 107     7675  10294  12753   1548   -348   -808  A    C  
ATOM    690  C   GLU A 107      61.002 -16.082 -11.672  1.00 78.33      A    C  
ANISOU  690  C   GLU A 107     7505   9700  12557   1653   -531   -787  A    C  
ATOM    691  O   GLU A 107      60.916 -17.239 -12.091  1.00 74.27      A    O  
ANISOU  691  O   GLU A 107     7057   9054  12109   1829   -566   -912  A    O  
ATOM    692  CB  GLU A 107      62.711 -14.433 -12.515  1.00 97.95      A    C  
ANISOU  692  CB  GLU A 107     9567  12694  14955   1591   -326   -795  A    C  
ATOM    693  CG  GLU A 107      63.763 -15.529 -12.677  1.00108.45      A    C  
ANISOU  693  CG  GLU A 107    10743  14050  16415   1867   -377   -921  A    C  
ATOM    694  CD  GLU A 107      63.829 -16.079 -14.090  1.00113.93      A    C  
ANISOU  694  CD  GLU A 107    11388  14825  17074   2025   -242  -1117  A    C  
ATOM    695  OE1 GLU A 107      63.909 -15.270 -15.043  1.00118.86      A    O  
ANISOU  695  OE1 GLU A 107    11916  15668  17578   1932    -72  -1150  A    O  
ATOM    696  OE2 GLU A 107      63.805 -17.321 -14.244  1.00109.64      A    O1-
ANISOU  696  OE2 GLU A 107    10919  14120  16619   2241   -309  -1236  A    O1-
ATOM    697  N   HIS A 108      60.866 -15.776 -10.386  1.00 81.56      A    N  
ANISOU  697  N   HIS A 108     7986  10014  12989   1540   -648   -628  A    N  
ATOM    698  CA  HIS A 108      60.790 -16.821  -9.367  1.00 80.59      A    C  
ANISOU  698  CA  HIS A 108     7994   9647  12978   1632   -831   -583  A    C  
ATOM    699  C   HIS A 108      59.417 -17.005  -8.724  1.00 72.53      A    C  
ANISOU  699  C   HIS A 108     7240   8397  11919   1483   -891   -491  A    C  
ATOM    700  O   HIS A 108      58.537 -16.156  -8.831  1.00 67.01      A    O  
ANISOU  700  O   HIS A 108     6612   7738  11109   1295   -807   -435  A    O  
ATOM    701  CB  HIS A 108      61.824 -16.556  -8.271  1.00 83.11      A    C  
ANISOU  701  CB  HIS A 108     8188  10028  13362   1648   -948   -473  A    C  
ATOM    702  CG  HIS A 108      63.161 -16.157  -8.802  1.00 93.15      A    C  
ANISOU  702  CG  HIS A 108     9164  11573  14658   1745   -881   -539  A    C  
ATOM    703  CD2 HIS A 108      64.188 -16.899  -9.278  1.00 92.82      A    C  
ANISOU  703  CD2 HIS A 108     8943  11613  14712   1992   -890   -663  A    C  
ATOM    704  ND1 HIS A 108      63.551 -14.838  -8.917  1.00 91.06      A    N  
ANISOU  704  ND1 HIS A 108     8749  11544  14306   1573   -782   -480  A    N  
ATOM    705  CE1 HIS A 108      64.767 -14.788  -9.431  1.00 91.45      A    C  
ANISOU  705  CE1 HIS A 108     8530  11820  14397   1691   -732   -557  A    C  
ATOM    706  NE2 HIS A 108      65.174 -16.024  -9.662  1.00 93.72      A    N  
ANISOU  706  NE2 HIS A 108     8784  12029  14795   1956   -792   -673  A    N  
ATOM    707  N   ASP A 109      59.268 -18.132  -8.040  1.00 71.10      A    N  
ANISOU  707  N   ASP A 109     7206   7976  11832   1575  -1039   -474  A    N  
ATOM    708  CA  ASP A 109      58.101 -18.417  -7.233  1.00 74.56      A    C  
ANISOU  708  CA  ASP A 109     7887   8196  12247   1434  -1116   -369  A    C  
ATOM    709  C   ASP A 109      58.518 -19.188  -5.970  1.00 74.11      A    C  
ANISOU  709  C   ASP A 109     7918   7954  12286   1508  -1308   -268  A    C  
ATOM    710  O   ASP A 109      59.375 -20.069  -6.017  1.00 79.47      A    O  
ANISOU  710  O   ASP A 109     8549   8571  13076   1725  -1396   -335  A    O  
ATOM    711  CB  ASP A 109      57.089 -19.215  -8.044  1.00 84.70      A    C  
ANISOU  711  CB  ASP A 109     9326   9336  13522   1441  -1077   -479  A    C  
ATOM    712  CG  ASP A 109      57.528 -20.630  -8.273  1.00 99.71      A    C  
ANISOU  712  CG  ASP A 109    11286  11055  15544   1662  -1173   -591  A    C  
ATOM    713  OD1 ASP A 109      58.414 -20.845  -9.129  1.00114.12      A    O  
ANISOU  713  OD1 ASP A 109    12958  12994  17410   1853  -1121   -732  A    O  
ATOM    714  OD2 ASP A 109      56.986 -21.525  -7.590  1.00103.73      A    O1-
ANISOU  714  OD2 ASP A 109    12002  11307  16103   1646  -1296   -537  A    O1-
ATOM    715  N   LEU A 110      57.907 -18.842  -4.844  1.00 67.96      A    N  
ANISOU  715  N   LEU A 110     7273   7092  11456   1333  -1371   -109  A    N  
ATOM    716  CA  LEU A 110      58.257 -19.417  -3.555  1.00 65.65      A    C  
ANISOU  716  CA  LEU A 110     7078   6640  11225   1370  -1553     13  A    C  
ATOM    717  C   LEU A 110      58.379 -20.948  -3.565  1.00 70.41      A    C  
ANISOU  717  C   LEU A 110     7813   6994  11946   1558  -1679    -43  A    C  
ATOM    718  O   LEU A 110      59.271 -21.499  -2.919  1.00 72.45      A    O  
ANISOU  718  O   LEU A 110     8050   7185  12291   1713  -1827     -2  A    O  
ATOM    719  CB  LEU A 110      57.256 -18.954  -2.498  1.00 65.97      A    C  
ANISOU  719  CB  LEU A 110     7295   6603  11168   1137  -1575    173  A    C  
ATOM    720  CG  LEU A 110      57.769 -18.757  -1.078  1.00 68.44      A    C  
ANISOU  720  CG  LEU A 110     7640   6891  11475   1099  -1717    332  A    C  
ATOM    721  CD1 LEU A 110      59.135 -18.076  -1.085  1.00 73.69      A    C  
ANISOU  721  CD1 LEU A 110     8058   7774  12168   1187  -1735    320  A    C  
ATOM    722  CD2 LEU A 110      56.757 -17.950  -0.270  1.00 64.26      A    C  
ANISOU  722  CD2 LEU A 110     7242   6363  10813    853  -1676    460  A    C  
ATOM    723  N   ALA A 111      57.502 -21.639  -4.289  1.00 68.41      A    N  
ANISOU  723  N   ALA A 111     7698   6599  11695   1550  -1631   -137  A    N  
ATOM    724  CA  ALA A 111      57.592 -23.101  -4.358  1.00 67.45      A    C  
ANISOU  724  CA  ALA A 111     7730   6214  11683   1722  -1748   -202  A    C  
ATOM    725  C   ALA A 111      58.913 -23.560  -4.991  1.00 78.15      A    C  
ANISOU  725  C   ALA A 111     8909   7638  13146   2023  -1773   -340  A    C  
ATOM    726  O   ALA A 111      59.556 -24.506  -4.507  1.00 80.00      A    O  
ANISOU  726  O   ALA A 111     9207   7703  13488   2217  -1929   -330  A    O  
ATOM    727  CB  ALA A 111      56.409 -23.694  -5.105  1.00 58.25      A    C  
ANISOU  727  CB  ALA A 111     6740   4901  10493   1636  -1687   -292  A    C  
ATOM    728  N   GLY A 112      59.306 -22.888  -6.073  1.00 73.86      A    N  
ANISOU  728  N   GLY A 112     8148   7349  12569   2067  -1618   -468  A    N  
ATOM    729  CA  GLY A 112      60.572 -23.157  -6.733  1.00 73.60      A    C  
ANISOU  729  CA  GLY A 112     7903   7445  12618   2337  -1605   -605  A    C  
ATOM    730  C   GLY A 112      61.795 -22.868  -5.875  1.00 79.50      A    C  
ANISOU  730  C   GLY A 112     8470   8312  13425   2441  -1712   -511  A    C  
ATOM    731  O   GLY A 112      62.688 -23.719  -5.745  1.00 84.24      A    O  
ANISOU  731  O   GLY A 112     9025   8841  14141   2703  -1828   -561  A    O  
ATOM    732  N   LEU A 113      61.841 -21.673  -5.290  1.00 72.97      A    N  
ANISOU  732  N   LEU A 113     7540   7667  12517   2243  -1680   -381  A    N  
ATOM    733  CA  LEU A 113      62.975 -21.277  -4.465  1.00 74.11      A    C  
ANISOU  733  CA  LEU A 113     7504   7953  12702   2303  -1784   -289  A    C  
ATOM    734  C   LEU A 113      63.129 -22.209  -3.256  1.00 85.35      A    C  
ANISOU  734  C   LEU A 113     9098   9126  14205   2400  -2014   -174  A    C  
ATOM    735  O   LEU A 113      64.243 -22.549  -2.850  1.00 92.65      A    O  
ANISOU  735  O   LEU A 113     9885  10097  15220   2601  -2142   -164  A    O  
ATOM    736  CB  LEU A 113      62.834 -19.822  -4.018  1.00 70.41      A    C  
ANISOU  736  CB  LEU A 113     6952   7684  12116   2038  -1714   -169  A    C  
ATOM    737  CG  LEU A 113      62.635 -18.776  -5.127  1.00 71.80      A    C  
ANISOU  737  CG  LEU A 113     6988   8097  12197   1913  -1494   -252  A    C  
ATOM    738  CD1 LEU A 113      62.046 -17.461  -4.593  1.00 58.16      A    C  
ANISOU  738  CD1 LEU A 113     5302   6458  10340   1623  -1436   -119  A    C  
ATOM    739  CD2 LEU A 113      63.934 -18.511  -5.873  1.00 71.54      A    C  
ANISOU  739  CD2 LEU A 113     6639   8336  12208   2065  -1424   -359  A    C  
ATOM    740  N   LEU A 114      62.006 -22.636  -2.696  1.00 79.57      A    N  
ANISOU  740  N   LEU A 114     8662   8137  13436   2260  -2068    -84  A    N  
ATOM    741  CA  LEU A 114      62.025 -23.492  -1.522  1.00 82.04      A    C  
ANISOU  741  CA  LEU A 114     9175   8196  13801   2316  -2280     47  A    C  
ATOM    742  C   LEU A 114      62.409 -24.943  -1.853  1.00 91.54      A    C  
ANISOU  742  C   LEU A 114    10473   9168  15137   2609  -2390    -55  A    C  
ATOM    743  O   LEU A 114      62.943 -25.664  -1.001  1.00 81.21      A    O  
ANISOU  743  O   LEU A 114     9249   7706  13904   2758  -2586     30  A    O  
ATOM    744  CB  LEU A 114      60.671 -23.447  -0.808  1.00 81.41      A    C  
ANISOU  744  CB  LEU A 114     9377   7933  13623   2046  -2286    182  A    C  
ATOM    745  CG  LEU A 114      60.356 -22.178  -0.017  1.00 78.83      A    C  
ANISOU  745  CG  LEU A 114     9018   7766  13168   1787  -2245    326  A    C  
ATOM    746  CD1 LEU A 114      59.043 -22.327   0.733  1.00 72.85      A    C  
ANISOU  746  CD1 LEU A 114     8543   6814  12322   1559  -2260    453  A    C  
ATOM    747  CD2 LEU A 114      61.489 -21.843   0.939  1.00 81.05      A    C  
ANISOU  747  CD2 LEU A 114     9167   8159  13469   1855  -2390    429  A    C  
ATOM    748  N   SER A 115      62.130 -25.372  -3.082  1.00 94.63      A    N  
ANISOU  748  N   SER A 115    10870   9530  15554   2697  -2270   -237  A    N  
ATOM    749  CA  SER A 115      62.486 -26.719  -3.508  1.00 92.96      A    C  
ANISOU  749  CA  SER A 115    10759   9097  15465   2986  -2360   -361  A    C  
ATOM    750  C   SER A 115      63.894 -26.723  -4.096  1.00100.65      A    C  
ANISOU  750  C   SER A 115    11425  10291  16527   3289  -2346   -496  A    C  
ATOM    751  O   SER A 115      64.287 -27.662  -4.793  1.00105.25      A    O  
ANISOU  751  O   SER A 115    12023  10767  17201   3560  -2361   -657  A    O  
ATOM    752  CB  SER A 115      61.486 -27.250  -4.533  1.00 88.94      A    C  
ANISOU  752  CB  SER A 115    10426   8434  14934   2933  -2249   -505  A    C  
ATOM    753  OG  SER A 115      61.766 -26.733  -5.825  1.00 91.66      A    O  
ANISOU  753  OG  SER A 115    10544   9034  15250   2991  -2060   -686  A    O  
ATOM    754  N   ASN A 116      64.649 -25.669  -3.813  1.00100.19      A    N  
ANISOU  754  N   ASN A 116    11087  10545  16437   3240  -2314   -435  A    N  
ATOM    755  CA  ASN A 116      66.010 -25.543  -4.315  1.00106.34      A    C  
ANISOU  755  CA  ASN A 116    11530  11586  17288   3492  -2289   -548  A    C  
ATOM    756  C   ASN A 116      67.033 -25.447  -3.177  1.00114.28      A    C  
ANISOU  756  C   ASN A 116    12398  12672  18352   3592  -2480   -411  A    C  
ATOM    757  O   ASN A 116      67.128 -24.420  -2.496  1.00114.76      A    O  
ANISOU  757  O   ASN A 116    12358  12909  18338   3376  -2486   -275  A    O  
ATOM    758  CB  ASN A 116      66.118 -24.332  -5.242  1.00102.18      A    C  
ANISOU  758  CB  ASN A 116    10740  11414  16668   3347  -2058   -629  A    C  
ATOM    759  CG  ASN A 116      67.418 -24.303  -6.019  1.00106.41      A    C  
ANISOU  759  CG  ASN A 116    10930  12229  17270   3604  -1989   -781  A    C  
ATOM    760  ND2 ASN A 116      67.340 -23.884  -7.274  1.00103.83      A    N  
ANISOU  760  ND2 ASN A 116    10476  12092  16883   3579  -1772   -932  A    N  
ATOM    761  OD1 ASN A 116      68.483 -24.645  -5.498  1.00110.78      A    O  
ANISOU  761  OD1 ASN A 116    11327  12841  17923   3824  -2128   -761  A    O  
ATOM    762  N   VAL A 117      67.795 -26.521  -2.978  1.00110.73      A    N  
ANISOU  762  N   VAL A 117    11953  12088  18032   3924  -2642   -453  A    N  
ATOM    763  CA  VAL A 117      68.739 -26.596  -1.868  1.00111.92      A    C  
ANISOU  763  CA  VAL A 117    11998  12283  18243   4050  -2857   -319  A    C  
ATOM    764  C   VAL A 117      69.803 -25.496  -1.899  1.00111.61      A    C  
ANISOU  764  C   VAL A 117    11543  12675  18189   4023  -2801   -319  A    C  
ATOM    765  O   VAL A 117      70.297 -25.078  -0.852  1.00115.51      A    O  
ANISOU  765  O   VAL A 117    11957  13260  18672   3960  -2949   -166  A    O  
ATOM    766  CB  VAL A 117      69.427 -27.980  -1.792  1.00115.89      A    C  
ANISOU  766  CB  VAL A 117    12564  12573  18897   4461  -3038   -386  A    C  
ATOM    767  CG1 VAL A 117      68.396 -29.071  -1.538  1.00117.56      A    C  
ANISOU  767  CG1 VAL A 117    13224  12323  19121   4452  -3134   -347  A    C  
ATOM    768  CG2 VAL A 117      70.214 -28.261  -3.066  1.00111.16      A    C  
ANISOU  768  CG2 VAL A 117    11703  12157  18377   4757  -2907   -629  A    C  
ATOM    769  N   LEU A 118      70.150 -25.027  -3.095  1.00106.01      A    N  
ANISOU  769  N   LEU A 118    10576  12233  17469   4056  -2589   -488  A    N  
ATOM    770  CA  LEU A 118      71.157 -23.978  -3.234  1.00106.01      A    C  
ANISOU  770  CA  LEU A 118    10175  12654  17451   4007  -2515   -495  A    C  
ATOM    771  C   LEU A 118      70.636 -22.633  -2.741  1.00105.62      A    C  
ANISOU  771  C   LEU A 118    10136  12733  17262   3600  -2449   -348  A    C  
ATOM    772  O   LEU A 118      71.406 -21.801  -2.265  1.00108.98      A    O  
ANISOU  772  O   LEU A 118    10318  13422  17669   3506  -2487   -273  A    O  
ATOM    773  CB  LEU A 118      71.630 -23.860  -4.687  1.00112.09      A    C  
ANISOU  773  CB  LEU A 118    10684  13674  18231   4140  -2291   -713  A    C  
ATOM    774  CG  LEU A 118      72.335 -25.078  -5.302  1.00116.13      A    C  
ANISOU  774  CG  LEU A 118    11117  14129  18876   4576  -2327   -893  A    C  
ATOM    775  CD1 LEU A 118      72.704 -24.812  -6.759  1.00116.82      A    C  
ANISOU  775  CD1 LEU A 118    10955  14494  18938   4657  -2072  -1105  A    C  
ATOM    776  CD2 LEU A 118      73.568 -25.487  -4.489  1.00108.83      A    C  
ANISOU  776  CD2 LEU A 118     9983  13294  18074   4847  -2545   -840  A    C  
ATOM    777  N   VAL A 119      69.326 -22.430  -2.867  1.00103.14      A    N  
ANISOU  777  N   VAL A 119    10107  12232  16851   3362  -2354   -316  A    N  
ATOM    778  CA  VAL A 119      68.663 -21.212  -2.411  1.00 91.89      A    C  
ANISOU  778  CA  VAL A 119     8745  10882  15288   2991  -2287   -184  A    C  
ATOM    779  C   VAL A 119      68.584 -21.204  -0.892  1.00 95.61      A    C  
ANISOU  779  C   VAL A 119     9370  11216  15741   2893  -2504     17  A    C  
ATOM    780  O   VAL A 119      68.149 -22.188  -0.295  1.00 98.73      A    O  
ANISOU  780  O   VAL A 119    10028  11309  16176   2988  -2652     76  A    O  
ATOM    781  CB  VAL A 119      67.220 -21.140  -2.951  1.00 84.12      A    C  
ANISOU  781  CB  VAL A 119     8031   9720  14212   2801  -2140   -209  A    C  
ATOM    782  CG1 VAL A 119      66.536 -19.880  -2.463  1.00 69.37      A    C  
ANISOU  782  CG1 VAL A 119     6228   7926  12203   2448  -2072    -79  A    C  
ATOM    783  CG2 VAL A 119      67.203 -21.227  -4.473  1.00 83.03      A    C  
ANISOU  783  CG2 VAL A 119     7779   9693  14075   2898  -1934   -409  A    C  
ATOM    784  N   LYS A 120      68.983 -20.101  -0.264  1.00 97.12      A    N  
ANISOU  784  N   LYS A 120     9419  11620  15862   2693  -2524    121  A    N  
ATOM    785  CA  LYS A 120      69.017 -20.049   1.199  1.00102.53      A    C  
ANISOU  785  CA  LYS A 120    10235  12207  16516   2605  -2737    306  A    C  
ATOM    786  C   LYS A 120      68.514 -18.716   1.766  1.00104.84      A    C  
ANISOU  786  C   LYS A 120    10581  12597  16658   2246  -2677    420  A    C  
ATOM    787  O   LYS A 120      69.014 -17.646   1.408  1.00100.92      A    O  
ANISOU  787  O   LYS A 120     9850  12377  16117   2113  -2571    391  A    O  
ATOM    788  CB  LYS A 120      70.434 -20.355   1.705  1.00104.34      A    C  
ANISOU  788  CB  LYS A 120    10208  12590  16846   2830  -2929    323  A    C  
ATOM    789  CG  LYS A 120      70.493 -21.039   3.067  1.00108.58      A    C  
ANISOU  789  CG  LYS A 120    10942  12913  17399   2903  -3202    481  A    C  
ATOM    790  CD  LYS A 120      71.850 -21.704   3.286  1.00114.66      A    C  
ANISOU  790  CD  LYS A 120    11470  13792  18305   3231  -3393    458  A    C  
ATOM    791  CE  LYS A 120      71.848 -22.636   4.498  1.00116.55      A    C  
ANISOU  791  CE  LYS A 120    11951  13763  18570   3364  -3673    607  A    C  
ATOM    792  NZ  LYS A 120      73.131 -23.394   4.643  1.00117.30      A    N1+
ANISOU  792  NZ  LYS A 120    11820  13942  18806   3732  -3867    575  A    N1+
ATOM    793  N   PHE A 121      67.522 -18.789   2.651  1.00106.39      A    N  
ANISOU  793  N   PHE A 121    11093  12560  16770   2088  -2743    549  A    N  
ATOM    794  CA  PHE A 121      66.989 -17.598   3.309  1.00101.86      A    C  
ANISOU  794  CA  PHE A 121    10608  12048  16048   1770  -2701    659  A    C  
ATOM    795  C   PHE A 121      67.572 -17.457   4.716  1.00 99.74      A    C  
ANISOU  795  C   PHE A 121    10355  11795  15746   1729  -2928    809  A    C  
ATOM    796  O   PHE A 121      67.712 -18.448   5.440  1.00 99.59      A    O  
ANISOU  796  O   PHE A 121    10464  11598  15778   1884  -3120    882  A    O  
ATOM    797  CB  PHE A 121      65.459 -17.668   3.430  1.00100.44      A    C  
ANISOU  797  CB  PHE A 121    10758  11631  15772   1601  -2613    706  A    C  
ATOM    798  CG  PHE A 121      64.726 -17.732   2.111  1.00105.13      A    C  
ANISOU  798  CG  PHE A 121    11366  12206  16374   1603  -2399    570  A    C  
ATOM    799  CD1 PHE A 121      64.370 -16.571   1.438  1.00 97.60      A    C  
ANISOU  799  CD1 PHE A 121    10331  11422  15330   1416  -2202    525  A    C  
ATOM    800  CD2 PHE A 121      64.355 -18.955   1.566  1.00105.63      A    C  
ANISOU  800  CD2 PHE A 121    11545  12066  16524   1786  -2404    492  A    C  
ATOM    801  CE1 PHE A 121      63.685 -16.630   0.239  1.00 84.33      A    C  
ANISOU  801  CE1 PHE A 121     8669   9729  13644   1420  -2018    407  A    C  
ATOM    802  CE2 PHE A 121      63.667 -19.015   0.366  1.00 96.83      A    C  
ANISOU  802  CE2 PHE A 121    10449  10938  15403   1779  -2218    364  A    C  
ATOM    803  CZ  PHE A 121      63.336 -17.851  -0.297  1.00 83.85      A    C  
ANISOU  803  CZ  PHE A 121     8709   9483  13666   1598  -2027    324  A    C  
ATOM    804  N   THR A 122      67.904 -16.227   5.097  1.00 91.73      A    N  
ANISOU  804  N   THR A 122     9227  10987  14640   1516  -2910    856  A    N  
ATOM    805  CA  THR A 122      68.222 -15.922   6.487  1.00 88.96      A    C  
ANISOU  805  CA  THR A 122     8947  10641  14214   1411  -3109   1002  A    C  
ATOM    806  C   THR A 122      66.922 -15.664   7.242  1.00 88.65      A    C  
ANISOU  806  C   THR A 122     9257  10397  14028   1192  -3080   1109  A    C  
ATOM    807  O   THR A 122      65.879 -15.427   6.626  1.00 92.98      A    O  
ANISOU  807  O   THR A 122     9932  10868  14528   1087  -2888   1063  A    O  
ATOM    808  CB  THR A 122      69.122 -14.672   6.615  1.00 92.06      A    C  
ANISOU  808  CB  THR A 122     9084  11336  14560   1249  -3108   1002  A    C  
ATOM    809  CG2 THR A 122      70.421 -14.853   5.829  1.00 90.13      A    C  
ANISOU  809  CG2 THR A 122     8456  11337  14454   1446  -3114    893  A    C  
ATOM    810  OG1 THR A 122      68.422 -13.510   6.142  1.00 85.28      A    O  
ANISOU  810  OG1 THR A 122     8276  10536  13589    994  -2895    972  A    O  
ATOM    811  N   LEU A 123      66.974 -15.702   8.569  1.00 80.69      A    N  
ANISOU  811  N   LEU A 123     8399   9317  12941   1126  -3268   1250  A    N  
ATOM    812  CA  LEU A 123      65.797 -15.387   9.369  1.00 84.20      A    C  
ANISOU  812  CA  LEU A 123     9161   9603  13229    911  -3236   1353  A    C  
ATOM    813  C   LEU A 123      65.236 -14.014   8.990  1.00 86.06      A    C  
ANISOU  813  C   LEU A 123     9388   9961  13351    661  -3028   1308  A    C  
ATOM    814  O   LEU A 123      64.026 -13.790   9.003  1.00 86.77      A    O  
ANISOU  814  O   LEU A 123     9693   9928  13346    526  -2897   1325  A    O  
ATOM    815  CB  LEU A 123      66.137 -15.409  10.858  1.00 85.31      A    C  
ANISOU  815  CB  LEU A 123     9425   9711  13279    856  -3468   1503  A    C  
ATOM    816  CG  LEU A 123      65.005 -14.989  11.801  1.00 87.58      A    C  
ANISOU  816  CG  LEU A 123    10029   9868  13380    624  -3436   1611  A    C  
ATOM    817  CD1 LEU A 123      63.840 -15.962  11.714  1.00 87.14      A    C  
ANISOU  817  CD1 LEU A 123    10232   9549  13327    661  -3373   1642  A    C  
ATOM    818  CD2 LEU A 123      65.499 -14.879  13.233  1.00 85.84      A    C  
ANISOU  818  CD2 LEU A 123     9902   9661  13053    563  -3666   1749  A    C  
ATOM    819  N   SER A 124      66.135 -13.100   8.646  1.00 84.90      A    N  
ANISOU  819  N   SER A 124     8987  10057  13215    605  -3004   1252  A    N  
ATOM    820  CA  SER A 124      65.781 -11.720   8.371  1.00 78.86      A    C  
ANISOU  820  CA  SER A 124     8215   9408  12340    367  -2836   1222  A    C  
ATOM    821  C   SER A 124      64.954 -11.587   7.087  1.00 83.68      A    C  
ANISOU  821  C   SER A 124     8831   9994  12971    364  -2590   1118  A    C  
ATOM    822  O   SER A 124      64.047 -10.753   6.987  1.00 71.99      A    O  
ANISOU  822  O   SER A 124     7490   8486  11377    187  -2443   1119  A    O  
ATOM    823  CB  SER A 124      67.060 -10.891   8.255  1.00 76.03      A    C  
ANISOU  823  CB  SER A 124     7568   9316  12004    309  -2883   1189  A    C  
ATOM    824  OG  SER A 124      66.761  -9.517   8.102  1.00 81.77      A    O  
ANISOU  824  OG  SER A 124     8322  10131  12614     63  -2744   1173  A    O  
ATOM    825  N   GLU A 125      65.285 -12.408   6.100  1.00 88.58      A    N  
ANISOU  825  N   GLU A 125     9298  10626  13730    571  -2551   1024  A    N  
ATOM    826  CA  GLU A 125      64.618 -12.349   4.811  1.00 87.01      A    C  
ANISOU  826  CA  GLU A 125     9085  10423  13553    585  -2332    915  A    C  
ATOM    827  C   GLU A 125      63.274 -13.076   4.878  1.00 80.98      A    C  
ANISOU  827  C   GLU A 125     8597   9412  12761    596  -2287    937  A    C  
ATOM    828  O   GLU A 125      62.270 -12.605   4.335  1.00 73.32      A    O  
ANISOU  828  O   GLU A 125     7726   8411  11721    486  -2116    905  A    O  
ATOM    829  CB  GLU A 125      65.530 -12.929   3.728  1.00 92.42      A    C  
ANISOU  829  CB  GLU A 125     9499  11232  14383    801  -2304    794  A    C  
ATOM    830  CG  GLU A 125      66.801 -12.111   3.513  1.00 95.11      A    C  
ANISOU  830  CG  GLU A 125     9536  11857  14745    759  -2310    763  A    C  
ATOM    831  CD  GLU A 125      67.967 -12.941   2.998  1.00102.74      A    C  
ANISOU  831  CD  GLU A 125    10226  12947  15865   1019  -2379    682  A    C  
ATOM    832  OE1 GLU A 125      68.155 -14.083   3.476  1.00102.03      A    O  
ANISOU  832  OE1 GLU A 125    10188  12720  15860   1225  -2540    706  A    O  
ATOM    833  OE2 GLU A 125      68.704 -12.442   2.120  1.00107.92      A    O1-
ANISOU  833  OE2 GLU A 125    10614  13840  16553   1020  -2269    594  A    O1-
ATOM    834  N   ILE A 126      63.261 -14.216   5.560  1.00 81.36      A    N  
ANISOU  834  N   ILE A 126     8769   9285  12861    723  -2448   1000  A    N  
ATOM    835  CA  ILE A 126      62.020 -14.927   5.813  1.00 72.36      A    C  
ANISOU  835  CA  ILE A 126     7903   7906  11685    700  -2428   1045  A    C  
ATOM    836  C   ILE A 126      61.026 -13.963   6.459  1.00 75.64      A    C  
ANISOU  836  C   ILE A 126     8500   8308  11931    451  -2346   1122  A    C  
ATOM    837  O   ILE A 126      59.852 -13.934   6.087  1.00 75.66      A    O  
ANISOU  837  O   ILE A 126     8636   8226  11883    372  -2207   1102  A    O  
ATOM    838  CB  ILE A 126      62.238 -16.154   6.712  1.00 70.93      A    C  
ANISOU  838  CB  ILE A 126     7857   7536  11557    833  -2640   1137  A    C  
ATOM    839  CG1 ILE A 126      63.059 -17.216   5.982  1.00 78.18      A    C  
ANISOU  839  CG1 ILE A 126     8626   8430  12648   1112  -2708   1045  A    C  
ATOM    840  CG2 ILE A 126      60.910 -16.750   7.150  1.00 64.28      A    C  
ANISOU  840  CG2 ILE A 126     7318   6456  10649    746  -2619   1210  A    C  
ATOM    841  CD1 ILE A 126      63.212 -18.521   6.768  1.00 74.91      A    C  
ANISOU  841  CD1 ILE A 126     8378   7790  12295   1269  -2919   1134  A    C  
ATOM    842  N   LYS A 127      61.499 -13.159   7.410  1.00 78.86      A    N  
ANISOU  842  N   LYS A 127     8907   8808  12250    332  -2433   1202  A    N  
ATOM    843  CA  LYS A 127      60.661 -12.123   8.014  1.00 77.23      A    C  
ANISOU  843  CA  LYS A 127     8863   8606  11875    109  -2350   1258  A    C  
ATOM    844  C   LYS A 127      60.096 -11.185   6.956  1.00 77.27      A    C  
ANISOU  844  C   LYS A 127     8808   8705  11846     22  -2128   1164  A    C  
ATOM    845  O   LYS A 127      58.914 -10.825   6.984  1.00 76.55      A    O  
ANISOU  845  O   LYS A 127     8880   8549  11657    -88  -2005   1176  A    O  
ATOM    846  CB  LYS A 127      61.450 -11.297   9.028  1.00 72.09      A    C  
ANISOU  846  CB  LYS A 127     8188   8066  11139     -1  -2476   1329  A    C  
ATOM    847  CG  LYS A 127      61.439 -11.866  10.418  1.00 72.26      A    C  
ANISOU  847  CG  LYS A 127     8392   7968  11093    -10  -2666   1459  A    C  
ATOM    848  CD  LYS A 127      62.275 -11.026  11.356  1.00 71.20      A    C  
ANISOU  848  CD  LYS A 127     8222   7960  10870   -121  -2799   1515  A    C  
ATOM    849  CE  LYS A 127      62.503 -11.771  12.659  1.00 77.82      A    C  
ANISOU  849  CE  LYS A 127     9211   8696  11662    -86  -3023   1645  A    C  
ATOM    850  NZ  LYS A 127      62.967 -10.858  13.734  1.00 85.90      A    N1+
ANISOU  850  NZ  LYS A 127    10279   9817  12542   -244  -3136   1707  A    N1+
ATOM    851  N   ARG A 128      60.952 -10.782   6.026  1.00 68.55      A    N  
ANISOU  851  N   ARG A 128     7467   7763  10815     72  -2076   1073  A    N  
ATOM    852  CA  ARG A 128      60.554  -9.823   5.017  1.00 70.59      A    C  
ANISOU  852  CA  ARG A 128     7666   8121  11033    -13  -1878    994  A    C  
ATOM    853  C   ARG A 128      59.505 -10.428   4.095  1.00 68.32      A    C  
ANISOU  853  C   ARG A 128     7447   7737  10777     55  -1743    930  A    C  
ATOM    854  O   ARG A 128      58.484  -9.796   3.804  1.00 60.39      A    O  
ANISOU  854  O   ARG A 128     6547   6718   9681    -49  -1602    920  A    O  
ATOM    855  CB  ARG A 128      61.769  -9.354   4.224  1.00 73.67      A    C  
ANISOU  855  CB  ARG A 128     7782   8715  11493     21  -1855    920  A    C  
ATOM    856  CG  ARG A 128      61.471  -8.230   3.264  1.00 67.70      A    C  
ANISOU  856  CG  ARG A 128     6979   8068  10676    -92  -1662    859  A    C  
ATOM    857  CD  ARG A 128      61.047  -6.965   3.985  1.00 68.42      A    C  
ANISOU  857  CD  ARG A 128     7223   8157  10616   -302  -1636    924  A    C  
ATOM    858  NE  ARG A 128      60.618  -5.960   3.015  1.00 67.48      A    N  
ANISOU  858  NE  ARG A 128     7098   8106  10437   -391  -1451    871  A    N  
ATOM    859  CZ  ARG A 128      59.371  -5.519   2.886  1.00 62.99      A    C  
ANISOU  859  CZ  ARG A 128     6710   7450   9772   -452  -1331    876  A    C  
ATOM    860  NH1 ARG A 128      58.411  -5.964   3.694  1.00 62.69      A    N1+
ANISOU  860  NH1 ARG A 128     6868   7266   9685   -451  -1366    928  A    N1+
ATOM    861  NH2 ARG A 128      59.091  -4.618   1.956  1.00 56.31      A    N  
ANISOU  861  NH2 ARG A 128     5848   6671   8877   -513  -1178    831  A    N  
ATOM    862  N   VAL A 129      59.764 -11.655   3.645  1.00 67.03      A    N  
ANISOU  862  N   VAL A 129     7224   7505  10739    235  -1795    882  A    N  
ATOM    863  CA  VAL A 129      58.827 -12.383   2.798  1.00 65.18      A    C  
ANISOU  863  CA  VAL A 129     7060   7163  10541    302  -1695    813  A    C  
ATOM    864  C   VAL A 129      57.432 -12.450   3.434  1.00 68.84      A    C  
ANISOU  864  C   VAL A 129     7771   7480  10906    180  -1662    888  A    C  
ATOM    865  O   VAL A 129      56.434 -12.074   2.816  1.00 66.87      A    O  
ANISOU  865  O   VAL A 129     7571   7236  10600    112  -1514    847  A    O  
ATOM    866  CB  VAL A 129      59.346 -13.807   2.478  1.00 67.45      A    C  
ANISOU  866  CB  VAL A 129     7296   7354  10976    518  -1794    763  A    C  
ATOM    867  CG1 VAL A 129      58.204 -14.708   1.980  1.00 70.79      A    C  
ANISOU  867  CG1 VAL A 129     7873   7603  11419    549  -1734    722  A    C  
ATOM    868  CG2 VAL A 129      60.466 -13.739   1.451  1.00 57.86      A    C  
ANISOU  868  CG2 VAL A 129     5816   6313   9855    655  -1756    648  A    C  
ATOM    869  N   MET A 130      57.368 -12.919   4.674  1.00 68.44      A    N  
ANISOU  869  N   MET A 130     7868   7310  10827    152  -1801    999  A    N  
ATOM    870  CA  MET A 130      56.097 -13.001   5.382  1.00 66.71      A    C  
ANISOU  870  CA  MET A 130     7874   6969  10502     26  -1770   1079  A    C  
ATOM    871  C   MET A 130      55.428 -11.634   5.537  1.00 72.59      A    C  
ANISOU  871  C   MET A 130     8663   7814  11102   -139  -1638   1092  A    C  
ATOM    872  O   MET A 130      54.196 -11.522   5.543  1.00 72.41      A    O  
ANISOU  872  O   MET A 130     8762   7748  11002   -223  -1533   1102  A    O  
ATOM    873  CB  MET A 130      56.289 -13.663   6.745  1.00 64.76      A    C  
ANISOU  873  CB  MET A 130     7776   6597  10232     17  -1947   1207  A    C  
ATOM    874  CG  MET A 130      56.601 -15.150   6.651  1.00 76.09      A    C  
ANISOU  874  CG  MET A 130     9240   7872  11799    177  -2073   1209  A    C  
ATOM    875  SD  MET A 130      55.554 -15.981   5.434  1.00 77.23      A    S  
ANISOU  875  SD  MET A 130     9424   7906  12013    219  -1942   1106  A    S  
ATOM    876  CE  MET A 130      53.922 -15.644   6.092  1.00 52.82      A    C  
ANISOU  876  CE  MET A 130     6544   4761   8763     -6  -1836   1191  A    C  
ATOM    877  N   GLN A 131      56.244 -10.595   5.657  1.00 68.89      A    N  
ANISOU  877  N   GLN A 131     8095   7482  10597   -182  -1647   1089  A    N  
ATOM    878  CA  GLN A 131      55.736  -9.244   5.816  1.00 56.59      A    C  
ANISOU  878  CA  GLN A 131     6596   6003   8904   -326  -1536   1097  A    C  
ATOM    879  C   GLN A 131      55.054  -8.791   4.531  1.00 56.16      A    C  
ANISOU  879  C   GLN A 131     6482   6006   8849   -321  -1353   1004  A    C  
ATOM    880  O   GLN A 131      53.947  -8.249   4.557  1.00 51.90      A    O  
ANISOU  880  O   GLN A 131     6054   5456   8211   -399  -1242   1011  A    O  
ATOM    881  CB  GLN A 131      56.872  -8.290   6.176  1.00 64.36      A    C  
ANISOU  881  CB  GLN A 131     7489   7107   9860   -384  -1602   1109  A    C  
ATOM    882  CG  GLN A 131      56.409  -6.910   6.593  1.00 68.08      A    C  
ANISOU  882  CG  GLN A 131     8069   7621  10178   -539  -1519   1129  A    C  
ATOM    883  CD  GLN A 131      57.538  -6.067   7.142  1.00 67.29      A    C  
ANISOU  883  CD  GLN A 131     7910   7614  10042   -622  -1615   1151  A    C  
ATOM    884  NE2 GLN A 131      57.384  -5.610   8.376  1.00 59.10      A    N  
ANISOU  884  NE2 GLN A 131     7039   6538   8880   -730  -1685   1223  A    N  
ATOM    885  OE1 GLN A 131      58.539  -5.831   6.466  1.00 64.40      A    O  
ANISOU  885  OE1 GLN A 131     7351   7362   9755   -598  -1625   1103  A    O  
ATOM    886  N   MET A 132      55.712  -9.015   3.402  1.00 55.31      A    N  
ANISOU  886  N   MET A 132     6196   5971   8847   -220  -1324    915  A    N  
ATOM    887  CA  MET A 132      55.129  -8.629   2.130  1.00 55.65      A    C  
ANISOU  887  CA  MET A 132     6184   6077   8883   -208  -1161    828  A    C  
ATOM    888  C   MET A 132      53.849  -9.441   1.870  1.00 60.15      A    C  
ANISOU  888  C   MET A 132     6860   6539   9456   -185  -1108    813  A    C  
ATOM    889  O   MET A 132      52.832  -8.890   1.465  1.00 55.32      A    O  
ANISOU  889  O   MET A 132     6302   5950   8766   -240   -985    794  A    O  
ATOM    890  CB  MET A 132      56.141  -8.819   0.999  1.00 54.91      A    C  
ANISOU  890  CB  MET A 132     5880   6090   8894   -100  -1142    735  A    C  
ATOM    891  CG  MET A 132      57.341  -7.877   1.073  1.00 62.69      A    C  
ANISOU  891  CG  MET A 132     6732   7218   9869   -152  -1165    743  A    C  
ATOM    892  SD  MET A 132      58.632  -8.276  -0.141  1.00 66.04      A    S  
ANISOU  892  SD  MET A 132     6880   7790  10421    -14  -1149    637  A    S  
ATOM    893  CE  MET A 132      58.278  -7.047  -1.389  1.00 92.26      A    C  
ANISOU  893  CE  MET A 132    10163  11240  13653   -103   -948    581  A    C  
ATOM    894  N   LEU A 133      53.911 -10.747   2.118  1.00 54.19      A    N  
ANISOU  894  N   LEU A 133     6137   5663   8788   -106  -1208    822  A    N  
ATOM    895  CA  LEU A 133      52.779 -11.628   1.883  1.00 55.40      A    C  
ANISOU  895  CA  LEU A 133     6390   5704   8954   -103  -1175    808  A    C  
ATOM    896  C   LEU A 133      51.573 -11.169   2.693  1.00 58.22      A    C  
ANISOU  896  C   LEU A 133     6904   6033   9181   -243  -1122    888  A    C  
ATOM    897  O   LEU A 133      50.494 -10.959   2.146  1.00 59.30      A    O  
ANISOU  897  O   LEU A 133     7064   6198   9272   -283  -1004    851  A    O  
ATOM    898  CB  LEU A 133      53.148 -13.076   2.214  1.00 57.89      A    C  
ANISOU  898  CB  LEU A 133     6750   5867   9380     -9  -1315    824  A    C  
ATOM    899  CG  LEU A 133      52.195 -14.193   1.779  1.00 68.96      A    C  
ANISOU  899  CG  LEU A 133     8242   7134  10825      5  -1299    789  A    C  
ATOM    900  CD1 LEU A 133      52.955 -15.485   1.568  1.00 71.41      A    C  
ANISOU  900  CD1 LEU A 133     8539   7317  11275    158  -1420    750  A    C  
ATOM    901  CD2 LEU A 133      51.097 -14.395   2.801  1.00 73.75      A    C  
ANISOU  901  CD2 LEU A 133     9034   7644  11344   -136  -1306    897  A    C  
ATOM    902  N   LEU A 134      51.769 -10.989   3.994  1.00 56.98      A    N  
ANISOU  902  N   LEU A 134     6850   5838   8962   -310  -1207    991  A    N  
ATOM    903  CA  LEU A 134      50.703 -10.541   4.879  1.00 50.50      A    C  
ANISOU  903  CA  LEU A 134     6178   5004   8005   -436  -1154   1066  A    C  
ATOM    904  C   LEU A 134      50.186  -9.159   4.486  1.00 48.50      A    C  
ANISOU  904  C   LEU A 134     5903   4873   7650   -489  -1010   1029  A    C  
ATOM    905  O   LEU A 134      48.993  -8.862   4.626  1.00 51.05      A    O  
ANISOU  905  O   LEU A 134     6302   5210   7883   -551   -911   1041  A    O  
ATOM    906  CB  LEU A 134      51.173 -10.557   6.337  1.00 52.15      A    C  
ANISOU  906  CB  LEU A 134     6502   5160   8152   -493  -1280   1179  A    C  
ATOM    907  CG  LEU A 134      51.318 -11.963   6.939  1.00 57.75      A    C  
ANISOU  907  CG  LEU A 134     7298   5717   8928   -461  -1418   1248  A    C  
ATOM    908  CD1 LEU A 134      51.982 -11.910   8.295  1.00 57.26      A    C  
ANISOU  908  CD1 LEU A 134     7332   5622   8801   -501  -1561   1357  A    C  
ATOM    909  CD2 LEU A 134      49.954 -12.668   7.027  1.00 50.72      A    C  
ANISOU  909  CD2 LEU A 134     6526   4741   8003   -536  -1352   1277  A    C  
ATOM    910  N   ASN A 135      51.078  -8.325   3.971  1.00 45.12      A    N  
ANISOU  910  N   ASN A 135     5368   4537   7236   -459   -997    984  A    N  
ATOM    911  CA  ASN A 135      50.689  -6.997   3.514  1.00 43.90      A    C  
ANISOU  911  CA  ASN A 135     5209   4481   6991   -501   -870    950  A    C  
ATOM    912  C   ASN A 135      49.839  -7.058   2.240  1.00 47.34      A    C  
ANISOU  912  C   ASN A 135     5582   4959   7445   -453   -746    870  A    C  
ATOM    913  O   ASN A 135      48.909  -6.277   2.065  1.00 50.23      A    O  
ANISOU  913  O   ASN A 135     5996   5371   7718   -484   -638    864  A    O  
ATOM    914  CB  ASN A 135      51.918  -6.117   3.288  1.00 43.74      A    C  
ANISOU  914  CB  ASN A 135     5097   4541   6979   -507   -894    931  A    C  
ATOM    915  CG  ASN A 135      51.565  -4.635   3.216  1.00 54.88      A    C  
ANISOU  915  CG  ASN A 135     6570   6012   8270   -577   -792    927  A    C  
ATOM    916  ND2 ASN A 135      52.251  -3.903   2.353  1.00 48.55      A    N  
ANISOU  916  ND2 ASN A 135     5670   5292   7485   -575   -749    882  A    N  
ATOM    917  OD1 ASN A 135      50.670  -4.164   3.920  1.00 55.87      A    O  
ANISOU  917  OD1 ASN A 135     6836   6107   8284   -630   -748    963  A    O  
ATOM    918  N   GLY A 136      50.166  -7.986   1.350  1.00 47.79      A    N  
ANISOU  918  N   GLY A 136     5535   5003   7618   -367   -767    808  A    N  
ATOM    919  CA  GLY A 136      49.339  -8.245   0.190  1.00 47.77      A    C  
ANISOU  919  CA  GLY A 136     5485   5032   7632   -327   -672    730  A    C  
ATOM    920  C   GLY A 136      47.945  -8.712   0.603  1.00 54.16      A    C  
ANISOU  920  C   GLY A 136     6395   5790   8393   -383   -641    761  A    C  
ATOM    921  O   GLY A 136      46.931  -8.196   0.122  1.00 54.48      A    O  
ANISOU  921  O   GLY A 136     6437   5898   8366   -400   -536    736  A    O  
ATOM    922  N   LEU A 137      47.890  -9.686   1.505  1.00 43.00      A    N  
ANISOU  922  N   LEU A 137     5062   4264   7012   -415   -734    822  A    N  
ATOM    923  CA  LEU A 137      46.616 -10.183   2.003  1.00 48.35      A    C  
ANISOU  923  CA  LEU A 137     5834   4897   7641   -495   -704    864  A    C  
ATOM    924  C   LEU A 137      45.775  -9.074   2.633  1.00 53.18      A    C  
ANISOU  924  C   LEU A 137     6510   5590   8107   -567   -611    911  A    C  
ATOM    925  O   LEU A 137      44.577  -8.977   2.385  1.00 56.01      A    O  
ANISOU  925  O   LEU A 137     6866   6002   8411   -600   -519    897  A    O  
ATOM    926  CB  LEU A 137      46.834 -11.319   3.003  1.00 50.77      A    C  
ANISOU  926  CB  LEU A 137     6242   5059   7989   -531   -827    944  A    C  
ATOM    927  CG  LEU A 137      47.275 -12.620   2.328  1.00 54.59      A    C  
ANISOU  927  CG  LEU A 137     6692   5436   8615   -454   -908    889  A    C  
ATOM    928  CD1 LEU A 137      47.552 -13.698   3.370  1.00 54.72      A    C  
ANISOU  928  CD1 LEU A 137     6834   5288   8669   -481  -1044    982  A    C  
ATOM    929  CD2 LEU A 137      46.234 -13.088   1.289  1.00 47.96      A    C  
ANISOU  929  CD2 LEU A 137     5816   4609   7796   -467   -829    807  A    C  
ATOM    930  N   TYR A 138      46.403  -8.229   3.439  1.00 51.15      A    N  
ANISOU  930  N   TYR A 138     6305   5345   7784   -588   -636    960  A    N  
ATOM    931  CA  TYR A 138      45.678  -7.149   4.084  1.00 41.91      A    C  
ANISOU  931  CA  TYR A 138     5215   4236   6470   -640   -550    994  A    C  
ATOM    932  C   TYR A 138      45.005  -6.301   3.017  1.00 49.55      A    C  
ANISOU  932  C   TYR A 138     6114   5309   7404   -592   -425    923  A    C  
ATOM    933  O   TYR A 138      43.846  -5.901   3.155  1.00 47.14      A    O  
ANISOU  933  O   TYR A 138     5839   5062   7010   -609   -331    926  A    O  
ATOM    934  CB  TYR A 138      46.637  -6.282   4.899  1.00 47.18      A    C  
ANISOU  934  CB  TYR A 138     5947   4898   7080   -663   -605   1034  A    C  
ATOM    935  CG  TYR A 138      46.020  -4.983   5.353  1.00 53.29      A    C  
ANISOU  935  CG  TYR A 138     6809   5731   7708   -692   -509   1041  A    C  
ATOM    936  CD1 TYR A 138      45.368  -4.887   6.588  1.00 55.20      A    C  
ANISOU  936  CD1 TYR A 138     7183   5960   7831   -759   -494   1104  A    C  
ATOM    937  CD2 TYR A 138      46.084  -3.845   4.548  1.00 49.40      A    C  
ANISOU  937  CD2 TYR A 138     6281   5301   7187   -648   -432    985  A    C  
ATOM    938  CE1 TYR A 138      44.796  -3.686   7.006  1.00 54.56      A    C  
ANISOU  938  CE1 TYR A 138     7191   5929   7610   -765   -402   1097  A    C  
ATOM    939  CE2 TYR A 138      45.510  -2.643   4.956  1.00 57.97      A    C  
ANISOU  939  CE2 TYR A 138     7468   6419   8139   -658   -349    987  A    C  
ATOM    940  CZ  TYR A 138      44.866  -2.571   6.186  1.00 64.80      A    C  
ANISOU  940  CZ  TYR A 138     8459   7271   8891   -708   -333   1035  A    C  
ATOM    941  OH  TYR A 138      44.296  -1.383   6.597  1.00 80.67      A    O  
ANISOU  941  OH  TYR A 138    10577   9310  10766   -696   -247   1023  A    O  
ATOM    942  N   TYR A 139      45.748  -6.023   1.951  1.00 42.21      A    N  
ANISOU  942  N   TYR A 139     5087   4411   6539   -526   -424    859  A    N  
ATOM    943  CA  TYR A 139      45.232  -5.217   0.855  1.00 39.91      A    C  
ANISOU  943  CA  TYR A 139     4740   4213   6211   -474   -319    798  A    C  
ATOM    944  C   TYR A 139      44.075  -5.887   0.109  1.00 49.35      A    C  
ANISOU  944  C   TYR A 139     5876   5449   7426   -455   -265    754  A    C  
ATOM    945  O   TYR A 139      43.045  -5.256  -0.122  1.00 50.37      A    O  
ANISOU  945  O   TYR A 139     6008   5657   7474   -440   -176    743  A    O  
ATOM    946  CB  TYR A 139      46.343  -4.871  -0.137  1.00 39.42      A    C  
ANISOU  946  CB  TYR A 139     4588   4182   6207   -423   -329    747  A    C  
ATOM    947  CG  TYR A 139      45.819  -4.156  -1.342  1.00 37.53      A    C  
ANISOU  947  CG  TYR A 139     4301   4033   5926   -370   -228    692  A    C  
ATOM    948  CD1 TYR A 139      45.548  -2.792  -1.289  1.00 36.20      A    C  
ANISOU  948  CD1 TYR A 139     4203   3901   5650   -371   -160    710  A    C  
ATOM    949  CD2 TYR A 139      45.559  -4.838  -2.530  1.00 27.90      A    C  
ANISOU  949  CD2 TYR A 139     2981   2854   4767   -315   -209    620  A    C  
ATOM    950  CE1 TYR A 139      45.048  -2.110  -2.397  1.00 33.49      A    C  
ANISOU  950  CE1 TYR A 139     3831   3633   5259   -312    -76    671  A    C  
ATOM    951  CE2 TYR A 139      45.052  -4.166  -3.648  1.00 35.76      A    C  
ANISOU  951  CE2 TYR A 139     3940   3939   5708   -266   -124    575  A    C  
ATOM    952  CZ  TYR A 139      44.793  -2.803  -3.569  1.00 44.88      A    C  
ANISOU  952  CZ  TYR A 139     5166   5130   6756   -261    -60    608  A    C  
ATOM    953  OH  TYR A 139      44.302  -2.116  -4.660  1.00 48.28      A    O  
ANISOU  953  OH  TYR A 139     5577   5640   7127   -203     12    575  A    O  
ATOM    954  N   ILE A 140      44.237  -7.148  -0.286  1.00 50.63      A    N  
ANISOU  954  N   ILE A 140     5985   5558   7693   -450   -325    724  A    N  
ATOM    955  CA  ILE A 140      43.188  -7.793  -1.074  1.00 57.05      A    C  
ANISOU  955  CA  ILE A 140     6741   6409   8524   -448   -285    671  A    C  
ATOM    956  C   ILE A 140      41.910  -7.960  -0.242  1.00 55.60      A    C  
ANISOU  956  C   ILE A 140     6611   6244   8271   -530   -246    724  A    C  
ATOM    957  O   ILE A 140      40.809  -7.770  -0.744  1.00 50.03      A    O  
ANISOU  957  O   ILE A 140     5854   5637   7519   -528   -173    694  A    O  
ATOM    958  CB  ILE A 140      43.621  -9.135  -1.749  1.00 48.95      A    C  
ANISOU  958  CB  ILE A 140     5667   5307   7625   -425   -359    610  A    C  
ATOM    959  CG1 ILE A 140      43.688 -10.272  -0.752  1.00 46.36      A    C  
ANISOU  959  CG1 ILE A 140     5421   4844   7351   -493   -450    671  A    C  
ATOM    960  CG2 ILE A 140      44.966  -9.013  -2.471  1.00 52.19      A    C  
ANISOU  960  CG2 ILE A 140     6011   5715   8103   -337   -391    556  A    C  
ATOM    961  CD1 ILE A 140      43.631 -11.618  -1.427  1.00 56.40      A    C  
ANISOU  961  CD1 ILE A 140     6674   6030   8728   -483   -508    607  A    C  
ATOM    962  N   HIS A 141      42.062  -8.275   1.038  1.00 50.00      A    N  
ANISOU  962  N   HIS A 141     5998   5457   7543   -601   -294    807  A    N  
ATOM    963  CA  HIS A 141      40.905  -8.430   1.908  1.00 48.72      A    C  
ANISOU  963  CA  HIS A 141     5886   5324   7299   -691   -246    864  A    C  
ATOM    964  C   HIS A 141      40.178  -7.100   2.143  1.00 49.56      A    C  
ANISOU  964  C   HIS A 141     6000   5556   7276   -661   -134    869  A    C  
ATOM    965  O   HIS A 141      38.959  -7.027   2.113  1.00 54.15      A    O  
ANISOU  965  O   HIS A 141     6540   6237   7798   -683    -53    864  A    O  
ATOM    966  CB  HIS A 141      41.336  -9.038   3.233  1.00 42.59      A    C  
ANISOU  966  CB  HIS A 141     5229   4435   6518   -774   -325    959  A    C  
ATOM    967  CG  HIS A 141      41.816 -10.447   3.113  1.00 52.93      A    C  
ANISOU  967  CG  HIS A 141     6554   5609   7949   -800   -436    964  A    C  
ATOM    968  CD2 HIS A 141      41.602 -11.382   2.156  1.00 44.34      A    C  
ANISOU  968  CD2 HIS A 141     5405   4485   6958   -794   -460    899  A    C  
ATOM    969  ND1 HIS A 141      42.647 -11.030   4.046  1.00 52.63      A    N  
ANISOU  969  ND1 HIS A 141     6617   5442   7939   -829   -548   1040  A    N  
ATOM    970  CE1 HIS A 141      42.902 -12.277   3.680  1.00 51.61      A    C  
ANISOU  970  CE1 HIS A 141     6493   5191   7923   -829   -634   1025  A    C  
ATOM    971  NE2 HIS A 141      42.285 -12.512   2.536  1.00 46.55      A    N  
ANISOU  971  NE2 HIS A 141     5760   4602   7327   -812   -580    935  A    N  
ATOM    972  N   ARG A 142      40.953  -6.055   2.385  1.00 49.45      A    N  
ANISOU  972  N   ARG A 142     6040   5531   7217   -611   -134    877  A    N  
ATOM    973  CA  ARG A 142      40.442  -4.708   2.546  1.00 45.54      A    C  
ANISOU  973  CA  ARG A 142     5579   5122   6602   -561    -40    872  A    C  
ATOM    974  C   ARG A 142      39.591  -4.344   1.336  1.00 48.94      A    C  
ANISOU  974  C   ARG A 142     5904   5665   7027   -482     38    806  A    C  
ATOM    975  O   ARG A 142      38.677  -3.529   1.435  1.00 50.97      A    O  
ANISOU  975  O   ARG A 142     6166   6015   7188   -434    126    801  A    O  
ATOM    976  CB  ARG A 142      41.629  -3.755   2.684  1.00 51.12      A    C  
ANISOU  976  CB  ARG A 142     6357   5776   7292   -529    -75    876  A    C  
ATOM    977  CG  ARG A 142      41.291  -2.352   3.052  1.00 60.84      A    C  
ANISOU  977  CG  ARG A 142     7676   7045   8396   -487      2    877  A    C  
ATOM    978  CD  ARG A 142      42.559  -1.520   3.139  1.00 85.56      A    C  
ANISOU  978  CD  ARG A 142    10878  10110  11522   -489    -49    881  A    C  
ATOM    979  NE  ARG A 142      42.271  -0.111   3.382  1.00109.75      A    N  
ANISOU  979  NE  ARG A 142    14052  13184  14466   -446     20    873  A    N  
ATOM    980  CZ  ARG A 142      43.123   0.741   3.944  1.00122.41      A    C  
ANISOU  980  CZ  ARG A 142    15774  14720  16018   -481    -17    888  A    C  
ATOM    981  NH1 ARG A 142      44.323   0.322   4.323  1.00123.08      A    N1+
ANISOU  981  NH1 ARG A 142    15857  14744  16162   -558   -125    915  A    N1+
ATOM    982  NH2 ARG A 142      42.771   2.010   4.129  1.00124.56      A    N  
ANISOU  982  NH2 ARG A 142    16166  14984  16176   -435     48    874  A    N  
ATOM    983  N   ASN A 143      39.891  -4.972   0.201  1.00 47.27      A    N  
ANISOU  983  N   ASN A 143     5598   5448   6914   -460     -0    752  A    N  
ATOM    984  CA  ASN A 143      39.170  -4.734  -1.042  1.00 45.68      A    C  
ANISOU  984  CA  ASN A 143     5295   5353   6706   -388     53    688  A    C  
ATOM    985  C   ASN A 143      38.139  -5.799  -1.327  1.00 48.19      A    C  
ANISOU  985  C   ASN A 143     5524   5725   7058   -445     55    664  A    C  
ATOM    986  O   ASN A 143      37.695  -5.942  -2.465  1.00 45.22      A    O  
ANISOU  986  O   ASN A 143     5054   5426   6702   -404     66    601  A    O  
ATOM    987  CB  ASN A 143      40.142  -4.663  -2.217  1.00 45.67      A    C  
ANISOU  987  CB  ASN A 143     5250   5333   6771   -330     19    633  A    C  
ATOM    988  CG  ASN A 143      40.815  -3.324  -2.323  1.00 51.79      A    C  
ANISOU  988  CG  ASN A 143     6085   6106   7486   -271     48    644  A    C  
ATOM    989  ND2 ASN A 143      42.028  -3.213  -1.767  1.00 45.59      A    N  
ANISOU  989  ND2 ASN A 143     5359   5231   6731   -307     -7    674  A    N  
ATOM    990  OD1 ASN A 143      40.257  -2.389  -2.898  1.00 58.58      A    O  
ANISOU  990  OD1 ASN A 143     6944   7043   8272   -197    113    628  A    O  
ATOM    991  N   LYS A 144      37.785  -6.565  -0.295  1.00 49.92      A    N  
ANISOU  991  N   LYS A 144     5784   5905   7280   -552     39    719  A    N  
ATOM    992  CA  LYS A 144      36.672  -7.502  -0.367  1.00 49.94      A    C  
ANISOU  992  CA  LYS A 144     5713   5965   7298   -640     51    713  A    C  
ATOM    993  C   LYS A 144      36.955  -8.628  -1.332  1.00 52.73      A    C  
ANISOU  993  C   LYS A 144     6015   6255   7767   -668    -26    652  A    C  
ATOM    994  O   LYS A 144      36.060  -9.132  -1.994  1.00 57.43      A    O  
ANISOU  994  O   LYS A 144     6519   6929   8372   -705    -15    605  A    O  
ATOM    995  CB  LYS A 144      35.386  -6.779  -0.772  1.00 52.24      A    C  
ANISOU  995  CB  LYS A 144     5904   6442   7503   -587    146    684  A    C  
ATOM    996  CG  LYS A 144      35.042  -5.641   0.152  1.00 55.71      A    C  
ANISOU  996  CG  LYS A 144     6401   6943   7823   -536    229    729  A    C  
ATOM    997  CD  LYS A 144      35.065  -6.136   1.576  1.00 73.95      A    C  
ANISOU  997  CD  LYS A 144     8803   9191  10104   -655    227    808  A    C  
ATOM    998  CE  LYS A 144      35.026  -4.995   2.573  1.00 88.42      A    C  
ANISOU  998  CE  LYS A 144    10733  11048  11813   -599    297    845  A    C  
ATOM    999  NZ  LYS A 144      35.148  -5.499   3.978  1.00 95.12      A    N1+
ANISOU  999  NZ  LYS A 144    11688  11834  12618   -720    287    925  A    N1+
ATOM   1000  N   ILE A 145      38.212  -9.033  -1.406  1.00 52.49      A    N  
ANISOU 1000  N   ILE A 145     6041   6085   7817   -647   -107    645  A    N  
ATOM   1001  CA  ILE A 145      38.567 -10.179  -2.219  1.00 43.61      A    C  
ANISOU 1001  CA  ILE A 145     4890   4878   6803   -660   -182    581  A    C  
ATOM   1002  C   ILE A 145      39.163 -11.282  -1.363  1.00 47.99      A    C  
ANISOU 1002  C   ILE A 145     5545   5257   7432   -737   -274    635  A    C  
ATOM   1003  O   ILE A 145      39.952 -11.013  -0.461  1.00 52.10      A    O  
ANISOU 1003  O   ILE A 145     6145   5707   7944   -727   -306    703  A    O  
ATOM   1004  CB  ILE A 145      39.565  -9.811  -3.317  1.00 38.42      A    C  
ANISOU 1004  CB  ILE A 145     4193   4219   6187   -537   -198    504  A    C  
ATOM   1005  CG1 ILE A 145      39.028  -8.653  -4.175  1.00 40.04      A    C  
ANISOU 1005  CG1 ILE A 145     4322   4584   6307   -456   -113    465  A    C  
ATOM   1006  CG2 ILE A 145      39.881 -11.030  -4.149  1.00 44.13      A    C  
ANISOU 1006  CG2 ILE A 145     4894   4859   7015   -538   -269    422  A    C  
ATOM   1007  CD1 ILE A 145      37.771  -8.980  -4.922  1.00 44.58      A    C  
ANISOU 1007  CD1 ILE A 145     4809   5272   6859   -482    -87    411  A    C  
ATOM   1008  N   LEU A 146      38.747 -12.515  -1.636  1.00 51.59      A    N  
ANISOU 1008  N   LEU A 146     6006   5641   7955   -819   -325    608  A    N  
ATOM   1009  CA  LEU A 146      39.382 -13.707  -1.099  1.00 47.98      A    C  
ANISOU 1009  CA  LEU A 146     5657   4987   7588   -870   -432    643  A    C  
ATOM   1010  C   LEU A 146      40.203 -14.305  -2.223  1.00 55.17      A    C  
ANISOU 1010  C   LEU A 146     6541   5817   8605   -770   -497    535  A    C  
ATOM   1011  O   LEU A 146      39.730 -14.411  -3.360  1.00 57.84      A    O  
ANISOU 1011  O   LEU A 146     6800   6227   8951   -752   -470    434  A    O  
ATOM   1012  CB  LEU A 146      38.327 -14.719  -0.671  1.00 56.80      A    C  
ANISOU 1012  CB  LEU A 146     6818   6058   8705  -1041   -444    683  A    C  
ATOM   1013  CG  LEU A 146      37.274 -14.234   0.319  1.00 52.15      A    C  
ANISOU 1013  CG  LEU A 146     6228   5589   7999  -1155   -358    777  A    C  
ATOM   1014  CD1 LEU A 146      36.327 -15.370   0.647  1.00 49.41      A    C  
ANISOU 1014  CD1 LEU A 146     5920   5192   7663  -1347   -375    816  A    C  
ATOM   1015  CD2 LEU A 146      37.928 -13.694   1.584  1.00 50.89      A    C  
ANISOU 1015  CD2 LEU A 146     6168   5386   7783  -1138   -363    881  A    C  
ATOM   1016  N   HIS A 147      41.439 -14.677  -1.919  1.00 52.90      A    N  
ANISOU 1016  N   HIS A 147     6314   5392   8392   -697   -581    549  A    N  
ATOM   1017  CA  HIS A 147      42.320 -15.238  -2.928  1.00 53.73      A    C  
ANISOU 1017  CA  HIS A 147     6390   5428   8597   -580   -637    440  A    C  
ATOM   1018  C   HIS A 147      41.971 -16.698  -3.223  1.00 53.18      A    C  
ANISOU 1018  C   HIS A 147     6395   5202   8610   -638   -712    392  A    C  
ATOM   1019  O   HIS A 147      41.936 -17.113  -4.379  1.00 49.01      A    O  
ANISOU 1019  O   HIS A 147     5823   4676   8121   -588   -715    269  A    O  
ATOM   1020  CB  HIS A 147      43.780 -15.134  -2.498  1.00 56.04      A    C  
ANISOU 1020  CB  HIS A 147     6700   5647   8944   -469   -703    468  A    C  
ATOM   1021  CG  HIS A 147      44.731 -15.739  -3.482  1.00 47.81      A    C  
ANISOU 1021  CG  HIS A 147     5615   4547   8005   -332   -752    353  A    C  
ATOM   1022  CD2 HIS A 147      45.593 -15.169  -4.357  1.00 45.66      A    C  
ANISOU 1022  CD2 HIS A 147     5232   4373   7744   -204   -715    271  A    C  
ATOM   1023  ND1 HIS A 147      44.850 -17.101  -3.657  1.00 48.84      A    N  
ANISOU 1023  ND1 HIS A 147     5824   4502   8234   -317   -844    306  A    N  
ATOM   1024  CE1 HIS A 147      45.748 -17.345  -4.595  1.00 56.09      A    C  
ANISOU 1024  CE1 HIS A 147     6677   5415   9220   -167   -859    190  A    C  
ATOM   1025  NE2 HIS A 147      46.220 -16.188  -5.029  1.00 55.98      A    N  
ANISOU 1025  NE2 HIS A 147     6539   5577   9154   -103   -778    170  A    N  
ATOM   1026  N   ARG A 148      41.740 -17.472  -2.167  1.00 57.46      A    N  
ANISOU 1026  N   ARG A 148     7064   5599   9169   -748   -778    492  A    N  
ATOM   1027  CA  ARG A 148      41.196 -18.827  -2.288  1.00 59.66      A    C  
ANISOU 1027  CA  ARG A 148     7444   5715   9509   -851   -848    469  A    C  
ATOM   1028  C   ARG A 148      42.129 -19.849  -2.936  1.00 64.31      A    C  
ANISOU 1028  C   ARG A 148     8093   6119  10223   -727   -951    371  A    C  
ATOM   1029  O   ARG A 148      41.740 -20.985  -3.161  1.00 78.09      A    O  
ANISOU 1029  O   ARG A 148     9939   7706  12024   -800  -1015    334  A    O  
ATOM   1030  CB  ARG A 148      39.865 -18.812  -3.046  1.00 58.50      A    C  
ANISOU 1030  CB  ARG A 148     7221   5695   9312   -968   -775    404  A    C  
ATOM   1031  CG  ARG A 148      38.787 -18.012  -2.369  1.00 56.56      A    C  
ANISOU 1031  CG  ARG A 148     6919   5622   8949  -1094   -678    496  A    C  
ATOM   1032  CD  ARG A 148      37.420 -18.546  -2.721  1.00 60.90      A    C  
ANISOU 1032  CD  ARG A 148     7438   6227   9474  -1267   -653    469  A    C  
ATOM   1033  NE  ARG A 148      37.095 -18.369  -4.127  1.00 62.74      A    N  
ANISOU 1033  NE  ARG A 148     7553   6577   9707  -1209   -627    326  A    N  
ATOM   1034  CZ  ARG A 148      35.939 -18.741  -4.660  1.00 63.33      A    C  
ANISOU 1034  CZ  ARG A 148     7570   6734   9759  -1343   -612    277  A    C  
ATOM   1035  NH1 ARG A 148      35.022 -19.305  -3.889  1.00 64.90      A    N1+
ANISOU 1035  NH1 ARG A 148     7810   6912   9937  -1551   -613    361  A    N1+
ATOM   1036  NH2 ARG A 148      35.700 -18.551  -5.952  1.00 60.77      A    N  
ANISOU 1036  NH2 ARG A 148     7144   6522   9424  -1280   -599    147  A    N  
ATOM   1037  N   ASP A 149      43.354 -19.458  -3.244  1.00 59.38      A    N  
ANISOU 1037  N   ASP A 149     7407   5515   9641   -542   -966    325  A    N  
ATOM   1038  CA  ASP A 149      44.294 -20.411  -3.792  1.00 59.28      A    C  
ANISOU 1038  CA  ASP A 149     7441   5339   9745   -398  -1058    230  A    C  
ATOM   1039  C   ASP A 149      45.709 -20.165  -3.252  1.00 60.86      A    C  
ANISOU 1039  C   ASP A 149     7620   5510   9994   -239  -1116    275  A    C  
ATOM   1040  O   ASP A 149      46.698 -20.282  -3.975  1.00 59.41      A    O  
ANISOU 1040  O   ASP A 149     7367   5330   9879    -63  -1134    172  A    O  
ATOM   1041  CB  ASP A 149      44.255 -20.398  -5.321  1.00 63.71      A    C  
ANISOU 1041  CB  ASP A 149     7903   5988  10315   -313  -1003     54  A    C  
ATOM   1042  CG  ASP A 149      44.812 -21.681  -5.932  1.00 72.97      A    C  
ANISOU 1042  CG  ASP A 149     9166   6958  11601   -205  -1098    -65  A    C  
ATOM   1043  OD1 ASP A 149      44.889 -22.709  -5.217  1.00 68.19      A    O  
ANISOU 1043  OD1 ASP A 149     8724   6121  11064   -238  -1208     -8  A    O  
ATOM   1044  OD2 ASP A 149      45.176 -21.655  -7.127  1.00 76.11      A    O1-
ANISOU 1044  OD2 ASP A 149     9484   7426  12010    -82  -1061   -217  A    O1-
ATOM   1045  N   MET A 150      45.784 -19.840  -1.965  1.00 59.55      A    N  
ANISOU 1045  N   MET A 150     7512   5328   9788   -307  -1147    428  A    N  
ATOM   1046  CA  MET A 150      47.062 -19.637  -1.292  1.00 61.66      A    C  
ANISOU 1046  CA  MET A 150     7766   5568  10092   -183  -1224    487  A    C  
ATOM   1047  C   MET A 150      47.933 -20.881  -1.361  1.00 75.15      A    C  
ANISOU 1047  C   MET A 150     9559   7063  11932    -41  -1361    447  A    C  
ATOM   1048  O   MET A 150      47.564 -21.943  -0.847  1.00 82.24      A    O  
ANISOU 1048  O   MET A 150    10632   7749  12866   -106  -1452    502  A    O  
ATOM   1049  CB  MET A 150      46.840 -19.253   0.178  1.00 58.25      A    C  
ANISOU 1049  CB  MET A 150     7422   5129   9581   -305  -1249    661  A    C  
ATOM   1050  CG  MET A 150      46.394 -17.805   0.403  1.00 53.91      A    C  
ANISOU 1050  CG  MET A 150     6779   4799   8905   -382  -1125    701  A    C  
ATOM   1051  SD  MET A 150      47.689 -16.596   0.021  1.00 74.96      A    S  
ANISOU 1051  SD  MET A 150     9274   7635  11571   -232  -1095    653  A    S  
ATOM   1052  CE  MET A 150      47.328 -16.244  -1.685  1.00 66.75      A    C  
ANISOU 1052  CE  MET A 150     8094   6733  10535   -177   -972    490  A    C  
ATOM   1053  N   LYS A 151      49.086 -20.748  -2.009  1.00 76.33      A    N  
ANISOU 1053  N   LYS A 151     9584   7269  12149    156  -1372    350  A    N  
ATOM   1054  CA  LYS A 151      50.113 -21.784  -1.977  1.00 76.17      A    C  
ANISOU 1054  CA  LYS A 151     9616   7072  12255    338  -1506    315  A    C  
ATOM   1055  C   LYS A 151      51.448 -21.217  -2.435  1.00 71.44      A    C  
ANISOU 1055  C   LYS A 151     8820   6625  11697    534  -1494    244  A    C  
ATOM   1056  O   LYS A 151      51.488 -20.206  -3.131  1.00 73.58      A    O  
ANISOU 1056  O   LYS A 151     8931   7116  11912    528  -1369    183  A    O  
ATOM   1057  CB  LYS A 151      49.712 -23.000  -2.819  1.00 80.21      A    C  
ANISOU 1057  CB  LYS A 151    10235   7402  12840    375  -1536    192  A    C  
ATOM   1058  CG  LYS A 151      49.471 -22.718  -4.293  1.00 75.54      A    C  
ANISOU 1058  CG  LYS A 151     9518   6951  12231    417  -1416     15  A    C  
ATOM   1059  CD  LYS A 151      48.741 -23.890  -4.954  1.00 75.28      A    C  
ANISOU 1059  CD  LYS A 151     9633   6729  12240    380  -1449    -89  A    C  
ATOM   1060  CE  LYS A 151      48.948 -23.896  -6.467  1.00 77.19      A    C  
ANISOU 1060  CE  LYS A 151     9766   7071  12492    505  -1371   -295  A    C  
ATOM   1061  NZ  LYS A 151      47.876 -24.650  -7.182  1.00 73.01      A    N1+
ANISOU 1061  NZ  LYS A 151     9356   6433  11951    391  -1367   -394  A    N1+
ATOM   1062  N   ALA A 152      52.537 -21.865  -2.038  1.00 72.48      A    N  
ANISOU 1062  N   ALA A 152     8963   6648  11928    705  -1625    255  A    N  
ATOM   1063  CA  ALA A 152      53.880 -21.372  -2.338  1.00 74.92      A    C  
ANISOU 1063  CA  ALA A 152     9067   7116  12282    887  -1626    201  A    C  
ATOM   1064  C   ALA A 152      54.065 -21.041  -3.816  1.00 69.67      A    C  
ANISOU 1064  C   ALA A 152     8236   6616  11620    975  -1491     23  A    C  
ATOM   1065  O   ALA A 152      54.696 -20.044  -4.163  1.00 69.70      A    O  
ANISOU 1065  O   ALA A 152     8047   6847  11589   1003  -1409     -1  A    O  
ATOM   1066  CB  ALA A 152      54.931 -22.371  -1.882  1.00 81.85      A    C  
ANISOU 1066  CB  ALA A 152     9984   7833  13283   1093  -1794    211  A    C  
ATOM   1067  N   ALA A 153      53.504 -21.867  -4.686  1.00 66.61      A    N  
ANISOU 1067  N   ALA A 153     7932   6113  11262   1006  -1468    -99  A    N  
ATOM   1068  CA  ALA A 153      53.671 -21.656  -6.120  1.00 72.58      A    C  
ANISOU 1068  CA  ALA A 153     8551   7017  12008   1096  -1347   -276  A    C  
ATOM   1069  C   ALA A 153      52.898 -20.438  -6.653  1.00 72.41      A    C  
ANISOU 1069  C   ALA A 153     8443   7212  11856    931  -1190   -274  A    C  
ATOM   1070  O   ALA A 153      53.186 -19.947  -7.745  1.00 76.78      A    O  
ANISOU 1070  O   ALA A 153     8855   7943  12375    993  -1078   -390  A    O  
ATOM   1071  CB  ALA A 153      53.303 -22.917  -6.889  1.00 65.33      A    C  
ANISOU 1071  CB  ALA A 153     7767   5904  11151   1177  -1380   -418  A    C  
ATOM   1072  N   ASN A 154      51.929 -19.952  -5.881  1.00 67.06      A    N  
ANISOU 1072  N   ASN A 154     7854   6525  11099    728  -1180   -142  A    N  
ATOM   1073  CA  ASN A 154      51.182 -18.744  -6.255  1.00 63.07      A    C  
ANISOU 1073  CA  ASN A 154     7277   6217  10470    586  -1043   -125  A    C  
ATOM   1074  C   ASN A 154      51.755 -17.469  -5.651  1.00 64.60      A    C  
ANISOU 1074  C   ASN A 154     7360   6578  10607    549  -1007    -22  A    C  
ATOM   1075  O   ASN A 154      51.201 -16.388  -5.838  1.00 66.55      A    O  
ANISOU 1075  O   ASN A 154     7565   6973  10750    442   -903      6  A    O  
ATOM   1076  CB  ASN A 154      49.716 -18.869  -5.859  1.00 57.66      A    C  
ANISOU 1076  CB  ASN A 154     6733   5456   9722    393  -1035    -58  A    C  
ATOM   1077  CG  ASN A 154      48.963 -19.790  -6.765  1.00 68.55      A    C  
ANISOU 1077  CG  ASN A 154     8188   6738  11121    383  -1030   -180  A    C  
ATOM   1078  ND2 ASN A 154      47.800 -20.265  -6.313  1.00 62.92      A    N  
ANISOU 1078  ND2 ASN A 154     7612   5912  10384    219  -1059   -122  A    N  
ATOM   1079  OD1 ASN A 154      49.421 -20.085  -7.870  1.00 75.70      A    O  
ANISOU 1079  OD1 ASN A 154     9030   7677  12056    515  -1002   -330  A    O  
ATOM   1080  N   VAL A 155      52.845 -17.608  -4.900  1.00 53.57      A    N  
ANISOU 1080  N   VAL A 155     5928   5150   9278    638  -1104     34  A    N  
ATOM   1081  CA  VAL A 155      53.575 -16.462  -4.381  1.00 53.53      A    C  
ANISOU 1081  CA  VAL A 155     5808   5303   9227    610  -1086    114  A    C  
ATOM   1082  C   VAL A 155      54.786 -16.212  -5.275  1.00 64.99      A    C  
ANISOU 1082  C   VAL A 155     7057   6913  10723    758  -1040      8  A    C  
ATOM   1083  O   VAL A 155      55.682 -17.053  -5.374  1.00 72.29      A    O  
ANISOU 1083  O   VAL A 155     7929   7784  11754    927  -1118    -51  A    O  
ATOM   1084  CB  VAL A 155      54.025 -16.709  -2.931  1.00 58.35      A    C  
ANISOU 1084  CB  VAL A 155     6495   5805   9871    596  -1230    251  A    C  
ATOM   1085  CG1 VAL A 155      54.800 -15.526  -2.393  1.00 52.30      A    C  
ANISOU 1085  CG1 VAL A 155     5613   5202   9054    553  -1223    325  A    C  
ATOM   1086  CG2 VAL A 155      52.825 -17.013  -2.052  1.00 57.36      A    C  
ANISOU 1086  CG2 VAL A 155     6572   5531   9692    443  -1264    357  A    C  
ATOM   1087  N   LEU A 156      54.804 -15.067  -5.945  1.00 59.81      A    N  
ANISOU 1087  N   LEU A 156     6290   6455   9981    697   -908    -15  A    N  
ATOM   1088  CA  LEU A 156      55.908 -14.739  -6.840  1.00 60.37      A    C  
ANISOU 1088  CA  LEU A 156     6160   6704  10073    808   -842   -109  A    C  
ATOM   1089  C   LEU A 156      56.919 -13.818  -6.179  1.00 73.94      A    C  
ANISOU 1089  C   LEU A 156     7755   8556  11782    768   -864    -22  A    C  
ATOM   1090  O   LEU A 156      56.583 -13.059  -5.266  1.00 77.17      A    O  
ANISOU 1090  O   LEU A 156     8237   8957  12125    623   -886    100  A    O  
ATOM   1091  CB  LEU A 156      55.387 -14.083  -8.114  1.00 61.40      A    C  
ANISOU 1091  CB  LEU A 156     6246   6977  10107    764   -682   -191  A    C  
ATOM   1092  CG  LEU A 156      54.370 -14.929  -8.879  1.00 68.06      A    C  
ANISOU 1092  CG  LEU A 156     7200   7714  10946    789   -659   -290  A    C  
ATOM   1093  CD1 LEU A 156      54.065 -14.314 -10.230  1.00 64.04      A    C  
ANISOU 1093  CD1 LEU A 156     6625   7369  10338    775   -512   -381  A    C  
ATOM   1094  CD2 LEU A 156      54.888 -16.340  -9.036  1.00 68.34      A    C  
ANISOU 1094  CD2 LEU A 156     7250   7612  11106    965   -748   -390  A    C  
ATOM   1095  N   ILE A 157      58.162 -13.892  -6.643  1.00 82.33      A    N  
ANISOU 1095  N   ILE A 157     8625   9750  12907    896   -858    -92  A    N  
ATOM   1096  CA  ILE A 157      59.201 -12.969  -6.207  1.00 76.48      A    C  
ANISOU 1096  CA  ILE A 157     7730   9175  12154    844   -867    -27  A    C  
ATOM   1097  C   ILE A 157      59.934 -12.432  -7.427  1.00 74.90      A    C  
ANISOU 1097  C   ILE A 157     7324   9205  11929    880   -728   -126  A    C  
ATOM   1098  O   ILE A 157      60.374 -13.204  -8.274  1.00 88.11      A    O  
ANISOU 1098  O   ILE A 157     8901  10914  13665   1050   -698   -253  A    O  
ATOM   1099  CB  ILE A 157      60.170 -13.639  -5.233  1.00 68.32      A    C  
ANISOU 1099  CB  ILE A 157     6638   8088  11231    954  -1037     17  A    C  
ATOM   1100  CG1 ILE A 157      59.388 -14.217  -4.055  1.00 65.77      A    C  
ANISOU 1100  CG1 ILE A 157     6543   7529  10917    908  -1169    122  A    C  
ATOM   1101  CG2 ILE A 157      61.191 -12.636  -4.734  1.00 65.43      A    C  
ANISOU 1101  CG2 ILE A 157     6110   7904  10846    871  -1058     87  A    C  
ATOM   1102  CD1 ILE A 157      60.234 -14.585  -2.873  1.00 71.72      A    C  
ANISOU 1102  CD1 ILE A 157     7275   8235  11740    966  -1349    210  A    C  
ATOM   1103  N   THR A 158      60.027 -11.109  -7.535  1.00 65.78      A    N  
ANISOU 1103  N   THR A 158     6120   8199  10675    719   -638    -68  A    N  
ATOM   1104  CA  THR A 158      60.665 -10.479  -8.694  1.00 73.76      A    C  
ANISOU 1104  CA  THR A 158     6953   9434  11638    715   -493   -141  A    C  
ATOM   1105  C   THR A 158      62.179 -10.462  -8.559  1.00 82.39      A    C  
ANISOU 1105  C   THR A 158     7799  10698  12807    780   -528   -155  A    C  
ATOM   1106  O   THR A 158      62.717 -10.641  -7.459  1.00 73.57      A    O  
ANISOU 1106  O   THR A 158     6656   9538  11759    789   -672    -83  A    O  
ATOM   1107  CB  THR A 158      60.198  -9.022  -8.909  1.00 67.36      A    C  
ANISOU 1107  CB  THR A 158     6200   8708  10685    506   -382    -66  A    C  
ATOM   1108  CG2 THR A 158      58.728  -8.976  -9.157  1.00 59.46      A    C  
ANISOU 1108  CG2 THR A 158     5407   7579   9606    458   -337    -61  A    C  
ATOM   1109  OG1 THR A 158      60.516  -8.232  -7.752  1.00 65.98      A    O  
ANISOU 1109  OG1 THR A 158     6047   8527  10495    365   -462     59  A    O  
ATOM   1110  N   ARG A 159      62.859 -10.232  -9.681  1.00 92.02      A    N  
ANISOU 1110  N   ARG A 159     8832  12127  14004    821   -396   -247  A    N  
ATOM   1111  CA  ARG A 159      64.315 -10.151  -9.693  1.00 94.44      A    C  
ANISOU 1111  CA  ARG A 159     8864  12645  14373    875   -404   -270  A    C  
ATOM   1112  C   ARG A 159      64.792  -9.165  -8.640  1.00 83.13      A    C  
ANISOU 1112  C   ARG A 159     7399  11267  12922    685   -482   -131  A    C  
ATOM   1113  O   ARG A 159      65.925  -9.254  -8.177  1.00 90.46      A    O  
ANISOU 1113  O   ARG A 159     8125  12318  13927    726   -562   -121  A    O  
ATOM   1114  CB  ARG A 159      64.844  -9.735 -11.072  1.00113.97      A    C  
ANISOU 1114  CB  ARG A 159    11157  15365  16782    878   -214   -366  A    C  
ATOM   1115  CG  ARG A 159      64.913 -10.862 -12.106  1.00135.90      A    C  
ANISOU 1115  CG  ARG A 159    13874  18157  19603   1119   -152   -537  A    C  
ATOM   1116  CD  ARG A 159      65.503 -10.371 -13.430  1.00154.31      A    C  
ANISOU 1116  CD  ARG A 159    16020  20761  21849   1107     46   -624  A    C  
ATOM   1117  NE  ARG A 159      64.926 -11.062 -14.585  1.00168.87      A    N  
ANISOU 1117  NE  ARG A 159    17940  22573  23650   1245    145   -768  A    N  
ATOM   1118  CZ  ARG A 159      65.080 -10.672 -15.848  1.00177.96      A    C  
ANISOU 1118  CZ  ARG A 159    19008  23921  24690   1226    327   -846  A    C  
ATOM   1119  NH1 ARG A 159      65.801  -9.593 -16.132  1.00181.48      A    N1+
ANISOU 1119  NH1 ARG A 159    19291  24607  25058   1065    437   -785  A    N1+
ATOM   1120  NH2 ARG A 159      64.512 -11.361 -16.833  1.00177.42      A    N  
ANISOU 1120  NH2 ARG A 159    19028  23808  24578   1354    398   -982  A    N  
ATOM   1121  N   ASP A 160      63.924  -8.235  -8.255  1.00 65.97      A    N  
ANISOU 1121  N   ASP A 160     5423   9001  10643    485   -464    -30  A    N  
ATOM   1122  CA  ASP A 160      64.297  -7.205  -7.293  1.00 71.77      A    C  
ANISOU 1122  CA  ASP A 160     6161   9770  11338    286   -530     93  A    C  
ATOM   1123  C   ASP A 160      63.816  -7.490  -5.872  1.00 77.43      A    C  
ANISOU 1123  C   ASP A 160     7057  10280  12081    268   -703    187  A    C  
ATOM   1124  O   ASP A 160      63.878  -6.620  -5.001  1.00 78.43      A    O  
ANISOU 1124  O   ASP A 160     7250  10396  12152     94   -761    288  A    O  
ATOM   1125  CB  ASP A 160      63.806  -5.843  -7.764  1.00 84.63      A    C  
ANISOU 1125  CB  ASP A 160     7889  11445  12821     70   -396    145  A    C  
ATOM   1126  CG  ASP A 160      64.316  -5.499  -9.144  1.00107.16      A    C  
ANISOU 1126  CG  ASP A 160    10576  14512  15628     66   -223     70  A    C  
ATOM   1127  OD1 ASP A 160      64.975  -6.366  -9.765  1.00107.06      A    O  
ANISOU 1127  OD1 ASP A 160    10371  14612  15693    242   -196    -38  A    O  
ATOM   1128  OD2 ASP A 160      64.063  -4.367  -9.611  1.00118.76      A    O1-
ANISOU 1128  OD2 ASP A 160    12114  16034  16977   -110   -112    116  A    O1-
ATOM   1129  N   GLY A 161      63.336  -8.709  -5.645  1.00 74.69      A    N  
ANISOU 1129  N   GLY A 161     6801   9767  11812    439   -784    151  A    N  
ATOM   1130  CA  GLY A 161      62.995  -9.157  -4.309  1.00 67.78      A    C  
ANISOU 1130  CA  GLY A 161     6081   8705  10967    441   -953    240  A    C  
ATOM   1131  C   GLY A 161      61.656  -8.655  -3.814  1.00 68.11      A    C  
ANISOU 1131  C   GLY A 161     6391   8584  10904    297   -933    317  A    C  
ATOM   1132  O   GLY A 161      61.431  -8.574  -2.607  1.00 75.79      A    O  
ANISOU 1132  O   GLY A 161     7493   9447  11856    226  -1050    415  A    O  
ATOM   1133  N   VAL A 162      60.770  -8.305  -4.740  1.00 60.83      A    N  
ANISOU 1133  N   VAL A 162     5549   7656   9906    260   -785    275  A    N  
ATOM   1134  CA  VAL A 162      59.408  -7.928  -4.373  1.00 59.73      A    C  
ANISOU 1134  CA  VAL A 162     5647   7374   9673    156   -757    333  A    C  
ATOM   1135  C   VAL A 162      58.458  -9.124  -4.515  1.00 61.51      A    C  
ANISOU 1135  C   VAL A 162     5992   7436   9943    272   -778    289  A    C  
ATOM   1136  O   VAL A 162      58.335  -9.704  -5.596  1.00 61.38      A    O  
ANISOU 1136  O   VAL A 162     5920   7443   9957    381   -705    184  A    O  
ATOM   1137  CB  VAL A 162      58.896  -6.752  -5.219  1.00 59.63      A    C  
ANISOU 1137  CB  VAL A 162     5669   7447   9540     38   -597    328  A    C  
ATOM   1138  CG1 VAL A 162      57.536  -6.310  -4.730  1.00 47.83      A    C  
ANISOU 1138  CG1 VAL A 162     4403   5820   7950    -52   -578    391  A    C  
ATOM   1139  CG2 VAL A 162      59.885  -5.587  -5.171  1.00 58.01      A    C  
ANISOU 1139  CG2 VAL A 162     5354   7397   9291    -95   -572    369  A    C  
ATOM   1140  N   LEU A 163      57.811  -9.494  -3.410  1.00 65.88      A    N  
ANISOU 1140  N   LEU A 163     6712   7826  10492    239   -878    369  A    N  
ATOM   1141  CA  LEU A 163      56.827 -10.584  -3.379  1.00 59.42      A    C  
ANISOU 1141  CA  LEU A 163     6032   6838   9708    304   -906    348  A    C  
ATOM   1142  C   LEU A 163      55.461 -10.133  -3.910  1.00 58.72      A    C  
ANISOU 1142  C   LEU A 163     6062   6731   9520    220   -785    337  A    C  
ATOM   1143  O   LEU A 163      54.967  -9.064  -3.544  1.00 52.74      A    O  
ANISOU 1143  O   LEU A 163     5379   6004   8657     91   -735    404  A    O  
ATOM   1144  CB  LEU A 163      56.683 -11.119  -1.956  1.00 50.95      A    C  
ANISOU 1144  CB  LEU A 163     5092   5611   8655    282  -1056    451  A    C  
ATOM   1145  CG  LEU A 163      55.705 -12.276  -1.737  1.00 55.51      A    C  
ANISOU 1145  CG  LEU A 163     5830   5996   9263    317  -1102    454  A    C  
ATOM   1146  CD1 LEU A 163      56.152 -13.142  -0.555  1.00 57.18      A    C  
ANISOU 1146  CD1 LEU A 163     6114   6072   9540    365  -1279    535  A    C  
ATOM   1147  CD2 LEU A 163      54.286 -11.768  -1.538  1.00 46.64      A    C  
ANISOU 1147  CD2 LEU A 163     4860   4833   8027    176  -1019    500  A    C  
ATOM   1148  N   LYS A 164      54.868 -10.944  -4.783  1.00 60.13      A    N  
ANISOU 1148  N   LYS A 164     6257   6862   9729    300   -742    246  A    N  
ATOM   1149  CA  LYS A 164      53.562 -10.632  -5.371  1.00 55.60      A    C  
ANISOU 1149  CA  LYS A 164     5773   6286   9067    235   -640    226  A    C  
ATOM   1150  C   LYS A 164      52.652 -11.816  -5.197  1.00 56.19      A    C  
ANISOU 1150  C   LYS A 164     5966   6199   9186    258   -694    209  A    C  
ATOM   1151  O   LYS A 164      53.036 -12.949  -5.521  1.00 56.50      A    O  
ANISOU 1151  O   LYS A 164     5984   6160   9323    374   -753    135  A    O  
ATOM   1152  CB  LYS A 164      53.663 -10.360  -6.873  1.00 51.11      A    C  
ANISOU 1152  CB  LYS A 164     5099   5852   8470    288   -518    115  A    C  
ATOM   1153  CG  LYS A 164      54.815  -9.484  -7.303  1.00 54.71      A    C  
ANISOU 1153  CG  LYS A 164     5404   6476   8908    286   -461    106  A    C  
ATOM   1154  CD  LYS A 164      54.484  -8.032  -7.139  1.00 54.60      A    C  
ANISOU 1154  CD  LYS A 164     5440   6532   8772    146   -389    188  A    C  
ATOM   1155  CE  LYS A 164      55.424  -7.164  -7.951  1.00 54.63      A    C  
ANISOU 1155  CE  LYS A 164     5307   6713   8738    126   -301    164  A    C  
ATOM   1156  NZ  LYS A 164      55.127  -5.709  -7.701  1.00 59.38      A    N1+
ANISOU 1156  NZ  LYS A 164     5990   7349   9221    -19   -245    253  A    N1+
ATOM   1157  N   LEU A 165      51.444 -11.566  -4.702  1.00 51.06      A    N  
ANISOU 1157  N   LEU A 165     5443   5497   8459    147   -674    273  A    N  
ATOM   1158  CA  LEU A 165      50.406 -12.589  -4.737  1.00 51.85      A    C  
ANISOU 1158  CA  LEU A 165     5646   5472   8583    133   -699    250  A    C  
ATOM   1159  C   LEU A 165      49.967 -12.733  -6.191  1.00 52.21      A    C  
ANISOU 1159  C   LEU A 165     5636   5588   8615    181   -611    124  A    C  
ATOM   1160  O   LEU A 165      49.751 -11.741  -6.878  1.00 58.64      A    O  
ANISOU 1160  O   LEU A 165     6396   6543   9343    157   -508    105  A    O  
ATOM   1161  CB  LEU A 165      49.227 -12.199  -3.858  1.00 59.62      A    C  
ANISOU 1161  CB  LEU A 165     6750   6424   9479     -3   -682    350  A    C  
ATOM   1162  CG  LEU A 165      49.509 -11.939  -2.382  1.00 64.95      A    C  
ANISOU 1162  CG  LEU A 165     7503   7042  10133    -70   -757    477  A    C  
ATOM   1163  CD1 LEU A 165      48.245 -11.473  -1.659  1.00 66.07      A    C  
ANISOU 1163  CD1 LEU A 165     7752   7183  10168   -197   -709    557  A    C  
ATOM   1164  CD2 LEU A 165      50.068 -13.192  -1.754  1.00 70.53      A    C  
ANISOU 1164  CD2 LEU A 165     8263   7590  10944    -18   -896    502  A    C  
ATOM   1165  N   ALA A 166      49.861 -13.964  -6.666  1.00 49.96      A    N  
ANISOU 1165  N   ALA A 166     5377   5198   8407    248   -658     37  A    N  
ATOM   1166  CA  ALA A 166      49.583 -14.211  -8.074  1.00 49.38      A    C  
ANISOU 1166  CA  ALA A 166     5255   5189   8320    304   -588    -99  A    C  
ATOM   1167  C   ALA A 166      48.432 -15.188  -8.231  1.00 55.60      A    C  
ANISOU 1167  C   ALA A 166     6151   5854   9120    250   -621   -140  A    C  
ATOM   1168  O   ALA A 166      47.985 -15.790  -7.245  1.00 53.51      A    O  
ANISOU 1168  O   ALA A 166     5997   5444   8889    177   -701    -62  A    O  
ATOM   1169  CB  ALA A 166      50.829 -14.755  -8.761  1.00 49.19      A    C  
ANISOU 1169  CB  ALA A 166     5133   5179   8379    466   -604   -208  A    C  
ATOM   1170  N   ASP A 167      47.957 -15.355  -9.466  1.00 53.97      A    N  
ANISOU 1170  N   ASP A 167     5918   5711   8878    273   -565   -260  A    N  
ATOM   1171  CA  ASP A 167      46.941 -16.370  -9.751  1.00 65.04      A    C  
ANISOU 1171  CA  ASP A 167     7414   7000  10296    215   -606   -320  A    C  
ATOM   1172  C   ASP A 167      45.622 -16.136  -9.029  1.00 57.99      A    C  
ANISOU 1172  C   ASP A 167     6590   6100   9344     47   -603   -217  A    C  
ATOM   1173  O   ASP A 167      45.315 -16.816  -8.053  1.00 56.88      A    O  
ANISOU 1173  O   ASP A 167     6552   5808   9251    -30   -680   -142  A    O  
ATOM   1174  CB  ASP A 167      47.457 -17.761  -9.392  1.00 74.45      A    C  
ANISOU 1174  CB  ASP A 167     8699   7973  11615    282   -722   -358  A    C  
ATOM   1175  CG  ASP A 167      48.478 -18.265 -10.380  1.00102.76      A    C  
ANISOU 1175  CG  ASP A 167    12224  11562  15258    462   -719   -509  A    C  
ATOM   1176  OD1 ASP A 167      48.127 -18.375 -11.576  1.00108.32      A    O  
ANISOU 1176  OD1 ASP A 167    12904  12337  15914    486   -663   -638  A    O  
ATOM   1177  OD2 ASP A 167      49.629 -18.543  -9.965  1.00114.13      A    O1-
ANISOU 1177  OD2 ASP A 167    13635  12947  16783    587   -772   -500  A    O1-
ATOM   1178  N   PHE A 168      44.838 -15.196  -9.541  1.00 48.64      A    N  
ANISOU 1178  N   PHE A 168     5347   5083   8050     -6   -514   -213  A    N  
ATOM   1179  CA  PHE A 168      43.546 -14.867  -8.959  1.00 58.69      A    C  
ANISOU 1179  CA  PHE A 168     6653   6391   9257   -147   -495   -128  A    C  
ATOM   1180  C   PHE A 168      42.388 -15.556  -9.675  1.00 54.73      A    C  
ANISOU 1180  C   PHE A 168     6165   5893   8735   -224   -505   -210  A    C  
ATOM   1181  O   PHE A 168      41.237 -15.155  -9.534  1.00 58.26      A    O  
ANISOU 1181  O   PHE A 168     6592   6433   9110   -325   -470   -165  A    O  
ATOM   1182  CB  PHE A 168      43.364 -13.338  -8.925  1.00 56.33      A    C  
ANISOU 1182  CB  PHE A 168     6286   6269   8848   -146   -401    -60  A    C  
ATOM   1183  CG  PHE A 168      44.169 -12.675  -7.854  1.00 55.96      A    C  
ANISOU 1183  CG  PHE A 168     6256   6199   8807   -136   -406     50  A    C  
ATOM   1184  CD1 PHE A 168      43.584 -12.331  -6.642  1.00 39.50      A    C  
ANISOU 1184  CD1 PHE A 168     4230   4093   6684   -230   -407    168  A    C  
ATOM   1185  CD2 PHE A 168      45.539 -12.462  -8.026  1.00 54.08      A    C  
ANISOU 1185  CD2 PHE A 168     5972   5965   8612    -36   -412     29  A    C  
ATOM   1186  CE1 PHE A 168      44.346 -11.731  -5.630  1.00 45.33      A    C  
ANISOU 1186  CE1 PHE A 168     4997   4808   7419   -226   -421    262  A    C  
ATOM   1187  CE2 PHE A 168      46.304 -11.870  -7.022  1.00 45.26      A    C  
ANISOU 1187  CE2 PHE A 168     4866   4831   7500    -41   -431    126  A    C  
ATOM   1188  CZ  PHE A 168      45.707 -11.501  -5.823  1.00 45.42      A    C  
ANISOU 1188  CZ  PHE A 168     4962   4820   7475   -137   -441    241  A    C  
ATOM   1189  N   GLY A 169      42.698 -16.606 -10.426  1.00 50.22      A    N  
ANISOU 1189  N   GLY A 169     5628   5224   8230   -175   -558   -334  A    N  
ATOM   1190  CA  GLY A 169      41.704 -17.285 -11.239  1.00 42.70      A    C  
ANISOU 1190  CA  GLY A 169     4694   4275   7257   -251   -578   -434  A    C  
ATOM   1191  C   GLY A 169      40.644 -18.018 -10.444  1.00 48.28      A    C  
ANISOU 1191  C   GLY A 169     5480   4877   7986   -428   -634   -370  A    C  
ATOM   1192  O   GLY A 169      39.597 -18.372 -10.976  1.00 70.87      A    O  
ANISOU 1192  O   GLY A 169     8333   7783  10811   -533   -643   -426  A    O  
ATOM   1193  N   LEU A 170      40.922 -18.258  -9.169  1.00 53.38      A    N  
ANISOU 1193  N   LEU A 170     6204   5392   8686   -472   -674   -250  A    N  
ATOM   1194  CA  LEU A 170      39.945 -18.863  -8.277  1.00 56.16      A    C  
ANISOU 1194  CA  LEU A 170     6636   5658   9045   -659   -714   -163  A    C  
ATOM   1195  C   LEU A 170      39.499 -17.861  -7.221  1.00 57.72      A    C  
ANISOU 1195  C   LEU A 170     6790   5974   9167   -725   -648    -12  A    C  
ATOM   1196  O   LEU A 170      38.697 -18.189  -6.346  1.00 54.38      A    O  
ANISOU 1196  O   LEU A 170     6417   5515   8730   -882   -658     80  A    O  
ATOM   1197  CB  LEU A 170      40.523 -20.090  -7.580  1.00 61.05      A    C  
ANISOU 1197  CB  LEU A 170     7415   6007   9775   -673   -824   -135  A    C  
ATOM   1198  CG  LEU A 170      40.931 -21.314  -8.404  1.00 73.41      A    C  
ANISOU 1198  CG  LEU A 170     9073   7391  11428   -614   -907   -279  A    C  
ATOM   1199  CD1 LEU A 170      41.084 -22.530  -7.487  1.00 72.68      A    C  
ANISOU 1199  CD1 LEU A 170     9169   7018  11429   -684  -1022   -213  A    C  
ATOM   1200  CD2 LEU A 170      39.935 -21.601  -9.506  1.00 69.84      A    C  
ANISOU 1200  CD2 LEU A 170     8589   7017  10933   -703   -894   -404  A    C  
ATOM   1201  N   ALA A 171      40.027 -16.640  -7.288  1.00 47.41      A    N  
ANISOU 1201  N   ALA A 171     5400   4806   7807   -610   -578     11  A    N  
ATOM   1202  CA  ALA A 171      39.629 -15.629  -6.321  1.00 45.67      A    C  
ANISOU 1202  CA  ALA A 171     5155   4692   7508   -656   -513    138  A    C  
ATOM   1203  C   ALA A 171      38.161 -15.211  -6.518  1.00 57.90      A    C  
ANISOU 1203  C   ALA A 171     6623   6411   8965   -759   -447    144  A    C  
ATOM   1204  O   ALA A 171      37.530 -15.517  -7.527  1.00 57.53      A    O  
ANISOU 1204  O   ALA A 171     6520   6432   8908   -781   -451     48  A    O  
ATOM   1205  CB  ALA A 171      40.536 -14.437  -6.396  1.00 41.86      A    C  
ANISOU 1205  CB  ALA A 171     4619   4297   6988   -522   -462    155  A    C  
ATOM   1206  N   ARG A 172      37.634 -14.490  -5.544  1.00 54.75      A    N  
ANISOU 1206  N   ARG A 172     6213   6093   8494   -812   -391    254  A    N  
ATOM   1207  CA  ARG A 172      36.231 -14.163  -5.522  1.00 51.46      A    C  
ANISOU 1207  CA  ARG A 172     5713   5842   7997   -906   -329    272  A    C  
ATOM   1208  C   ARG A 172      35.996 -12.969  -4.595  1.00 51.69      A    C  
ANISOU 1208  C   ARG A 172     5726   5982   7934   -881   -245    373  A    C  
ATOM   1209  O   ARG A 172      36.596 -12.881  -3.526  1.00 53.99      A    O  
ANISOU 1209  O   ARG A 172     6107   6177   8228   -889   -254    459  A    O  
ATOM   1210  CB  ARG A 172      35.449 -15.387  -5.023  1.00 57.68      A    C  
ANISOU 1210  CB  ARG A 172     6549   6543   8822  -1100   -376    299  A    C  
ATOM   1211  CG  ARG A 172      34.252 -15.048  -4.188  1.00 66.75      A    C  
ANISOU 1211  CG  ARG A 172     7644   7832   9887  -1224   -304    388  A    C  
ATOM   1212  CD  ARG A 172      33.463 -16.262  -3.787  1.00 77.45      A    C  
ANISOU 1212  CD  ARG A 172     9041   9116  11274  -1442   -345    417  A    C  
ATOM   1213  NE  ARG A 172      32.070 -15.897  -3.537  1.00 86.48      A    N  
ANISOU 1213  NE  ARG A 172    10052  10478  12328  -1553   -262    450  A    N  
ATOM   1214  CZ  ARG A 172      31.128 -15.852  -4.476  1.00 87.36      A    C  
ANISOU 1214  CZ  ARG A 172    10018  10761  12413  -1584   -250    369  A    C  
ATOM   1215  NH1 ARG A 172      31.416 -16.158  -5.733  1.00 88.79      A    N1+
ANISOU 1215  NH1 ARG A 172    10183  10911  12641  -1521   -313    247  A    N1+
ATOM   1216  NH2 ARG A 172      29.893 -15.505  -4.159  1.00 92.94      A    N  
ANISOU 1216  NH2 ARG A 172    10588  11682  13041  -1676   -173    406  A    N  
ATOM   1217  N   ALA A 173      35.127 -12.051  -5.004  1.00 54.16      A    N  
ANISOU 1217  N   ALA A 173     5929   6493   8156   -841   -168    358  A    N  
ATOM   1218  CA  ALA A 173      34.658 -10.988  -4.108  1.00 54.94      A    C  
ANISOU 1218  CA  ALA A 173     6015   6701   8158   -821    -82    443  A    C  
ATOM   1219  C   ALA A 173      33.787 -11.556  -2.984  1.00 51.33      A    C  
ANISOU 1219  C   ALA A 173     5572   6254   7679   -985    -61    522  A    C  
ATOM   1220  O   ALA A 173      33.088 -12.550  -3.172  1.00 52.67      A    O  
ANISOU 1220  O   ALA A 173     5706   6423   7883  -1121    -92    502  A    O  
ATOM   1221  CB  ALA A 173      33.877  -9.947  -4.891  1.00 44.92      A    C  
ANISOU 1221  CB  ALA A 173     4627   5636   6804   -721    -14    402  A    C  
ATOM   1222  N   PHE A 174      33.823 -10.931  -1.814  1.00 53.04      A    N  
ANISOU 1222  N   PHE A 174     5846   6480   7829   -983     -6    611  A    N  
ATOM   1223  CA  PHE A 174      32.968 -11.368  -0.714  1.00 54.58      A    C  
ANISOU 1223  CA  PHE A 174     6051   6710   7976  -1138     33    692  A    C  
ATOM   1224  C   PHE A 174      32.241 -10.189  -0.084  1.00 66.06      A    C  
ANISOU 1224  C   PHE A 174     7453   8343   9304  -1079    151    731  A    C  
ATOM   1225  O   PHE A 174      32.484  -9.035  -0.448  1.00 67.68      A    O  
ANISOU 1225  O   PHE A 174     7642   8610   9465   -915    189    700  A    O  
ATOM   1226  CB  PHE A 174      33.766 -12.157   0.340  1.00 59.74      A    C  
ANISOU 1226  CB  PHE A 174     6869   7159   8671  -1233    -33    777  A    C  
ATOM   1227  CG  PHE A 174      34.685 -11.308   1.195  1.00 69.93      A    C  
ANISOU 1227  CG  PHE A 174     8265   8390   9914  -1141    -24    835  A    C  
ATOM   1228  CD1 PHE A 174      35.974 -10.994   0.767  1.00 67.25      A    C  
ANISOU 1228  CD1 PHE A 174     7974   7944   9633  -1014    -87    800  A    C  
ATOM   1229  CD2 PHE A 174      34.274 -10.851   2.438  1.00 68.35      A    C  
ANISOU 1229  CD2 PHE A 174     8115   8249   9606  -1190     47    920  A    C  
ATOM   1230  CE1 PHE A 174      36.830 -10.233   1.561  1.00 59.79      A    C  
ANISOU 1230  CE1 PHE A 174     7123   6950   8645   -951    -90    853  A    C  
ATOM   1231  CE2 PHE A 174      35.128 -10.084   3.233  1.00 65.69      A    C  
ANISOU 1231  CE2 PHE A 174     7890   7853   9218  -1117     44    966  A    C  
ATOM   1232  CZ  PHE A 174      36.408  -9.780   2.790  1.00 63.52      A    C  
ANISOU 1232  CZ  PHE A 174     7660   7468   9008  -1004    -30    934  A    C  
ATOM   1233  N   SER A 175      31.350 -10.485   0.859  1.00 86.88      A    N  
ANISOU 1233  N   SER A 175    10071  11059  11878  -1212    212    797  A    N  
ATOM   1234  CA  SER A 175      30.529  -9.459   1.497  1.00 98.05      A    C  
ANISOU 1234  CA  SER A 175    11426  12663  13168  -1155    336    823  A    C  
ATOM   1235  C   SER A 175      29.990  -9.911   2.848  1.00107.29      A    C  
ANISOU 1235  C   SER A 175    12640  13860  14267  -1318    393    918  A    C  
ATOM   1236  O   SER A 175      30.564 -10.784   3.503  1.00102.97      A    O  
ANISOU 1236  O   SER A 175    12228  13141  13756  -1448    329    985  A    O  
ATOM   1237  CB  SER A 175      29.355  -9.100   0.593  1.00 95.46      A    C  
ANISOU 1237  CB  SER A 175    10893  12564  12812  -1102    389    754  A    C  
ATOM   1238  OG  SER A 175      28.614 -10.265   0.279  1.00 93.82      A    O  
ANISOU 1238  OG  SER A 175    10591  12401  12655  -1286    357    744  A    O  
ATOM   1239  N   LEU A 176      28.880  -9.297   3.253  1.00124.29      A    N  
ANISOU 1239  N   LEU A 176    14679  16235  16311  -1302    518    924  A    N  
ATOM   1240  CA  LEU A 176      28.159  -9.678   4.465  1.00136.59      A    C  
ANISOU 1240  CA  LEU A 176    16241  17876  17779  -1464    602   1008  A    C  
ATOM   1241  C   LEU A 176      26.655  -9.563   4.245  1.00139.06      A    C  
ANISOU 1241  C   LEU A 176    16324  18477  18035  -1499    708    979  A    C  
ATOM   1242  O   LEU A 176      26.153  -8.473   3.987  1.00141.58      A    O  
ANISOU 1242  O   LEU A 176    16535  18970  18290  -1317    787    926  A    O  
ATOM   1243  CB  LEU A 176      28.565  -8.788   5.642  1.00139.42      A    C  
ANISOU 1243  CB  LEU A 176    16739  18213  18019  -1380    669   1057  A    C  
ATOM   1244  CG  LEU A 176      29.853  -9.128   6.393  1.00142.00      A    C  
ANISOU 1244  CG  LEU A 176    17296  18291  18367  -1425    577   1126  A    C  
ATOM   1245  CD1 LEU A 176      29.889  -8.392   7.721  1.00140.22      A    C  
ANISOU 1245  CD1 LEU A 176    17186  18100  17989  -1399    663   1181  A    C  
ATOM   1246  CD2 LEU A 176      29.954 -10.627   6.621  1.00146.55      A    C  
ANISOU 1246  CD2 LEU A 176    17932  18734  19015  -1649    494   1196  A    C  
ATOM   1247  N   PRO A 182      23.357 -14.679   4.672  1.00133.24      A    N  
ANISOU 1247  N   PRO A 182    15288  17939  17398  -2684    687   1158  A    N  
ATOM   1248  CA  PRO A 182      23.987 -15.988   4.871  1.00132.58      A    C  
ANISOU 1248  CA  PRO A 182    15417  17559  17397  -2894    568   1223  A    C  
ATOM   1249  C   PRO A 182      24.649 -16.461   3.577  1.00129.22      A    C  
ANISOU 1249  C   PRO A 182    15035  16942  17121  -2829    409   1123  A    C  
ATOM   1250  O   PRO A 182      23.990 -17.102   2.757  1.00135.17      A    O  
ANISOU 1250  O   PRO A 182    15669  17758  17932  -2964    364   1065  A    O  
ATOM   1251  CB  PRO A 182      22.802 -16.900   5.226  1.00134.85      A    C  
ANISOU 1251  CB  PRO A 182    15597  17990  17649  -3222    623   1285  A    C  
ATOM   1252  CG  PRO A 182      21.640 -15.969   5.511  1.00134.55      A    C  
ANISOU 1252  CG  PRO A 182    15294  18342  17487  -3168    798   1270  A    C  
ATOM   1253  CD  PRO A 182      21.888 -14.769   4.667  1.00133.50      A    C  
ANISOU 1253  CD  PRO A 182    15058  18295  17369  -2832    794   1153  A    C  
ATOM   1254  N   ASN A 183      25.930 -16.145   3.396  1.00115.42      A    N  
ANISOU 1254  N   ASN A 183    13451  14976  15428  -2629    328   1099  A    N  
ATOM   1255  CA  ASN A 183      26.632 -16.440   2.146  1.00103.61      A    C  
ANISOU 1255  CA  ASN A 183    11988  13323  14058  -2525    197    993  A    C  
ATOM   1256  C   ASN A 183      26.805 -17.934   1.869  1.00 99.96      A    C  
ANISOU 1256  C   ASN A 183    11652  12627  13700  -2737     72    998  A    C  
ATOM   1257  O   ASN A 183      27.102 -18.712   2.775  1.00100.27      A    O  
ANISOU 1257  O   ASN A 183    11873  12483  13743  -2890     40   1104  A    O  
ATOM   1258  CB  ASN A 183      28.005 -15.761   2.128  1.00100.72      A    C  
ANISOU 1258  CB  ASN A 183    11760  12790  13719  -2277    151    977  A    C  
ATOM   1259  CG  ASN A 183      27.914 -14.244   2.127  1.00 92.86      A    C  
ANISOU 1259  CG  ASN A 183    10658  11990  12635  -2049    252    946  A    C  
ATOM   1260  ND2 ASN A 183      28.894 -13.594   2.748  1.00 88.09      A    N  
ANISOU 1260  ND2 ASN A 183    10192  11275  12002  -1909    253    986  A    N  
ATOM   1261  OD1 ASN A 183      26.984 -13.665   1.566  1.00 87.06      A    O  
ANISOU 1261  OD1 ASN A 183     9724  11497  11857  -1997    320    887  A    O  
ATOM   1262  N   ARG A 184      26.623 -18.325   0.611  1.00 94.11      A    N  
ANISOU 1262  N   ARG A 184    10832  11887  13039  -2739     -4    880  A    N  
ATOM   1263  CA  ARG A 184      26.842 -19.707   0.203  1.00100.51      A    C  
ANISOU 1263  CA  ARG A 184    11781  12455  13955  -2912   -133    858  A    C  
ATOM   1264  C   ARG A 184      27.923 -19.768  -0.857  1.00102.74      A    C  
ANISOU 1264  C   ARG A 184    12144  12555  14337  -2710   -244    741  A    C  
ATOM   1265  O   ARG A 184      27.642 -20.066  -2.017  1.00107.62      A    O  
ANISOU 1265  O   ARG A 184    12684  13205  15001  -2716   -300    619  A    O  
ATOM   1266  CB  ARG A 184      25.567 -20.335  -0.365  1.00102.97      A    C  
ANISOU 1266  CB  ARG A 184    11935  12921  14266  -3149   -134    810  A    C  
ATOM   1267  CG  ARG A 184      24.598 -20.876   0.662  1.00109.27      A    C  
ANISOU 1267  CG  ARG A 184    12712  13807  14997  -3450    -62    935  A    C  
ATOM   1268  CD  ARG A 184      23.338 -21.368  -0.025  1.00120.43      A    C  
ANISOU 1268  CD  ARG A 184    13929  15417  16413  -3676    -66    873  A    C  
ATOM   1269  NE  ARG A 184      22.313 -21.780   0.928  1.00136.65      A    N  
ANISOU 1269  NE  ARG A 184    15917  17612  18390  -3975     26    991  A    N  
ATOM   1270  CZ  ARG A 184      21.136 -22.292   0.578  1.00151.37      A    C  
ANISOU 1270  CZ  ARG A 184    17605  19664  20246  -4234     34    966  A    C  
ATOM   1271  NH1 ARG A 184      20.835 -22.452  -0.705  1.00155.93      A    N1+
ANISOU 1271  NH1 ARG A 184    18063  20301  20882  -4222    -53    824  A    N1+
ATOM   1272  NH2 ARG A 184      20.256 -22.647   1.508  1.00154.32      A    N  
ANISOU 1272  NH2 ARG A 184    17917  20176  20543  -4514    130   1084  A    N  
ATOM   1273  N   TYR A 185      29.159 -19.485  -0.462  1.00 97.39      A    N  
ANISOU 1273  N   TYR A 185    11618  11700  13685  -2534   -275    773  A    N  
ATOM   1274  CA  TYR A 185      30.273 -19.555  -1.396  1.00 89.38      A    C  
ANISOU 1274  CA  TYR A 185    10676  10522  12763  -2339   -369    667  A    C  
ATOM   1275  C   TYR A 185      30.628 -21.012  -1.636  1.00 88.05      A    C  
ANISOU 1275  C   TYR A 185    10686  10067  12701  -2466   -501    642  A    C  
ATOM   1276  O   TYR A 185      30.310 -21.875  -0.824  1.00 93.70      A    O  
ANISOU 1276  O   TYR A 185    11522  10659  13419  -2679   -525    741  A    O  
ATOM   1277  CB  TYR A 185      31.484 -18.782  -0.868  1.00 83.65      A    C  
ANISOU 1277  CB  TYR A 185    10036   9717  12030  -2123   -362    711  A    C  
ATOM   1278  CG  TYR A 185      31.197 -17.332  -0.542  1.00 82.44      A    C  
ANISOU 1278  CG  TYR A 185     9749   9806  11768  -1997   -237    739  A    C  
ATOM   1279  CD1 TYR A 185      30.301 -16.592  -1.310  1.00 79.42      A    C  
ANISOU 1279  CD1 TYR A 185     9164   9681  11332  -1949   -165    665  A    C  
ATOM   1280  CD2 TYR A 185      31.830 -16.696   0.525  1.00 80.52      A    C  
ANISOU 1280  CD2 TYR A 185     9592   9527  11473  -1918   -202    834  A    C  
ATOM   1281  CE1 TYR A 185      30.038 -15.260  -1.023  1.00 77.69      A    C  
ANISOU 1281  CE1 TYR A 185     8843   9662  11014  -1816    -57    687  A    C  
ATOM   1282  CE2 TYR A 185      31.575 -15.362   0.824  1.00 74.99      A    C  
ANISOU 1282  CE2 TYR A 185     8795   9028  10670  -1800    -92    849  A    C  
ATOM   1283  CZ  TYR A 185      30.680 -14.651   0.043  1.00 76.66      A    C  
ANISOU 1283  CZ  TYR A 185     8815   9476  10834  -1742    -18    775  A    C  
ATOM   1284  OH  TYR A 185      30.412 -13.332   0.326  1.00 72.72      A    O  
ANISOU 1284  OH  TYR A 185     8239   9157  10235  -1608     86    785  A    O  
HETATM 1285  N   TPO A 186      31.285 -21.281  -2.756  1.00 84.95      A    N  
ANISOU 1285  N   TPO A 186    10321   9566  12389  -2333   -582    509  A    N  
HETATM 1286  CA  TPO A 186      31.675 -22.672  -3.134  1.00 86.63      A    C  
ANISOU 1286  CA  TPO A 186    10717   9490  12710  -2417   -715    455  A    C  
HETATM 1287  C   TPO A 186      32.763 -23.252  -2.254  1.00 91.82      A    C  
ANISOU 1287  C   TPO A 186    11601   9857  13428  -2370   -790    546  A    C  
HETATM 1288  O   TPO A 186      33.667 -22.542  -1.801  1.00 83.48      A    O  
ANISOU 1288  O   TPO A 186    10558   8799  12363  -2183   -771    592  A    O  
HETATM 1289  CB  TPO A 186      32.038 -22.584  -4.610  1.00 82.32      A    C  
ANISOU 1289  CB  TPO A 186    10107   8965  12207  -2254   -755    274  A    C  
HETATM 1290  CG2 TPO A 186      33.075 -23.615  -5.037  1.00 71.45      A    C  
ANISOU 1290  CG2 TPO A 186     8929   7274  10944  -2175   -880    194  A    C  
HETATM 1291  OG1 TPO A 186      32.533 -21.261  -4.790  1.00 91.79      A    O  
ANISOU 1291  OG1 TPO A 186    11181  10339  13357  -2022   -676    264  A    O  
HETATM 1292  P   TPO A 186      32.125 -20.314  -6.026  1.00 84.75      A    P  
ANISOU 1292  P   TPO A 186    10085   9711  12405  -1898   -621    143  A    P  
HETATM 1293  O1P TPO A 186      33.242 -20.512  -7.035  1.00 71.11      A    O  
ANISOU 1293  O1P TPO A 186     8422   7852  10743  -1707   -684     15  A    O  
HETATM 1294  O2P TPO A 186      30.788 -20.856  -6.472  1.00106.18      A    O1-
ANISOU 1294  O2P TPO A 186    12708  12540  15094  -2116   -633     98  A    O1-
HETATM 1295  O3P TPO A 186      32.046 -18.961  -5.361  1.00 77.23      A    O  
ANISOU 1295  O3P TPO A 186     9025   8954  11365  -1796   -508    238  A    O  
ATOM   1296  N   ASN A 187      32.610 -24.527  -1.917  1.00 95.68      A    N  
ANISOU 1296  N   ASN A 187    12279  10094  13979  -2545   -888    575  A    N  
ATOM   1297  CA  ASN A 187      33.524 -25.191  -0.998  1.00100.57      A    C  
ANISOU 1297  CA  ASN A 187    13135  10430  14647  -2540   -973    690  A    C  
ATOM   1298  C   ASN A 187      34.618 -25.863  -1.800  1.00105.79      A    C  
ANISOU 1298  C   ASN A 187    13947  10816  15431  -2341  -1101    591  A    C  
ATOM   1299  O   ASN A 187      35.565 -26.425  -1.248  1.00104.40      A    O  
ANISOU 1299  O   ASN A 187    13914  10457  15296  -2221  -1167    667  A    O  
ATOM   1300  CB  ASN A 187      32.778 -26.225  -0.154  1.00110.35      A    C  
ANISOU 1300  CB  ASN A 187    14518  11538  15870  -2860  -1003    805  A    C  
ATOM   1301  CG  ASN A 187      33.604 -26.728   1.014  1.00111.02      A    C  
ANISOU 1301  CG  ASN A 187    14820  11411  15950  -2887  -1055    980  A    C  
ATOM   1302  ND2 ASN A 187      32.965 -26.873   2.170  1.00108.62      A    N  
ANISOU 1302  ND2 ASN A 187    14767  10781  15721  -2996  -1183   1015  A    N  
ATOM   1303  OD1 ASN A 187      34.801 -26.982   0.881  1.00114.50      A    O  
ANISOU 1303  OD1 ASN A 187    15216  11976  16313  -2814   -986   1084  A    O  
ATOM   1304  N   ARG A 188      34.493 -25.810  -3.120  1.00115.50      A    N  
ANISOU 1304  N   ARG A 188    15141  12029  16714  -2300  -1138    416  A    N  
ATOM   1305  CA  ARG A 188      35.525 -26.351  -3.996  1.00122.39      A    C  
ANISOU 1305  CA  ARG A 188    16142  12666  17697  -2098  -1245    294  A    C  
ATOM   1306  C   ARG A 188      36.652 -25.331  -4.103  1.00112.62      A    C  
ANISOU 1306  C   ARG A 188    14811  11508  16471  -1791  -1216    263  A    C  
ATOM   1307  O   ARG A 188      37.026 -24.916  -5.200  1.00115.58      A    O  
ANISOU 1307  O   ARG A 188    15169  11843  16904  -1596  -1247    114  A    O  
ATOM   1308  CB  ARG A 188      34.951 -26.646  -5.382  1.00133.83      A    C  
ANISOU 1308  CB  ARG A 188    17546  14133  19170  -2123  -1269    100  A    C  
ATOM   1309  CG  ARG A 188      36.001 -26.807  -6.469  1.00137.97      A    C  
ANISOU 1309  CG  ARG A 188    17806  15001  19616  -2034  -1159      4  A    C  
ATOM   1310  CD  ARG A 188      35.689 -25.933  -7.672  1.00143.43      A    C  
ANISOU 1310  CD  ARG A 188    18473  15680  20346  -1850  -1191   -202  A    C  
ATOM   1311  NE  ARG A 188      36.466 -26.320  -8.846  1.00146.52      A    N  
ANISOU 1311  NE  ARG A 188    18888  15994  20789  -1560  -1203   -232  A    N  
ATOM   1312  CZ  ARG A 188      37.523 -25.651  -9.295  1.00143.90      A    C  
ANISOU 1312  CZ  ARG A 188    18501  15703  20473  -1353  -1198   -393  A    C  
ATOM   1313  NH1 ARG A 188      37.934 -24.556  -8.669  1.00146.28      A    N1+
ANISOU 1313  NH1 ARG A 188    18733  16113  20733  -1397  -1189   -541  A    N1+
ATOM   1314  NH2 ARG A 188      38.171 -26.076 -10.372  1.00137.23      A    N  
ANISOU 1314  NH2 ARG A 188    17661  14803  19676  -1107  -1202   -407  A    N  
ATOM   1315  N   VAL A 189      37.184 -24.924  -2.954  1.00101.54      A    N  
ANISOU 1315  N   VAL A 189    13349  10225  15008  -1753  -1154    399  A    N  
ATOM   1316  CA  VAL A 189      38.187 -23.868  -2.915  1.00 88.42      A    C  
ANISOU 1316  CA  VAL A 189    11565   8693  13338  -1502  -1110    369  A    C  
ATOM   1317  C   VAL A 189      39.472 -24.229  -2.174  1.00 82.24      A    C  
ANISOU 1317  C   VAL A 189    10909   7721  12618  -1351  -1196    447  A    C  
ATOM   1318  O   VAL A 189      39.446 -24.820  -1.094  1.00 77.34      A    O  
ANISOU 1318  O   VAL A 189    10451   6933  12001  -1458  -1260    585  A    O  
ATOM   1319  CB  VAL A 189      37.614 -22.567  -2.324  1.00 88.06      A    C  
ANISOU 1319  CB  VAL A 189    11340   8946  13173  -1533   -974    437  A    C  
ATOM   1320  CG1 VAL A 189      36.682 -21.897  -3.321  1.00 83.16      A    C  
ANISOU 1320  CG1 VAL A 189    10551   8544  12499  -1586   -897    326  A    C  
ATOM   1321  CG2 VAL A 189      36.892 -22.851  -1.016  1.00 90.40      A    C  
ANISOU 1321  CG2 VAL A 189    11708   9241  13400  -1733   -951    614  A    C  
ATOM   1322  N   VAL A 190      40.594 -23.853  -2.778  1.00 83.43      A    N  
ANISOU 1322  N   VAL A 190    10980   7908  12812  -1105  -1201    359  A    N  
ATOM   1323  CA  VAL A 190      41.928 -23.993  -2.184  1.00 82.29      A    C  
ANISOU 1323  CA  VAL A 190    10910   7626  12734   -927  -1287    410  A    C  
ATOM   1324  C   VAL A 190      42.491 -25.397  -2.364  1.00 82.67      A    C  
ANISOU 1324  C   VAL A 190    11144   7365  12902   -858  -1428    358  A    C  
ATOM   1325  O   VAL A 190      41.813 -26.381  -2.087  1.00 82.09      A    O  
ANISOU 1325  O   VAL A 190    11239   7105  12846  -1029  -1489    399  A    O  
ATOM   1326  CB  VAL A 190      41.938 -23.662  -0.668  1.00 71.29      A    C  
ANISOU 1326  CB  VAL A 190     9584   6228  11278  -1014  -1297    609  A    C  
ATOM   1327  CG1 VAL A 190      43.374 -23.688  -0.114  1.00 61.37      A    C  
ANISOU 1327  CG1 VAL A 190     8372   4863  10081   -815  -1395    656  A    C  
ATOM   1328  CG2 VAL A 190      41.235 -22.320  -0.385  1.00 55.17      A    C  
ANISOU 1328  CG2 VAL A 190     7386   4471   9106  -1097  -1154    662  A    C  
ATOM   1329  N   THR A 191      43.737 -25.487  -2.817  1.00 86.78      A    N  
ANISOU 1329  N   THR A 191    11637   7830  13505   -606  -1480    271  A    N  
ATOM   1330  CA  THR A 191      44.417 -26.772  -2.908  1.00 84.38      A    C  
ANISOU 1330  CA  THR A 191    11514   7225  13321   -489  -1620    221  A    C  
ATOM   1331  C   THR A 191      44.334 -27.501  -1.576  1.00 89.88      A    C  
ANISOU 1331  C   THR A 191    12429   7693  14028   -603  -1731    404  A    C  
ATOM   1332  O   THR A 191      44.433 -26.885  -0.512  1.00 88.77      A    O  
ANISOU 1332  O   THR A 191    12269   7636  13824   -651  -1721    561  A    O  
ATOM   1333  CB  THR A 191      45.886 -26.604  -3.298  1.00 89.52      A    C  
ANISOU 1333  CB  THR A 191    12073   7892  14050   -184  -1655    135  A    C  
ATOM   1334  CG2 THR A 191      46.684 -27.858  -2.958  1.00 98.87      A    C  
ANISOU 1334  CG2 THR A 191    13457   8757  15353    -41  -1820    140  A    C  
ATOM   1335  OG1 THR A 191      45.969 -26.362  -4.705  1.00 90.14      A    O  
ANISOU 1335  OG1 THR A 191    12014   8104  14133    -78  -1574    -61  A    O  
ATOM   1336  N   LEU A 192      44.152 -28.817  -1.643  1.00 90.83      A    N  
ANISOU 1336  N   LEU A 192    12774   7517  14221   -650  -1842    383  A    N  
ATOM   1337  CA  LEU A 192      43.937 -29.635  -0.455  1.00 90.28      A    C  
ANISOU 1337  CA  LEU A 192    12950   7200  14155   -791  -1951    562  A    C  
ATOM   1338  C   LEU A 192      44.937 -29.401   0.695  1.00 84.98      A    C  
ANISOU 1338  C   LEU A 192    12312   6490  13485   -656  -2032    714  A    C  
ATOM   1339  O   LEU A 192      44.536 -29.285   1.854  1.00 92.64      A    O  
ANISOU 1339  O   LEU A 192    13370   7454  14374   -826  -2041    901  A    O  
ATOM   1340  CB  LEU A 192      43.907 -31.121  -0.831  1.00 87.60      A    C  
ANISOU 1340  CB  LEU A 192    12865   6503  13916   -793  -2081    492  A    C  
ATOM   1341  CG  LEU A 192      43.562 -32.049   0.336  1.00 92.88      A    C  
ANISOU 1341  CG  LEU A 192    13823   6890  14578   -976  -2196    684  A    C  
ATOM   1342  CD1 LEU A 192      42.082 -31.941   0.713  1.00 87.48      A    C  
ANISOU 1342  CD1 LEU A 192    13155   6301  13785  -1352  -2104    784  A    C  
ATOM   1343  CD2 LEU A 192      43.954 -33.492   0.023  1.00105.76      A    C  
ANISOU 1343  CD2 LEU A 192    15730   8122  16332   -882  -2357    616  A    C  
ATOM   1344  N   TRP A 193      46.229 -29.342   0.384  1.00 65.37      A    N  
ANISOU 1344  N   TRP A 193     9756   3995  11087   -358  -2093    636  A    N  
ATOM   1345  CA  TRP A 193      47.241 -29.244   1.437  1.00 75.63      A    C  
ANISOU 1345  CA  TRP A 193    11092   5245  12399   -218  -2199    773  A    C  
ATOM   1346  C   TRP A 193      47.195 -27.906   2.173  1.00 83.41      A    C  
ANISOU 1346  C   TRP A 193    11910   6518  13265   -295  -2105    887  A    C  
ATOM   1347  O   TRP A 193      47.668 -27.775   3.311  1.00 76.99      A    O  
ANISOU 1347  O   TRP A 193    11161   5676  12416   -284  -2186   1044  A    O  
ATOM   1348  CB  TRP A 193      48.641 -29.462   0.866  1.00 83.16      A    C  
ANISOU 1348  CB  TRP A 193    11966   6155  13474    126  -2280    649  A    C  
ATOM   1349  CG  TRP A 193      48.852 -30.819   0.276  1.00 87.64      A    C  
ANISOU 1349  CG  TRP A 193    12727   6410  14162    250  -2393    540  A    C  
ATOM   1350  CD1 TRP A 193      48.036 -31.915   0.403  1.00 89.39      A    C  
ANISOU 1350  CD1 TRP A 193    13222   6344  14398     77  -2461    574  A    C  
ATOM   1351  CD2 TRP A 193      49.968 -31.239  -0.511  1.00 87.23      A    C  
ANISOU 1351  CD2 TRP A 193    12621   6293  14232    575  -2453    376  A    C  
ATOM   1352  CE2 TRP A 193      49.761 -32.597  -0.841  1.00 92.48      A    C  
ANISOU 1352  CE2 TRP A 193    13548   6611  14980    598  -2558    309  A    C  
ATOM   1353  CE3 TRP A 193      51.120 -30.600  -0.975  1.00 83.99      A    C  
ANISOU 1353  CE3 TRP A 193    11962   6086  13863    843  -2422    277  A    C  
ATOM   1354  NE1 TRP A 193      48.573 -32.983  -0.274  1.00 90.26      A    N  
ANISOU 1354  NE1 TRP A 193    13469   6193  14632    280  -2565    436  A    N  
ATOM   1355  CZ2 TRP A 193      50.667 -33.325  -1.608  1.00 88.10      A    C  
ANISOU 1355  CZ2 TRP A 193    13019   5907  14547    905  -2633    138  A    C  
ATOM   1356  CZ3 TRP A 193      52.019 -31.326  -1.739  1.00 90.54      A    C  
ANISOU 1356  CZ3 TRP A 193    12795   6792  14813   1139  -2488    112  A    C  
ATOM   1357  CH2 TRP A 193      51.790 -32.674  -2.044  1.00 87.05      A    C  
ANISOU 1357  CH2 TRP A 193    12623   6003  14451   1179  -2592     41  A    C  
ATOM   1358  N   TYR A 194      46.620 -26.909   1.513  1.00 79.45      A    N  
ANISOU 1358  N   TYR A 194    11205   6287  12695   -369  -1941    804  A    N  
ATOM   1359  CA  TYR A 194      46.561 -25.587   2.091  1.00 76.54      A    C  
ANISOU 1359  CA  TYR A 194    10684   6183  12214   -429  -1844    887  A    C  
ATOM   1360  C   TYR A 194      45.161 -25.268   2.600  1.00 75.88      A    C  
ANISOU 1360  C   TYR A 194    10638   6190  12005   -716  -1741    983  A    C  
ATOM   1361  O   TYR A 194      44.941 -24.224   3.219  1.00 67.66      A    O  
ANISOU 1361  O   TYR A 194     9509   5347  10854   -789  -1658   1064  A    O  
ATOM   1362  CB  TYR A 194      47.034 -24.556   1.071  1.00 76.62      A    C  
ANISOU 1362  CB  TYR A 194    10437   6445  12230   -282  -1736    739  A    C  
ATOM   1363  CG  TYR A 194      48.509 -24.662   0.754  1.00 82.35      A    C  
ANISOU 1363  CG  TYR A 194    11084   7146  13060     -4  -1820    666  A    C  
ATOM   1364  CD1 TYR A 194      49.434 -23.850   1.405  1.00 89.71      A    C  
ANISOU 1364  CD1 TYR A 194    11909   8208  13968     88  -1845    739  A    C  
ATOM   1365  CD2 TYR A 194      48.981 -25.569  -0.187  1.00 77.46      A    C  
ANISOU 1365  CD2 TYR A 194    10490   6383  12559    165  -1876    519  A    C  
ATOM   1366  CE1 TYR A 194      50.788 -23.937   1.127  1.00 89.95      A    C  
ANISOU 1366  CE1 TYR A 194    11838   8245  14094    335  -1921    673  A    C  
ATOM   1367  CE2 TYR A 194      50.335 -25.665  -0.473  1.00 80.79      A    C  
ANISOU 1367  CE2 TYR A 194    10817   6806  13075    433  -1944    446  A    C  
ATOM   1368  CZ  TYR A 194      51.235 -24.843   0.186  1.00 87.03      A    C  
ANISOU 1368  CZ  TYR A 194    11478   7746  13843    515  -1965    527  A    C  
ATOM   1369  OH  TYR A 194      52.588 -24.909  -0.089  1.00 86.04      A    O  
ANISOU 1369  OH  TYR A 194    11226   7654  13810    773  -2030    457  A    O  
ATOM   1370  N   ARG A 195      44.220 -26.181   2.364  1.00 76.93      A    N  
ANISOU 1370  N   ARG A 195    10905   6174  12151   -883  -1748    973  A    N  
ATOM   1371  CA  ARG A 195      42.823 -25.919   2.702  1.00 81.02      A    C  
ANISOU 1371  CA  ARG A 195    11422   6807  12555  -1160  -1638   1045  A    C  
ATOM   1372  C   ARG A 195      42.568 -25.938   4.206  1.00 78.57      A    C  
ANISOU 1372  C   ARG A 195    11253   6454  12145  -1316  -1664   1257  A    C  
ATOM   1373  O   ARG A 195      42.958 -26.874   4.887  1.00 87.67      A    O  
ANISOU 1373  O   ARG A 195    12620   7355  13335  -1322  -1801   1360  A    O  
ATOM   1374  CB  ARG A 195      41.885 -26.891   1.987  1.00 82.01      A    C  
ANISOU 1374  CB  ARG A 195    11636   6803  12720  -1317  -1642    968  A    C  
ATOM   1375  CG  ARG A 195      40.415 -26.575   2.225  1.00 84.54      A    C  
ANISOU 1375  CG  ARG A 195    11907   7290  12926  -1603  -1518   1027  A    C  
ATOM   1376  CD  ARG A 195      39.532 -27.585   1.543  1.00 81.26      A    C  
ANISOU 1376  CD  ARG A 195    11579   6742  12553  -1778  -1538    953  A    C  
ATOM   1377  NE  ARG A 195      39.926 -27.723   0.152  1.00 82.70      A    N  
ANISOU 1377  NE  ARG A 195    11682   6915  12828  -1606  -1554    747  A    N  
ATOM   1378  CZ  ARG A 195      39.825 -28.844  -0.547  1.00 84.72      A    C  
ANISOU 1378  CZ  ARG A 195    12076   6943  13170  -1633  -1640    644  A    C  
ATOM   1379  NH1 ARG A 195      39.340 -29.945   0.017  1.00 89.07      A    N1+
ANISOU 1379  NH1 ARG A 195    12862   7243  13736  -1836  -1725    738  A    N1+
ATOM   1380  NH2 ARG A 195      40.220 -28.862  -1.813  1.00 79.72      A    N  
ANISOU 1380  NH2 ARG A 195    11360   6332  12601  -1461  -1640    447  A    N  
ATOM   1381  N   PRO A 196      41.916 -24.886   4.724  1.00 80.37      A    N  
ANISOU 1381  N   PRO A 196    11368   6929  12239  -1436  -1532   1322  A    N  
ATOM   1382  CA  PRO A 196      41.616 -24.725   6.153  1.00 79.99      A    C  
ANISOU 1382  CA  PRO A 196    11433   6894  12066  -1586  -1528   1514  A    C  
ATOM   1383  C   PRO A 196      40.520 -25.688   6.626  1.00 81.72      A    C  
ANISOU 1383  C   PRO A 196    11824   6983  12241  -1863  -1528   1618  A    C  
ATOM   1384  O   PRO A 196      39.725 -26.143   5.807  1.00 74.75      A    O  
ANISOU 1384  O   PRO A 196    10911   6091  11400  -1975  -1487   1529  A    O  
ATOM   1385  CB  PRO A 196      41.096 -23.285   6.219  1.00 72.87      A    C  
ANISOU 1385  CB  PRO A 196    10330   6315  11042  -1615  -1360   1497  A    C  
ATOM   1386  CG  PRO A 196      40.490 -23.074   4.864  1.00 71.66      A    C  
ANISOU 1386  CG  PRO A 196    10005   6287  10936  -1606  -1266   1330  A    C  
ATOM   1387  CD  PRO A 196      41.505 -23.697   3.959  1.00 73.46      A    C  
ANISOU 1387  CD  PRO A 196    10249   6346  11315  -1405  -1380   1210  A    C  
ATOM   1388  N   PRO A 197      40.475 -25.973   7.940  1.00 88.43      A    N  
ANISOU 1388  N   PRO A 197    12854   7744  13001  -1987  -1574   1806  A    N  
ATOM   1389  CA  PRO A 197      39.488 -26.846   8.587  1.00 90.56      A    C  
ANISOU 1389  CA  PRO A 197    13307   7897  13205  -2276  -1571   1939  A    C  
ATOM   1390  C   PRO A 197      38.063 -26.520   8.158  1.00 94.38      A    C  
ANISOU 1390  C   PRO A 197    13637   8603  13622  -2495  -1397   1889  A    C  
ATOM   1391  O   PRO A 197      37.340 -27.434   7.755  1.00 89.71      A    O  
ANISOU 1391  O   PRO A 197    13121   7893  13073  -2675  -1411   1874  A    O  
ATOM   1392  CB  PRO A 197      39.644 -26.505  10.067  1.00 94.24      A    C  
ANISOU 1392  CB  PRO A 197    13884   8399  13524  -2341  -1577   2131  A    C  
ATOM   1393  CG  PRO A 197      41.034 -26.011  10.207  1.00 90.11      A    C  
ANISOU 1393  CG  PRO A 197    13334   7859  13044  -2060  -1679   2111  A    C  
ATOM   1394  CD  PRO A 197      41.417 -25.380   8.907  1.00 85.43      A    C  
ANISOU 1394  CD  PRO A 197    12504   7395  12559  -1857  -1632   1905  A    C  
ATOM   1395  N   GLU A 198      37.678 -25.243   8.249  1.00 92.79      A    N  
ANISOU 1395  N   GLU A 198    13225   8715  13316  -2476  -1245   1862  A    N  
ATOM   1396  CA  GLU A 198      36.332 -24.783   7.889  1.00 89.05      A    C  
ANISOU 1396  CA  GLU A 198    12572   8495  12768  -2650  -1076   1813  A    C  
ATOM   1397  C   GLU A 198      35.846 -25.427   6.600  1.00 86.69      A    C  
ANISOU 1397  C   GLU A 198    12211   8142  12584  -2697  -1090   1671  A    C  
ATOM   1398  O   GLU A 198      34.778 -26.035   6.556  1.00 92.25      A    O  
ANISOU 1398  O   GLU A 198    12933   8853  13264  -2949  -1050   1697  A    O  
ATOM   1399  CB  GLU A 198      36.278 -23.256   7.703  1.00 95.04      A    C  
ANISOU 1399  CB  GLU A 198    13092   9565  13453  -2508   -940   1738  A    C  
ATOM   1400  CG  GLU A 198      36.999 -22.415   8.750  1.00 98.05      A    C  
ANISOU 1400  CG  GLU A 198    13513  10006  13736  -2397   -937   1828  A    C  
ATOM   1401  CD  GLU A 198      38.380 -21.967   8.301  1.00 96.41      A    C  
ANISOU 1401  CD  GLU A 198    13270   9738  13621  -2117  -1031   1746  A    C  
ATOM   1402  OE1 GLU A 198      39.312 -22.787   8.375  1.00102.11      A    O  
ANISOU 1402  OE1 GLU A 198    14141  10217  14440  -2033  -1189   1774  A    O  
ATOM   1403  OE2 GLU A 198      38.539 -20.795   7.885  1.00 91.29      A    O1-
ANISOU 1403  OE2 GLU A 198    12449   9289  12950  -1980   -947   1655  A    O1-
ATOM   1404  N   LEU A 199      36.630 -25.275   5.542  1.00 85.89      A    N  
ANISOU 1404  N   LEU A 199    12033   8004  12600  -2462  -1146   1516  A    N  
ATOM   1405  CA  LEU A 199      36.236 -25.803   4.247  1.00 89.55      A    C  
ANISOU 1405  CA  LEU A 199    12435   8431  13160  -2482  -1160   1360  A    C  
ATOM   1406  C   LEU A 199      36.103 -27.327   4.284  1.00 91.33      A    C  
ANISOU 1406  C   LEU A 199    12902   8336  13461  -2643  -1287   1398  A    C  
ATOM   1407  O   LEU A 199      35.137 -27.879   3.764  1.00 91.57      A    O  
ANISOU 1407  O   LEU A 199    12921   8371  13501  -2847  -1265   1351  A    O  
ATOM   1408  CB  LEU A 199      37.205 -25.348   3.155  1.00 84.19      A    C  
ANISOU 1408  CB  LEU A 199    11641   7770  12578  -2188  -1193   1192  A    C  
ATOM   1409  CG  LEU A 199      37.320 -23.825   3.035  1.00 81.72      A    C  
ANISOU 1409  CG  LEU A 199    11104   7757  12189  -2043  -1070   1153  A    C  
ATOM   1410  CD1 LEU A 199      38.191 -23.442   1.855  1.00 86.17      A    C  
ANISOU 1410  CD1 LEU A 199    11554   8345  12840  -1788  -1092    987  A    C  
ATOM   1411  CD2 LEU A 199      35.952 -23.188   2.914  1.00 72.05      A    C  
ANISOU 1411  CD2 LEU A 199     9707   6807  10859  -2206   -919   1145  A    C  
ATOM   1412  N   LEU A 200      37.064 -27.996   4.913  1.00 89.75      A    N  
ANISOU 1412  N   LEU A 200    12928   7859  13312  -2555  -1427   1487  A    N  
ATOM   1413  CA  LEU A 200      37.038 -29.449   5.025  1.00 92.94      A    C  
ANISOU 1413  CA  LEU A 200    13607   7919  13790  -2685  -1563   1537  A    C  
ATOM   1414  C   LEU A 200      35.812 -29.950   5.801  1.00 95.69      A    C  
ANISOU 1414  C   LEU A 200    14055   8267  14036  -3058  -1510   1688  A    C  
ATOM   1415  O   LEU A 200      35.358 -31.072   5.603  1.00 96.47      A    O  
ANISOU 1415  O   LEU A 200    14327   8143  14184  -3249  -1582   1696  A    O  
ATOM   1416  CB  LEU A 200      38.328 -29.944   5.676  1.00 90.13      A    C  
ANISOU 1416  CB  LEU A 200    13465   7289  13492  -2493  -1724   1623  A    C  
ATOM   1417  CG  LEU A 200      39.581 -29.687   4.845  1.00 84.15      A    C  
ANISOU 1417  CG  LEU A 200    12620   6498  12854  -2136  -1792   1467  A    C  
ATOM   1418  CD1 LEU A 200      40.821 -29.716   5.725  1.00 87.41      A    C  
ANISOU 1418  CD1 LEU A 200    13153   6777  13283  -1936  -1916   1578  A    C  
ATOM   1419  CD2 LEU A 200      39.685 -30.691   3.700  1.00 79.69      A    C  
ANISOU 1419  CD2 LEU A 200    12145   5708  12427  -2081  -1881   1306  A    C  
ATOM   1420  N   LEU A 201      35.276 -29.110   6.678  1.00 94.64      A    N  
ANISOU 1420  N   LEU A 201    13814   8389  13756  -3165  -1380   1803  A    N  
ATOM   1421  CA  LEU A 201      34.070 -29.450   7.418  1.00 92.54      A    C  
ANISOU 1421  CA  LEU A 201    13598   8189  13375  -3518  -1296   1943  A    C  
ATOM   1422  C   LEU A 201      32.810 -28.981   6.697  1.00102.52      A    C  
ANISOU 1422  C   LEU A 201    14596   9757  14599  -3677  -1145   1839  A    C  
ATOM   1423  O   LEU A 201      31.712 -29.080   7.241  1.00107.62      A    O  
ANISOU 1423  O   LEU A 201    15211  10541  15140  -3967  -1045   1938  A    O  
ATOM   1424  CB  LEU A 201      34.118 -28.850   8.820  1.00 85.73      A    C  
ANISOU 1424  CB  LEU A 201    12770   7446  12357  -3558  -1231   2126  A    C  
ATOM   1425  CG  LEU A 201      34.972 -29.625   9.820  1.00 85.99      A    C  
ANISOU 1425  CG  LEU A 201    13122   7163  12387  -3539  -1385   2296  A    C  
ATOM   1426  CD1 LEU A 201      34.965 -28.951  11.193  1.00 85.63      A    C  
ANISOU 1426  CD1 LEU A 201    13103   7271  12163  -3586  -1312   2467  A    C  
ATOM   1427  CD2 LEU A 201      34.490 -31.073   9.909  1.00 83.05      A    C  
ANISOU 1427  CD2 LEU A 201    13010   6491  12053  -3808  -1478   2381  A    C  
ATOM   1428  N   GLY A 202      32.975 -28.453   5.487  1.00106.18      A    N  
ANISOU 1428  N   GLY A 202    14862  10341  15139  -3484  -1128   1645  A    N  
ATOM   1429  CA  GLY A 202      31.852 -28.071   4.644  1.00103.64      A    C  
ANISOU 1429  CA  GLY A 202    14293  10290  14795  -3603  -1015   1529  A    C  
ATOM   1430  C   GLY A 202      31.299 -26.655   4.781  1.00 98.61      A    C  
ANISOU 1430  C   GLY A 202    13371  10055  14041  -3542   -839   1517  A    C  
ATOM   1431  O   GLY A 202      30.155 -26.407   4.400  1.00102.13      A    O  
ANISOU 1431  O   GLY A 202    13621  10746  14438  -3698   -736   1472  A    O  
ATOM   1432  N   GLU A 203      32.093 -25.726   5.309  1.00 88.02      A    N  
ANISOU 1432  N   GLU A 203    12007   8782  12655  -3317   -810   1552  A    N  
ATOM   1433  CA  GLU A 203      31.648 -24.334   5.450  1.00 87.78      A    C  
ANISOU 1433  CA  GLU A 203    11735   9103  12515  -3231   -651   1535  A    C  
ATOM   1434  C   GLU A 203      31.523 -23.607   4.103  1.00 85.60      A    C  
ANISOU 1434  C   GLU A 203    11225   9012  12288  -3060   -611   1347  A    C  
ATOM   1435  O   GLU A 203      32.372 -23.752   3.225  1.00 83.72      A    O  
ANISOU 1435  O   GLU A 203    11014   8636  12159  -2873   -705   1232  A    O  
ATOM   1436  CB  GLU A 203      32.587 -23.555   6.372  1.00 86.75      A    C  
ANISOU 1436  CB  GLU A 203    11671   8970  12322  -3046   -646   1617  A    C  
ATOM   1437  CG  GLU A 203      32.312 -22.061   6.405  1.00 85.43      A    C  
ANISOU 1437  CG  GLU A 203    11284   9122  12054  -2911   -498   1574  A    C  
ATOM   1438  CD  GLU A 203      31.087 -21.703   7.225  1.00 92.05      A    C  
ANISOU 1438  CD  GLU A 203    12032  10206  12739  -3110   -342   1664  A    C  
ATOM   1439  OE1 GLU A 203      31.132 -21.857   8.464  1.00 89.52      A    O  
ANISOU 1439  OE1 GLU A 203    11856   9840  12319  -3217   -326   1815  A    O  
ATOM   1440  OE2 GLU A 203      30.083 -21.251   6.634  1.00 95.29      A    O1-
ANISOU 1440  OE2 GLU A 203    12220  10864  13119  -3153   -234   1585  A    O1-
ATOM   1441  N   ARG A 204      30.458 -22.827   3.949  1.00 83.16      A    N  
ANISOU 1441  N   ARG A 204    10686   9021  11890  -3119   -471   1318  A    N  
ATOM   1442  CA  ARG A 204      30.213 -22.102   2.703  1.00 83.77      A    C  
ANISOU 1442  CA  ARG A 204    10542   9293  11995  -2968   -432   1156  A    C  
ATOM   1443  C   ARG A 204      30.046 -20.619   2.979  1.00 85.80      A    C  
ANISOU 1443  C   ARG A 204    10626   9828  12144  -2807   -297   1157  A    C  
ATOM   1444  O   ARG A 204      29.911 -19.812   2.066  1.00 92.92      A    O  
ANISOU 1444  O   ARG A 204    11355  10901  13050  -2651   -257   1043  A    O  
ATOM   1445  CB  ARG A 204      28.971 -22.646   1.994  1.00 84.35      A    C  
ANISOU 1445  CB  ARG A 204    10484   9489  12076  -3187   -413   1092  A    C  
ATOM   1446  CG  ARG A 204      29.120 -24.080   1.532  1.00 90.73      A    C  
ANISOU 1446  CG  ARG A 204    11470  10010  12995  -3339   -554   1060  A    C  
ATOM   1447  CD  ARG A 204      27.848 -24.592   0.904  1.00101.25      A    C  
ANISOU 1447  CD  ARG A 204    12670  11477  14322  -3588   -539   1002  A    C  
ATOM   1448  NE  ARG A 204      27.566 -23.953  -0.377  1.00105.13      A    N  
ANISOU 1448  NE  ARG A 204    12943  12174  14827  -3444   -523    837  A    N  
ATOM   1449  CZ  ARG A 204      28.059 -24.369  -1.538  1.00110.29      A    C  
ANISOU 1449  CZ  ARG A 204    13642  12688  15574  -3343   -629    690  A    C  
ATOM   1450  NH1 ARG A 204      28.871 -25.420  -1.578  1.00109.15      A    N1+
ANISOU 1450  NH1 ARG A 204    13750  12193  15528  -3353   -758    680  A    N1+
ATOM   1451  NH2 ARG A 204      27.748 -23.730  -2.660  1.00111.15      A    N  
ANISOU 1451  NH2 ARG A 204    13551  13007  15673  -3220   -608    553  A    N  
ATOM   1452  N   ASP A 205      30.043 -20.271   4.256  1.00 83.08      A    N  
ANISOU 1452  N   ASP A 205    10349   9521  11699  -2849   -230   1289  A    N  
ATOM   1453  CA  ASP A 205      29.972 -18.887   4.671  1.00 88.72      A    C  
ANISOU 1453  CA  ASP A 205    10947  10460  12304  -2693   -108   1296  A    C  
ATOM   1454  C   ASP A 205      31.307 -18.548   5.322  1.00 88.39      A    C  
ANISOU 1454  C   ASP A 205    11076  10244  12264  -2528   -171   1348  A    C  
ATOM   1455  O   ASP A 205      31.386 -18.303   6.525  1.00 92.21      A    O  
ANISOU 1455  O   ASP A 205    11652  10736  12645  -2570   -127   1464  A    O  
ATOM   1456  CB  ASP A 205      28.825 -18.698   5.659  1.00 96.56      A    C  
ANISOU 1456  CB  ASP A 205    11867  11667  13155  -2876     32   1394  A    C  
ATOM   1457  CG  ASP A 205      28.354 -17.264   5.735  1.00110.14      A    C  
ANISOU 1457  CG  ASP A 205    13404  13676  14767  -2716    176   1354  A    C  
ATOM   1458  OD1 ASP A 205      28.887 -16.418   4.989  1.00115.21      A    O  
ANISOU 1458  OD1 ASP A 205    13984  14345  15446  -2478    161   1255  A    O  
ATOM   1459  OD2 ASP A 205      27.445 -16.983   6.543  1.00119.12      A    O1-
ANISOU 1459  OD2 ASP A 205    14465  15014  15779  -2827    306   1420  A    O1-
ATOM   1460  N   TYR A 206      32.362 -18.571   4.516  1.00 82.43      A    N  
ANISOU 1460  N   TYR A 206    10359   9340  11622  -2346   -275   1262  A    N  
ATOM   1461  CA  TYR A 206      33.718 -18.342   5.002  1.00 78.23      A    C  
ANISOU 1461  CA  TYR A 206     9968   8644  11113  -2190   -355   1300  A    C  
ATOM   1462  C   TYR A 206      34.230 -16.998   4.504  1.00 77.09      A    C  
ANISOU 1462  C   TYR A 206     9707   8633  10951  -1954   -307   1215  A    C  
ATOM   1463  O   TYR A 206      33.641 -16.397   3.599  1.00 78.78      A    O  
ANISOU 1463  O   TYR A 206     9751   9024  11159  -1894   -235   1116  A    O  
ATOM   1464  CB  TYR A 206      34.643 -19.459   4.521  1.00 68.48      A    C  
ANISOU 1464  CB  TYR A 206     8872   7125  10023  -2158   -517   1272  A    C  
ATOM   1465  CG  TYR A 206      34.576 -19.659   3.032  1.00 70.89      A    C  
ANISOU 1465  CG  TYR A 206     9064   7440  10430  -2086   -543   1114  A    C  
ATOM   1466  CD1 TYR A 206      33.800 -20.677   2.474  1.00 70.30      A    C  
ANISOU 1466  CD1 TYR A 206     8993   7312  10405  -2257   -574   1075  A    C  
ATOM   1467  CD2 TYR A 206      35.265 -18.814   2.175  1.00 67.60      A    C  
ANISOU 1467  CD2 TYR A 206     8545   7095  10047  -1859   -537   1005  A    C  
ATOM   1468  CE1 TYR A 206      33.732 -20.856   1.095  1.00 69.00      A    C  
ANISOU 1468  CE1 TYR A 206     8736   7163  10320  -2191   -602    923  A    C  
ATOM   1469  CE2 TYR A 206      35.202 -18.977   0.805  1.00 68.19      A    C  
ANISOU 1469  CE2 TYR A 206     8524   7191  10195  -1793   -556    862  A    C  
ATOM   1470  CZ  TYR A 206      34.441 -19.996   0.267  1.00 70.30      A    C  
ANISOU 1470  CZ  TYR A 206     8799   7404  10508  -1953   -592    816  A    C  
ATOM   1471  OH  TYR A 206      34.401 -20.133  -1.103  1.00 68.47      A    O  
ANISOU 1471  OH  TYR A 206     8481   7199  10334  -1882   -615    667  A    O  
ATOM   1472  N   GLY A 207      35.329 -16.533   5.094  1.00 71.12      A    N  
ANISOU 1472  N   GLY A 207     9049   7791  10184  -1830   -353   1257  A    N  
ATOM   1473  CA  GLY A 207      35.888 -15.233   4.768  1.00 65.16      A    C  
ANISOU 1473  CA  GLY A 207     8212   7143   9401  -1633   -311   1193  A    C  
ATOM   1474  C   GLY A 207      37.399 -15.243   4.679  1.00 66.80      A    C  
ANISOU 1474  C   GLY A 207     8501   7187   9692  -1487   -428   1181  A    C  
ATOM   1475  O   GLY A 207      37.998 -16.279   4.379  1.00 63.24      A    O  
ANISOU 1475  O   GLY A 207     8122   6551   9355  -1487   -545   1171  A    O  
ATOM   1476  N   PRO A 208      38.026 -14.079   4.928  1.00 65.47      A    N  
ANISOU 1476  N   PRO A 208     8318   7089   9469  -1362   -400   1176  A    N  
ATOM   1477  CA  PRO A 208      39.483 -13.884   4.830  1.00 59.50      A    C  
ANISOU 1477  CA  PRO A 208     7602   6225   8783  -1222   -500   1160  A    C  
ATOM   1478  C   PRO A 208      40.333 -14.862   5.639  1.00 61.57      A    C  
ANISOU 1478  C   PRO A 208     8016   6282   9095  -1254   -641   1249  A    C  
ATOM   1479  O   PRO A 208      41.457 -15.146   5.241  1.00 60.73      A    O  
ANISOU 1479  O   PRO A 208     7914   6069   9092  -1140   -744   1213  A    O  
ATOM   1480  CB  PRO A 208      39.676 -12.452   5.335  1.00 52.59      A    C  
ANISOU 1480  CB  PRO A 208     6715   5473   7794  -1155   -428   1172  A    C  
ATOM   1481  CG  PRO A 208      38.414 -11.766   4.932  1.00 59.46      A    C  
ANISOU 1481  CG  PRO A 208     7477   6532   8585  -1171   -286   1127  A    C  
ATOM   1482  CD  PRO A 208      37.311 -12.795   5.071  1.00 58.41      A    C  
ANISOU 1482  CD  PRO A 208     7341   6402   8451  -1330   -263   1162  A    C  
ATOM   1483  N   PRO A 209      39.816 -15.366   6.766  1.00 66.64      A    N  
ANISOU 1483  N   PRO A 209     8783   6879   9660  -1402   -646   1367  A    N  
ATOM   1484  CA  PRO A 209      40.602 -16.345   7.523  1.00 63.98      A    C  
ANISOU 1484  CA  PRO A 209     8609   6333   9367  -1428   -794   1465  A    C  
ATOM   1485  C   PRO A 209      41.078 -17.556   6.716  1.00 62.61      A    C  
ANISOU 1485  C   PRO A 209     8460   5972   9356  -1383   -911   1414  A    C  
ATOM   1486  O   PRO A 209      42.071 -18.165   7.112  1.00 63.83      A    O  
ANISOU 1486  O   PRO A 209     8722   5957   9575  -1321  -1052   1463  A    O  
ATOM   1487  CB  PRO A 209      39.637 -16.775   8.627  1.00 65.58      A    C  
ANISOU 1487  CB  PRO A 209     8929   6537   9450  -1629   -750   1591  A    C  
ATOM   1488  CG  PRO A 209      38.839 -15.544   8.885  1.00 63.67      A    C  
ANISOU 1488  CG  PRO A 209     8596   6529   9068  -1648   -587   1575  A    C  
ATOM   1489  CD  PRO A 209      38.644 -14.900   7.529  1.00 61.73      A    C  
ANISOU 1489  CD  PRO A 209     8162   6404   8887  -1532   -517   1429  A    C  
ATOM   1490  N   ILE A 210      40.421 -17.911   5.616  1.00 59.42      A    N  
ANISOU 1490  N   ILE A 210     7966   5595   9018  -1403   -864   1312  A    N  
ATOM   1491  CA  ILE A 210      40.905 -19.066   4.848  1.00 70.23      A    C  
ANISOU 1491  CA  ILE A 210     9378   6772  10536  -1350   -977   1250  A    C  
ATOM   1492  C   ILE A 210      42.250 -18.781   4.186  1.00 67.25      A    C  
ANISOU 1492  C   ILE A 210     8929   6366  10254  -1127  -1046   1160  A    C  
ATOM   1493  O   ILE A 210      43.092 -19.677   4.060  1.00 67.48      A    O  
ANISOU 1493  O   ILE A 210     9036   6208  10393  -1039  -1174   1149  A    O  
ATOM   1494  CB  ILE A 210      39.910 -19.566   3.771  1.00 68.12      A    C  
ANISOU 1494  CB  ILE A 210     9038   6534  10312  -1431   -923   1149  A    C  
ATOM   1495  CG1 ILE A 210      39.867 -18.591   2.589  1.00 59.34      A    C  
ANISOU 1495  CG1 ILE A 210     7730   5614   9203  -1306   -831   1009  A    C  
ATOM   1496  CG2 ILE A 210      38.526 -19.842   4.385  1.00 56.32      A    C  
ANISOU 1496  CG2 ILE A 210     7580   5098   8721  -1672   -846   1235  A    C  
ATOM   1497  CD1 ILE A 210      38.995 -19.068   1.427  1.00 57.53      A    C  
ANISOU 1497  CD1 ILE A 210     7422   5422   9014  -1367   -796    896  A    C  
ATOM   1498  N   ASP A 211      42.450 -17.536   3.766  1.00 56.85      A    N  
ANISOU 1498  N   ASP A 211     7468   5237   8895  -1034   -958   1097  A    N  
ATOM   1499  CA  ASP A 211      43.708 -17.154   3.140  1.00 61.03      A    C  
ANISOU 1499  CA  ASP A 211     7910   5775   9501   -845  -1004   1017  A    C  
ATOM   1500  C   ASP A 211      44.836 -17.134   4.170  1.00 65.56      A    C  
ANISOU 1500  C   ASP A 211     8565   6266  10078   -786  -1117   1112  A    C  
ATOM   1501  O   ASP A 211      45.998 -17.426   3.856  1.00 59.29      A    O  
ANISOU 1501  O   ASP A 211     7741   5402   9384   -640  -1214   1070  A    O  
ATOM   1502  CB  ASP A 211      43.588 -15.799   2.431  1.00 57.45      A    C  
ANISOU 1502  CB  ASP A 211     7301   5537   8990   -786   -879    938  A    C  
ATOM   1503  CG  ASP A 211      42.795 -15.885   1.138  1.00 58.67      A    C  
ANISOU 1503  CG  ASP A 211     7355   5769   9168   -786   -800    820  A    C  
ATOM   1504  OD1 ASP A 211      42.633 -17.006   0.608  1.00 58.77      A    O  
ANISOU 1504  OD1 ASP A 211     7404   5661   9264   -802   -855    769  A    O  
ATOM   1505  OD2 ASP A 211      42.335 -14.834   0.650  1.00 61.13      A    O1-
ANISOU 1505  OD2 ASP A 211     7562   6258   9408   -771   -690    778  A    O1-
ATOM   1506  N   LEU A 212      44.484 -16.804   5.407  1.00 61.00      A    N  
ANISOU 1506  N   LEU A 212     8084   5708   9385   -898  -1109   1237  A    N  
ATOM   1507  CA  LEU A 212      45.491 -16.692   6.454  1.00 64.17      A    C  
ANISOU 1507  CA  LEU A 212     8566   6052   9765   -857  -1221   1333  A    C  
ATOM   1508  C   LEU A 212      45.982 -18.051   6.941  1.00 68.15      A    C  
ANISOU 1508  C   LEU A 212     9217   6328  10349   -843  -1384   1407  A    C  
ATOM   1509  O   LEU A 212      47.156 -18.216   7.267  1.00 69.20      A    O  
ANISOU 1509  O   LEU A 212     9365   6392  10537   -725  -1515   1433  A    O  
ATOM   1510  CB  LEU A 212      44.985 -15.812   7.596  1.00 60.70      A    C  
ANISOU 1510  CB  LEU A 212     8189   5718   9155   -972  -1154   1430  A    C  
ATOM   1511  CG  LEU A 212      45.223 -14.345   7.216  1.00 64.22      A    C  
ANISOU 1511  CG  LEU A 212     8504   6348   9548   -907  -1059   1357  A    C  
ATOM   1512  CD1 LEU A 212      44.227 -13.439   7.872  1.00 76.10      A    C  
ANISOU 1512  CD1 LEU A 212    10042   7984  10890  -1014   -930   1398  A    C  
ATOM   1513  CD2 LEU A 212      46.650 -13.927   7.562  1.00 62.22      A    C  
ANISOU 1513  CD2 LEU A 212     8233   6086   9321   -805  -1171   1371  A    C  
ATOM   1514  N   TRP A 213      45.078 -19.023   6.970  1.00 72.45      A    N  
ANISOU 1514  N   TRP A 213     9870   6757  10902   -964  -1381   1440  A    N  
ATOM   1515  CA  TRP A 213      45.448 -20.395   7.251  1.00 68.13      A    C  
ANISOU 1515  CA  TRP A 213     9484   5960  10441   -950  -1533   1499  A    C  
ATOM   1516  C   TRP A 213      46.521 -20.796   6.258  1.00 67.59      A    C  
ANISOU 1516  C   TRP A 213     9330   5817  10533   -734  -1619   1377  A    C  
ATOM   1517  O   TRP A 213      47.520 -21.424   6.616  1.00 67.65      A    O  
ANISOU 1517  O   TRP A 213     9410   5676  10615   -612  -1774   1418  A    O  
ATOM   1518  CB  TRP A 213      44.245 -21.321   7.094  1.00 70.72      A    C  
ANISOU 1518  CB  TRP A 213     9915   6186  10769  -1125  -1495   1518  A    C  
ATOM   1519  CG  TRP A 213      44.634 -22.763   7.171  1.00 74.84      A    C  
ANISOU 1519  CG  TRP A 213    10615   6422  11398  -1098  -1654   1556  A    C  
ATOM   1520  CD1 TRP A 213      45.021 -23.565   6.137  1.00 76.60      A    C  
ANISOU 1520  CD1 TRP A 213    10832   6505  11770   -973  -1719   1436  A    C  
ATOM   1521  CD2 TRP A 213      44.700 -23.566   8.351  1.00 74.04      A    C  
ANISOU 1521  CD2 TRP A 213    10746   6130  11256  -1187  -1774   1727  A    C  
ATOM   1522  CE2 TRP A 213      45.129 -24.848   7.958  1.00 81.22      A    C  
ANISOU 1522  CE2 TRP A 213    11785   6771  12303  -1104  -1913   1703  A    C  
ATOM   1523  CE3 TRP A 213      44.436 -23.328   9.702  1.00 78.60      A    C  
ANISOU 1523  CE3 TRP A 213    11444   6735  11685  -1325  -1776   1897  A    C  
ATOM   1524  NE1 TRP A 213      45.320 -24.820   6.601  1.00 83.34      A    N  
ANISOU 1524  NE1 TRP A 213    11902   7077  12685   -970  -1874   1517  A    N  
ATOM   1525  CZ2 TRP A 213      45.298 -25.890   8.868  1.00 81.56      A    C  
ANISOU 1525  CZ2 TRP A 213    12083   6560  12344  -1155  -2062   1855  A    C  
ATOM   1526  CZ3 TRP A 213      44.605 -24.367  10.608  1.00 79.86      A    C  
ANISOU 1526  CZ3 TRP A 213    11851   6658  11834  -1387  -1919   2050  A    C  
ATOM   1527  CH2 TRP A 213      45.031 -25.628  10.186  1.00 79.29      A    C  
ANISOU 1527  CH2 TRP A 213    11910   6310  11906  -1302  -2064   2033  A    C  
ATOM   1528  N   GLY A 214      46.301 -20.423   5.002  1.00 65.43      A    N  
ANISOU 1528  N   GLY A 214     8897   5658  10306   -679  -1515   1226  A    N  
ATOM   1529  CA  GLY A 214      47.275 -20.668   3.958  1.00 71.50      A    C  
ANISOU 1529  CA  GLY A 214     9559   6400  11208   -474  -1564   1092  A    C  
ATOM   1530  C   GLY A 214      48.581 -19.922   4.185  1.00 66.66      A    C  
ANISOU 1530  C   GLY A 214     8833   5885  10608   -321  -1613   1094  A    C  
ATOM   1531  O   GLY A 214      49.647 -20.403   3.806  1.00 66.35      A    O  
ANISOU 1531  O   GLY A 214     8751   5777  10684   -141  -1711   1036  A    O  
ATOM   1532  N   ALA A 215      48.499 -18.739   4.785  1.00 58.26      A    N  
ANISOU 1532  N   ALA A 215     7719   4989   9427   -394  -1546   1152  A    N  
ATOM   1533  CA  ALA A 215      49.689 -17.962   5.090  1.00 58.44      A    C  
ANISOU 1533  CA  ALA A 215     7642   5113   9448   -289  -1598   1163  A    C  
ATOM   1534  C   ALA A 215      50.486 -18.751   6.115  1.00 63.90      A    C  
ANISOU 1534  C   ALA A 215     8457   5645  10175   -234  -1784   1275  A    C  
ATOM   1535  O   ALA A 215      51.703 -18.882   6.011  1.00 62.14      A    O  
ANISOU 1535  O   ALA A 215     8152   5419  10041    -71  -1891   1248  A    O  
ATOM   1536  CB  ALA A 215      49.311 -16.579   5.642  1.00 49.91      A    C  
ANISOU 1536  CB  ALA A 215     6531   4212   8221   -402  -1495   1210  A    C  
ATOM   1537  N   GLY A 216      49.778 -19.281   7.105  1.00 65.03      A    N  
ANISOU 1537  N   GLY A 216     8796   5666  10243   -371  -1824   1405  A    N  
ATOM   1538  CA  GLY A 216      50.376 -20.173   8.076  1.00 75.55      A    C  
ANISOU 1538  CA  GLY A 216    10288   6817  11600   -332  -2010   1527  A    C  
ATOM   1539  C   GLY A 216      51.156 -21.321   7.451  1.00 78.66      A    C  
ANISOU 1539  C   GLY A 216    10686   7036  12164   -139  -2138   1462  A    C  
ATOM   1540  O   GLY A 216      52.333 -21.511   7.763  1.00 81.96      A    O  
ANISOU 1540  O   GLY A 216    11073   7423  12645     22  -2284   1485  A    O  
ATOM   1541  N   CYS A 217      50.507 -22.090   6.575  1.00 73.65      A    N  
ANISOU 1541  N   CYS A 217    10090   6290  11602   -147  -2089   1378  A    N  
ATOM   1542  CA  CYS A 217      51.146 -23.260   5.973  1.00 76.26      A    C  
ANISOU 1542  CA  CYS A 217    10460   6426  12089     40  -2207   1304  A    C  
ATOM   1543  C   CYS A 217      52.387 -22.862   5.181  1.00 79.94      A    C  
ANISOU 1543  C   CYS A 217    10697   7022  12655    275  -2221   1174  A    C  
ATOM   1544  O   CYS A 217      53.379 -23.600   5.135  1.00 82.08      A    O  
ANISOU 1544  O   CYS A 217    10973   7176  13040    481  -2363   1154  A    O  
ATOM   1545  CB  CYS A 217      50.174 -24.022   5.068  1.00 77.03      A    C  
ANISOU 1545  CB  CYS A 217    10631   6403  12235    -31  -2136   1212  A    C  
ATOM   1546  SG  CYS A 217      48.678 -24.651   5.880  1.00 83.65      A    S  
ANISOU 1546  SG  CYS A 217    11725   7088  12970   -329  -2116   1357  A    S  
ATOM   1547  N   ILE A 218      52.325 -21.691   4.560  1.00 71.19      A    N  
ANISOU 1547  N   ILE A 218     9390   6159  11500    246  -2071   1089  A    N  
ATOM   1548  CA  ILE A 218      53.445 -21.182   3.782  1.00 69.07      A    C  
ANISOU 1548  CA  ILE A 218     8888   6049  11305    432  -2057    970  A    C  
ATOM   1549  C   ILE A 218      54.571 -20.711   4.696  1.00 74.32      A    C  
ANISOU 1549  C   ILE A 218     9485   6795  11958    502  -2175   1060  A    C  
ATOM   1550  O   ILE A 218      55.754 -20.949   4.425  1.00 71.93      A    O  
ANISOU 1550  O   ILE A 218     9054   6517  11758    704  -2264   1005  A    O  
ATOM   1551  CB  ILE A 218      53.008 -20.034   2.852  1.00 53.72      A    C  
ANISOU 1551  CB  ILE A 218     6774   4337   9301    360  -1861    866  A    C  
ATOM   1552  CG1 ILE A 218      52.202 -20.591   1.692  1.00 50.32      A    C  
ANISOU 1552  CG1 ILE A 218     6362   3848   8911    355  -1768    740  A    C  
ATOM   1553  CG2 ILE A 218      54.221 -19.282   2.295  1.00 54.95      A    C  
ANISOU 1553  CG2 ILE A 218     6691   4690   9500    505  -1842    783  A    C  
ATOM   1554  CD1 ILE A 218      51.294 -19.560   1.037  1.00 53.76      A    C  
ANISOU 1554  CD1 ILE A 218     6707   4470   9248    222  -1584    686  A    C  
ATOM   1555  N   MET A 219      54.207 -20.035   5.779  1.00 71.81      A    N  
ANISOU 1555  N   MET A 219     9246   6529  11508    335  -2177   1192  A    N  
ATOM   1556  CA  MET A 219      55.218 -19.560   6.707  1.00 72.07      A    C  
ANISOU 1556  CA  MET A 219     9230   6642  11512    375  -2300   1280  A    C  
ATOM   1557  C   MET A 219      56.040 -20.745   7.201  1.00 69.23      A    C  
ANISOU 1557  C   MET A 219     8956   6096  11252    547  -2513   1340  A    C  
ATOM   1558  O   MET A 219      57.262 -20.732   7.120  1.00 73.55      A    O  
ANISOU 1558  O   MET A 219     9347   6718  11882    724  -2615   1307  A    O  
ATOM   1559  CB  MET A 219      54.603 -18.793   7.880  1.00 65.97      A    C  
ANISOU 1559  CB  MET A 219     8579   5920  10568    165  -2278   1416  A    C  
ATOM   1560  CG  MET A 219      55.649 -18.088   8.726  1.00 67.82      A    C  
ANISOU 1560  CG  MET A 219     8740   6274  10755    186  -2391   1483  A    C  
ATOM   1561  SD  MET A 219      54.979 -16.995   9.982  1.00 80.61      A    S  
ANISOU 1561  SD  MET A 219    10491   7982  12155    -52  -2342   1606  A    S  
ATOM   1562  CE  MET A 219      56.434 -16.651  10.966  1.00 97.49      A    C  
ANISOU 1562  CE  MET A 219    12567  10199  14276     16  -2550   1683  A    C  
ATOM   1563  N   ALA A 220      55.357 -21.771   7.698  1.00 72.82      A    N  
ANISOU 1563  N   ALA A 220     9656   6313  11700    494  -2582   1428  A    N  
ATOM   1564  CA  ALA A 220      56.016 -22.973   8.201  1.00 81.97      A    C  
ANISOU 1564  CA  ALA A 220    10945   7252  12947    655  -2794   1499  A    C  
ATOM   1565  C   ALA A 220      56.895 -23.591   7.122  1.00 83.64      A    C  
ANISOU 1565  C   ALA A 220    11010   7435  13334    926  -2832   1345  A    C  
ATOM   1566  O   ALA A 220      57.931 -24.180   7.412  1.00 83.69      A    O  
ANISOU 1566  O   ALA A 220    10998   7370  13429   1135  -3009   1369  A    O  
ATOM   1567  CB  ALA A 220      54.979 -23.986   8.684  1.00 83.79      A    C  
ANISOU 1567  CB  ALA A 220    11478   7217  13143    526  -2827   1602  A    C  
ATOM   1568  N   GLU A 221      56.470 -23.436   5.874  1.00 86.20      A    N  
ANISOU 1568  N   GLU A 221    11226   7824  13700    928  -2667   1186  A    N  
ATOM   1569  CA  GLU A 221      57.165 -24.004   4.730  1.00 84.11      A    C  
ANISOU 1569  CA  GLU A 221    10829   7542  13585   1172  -2669   1017  A    C  
ATOM   1570  C   GLU A 221      58.488 -23.289   4.462  1.00 81.43      A    C  
ANISOU 1570  C   GLU A 221    10195   7451  13294   1338  -2683    951  A    C  
ATOM   1571  O   GLU A 221      59.365 -23.831   3.790  1.00 90.12      A    O  
ANISOU 1571  O   GLU A 221    11172   8548  14521   1586  -2730    836  A    O  
ATOM   1572  CB  GLU A 221      56.257 -23.943   3.498  1.00 92.97      A    C  
ANISOU 1572  CB  GLU A 221    11927   8689  14708   1096  -2480    871  A    C  
ATOM   1573  CG  GLU A 221      56.688 -24.815   2.331  1.00101.27      A    C  
ANISOU 1573  CG  GLU A 221    12931   9650  15898   1325  -2483    695  A    C  
ATOM   1574  CD  GLU A 221      55.526 -25.181   1.413  1.00102.77      A    C  
ANISOU 1574  CD  GLU A 221    13222   9750  16076   1213  -2356    591  A    C  
ATOM   1575  OE1 GLU A 221      54.358 -25.058   1.847  1.00 96.30      A    O  
ANISOU 1575  OE1 GLU A 221    12552   8877  15159    967  -2305    682  A    O  
ATOM   1576  OE2 GLU A 221      55.785 -25.601   0.263  1.00104.77      A    O1-
ANISOU 1576  OE2 GLU A 221    13402   9996  16411   1370  -2309    417  A    O1-
ATOM   1577  N   MET A 222      58.636 -22.080   5.000  1.00 73.98      A    N  
ANISOU 1577  N   MET A 222     9141   6723  12246   1198  -2641   1019  A    N  
ATOM   1578  CA  MET A 222      59.868 -21.305   4.821  1.00 81.93      A    C  
ANISOU 1578  CA  MET A 222     9865   7981  13285   1307  -2655    969  A    C  
ATOM   1579  C   MET A 222      61.065 -21.946   5.532  1.00 86.33      A    C  
ANISOU 1579  C   MET A 222    10388   8488  13927   1517  -2885   1033  A    C  
ATOM   1580  O   MET A 222      62.218 -21.686   5.183  1.00 79.98      A    O  
ANISOU 1580  O   MET A 222     9326   7866  13195   1678  -2916    961  A    O  
ATOM   1581  CB  MET A 222      59.679 -19.855   5.289  1.00 77.10      A    C  
ANISOU 1581  CB  MET A 222     9180   7581  12531   1083  -2566   1031  A    C  
ATOM   1582  CG  MET A 222      58.651 -19.059   4.479  1.00 76.81      A    C  
ANISOU 1582  CG  MET A 222     9128   7637  12416    912  -2338    955  A    C  
ATOM   1583  SD  MET A 222      59.172 -18.700   2.780  1.00 73.68      A    S  
ANISOU 1583  SD  MET A 222     8456   7436  12102   1040  -2177    751  A    S  
ATOM   1584  CE  MET A 222      60.620 -17.677   3.056  1.00 70.63      A    C  
ANISOU 1584  CE  MET A 222     7799   7321  11717   1073  -2226    763  A    C  
ATOM   1585  N   TRP A 223      60.779 -22.781   6.529  1.00 87.74      A    N  
ANISOU 1585  N   TRP A 223    10821   8428  14089   1511  -3045   1173  A    N  
ATOM   1586  CA  TRP A 223      61.816 -23.502   7.260  1.00 85.80      A    C  
ANISOU 1586  CA  TRP A 223    10585   8099  13917   1721  -3285   1251  A    C  
ATOM   1587  C   TRP A 223      61.813 -24.984   6.895  1.00 94.14      A    C  
ANISOU 1587  C   TRP A 223    11800   8866  15101   1940  -3381   1209  A    C  
ATOM   1588  O   TRP A 223      62.866 -25.562   6.649  1.00 96.65      A    O  
ANISOU 1588  O   TRP A 223    11994   9181  15549   2226  -3501   1148  A    O  
ATOM   1589  CB  TRP A 223      61.642 -23.345   8.772  1.00 80.14      A    C  
ANISOU 1589  CB  TRP A 223    10057   7321  13071   1569  -3429   1459  A    C  
ATOM   1590  CG  TRP A 223      62.027 -21.993   9.299  1.00 80.48      A    C  
ANISOU 1590  CG  TRP A 223     9936   7639  13004   1419  -3405   1502  A    C  
ATOM   1591  CD1 TRP A 223      63.271 -21.590   9.685  1.00 79.25      A    C  
ANISOU 1591  CD1 TRP A 223     9571   7667  12873   1525  -3540   1519  A    C  
ATOM   1592  CD2 TRP A 223      61.156 -20.869   9.512  1.00 78.51      A    C  
ANISOU 1592  CD2 TRP A 223     9727   7504  12598   1132  -3242   1530  A    C  
ATOM   1593  CE2 TRP A 223      61.944 -19.822  10.026  1.00 78.23      A    C  
ANISOU 1593  CE2 TRP A 223     9521   7702  12499   1075  -3289   1560  A    C  
ATOM   1594  CE3 TRP A 223      59.787 -20.649   9.318  1.00 73.19      A    C  
ANISOU 1594  CE3 TRP A 223     9212   6763  11835    926  -3065   1529  A    C  
ATOM   1595  NE1 TRP A 223      63.230 -20.285  10.122  1.00 81.67      A    N  
ANISOU 1595  NE1 TRP A 223     9798   8183  13047   1307  -3474   1554  A    N  
ATOM   1596  CZ2 TRP A 223      61.412 -18.573  10.343  1.00 77.11      A    C  
ANISOU 1596  CZ2 TRP A 223     9389   7703  12206    827  -3165   1584  A    C  
ATOM   1597  CZ3 TRP A 223      59.258 -19.412   9.640  1.00 68.05      A    C  
ANISOU 1597  CZ3 TRP A 223     8551   6271  11035    697  -2940   1556  A    C  
ATOM   1598  CH2 TRP A 223      60.068 -18.390  10.143  1.00 72.95      A    C  
ANISOU 1598  CH2 TRP A 223     9026   7098  11595    654  -2989   1581  A    C  
ATOM   1599  N   THR A 224      60.634 -25.601   6.857  1.00 95.44      A    N  
ANISOU 1599  N   THR A 224    12239   8791  15235   1809  -3330   1237  A    N  
ATOM   1600  CA  THR A 224      60.562 -27.030   6.551  1.00 98.14      A    C  
ANISOU 1600  CA  THR A 224    12776   8821  15691   1989  -3428   1202  A    C  
ATOM   1601  C   THR A 224      60.847 -27.318   5.081  1.00100.41      A    C  
ANISOU 1601  C   THR A 224    12900   9148  16103   2184  -3316    973  A    C  
ATOM   1602  O   THR A 224      61.066 -28.468   4.707  1.00104.45      A    O  
ANISOU 1602  O   THR A 224    13527   9427  16731   2400  -3406    906  A    O  
ATOM   1603  CB  THR A 224      59.205 -27.666   6.925  1.00 90.11      A    C  
ANISOU 1603  CB  THR A 224    12109   7527  14603   1766  -3410   1299  A    C  
ATOM   1604  CG2 THR A 224      58.858 -27.389   8.376  1.00 88.66      A    C  
ANISOU 1604  CG2 THR A 224    12099   7314  14275   1562  -3501   1526  A    C  
ATOM   1605  OG1 THR A 224      58.176 -27.155   6.068  1.00 82.15      A    O  
ANISOU 1605  OG1 THR A 224    11062   6608  13544   1570  -3180   1194  A    O  
ATOM   1606  N   ARG A 225      60.832 -26.281   4.250  1.00 97.73      A    N  
ANISOU 1606  N   ARG A 225    12309   9091  15733   2110  -3121    852  A    N  
ATOM   1607  CA  ARG A 225      61.155 -26.457   2.839  1.00 95.56      A    C  
ANISOU 1607  CA  ARG A 225    11861   8893  15553   2289  -3002    632  A    C  
ATOM   1608  C   ARG A 225      60.211 -27.455   2.165  1.00 97.73      A    C  
ANISOU 1608  C   ARG A 225    12376   8893  15865   2277  -2956    547  A    C  
ATOM   1609  O   ARG A 225      60.545 -28.051   1.142  1.00 97.64      A    O  
ANISOU 1609  O   ARG A 225    12310   8837  15952   2487  -2924    371  A    O  
ATOM   1610  CB  ARG A 225      62.596 -26.939   2.701  1.00 91.53      A    C  
ANISOU 1610  CB  ARG A 225    11168   8430  15178   2639  -3134    564  A    C  
ATOM   1611  CG  ARG A 225      63.622 -25.873   2.973  1.00 88.57      A    C  
ANISOU 1611  CG  ARG A 225    10475   8396  14783   2658  -3139    587  A    C  
ATOM   1612  CD  ARG A 225      63.804 -24.996   1.754  1.00 90.28      A    C  
ANISOU 1612  CD  ARG A 225    10406   8905  14990   2637  -2916    419  A    C  
ATOM   1613  NE  ARG A 225      64.666 -23.858   2.044  1.00 93.13      A    N  
ANISOU 1613  NE  ARG A 225    10480   9592  15314   2587  -2905    455  A    N  
ATOM   1614  CZ  ARG A 225      65.469 -23.281   1.157  1.00 93.29      A    C  
ANISOU 1614  CZ  ARG A 225    10179   9897  15369   2679  -2790    322  A    C  
ATOM   1615  NH1 ARG A 225      65.530 -23.746  -0.087  1.00 86.85      A    N1+
ANISOU 1615  NH1 ARG A 225     9291   9088  14621   2844  -2670    136  A    N1+
ATOM   1616  NH2 ARG A 225      66.221 -22.244   1.521  1.00 94.15      A    N  
ANISOU 1616  NH2 ARG A 225    10047  10287  15437   2596  -2795    373  A    N  
ATOM   1617  N   SER A 226      59.027 -27.627   2.739  1.00 98.72      A    N  
ANISOU 1617  N   SER A 226    12765   8842  15902   2023  -2952    666  A    N  
ATOM   1618  CA  SER A 226      58.090 -28.627   2.251  1.00102.85      A    C  
ANISOU 1618  CA  SER A 226    13538   9085  16453   1973  -2934    610  A    C  
ATOM   1619  C   SER A 226      56.746 -28.471   2.954  1.00100.98      A    C  
ANISOU 1619  C   SER A 226    13521   8758  16090   1629  -2892    759  A    C  
ATOM   1620  O   SER A 226      56.700 -28.188   4.153  1.00104.85      A    O  
ANISOU 1620  O   SER A 226    14091   9247  16499   1510  -2974    945  A    O  
ATOM   1621  CB  SER A 226      58.660 -30.028   2.497  1.00105.52      A    C  
ANISOU 1621  CB  SER A 226    14074   9103  16916   2226  -3141    618  A    C  
ATOM   1622  OG  SER A 226      57.834 -31.017   1.917  1.00112.23      A    O  
ANISOU 1622  OG  SER A 226    15169   9671  17803   2187  -3126    538  A    O  
ATOM   1623  N   PRO A 227      55.645 -28.656   2.210  1.00 93.56      A    N  
ANISOU 1623  N   PRO A 227    12671   7754  15124   1470  -2764    673  A    N  
ATOM   1624  CA  PRO A 227      54.295 -28.481   2.763  1.00 93.64      A    C  
ANISOU 1624  CA  PRO A 227    12852   7715  15011   1137  -2699    797  A    C  
ATOM   1625  C   PRO A 227      54.040 -29.359   3.989  1.00 89.90      A    C  
ANISOU 1625  C   PRO A 227    12683   6954  14520   1056  -2869    993  A    C  
ATOM   1626  O   PRO A 227      54.012 -30.580   3.885  1.00 88.57      A    O  
ANISOU 1626  O   PRO A 227    12736   6481  14436   1139  -2982    979  A    O  
ATOM   1627  CB  PRO A 227      53.381 -28.878   1.600  1.00 92.43      A    C  
ANISOU 1627  CB  PRO A 227    12747   7497  14877   1056  -2581    640  A    C  
ATOM   1628  CG  PRO A 227      54.205 -28.634   0.378  1.00 91.40      A    C  
ANISOU 1628  CG  PRO A 227    12379   7525  14824   1296  -2510    431  A    C  
ATOM   1629  CD  PRO A 227      55.621 -28.961   0.770  1.00 91.16      A    C  
ANISOU 1629  CD  PRO A 227    12286   7459  14891   1591  -2664    447  A    C  
ATOM   1630  N   ILE A 228      53.843 -28.718   5.136  1.00 90.41      A    N  
ANISOU 1630  N   ILE A 228    12773   7114  14466    887  -2883   1174  A    N  
ATOM   1631  CA  ILE A 228      53.708 -29.395   6.425  1.00 88.31      A    C  
ANISOU 1631  CA  ILE A 228    12781   6619  14154    806  -3044   1385  A    C  
ATOM   1632  C   ILE A 228      52.637 -30.492   6.495  1.00 90.43      A    C  
ANISOU 1632  C   ILE A 228    13361   6581  14418    627  -3066   1437  A    C  
ATOM   1633  O   ILE A 228      52.800 -31.463   7.235  1.00105.06      A    O  
ANISOU 1633  O   ILE A 228    15473   8151  16292    658  -3240   1568  A    O  
ATOM   1634  CB  ILE A 228      53.446 -28.372   7.547  1.00 87.01      A    C  
ANISOU 1634  CB  ILE A 228    12584   6650  13827    604  -3007   1551  A    C  
ATOM   1635  CG1 ILE A 228      52.201 -27.541   7.217  1.00 84.49      A    C  
ANISOU 1635  CG1 ILE A 228    12193   6514  13395    331  -2785   1517  A    C  
ATOM   1636  CG2 ILE A 228      54.649 -27.463   7.712  1.00 89.65      A    C  
ANISOU 1636  CG2 ILE A 228    12667   7229  14169    779  -3043   1533  A    C  
ATOM   1637  CD1 ILE A 228      51.742 -26.631   8.333  1.00 79.58      A    C  
ANISOU 1637  CD1 ILE A 228    11585   6053  12600    117  -2734   1675  A    C  
ATOM   1638  N   MET A 229      51.555 -30.342   5.735  1.00 84.55      A    N  
ANISOU 1638  N   MET A 229    12592   5890  13642    435  -2900   1343  A    N  
ATOM   1639  CA  MET A 229      50.432 -31.283   5.794  1.00 94.76      A    C  
ANISOU 1639  CA  MET A 229    14157   6930  14917    212  -2904   1392  A    C  
ATOM   1640  C   MET A 229      49.953 -31.732   4.409  1.00100.20      A    C  
ANISOU 1640  C   MET A 229    14824   7559  15690    221  -2820   1182  A    C  
ATOM   1641  O   MET A 229      49.125 -31.062   3.786  1.00 96.68      A    O  
ANISOU 1641  O   MET A 229    14231   7320  15183     58  -2647   1099  A    O  
ATOM   1642  CB  MET A 229      49.265 -30.661   6.562  1.00 96.39      A    C  
ANISOU 1642  CB  MET A 229    14396   7273  14956   -134  -2786   1538  A    C  
ATOM   1643  CG  MET A 229      49.539 -30.457   8.038  1.00 97.09      A    C  
ANISOU 1643  CG  MET A 229    14594   7358  14939   -192  -2881   1763  A    C  
ATOM   1644  SD  MET A 229      48.199 -29.575   8.857  1.00125.97      A    S  
ANISOU 1644  SD  MET A 229    18246  11232  18385   -570  -2708   1901  A    S  
ATOM   1645  CE  MET A 229      48.366 -27.965   8.107  1.00101.82      A    C  
ANISOU 1645  CE  MET A 229    14804   8582  15298   -498  -2522   1743  A    C  
ATOM   1646  N   GLN A 230      50.451 -32.880   3.950  1.00109.24      A    N  
ANISOU 1646  N   GLN A 230    16129   8413  16965    416  -2950   1098  A    N  
ATOM   1647  CA  GLN A 230      50.216 -33.331   2.577  1.00112.31      A    C  
ANISOU 1647  CA  GLN A 230    16495   8740  17437    480  -2888    871  A    C  
ATOM   1648  C   GLN A 230      49.218 -34.479   2.462  1.00113.40      A    C  
ANISOU 1648  C   GLN A 230    16942   8558  17588    272  -2933    881  A    C  
ATOM   1649  O   GLN A 230      49.585 -35.582   2.070  1.00112.68      A    O  
ANISOU 1649  O   GLN A 230    17046   8160  17608    431  -3056    798  A    O  
ATOM   1650  CB  GLN A 230      51.538 -33.738   1.922  1.00112.34      A    C  
ANISOU 1650  CB  GLN A 230    16426   8676  17584    879  -2980    716  A    C  
ATOM   1651  CG  GLN A 230      52.700 -32.836   2.287  1.00110.43      A    C  
ANISOU 1651  CG  GLN A 230    15926   8690  17344   1091  -2992    747  A    C  
ATOM   1652  CD  GLN A 230      53.912 -33.059   1.412  1.00108.27      A    C  
ANISOU 1652  CD  GLN A 230    15499   8440  17199   1469  -3029    558  A    C  
ATOM   1653  NE2 GLN A 230      55.084 -32.692   1.918  1.00101.63      A    N  
ANISOU 1653  NE2 GLN A 230    14504   7720  16392   1690  -3113    610  A    N  
ATOM   1654  OE1 GLN A 230      53.797 -33.550   0.292  1.00114.48      A    O  
ANISOU 1654  OE1 GLN A 230    16298   9150  18050   1557  -2981    362  A    O  
ATOM   1655  N   GLY A 231      47.955 -34.207   2.776  1.00117.64      A    N  
ANISOU 1655  N   GLY A 231    17516   9172  18010    -84  -2831    973  A    N  
ATOM   1656  CA  GLY A 231      46.917 -35.222   2.723  1.00122.41      A    C  
ANISOU 1656  CA  GLY A 231    18394   9505  18612   -338  -2862    998  A    C  
ATOM   1657  C   GLY A 231      46.661 -35.778   1.334  1.00126.24      A    C  
ANISOU 1657  C   GLY A 231    18891   9895  19180   -292  -2834    758  A    C  
ATOM   1658  O   GLY A 231      47.134 -35.235   0.335  1.00126.06      A    O  
ANISOU 1658  O   GLY A 231    18632  10071  19194    -93  -2752    566  A    O  
ATOM   1659  N   ASN A 232      45.907 -36.872   1.271  1.00128.03      A    N  
ANISOU 1659  N   ASN A 232    19406   9813  19426   -491  -2902    767  A    N  
ATOM   1660  CA  ASN A 232      45.568 -37.496  -0.003  1.00125.08      A    C  
ANISOU 1660  CA  ASN A 232    19087   9319  19120   -484  -2890    539  A    C  
ATOM   1661  C   ASN A 232      44.082 -37.407  -0.302  1.00121.82      A    C  
ANISOU 1661  C   ASN A 232    18661   9007  18617   -881  -2776    532  A    C  
ATOM   1662  O   ASN A 232      43.670 -37.403  -1.461  1.00120.82      A    O  
ANISOU 1662  O   ASN A 232    18445   8958  18504   -905  -2707    331  A    O  
ATOM   1663  CB  ASN A 232      46.044 -38.945  -0.034  1.00130.00      A    C  
ANISOU 1663  CB  ASN A 232    20070   9465  19861   -343  -3083    508  A    C  
ATOM   1664  CG  ASN A 232      47.549 -39.051  -0.152  1.00134.43      A    C  
ANISOU 1664  CG  ASN A 232    20586   9962  20530    115  -3181    431  A    C  
ATOM   1665  ND2 ASN A 232      48.111 -38.360  -1.139  1.00135.10      A    N  
ANISOU 1665  ND2 ASN A 232    20374  10317  20640    346  -3077    229  A    N  
ATOM   1666  OD1 ASN A 232      48.204 -39.730   0.641  1.00136.22      A    O  
ANISOU 1666  OD1 ASN A 232    21034   9913  20812    259  -3349    557  A    O  
ATOM   1667  N   THR A 233      43.283 -37.342   0.759  1.00121.27      A    N  
ANISOU 1667  N   THR A 233    18677   8948  18452  -1192  -2759    754  A    N  
ATOM   1668  CA  THR A 233      41.858 -37.055   0.640  1.00119.55      A    C  
ANISOU 1668  CA  THR A 233    18382   8911  18134  -1575  -2631    776  A    C  
ATOM   1669  C   THR A 233      41.467 -36.070   1.737  1.00111.75      A    C  
ANISOU 1669  C   THR A 233    17243   8203  17013  -1736  -2528    985  A    C  
ATOM   1670  O   THR A 233      42.239 -35.832   2.666  1.00111.72      A    O  
ANISOU 1670  O   THR A 233    17270   8183  16997  -1594  -2584   1128  A    O  
ATOM   1671  CB  THR A 233      40.988 -38.332   0.758  1.00115.44      A    C  
ANISOU 1671  CB  THR A 233    18193   8042  17625  -1882  -2722    825  A    C  
ATOM   1672  CG2 THR A 233      41.496 -39.422  -0.175  1.00116.23      A    C  
ANISOU 1672  CG2 THR A 233    18510   7794  17858  -1697  -2854    631  A    C  
ATOM   1673  OG1 THR A 233      41.006 -38.813   2.109  1.00118.01      A    O  
ANISOU 1673  OG1 THR A 233    18766   8158  17914  -2010  -2814   1082  A    O  
ATOM   1674  N   GLU A 234      40.271 -35.499   1.627  1.00104.37      A    N  
ANISOU 1674  N   GLU A 234    16146   7533  15977  -2025  -2381    995  A    N  
ATOM   1675  CA  GLU A 234      39.764 -34.590   2.650  1.00106.20      A    C  
ANISOU 1675  CA  GLU A 234    16244   8034  16072  -2194  -2269   1180  A    C  
ATOM   1676  C   GLU A 234      39.839 -35.187   4.063  1.00111.91      A    C  
ANISOU 1676  C   GLU A 234    17241   8531  16751  -2323  -2365   1431  A    C  
ATOM   1677  O   GLU A 234      40.208 -34.502   5.022  1.00106.38      A    O  
ANISOU 1677  O   GLU A 234    16481   7968  15970  -2269  -2341   1576  A    O  
ATOM   1678  CB  GLU A 234      38.330 -34.163   2.329  1.00107.52      A    C  
ANISOU 1678  CB  GLU A 234    16243   8467  16146  -2512  -2115   1157  A    C  
ATOM   1679  CG  GLU A 234      38.181 -33.464   0.988  1.00114.65      A    C  
ANISOU 1679  CG  GLU A 234    16867   9626  17068  -2396  -2016    928  A    C  
ATOM   1680  CD  GLU A 234      36.893 -32.672   0.891  1.00121.42      A    C  
ANISOU 1680  CD  GLU A 234    17490  10835  17810  -2649  -1851    938  A    C  
ATOM   1681  OE1 GLU A 234      36.125 -32.678   1.876  1.00124.91      A    O  
ANISOU 1681  OE1 GLU A 234    17975  11328  18158  -2913  -1804   1116  A    O  
ATOM   1682  OE2 GLU A 234      36.651 -32.040  -0.161  1.00119.43      A    O1-
ANISOU 1682  OE2 GLU A 234    17009  10815  17554  -2575  -1768    771  A    O1-
ATOM   1683  N   GLN A 235      39.490 -36.463   4.191  1.00118.83      A    N  
ANISOU 1683  N   GLN A 235    18430   9052  17667  -2501  -2481   1484  A    N  
ATOM   1684  CA  GLN A 235      39.565 -37.127   5.489  1.00121.97      A    C  
ANISOU 1684  CA  GLN A 235    19124   9202  18017  -2629  -2586   1729  A    C  
ATOM   1685  C   GLN A 235      41.004 -37.263   5.974  1.00114.64      A    C  
ANISOU 1685  C   GLN A 235    18310   8094  17157  -2271  -2739   1782  A    C  
ATOM   1686  O   GLN A 235      41.283 -37.094   7.162  1.00111.17      A    O  
ANISOU 1686  O   GLN A 235    17956   7651  16634  -2287  -2776   1988  A    O  
ATOM   1687  CB  GLN A 235      38.874 -38.489   5.457  1.00130.87      A    C  
ANISOU 1687  CB  GLN A 235    20583   9965  19176  -2910  -2681   1773  A    C  
ATOM   1688  CG  GLN A 235      37.373 -38.398   5.639  1.00142.04      A    C  
ANISOU 1688  CG  GLN A 235    21934  11561  20474  -3361  -2542   1846  A    C  
ATOM   1689  CD  GLN A 235      36.781 -39.663   6.227  1.00159.23      A    C  
ANISOU 1689  CD  GLN A 235    24486  13379  22635  -3693  -2642   2007  A    C  
ATOM   1690  NE2 GLN A 235      35.669 -39.517   6.942  1.00163.07      A    N  
ANISOU 1690  NE2 GLN A 235    24943  14035  22981  -4082  -2526   2169  A    N  
ATOM   1691  OE1 GLN A 235      37.314 -40.760   6.042  1.00166.85      A    O  
ANISOU 1691  OE1 GLN A 235    25769  13920  23708  -3600  -2819   1985  A    O  
ATOM   1692  N   HIS A 236      41.915 -37.568   5.056  1.00108.62      A    N  
ANISOU 1692  N   HIS A 236    17539   7195  16536  -1946  -2827   1593  A    N  
ATOM   1693  CA  HIS A 236      43.328 -37.643   5.398  1.00106.12      A    C  
ANISOU 1693  CA  HIS A 236    17277   6750  16294  -1574  -2968   1617  A    C  
ATOM   1694  C   HIS A 236      43.831 -36.261   5.806  1.00108.96      A    C  
ANISOU 1694  C   HIS A 236    17326   7496  16579  -1433  -2869   1652  A    C  
ATOM   1695  O   HIS A 236      44.608 -36.120   6.757  1.00109.71      A    O  
ANISOU 1695  O   HIS A 236    17476   7559  16647  -1297  -2961   1800  A    O  
ATOM   1696  CB  HIS A 236      44.141 -38.197   4.224  1.00106.89      A    C  
ANISOU 1696  CB  HIS A 236    17390   6667  16554  -1251  -3054   1381  A    C  
ATOM   1697  CG  HIS A 236      45.574 -38.476   4.559  1.00114.93      A    C  
ANISOU 1697  CG  HIS A 236    18486   7519  17665   -864  -3218   1403  A    C  
ATOM   1698  CD2 HIS A 236      46.181 -38.726   5.745  1.00118.92      A    C  
ANISOU 1698  CD2 HIS A 236    19162   7874  18147   -787  -3358   1614  A    C  
ATOM   1699  ND1 HIS A 236      46.573 -38.498   3.608  1.00114.88      A    N  
ANISOU 1699  ND1 HIS A 236    18357   7509  17784   -490  -3254   1189  A    N  
ATOM   1700  CE1 HIS A 236      47.728 -38.761   4.191  1.00115.12      A    C  
ANISOU 1700  CE1 HIS A 236    18467   7398  17874   -196  -3409   1265  A    C  
ATOM   1701  NE2 HIS A 236      47.520 -38.901   5.488  1.00119.24      A    N  
ANISOU 1701  NE2 HIS A 236    19171   7826  18308   -367  -3482   1523  A    N  
ATOM   1702  N   GLN A 237      43.370 -35.239   5.089  1.00103.66      A    N  
ANISOU 1702  N   GLN A 237    16338   7180  15868  -1473  -2689   1519  A    N  
ATOM   1703  CA  GLN A 237      43.729 -33.861   5.390  1.00100.82      A    C  
ANISOU 1703  CA  GLN A 237    15688   7188  15430  -1370  -2581   1538  A    C  
ATOM   1704  C   GLN A 237      43.228 -33.480   6.780  1.00101.19      A    C  
ANISOU 1704  C   GLN A 237    15798   7328  15322  -1602  -2546   1780  A    C  
ATOM   1705  O   GLN A 237      43.970 -32.910   7.582  1.00 91.05      A    O  
ANISOU 1705  O   GLN A 237    14469   6135  13989  -1468  -2582   1882  A    O  
ATOM   1706  CB  GLN A 237      43.150 -32.909   4.337  1.00 97.37      A    C  
ANISOU 1706  CB  GLN A 237    14941   7087  14970  -1407  -2395   1360  A    C  
ATOM   1707  CG  GLN A 237      43.800 -31.534   4.315  1.00 99.80      A    C  
ANISOU 1707  CG  GLN A 237    14952   7728  15238  -1216  -2303   1323  A    C  
ATOM   1708  CD  GLN A 237      45.270 -31.580   3.914  1.00102.19      A    C  
ANISOU 1708  CD  GLN A 237    15200   7966  15660   -841  -2408   1222  A    C  
ATOM   1709  NE2 GLN A 237      45.572 -32.319   2.850  1.00103.21      A    N  
ANISOU 1709  NE2 GLN A 237    15373   7930  15912   -692  -2460   1046  A    N  
ATOM   1710  OE1 GLN A 237      46.123 -30.961   4.558  1.00100.08      A    O  
ANISOU 1710  OE1 GLN A 237    14850   7806  15371   -691  -2441   1299  A    O  
ATOM   1711  N   LEU A 238      41.968 -33.806   7.062  1.00106.82      A    N  
ANISOU 1711  N   LEU A 238    16612   8026  15949  -1954  -2473   1866  A    N  
ATOM   1712  CA  LEU A 238      41.377 -33.490   8.360  1.00109.91      A    C  
ANISOU 1712  CA  LEU A 238    17067   8518  16176  -2199  -2418   2091  A    C  
ATOM   1713  C   LEU A 238      42.082 -34.239   9.483  1.00113.80      A    C  
ANISOU 1713  C   LEU A 238    17863   8718  16656  -2148  -2603   2290  A    C  
ATOM   1714  O   LEU A 238      42.211 -33.735  10.601  1.00113.61      A    O  
ANISOU 1714  O   LEU A 238    17857   8806  16505  -2190  -2594   2459  A    O  
ATOM   1715  CB  LEU A 238      39.879 -33.791   8.372  1.00110.87      A    C  
ANISOU 1715  CB  LEU A 238    17228   8683  16216  -2595  -2303   2136  A    C  
ATOM   1716  CG  LEU A 238      38.969 -32.590   8.110  1.00112.42      A    C  
ANISOU 1716  CG  LEU A 238    17102   9304  16309  -2724  -2081   2071  A    C  
ATOM   1717  CD1 LEU A 238      37.526 -33.041   7.928  1.00117.27      A    C  
ANISOU 1717  CD1 LEU A 238    17735   9950  16871  -3096  -1987   2087  A    C  
ATOM   1718  CD2 LEU A 238      39.081 -31.568   9.237  1.00104.06      A    C  
ANISOU 1718  CD2 LEU A 238    15954   8486  15098  -2723  -2003   2215  A    C  
ATOM   1719  N   ALA A 239      42.540 -35.448   9.178  1.00112.88      A    N  
ANISOU 1719  N   ALA A 239    17999   8223  16668  -2048  -2774   2268  A    N  
ATOM   1720  CA  ALA A 239      43.292 -36.225  10.144  1.00110.80      A    C  
ANISOU 1720  CA  ALA A 239    18039   7652  16409  -1955  -2974   2449  A    C  
ATOM   1721  C   ALA A 239      44.641 -35.560  10.358  1.00108.41      A    C  
ANISOU 1721  C   ALA A 239    17586   7462  16141  -1589  -3053   2428  A    C  
ATOM   1722  O   ALA A 239      45.054 -35.337  11.496  1.00114.11      A    O  
ANISOU 1722  O   ALA A 239    18387   8204  16766  -1573  -3122   2612  A    O  
ATOM   1723  CB  ALA A 239      43.468 -37.656   9.662  1.00107.68      A    C  
ANISOU 1723  CB  ALA A 239    17947   6812  16153  -1906  -3141   2408  A    C  
ATOM   1724  N   LEU A 240      45.323 -35.241   9.261  1.00 98.96      A    N  
ANISOU 1724  N   LEU A 240    16171   6354  15076  -1304  -3042   2205  A    N  
ATOM   1725  CA  LEU A 240      46.639 -34.616   9.347  1.00103.15      A    C  
ANISOU 1725  CA  LEU A 240    16529   7010  15652   -960  -3111   2166  A    C  
ATOM   1726  C   LEU A 240      46.590 -33.334  10.172  1.00101.82      A    C  
ANISOU 1726  C   LEU A 240    16172   7188  15329  -1039  -3007   2268  A    C  
ATOM   1727  O   LEU A 240      47.432 -33.128  11.050  1.00 99.48      A    O  
ANISOU 1727  O   LEU A 240    15906   6898  14994   -902  -3122   2390  A    O  
ATOM   1728  CB  LEU A 240      47.216 -34.348   7.956  1.00104.63      A    C  
ANISOU 1728  CB  LEU A 240    16474   7300  15982   -693  -3068   1900  A    C  
ATOM   1729  CG  LEU A 240      47.809 -35.580   7.270  1.00113.57      A    C  
ANISOU 1729  CG  LEU A 240    17792   8075  17282   -469  -3225   1790  A    C  
ATOM   1730  CD1 LEU A 240      48.451 -35.217   5.943  1.00115.42      A    C  
ANISOU 1730  CD1 LEU A 240    17764   8454  17635   -192  -3165   1526  A    C  
ATOM   1731  CD2 LEU A 240      48.820 -36.242   8.183  1.00117.03      A    C  
ANISOU 1731  CD2 LEU A 240    18446   8262  17760   -261  -3451   1940  A    C  
ATOM   1732  N   ILE A 241      45.596 -32.492   9.890  1.00 98.50      A    N  
ANISOU 1732  N   ILE A 241    15560   7049  14817  -1255  -2797   2216  A    N  
ATOM   1733  CA  ILE A 241      45.372 -31.252  10.638  1.00101.72      A    C  
ANISOU 1733  CA  ILE A 241    15803   7781  15064  -1354  -2675   2299  A    C  
ATOM   1734  C   ILE A 241      45.223 -31.497  12.142  1.00103.92      A    C  
ANISOU 1734  C   ILE A 241    16319   7971  15194  -1519  -2748   2556  A    C  
ATOM   1735  O   ILE A 241      45.743 -30.737  12.961  1.00 99.49      A    O  
ANISOU 1735  O   ILE A 241    15698   7569  14536  -1455  -2766   2642  A    O  
ATOM   1736  CB  ILE A 241      44.123 -30.477  10.117  1.00 87.84      A    C  
ANISOU 1736  CB  ILE A 241    13846   6302  13226  -1583  -2439   2214  A    C  
ATOM   1737  CG1 ILE A 241      44.444 -29.746   8.807  1.00 83.95      A    C  
ANISOU 1737  CG1 ILE A 241    13059   6008  12832  -1389  -2348   1979  A    C  
ATOM   1738  CG2 ILE A 241      43.622 -29.479  11.164  1.00 80.98      A    C  
ANISOU 1738  CG2 ILE A 241    12912   5693  12165  -1753  -2321   2348  A    C  
ATOM   1739  CD1 ILE A 241      43.268 -28.980   8.224  1.00 77.09      A    C  
ANISOU 1739  CD1 ILE A 241    11989   5409  11891  -1576  -2136   1890  A    C  
ATOM   1740  N   SER A 242      44.510 -32.559  12.500  1.00107.88      A    N  
ANISOU 1740  N   SER A 242    17100   8220  15671  -1743  -2794   2677  A    N  
ATOM   1741  CA  SER A 242      44.320 -32.910  13.903  1.00111.37      A    C  
ANISOU 1741  CA  SER A 242    17799   8554  15962  -1921  -2865   2932  A    C  
ATOM   1742  C   SER A 242      45.625 -33.364  14.550  1.00109.91      A    C  
ANISOU 1742  C   SER A 242    17784   8159  15819  -1660  -3106   3036  A    C  
ATOM   1743  O   SER A 242      45.880 -33.081  15.722  1.00105.13      A    O  
ANISOU 1743  O   SER A 242    17270   7606  15071  -1696  -3162   3214  A    O  
ATOM   1744  CB  SER A 242      43.246 -33.991  14.052  1.00118.76      A    C  
ANISOU 1744  CB  SER A 242    19002   9255  16866  -2239  -2856   3037  A    C  
ATOM   1745  OG  SER A 242      41.945 -33.435  13.961  1.00120.47      A    O  
ANISOU 1745  OG  SER A 242    19073   9730  16971  -2540  -2630   3019  A    O  
ATOM   1746  N   GLN A 243      46.448 -34.065  13.776  1.00113.49      A    N  
ANISOU 1746  N   GLN A 243    18273   8386  16463  -1390  -3251   2921  A    N  
ATOM   1747  CA  GLN A 243      47.725 -34.563  14.274  1.00117.52      A    C  
ANISOU 1747  CA  GLN A 243    18921   8694  17036  -1103  -3493   3001  A    C  
ATOM   1748  C   GLN A 243      48.739 -33.433  14.436  1.00116.60      A    C  
ANISOU 1748  C   GLN A 243    18526   8868  16907   -864  -3503   2948  A    C  
ATOM   1749  O   GLN A 243      49.850 -33.650  14.929  1.00117.96      A    O  
ANISOU 1749  O   GLN A 243    18757   8947  17116   -622  -3701   3017  A    O  
ATOM   1750  CB  GLN A 243      48.273 -35.652  13.349  1.00121.21      A    C  
ANISOU 1750  CB  GLN A 243    19501   8839  17715   -869  -3633   2874  A    C  
ATOM   1751  CG  GLN A 243      47.447 -36.932  13.345  1.00127.92      A    C  
ANISOU 1751  CG  GLN A 243    20701   9322  18579  -1092  -3681   2954  A    C  
ATOM   1752  CD  GLN A 243      47.825 -37.854  12.206  1.00131.15      A    C  
ANISOU 1752  CD  GLN A 243    21183   9453  19195   -878  -3772   2770  A    C  
ATOM   1753  NE2 GLN A 243      47.148 -38.995  12.108  1.00122.98      A    N  
ANISOU 1753  NE2 GLN A 243    20465   8073  18187  -1066  -3825   2818  A    N  
ATOM   1754  OE1 GLN A 243      48.715 -37.540  11.414  1.00138.23      A    O  
ANISOU 1754  OE1 GLN A 243    21856  10445  20219   -552  -3791   2583  A    O  
ATOM   1755  N   LEU A 244      48.349 -32.228  14.028  1.00108.24      A    N  
ANISOU 1755  N   LEU A 244    17167   8163  15795   -937  -3297   2830  A    N  
ATOM   1756  CA  LEU A 244      49.212 -31.061  14.176  1.00 99.10      A    C  
ANISOU 1756  CA  LEU A 244    15748   7294  14612   -758  -3288   2778  A    C  
ATOM   1757  C   LEU A 244      48.627 -30.003  15.102  1.00 99.42      A    C  
ANISOU 1757  C   LEU A 244    15733   7604  14437   -983  -3156   2886  A    C  
ATOM   1758  O   LEU A 244      49.329 -29.460  15.957  1.00100.72      A    O  
ANISOU 1758  O   LEU A 244    15879   7876  14513   -907  -3242   2976  A    O  
ATOM   1759  CB  LEU A 244      49.523 -30.427  12.822  1.00 94.37      A    C  
ANISOU 1759  CB  LEU A 244    14827   6884  14146   -584  -3175   2526  A    C  
ATOM   1760  CG  LEU A 244      50.577 -29.318  12.916  1.00 93.45      A    C  
ANISOU 1760  CG  LEU A 244    14450   7033  14025   -385  -3190   2472  A    C  
ATOM   1761  CD1 LEU A 244      51.914 -29.918  13.296  1.00 93.80      A    C  
ANISOU 1761  CD1 LEU A 244    14565   6915  14160   -102  -3439   2526  A    C  
ATOM   1762  CD2 LEU A 244      50.690 -28.545  11.614  1.00 92.97      A    C  
ANISOU 1762  CD2 LEU A 244    14073   7194  14056   -278  -3038   2239  A    C  
ATOM   1763  N   CYS A 245      47.344 -29.705  14.932  1.00 99.54      A    N  
ANISOU 1763  N   CYS A 245    15719   7738  14364  -1254  -2951   2869  A    N  
ATOM   1764  CA  CYS A 245      46.747 -28.568  15.626  1.00108.47      A    C  
ANISOU 1764  CA  CYS A 245    16751   9163  15300  -1437  -2791   2924  A    C  
ATOM   1765  C   CYS A 245      45.871 -28.979  16.806  1.00107.71      A    C  
ANISOU 1765  C   CYS A 245    16914   8996  15016  -1730  -2771   3142  A    C  
ATOM   1766  O   CYS A 245      45.108 -28.168  17.332  1.00100.87      A    O  
ANISOU 1766  O   CYS A 245    15986   8364  13977  -1920  -2606   3182  A    O  
ATOM   1767  CB  CYS A 245      45.936 -27.713  14.642  1.00115.57      A    C  
ANISOU 1767  CB  CYS A 245    17385  10314  16211  -1514  -2556   2746  A    C  
ATOM   1768  SG  CYS A 245      46.795 -27.310  13.088  1.00104.70      A    S  
ANISOU 1768  SG  CYS A 245    15716   9019  15048  -1210  -2549   2483  A    S  
ATOM   1769  N   GLY A 246      45.995 -30.232  17.227  1.00113.29      A    N  
ANISOU 1769  N   GLY A 246    17916   9379  15747  -1758  -2938   3284  A    N  
ATOM   1770  CA  GLY A 246      45.083 -30.787  18.210  1.00115.75      A    C  
ANISOU 1770  CA  GLY A 246    18495   9593  15891  -2065  -2912   3493  A    C  
ATOM   1771  C   GLY A 246      43.846 -31.251  17.475  1.00120.43      A    C  
ANISOU 1771  C   GLY A 246    19084  10148  16524  -2301  -2758   3429  A    C  
ATOM   1772  O   GLY A 246      43.820 -31.242  16.247  1.00116.27      A    O  
ANISOU 1772  O   GLY A 246    18384   9633  16160  -2197  -2708   3232  A    O  
ATOM   1773  N   SER A 247      42.815 -31.654  18.206  1.00130.20      A    N  
ANISOU 1773  N   SER A 247    20506  11354  17608  -2627  -2680   3592  A    N  
ATOM   1774  CA  SER A 247      41.616 -32.168  17.553  1.00130.95      A    C  
ANISOU 1774  CA  SER A 247    20604  11413  17738  -2881  -2546   3543  A    C  
ATOM   1775  C   SER A 247      40.445 -31.196  17.613  1.00128.71      A    C  
ANISOU 1775  C   SER A 247    20095  11499  17309  -3109  -2279   3504  A    C  
ATOM   1776  O   SER A 247      40.337 -30.377  18.529  1.00125.93      A    O  
ANISOU 1776  O   SER A 247    19703  11371  16773  -3163  -2195   3590  A    O  
ATOM   1777  CB  SER A 247      41.224 -33.533  18.124  1.00135.97      A    C  
ANISOU 1777  CB  SER A 247    21614  11708  18341  -3107  -2656   3741  A    C  
ATOM   1778  OG  SER A 247      41.217 -33.513  19.538  1.00139.74      A    O  
ANISOU 1778  OG  SER A 247    22293  12195  18608  -3241  -2688   3978  A    O  
ATOM   1779  N   ILE A 248      39.576 -31.297  16.614  1.00127.94      A    N  
ANISOU 1779  N   ILE A 248    19852  11464  17295  -3229  -2150   3367  A    N  
ATOM   1780  CA  ILE A 248      38.423 -30.417  16.485  1.00121.02      A    C  
ANISOU 1780  CA  ILE A 248    18733  10942  16309  -3418  -1900   3304  A    C  
ATOM   1781  C   ILE A 248      37.473 -30.618  17.663  1.00120.76      A    C  
ANISOU 1781  C   ILE A 248    18852  10974  16056  -3758  -1800   3514  A    C  
ATOM   1782  O   ILE A 248      36.786 -31.636  17.754  1.00113.99      A    O  
ANISOU 1782  O   ILE A 248    18179   9940  15194  -4021  -1811   3614  A    O  
ATOM   1783  CB  ILE A 248      37.670 -30.691  15.166  1.00115.32      A    C  
ANISOU 1783  CB  ILE A 248    17854  10238  15724  -3496  -1816   3129  A    C  
ATOM   1784  CG1 ILE A 248      38.604 -31.323  14.125  1.00110.58      A    C  
ANISOU 1784  CG1 ILE A 248    17293   9370  15352  -3238  -1989   2989  A    C  
ATOM   1785  CG2 ILE A 248      37.030 -29.421  14.633  1.00100.53      A    C  
ANISOU 1785  CG2 ILE A 248    15628   8762  13808  -3480  -1601   2976  A    C  
ATOM   1786  CD1 ILE A 248      39.527 -30.351  13.442  1.00 87.77      A    C  
ANISOU 1786  CD1 ILE A 248    14157   6639  12554  -2896  -1993   2812  A    C  
ATOM   1787  N   THR A 249      37.441 -29.643  18.564  1.00126.88      A    N  
ANISOU 1787  N   THR A 249    19557  12004  16646  -3759  -1701   3578  A    N  
ATOM   1788  CA  THR A 249      36.648 -29.749  19.780  1.00134.00      A    C  
ANISOU 1788  CA  THR A 249    20607  12994  17313  -4056  -1600   3779  A    C  
ATOM   1789  C   THR A 249      35.777 -28.521  19.961  1.00128.62      A    C  
ANISOU 1789  C   THR A 249    19658  12734  16479  -4135  -1344   3713  A    C  
ATOM   1790  O   THR A 249      36.264 -27.402  19.873  1.00124.23      A    O  
ANISOU 1790  O   THR A 249    18922  12371  15911  -3909  -1305   3601  A    O  
ATOM   1791  CB  THR A 249      37.551 -29.873  21.015  1.00139.96      A    C  
ANISOU 1791  CB  THR A 249    21622  13615  17942  -3980  -1757   3968  A    C  
ATOM   1792  CG2 THR A 249      36.717 -29.947  22.281  1.00143.91      A    C  
ANISOU 1792  CG2 THR A 249    22277  14224  18175  -4293  -1638   4176  A    C  
ATOM   1793  OG1 THR A 249      38.352 -31.055  20.903  1.00143.30      A    O  
ANISOU 1793  OG1 THR A 249    22310  13634  18503  -3891  -2006   4043  A    O  
ATOM   1794  N   PRO A 250      34.480 -28.727  20.222  1.00127.77      A    N  
ANISOU 1794  N   PRO A 250    19524  12770  16251  -4458  -1167   3780  A    N  
ATOM   1795  CA  PRO A 250      33.587 -27.595  20.485  1.00124.22      A    C  
ANISOU 1795  CA  PRO A 250    18827  12730  15640  -4530   -915   3725  A    C  
ATOM   1796  C   PRO A 250      34.129 -26.724  21.615  1.00120.90      A    C  
ANISOU 1796  C   PRO A 250    18469  12442  15024  -4417   -901   3799  A    C  
ATOM   1797  O   PRO A 250      33.716 -25.573  21.762  1.00119.02      A    O  
ANISOU 1797  O   PRO A 250    18025  12524  14674  -4366   -724   3713  A    O  
ATOM   1798  CB  PRO A 250      32.282 -28.273  20.906  1.00123.66      A    C  
ANISOU 1798  CB  PRO A 250    18812  12726  15447  -4929   -775   3856  A    C  
ATOM   1799  CG  PRO A 250      32.325 -29.604  20.232  1.00119.95      A    C  
ANISOU 1799  CG  PRO A 250    18504  11915  15157  -5040   -928   3879  A    C  
ATOM   1800  CD  PRO A 250      33.768 -30.016  20.251  1.00121.97      A    C  
ANISOU 1800  CD  PRO A 250    18983  11831  15531  -4773  -1190   3905  A    C  
ATOM   1801  N   GLU A 251      35.046 -27.273  22.404  1.00120.08      A    N  
ANISOU 1801  N   GLU A 251    18656  12089  14879  -4371  -1096   3954  A    N  
ATOM   1802  CA  GLU A 251      35.696 -26.507  23.454  1.00121.70      A    C  
ANISOU 1802  CA  GLU A 251    18942  12393  14907  -4252  -1122   4022  A    C  
ATOM   1803  C   GLU A 251      36.743 -25.600  22.840  1.00115.72      A    C  
ANISOU 1803  C   GLU A 251    18014  11673  14280  -3900  -1207   3842  A    C  
ATOM   1804  O   GLU A 251      36.859 -24.427  23.195  1.00113.56      A    O  
ANISOU 1804  O   GLU A 251    17621  11637  13890  -3793  -1115   3775  A    O  
ATOM   1805  CB  GLU A 251      36.368 -27.429  24.462  1.00132.56      A    C  
ANISOU 1805  CB  GLU A 251    20684  13486  16195  -4313  -1326   4251  A    C  
ATOM   1806  CG  GLU A 251      37.444 -26.729  25.263  1.00141.64      A    C  
ANISOU 1806  CG  GLU A 251    21912  14666  17237  -4099  -1444   4284  A    C  
ATOM   1807  CD  GLU A 251      38.253 -27.680  26.108  1.00154.41      A    C  
ANISOU 1807  CD  GLU A 251    23882  15980  18804  -4106  -1689   4498  A    C  
ATOM   1808  OE1 GLU A 251      37.714 -28.740  26.491  1.00158.67      A    O  
ANISOU 1808  OE1 GLU A 251    24650  16348  19287  -4356  -1704   4673  A    O  
ATOM   1809  OE2 GLU A 251      39.429 -27.366  26.391  1.00158.02      A    O1-
ANISOU 1809  OE2 GLU A 251    24391  16373  19278  -3865  -1871   4496  A    O1-
ATOM   1810  N   VAL A 252      37.511 -26.163  21.917  1.00112.24      A    N  
ANISOU 1810  N   VAL A 252    17573  10993  14080  -3726  -1382   3766  A    N  
ATOM   1811  CA  VAL A 252      38.551 -25.434  21.209  1.00105.47      A    C  
ANISOU 1811  CA  VAL A 252    16547  10155  13371  -3401  -1471   3597  A    C  
ATOM   1812  C   VAL A 252      37.934 -24.504  20.159  1.00110.29      A    C  
ANISOU 1812  C   VAL A 252    16829  11021  14055  -3342  -1280   3383  A    C  
ATOM   1813  O   VAL A 252      38.341 -23.349  20.000  1.00108.74      A    O  
ANISOU 1813  O   VAL A 252    16464  11005  13847  -3159  -1234   3264  A    O  
ATOM   1814  CB  VAL A 252      39.541 -26.431  20.555  1.00 97.75      A    C  
ANISOU 1814  CB  VAL A 252    15679   8840  12622  -3235  -1712   3584  A    C  
ATOM   1815  CG1 VAL A 252      40.313 -25.791  19.437  1.00 95.82      A    C  
ANISOU 1815  CG1 VAL A 252    15194   8646  12566  -2945  -1748   3372  A    C  
ATOM   1816  CG2 VAL A 252      40.500 -26.980  21.596  1.00 99.69      A    C  
ANISOU 1816  CG2 VAL A 252    16207   8871  12797  -3178  -1932   3768  A    C  
ATOM   1817  N   TRP A 253      36.918 -25.017  19.480  1.00112.44      A    N  
ANISOU 1817  N   TRP A 253    17022  11308  14393  -3513  -1173   3343  A    N  
ATOM   1818  CA  TRP A 253      36.295 -24.354  18.344  1.00103.56      A    C  
ANISOU 1818  CA  TRP A 253    15597  10389  13361  -3461  -1022   3147  A    C  
ATOM   1819  C   TRP A 253      34.785 -24.315  18.572  1.00104.05      A    C  
ANISOU 1819  C   TRP A 253    15573  10672  13289  -3741   -802   3181  A    C  
ATOM   1820  O   TRP A 253      34.053 -25.182  18.084  1.00 98.54      A    O  
ANISOU 1820  O   TRP A 253    14878   9900  12662  -3931   -781   3191  A    O  
ATOM   1821  CB  TRP A 253      36.611 -25.159  17.085  1.00102.05      A    C  
ANISOU 1821  CB  TRP A 253    15378   9982  13414  -3377  -1140   3040  A    C  
ATOM   1822  CG  TRP A 253      36.074 -24.614  15.809  1.00 97.74      A    C  
ANISOU 1822  CG  TRP A 253    14546   9613  12978  -3312  -1020   2839  A    C  
ATOM   1823  CD1 TRP A 253      35.163 -23.612  15.656  1.00 93.31      A    C  
ANISOU 1823  CD1 TRP A 253    13754   9375  12324  -3353   -812   2757  A    C  
ATOM   1824  CD2 TRP A 253      36.390 -25.078  14.492  1.00 90.32      A    C  
ANISOU 1824  CD2 TRP A 253    13529   8533  12252  -3192  -1104   2694  A    C  
ATOM   1825  CE2 TRP A 253      35.644 -24.302  13.585  1.00 84.56      A    C  
ANISOU 1825  CE2 TRP A 253    12523   8061  11544  -3174   -944   2536  A    C  
ATOM   1826  CE3 TRP A 253      37.238 -26.068  13.991  1.00 89.55      A    C  
ANISOU 1826  CE3 TRP A 253    13578   8123  12325  -3084  -1299   2678  A    C  
ATOM   1827  NE1 TRP A 253      34.904 -23.412  14.319  1.00 89.67      A    N  
ANISOU 1827  NE1 TRP A 253    13079   8985  12008  -3266   -771   2579  A    N  
ATOM   1828  CZ2 TRP A 253      35.721 -24.485  12.210  1.00 81.65      A    C  
ANISOU 1828  CZ2 TRP A 253    12024   7649  11350  -3068   -975   2368  A    C  
ATOM   1829  CZ3 TRP A 253      37.313 -26.250  12.630  1.00 89.92      A    C  
ANISOU 1829  CZ3 TRP A 253    13491   8126  12547  -2973  -1320   2502  A    C  
ATOM   1830  CH2 TRP A 253      36.560 -25.461  11.753  1.00 86.22      A    C  
ANISOU 1830  CH2 TRP A 253    12752   7923  12085  -2973  -1159   2351  A    C  
ATOM   1831  N   PRO A 254      34.319 -23.311  19.330  1.00106.57      A    N  
ANISOU 1831  N   PRO A 254    15812  11270  13409  -3769   -636   3196  A    N  
ATOM   1832  CA  PRO A 254      32.918 -23.099  19.713  1.00107.97      A    C  
ANISOU 1832  CA  PRO A 254    15885  11715  13426  -4008   -405   3230  A    C  
ATOM   1833  C   PRO A 254      31.931 -23.312  18.568  1.00109.95      A    C  
ANISOU 1833  C   PRO A 254    15906  12069  13801  -4102   -303   3110  A    C  
ATOM   1834  O   PRO A 254      31.955 -22.564  17.595  1.00108.90      A    O  
ANISOU 1834  O   PRO A 254    15544  12060  13773  -3913   -262   2931  A    O  
ATOM   1835  CB  PRO A 254      32.900 -21.630  20.142  1.00107.13      A    C  
ANISOU 1835  CB  PRO A 254    15642  11891  13172  -3855   -267   3152  A    C  
ATOM   1836  CG  PRO A 254      34.259 -21.400  20.689  1.00108.34      A    C  
ANISOU 1836  CG  PRO A 254    15971  11880  13312  -3667   -444   3193  A    C  
ATOM   1837  CD  PRO A 254      35.201 -22.268  19.882  1.00107.99      A    C  
ANISOU 1837  CD  PRO A 254    16002  11526  13504  -3554   -669   3172  A    C  
ATOM   1838  N   ASN A 255      31.071 -24.319  18.696  1.00118.66      A    N  
ANISOU 1838  N   ASN A 255    17077  13126  14882  -4404   -267   3214  A    N  
ATOM   1839  CA  ASN A 255      30.029 -24.594  17.704  1.00122.55      A    C  
ANISOU 1839  CA  ASN A 255    17356  13735  15472  -4542   -171   3114  A    C  
ATOM   1840  C   ASN A 255      30.471 -25.472  16.535  1.00118.08      A    C  
ANISOU 1840  C   ASN A 255    16829  12890  15148  -4494   -345   3031  A    C  
ATOM   1841  O   ASN A 255      29.667 -25.777  15.651  1.00115.46      A    O  
ANISOU 1841  O   ASN A 255    16336  12631  14902  -4614   -292   2942  A    O  
ATOM   1842  CB  ASN A 255      29.407 -23.298  17.167  1.00123.47      A    C  
ANISOU 1842  CB  ASN A 255    17136  14215  15563  -4400     12   2945  A    C  
ATOM   1843  CG  ASN A 255      28.134 -22.916  17.890  1.00127.96      A    C  
ANISOU 1843  CG  ASN A 255    17574  15117  15926  -4608    248   3002  A    C  
ATOM   1844  ND2 ASN A 255      27.307 -22.105  17.238  1.00126.08      A    N  
ANISOU 1844  ND2 ASN A 255    17026  15186  15694  -4545    404   2857  A    N  
ATOM   1845  OD1 ASN A 255      27.892 -23.345  19.019  1.00132.74      A    O  
ANISOU 1845  OD1 ASN A 255    18354  15715  16366  -4820    289   3175  A    O  
ATOM   1846  N   VAL A 256      31.737 -25.882  16.529  1.00113.58      A    N  
ANISOU 1846  N   VAL A 256    16465  12012  14679  -4316   -553   3055  A    N  
ATOM   1847  CA  VAL A 256      32.245 -26.702  15.431  1.00110.74      A    C  
ANISOU 1847  CA  VAL A 256    16154  11379  14543  -4235   -718   2962  A    C  
ATOM   1848  C   VAL A 256      31.328 -27.890  15.149  1.00118.09      A    C  
ANISOU 1848  C   VAL A 256    17161  12193  15516  -4556   -719   3014  A    C  
ATOM   1849  O   VAL A 256      31.142 -28.285  13.999  1.00115.51      A    O  
ANISOU 1849  O   VAL A 256    16743  11799  15345  -4550   -760   2880  A    O  
ATOM   1850  CB  VAL A 256      33.673 -27.217  15.682  1.00101.42      A    C  
ANISOU 1850  CB  VAL A 256    15228   9859  13448  -4040   -950   3021  A    C  
ATOM   1851  CG1 VAL A 256      33.730 -28.068  16.944  1.00103.02      A    C  
ANISOU 1851  CG1 VAL A 256    15751   9866  13525  -4242  -1025   3260  A    C  
ATOM   1852  CG2 VAL A 256      34.147 -28.012  14.481  1.00 92.22      A    C  
ANISOU 1852  CG2 VAL A 256    14093   8437  12512  -3934  -1099   2900  A    C  
ATOM   1853  N   ASP A 257      30.752 -28.458  16.200  1.00129.69      A    N  
ANISOU 1853  N   ASP A 257    18801  13640  16834  -4849   -674   3209  A    N  
ATOM   1854  CA  ASP A 257      29.849 -29.584  16.019  1.00142.55      A    C  
ANISOU 1854  CA  ASP A 257    20515  15160  18486  -5197   -669   3276  A    C  
ATOM   1855  C   ASP A 257      28.519 -29.136  15.427  1.00146.29      A    C  
ANISOU 1855  C   ASP A 257    20659  15990  18935  -5362   -469   3168  A    C  
ATOM   1856  O   ASP A 257      27.526 -28.988  16.141  1.00151.52      A    O  
ANISOU 1856  O   ASP A 257    21245  16897  19428  -5615   -297   3267  A    O  
ATOM   1857  CB  ASP A 257      29.654 -30.344  17.328  1.00146.24      A    C  
ANISOU 1857  CB  ASP A 257    21278  15493  18792  -5478   -681   3532  A    C  
ATOM   1858  CG  ASP A 257      30.775 -31.326  17.593  1.00152.76      A    C  
ANISOU 1858  CG  ASP A 257    22476  15864  19702  -5392   -932   3640  A    C  
ATOM   1859  OD1 ASP A 257      31.531 -31.642  16.646  1.00148.79      A    O  
ANISOU 1859  OD1 ASP A 257    21997  15132  19402  -5171  -1091   3509  A    O  
ATOM   1860  OD2 ASP A 257      30.898 -31.786  18.745  1.00162.67      A    O1-
ANISOU 1860  OD2 ASP A 257    23999  16993  20814  -5539   -971   3857  A    O1-
ATOM   1861  N   ASN A 258      28.526 -28.918  14.113  1.00139.60      A    N  
ANISOU 1861  N   ASN A 258    19611  15180  18251  -5208   -494   2962  A    N  
ATOM   1862  CA  ASN A 258      27.337 -28.537  13.363  1.00130.81      A    C  
ANISOU 1862  CA  ASN A 258    18174  14386  17140  -5330   -341   2839  A    C  
ATOM   1863  C   ASN A 258      27.448 -28.904  11.882  1.00127.61      A    C  
ANISOU 1863  C   ASN A 258    17685  13862  16938  -5240   -449   2650  A    C  
ATOM   1864  O   ASN A 258      27.181 -28.069  11.023  1.00123.60      A    O  
ANISOU 1864  O   ASN A 258    16892  13600  16471  -5080   -374   2481  A    O  
ATOM   1865  CB  ASN A 258      27.066 -27.034  13.500  1.00121.43      A    C  
ANISOU 1865  CB  ASN A 258    16695  13599  15845  -5136   -161   2759  A    C  
ATOM   1866  CG  ASN A 258      26.328 -26.678  14.783  1.00124.39      A    C  
ANISOU 1866  CG  ASN A 258    17050  14223  15992  -5327     20   2910  A    C  
ATOM   1867  ND2 ASN A 258      26.401 -25.413  15.174  1.00118.90      A    N  
ANISOU 1867  ND2 ASN A 258    16203  13786  15185  -5116    144   2867  A    N  
ATOM   1868  OD1 ASN A 258      25.693 -27.525  15.406  1.00136.87      A    O  
ANISOU 1868  OD1 ASN A 258    18754  15761  17491  -5666     52   3062  A    O  
ATOM   1869  N   TYR A 259      27.844 -30.141  11.574  1.00128.88      A    N  
ANISOU 1869  N   TYR A 259    18107  13643  17220  -5335   -625   2674  A    N  
ATOM   1870  CA  TYR A 259      27.889 -30.566  10.174  1.00131.69      A    C  
ANISOU 1870  CA  TYR A 259    18402  13881  17755  -5274   -724   2489  A    C  
ATOM   1871  C   TYR A 259      27.801 -32.062   9.912  1.00125.05      A    C  
ANISOU 1871  C   TYR A 259    17833  12670  17010  -5518   -874   2528  A    C  
ATOM   1872  O   TYR A 259      26.812 -32.523   9.359  1.00128.61      A    O  
ANISOU 1872  O   TYR A 259    18189  13196  17480  -5786   -839   2478  A    O  
ATOM   1873  CB  TYR A 259      29.111 -30.014   9.452  1.00145.99      A    C  
ANISOU 1873  CB  TYR A 259    20185  15599  19687  -4849   -823   2337  A    C  
ATOM   1874  CG  TYR A 259      29.071 -30.302   7.970  1.00151.91      A    C  
ANISOU 1874  CG  TYR A 259    20835  16293  20592  -4777   -894   2129  A    C  
ATOM   1875  CD1 TYR A 259      28.620 -29.340   7.073  1.00148.37      A    C  
ANISOU 1875  CD1 TYR A 259    20056  16169  20149  -4653   -789   1963  A    C  
ATOM   1876  CD2 TYR A 259      29.458 -31.545   7.468  1.00153.57      A    C  
ANISOU 1876  CD2 TYR A 259    21296  16122  20934  -4832  -1069   2099  A    C  
ATOM   1877  CE1 TYR A 259      28.572 -29.592   5.720  1.00148.48      A    C  
ANISOU 1877  CE1 TYR A 259    19986  16145  20286  -4592   -856   1775  A    C  
ATOM   1878  CE2 TYR A 259      29.413 -31.806   6.112  1.00153.87      A    C  
ANISOU 1878  CE2 TYR A 259    21253  16112  21099  -4767  -1131   1899  A    C  
ATOM   1879  CZ  TYR A 259      28.969 -30.824   5.243  1.00152.25      A    C  
ANISOU 1879  CZ  TYR A 259    20711  16250  20887  -4651  -1023   1739  A    C  
ATOM   1880  OH  TYR A 259      28.916 -31.065   3.890  1.00151.87      A    O  
ANISOU 1880  OH  TYR A 259    20587  16171  20948  -4589  -1085   1540  A    O  
ATOM   1881  N   LEU A 267      36.136 -38.069  12.672  1.00130.94      A    N  
ANISOU 1881  N   LEU A 267    21160  10298  18295  -4337  -2424   3171  A    N  
ATOM   1882  CA  LEU A 267      37.367 -37.430  13.140  1.00132.12      A    C  
ANISOU 1882  CA  LEU A 267    21267  10490  18441  -3966  -2502   3193  A    C  
ATOM   1883  C   LEU A 267      38.016 -38.099  14.343  1.00144.48      A    C  
ANISOU 1883  C   LEU A 267    23194  11761  19942  -3947  -2674   3440  A    C  
ATOM   1884  O   LEU A 267      37.442 -39.003  14.956  1.00144.50      A    O  
ANISOU 1884  O   LEU A 267    23494  11537  19872  -4253  -2715   3623  A    O  
ATOM   1885  CB  LEU A 267      37.104 -35.964  13.480  1.00120.95      A    C  
ANISOU 1885  CB  LEU A 267    19509   9556  16890  -3944  -2304   3177  A    C  
ATOM   1886  CG  LEU A 267      36.649 -35.063  12.334  1.00116.05      A    C  
ANISOU 1886  CG  LEU A 267    18501   9266  16325  -3880  -2141   2937  A    C  
ATOM   1887  CD1 LEU A 267      36.210 -33.709  12.871  1.00110.90      A    C  
ANISOU 1887  CD1 LEU A 267    17571   9055  15511  -3916  -1942   2963  A    C  
ATOM   1888  CD2 LEU A 267      37.761 -34.910  11.313  1.00117.10      A    C  
ANISOU 1888  CD2 LEU A 267    18533   9321  16638  -3479  -2243   2729  A    C  
ATOM   1889  N   VAL A 268      39.220 -37.630  14.671  1.00151.42      A    N  
ANISOU 1889  N   VAL A 268    24041  12651  20841  -3591  -2778   3444  A    N  
ATOM   1890  CA  VAL A 268      39.964 -38.105  15.834  1.00157.94      A    C  
ANISOU 1890  CA  VAL A 268    25173  13242  21596  -3519  -2955   3672  A    C  
ATOM   1891  C   VAL A 268      39.347 -37.523  17.098  1.00159.65      A    C  
ANISOU 1891  C   VAL A 268    25390  13705  21564  -3780  -2827   3881  A    C  
ATOM   1892  O   VAL A 268      38.433 -36.701  17.026  1.00159.59      A    O  
ANISOU 1892  O   VAL A 268    25123  14058  21457  -3971  -2601   3830  A    O  
ATOM   1893  CB  VAL A 268      41.442 -37.673  15.779  1.00151.83      A    C  
ANISOU 1893  CB  VAL A 268    24312  12463  20913  -3057  -3101   3599  A    C  
ATOM   1894  CG1 VAL A 268      42.088 -38.127  14.480  1.00149.20      A    C  
ANISOU 1894  CG1 VAL A 268    23932  11941  20818  -2768  -3201   3368  A    C  
ATOM   1895  CG2 VAL A 268      41.546 -36.171  15.930  1.00143.81      A    C  
ANISOU 1895  CG2 VAL A 268    22934  11904  19804  -2961  -2942   3530  A    C  
ATOM   1896  N   LYS A 269      39.852 -37.939  18.256  1.00156.09      A    N  
ANISOU 1896  N   LYS A 269    25232  13069  21007  -3776  -2972   4114  A    N  
ATOM   1897  CA  LYS A 269      39.275 -37.489  19.517  1.00151.03      A    C  
ANISOU 1897  CA  LYS A 269    24635  12639  20109  -4035  -2857   4325  A    C  
ATOM   1898  C   LYS A 269      40.311 -37.206  20.605  1.00145.89      A    C  
ANISOU 1898  C   LYS A 269    24110  11970  19351  -3824  -3005   4480  A    C  
ATOM   1899  O   LYS A 269      40.053 -36.426  21.521  1.00141.71      A    O  
ANISOU 1899  O   LYS A 269    23512  11718  18613  -3934  -2891   4585  A    O  
ATOM   1900  CB  LYS A 269      38.233 -38.498  20.012  1.00155.56      A    C  
ANISOU 1900  CB  LYS A 269    25508  13018  20581  -4472  -2828   4522  A    C  
ATOM   1901  CG  LYS A 269      37.124 -38.777  18.998  1.00151.75      A    C  
ANISOU 1901  CG  LYS A 269    24894  12578  20186  -4726  -2682   4377  A    C  
ATOM   1902  CD  LYS A 269      36.196 -39.895  19.447  1.00146.87      A    C  
ANISOU 1902  CD  LYS A 269    24598  11720  19486  -5165  -2683   4573  A    C  
ATOM   1903  CE  LYS A 269      35.137 -40.164  18.391  1.00142.51      A    C  
ANISOU 1903  CE  LYS A 269    23897  11220  19031  -5415  -2556   4415  A    C  
ATOM   1904  NZ  LYS A 269      34.132 -41.152  18.858  1.00149.80      A    N1+
ANISOU 1904  NZ  LYS A 269    25098  11964  19856  -5895  -2530   4608  A    N1+
ATOM   1905  N   GLY A 270      41.485 -37.825  20.500  1.00146.83      A    N  
ANISOU 1905  N   GLY A 270    24406  11775  19609  -3513  -3259   4487  A    N  
ATOM   1906  CA  GLY A 270      42.497 -37.691  21.535  1.00151.48      A    C  
ANISOU 1906  CA  GLY A 270    25135  12317  20102  -3313  -3435   4646  A    C  
ATOM   1907  C   GLY A 270      43.656 -36.751  21.235  1.00151.24      A    C  
ANISOU 1907  C   GLY A 270    24820  12484  20159  -2908  -3496   4487  A    C  
ATOM   1908  O   GLY A 270      44.414 -36.382  22.133  1.00148.43      A    O  
ANISOU 1908  O   GLY A 270    24511  12190  19695  -2769  -3609   4604  A    O  
ATOM   1909  N   GLN A 271      43.793 -36.359  19.972  1.00152.21      A    N  
ANISOU 1909  N   GLN A 271    24649  12715  20470  -2731  -3422   4223  A    N  
ATOM   1910  CA  GLN A 271      44.940 -35.571  19.530  1.00152.74      A    C  
ANISOU 1910  CA  GLN A 271    24446  12943  20647  -2346  -3485   4059  A    C  
ATOM   1911  C   GLN A 271      45.155 -34.299  20.355  1.00150.80      A    C  
ANISOU 1911  C   GLN A 271    24019  13057  20220  -2333  -3405   4103  A    C  
ATOM   1912  O   GLN A 271      44.202 -33.681  20.823  1.00152.30      A    O  
ANISOU 1912  O   GLN A 271    24146  13491  20230  -2606  -3206   4154  A    O  
ATOM   1913  CB  GLN A 271      44.800 -35.228  18.046  1.00153.41      A    C  
ANISOU 1913  CB  GLN A 271    24228  13144  20919  -2234  -3360   3774  A    C  
ATOM   1914  CG  GLN A 271      44.639 -36.441  17.138  1.00156.04      A    C  
ANISOU 1914  CG  GLN A 271    24730  13125  21434  -2226  -3441   3695  A    C  
ATOM   1915  CD  GLN A 271      45.931 -37.217  16.948  1.00159.64      A    C  
ANISOU 1915  CD  GLN A 271    25335  13264  22055  -1859  -3705   3677  A    C  
ATOM   1916  NE2 GLN A 271      45.813 -38.530  16.788  1.00165.42      A    N  
ANISOU 1916  NE2 GLN A 271    26393  13585  22875  -1900  -3840   3732  A    N  
ATOM   1917  OE1 GLN A 271      47.020 -36.643  16.940  1.00157.90      A    O  
ANISOU 1917  OE1 GLN A 271    24939  13171  21886  -1543  -3787   3613  A    O  
ATOM   1918  N   LYS A 272      46.416 -33.915  20.524  1.00147.18      A    N  
ANISOU 1918  N   LYS A 272    23476  12635  19809  -2013  -3563   4077  A    N  
ATOM   1919  CA  LYS A 272      46.765 -32.728  21.296  1.00143.21      A    C  
ANISOU 1919  CA  LYS A 272    22820  12450  19144  -1980  -3522   4109  A    C  
ATOM   1920  C   LYS A 272      47.734 -31.849  20.509  1.00140.87      A    C  
ANISOU 1920  C   LYS A 272    22182  12350  18992  -1663  -3533   3892  A    C  
ATOM   1921  O   LYS A 272      48.554 -32.358  19.747  1.00144.52      A    O  
ANISOU 1921  O   LYS A 272    22604  12646  19662  -1394  -3672   3786  A    O  
ATOM   1922  CB  LYS A 272      47.379 -33.133  22.635  1.00145.33      A    C  
ANISOU 1922  CB  LYS A 272    23375  12577  19266  -1957  -3737   4356  A    C  
ATOM   1923  CG  LYS A 272      46.556 -34.165  23.395  1.00149.00      A    C  
ANISOU 1923  CG  LYS A 272    24221  12793  19598  -2255  -3758   4591  A    C  
ATOM   1924  CD  LYS A 272      47.285 -34.649  24.630  1.00149.90      A    C  
ANISOU 1924  CD  LYS A 272    24639  12734  19583  -2190  -4004   4836  A    C  
ATOM   1925  CE  LYS A 272      46.439 -35.631  25.414  1.00155.54      A    C  
ANISOU 1925  CE  LYS A 272    25746  13210  20144  -2513  -4014   5085  A    C  
ATOM   1926  NZ  LYS A 272      47.185 -36.186  26.580  1.00159.07      A    N1+
ANISOU 1926  NZ  LYS A 272    26518  13457  20465  -2433  -4277   5336  A    N1+
ATOM   1927  N   ARG A 273      47.638 -30.534  20.704  1.00133.63      A    N  
ANISOU 1927  N   ARG A 273    21028  11785  17961  -1697  -3385   3825  A    N  
ATOM   1928  CA  ARG A 273      48.382 -29.559  19.899  1.00131.34      A    C  
ANISOU 1928  CA  ARG A 273    20396  11716  17790  -1456  -3350   3613  A    C  
ATOM   1929  C   ARG A 273      49.892 -29.778  19.883  1.00118.26      A    C  
ANISOU 1929  C   ARG A 273    18710   9962  16261  -1118  -3600   3599  A    C  
ATOM   1930  O   ARG A 273      50.553 -29.718  20.919  1.00112.78      A    O  
ANISOU 1930  O   ARG A 273    18129   9264  15456  -1064  -3762   3745  A    O  
ATOM   1931  CB  ARG A 273      48.081 -28.128  20.356  1.00143.31      A    C  
ANISOU 1931  CB  ARG A 273    21730  13593  19129  -1562  -3180   3584  A    C  
ATOM   1932  CG  ARG A 273      46.631 -27.711  20.205  1.00156.05      A    C  
ANISOU 1932  CG  ARG A 273    23289  15367  20634  -1846  -2908   3552  A    C  
ATOM   1933  CD  ARG A 273      46.413 -26.284  20.693  1.00166.29      A    C  
ANISOU 1933  CD  ARG A 273    24424  17003  21757  -1912  -2755   3516  A    C  
ATOM   1934  NE  ARG A 273      45.004 -26.014  20.974  1.00174.93      A    N  
ANISOU 1934  NE  ARG A 273    25537  18237  22691  -2199  -2522   3552  A    N  
ATOM   1935  CZ  ARG A 273      44.540 -24.867  21.459  1.00178.09      A    C  
ANISOU 1935  CZ  ARG A 273    25835  18917  22914  -2293  -2357   3530  A    C  
ATOM   1936  NH1 ARG A 273      45.373 -23.868  21.721  1.00176.98      A    N1+
ANISOU 1936  NH1 ARG A 273    25582  18930  22731  -2140  -2403   3474  A    N1+
ATOM   1937  NH2 ARG A 273      43.241 -24.716  21.684  1.00179.73      A    N  
ANISOU 1937  NH2 ARG A 273    26051  19254  22985  -2541  -2146   3560  A    N  
ATOM   1938  N   LYS A 274      50.433 -30.001  18.691  1.00112.11      A    N  
ANISOU 1938  N   LYS A 274    17762   9127  15706   -889  -3627   3416  A    N  
ATOM   1939  CA  LYS A 274      51.861 -30.233  18.527  1.00109.48      A    C  
ANISOU 1939  CA  LYS A 274    17358   8722  15518   -545  -3846   3377  A    C  
ATOM   1940  C   LYS A 274      52.486 -29.258  17.527  1.00102.88      A    C  
ANISOU 1940  C   LYS A 274    16140   8147  14802   -357  -3757   3146  A    C  
ATOM   1941  O   LYS A 274      53.576 -29.509  17.007  1.00 99.73      A    O  
ANISOU 1941  O   LYS A 274    15622   7703  14567    -62  -3894   3057  A    O  
ATOM   1942  CB  LYS A 274      52.117 -31.684  18.092  1.00112.85      A    C  
ANISOU 1942  CB  LYS A 274    17994   8773  16113   -397  -4011   3390  A    C  
ATOM   1943  CG  LYS A 274      51.390 -32.723  18.943  1.00117.95      A    C  
ANISOU 1943  CG  LYS A 274    19040   9126  16649   -616  -4083   3614  A    C  
ATOM   1944  CD  LYS A 274      51.996 -34.105  18.814  1.00125.08      A    C  
ANISOU 1944  CD  LYS A 274    20189   9634  17702   -406  -4321   3667  A    C  
ATOM   1945  CE  LYS A 274      51.456 -35.025  19.907  1.00137.27      A    C  
ANISOU 1945  CE  LYS A 274    22157  10899  19102   -621  -4429   3935  A    C  
ATOM   1946  NZ  LYS A 274      52.292 -36.247  20.137  1.00139.90      A    N1+
ANISOU 1946  NZ  LYS A 274    22763  10853  19540   -374  -4720   4040  A    N1+
ATOM   1947  N   VAL A 275      51.800 -28.144  17.261  1.00 96.82      A    N  
ANISOU 1947  N   VAL A 275    15183   7655  13950   -522  -3526   3054  A    N  
ATOM   1948  CA  VAL A 275      52.268 -27.188  16.258  1.00 90.27      A    C  
ANISOU 1948  CA  VAL A 275    14010   7068  13221   -379  -3420   2843  A    C  
ATOM   1949  C   VAL A 275      53.660 -26.688  16.586  1.00 88.56      A    C  
ANISOU 1949  C   VAL A 275    13645   6973  13032   -153  -3581   2838  A    C  
ATOM   1950  O   VAL A 275      54.532 -26.639  15.715  1.00 86.63      A    O  
ANISOU 1950  O   VAL A 275    13187   6774  12951     84  -3621   2692  A    O  
ATOM   1951  CB  VAL A 275      51.339 -25.961  16.115  1.00 85.49      A    C  
ANISOU 1951  CB  VAL A 275    13251   6742  12489   -591  -3165   2774  A    C  
ATOM   1952  CG1 VAL A 275      52.002 -24.894  15.232  1.00 65.35      A    C  
ANISOU 1952  CG1 VAL A 275    10368   4438  10022   -435  -3085   2584  A    C  
ATOM   1953  CG2 VAL A 275      49.981 -26.368  15.552  1.00 85.18      A    C  
ANISOU 1953  CG2 VAL A 275    13280   6633  12449   -794  -2989   2739  A    C  
ATOM   1954  N   LYS A 276      53.864 -26.311  17.842  1.00 92.79      A    N  
ANISOU 1954  N   LYS A 276    14285   7574  13395   -236  -3672   2996  A    N  
ATOM   1955  CA  LYS A 276      55.155 -25.783  18.263  1.00104.43      A    C  
ANISOU 1955  CA  LYS A 276    15619   9187  14875    -55  -3837   3003  A    C  
ATOM   1956  C   LYS A 276      56.198 -26.882  18.478  1.00110.46      A    C  
ANISOU 1956  C   LYS A 276    16483   9730  15757    201  -4115   3078  A    C  
ATOM   1957  O   LYS A 276      57.390 -26.646  18.300  1.00113.05      A    O  
ANISOU 1957  O   LYS A 276    16610  10163  16182    432  -4245   3015  A    O  
ATOM   1958  CB  LYS A 276      55.018 -24.901  19.510  1.00106.19      A    C  
ANISOU 1958  CB  LYS A 276    15912   9578  14857   -236  -3836   3127  A    C  
ATOM   1959  CG  LYS A 276      54.625 -23.460  19.210  1.00 98.29      A    C  
ANISOU 1959  CG  LYS A 276    14698   8871  13775   -364  -3614   3002  A    C  
ATOM   1960  CD  LYS A 276      54.664 -22.583  20.453  1.00 99.76      A    C  
ANISOU 1960  CD  LYS A 276    14958   9216  13730   -508  -3639   3107  A    C  
ATOM   1961  CE  LYS A 276      54.390 -21.119  20.092  1.00109.50      A    C  
ANISOU 1961  CE  LYS A 276    15982  10723  14900   -601  -3434   2966  A    C  
ATOM   1962  NZ  LYS A 276      54.915 -20.121  21.082  1.00111.75      A    N1+
ANISOU 1962  NZ  LYS A 276    16264  11185  15012   -659  -3505   3013  A    N1+
ATOM   1963  N   ASP A 277      55.747 -28.077  18.847  1.00113.38      A    N  
ANISOU 1963  N   ASP A 277    17160   9797  16121    162  -4207   3214  A    N  
ATOM   1964  CA  ASP A 277      56.653 -29.211  19.034  1.00118.88      A    C  
ANISOU 1964  CA  ASP A 277    17992  10243  16934    419  -4477   3292  A    C  
ATOM   1965  C   ASP A 277      57.181 -29.777  17.714  1.00111.36      A    C  
ANISOU 1965  C   ASP A 277    16882   9195  16235    692  -4488   3102  A    C  
ATOM   1966  O   ASP A 277      58.372 -30.063  17.578  1.00106.12      A    O  
ANISOU 1966  O   ASP A 277    16105   8518  15700    993  -4672   3067  A    O  
ATOM   1967  CB  ASP A 277      55.970 -30.327  19.831  1.00130.77      A    C  
ANISOU 1967  CB  ASP A 277    19909  11429  18348    278  -4571   3503  A    C  
ATOM   1968  CG  ASP A 277      56.061 -30.117  21.328  1.00141.44      A    C  
ANISOU 1968  CG  ASP A 277    21451  12817  19473    152  -4699   3729  A    C  
ATOM   1969  OD1 ASP A 277      56.290 -28.963  21.755  1.00144.36      A    O  
ANISOU 1969  OD1 ASP A 277    21648  13481  19721     87  -4649   3710  A    O  
ATOM   1970  OD2 ASP A 277      55.907 -31.108  22.075  1.00146.14      A    O1-
ANISOU 1970  OD2 ASP A 277    22381  13140  20003    116  -4854   3925  A    O1-
ATOM   1971  N   ARG A 278      56.289 -29.941  16.743  1.00107.83      A    N  
ANISOU 1971  N   ARG A 278    16422   8692  15856    587  -4290   2976  A    N  
ATOM   1972  CA  ARG A 278      56.654 -30.581  15.490  1.00108.95      A    C  
ANISOU 1972  CA  ARG A 278    16464   8714  16218    823  -4289   2795  A    C  
ATOM   1973  C   ARG A 278      57.479 -29.650  14.609  1.00103.03      A    C  
ANISOU 1973  C   ARG A 278    15313   8266  15570   1004  -4211   2592  A    C  
ATOM   1974  O   ARG A 278      58.259 -30.107  13.777  1.00104.83      A    O  
ANISOU 1974  O   ARG A 278    15411   8444  15976   1287  -4273   2456  A    O  
ATOM   1975  CB  ARG A 278      55.402 -31.066  14.750  1.00119.21      A    C  
ANISOU 1975  CB  ARG A 278    17892   9861  17542    632  -4112   2727  A    C  
ATOM   1976  CG  ARG A 278      55.651 -32.223  13.784  1.00129.32      A    C  
ANISOU 1976  CG  ARG A 278    19249  10864  19023    853  -4184   2607  A    C  
ATOM   1977  CD  ARG A 278      54.353 -32.714  13.159  1.00135.10      A    C  
ANISOU 1977  CD  ARG A 278    20132  11440  19758    621  -4024   2555  A    C  
ATOM   1978  NE  ARG A 278      54.581 -33.475  11.934  1.00141.32      A    N  
ANISOU 1978  NE  ARG A 278    20900  12058  20737    829  -4031   2365  A    N  
ATOM   1979  CZ  ARG A 278      54.732 -32.932  10.727  1.00144.47      A    C  
ANISOU 1979  CZ  ARG A 278    21009  12656  21227    931  -3882   2134  A    C  
ATOM   1980  NH1 ARG A 278      54.687 -31.614  10.571  1.00137.25      A    N1+
ANISOU 1980  NH1 ARG A 278    19804  12107  20239    845  -3720   2073  A    N1+
ATOM   1981  NH2 ARG A 278      54.935 -33.709   9.672  1.00150.66      A    N  
ANISOU 1981  NH2 ARG A 278    21809  13266  22169   1122  -3898   1965  A    N  
ATOM   1982  N   LEU A 279      57.311 -28.345  14.806  1.00 97.48      A    N  
ANISOU 1982  N   LEU A 279    14420   7872  14745    841  -4071   2573  A    N  
ATOM   1983  CA  LEU A 279      58.038 -27.345  14.031  1.00 90.64      A    C  
ANISOU 1983  CA  LEU A 279    13183   7305  13950    964  -3983   2397  A    C  
ATOM   1984  C   LEU A 279      59.211 -26.770  14.820  1.00 84.24      A    C  
ANISOU 1984  C   LEU A 279    12234   6673  13099   1078  -4152   2466  A    C  
ATOM   1985  O   LEU A 279      60.092 -26.103  14.263  1.00 80.18      A    O  
ANISOU 1985  O   LEU A 279    11412   6387  12664   1221  -4136   2338  A    O  
ATOM   1986  CB  LEU A 279      57.097 -26.219  13.599  1.00 87.81      A    C  
ANISOU 1986  CB  LEU A 279    12700   7167  13494    714  -3713   2313  A    C  
ATOM   1987  CG  LEU A 279      56.122 -26.592  12.489  1.00 91.74      A    C  
ANISOU 1987  CG  LEU A 279    13222   7573  14063    643  -3531   2184  A    C  
ATOM   1988  CD1 LEU A 279      55.314 -25.376  12.055  1.00 93.52      A    C  
ANISOU 1988  CD1 LEU A 279    13289   8051  14193    435  -3281   2099  A    C  
ATOM   1989  CD2 LEU A 279      56.885 -27.179  11.314  1.00 90.56      A    C  
ANISOU 1989  CD2 LEU A 279    12926   7363  14119    930  -3567   2011  A    C  
ATOM   1990  N   LYS A 280      59.185 -27.015  16.127  1.00 84.75      A    N  
ANISOU 1990  N   LYS A 280    12530   6640  13028    994  -4310   2673  A    N  
ATOM   1991  CA  LYS A 280      60.270 -26.670  17.045  1.00103.46      A    C  
ANISOU 1991  CA  LYS A 280    14829   9137  15344   1098  -4520   2769  A    C  
ATOM   1992  C   LYS A 280      61.647 -26.936  16.428  1.00112.93      A    C  
ANISOU 1992  C   LYS A 280    15770  10398  16740   1448  -4664   2658  A    C  
ATOM   1993  O   LYS A 280      62.580 -26.142  16.594  1.00106.46      A    O  
ANISOU 1993  O   LYS A 280    14698   9837  15916   1517  -4729   2626  A    O  
ATOM   1994  CB  LYS A 280      60.114 -27.500  18.326  1.00109.59      A    C  
ANISOU 1994  CB  LYS A 280    15960   9676  16002   1052  -4725   3007  A    C  
ATOM   1995  CG  LYS A 280      60.945 -27.061  19.518  1.00107.97      A    C  
ANISOU 1995  CG  LYS A 280    15748   9607  15671   1073  -4932   3145  A    C  
ATOM   1996  CD  LYS A 280      60.716 -28.018  20.688  1.00107.18      A    C  
ANISOU 1996  CD  LYS A 280    16032   9238  15453   1034  -5131   3387  A    C  
ATOM   1997  CE  LYS A 280      61.618 -27.686  21.862  1.00108.22      A    C  
ANISOU 1997  CE  LYS A 280    16166   9493  15460   1084  -5371   3526  A    C  
ATOM   1998  NZ  LYS A 280      61.450 -28.644  22.986  1.00109.32      A    N1+
ANISOU 1998  NZ  LYS A 280    16689   9368  15477   1061  -5578   3771  A    N1+
ATOM   1999  N   ALA A 281      61.762 -28.065  15.728  1.00119.45      A    N  
ANISOU 1999  N   ALA A 281    16663  10989  17735   1664  -4715   2596  A    N  
ATOM   2000  CA  ALA A 281      63.001 -28.457  15.060  1.00112.02      A    C  
ANISOU 2000  CA  ALA A 281    15487  10088  16989   2026  -4836   2476  A    C  
ATOM   2001  C   ALA A 281      63.455 -27.401  14.054  1.00104.25      A    C  
ANISOU 2001  C   ALA A 281    14099   9439  16072   2053  -4659   2270  A    C  
ATOM   2002  O   ALA A 281      64.472 -26.727  14.246  1.00 99.34      A    O  
ANISOU 2002  O   ALA A 281    13212   9073  15457   2144  -4740   2251  A    O  
ATOM   2003  CB  ALA A 281      62.822 -29.814  14.366  1.00103.46      A    C  
ANISOU 2003  CB  ALA A 281    14579   8671  16061   2222  -4873   2418  A    C  
ATOM   2004  N   TYR A 282      62.671 -27.252  12.992  1.00100.24      A    N  
ANISOU 2004  N   TYR A 282    13553   8930  15603   1958  -4418   2124  A    N  
ATOM   2005  CA  TYR A 282      63.016 -26.397  11.863  1.00 91.14      A    C  
ANISOU 2005  CA  TYR A 282    12050   8056  14523   1996  -4234   1922  A    C  
ATOM   2006  C   TYR A 282      63.164 -24.916  12.198  1.00 92.98      A    C  
ANISOU 2006  C   TYR A 282    12081   8616  14630   1795  -4145   1931  A    C  
ATOM   2007  O   TYR A 282      64.100 -24.262  11.733  1.00 94.17      A    O  
ANISOU 2007  O   TYR A 282    11912   9026  14843   1901  -4130   1826  A    O  
ATOM   2008  CB  TYR A 282      61.975 -26.572  10.759  1.00 86.27      A    C  
ANISOU 2008  CB  TYR A 282    11491   7347  13942   1901  -4004   1789  A    C  
ATOM   2009  CG  TYR A 282      61.776 -28.009  10.360  1.00 93.53      A    C  
ANISOU 2009  CG  TYR A 282    12626   7930  14982   2076  -4081   1761  A    C  
ATOM   2010  CD1 TYR A 282      60.826 -28.799  10.993  1.00 98.07      A    C  
ANISOU 2010  CD1 TYR A 282    13571   8202  15490   1927  -4133   1903  A    C  
ATOM   2011  CD2 TYR A 282      62.553 -28.584   9.360  1.00100.52      A    C  
ANISOU 2011  CD2 TYR A 282    13352   8797  16044   2387  -4102   1594  A    C  
ATOM   2012  CE1 TYR A 282      60.648 -30.126  10.637  1.00104.30      A    C  
ANISOU 2012  CE1 TYR A 282    14585   8658  16389   2072  -4213   1881  A    C  
ATOM   2013  CE2 TYR A 282      62.384 -29.909   8.993  1.00105.89      A    C  
ANISOU 2013  CE2 TYR A 282    14254   9146  16832   2557  -4178   1557  A    C  
ATOM   2014  CZ  TYR A 282      61.428 -30.676   9.634  1.00109.11      A    C  
ANISOU 2014  CZ  TYR A 282    15047   9235  17175   2393  -4239   1704  A    C  
ATOM   2015  OH  TYR A 282      61.252 -31.995   9.275  1.00115.12      A    O  
ANISOU 2015  OH  TYR A 282    16053   9645  18044   2544  -4322   1669  A    O  
ATOM   2016  N   VAL A 283      62.243 -24.387  13.001  1.00 97.75      A    N  
ANISOU 2016  N   VAL A 283    12875   9210  15054   1504  -4083   2051  A    N  
ATOM   2017  CA  VAL A 283      62.122 -22.937  13.158  1.00102.70      A    C  
ANISOU 2017  CA  VAL A 283    13352  10116  15554   1285  -3951   2032  A    C  
ATOM   2018  C   VAL A 283      63.085 -22.346  14.187  1.00105.98      A    C  
ANISOU 2018  C   VAL A 283    13677  10699  15891   1287  -4134   2131  A    C  
ATOM   2019  O   VAL A 283      63.833 -21.411  13.883  1.00108.27      A    O  
ANISOU 2019  O   VAL A 283    13685  11254  16197   1294  -4102   2045  A    O  
ATOM   2020  CB  VAL A 283      60.667 -22.524  13.493  1.00100.71      A    C  
ANISOU 2020  CB  VAL A 283    13322   9806  15137    978  -3778   2093  A    C  
ATOM   2021  CG1 VAL A 283      60.518 -21.005  13.490  1.00 92.71      A    C  
ANISOU 2021  CG1 VAL A 283    12154   9066  14007    781  -3622   2045  A    C  
ATOM   2022  CG2 VAL A 283      59.703 -23.154  12.503  1.00 96.73      A    C  
ANISOU 2022  CG2 VAL A 283    12904   9140  14708    965  -3616   2001  A    C  
ATOM   2023  N   ARG A 284      63.044 -22.881  15.404  1.00101.02      A    N  
ANISOU 2023  N   ARG A 284    13296   9920  15167   1263  -4326   2313  A    N  
ATOM   2024  CA  ARG A 284      63.959 -22.460  16.466  1.00104.65      A    C  
ANISOU 2024  CA  ARG A 284    13702  10519  15543   1273  -4536   2419  A    C  
ATOM   2025  C   ARG A 284      63.621 -21.095  17.081  1.00 98.50      A    C  
ANISOU 2025  C   ARG A 284    12914   9943  14567    987  -4441   2448  A    C  
ATOM   2026  O   ARG A 284      63.484 -20.988  18.301  1.00 94.93      A    O  
ANISOU 2026  O   ARG A 284    12659   9462  13947    863  -4561   2600  A    O  
ATOM   2027  CB  ARG A 284      65.410 -22.497  15.976  1.00109.74      A    C  
ANISOU 2027  CB  ARG A 284    14011  11332  16352   1545  -4669   2326  A    C  
ATOM   2028  CG  ARG A 284      65.868 -23.884  15.547  1.00115.77      A    C  
ANISOU 2028  CG  ARG A 284    14802  11888  17299   1868  -4804   2309  A    C  
ATOM   2029  CD  ARG A 284      67.266 -23.850  14.960  1.00123.47      A    C  
ANISOU 2029  CD  ARG A 284    15405  13070  18439   2144  -4899   2193  A    C  
ATOM   2030  NE  ARG A 284      67.793 -25.194  14.735  1.00134.50      A    N  
ANISOU 2030  NE  ARG A 284    16844  14261  19997   2485  -5066   2190  A    N  
ATOM   2031  CZ  ARG A 284      69.078 -25.464  14.525  1.00140.22      A    C  
ANISOU 2031  CZ  ARG A 284    17297  15120  20860   2785  -5224   2133  A    C  
ATOM   2032  NH1 ARG A 284      69.970 -24.480  14.511  1.00138.59      A    N1+
ANISOU 2032  NH1 ARG A 284    16745  15263  20649   2760  -5234   2080  A    N1+
ATOM   2033  NH2 ARG A 284      69.474 -26.717  14.332  1.00141.84      A    N  
ANISOU 2033  NH2 ARG A 284    17576  15111  21209   3111  -5372   2129  A    N  
ATOM   2034  N   ASP A 285      63.484 -20.063  16.249  1.00 94.78      A    N  
ANISOU 2034  N   ASP A 285    12233   9668  14111    887  -4227   2300  A    N  
ATOM   2035  CA  ASP A 285      63.104 -18.739  16.747  1.00 87.24      A    C  
ANISOU 2035  CA  ASP A 285    11289   8884  12974    623  -4120   2310  A    C  
ATOM   2036  C   ASP A 285      61.732 -18.740  17.416  1.00 85.07      A    C  
ANISOU 2036  C   ASP A 285    11335   8465  12521    402  -4013   2409  A    C  
ATOM   2037  O   ASP A 285      60.733 -19.113  16.802  1.00 81.97      A    O  
ANISOU 2037  O   ASP A 285    11037   7947  12160    362  -3842   2370  A    O  
ATOM   2038  CB  ASP A 285      63.124 -17.702  15.630  1.00 89.17      A    C  
ANISOU 2038  CB  ASP A 285    11278   9330  13274    565  -3901   2137  A    C  
ATOM   2039  CG  ASP A 285      62.766 -16.306  16.127  1.00 95.92      A    C  
ANISOU 2039  CG  ASP A 285    12159  10340  13946    307  -3799   2141  A    C  
ATOM   2040  OD1 ASP A 285      61.562 -15.994  16.261  1.00 83.88      A    O  
ANISOU 2040  OD1 ASP A 285    10824   8746  12300    134  -3632   2157  A    O  
ATOM   2041  OD2 ASP A 285      63.698 -15.515  16.384  1.00108.39      A    O1-
ANISOU 2041  OD2 ASP A 285    13568  12114  15502    279  -3886   2122  A    O1-
ATOM   2042  N   PRO A 286      61.681 -18.311  18.683  1.00 89.67      A    N  
ANISOU 2042  N   PRO A 286    12081   9082  12910    253  -4112   2535  A    N  
ATOM   2043  CA  PRO A 286      60.437 -18.272  19.459  1.00 90.73      A    C  
ANISOU 2043  CA  PRO A 286    12516   9109  12848     38  -4015   2639  A    C  
ATOM   2044  C   PRO A 286      59.325 -17.507  18.737  1.00 90.04      A    C  
ANISOU 2044  C   PRO A 286    12406   9081  12726   -120  -3714   2528  A    C  
ATOM   2045  O   PRO A 286      58.210 -18.025  18.636  1.00 96.15      A    O  
ANISOU 2045  O   PRO A 286    13350   9711  13471   -198  -3590   2558  A    O  
ATOM   2046  CB  PRO A 286      60.841 -17.520  20.732  1.00 84.55      A    C  
ANISOU 2046  CB  PRO A 286    11812   8448  11864    -88  -4148   2733  A    C  
ATOM   2047  CG  PRO A 286      62.300 -17.693  20.833  1.00 90.02      A    C  
ANISOU 2047  CG  PRO A 286    12313   9228  12661     97  -4395   2738  A    C  
ATOM   2048  CD  PRO A 286      62.819 -17.760  19.434  1.00 91.00      A    C  
ANISOU 2048  CD  PRO A 286    12137   9418  13021    268  -4315   2576  A    C  
ATOM   2049  N   TYR A 287      59.622 -16.300  18.253  1.00 81.69      A    N  
ANISOU 2049  N   TYR A 287    11144   8229  11667   -173  -3607   2405  A    N  
ATOM   2050  CA  TYR A 287      58.599 -15.426  17.660  1.00 90.57      A    C  
ANISOU 2050  CA  TYR A 287    12256   9421  12735   -321  -3336   2307  A    C  
ATOM   2051  C   TYR A 287      57.965 -16.018  16.408  1.00 86.61      A    C  
ANISOU 2051  C   TYR A 287    11691   8832  12387   -244  -3178   2215  A    C  
ATOM   2052  O   TYR A 287      56.742 -15.995  16.250  1.00 79.10      A    O  
ANISOU 2052  O   TYR A 287    10857   7826  11371   -361  -3003   2209  A    O  
ATOM   2053  CB  TYR A 287      59.159 -14.032  17.358  1.00 91.59      A    C  
ANISOU 2053  CB  TYR A 287    12189   9770  12841   -381  -3275   2201  A    C  
ATOM   2054  CG  TYR A 287      59.586 -13.283  18.592  1.00 98.49      A    C  
ANISOU 2054  CG  TYR A 287    13154  10736  13534   -503  -3400   2275  A    C  
ATOM   2055  CD1 TYR A 287      58.732 -13.163  19.682  1.00100.17      A    C  
ANISOU 2055  CD1 TYR A 287    13638  10889  13535   -658  -3376   2375  A    C  
ATOM   2056  CD2 TYR A 287      60.844 -12.697  18.675  1.00 99.40      A    C  
ANISOU 2056  CD2 TYR A 287    13081  11006  13681   -474  -3542   2241  A    C  
ATOM   2057  CE1 TYR A 287      59.116 -12.484  20.818  1.00100.03      A    C  
ANISOU 2057  CE1 TYR A 287    13719  10952  13334   -769  -3494   2435  A    C  
ATOM   2058  CE2 TYR A 287      61.237 -12.012  19.807  1.00 98.69      A    C  
ANISOU 2058  CE2 TYR A 287    13083  10997  13417   -598  -3669   2302  A    C  
ATOM   2059  CZ  TYR A 287      60.369 -11.908  20.876  1.00 98.61      A    C  
ANISOU 2059  CZ  TYR A 287    13360  10915  13191   -742  -3646   2396  A    C  
ATOM   2060  OH  TYR A 287      60.752 -11.228  22.007  1.00 97.91      A    O  
ANISOU 2060  OH  TYR A 287    13380  10908  12915   -865  -3773   2448  A    O  
ATOM   2061  N   ALA A 288      58.807 -16.539  15.523  1.00 86.36      A    N  
ANISOU 2061  N   ALA A 288    11463   8799  12551    -46  -3243   2135  A    N  
ATOM   2062  CA  ALA A 288      58.339 -17.248  14.346  1.00 86.17      A    C  
ANISOU 2062  CA  ALA A 288    11389   8675  12675     51  -3127   2043  A    C  
ATOM   2063  C   ALA A 288      57.369 -18.368  14.730  1.00 88.23      A    C  
ANISOU 2063  C   ALA A 288    11916   8700  12909     10  -3136   2143  A    C  
ATOM   2064  O   ALA A 288      56.298 -18.514  14.134  1.00 87.77      A    O  
ANISOU 2064  O   ALA A 288    11910   8584  12853    -69  -2964   2096  A    O  
ATOM   2065  CB  ALA A 288      59.508 -17.806  13.574  1.00 81.67      A    C  
ANISOU 2065  CB  ALA A 288    10605   8124  12305    294  -3236   1963  A    C  
ATOM   2066  N   LEU A 289      57.743 -19.161  15.723  1.00 90.35      A    N  
ANISOU 2066  N   LEU A 289    12350   8834  13144     55  -3344   2288  A    N  
ATOM   2067  CA  LEU A 289      56.891 -20.260  16.153  1.00 91.54      A    C  
ANISOU 2067  CA  LEU A 289    12772   8747  13261      0  -3369   2402  A    C  
ATOM   2068  C   LEU A 289      55.579 -19.741  16.735  1.00 88.00      A    C  
ANISOU 2068  C   LEU A 289    12495   8323  12617   -261  -3202   2464  A    C  
ATOM   2069  O   LEU A 289      54.521 -20.333  16.521  1.00 85.67      A    O  
ANISOU 2069  O   LEU A 289    12335   7901  12316   -353  -3094   2482  A    O  
ATOM   2070  CB  LEU A 289      57.613 -21.164  17.156  1.00 88.47      A    C  
ANISOU 2070  CB  LEU A 289    12542   8208  12862    104  -3640   2560  A    C  
ATOM   2071  CG  LEU A 289      58.669 -22.112  16.581  1.00 89.81      A    C  
ANISOU 2071  CG  LEU A 289    12608   8272  13243    393  -3811   2517  A    C  
ATOM   2072  CD1 LEU A 289      59.566 -22.639  17.690  1.00 85.84      A    C  
ANISOU 2072  CD1 LEU A 289    12215   7698  12704    501  -4097   2673  A    C  
ATOM   2073  CD2 LEU A 289      58.026 -23.266  15.817  1.00 88.63      A    C  
ANISOU 2073  CD2 LEU A 289    12575   7881  13218    453  -3759   2482  A    C  
ATOM   2074  N   ASP A 290      55.640 -18.628  17.460  1.00 82.37      A    N  
ANISOU 2074  N   ASP A 290    11774   7782  11742   -381  -3176   2488  A    N  
ATOM   2075  CA  ASP A 290      54.428 -18.085  18.057  1.00 83.08      A    C  
ANISOU 2075  CA  ASP A 290    12018   7913  11635   -608  -3013   2538  A    C  
ATOM   2076  C   ASP A 290      53.459 -17.588  16.987  1.00 81.40      A    C  
ANISOU 2076  C   ASP A 290    11692   7775  11461   -672  -2757   2401  A    C  
ATOM   2077  O   ASP A 290      52.256 -17.845  17.067  1.00 84.57      A    O  
ANISOU 2077  O   ASP A 290    12219   8124  11789   -809  -2622   2435  A    O  
ATOM   2078  CB  ASP A 290      54.737 -16.964  19.040  1.00 88.91      A    C  
ANISOU 2078  CB  ASP A 290    12781   8813  12187   -709  -3042   2574  A    C  
ATOM   2079  CG  ASP A 290      53.493 -16.477  19.764  1.00 93.86      A    C  
ANISOU 2079  CG  ASP A 290    13587   9480  12595   -925  -2878   2629  A    C  
ATOM   2080  OD1 ASP A 290      52.788 -17.315  20.369  1.00 91.94      A    O  
ANISOU 2080  OD1 ASP A 290    13556   9104  12271  -1012  -2886   2755  A    O  
ATOM   2081  OD2 ASP A 290      53.220 -15.259  19.725  1.00 94.29      A    O1-
ANISOU 2081  OD2 ASP A 290    13574   9698  12555  -1004  -2738   2546  A    O1-
ATOM   2082  N   LEU A 291      53.982 -16.883  15.986  1.00 70.45      A    N  
ANISOU 2082  N   LEU A 291    10064   6520  10185   -577  -2693   2252  A    N  
ATOM   2083  CA  LEU A 291      53.140 -16.397  14.900  1.00 73.11      A    C  
ANISOU 2083  CA  LEU A 291    10287   6931  10561   -618  -2467   2122  A    C  
ATOM   2084  C   LEU A 291      52.517 -17.536  14.087  1.00 77.68      A    C  
ANISOU 2084  C   LEU A 291    10894   7353  11266   -577  -2422   2093  A    C  
ATOM   2085  O   LEU A 291      51.323 -17.483  13.757  1.00 74.56      A    O  
ANISOU 2085  O   LEU A 291    10536   6966  10828   -693  -2252   2068  A    O  
ATOM   2086  CB  LEU A 291      53.904 -15.437  13.984  1.00 64.64      A    C  
ANISOU 2086  CB  LEU A 291     8963   6024   9572   -527  -2418   1979  A    C  
ATOM   2087  CG  LEU A 291      53.121 -14.880  12.782  1.00 60.90      A    C  
ANISOU 2087  CG  LEU A 291     8367   5635   9138   -551  -2195   1845  A    C  
ATOM   2088  CD1 LEU A 291      51.747 -14.368  13.190  1.00 58.24      A    C  
ANISOU 2088  CD1 LEU A 291     8157   5334   8639   -724  -2028   1874  A    C  
ATOM   2089  CD2 LEU A 291      53.912 -13.781  12.079  1.00 61.21      A    C  
ANISOU 2089  CD2 LEU A 291     8192   5845   9220   -495  -2152   1732  A    C  
ATOM   2090  N   ILE A 292      53.314 -18.557  13.765  1.00 72.74      A    N  
ANISOU 2090  N   ILE A 292    10251   6591  10796   -411  -2578   2093  A    N  
ATOM   2091  CA  ILE A 292      52.793 -19.689  13.003  1.00 75.03      A    C  
ANISOU 2091  CA  ILE A 292    10593   6707  11210   -367  -2554   2058  A    C  
ATOM   2092  C   ILE A 292      51.692 -20.379  13.784  1.00 82.12      A    C  
ANISOU 2092  C   ILE A 292    11746   7458  11997   -546  -2538   2192  A    C  
ATOM   2093  O   ILE A 292      50.687 -20.813  13.221  1.00 87.11      A    O  
ANISOU 2093  O   ILE A 292    12418   8027  12653   -632  -2418   2157  A    O  
ATOM   2094  CB  ILE A 292      53.854 -20.738  12.707  1.00 73.88      A    C  
ANISOU 2094  CB  ILE A 292    10429   6409  11233   -145  -2744   2048  A    C  
ATOM   2095  CG1 ILE A 292      54.950 -20.167  11.813  1.00 69.57      A    C  
ANISOU 2095  CG1 ILE A 292     9604   6022  10809     37  -2748   1905  A    C  
ATOM   2096  CG2 ILE A 292      53.200 -21.957  12.054  1.00 75.46      A    C  
ANISOU 2096  CG2 ILE A 292    10741   6392  11537   -128  -2727   2021  A    C  
ATOM   2097  CD1 ILE A 292      56.211 -21.034  11.772  1.00 72.55      A    C  
ANISOU 2097  CD1 ILE A 292     9935   6298  11332    281  -2959   1907  A    C  
ATOM   2098  N   ASP A 293      51.897 -20.483  15.090  1.00 82.03      A    N  
ANISOU 2098  N   ASP A 293    11905   7402  11858   -609  -2661   2351  A    N  
ATOM   2099  CA  ASP A 293      50.894 -21.054  15.976  1.00 92.45      A    C  
ANISOU 2099  CA  ASP A 293    13476   8607  13043   -801  -2641   2500  A    C  
ATOM   2100  C   ASP A 293      49.574 -20.270  15.914  1.00 90.91      A    C  
ANISOU 2100  C   ASP A 293    13260   8565  12716  -1003  -2397   2464  A    C  
ATOM   2101  O   ASP A 293      48.485 -20.848  15.986  1.00 89.79      A    O  
ANISOU 2101  O   ASP A 293    13240   8345  12530  -1156  -2310   2516  A    O  
ATOM   2102  CB  ASP A 293      51.439 -21.085  17.407  1.00102.42      A    C  
ANISOU 2102  CB  ASP A 293    14910   9842  14164   -829  -2810   2669  A    C  
ATOM   2103  CG  ASP A 293      50.558 -21.866  18.352  1.00107.33      A    C  
ANISOU 2103  CG  ASP A 293    15816  10317  14649  -1015  -2819   2844  A    C  
ATOM   2104  OD1 ASP A 293      49.872 -22.809  17.897  1.00115.95      A    O  
ANISOU 2104  OD1 ASP A 293    16997  11244  15814  -1068  -2780   2853  A    O  
ATOM   2105  OD2 ASP A 293      50.558 -21.535  19.555  1.00103.83      A    O1-
ANISOU 2105  OD2 ASP A 293    15511   9925  14015  -1117  -2865   2971  A    O1-
ATOM   2106  N   LYS A 294      49.679 -18.951  15.772  1.00 87.10      A    N  
ANISOU 2106  N   LYS A 294    12618   8302  12174  -1000  -2291   2376  A    N  
ATOM   2107  CA  LYS A 294      48.502 -18.089  15.726  1.00 84.33      A    C  
ANISOU 2107  CA  LYS A 294    12236   8111  11697  -1155  -2066   2333  A    C  
ATOM   2108  C   LYS A 294      47.846 -18.052  14.345  1.00 80.15      A    C  
ANISOU 2108  C   LYS A 294    11544   7623  11287  -1133  -1911   2188  A    C  
ATOM   2109  O   LYS A 294      46.679 -17.683  14.222  1.00 77.48      A    O  
ANISOU 2109  O   LYS A 294    11193   7380  10866  -1262  -1734   2164  A    O  
ATOM   2110  CB  LYS A 294      48.857 -16.686  16.209  1.00 85.14      A    C  
ANISOU 2110  CB  LYS A 294    12273   8405  11671  -1161  -2026   2304  A    C  
ATOM   2111  CG  LYS A 294      49.303 -16.690  17.653  1.00 91.24      A    C  
ANISOU 2111  CG  LYS A 294    13226   9153  12288  -1218  -2164   2450  A    C  
ATOM   2112  CD  LYS A 294      49.587 -15.301  18.180  1.00 91.54      A    C  
ANISOU 2112  CD  LYS A 294    13227   9370  12183  -1245  -2124   2414  A    C  
ATOM   2113  CE  LYS A 294      50.013 -15.381  19.637  1.00 92.57      A    C  
ANISOU 2113  CE  LYS A 294    13555   9473  12144  -1308  -2274   2560  A    C  
ATOM   2114  NZ  LYS A 294      50.262 -14.040  20.226  1.00 96.25      A    N1+
ANISOU 2114  NZ  LYS A 294    14015  10101  12453  -1352  -2243   2522  A    N1+
ATOM   2115  N   LEU A 295      48.601 -18.438  13.317  1.00 77.06      A    N  
ANISOU 2115  N   LEU A 295    11027   7171  11082   -965  -1981   2087  A    N  
ATOM   2116  CA  LEU A 295      48.058 -18.620  11.973  1.00 69.16      A    C  
ANISOU 2116  CA  LEU A 295     9897   6181  10199   -935  -1865   1952  A    C  
ATOM   2117  C   LEU A 295      47.336 -19.969  11.830  1.00 79.17      A    C  
ANISOU 2117  C   LEU A 295    11306   7252  11524  -1012  -1887   1996  A    C  
ATOM   2118  O   LEU A 295      46.221 -20.030  11.314  1.00 80.64      A    O  
ANISOU 2118  O   LEU A 295    11468   7477  11696  -1128  -1746   1951  A    O  
ATOM   2119  CB  LEU A 295      49.166 -18.521  10.926  1.00 59.91      A    C  
ANISOU 2119  CB  LEU A 295     8542   5029   9192   -726  -1922   1821  A    C  
ATOM   2120  CG  LEU A 295      49.802 -17.154  10.694  1.00 62.63      A    C  
ANISOU 2120  CG  LEU A 295     8710   5578   9508   -664  -1868   1744  A    C  
ATOM   2121  CD1 LEU A 295      51.008 -17.295   9.795  1.00 65.61      A    C  
ANISOU 2121  CD1 LEU A 295     8921   5959  10048   -465  -1950   1640  A    C  
ATOM   2122  CD2 LEU A 295      48.801 -16.205  10.082  1.00 60.33      A    C  
ANISOU 2122  CD2 LEU A 295     8328   5446   9149   -750  -1659   1658  A    C  
ATOM   2123  N   LEU A 296      47.965 -21.050  12.285  1.00 78.41      A    N  
ANISOU 2123  N   LEU A 296    11360   6942  11489   -953  -2071   2088  A    N  
ATOM   2124  CA  LEU A 296      47.352 -22.370  12.155  1.00 83.90      A    C  
ANISOU 2124  CA  LEU A 296    12219   7417  12243  -1030  -2108   2133  A    C  
ATOM   2125  C   LEU A 296      46.396 -22.665  13.307  1.00 88.93      A    C  
ANISOU 2125  C   LEU A 296    13065   8010  12713  -1270  -2077   2304  A    C  
ATOM   2126  O   LEU A 296      46.461 -23.719  13.924  1.00 94.98      A    O  
ANISOU 2126  O   LEU A 296    14050   8559  13480  -1316  -2208   2433  A    O  
ATOM   2127  CB  LEU A 296      48.411 -23.468  12.021  1.00 81.97      A    C  
ANISOU 2127  CB  LEU A 296    12061   6934  12149   -843  -2319   2146  A    C  
ATOM   2128  CG  LEU A 296      49.345 -23.342  10.813  1.00 77.53      A    C  
ANISOU 2128  CG  LEU A 296    11290   6412  11759   -600  -2343   1970  A    C  
ATOM   2129  CD1 LEU A 296      50.325 -24.503  10.757  1.00 79.52      A    C  
ANISOU 2129  CD1 LEU A 296    11639   6423  12153   -402  -2551   1984  A    C  
ATOM   2130  CD2 LEU A 296      48.549 -23.252   9.524  1.00 74.24      A    C  
ANISOU 2130  CD2 LEU A 296    10746   6059  11401   -637  -2180   1811  A    C  
ATOM   2131  N   VAL A 297      45.510 -21.713  13.583  1.00 88.64      A    N  
ANISOU 2131  N   VAL A 297    12963   8186  12530  -1417  -1900   2302  A    N  
ATOM   2132  CA  VAL A 297      44.479 -21.866  14.603  1.00 79.44      A    C  
ANISOU 2132  CA  VAL A 297    11958   7036  11190  -1656  -1826   2446  A    C  
ATOM   2133  C   VAL A 297      43.218 -22.461  13.979  1.00 81.24      A    C  
ANISOU 2133  C   VAL A 297    12182   7238  11446  -1822  -1703   2413  A    C  
ATOM   2134  O   VAL A 297      42.818 -22.070  12.881  1.00 81.29      A    O  
ANISOU 2134  O   VAL A 297    12001   7359  11529  -1785  -1590   2262  A    O  
ATOM   2135  CB  VAL A 297      44.173 -20.507  15.279  1.00 78.91      A    C  
ANISOU 2135  CB  VAL A 297    11822   7221  10938  -1715  -1694   2453  A    C  
ATOM   2136  CG1 VAL A 297      42.782 -20.485  15.880  1.00 79.56      A    C  
ANISOU 2136  CG1 VAL A 297    11976   7399  10856  -1957  -1532   2532  A    C  
ATOM   2137  CG2 VAL A 297      45.217 -20.198  16.331  1.00 78.52      A    C  
ANISOU 2137  CG2 VAL A 297    11872   7157  10806  -1641  -1841   2548  A    C  
ATOM   2138  N   LEU A 298      42.600 -23.412  14.678  1.00 84.28      A    N  
ANISOU 2138  N   LEU A 298    12778   7479  11767  -2015  -1731   2559  A    N  
ATOM   2139  CA  LEU A 298      41.461 -24.160  14.145  1.00 79.41      A    C  
ANISOU 2139  CA  LEU A 298    12181   6808  11184  -2200  -1644   2545  A    C  
ATOM   2140  C   LEU A 298      40.208 -23.315  13.902  1.00 78.46      A    C  
ANISOU 2140  C   LEU A 298    11881   6968  10964  -2345  -1410   2479  A    C  
ATOM   2141  O   LEU A 298      39.653 -23.316  12.808  1.00 76.21      A    O  
ANISOU 2141  O   LEU A 298    11442   6743  10769  -2349  -1328   2347  A    O  
ATOM   2142  CB  LEU A 298      41.122 -25.319  15.074  1.00 78.51      A    C  
ANISOU 2142  CB  LEU A 298    12351   6477  11001  -2397  -1729   2738  A    C  
ATOM   2143  CG  LEU A 298      42.083 -26.500  15.039  1.00 86.33      A    C  
ANISOU 2143  CG  LEU A 298    13542   7129  12128  -2275  -1963   2792  A    C  
ATOM   2144  CD1 LEU A 298      41.842 -27.401  16.246  1.00 90.14      A    C  
ANISOU 2144  CD1 LEU A 298    14334   7422  12493  -2467  -2049   3021  A    C  
ATOM   2145  CD2 LEU A 298      41.938 -27.270  13.730  1.00 82.97      A    C  
ANISOU 2145  CD2 LEU A 298    13075   6553  11895  -2231  -1985   2652  A    C  
ATOM   2146  N   ASP A 299      39.745 -22.615  14.928  1.00 81.04      A    N  
ANISOU 2146  N   ASP A 299    12229   7469  11096  -2456  -1307   2570  A    N  
ATOM   2147  CA  ASP A 299      38.574 -21.767  14.773  1.00 86.95      A    C  
ANISOU 2147  CA  ASP A 299    12801   8495  11741  -2564  -1086   2508  A    C  
ATOM   2148  C   ASP A 299      38.944 -20.535  13.944  1.00 94.07      A    C  
ANISOU 2148  C   ASP A 299    13471   9576  12694  -2354  -1020   2337  A    C  
ATOM   2149  O   ASP A 299      39.744 -19.698  14.376  1.00 93.30      A    O  
ANISOU 2149  O   ASP A 299    13367   9537  12545  -2218  -1053   2333  A    O  
ATOM   2150  CB  ASP A 299      38.028 -21.359  16.141  1.00 94.03      A    C  
ANISOU 2150  CB  ASP A 299    13797   9525  12405  -2723   -989   2647  A    C  
ATOM   2151  CG  ASP A 299      36.748 -20.555  16.042  1.00103.34      A    C  
ANISOU 2151  CG  ASP A 299    14795  10997  13472  -2830   -754   2588  A    C  
ATOM   2152  OD1 ASP A 299      36.122 -20.566  14.960  1.00106.65      A    O  
ANISOU 2152  OD1 ASP A 299    15037  11491  13994  -2834   -678   2468  A    O  
ATOM   2153  OD2 ASP A 299      36.367 -19.911  17.046  1.00105.71      A    O1-
ANISOU 2153  OD2 ASP A 299    15130  11460  13577  -2901   -649   2655  A    O1-
ATOM   2154  N   PRO A 300      38.364 -20.426  12.740  1.00 94.16      A    N  
ANISOU 2154  N   PRO A 300    13299   9674  12804  -2335   -933   2197  A    N  
ATOM   2155  CA  PRO A 300      38.618 -19.312  11.819  1.00 81.40      A    C  
ANISOU 2155  CA  PRO A 300    11469   8221  11239  -2148   -866   2036  A    C  
ATOM   2156  C   PRO A 300      38.474 -17.969  12.512  1.00 81.54      A    C  
ANISOU 2156  C   PRO A 300    11433   8456  11094  -2117   -750   2043  A    C  
ATOM   2157  O   PRO A 300      39.114 -16.999  12.117  1.00 85.27      A    O  
ANISOU 2157  O   PRO A 300    11805   9005  11589  -1944   -746   1951  A    O  
ATOM   2158  CB  PRO A 300      37.502 -19.466  10.776  1.00 77.38      A    C  
ANISOU 2158  CB  PRO A 300    10804   7817  10783  -2230   -752   1935  A    C  
ATOM   2159  CG  PRO A 300      36.482 -20.369  11.436  1.00 85.15      A    C  
ANISOU 2159  CG  PRO A 300    11898   8765  11691  -2495   -714   2057  A    C  
ATOM   2160  CD  PRO A 300      37.333 -21.327  12.203  1.00 91.15      A    C  
ANISOU 2160  CD  PRO A 300    12905   9254  12473  -2516   -887   2188  A    C  
ATOM   2161  N   ALA A 301      37.636 -17.919  13.539  1.00 83.74      A    N  
ANISOU 2161  N   ALA A 301    11786   8827  11204  -2288   -653   2149  A    N  
ATOM   2162  CA  ALA A 301      37.330 -16.662  14.208  1.00 83.47      A    C  
ANISOU 2162  CA  ALA A 301    11709   9006  10998  -2264   -522   2142  A    C  
ATOM   2163  C   ALA A 301      38.365 -16.321  15.261  1.00 81.43      A    C  
ANISOU 2163  C   ALA A 301    11611   8678  10652  -2203   -627   2223  A    C  
ATOM   2164  O   ALA A 301      38.446 -15.174  15.702  1.00 81.84      A    O  
ANISOU 2164  O   ALA A 301    11641   8870  10584  -2136   -556   2192  A    O  
ATOM   2165  CB  ALA A 301      35.944 -16.708  14.823  1.00 84.55      A    C  
ANISOU 2165  CB  ALA A 301    11836   9308  10981  -2464   -354   2206  A    C  
ATOM   2166  N   GLN A 302      39.146 -17.317  15.667  1.00 81.38      A    N  
ANISOU 2166  N   GLN A 302    11773   8450  10699  -2223   -804   2326  A    N  
ATOM   2167  CA  GLN A 302      40.213 -17.100  16.639  1.00 84.99      A    C  
ANISOU 2167  CA  GLN A 302    12378   8833  11081  -2161   -937   2408  A    C  
ATOM   2168  C   GLN A 302      41.571 -17.042  15.944  1.00 84.55      A    C  
ANISOU 2168  C   GLN A 302    12265   8664  11196  -1953  -1099   2331  A    C  
ATOM   2169  O   GLN A 302      42.594 -16.753  16.571  1.00 80.92      A    O  
ANISOU 2169  O   GLN A 302    11882   8163  10701  -1872  -1224   2373  A    O  
ATOM   2170  CB  GLN A 302      40.213 -18.193  17.704  1.00 86.23      A    C  
ANISOU 2170  CB  GLN A 302    12774   8832  11158  -2313  -1038   2593  A    C  
ATOM   2171  CG  GLN A 302      39.012 -18.188  18.636  1.00 93.33      A    C  
ANISOU 2171  CG  GLN A 302    13753   9861  11850  -2532   -880   2694  A    C  
ATOM   2172  CD  GLN A 302      39.113 -19.276  19.703  1.00102.85      A    C  
ANISOU 2172  CD  GLN A 302    15220  10895  12966  -2688   -992   2893  A    C  
ATOM   2173  NE2 GLN A 302      38.129 -20.172  19.734  1.00 95.84      A    N  
ANISOU 2173  NE2 GLN A 302    14383   9972  12060  -2898   -922   2972  A    N  
ATOM   2174  OE1 GLN A 302      40.071 -19.314  20.480  1.00108.16      A    O  
ANISOU 2174  OE1 GLN A 302    16048  11466  13583  -2627  -1147   2979  A    O  
ATOM   2175  N   ARG A 303      41.568 -17.321  14.644  1.00 80.38      A    N  
ANISOU 2175  N   ARG A 303    11592   8101  10845  -1872  -1094   2216  A    N  
ATOM   2176  CA  ARG A 303      42.768 -17.236  13.821  1.00 73.81      A    C  
ANISOU 2176  CA  ARG A 303    10670   7197  10178  -1672  -1215   2122  A    C  
ATOM   2177  C   ARG A 303      43.166 -15.781  13.600  1.00 73.55      A    C  
ANISOU 2177  C   ARG A 303    10502   7339  10105  -1559  -1146   2022  A    C  
ATOM   2178  O   ARG A 303      42.337 -14.951  13.214  1.00 83.38      A    O  
ANISOU 2178  O   ARG A 303    11637   8751  11292  -1578   -980   1945  A    O  
ATOM   2179  CB  ARG A 303      42.518 -17.916  12.477  1.00 71.02      A    C  
ANISOU 2179  CB  ARG A 303    10207   6777  10001  -1631  -1205   2018  A    C  
ATOM   2180  CG  ARG A 303      43.740 -18.060  11.585  1.00 67.52      A    C  
ANISOU 2180  CG  ARG A 303     9677   6244   9733  -1428  -1328   1922  A    C  
ATOM   2181  CD  ARG A 303      43.375 -18.930  10.403  1.00 68.90      A    C  
ANISOU 2181  CD  ARG A 303     9795   6326  10056  -1415  -1322   1832  A    C  
ATOM   2182  NE  ARG A 303      42.612 -20.091  10.852  1.00 73.92      A    N  
ANISOU 2182  NE  ARG A 303    10596   6816  10674  -1588  -1347   1935  A    N  
ATOM   2183  CZ  ARG A 303      41.627 -20.670  10.173  1.00 69.51      A    C  
ANISOU 2183  CZ  ARG A 303    10011   6242  10157  -1700  -1274   1889  A    C  
ATOM   2184  NH1 ARG A 303      41.248 -20.207   8.987  1.00 62.57      A    N1+
ANISOU 2184  NH1 ARG A 303     8944   5491   9337  -1645  -1173   1738  A    N1+
ATOM   2185  NH2 ARG A 303      41.009 -21.715  10.697  1.00 71.73      A    N  
ANISOU 2185  NH2 ARG A 303    10461   6379  10413  -1880  -1307   1998  A    N  
ATOM   2186  N   ILE A 304      44.436 -15.480  13.840  1.00 64.10      A    N  
ANISOU 2186  N   ILE A 304     9316   6101   8938  -1440  -1282   2025  A    N  
ATOM   2187  CA  ILE A 304      44.948 -14.119  13.686  1.00 64.83      A    C  
ANISOU 2187  CA  ILE A 304     9304   6336   8992  -1350  -1240   1940  A    C  
ATOM   2188  C   ILE A 304      44.711 -13.571  12.266  1.00 63.43      A    C  
ANISOU 2188  C   ILE A 304     8928   6253   8919  -1263  -1126   1787  A    C  
ATOM   2189  O   ILE A 304      44.694 -14.325  11.288  1.00 62.12      A    O  
ANISOU 2189  O   ILE A 304     8686   6016   8900  -1215  -1145   1732  A    O  
ATOM   2190  CB  ILE A 304      46.452 -14.057  14.054  1.00 65.91      A    C  
ANISOU 2190  CB  ILE A 304     9460   6409   9173  -1246  -1428   1966  A    C  
ATOM   2191  CG1 ILE A 304      46.874 -12.627  14.379  1.00 61.14      A    C  
ANISOU 2191  CG1 ILE A 304     8820   5945   8465  -1225  -1391   1921  A    C  
ATOM   2192  CG2 ILE A 304      47.313 -14.661  12.946  1.00 66.18      A    C  
ANISOU 2192  CG2 ILE A 304     9367   6358   9419  -1098  -1524   1889  A    C  
ATOM   2193  CD1 ILE A 304      48.295 -12.525  14.870  1.00 60.83      A    C  
ANISOU 2193  CD1 ILE A 304     8796   5868   8447  -1155  -1580   1956  A    C  
ATOM   2194  N   ASP A 305      44.495 -12.264  12.156  1.00 63.49      A    N  
ANISOU 2194  N   ASP A 305     8868   6413   8842  -1242  -1010   1721  A    N  
ATOM   2195  CA  ASP A 305      44.282 -11.651  10.843  1.00 62.34      A    C  
ANISOU 2195  CA  ASP A 305     8550   6360   8775  -1158   -907   1588  A    C  
ATOM   2196  C   ASP A 305      45.552 -10.960  10.356  1.00 61.91      A    C  
ANISOU 2196  C   ASP A 305     8409   6321   8791  -1038   -978   1522  A    C  
ATOM   2197  O   ASP A 305      46.519 -10.815  11.107  1.00 59.46      A    O  
ANISOU 2197  O   ASP A 305     8162   5974   8457  -1027  -1097   1575  A    O  
ATOM   2198  CB  ASP A 305      43.096 -10.683  10.858  1.00 65.06      A    C  
ANISOU 2198  CB  ASP A 305     8868   6861   8991  -1202   -723   1551  A    C  
ATOM   2199  CG  ASP A 305      43.304  -9.505  11.805  1.00 82.31      A    C  
ANISOU 2199  CG  ASP A 305    11140   9118  11017  -1210   -696   1571  A    C  
ATOM   2200  OD1 ASP A 305      44.464  -9.184  12.158  1.00 85.97      A    O  
ANISOU 2200  OD1 ASP A 305    11641   9535  11487  -1172   -813   1585  A    O  
ATOM   2201  OD2 ASP A 305      42.294  -8.881  12.191  1.00 87.22      A    O1-
ANISOU 2201  OD2 ASP A 305    11789   9846  11504  -1254   -557   1566  A    O1-
ATOM   2202  N   SER A 306      45.559 -10.543   9.099  1.00 59.02      A    N  
ANISOU 2202  N   SER A 306     7896   6019   8510   -955   -909   1411  A    N  
ATOM   2203  CA  SER A 306      46.775  -9.996   8.528  1.00 62.61      A    C  
ANISOU 2203  CA  SER A 306     8252   6495   9041   -856   -968   1351  A    C  
ATOM   2204  C   SER A 306      47.241  -8.766   9.306  1.00 68.23      A    C  
ANISOU 2204  C   SER A 306     9023   7271   9633   -883   -972   1371  A    C  
ATOM   2205  O   SER A 306      48.439  -8.557   9.507  1.00 73.08      A    O  
ANISOU 2205  O   SER A 306     9616   7872  10280   -851  -1084   1379  A    O  
ATOM   2206  CB  SER A 306      46.579  -9.685   7.047  1.00 65.02      A    C  
ANISOU 2206  CB  SER A 306     8406   6872   9428   -779   -873   1235  A    C  
ATOM   2207  OG  SER A 306      45.414  -8.916   6.848  1.00 77.89      A    O  
ANISOU 2207  OG  SER A 306    10034   8601  10960   -813   -721   1205  A    O  
ATOM   2208  N   ASP A 307      46.295  -7.966   9.777  1.00 67.05      A    N  
ANISOU 2208  N   ASP A 307     8947   7191   9336   -942   -852   1378  A    N  
ATOM   2209  CA  ASP A 307      46.659  -6.736  10.463  1.00 62.11      A    C  
ANISOU 2209  CA  ASP A 307     8398   6614   8587   -967   -845   1381  A    C  
ATOM   2210  C   ASP A 307      47.404  -7.020  11.757  1.00 66.71      A    C  
ANISOU 2210  C   ASP A 307     9105   7134   9107  -1026   -991   1473  A    C  
ATOM   2211  O   ASP A 307      48.451  -6.428  12.022  1.00 71.15      A    O  
ANISOU 2211  O   ASP A 307     9671   7702   9661  -1023  -1082   1469  A    O  
ATOM   2212  CB  ASP A 307      45.434  -5.860  10.730  1.00 66.98      A    C  
ANISOU 2212  CB  ASP A 307     9081   7312   9055   -998   -683   1360  A    C  
ATOM   2213  CG  ASP A 307      45.811  -4.426  11.062  1.00 79.69      A    C  
ANISOU 2213  CG  ASP A 307    10760   8962  10557   -995   -659   1325  A    C  
ATOM   2214  OD1 ASP A 307      46.456  -3.752  10.217  1.00 84.96      A    O  
ANISOU 2214  OD1 ASP A 307    11345   9645  11289   -945   -661   1263  A    O  
ATOM   2215  OD2 ASP A 307      45.465  -3.977  12.175  1.00 82.90      A    O1-
ANISOU 2215  OD2 ASP A 307    11313   9378  10806  -1052   -636   1361  A    O1-
ATOM   2216  N   ASP A 308      46.867  -7.928  12.563  1.00 65.29      A    N  
ANISOU 2216  N   ASP A 308     9030   6900   8877  -1090  -1018   1562  A    N  
ATOM   2217  CA  ASP A 308      47.498  -8.265  13.832  1.00 72.17      A    C  
ANISOU 2217  CA  ASP A 308    10039   7711   9672  -1147  -1163   1663  A    C  
ATOM   2218  C   ASP A 308      48.783  -9.045  13.609  1.00 68.62      A    C  
ANISOU 2218  C   ASP A 308     9521   7179   9372  -1078  -1350   1686  A    C  
ATOM   2219  O   ASP A 308      49.745  -8.932  14.378  1.00 65.61      A    O  
ANISOU 2219  O   ASP A 308     9192   6782   8955  -1087  -1496   1737  A    O  
ATOM   2220  CB  ASP A 308      46.540  -9.062  14.717  1.00 80.26      A    C  
ANISOU 2220  CB  ASP A 308    11203   8698  10594  -1242  -1133   1763  A    C  
ATOM   2221  CG  ASP A 308      45.329  -8.255  15.126  1.00 86.22      A    C  
ANISOU 2221  CG  ASP A 308    12022   9558  11178  -1305   -951   1744  A    C  
ATOM   2222  OD1 ASP A 308      45.471  -7.028  15.320  1.00 91.34      A    O  
ANISOU 2222  OD1 ASP A 308    12697  10276  11731  -1290   -903   1688  A    O  
ATOM   2223  OD2 ASP A 308      44.236  -8.845  15.248  1.00 83.68      A    O1-
ANISOU 2223  OD2 ASP A 308    11725   9252  10818  -1369   -855   1782  A    O1-
ATOM   2224  N   ALA A 309      48.792  -9.837  12.547  1.00 65.51      A    N  
ANISOU 2224  N   ALA A 309     9005   6742   9144  -1002  -1347   1643  A    N  
ATOM   2225  CA  ALA A 309      49.949 -10.643  12.231  1.00 62.00      A    C  
ANISOU 2225  CA  ALA A 309     8481   6222   8852   -907  -1510   1650  A    C  
ATOM   2226  C   ALA A 309      51.087  -9.705  11.901  1.00 61.48      A    C  
ANISOU 2226  C   ALA A 309     8295   6244   8822   -855  -1556   1586  A    C  
ATOM   2227  O   ALA A 309      52.216  -9.918  12.341  1.00 63.59      A    O  
ANISOU 2227  O   ALA A 309     8542   6493   9127   -819  -1721   1625  A    O  
ATOM   2228  CB  ALA A 309      49.655 -11.579  11.063  1.00 60.44      A    C  
ANISOU 2228  CB  ALA A 309     8185   5966   8814   -830  -1475   1591  A    C  
ATOM   2229  N   LEU A 310      50.788  -8.661  11.130  1.00 57.91      A    N  
ANISOU 2229  N   LEU A 310     7760   5889   8353   -856  -1414   1494  A    N  
ATOM   2230  CA  LEU A 310      51.805  -7.678  10.769  1.00 62.53      A    C  
ANISOU 2230  CA  LEU A 310     8238   6560   8960   -836  -1439   1436  A    C  
ATOM   2231  C   LEU A 310      52.370  -6.998  12.015  1.00 65.94      A    C  
ANISOU 2231  C   LEU A 310     8783   7010   9260   -922  -1539   1496  A    C  
ATOM   2232  O   LEU A 310      53.532  -6.587  12.042  1.00 57.44      A    O  
ANISOU 2232  O   LEU A 310     7626   5982   8219   -919  -1644   1482  A    O  
ATOM   2233  CB  LEU A 310      51.243  -6.647   9.798  1.00 57.66      A    C  
ANISOU 2233  CB  LEU A 310     7559   6026   8323   -836  -1265   1343  A    C  
ATOM   2234  CG  LEU A 310      51.121  -7.184   8.376  1.00 56.77      A    C  
ANISOU 2234  CG  LEU A 310     7291   5923   8355   -740  -1199   1265  A    C  
ATOM   2235  CD1 LEU A 310      50.544  -6.124   7.447  1.00 49.90      A    C  
ANISOU 2235  CD1 LEU A 310     6375   5137   7448   -740  -1035   1185  A    C  
ATOM   2236  CD2 LEU A 310      52.476  -7.650   7.890  1.00 50.94      A    C  
ANISOU 2236  CD2 LEU A 310     6399   5195   7759   -657  -1318   1240  A    C  
ATOM   2237  N   ASN A 311      51.544  -6.910  13.052  1.00 63.32      A    N  
ANISOU 2237  N   ASN A 311     8637   6649   8772  -1006  -1508   1558  A    N  
ATOM   2238  CA  ASN A 311      51.923  -6.232  14.280  1.00 69.30      A    C  
ANISOU 2238  CA  ASN A 311     9534   7424   9375  -1095  -1589   1606  A    C  
ATOM   2239  C   ASN A 311      52.732  -7.128  15.223  1.00 74.30      A    C  
ANISOU 2239  C   ASN A 311    10221   8000  10012  -1097  -1800   1710  A    C  
ATOM   2240  O   ASN A 311      53.409  -6.644  16.131  1.00 77.48      A    O  
ANISOU 2240  O   ASN A 311    10697   8426  10314  -1158  -1918   1745  A    O  
ATOM   2241  CB  ASN A 311      50.668  -5.703  14.975  1.00 73.53      A    C  
ANISOU 2241  CB  ASN A 311    10245   7970   9723  -1174  -1451   1620  A    C  
ATOM   2242  CG  ASN A 311      50.985  -4.874  16.202  1.00 83.40      A    C  
ANISOU 2242  CG  ASN A 311    11658   9239  10789  -1266  -1514   1648  A    C  
ATOM   2243  ND2 ASN A 311      50.288  -5.157  17.300  1.00 86.79      A    N  
ANISOU 2243  ND2 ASN A 311    12266   9648  11061  -1331  -1501   1722  A    N  
ATOM   2244  OD1 ASN A 311      51.841  -3.986  16.165  1.00 78.47      A    O  
ANISOU 2244  OD1 ASN A 311    11006   8653  10157  -1290  -1572   1602  A    O  
ATOM   2245  N   HIS A 312      52.661  -8.434  14.984  1.00 74.43      A    N  
ANISOU 2245  N   HIS A 312    10206   7932  10143  -1026  -1855   1756  A    N  
ATOM   2246  CA  HIS A 312      53.349  -9.438  15.795  1.00 71.11      A    C  
ANISOU 2246  CA  HIS A 312     9848   7433   9740  -1001  -2059   1864  A    C  
ATOM   2247  C   HIS A 312      54.850  -9.171  15.949  1.00 71.99      A    C  
ANISOU 2247  C   HIS A 312     9847   7599   9906   -958  -2244   1860  A    C  
ATOM   2248  O   HIS A 312      55.513  -8.701  15.019  1.00 65.39      A    O  
ANISOU 2248  O   HIS A 312     8818   6841   9184   -904  -2224   1768  A    O  
ATOM   2249  CB  HIS A 312      53.123 -10.831  15.204  1.00 67.83      A    C  
ANISOU 2249  CB  HIS A 312     9394   6902   9475   -908  -2081   1886  A    C  
ATOM   2250  CG  HIS A 312      53.590 -11.944  16.086  1.00 77.81      A    C  
ANISOU 2250  CG  HIS A 312    10773   8051  10743   -881  -2279   2014  A    C  
ATOM   2251  CD2 HIS A 312      52.905 -12.781  16.904  1.00 79.19      A    C  
ANISOU 2251  CD2 HIS A 312    11145   8111  10830   -943  -2308   2132  A    C  
ATOM   2252  ND1 HIS A 312      54.916 -12.307  16.190  1.00 79.10      A    N  
ANISOU 2252  ND1 HIS A 312    10845   8206  11001   -774  -2484   2035  A    N  
ATOM   2253  CE1 HIS A 312      55.029 -13.316  17.033  1.00 86.52      A    C  
ANISOU 2253  CE1 HIS A 312    11934   9024  11917   -760  -2639   2162  A    C  
ATOM   2254  NE2 HIS A 312      53.823 -13.625  17.479  1.00 86.82      A    N  
ANISOU 2254  NE2 HIS A 312    12157   8989  11840   -870  -2533   2227  A    N  
ATOM   2255  N   ASP A 313      55.379  -9.491  17.128  1.00 78.63      A    N  
ANISOU 2255  N   ASP A 313    10806   8411  10661   -988  -2427   1964  A    N  
ATOM   2256  CA  ASP A 313      56.766  -9.175  17.472  1.00 85.29      A    C  
ANISOU 2256  CA  ASP A 313    11551   9328  11526   -969  -2619   1971  A    C  
ATOM   2257  C   ASP A 313      57.786  -9.772  16.500  1.00 86.28      A    C  
ANISOU 2257  C   ASP A 313    11429   9476  11878   -811  -2707   1923  A    C  
ATOM   2258  O   ASP A 313      58.921  -9.305  16.412  1.00 87.40      A    O  
ANISOU 2258  O   ASP A 313    11412   9726  12068   -796  -2814   1889  A    O  
ATOM   2259  CB  ASP A 313      57.079  -9.613  18.905  1.00 96.89      A    C  
ANISOU 2259  CB  ASP A 313    13199  10752  12861  -1013  -2816   2105  A    C  
ATOM   2260  CG  ASP A 313      56.497  -8.671  19.945  1.00102.18      A    C  
ANISOU 2260  CG  ASP A 313    14080  11458  13285  -1178  -2760   2126  A    C  
ATOM   2261  OD1 ASP A 313      56.310  -7.470  19.634  1.00 97.84      A    O  
ANISOU 2261  OD1 ASP A 313    13502  10989  12680  -1250  -2629   2028  A    O  
ATOM   2262  OD2 ASP A 313      56.234  -9.136  21.077  1.00106.72      A    O1-
ANISOU 2262  OD2 ASP A 313    14858  11976  13714  -1230  -2847   2241  A    O1-
ATOM   2263  N   PHE A 314      57.377 -10.808  15.779  1.00 84.22      A    N  
ANISOU 2263  N   PHE A 314    11134   9116  11749   -700  -2660   1916  A    N  
ATOM   2264  CA  PHE A 314      58.215 -11.421  14.755  1.00 78.85      A    C  
ANISOU 2264  CA  PHE A 314    10228   8449  11280   -530  -2712   1852  A    C  
ATOM   2265  C   PHE A 314      58.731 -10.384  13.732  1.00 73.52      A    C  
ANISOU 2265  C   PHE A 314     9328   7935  10672   -535  -2606   1722  A    C  
ATOM   2266  O   PHE A 314      59.829 -10.523  13.207  1.00 75.26      A    O  
ANISOU 2266  O   PHE A 314     9334   8238  11023   -429  -2691   1677  A    O  
ATOM   2267  CB  PHE A 314      57.418 -12.544  14.076  1.00 73.85      A    C  
ANISOU 2267  CB  PHE A 314     9635   7672  10750   -441  -2632   1842  A    C  
ATOM   2268  CG  PHE A 314      58.109 -13.183  12.897  1.00 73.95      A    C  
ANISOU 2268  CG  PHE A 314     9434   7690  10973   -257  -2650   1753  A    C  
ATOM   2269  CD1 PHE A 314      59.173 -14.052  13.082  1.00 78.51      A    C  
ANISOU 2269  CD1 PHE A 314     9938   8230  11663    -96  -2853   1788  A    C  
ATOM   2270  CD2 PHE A 314      57.656 -12.948  11.603  1.00 73.09      A    C  
ANISOU 2270  CD2 PHE A 314     9208   7623  10942   -232  -2462   1630  A    C  
ATOM   2271  CE1 PHE A 314      59.788 -14.655  12.002  1.00 81.31      A    C  
ANISOU 2271  CE1 PHE A 314    10098   8593  12204     90  -2859   1694  A    C  
ATOM   2272  CE2 PHE A 314      58.263 -13.545  10.519  1.00 75.64      A    C  
ANISOU 2272  CE2 PHE A 314     9345   7954  11441    -61  -2468   1539  A    C  
ATOM   2273  CZ  PHE A 314      59.333 -14.401  10.718  1.00 82.51      A    C  
ANISOU 2273  CZ  PHE A 314    10138   8790  12422    103  -2661   1566  A    C  
ATOM   2274  N   PHE A 315      57.944  -9.348  13.454  1.00 61.58      A    N  
ANISOU 2274  N   PHE A 315     7865   6469   9064   -655  -2421   1668  A    N  
ATOM   2275  CA  PHE A 315      58.360  -8.326  12.494  1.00 71.62      A    C  
ANISOU 2275  CA  PHE A 315     8958   7875  10379   -678  -2314   1559  A    C  
ATOM   2276  C   PHE A 315      59.002  -7.122  13.185  1.00 78.79      A    C  
ANISOU 2276  C   PHE A 315     9879   8887  11172   -816  -2378   1567  A    C  
ATOM   2277  O   PHE A 315      59.435  -6.171  12.526  1.00 78.93      A    O  
ANISOU 2277  O   PHE A 315     9771   9012  11208   -868  -2307   1491  A    O  
ATOM   2278  CB  PHE A 315      57.169  -7.865  11.632  1.00 68.67      A    C  
ANISOU 2278  CB  PHE A 315     8621   7488   9981   -710  -2078   1488  A    C  
ATOM   2279  CG  PHE A 315      56.471  -8.986  10.935  1.00 65.38      A    C  
ANISOU 2279  CG  PHE A 315     8199   6975   9667   -602  -2013   1472  A    C  
ATOM   2280  CD1 PHE A 315      55.273  -9.482  11.422  1.00 65.59      A    C  
ANISOU 2280  CD1 PHE A 315     8414   6892   9616   -644  -1959   1529  A    C  
ATOM   2281  CD2 PHE A 315      57.027  -9.572   9.810  1.00 66.77      A    C  
ANISOU 2281  CD2 PHE A 315     8181   7174  10013   -463  -2010   1398  A    C  
ATOM   2282  CE1 PHE A 315      54.628 -10.536  10.787  1.00 63.64      A    C  
ANISOU 2282  CE1 PHE A 315     8168   6550   9463   -566  -1909   1513  A    C  
ATOM   2283  CE2 PHE A 315      56.400 -10.635   9.181  1.00 65.72      A    C  
ANISOU 2283  CE2 PHE A 315     8063   6939   9971   -369  -1962   1375  A    C  
ATOM   2284  CZ  PHE A 315      55.192 -11.113   9.665  1.00 56.26      A    C  
ANISOU 2284  CZ  PHE A 315     7058   5621   8698   -429  -1916   1433  A    C  
ATOM   2285  N   TRP A 316      59.074  -7.168  14.510  1.00 79.17      A    N  
ANISOU 2285  N   TRP A 316    10091   8897  11091   -886  -2515   1659  A    N  
ATOM   2286  CA  TRP A 316      59.520  -6.005  15.266  1.00 79.52      A    C  
ANISOU 2286  CA  TRP A 316    10199   9022  10996  -1038  -2573   1661  A    C  
ATOM   2287  C   TRP A 316      60.609  -6.319  16.298  1.00 79.84      A    C  
ANISOU 2287  C   TRP A 316    10224   9100  11010  -1045  -2831   1739  A    C  
ATOM   2288  O   TRP A 316      60.841  -5.558  17.239  1.00 76.36      A    O  
ANISOU 2288  O   TRP A 316     9901   8696  10416  -1182  -2913   1764  A    O  
ATOM   2289  CB  TRP A 316      58.310  -5.305  15.885  1.00 71.79      A    C  
ANISOU 2289  CB  TRP A 316     9476   7981   9822  -1158  -2440   1669  A    C  
ATOM   2290  CG  TRP A 316      57.317  -4.870  14.828  1.00 74.45      A    C  
ANISOU 2290  CG  TRP A 316     9799   8305  10185  -1145  -2199   1587  A    C  
ATOM   2291  CD1 TRP A 316      56.112  -5.452  14.544  1.00 69.34      A    C  
ANISOU 2291  CD1 TRP A 316     9229   7577   9539  -1093  -2063   1594  A    C  
ATOM   2292  CD2 TRP A 316      57.462  -3.778  13.903  1.00 73.36      A    C  
ANISOU 2292  CD2 TRP A 316     9561   8240  10073  -1187  -2076   1492  A    C  
ATOM   2293  CE2 TRP A 316      56.303  -3.758  13.099  1.00 70.85      A    C  
ANISOU 2293  CE2 TRP A 316     9270   7883   9768  -1141  -1875   1446  A    C  
ATOM   2294  CE3 TRP A 316      58.454  -2.814  13.683  1.00 71.70      A    C  
ANISOU 2294  CE3 TRP A 316     9247   8126   9871  -1271  -2121   1446  A    C  
ATOM   2295  NE1 TRP A 316      55.498  -4.785  13.514  1.00 63.67      A    N  
ANISOU 2295  NE1 TRP A 316     8459   6887   8845  -1088  -1872   1506  A    N  
ATOM   2296  CZ2 TRP A 316      56.109  -2.805  12.088  1.00 68.60      A    C  
ANISOU 2296  CZ2 TRP A 316     8922   7643   9498  -1159  -1723   1361  A    C  
ATOM   2297  CZ3 TRP A 316      58.257  -1.866  12.678  1.00 66.89      A    C  
ANISOU 2297  CZ3 TRP A 316     8584   7553   9277  -1306  -1960   1364  A    C  
ATOM   2298  CH2 TRP A 316      57.095  -1.870  11.896  1.00 68.33      A    C  
ANISOU 2298  CH2 TRP A 316     8808   7687   9468  -1241  -1767   1325  A    C  
ATOM   2299  N   SER A 317      61.283  -7.442  16.095  1.00 82.45      A    N  
ANISOU 2299  N   SER A 317    10413   9423  11490   -888  -2966   1773  A    N  
ATOM   2300  CA  SER A 317      62.435  -7.801  16.903  1.00 86.12      A    C  
ANISOU 2300  CA  SER A 317    10814   9945  11961   -857  -3225   1842  A    C  
ATOM   2301  C   SER A 317      63.604  -8.155  15.988  1.00 89.66      A    C  
ANISOU 2301  C   SER A 317    10938  10512  12617   -717  -3295   1784  A    C  
ATOM   2302  O   SER A 317      63.417  -8.373  14.785  1.00 82.98      A    O  
ANISOU 2302  O   SER A 317     9954   9669  11907   -623  -3145   1704  A    O  
ATOM   2303  CB  SER A 317      62.102  -8.960  17.844  1.00 88.36      A    C  
ANISOU 2303  CB  SER A 317    11287  10088  12197   -783  -3362   1969  A    C  
ATOM   2304  OG  SER A 317      61.691 -10.107  17.124  1.00 95.48      A    O  
ANISOU 2304  OG  SER A 317    12159  10875  13245   -618  -3305   1970  A    O  
ATOM   2305  N   ASP A 318      64.808  -8.184  16.556  1.00 98.73      A    N  
ANISOU 2305  N   ASP A 318    11957  11774  13783   -704  -3518   1821  A    N  
ATOM   2306  CA  ASP A 318      66.017  -8.489  15.791  1.00 99.74      A    C  
ANISOU 2306  CA  ASP A 318    11749  12049  14097   -567  -3598   1768  A    C  
ATOM   2307  C   ASP A 318      66.117  -9.983  15.522  1.00 93.36      A    C  
ANISOU 2307  C   ASP A 318    10891  11140  13440   -309  -3676   1800  A    C  
ATOM   2308  O   ASP A 318      65.690 -10.791  16.345  1.00 91.48      A    O  
ANISOU 2308  O   ASP A 318    10867  10745  13145   -255  -3784   1903  A    O  
ATOM   2309  CB  ASP A 318      67.260  -8.016  16.543  1.00103.63      A    C  
ANISOU 2309  CB  ASP A 318    12108  12714  14553   -645  -3824   1798  A    C  
ATOM   2310  CG  ASP A 318      67.197  -6.544  16.898  1.00115.08      A    C  
ANISOU 2310  CG  ASP A 318    13640  14243  15844   -915  -3769   1766  A    C  
ATOM   2311  OD1 ASP A 318      66.633  -5.753  16.106  1.00117.77      A    O  
ANISOU 2311  OD1 ASP A 318    13994  14579  16175  -1011  -3542   1684  A    O  
ATOM   2312  OD2 ASP A 318      67.714  -6.176  17.973  1.00121.85      A    O1-
ANISOU 2312  OD2 ASP A 318    14560  15157  16579  -1028  -3958   1821  A    O1-
ATOM   2313  N   PRO A 319      66.672 -10.353  14.357  1.00 87.67      A    N  
ANISOU 2313  N   PRO A 319     9904  10502  12907   -151  -3618   1709  A    N  
ATOM   2314  CA  PRO A 319      67.115  -9.406  13.330  1.00 83.99      A    C  
ANISOU 2314  CA  PRO A 319     9196  10220  12495   -229  -3468   1592  A    C  
ATOM   2315  C   PRO A 319      65.904  -8.842  12.609  1.00 86.75      A    C  
ANISOU 2315  C   PRO A 319     9686  10485  12791   -332  -3200   1532  A    C  
ATOM   2316  O   PRO A 319      65.057  -9.619  12.169  1.00 84.94      A    O  
ANISOU 2316  O   PRO A 319     9564  10104  12608   -222  -3102   1523  A    O  
ATOM   2317  CB  PRO A 319      67.894 -10.301  12.363  1.00 85.74      A    C  
ANISOU 2317  CB  PRO A 319     9136  10517  12926     21  -3486   1525  A    C  
ATOM   2318  CG  PRO A 319      67.244 -11.647  12.515  1.00 86.00      A    C  
ANISOU 2318  CG  PRO A 319     9350  10320  13008    211  -3529   1576  A    C  
ATOM   2319  CD  PRO A 319      66.998 -11.743  13.989  1.00 87.40      A    C  
ANISOU 2319  CD  PRO A 319     9781  10388  13037    124  -3706   1715  A    C  
ATOM   2320  N   MET A 320      65.818  -7.524  12.493  1.00 83.51      A    N  
ANISOU 2320  N   MET A 320     9283  10164  12282   -540  -3091   1493  A    N  
ATOM   2321  CA  MET A 320      64.698  -6.907  11.798  1.00 79.57      A    C  
ANISOU 2321  CA  MET A 320     8911   9594  11727   -628  -2844   1437  A    C  
ATOM   2322  C   MET A 320      64.655  -7.361  10.343  1.00 84.71      A    C  
ANISOU 2322  C   MET A 320     9380  10275  12530   -482  -2690   1342  A    C  
ATOM   2323  O   MET A 320      65.685  -7.760   9.793  1.00 82.49      A    O  
ANISOU 2323  O   MET A 320     8834  10124  12384   -361  -2749   1300  A    O  
ATOM   2324  CB  MET A 320      64.793  -5.386  11.885  1.00 72.31      A    C  
ANISOU 2324  CB  MET A 320     8020   8768  10688   -862  -2775   1408  A    C  
ATOM   2325  CG  MET A 320      64.533  -4.859  13.271  1.00 76.69      A    C  
ANISOU 2325  CG  MET A 320     8818   9261  11060  -1016  -2883   1482  A    C  
ATOM   2326  SD  MET A 320      62.796  -4.920  13.715  1.00 88.69      A    S  
ANISOU 2326  SD  MET A 320    10693  10570  12436  -1042  -2739   1517  A    S  
ATOM   2327  CE  MET A 320      62.126  -3.695  12.589  1.00 54.04      A    C  
ANISOU 2327  CE  MET A 320     6310   6202   8021  -1144  -2471   1416  A    C  
ATOM   2328  N   PRO A 321      63.458  -7.310   9.718  1.00 86.85      A    N  
ANISOU 2328  N   PRO A 321     9788  10437  12773   -488  -2494   1306  A    N  
ATOM   2329  CA  PRO A 321      63.261  -7.753   8.327  1.00 82.71      A    C  
ANISOU 2329  CA  PRO A 321     9129   9927  12372   -358  -2341   1214  A    C  
ATOM   2330  C   PRO A 321      64.236  -7.072   7.365  1.00 79.71      A    C  
ANISOU 2330  C   PRO A 321     8474   9755  12057   -383  -2275   1132  A    C  
ATOM   2331  O   PRO A 321      64.462  -5.867   7.478  1.00 76.43      A    O  
ANISOU 2331  O   PRO A 321     8056   9430  11553   -568  -2238   1132  A    O  
ATOM   2332  CB  PRO A 321      61.829  -7.311   8.013  1.00 67.57      A    C  
ANISOU 2332  CB  PRO A 321     7417   7899  10357   -441  -2149   1198  A    C  
ATOM   2333  CG  PRO A 321      61.164  -7.170   9.338  1.00 68.49      A    C  
ANISOU 2333  CG  PRO A 321     7792   7900  10330   -544  -2221   1293  A    C  
ATOM   2334  CD  PRO A 321      62.217  -6.782  10.318  1.00 76.30      A    C  
ANISOU 2334  CD  PRO A 321     8739   8974  11276   -622  -2407   1347  A    C  
ATOM   2335  N   SER A 322      64.794  -7.828   6.426  1.00 78.51      A    N  
ANISOU 2335  N   SER A 322     8106   9673  12051   -203  -2253   1060  A    N  
ATOM   2336  CA  SER A 322      65.751  -7.262   5.483  1.00 84.36      A    C  
ANISOU 2336  CA  SER A 322     8567  10633  12852   -223  -2180    984  A    C  
ATOM   2337  C   SER A 322      65.393  -7.596   4.039  1.00 86.93      A    C  
ANISOU 2337  C   SER A 322     8806  10975  13249   -107  -1991    881  A    C  
ATOM   2338  O   SER A 322      64.687  -8.567   3.779  1.00 89.53      A    O  
ANISOU 2338  O   SER A 322     9236  11158  13626     41  -1966    859  A    O  
ATOM   2339  CB  SER A 322      67.182  -7.725   5.807  1.00 83.40      A    C  
ANISOU 2339  CB  SER A 322     8186  10668  12834   -121  -2363    990  A    C  
ATOM   2340  OG  SER A 322      67.358  -9.117   5.582  1.00 78.69      A    O  
ANISOU 2340  OG  SER A 322     7521  10008  12371    147  -2432    963  A    O  
ATOM   2341  N   ASP A 323      65.902  -6.792   3.109  1.00 87.02      A    N  
ANISOU 2341  N   ASP A 323     8636  11167  13261   -186  -1862    819  A    N  
ATOM   2342  CA  ASP A 323      65.620  -6.955   1.688  1.00 93.05      A    C  
ANISOU 2342  CA  ASP A 323     9314  11974  14065   -100  -1673    719  A    C  
ATOM   2343  C   ASP A 323      66.167  -8.241   1.069  1.00 96.75      A    C  
ANISOU 2343  C   ASP A 323     9598  12480  14684    164  -1701    639  A    C  
ATOM   2344  O   ASP A 323      67.063  -8.880   1.615  1.00101.45      A    O  
ANISOU 2344  O   ASP A 323    10056  13124  15366    284  -1865    654  A    O  
ATOM   2345  CB  ASP A 323      66.114  -5.740   0.906  1.00 99.27      A    C  
ANISOU 2345  CB  ASP A 323     9960  12954  14802   -267  -1537    687  A    C  
ATOM   2346  CG  ASP A 323      65.208  -4.541   1.077  1.00118.78      A    C  
ANISOU 2346  CG  ASP A 323    12669  15338  17124   -484  -1443    735  A    C  
ATOM   2347  OD1 ASP A 323      63.972  -4.741   1.182  1.00123.52      A    O  
ANISOU 2347  OD1 ASP A 323    13503  15756  17673   -457  -1395    748  A    O  
ATOM   2348  OD2 ASP A 323      65.729  -3.405   1.108  1.00125.60      A    O1-
ANISOU 2348  OD2 ASP A 323    13486  16315  17923   -679  -1420    758  A    O1-
ATOM   2349  N   LEU A 324      65.612  -8.602  -0.086  1.00 97.12      A    N  
ANISOU 2349  N   LEU A 324     9648  12501  14752    261  -1545    549  A    N  
ATOM   2350  CA  LEU A 324      65.955  -9.840  -0.770  1.00 97.32      A    C  
ANISOU 2350  CA  LEU A 324     9543  12527  14905    520  -1550    454  A    C  
ATOM   2351  C   LEU A 324      66.932  -9.602  -1.925  1.00108.78      A    C  
ANISOU 2351  C   LEU A 324    10693  14237  16402    572  -1430    351  A    C  
ATOM   2352  O   LEU A 324      66.835  -8.599  -2.641  1.00101.38      A    O  
ANISOU 2352  O   LEU A 324     9718  13419  15381    414  -1272    333  A    O  
ATOM   2353  CB  LEU A 324      64.684 -10.520  -1.284  1.00 87.74      A    C  
ANISOU 2353  CB  LEU A 324     8542  11112  13682    598  -1464    410  A    C  
ATOM   2354  CG  LEU A 324      63.902 -11.426  -0.326  1.00 82.83      A    C  
ANISOU 2354  CG  LEU A 324     8166  10231  13075    655  -1598    479  A    C  
ATOM   2355  CD1 LEU A 324      63.769 -10.813   1.048  1.00 79.66      A    C  
ANISOU 2355  CD1 LEU A 324     7901   9776  12589    486  -1717    615  A    C  
ATOM   2356  CD2 LEU A 324      62.528 -11.761  -0.901  1.00 79.22      A    C  
ANISOU 2356  CD2 LEU A 324     7911   9611  12579    651  -1482    441  A    C  
ATOM   2357  N   LYS A 325      67.871 -10.535  -2.093  1.00121.66      A    N  
ANISOU 2357  N   LYS A 325    12112  15951  18160    799  -1508    286  A    N  
ATOM   2358  CA  LYS A 325      68.877 -10.465  -3.156  1.00128.29      A    C  
ANISOU 2358  CA  LYS A 325    12637  17056  19051    883  -1397    179  A    C  
ATOM   2359  C   LYS A 325      69.477 -11.834  -3.506  1.00126.93      A    C  
ANISOU 2359  C   LYS A 325    12316  16889  19022   1213  -1457     75  A    C  
ATOM   2360  O   LYS A 325      69.606 -12.718  -2.655  1.00120.23      A    O  
ANISOU 2360  O   LYS A 325    11529  15897  18255   1368  -1646    113  A    O  
ATOM   2361  CB  LYS A 325      69.989  -9.478  -2.787  1.00132.55      A    C  
ANISOU 2361  CB  LYS A 325    12942  17851  19571    713  -1435    232  A    C  
ATOM   2362  CG  LYS A 325      69.614  -8.024  -3.026  1.00135.97      A    C  
ANISOU 2362  CG  LYS A 325    13453  18346  19863    404  -1297    282  A    C  
ATOM   2363  CD  LYS A 325      70.710  -7.068  -2.591  1.00138.05      A    C  
ANISOU 2363  CD  LYS A 325    13504  18841  20106    209  -1351    338  A    C  
ATOM   2364  CE  LYS A 325      70.243  -5.620  -2.698  1.00135.54      A    C  
ANISOU 2364  CE  LYS A 325    13332  18526  19643   -106  -1237    399  A    C  
ATOM   2365  NZ  LYS A 325      71.312  -4.649  -2.325  1.00136.46      A    N1+
ANISOU 2365  NZ  LYS A 325    13253  18860  19733   -328  -1286    450  A    N1+
TER   
CONECT 1275 1285
CONECT 1285 1275 1286
CONECT 1286 1285 1287 1289
CONECT 1287 1286 1288 1296
CONECT 1288 1287
CONECT 1289 1286 1290 1291
CONECT 1290 1289
CONECT 1291 1289 1292
CONECT 1292 1291 1293 1294 1295
CONECT 1293 1292
CONECT 1294 1292
CONECT 1295 1292
CONECT 1296 1287
END


A second structure was input as follows:


CRYST1  173.922  173.922   97.173  90.00  90.00 120.00 H 3           9
ATOM      1  N   SER A   7      39.641  -6.736 -39.577  1.00117.46      A    N  
ANISOU    1  N   SER A   7    14337  17925  12367   2357  -2478   -895  A    N  
ATOM      2  CA  SER A   7      39.178  -5.651 -40.441  1.00120.39      A    C  
ANISOU    2  CA  SER A   7    14797  18384  12559   2459  -2588   -775  A    C  
ATOM      3  C   SER A   7      38.592  -4.514 -39.601  1.00117.71      A    C  
ANISOU    3  C   SER A   7    14285  17990  12449   2391  -2593   -621  A    C  
ATOM      4  O   SER A   7      38.265  -3.441 -40.123  1.00114.90      A    O  
ANISOU    4  O   SER A   7    13986  17684  11987   2469  -2660   -485  A    O  
ATOM      5  CB  SER A   7      38.138  -6.170 -41.452  1.00117.79      A    C  
ANISOU    5  CB  SER A   7    14562  18099  12092   2533  -2894   -946  A    C  
ATOM      6  OG  SER A   7      37.760  -5.171 -42.391  1.00115.47      A    O  
ANISOU    6  OG  SER A   7    14389  17895  11588   2652  -3013   -829  A    O  
ATOM      7  N   VAL A   8      38.484  -4.756 -38.296  1.00113.07      A    N  
ANISOU    7  N   VAL A   8    13501  17294  12166   2250  -2518   -644  A    N  
ATOM      8  CA  VAL A   8      37.778  -3.854 -37.387  1.00107.91      A    C  
ANISOU    8  CA  VAL A   8    12668  16573  11761   2177  -2536   -544  A    C  
ATOM      9  C   VAL A   8      38.730  -3.066 -36.497  1.00108.11      A    C  
ANISOU    9  C   VAL A   8    12646  16553  11877   2115  -2274   -356  A    C  
ATOM     10  O   VAL A   8      39.737  -3.602 -36.031  1.00108.02      A    O  
ANISOU   10  O   VAL A   8    12641  16518  11884   2061  -2090   -360  A    O  
ATOM     11  CB  VAL A   8      36.795  -4.635 -36.493  1.00 95.14      A    C  
ANISOU   11  CB  VAL A   8    10855  14859  10435   2049  -2652   -708  A    C  
ATOM     12  CG1 VAL A   8      36.232  -3.740 -35.412  1.00 88.10      A    C  
ANISOU   12  CG1 VAL A   8     9774  13893   9805   1968  -2612   -606  A    C  
ATOM     13  CG2 VAL A   8      35.677  -5.223 -37.331  1.00 89.78      A    C  
ANISOU   13  CG2 VAL A   8    10189  14219   9704   2097  -2943   -883  A    C  
ATOM     14  N   GLU A   9      38.399  -1.796 -36.264  1.00110.17      A    N  
ANISOU   14  N   GLU A   9    12860  16799  12201   2126  -2270   -196  A    N  
ATOM     15  CA  GLU A   9      39.196  -0.914 -35.405  1.00106.65      A    C  
ANISOU   15  CA  GLU A   9    12371  16300  11853   2060  -2045    -14  A    C  
ATOM     16  C   GLU A   9      39.305  -1.401 -33.966  1.00 96.27      A    C  
ANISOU   16  C   GLU A   9    10890  14874  10814   1907  -1936    -67  A    C  
ATOM     17  O   GLU A   9      38.318  -1.802 -33.349  1.00 91.88      A    O  
ANISOU   17  O   GLU A   9    10194  14255  10461   1837  -2048   -183  A    O  
ATOM     18  CB  GLU A   9      38.606   0.490 -35.391  1.00116.20      A    C  
ANISOU   18  CB  GLU A   9    13560  17489  13103   2102  -2098    141  A    C  
ATOM     19  CG  GLU A   9      39.267   1.457 -36.336  1.00126.87      A    C  
ANISOU   19  CG  GLU A   9    15097  18910  14198   2207  -2033    326  A    C  
ATOM     20  CD  GLU A   9      38.767   2.865 -36.124  1.00135.61      A    C  
ANISOU   20  CD  GLU A   9    16182  19963  15382   2233  -2065    489  A    C  
ATOM     21  OE1 GLU A   9      38.396   3.189 -34.973  1.00137.05      A    O  
ANISOU   21  OE1 GLU A   9    16203  20043  15827   2143  -2028    496  A    O  
ATOM     22  OE2 GLU A   9      38.739   3.641 -37.102  1.00138.68      A    O1-
ANISOU   22  OE2 GLU A   9    16726  20404  15564   2348  -2126    609  A    O1-
ATOM     23  N   CYS A  10      40.508  -1.347 -33.417  1.00 94.38      A    N  
ANISOU   23  N   CYS A  10    10664  14612  10583   1849  -1717     23  A    N  
ATOM     24  CA  CYS A  10      40.695  -1.803 -32.054  1.00 86.31      A    C  
ANISOU   24  CA  CYS A  10     9510  13485   9800   1708  -1617    -17  A    C  
ATOM     25  C   CYS A  10      41.765  -0.994 -31.360  1.00 89.39      A    C  
ANISOU   25  C   CYS A  10     9893  13840  10229   1651  -1405    158  A    C  
ATOM     26  O   CYS A  10      42.903  -1.437 -31.229  1.00108.90      A    O  
ANISOU   26  O   CYS A  10    12397  16325  12655   1630  -1263    175  A    O  
ATOM     27  CB  CYS A  10      41.042  -3.283 -32.029  1.00 78.86      A    C  
ANISOU   27  CB  CYS A  10     8580  12534   8850   1681  -1618   -185  A    C  
ATOM     28  SG  CYS A  10      40.639  -4.050 -30.472  1.00118.34      A    S  
ANISOU   28  SG  CYS A  10    13421  17389  14153   1510  -1598   -287  A    S  
ATOM     29  N   PRO A  11      41.390   0.198 -30.896  1.00 77.29      A    N  
ANISOU   29  N   PRO A  11     8315  12258   8794   1627  -1392    284  A    N  
ATOM     30  CA  PRO A  11      42.295   1.161 -30.276  1.00 68.52      A    C  
ANISOU   30  CA  PRO A  11     7207  11104   7723   1569  -1214    461  A    C  
ATOM     31  C   PRO A  11      42.808   0.672 -28.922  1.00 73.11      A    C  
ANISOU   31  C   PRO A  11     7692  11593   8495   1430  -1097    430  A    C  
ATOM     32  O   PRO A  11      43.939   0.985 -28.565  1.00 77.91      A    O  
ANISOU   32  O   PRO A  11     8316  12192   9094   1384   -942    538  A    O  
ATOM     33  CB  PRO A  11      41.406   2.390 -30.069  1.00 69.99      A    C  
ANISOU   33  CB  PRO A  11     7361  11237   7996   1584  -1280    552  A    C  
ATOM     34  CG  PRO A  11      40.145   2.122 -30.820  1.00 81.01      A    C  
ANISOU   34  CG  PRO A  11     8748  12677   9357   1677  -1495    440  A    C  
ATOM     35  CD  PRO A  11      39.996   0.651 -30.839  1.00 83.75      A    C  
ANISOU   35  CD  PRO A  11     9058  13045   9720   1648  -1556    248  A    C  
ATOM     36  N   PHE A  12      41.999  -0.087 -28.187  1.00 73.28      A    N  
ANISOU   36  N   PHE A  12     7616  11546   8683   1361  -1173    288  A    N  
ATOM     37  CA  PHE A  12      42.333  -0.413 -26.802  1.00 62.66      A    C  
ANISOU   37  CA  PHE A  12     6192  10096   7521   1224  -1074    274  A    C  
ATOM     38  C   PHE A  12      42.610  -1.892 -26.531  1.00 63.88      A    C  
ANISOU   38  C   PHE A  12     6335  10231   7705   1180  -1079    128  A    C  
ATOM     39  O   PHE A  12      42.564  -2.343 -25.381  1.00 61.54      A    O  
ANISOU   39  O   PHE A  12     5977   9837   7569   1065  -1040     85  A    O  
ATOM     40  CB  PHE A  12      41.236   0.070 -25.860  1.00 65.00      A    C  
ANISOU   40  CB  PHE A  12     6386  10298   8014   1152  -1114    256  A    C  
ATOM     41  CG  PHE A  12      40.766   1.453 -26.141  1.00 69.61      A    C  
ANISOU   41  CG  PHE A  12     6978  10884   8585   1213  -1138    375  A    C  
ATOM     42  CD1 PHE A  12      41.660   2.495 -26.221  1.00 66.13      A    C  
ANISOU   42  CD1 PHE A  12     6611  10445   8072   1224  -1028    547  A    C  
ATOM     43  CD2 PHE A  12      39.423   1.714 -26.313  1.00 73.94      A    C  
ANISOU   43  CD2 PHE A  12     7457  11429   9208   1258  -1273    314  A    C  
ATOM     44  CE1 PHE A  12      41.223   3.772 -26.472  1.00 72.56      A    C  
ANISOU   44  CE1 PHE A  12     7450  11242   8878   1282  -1054    660  A    C  
ATOM     45  CE2 PHE A  12      38.981   2.989 -26.561  1.00 75.59      A    C  
ANISOU   45  CE2 PHE A  12     7679  11629   9414   1329  -1304    423  A    C  
ATOM     46  CZ  PHE A  12      39.880   4.019 -26.644  1.00 74.60      A    C  
ANISOU   46  CZ  PHE A  12     7648  11491   9206   1342  -1195    597  A    C  
ATOM     47  N   CYS A  13      42.887  -2.652 -27.580  1.00 63.05      A    N  
ANISOU   47  N   CYS A  13     6306  10212   7440   1272  -1128     52  A    N  
ATOM     48  CA  CYS A  13      43.310  -4.030 -27.397  1.00 63.48      A    C  
ANISOU   48  CA  CYS A  13     6372  10240   7508   1247  -1123    -77  A    C  
ATOM     49  C   CYS A  13      44.386  -4.292 -28.428  1.00 75.99      A    C  
ANISOU   49  C   CYS A  13     8059  11929   8885   1360  -1061    -58  A    C  
ATOM     50  O   CYS A  13      44.102  -4.534 -29.604  1.00 83.49      A    O  
ANISOU   50  O   CYS A  13     9088  12966   9667   1468  -1149   -122  A    O  
ATOM     51  CB  CYS A  13      42.141  -5.002 -27.544  1.00 61.34      A    C  
ANISOU   51  CB  CYS A  13     6074   9938   7295   1232  -1287   -260  A    C  
ATOM     52  SG  CYS A  13      42.493  -6.700 -27.035  1.00 74.18      A    S  
ANISOU   52  SG  CYS A  13     7715  11478   8991   1168  -1288   -421  A    S  
ATOM     53  N   ASP A  14      45.633  -4.196 -27.984  1.00 74.88      A    N  
ANISOU   53  N   ASP A  14     7914  11785   8752   1335   -908     32  A    N  
ATOM     54  CA  ASP A  14      46.759  -4.324 -28.890  1.00 74.95      A    C  
ANISOU   54  CA  ASP A  14     7998  11901   8579   1439   -811     68  A    C  
ATOM     55  C   ASP A  14      47.027  -5.795 -29.176  1.00 75.54      A    C  
ANISOU   55  C   ASP A  14     8114  11974   8614   1490   -844   -101  A    C  
ATOM     56  O   ASP A  14      46.701  -6.657 -28.359  1.00 71.80      A    O  
ANISOU   56  O   ASP A  14     7599  11393   8288   1415   -899   -207  A    O  
ATOM     57  CB  ASP A  14      47.995  -3.618 -28.317  1.00 79.42      A    C  
ANISOU   57  CB  ASP A  14     8520  12469   9187   1390   -637    230  A    C  
ATOM     58  CG  ASP A  14      47.884  -2.092 -28.374  1.00 93.35      A    C  
ANISOU   58  CG  ASP A  14    10284  14251  10935   1366   -594    407  A    C  
ATOM     59  OD1 ASP A  14      47.032  -1.568 -29.133  1.00 99.45      A    O  
ANISOU   59  OD1 ASP A  14    11110  15063  11611   1427   -684    418  A    O  
ATOM     60  OD2 ASP A  14      48.660  -1.418 -27.660  1.00 94.69      A    O1-
ANISOU   60  OD2 ASP A  14    10404  14387  11188   1288   -478    535  A    O1-
ATOM     61  N   GLU A  15      47.592  -6.080 -30.348  1.00 82.93      A    N  
ANISOU   61  N   GLU A  15     9143  13023   9342   1620   -810   -129  A    N  
ATOM     62  CA  GLU A  15      47.958  -7.446 -30.701  1.00 82.66      A    C  
ANISOU   62  CA  GLU A  15     9164  12987   9254   1690   -828   -292  A    C  
ATOM     63  C   GLU A  15      49.179  -7.887 -29.887  1.00 79.62      A    C  
ANISOU   63  C   GLU A  15     8716  12558   8976   1661   -691   -264  A    C  
ATOM     64  O   GLU A  15      50.141  -7.135 -29.746  1.00 80.96      A    O  
ANISOU   64  O   GLU A  15     8839  12781   9140   1656   -544   -115  A    O  
ATOM     65  CB  GLU A  15      48.228  -7.549 -32.200  1.00 86.65      A    C  
ANISOU   65  CB  GLU A  15     9799  13632   9491   1846   -816   -329  A    C  
ATOM     66  CG  GLU A  15      47.282  -6.702 -33.051  1.00 97.53      A    C  
ANISOU   66  CG  GLU A  15    11244  15080  10735   1885   -923   -286  A    C  
ATOM     67  CD  GLU A  15      47.298  -7.087 -34.530  1.00112.77      A    C  
ANISOU   67  CD  GLU A  15    13333  17127  12387   2037   -964   -373  A    C  
ATOM     68  OE1 GLU A  15      48.292  -7.691 -34.993  1.00112.25      A    O  
ANISOU   68  OE1 GLU A  15    13325  17119  12204   2124   -844   -417  A    O  
ATOM     69  OE2 GLU A  15      46.308  -6.782 -35.232  1.00121.38      A    O1-
ANISOU   69  OE2 GLU A  15    14492  18252  13373   2076  -1119   -401  A    O1-
ATOM     70  N   VAL A  16      49.131  -9.101 -29.344  1.00 72.97      A    N  
ANISOU   70  N   VAL A  16     7873  11612   8240   1638   -749   -403  A    N  
ATOM     71  CA  VAL A  16      50.199  -9.604 -28.486  1.00 71.09      A    C  
ANISOU   71  CA  VAL A  16     7578  11313   8121   1614   -653   -385  A    C  
ATOM     72  C   VAL A  16      51.547  -9.753 -29.217  1.00 72.46      A    C  
ANISOU   72  C   VAL A  16     7766  11602   8163   1748   -506   -362  A    C  
ATOM     73  O   VAL A  16      52.581  -9.993 -28.604  1.00 73.20      A    O  
ANISOU   73  O   VAL A  16     7791  11672   8350   1746   -413   -323  A    O  
ATOM     74  CB  VAL A  16      49.788 -10.932 -27.788  1.00 62.00      A    C  
ANISOU   74  CB  VAL A  16     6446  10009   7102   1565   -760   -542  A    C  
ATOM     75  CG1 VAL A  16      49.941 -12.111 -28.727  1.00 60.33      A    C  
ANISOU   75  CG1 VAL A  16     6341   9816   6764   1700   -803   -714  A    C  
ATOM     76  CG2 VAL A  16      50.606 -11.155 -26.517  1.00 60.16      A    C  
ANISOU   76  CG2 VAL A  16     6140   9678   7041   1491   -694   -481  A    C  
ATOM     77  N   SER A  17      51.540  -9.587 -30.530  1.00 77.15      A    N  
ANISOU   77  N   SER A  17     8449  12326   8540   1868   -483   -383  A    N  
ATOM     78  CA  SER A  17      52.779  -9.641 -31.301  1.00 73.85      A    C  
ANISOU   78  CA  SER A  17     8044  12035   7981   1997   -319   -356  A    C  
ATOM     79  C   SER A  17      53.755  -8.533 -30.902  1.00 73.28      A    C  
ANISOU   79  C   SER A  17     7856  12025   7962   1943   -151   -150  A    C  
ATOM     80  O   SER A  17      54.925  -8.579 -31.282  1.00 76.58      A    O  
ANISOU   80  O   SER A  17     8237  12538   8320   2024      7   -113  A    O  
ATOM     81  CB  SER A  17      52.481  -9.538 -32.795  1.00 74.65      A    C  
ANISOU   81  CB  SER A  17     8283  12266   7813   2124   -324   -404  A    C  
ATOM     82  OG  SER A  17      52.019  -8.233 -33.135  1.00 85.80      A    O  
ANISOU   82  OG  SER A  17     9707  13746   9147   2081   -321   -254  A    O  
ATOM     83  N   LYS A  18      53.273  -7.538 -30.152  1.00 64.36      A    N  
ANISOU   83  N   LYS A  18     6666  10841   6947   1806   -183    -22  A    N  
ATOM     84  CA  LYS A  18      54.121  -6.444 -29.675  1.00 63.81      A    C  
ANISOU   84  CA  LYS A  18     6492  10806   6946   1730    -44    172  A    C  
ATOM     85  C   LYS A  18      55.138  -6.973 -28.658  1.00 67.64      A    C  
ANISOU   85  C   LYS A  18     6861  11230   7610   1693     13    174  A    C  
ATOM     86  O   LYS A  18      56.155  -6.331 -28.383  1.00 63.23      A    O  
ANISOU   86  O   LYS A  18     6201  10719   7102   1657    143    307  A    O  
ATOM     87  CB  LYS A  18      53.277  -5.332 -29.039  1.00 60.85      A    C  
ANISOU   87  CB  LYS A  18     6097  10361   6661   1596   -111    285  A    C  
ATOM     88  CG  LYS A  18      52.708  -5.707 -27.667  1.00 65.54      A    C  
ANISOU   88  CG  LYS A  18     6638  10792   7473   1474   -220    235  A    C  
ATOM     89  CD  LYS A  18      51.674  -4.710 -27.166  1.00 73.27      A    C  
ANISOU   89  CD  LYS A  18     7612  11705   8522   1366   -293    311  A    C  
ATOM     90  CE  LYS A  18      52.320  -3.435 -26.654  1.00 80.37      A    C  
ANISOU   90  CE  LYS A  18     8446  12607   9482   1278   -185    501  A    C  
ATOM     91  NZ  LYS A  18      51.388  -2.633 -25.818  1.00 78.80      A    N1+
ANISOU   91  NZ  LYS A  18     8234  12304   9402   1164   -255    553  A    N1+
ATOM     92  N   TYR A  19      54.833  -8.140 -28.091  1.00 63.14      A    N  
ANISOU   92  N   TYR A  19     6307  10547   7138   1697    -95     27  A    N  
ATOM     93  CA  TYR A  19      55.728  -8.829 -27.180  1.00 61.27      A    C  
ANISOU   93  CA  TYR A  19     5985  10238   7056   1686    -72      8  A    C  
ATOM     94  C   TYR A  19      56.349 -10.006 -27.923  1.00 76.99      A    C  
ANISOU   94  C   TYR A  19     8015  12276   8962   1855    -35   -134  A    C  
ATOM     95  O   TYR A  19      55.724 -10.593 -28.806  1.00 90.28      A    O  
ANISOU   95  O   TYR A  19     9818  13980  10506   1945    -94   -264  A    O  
ATOM     96  CB  TYR A  19      54.976  -9.312 -25.928  1.00 56.69      A    C  
ANISOU   96  CB  TYR A  19     5412   9477   6651   1566   -215    -46  A    C  
ATOM     97  CG  TYR A  19      54.373  -8.190 -25.102  1.00 63.12      A    C  
ANISOU   97  CG  TYR A  19     6190  10235   7559   1405   -242     80  A    C  
ATOM     98  CD1 TYR A  19      55.163  -7.413 -24.273  1.00 67.57      A    C  
ANISOU   98  CD1 TYR A  19     6655  10789   8230   1316   -170    224  A    C  
ATOM     99  CD2 TYR A  19      53.017  -7.900 -25.162  1.00 67.44      A    C  
ANISOU   99  CD2 TYR A  19     6798  10739   8088   1347   -342     48  A    C  
ATOM    100  CE1 TYR A  19      54.627  -6.389 -23.529  1.00 71.53      A    C  
ANISOU  100  CE1 TYR A  19     7140  11231   8809   1177   -191    328  A    C  
ATOM    101  CE2 TYR A  19      52.469  -6.871 -24.417  1.00 66.99      A    C  
ANISOU  101  CE2 TYR A  19     6707  10628   8118   1216   -356    155  A    C  
ATOM    102  CZ  TYR A  19      53.279  -6.120 -23.604  1.00 72.42      A    C  
ANISOU  102  CZ  TYR A  19     7317  11299   8900   1134   -278    292  A    C  
ATOM    103  OH  TYR A  19      52.753  -5.091 -22.861  1.00 70.35      A    O  
ANISOU  103  OH  TYR A  19     7036  10975   8718   1010   -290    389  A    O  
ATOM    104  N   GLU A  20      57.587 -10.333 -27.570  1.00 77.54      A    N  
ANISOU  104  N   GLU A  20     7982  12363   9116   1902     57   -111  A    N  
ATOM    105  CA  GLU A  20      58.319 -11.433 -28.175  1.00 78.21      A    C  
ANISOU  105  CA  GLU A  20     8085  12488   9144   2076    108   -241  A    C  
ATOM    106  C   GLU A  20      58.487 -12.517 -27.109  1.00 77.89      A    C  
ANISOU  106  C   GLU A  20     8029  12281   9285   2066      2   -328  A    C  
ATOM    107  O   GLU A  20      59.127 -12.288 -26.083  1.00 78.11      A    O  
ANISOU  107  O   GLU A  20     7941  12260   9477   1991     10   -234  A    O  
ATOM    108  CB  GLU A  20      59.682 -10.920 -28.645  1.00 88.94      A    C  
ANISOU  108  CB  GLU A  20     9317  14009  10468   2150    311   -139  A    C  
ATOM    109  CG  GLU A  20      60.501 -11.862 -29.501  1.00107.69      A    C  
ANISOU  109  CG  GLU A  20    11701  16468  12749   2354    412   -264  A    C  
ATOM    110  CD  GLU A  20      61.808 -11.224 -29.973  1.00125.35      A    C  
ANISOU  110  CD  GLU A  20    13790  18881  14956   2409    637   -147  A    C  
ATOM    111  OE1 GLU A  20      62.308 -10.301 -29.289  1.00124.25      A    O  
ANISOU  111  OE1 GLU A  20    13507  18759  14945   2282    687     20  A    O  
ATOM    112  OE2 GLU A  20      62.330 -11.644 -31.032  1.00133.56      A    O1-
ANISOU  112  OE2 GLU A  20    14858  20042  15845   2575    767   -225  A    O1-
ATOM    113  N   LYS A  21      57.890 -13.685 -27.331  1.00 75.45      A    N  
ANISOU  113  N   LYS A  21     7847  11876   8945   2136   -109   -505  A    N  
ATOM    114  CA  LYS A  21      58.032 -14.797 -26.392  1.00 73.61      A    C  
ANISOU  114  CA  LYS A  21     7629  11470   8869   2136   -212   -591  A    C  
ATOM    115  C   LYS A  21      59.500 -15.239 -26.264  1.00 78.45      A    C  
ANISOU  115  C   LYS A  21     8131  12121   9555   2266   -114   -585  A    C  
ATOM    116  O   LYS A  21      60.249 -15.258 -27.241  1.00 74.48      A    O  
ANISOU  116  O   LYS A  21     7594  11765   8941   2417     22   -610  A    O  
ATOM    117  CB  LYS A  21      57.153 -15.983 -26.808  1.00 69.41      A    C  
ANISOU  117  CB  LYS A  21     7266  10828   8277   2192   -340   -789  A    C  
ATOM    118  CG  LYS A  21      55.663 -15.695 -26.828  1.00 72.20      A    C  
ANISOU  118  CG  LYS A  21     7709  11128   8596   2058   -461   -813  A    C  
ATOM    119  CD  LYS A  21      54.851 -16.910 -27.272  1.00 79.72      A    C  
ANISOU  119  CD  LYS A  21     8818  11972   9499   2106   -593  -1016  A    C  
ATOM    120  CE  LYS A  21      53.386 -16.539 -27.521  1.00 87.79      A    C  
ANISOU  120  CE  LYS A  21     9904  12981  10472   1990   -705  -1044  A    C  
ATOM    121  NZ  LYS A  21      52.650 -17.523 -28.380  1.00 93.03      A    N1+
ANISOU  121  NZ  LYS A  21    10717  13599  11030   2059   -819  -1245  A    N1+
ATOM    122  N   LEU A  22      59.909 -15.595 -25.053  1.00 79.19      A    N  
ANISOU  122  N   LEU A  22     8167  12085   9835   2211   -184   -551  A    N  
ATOM    123  CA  LEU A  22      61.280 -16.022 -24.813  1.00 79.20      A    C  
ANISOU  123  CA  LEU A  22     8046  12112   9935   2333   -119   -542  A    C  
ATOM    124  C   LEU A  22      61.340 -17.448 -24.284  1.00 88.69      A    C  
ANISOU  124  C   LEU A  22     9336  13129  11234   2415   -246   -676  A    C  
ATOM    125  O   LEU A  22      62.318 -18.171 -24.521  1.00 91.75      A    O  
ANISOU  125  O   LEU A  22     9673  13534  11654   2592   -199   -744  A    O  
ATOM    126  CB  LEU A  22      61.950 -15.101 -23.799  1.00 75.20      A    C  
ANISOU  126  CB  LEU A  22     7374  11623   9575   2208    -96   -361  A    C  
ATOM    127  CG  LEU A  22      62.116 -13.643 -24.203  1.00 75.08      A    C  
ANISOU  127  CG  LEU A  22     7255  11777   9496   2123     38   -206  A    C  
ATOM    128  CD1 LEU A  22      62.658 -12.831 -23.030  1.00 66.60      A    C  
ANISOU  128  CD1 LEU A  22     6044  10675   8584   1975     20    -45  A    C  
ATOM    129  CD2 LEU A  22      63.022 -13.542 -25.425  1.00 73.16      A    C  
ANISOU  129  CD2 LEU A  22     6927  11730   9139   2286    225   -219  A    C  
ATOM    130  N   ALA A  23      60.298 -17.843 -23.557  1.00 85.53      A    N  
ANISOU  130  N   ALA A  23     9065  12548  10884   2285   -401   -712  A    N  
ATOM    131  CA  ALA A  23      60.321 -19.104 -22.836  1.00 84.26      A    C  
ANISOU  131  CA  ALA A  23     8999  12181  10833   2322   -532   -806  A    C  
ATOM    132  C   ALA A  23      58.968 -19.425 -22.240  1.00 85.42      A    C  
ANISOU  132  C   ALA A  23     9301  12152  11003   2155   -676   -846  A    C  
ATOM    133  O   ALA A  23      58.318 -18.553 -21.676  1.00 89.21      A    O  
ANISOU  133  O   ALA A  23     9759  12632  11506   1973   -691   -739  A    O  
ATOM    134  CB  ALA A  23      61.376 -19.053 -21.734  1.00 74.36      A    C  
ANISOU  134  CB  ALA A  23     7620  10883   9750   2315   -550   -698  A    C  
ATOM    135  N   LYS A  24      58.558 -20.684 -22.364  1.00 84.46      A    N  
ANISOU  135  N   LYS A  24     9334  11876  10881   2216   -775  -1002  A    N  
ATOM    136  CA  LYS A  24      57.368 -21.195 -21.694  1.00 82.91      A    C  
ANISOU  136  CA  LYS A  24     9283  11485  10735   2056   -913  -1047  A    C  
ATOM    137  C   LYS A  24      57.746 -21.623 -20.275  1.00 84.78      A    C  
ANISOU  137  C   LYS A  24     9536  11543  11133   1986   -998   -974  A    C  
ATOM    138  O   LYS A  24      58.342 -22.676 -20.075  1.00 92.24      A    O  
ANISOU  138  O   LYS A  24    10544  12365  12139   2107  -1055  -1045  A    O  
ATOM    139  CB  LYS A  24      56.789 -22.370 -22.482  1.00 86.98      A    C  
ANISOU  139  CB  LYS A  24     9966  11903  11180   2144   -986  -1247  A    C  
ATOM    140  CG  LYS A  24      55.565 -23.033 -21.871  1.00 99.12      A    C  
ANISOU  140  CG  LYS A  24    11652  13231  12778   1977  -1126  -1310  A    C  
ATOM    141  CD  LYS A  24      55.122 -24.206 -22.740  1.00114.09      A    C  
ANISOU  141  CD  LYS A  24    13711  15034  14605   2075  -1200  -1517  A    C  
ATOM    142  CE  LYS A  24      53.917 -24.929 -22.157  1.00121.13      A    C  
ANISOU  142  CE  LYS A  24    14746  15708  15570   1896  -1338  -1584  A    C  
ATOM    143  NZ  LYS A  24      53.483 -26.058 -23.034  1.00123.72      A    N1+
ANISOU  143  NZ  LYS A  24    15236  15938  15834   1981  -1421  -1793  A    N1+
ATOM    144  N   ILE A  25      57.394 -20.801 -19.291  1.00 78.57      A    N  
ANISOU  144  N   ILE A  25     8706  10739  10409   1796  -1009   -835  A    N  
ATOM    145  CA  ILE A  25      57.889 -20.972 -17.931  1.00 83.78      A    C  
ANISOU  145  CA  ILE A  25     9370  11263  11200   1729  -1077   -738  A    C  
ATOM    146  C   ILE A  25      56.931 -21.683 -16.978  1.00 88.22      A    C  
ANISOU  146  C   ILE A  25    10103  11593  11823   1571  -1196   -763  A    C  
ATOM    147  O   ILE A  25      57.313 -22.039 -15.865  1.00 90.13      A    O  
ANISOU  147  O   ILE A  25    10394  11693  12157   1528  -1268   -698  A    O  
ATOM    148  CB  ILE A  25      58.235 -19.615 -17.307  1.00 86.96      A    C  
ANISOU  148  CB  ILE A  25     9629  11779  11635   1616  -1015   -563  A    C  
ATOM    149  CG1 ILE A  25      56.965 -18.779 -17.143  1.00 87.87      A    C  
ANISOU  149  CG1 ILE A  25     9769  11908  11709   1418  -1001   -521  A    C  
ATOM    150  CG2 ILE A  25      59.254 -18.890 -18.168  1.00 85.98      A    C  
ANISOU  150  CG2 ILE A  25     9327  11877  11465   1751   -889   -520  A    C  
ATOM    151  CD1 ILE A  25      57.132 -17.579 -16.262  1.00 90.16      A    C  
ANISOU  151  CD1 ILE A  25     9969  12243  12045   1278   -968   -358  A    C  
ATOM    152  N   GLY A  26      55.691 -21.888 -17.402  1.00 97.97      A    N  
ANISOU  152  N   GLY A  26    11430  12788  13006   1481  -1218   -853  A    N  
ATOM    153  CA  GLY A  26      54.698 -22.466 -16.516  1.00115.89      A    C  
ANISOU  153  CA  GLY A  26    13845  14851  15336   1305  -1307   -869  A    C  
ATOM    154  C   GLY A  26      53.836 -23.547 -17.137  1.00131.99      A    C  
ANISOU  154  C   GLY A  26    16027  16773  17351   1310  -1377  -1038  A    C  
ATOM    155  O   GLY A  26      53.013 -23.275 -18.025  1.00127.30      A    O  
ANISOU  155  O   GLY A  26    15414  16272  16683   1286  -1358  -1115  A    O  
ATOM    156  N   GLN A  27      54.020 -24.777 -16.655  1.00142.72      A    N  
ANISOU  156  N   GLN A  27    17536  17917  18775   1337  -1470  -1096  A    N  
ATOM    157  CA  GLN A  27      53.200 -25.904 -17.090  1.00149.01      A    C  
ANISOU  157  CA  GLN A  27    18492  18558  19567   1317  -1552  -1256  A    C  
ATOM    158  C   GLN A  27      52.343 -26.480 -15.963  1.00142.56      A    C  
ANISOU  158  C   GLN A  27    17818  17508  18839   1102  -1626  -1230  A    C  
ATOM    159  O   GLN A  27      52.790 -26.618 -14.820  1.00134.18      A    O  
ANISOU  159  O   GLN A  27    16810  16328  17846   1052  -1651  -1121  A    O  
ATOM    160  CB  GLN A  27      54.054 -26.996 -17.737  1.00158.90      A    C  
ANISOU  160  CB  GLN A  27    19827  19740  20807   1550  -1597  -1381  A    C  
ATOM    161  CG  GLN A  27      54.419 -26.702 -19.184  1.00165.19      A    C  
ANISOU  161  CG  GLN A  27    20535  20745  21484   1739  -1524  -1477  A    C  
ATOM    162  CD  GLN A  27      54.938 -27.923 -19.914  1.00170.79      A    C  
ANISOU  162  CD  GLN A  27    21365  21358  22171   1950  -1572  -1644  A    C  
ATOM    163  NE2 GLN A  27      55.077 -27.813 -21.232  1.00172.07      A    N  
ANISOU  163  NE2 GLN A  27    21494  21679  22207   2103  -1514  -1756  A    N  
ATOM    164  OE1 GLN A  27      55.211 -28.955 -19.302  1.00172.60      A    O  
ANISOU  164  OE1 GLN A  27    21728  21365  22486   1980  -1661  -1674  A    O  
ATOM    165  N   GLY A  28      51.104 -26.811 -16.315  1.00144.38      A    N  
ANISOU  165  N   GLY A  28    18112  17680  19065    971  -1660  -1331  A    N  
ATOM    166  CA  GLY A  28      50.106 -27.272 -15.370  1.00148.21      A    C  
ANISOU  166  CA  GLY A  28    18713  17970  19631    738  -1704  -1313  A    C  
ATOM    167  C   GLY A  28      48.737 -27.165 -16.015  1.00153.30      A    C  
ANISOU  167  C   GLY A  28    19328  18657  20263    605  -1712  -1414  A    C  
ATOM    168  O   GLY A  28      48.635 -27.086 -17.241  1.00152.07      A    O  
ANISOU  168  O   GLY A  28    19122  18629  20030    719  -1722  -1527  A    O  
ATOM    169  N   THR A  29      47.687 -27.149 -15.198  1.00158.72      A    N  
ANISOU  169  N   THR A  29    20042  19241  21022    364  -1707  -1375  A    N  
ATOM    170  CA  THR A  29      46.317 -27.080 -15.708  1.00163.01      A    C  
ANISOU  170  CA  THR A  29    20539  19816  21582    219  -1724  -1470  A    C  
ATOM    171  C   THR A  29      45.741 -25.665 -15.603  1.00162.21      A    C  
ANISOU  171  C   THR A  29    20249  19914  21469    128  -1631  -1378  A    C  
ATOM    172  O   THR A  29      44.537 -25.455 -15.772  1.00159.79      A    O  
ANISOU  172  O   THR A  29    19877  19636  21200    -18  -1634  -1428  A    O  
ATOM    173  CB  THR A  29      45.392 -28.086 -14.988  1.00165.78      A    C  
ANISOU  173  CB  THR A  29    21033  19918  22037      2  -1775  -1511  A    C  
ATOM    174  CG2 THR A  29      44.064 -28.232 -15.729  1.00165.25      A    C  
ANISOU  174  CG2 THR A  29    20913  19875  21998   -120  -1822  -1647  A    C  
ATOM    175  OG1 THR A  29      46.037 -29.365 -14.918  1.00168.72      A    O  
ANISOU  175  OG1 THR A  29    21603  20078  22426     90  -1861  -1571  A    O  
ATOM    176  N   PHE A  30      46.614 -24.701 -15.325  1.00164.79      A    N  
ANISOU  176  N   PHE A  30    20487  20375  21752    216  -1553  -1247  A    N  
ATOM    177  CA  PHE A  30      46.239 -23.290 -15.284  1.00162.05      A    C  
ANISOU  177  CA  PHE A  30    19971  20216  21384    163  -1465  -1156  A    C  
ATOM    178  C   PHE A  30      46.365 -22.664 -16.673  1.00168.45      A    C  
ANISOU  178  C   PHE A  30    20667  21243  22093    323  -1462  -1214  A    C  
ATOM    179  O   PHE A  30      45.939 -21.527 -16.902  1.00166.14      A    O  
ANISOU  179  O   PHE A  30    20241  21111  21775    296  -1407  -1161  A    O  
ATOM    180  CB  PHE A  30      47.138 -22.538 -14.305  1.00147.50      A    C  
ANISOU  180  CB  PHE A  30    18100  18402  19543    170  -1390   -986  A    C  
ATOM    181  CG  PHE A  30      48.603 -22.703 -14.589  1.00137.27      A    C  
ANISOU  181  CG  PHE A  30    16817  17142  18197    379  -1402   -961  A    C  
ATOM    182  CD1 PHE A  30      49.359 -23.624 -13.883  1.00133.30      A    C  
ANISOU  182  CD1 PHE A  30    16449  16465  17735    414  -1455   -941  A    C  
ATOM    183  CD2 PHE A  30      49.223 -21.949 -15.575  1.00134.35      A    C  
ANISOU  183  CD2 PHE A  30    16322  16980  17743    543  -1359   -957  A    C  
ATOM    184  CE1 PHE A  30      50.711 -23.779 -14.143  1.00134.48      A    C  
ANISOU  184  CE1 PHE A  30    16586  16654  17855    617  -1467   -923  A    C  
ATOM    185  CE2 PHE A  30      50.573 -22.104 -15.844  1.00132.86      A    C  
ANISOU  185  CE2 PHE A  30    16125  16836  17521    733  -1355   -937  A    C  
ATOM    186  CZ  PHE A  30      51.318 -23.016 -15.124  1.00133.98      A    C  
ANISOU  186  CZ  PHE A  30    16379  16810  17718    773  -1410   -923  A    C  
ATOM    187  N   GLY A  31      46.965 -23.416 -17.593  1.00171.61      A    N  
ANISOU  187  N   GLY A  31    21135  21639  22429    495  -1520  -1323  A    N  
ATOM    188  CA  GLY A  31      47.188 -22.944 -18.947  1.00168.90      A    C  
ANISOU  188  CA  GLY A  31    20719  21492  21965    661  -1513  -1383  A    C  
ATOM    189  C   GLY A  31      48.662 -22.850 -19.294  1.00165.07      A    C  
ANISOU  189  C   GLY A  31    20222  21090  21405    874  -1461  -1342  A    C  
ATOM    190  O   GLY A  31      49.472 -23.670 -18.854  1.00162.80      A    O  
ANISOU  190  O   GLY A  31    20026  20674  21158    943  -1483  -1348  A    O  
ATOM    191  N   GLU A  32      49.005 -21.841 -20.088  1.00161.74      A    N  
ANISOU  191  N   GLU A  32    19686  20885  20882    980  -1391  -1298  A    N  
ATOM    192  CA  GLU A  32      50.385 -21.623 -20.506  1.00154.52      A    C  
ANISOU  192  CA  GLU A  32    18731  20082  19898   1175  -1319  -1254  A    C  
ATOM    193  C   GLU A  32      50.871 -20.228 -20.139  1.00135.26      A    C  
ANISOU  193  C   GLU A  32    16147  17794  17454   1153  -1211  -1077  A    C  
ATOM    194  O   GLU A  32      50.291 -19.231 -20.573  1.00133.66      A    O  
ANISOU  194  O   GLU A  32    15863  17726  17197   1110  -1176  -1036  A    O  
ATOM    195  CB  GLU A  32      50.522 -21.822 -22.015  1.00160.88      A    C  
ANISOU  195  CB  GLU A  32    19557  21012  20557   1351  -1321  -1381  A    C  
ATOM    196  CG  GLU A  32      50.825 -23.246 -22.440  1.00165.49      A    C  
ANISOU  196  CG  GLU A  32    20288  21463  21129   1472  -1395  -1546  A    C  
ATOM    197  CD  GLU A  32      50.996 -23.373 -23.941  1.00168.68      A    C  
ANISOU  197  CD  GLU A  32    20723  22001  21365   1653  -1384  -1674  A    C  
ATOM    198  OE1 GLU A  32      50.181 -22.780 -24.683  1.00169.22      A    O  
ANISOU  198  OE1 GLU A  32    20764  22189  21342   1616  -1401  -1700  A    O  
ATOM    199  OE2 GLU A  32      51.942 -24.063 -24.378  1.00169.10      A    O1-
ANISOU  199  OE2 GLU A  32    20834  22041  21375   1839  -1360  -1749  A    O1-
ATOM    200  N   VAL A  33      51.941 -20.167 -19.348  1.00116.71      A    N  
ANISOU  200  N   VAL A  33    13768  15412  15164   1184  -1171   -975  A    N  
ATOM    201  CA  VAL A  33      52.574 -18.896 -19.001  1.00 94.77      A    C  
ANISOU  201  CA  VAL A  33    10855  12767  12386   1170  -1076   -811  A    C  
ATOM    202  C   VAL A  33      53.913 -18.706 -19.720  1.00 81.44      A    C  
ANISOU  202  C   VAL A  33     9086  11223  10634   1365   -997   -788  A    C  
ATOM    203  O   VAL A  33      54.796 -19.556 -19.633  1.00 82.95      A    O  
ANISOU  203  O   VAL A  33     9310  11350  10859   1484  -1016   -830  A    O  
ATOM    204  CB  VAL A  33      52.801 -18.795 -17.498  1.00 84.30      A    C  
ANISOU  204  CB  VAL A  33     9538  11315  11177   1040  -1090   -696  A    C  
ATOM    205  CG1 VAL A  33      53.299 -17.411 -17.135  1.00 74.57      A    C  
ANISOU  205  CG1 VAL A  33     8176  10211   9946    999  -1004   -537  A    C  
ATOM    206  CG2 VAL A  33      51.521 -19.105 -16.778  1.00 88.03      A    C  
ANISOU  206  CG2 VAL A  33    10099  11639  11711    850  -1149   -726  A    C  
ATOM    207  N   PHE A  34      54.053 -17.587 -20.425  1.00 68.28      A    N  
ANISOU  207  N   PHE A  34     7314   9748   8881   1396   -904   -720  A    N  
ATOM    208  CA  PHE A  34      55.255 -17.291 -21.194  1.00 67.38      A    C  
ANISOU  208  CA  PHE A  34     7110   9792   8698   1565   -801   -690  A    C  
ATOM    209  C   PHE A  34      55.977 -16.082 -20.627  1.00 66.77      A    C  
ANISOU  209  C   PHE A  34     6894   9808   8667   1506   -716   -510  A    C  
ATOM    210  O   PHE A  34      55.341 -15.098 -20.266  1.00 69.40      A    O  
ANISOU  210  O   PHE A  34     7197  10163   9009   1366   -704   -419  A    O  
ATOM    211  CB  PHE A  34      54.890 -16.946 -22.636  1.00 75.42      A    C  
ANISOU  211  CB  PHE A  34     8135  10969   9551   1655   -751   -752  A    C  
ATOM    212  CG  PHE A  34      54.487 -18.118 -23.472  1.00 86.50      A    C  
ANISOU  212  CG  PHE A  34     9668  12320  10878   1762   -820   -942  A    C  
ATOM    213  CD1 PHE A  34      55.442 -18.992 -23.969  1.00 95.82      A    C  
ANISOU  213  CD1 PHE A  34    10876  13503  12027   1948   -790  -1033  A    C  
ATOM    214  CD2 PHE A  34      53.158 -18.322 -23.803  1.00 92.92      A    C  
ANISOU  214  CD2 PHE A  34    10570  13084  11651   1681   -915  -1037  A    C  
ATOM    215  CE1 PHE A  34      55.077 -20.066 -24.754  1.00 99.80      A    C  
ANISOU  215  CE1 PHE A  34    11517  13949  12454   2050   -856  -1219  A    C  
ATOM    216  CE2 PHE A  34      52.784 -19.388 -24.591  1.00101.08      A    C  
ANISOU  216  CE2 PHE A  34    11729  14064  12612   1769   -992  -1219  A    C  
ATOM    217  CZ  PHE A  34      53.745 -20.264 -25.067  1.00103.63      A    C  
ANISOU  217  CZ  PHE A  34    12101  14378  12895   1954   -962  -1312  A    C  
ATOM    218  N   LYS A  35      57.304 -16.141 -20.562  1.00 68.27      A    N  
ANISOU  218  N   LYS A  35     6993  10051   8894   1613   -658   -464  A    N  
ATOM    219  CA  LYS A  35      58.085 -14.930 -20.365  1.00 62.39      A    C  
ANISOU  219  CA  LYS A  35     6100   9434   8172   1577   -560   -304  A    C  
ATOM    220  C   LYS A  35      58.165 -14.251 -21.721  1.00 69.59      A    C  
ANISOU  220  C   LYS A  35     6962  10542   8936   1664   -439   -298  A    C  
ATOM    221  O   LYS A  35      58.321 -14.902 -22.751  1.00 75.69      A    O  
ANISOU  221  O   LYS A  35     7776  11374   9609   1818   -407   -412  A    O  
ATOM    222  CB  LYS A  35      59.484 -15.252 -19.846  1.00 62.46      A    C  
ANISOU  222  CB  LYS A  35     6009   9438   8284   1661   -547   -261  A    C  
ATOM    223  CG  LYS A  35      60.380 -14.037 -19.588  1.00 66.29      A    C  
ANISOU  223  CG  LYS A  35     6324  10048   8814   1610   -456    -97  A    C  
ATOM    224  CD  LYS A  35      61.764 -14.470 -19.081  1.00 65.87      A    C  
ANISOU  224  CD  LYS A  35     6156   9990   8881   1702   -465    -69  A    C  
ATOM    225  CE  LYS A  35      62.753 -13.301 -18.976  1.00 71.04      A    C  
ANISOU  225  CE  LYS A  35     6619  10786   9586   1658   -368     82  A    C  
ATOM    226  NZ  LYS A  35      64.142 -13.735 -18.573  1.00 70.87      A    N1+
ANISOU  226  NZ  LYS A  35     6455  10780   9694   1760   -380    101  A    N1+
ATOM    227  N   ALA A  36      58.020 -12.940 -21.744  1.00 66.34      A    N  
ANISOU  227  N   ALA A  36     6483  10225   8499   1566   -373   -168  A    N  
ATOM    228  CA  ALA A  36      58.176 -12.241 -23.002  1.00 60.44      A    C  
ANISOU  228  CA  ALA A  36     5699   9661   7604   1644   -252   -140  A    C  
ATOM    229  C   ALA A  36      58.852 -10.889 -22.829  1.00 68.91      A    C  
ANISOU  229  C   ALA A  36     6641  10840   8703   1569   -145     40  A    C  
ATOM    230  O   ALA A  36      59.194 -10.475 -21.718  1.00 71.24      A    O  
ANISOU  230  O   ALA A  36     6870  11068   9132   1455   -173    136  A    O  
ATOM    231  CB  ALA A  36      56.864 -12.107 -23.704  1.00 51.26      A    C  
ANISOU  231  CB  ALA A  36     4650   8507   6321   1621   -299   -205  A    C  
ATOM    232  N   ARG A  37      59.049 -10.212 -23.948  1.00 65.40      A    N  
ANISOU  232  N   ARG A  37     6170  10557   8121   1631    -24     84  A    N  
ATOM    233  CA  ARG A  37      59.914  -9.059 -23.996  1.00 59.12      A    C  
ANISOU  233  CA  ARG A  37     5246   9877   7341   1584    105    247  A    C  
ATOM    234  C   ARG A  37      59.251  -8.064 -24.924  1.00 64.41      A    C  
ANISOU  234  C   ARG A  37     5973  10645   7854   1563    165    309  A    C  
ATOM    235  O   ARG A  37      58.917  -8.402 -26.051  1.00 66.31      A    O  
ANISOU  235  O   ARG A  37     6300  10963   7932   1678    193    226  A    O  
ATOM    236  CB  ARG A  37      61.266  -9.497 -24.548  1.00 62.65      A    C  
ANISOU  236  CB  ARG A  37     5581  10443   7782   1730    230    232  A    C  
ATOM    237  CG  ARG A  37      62.247  -8.386 -24.785  1.00 67.40      A    C  
ANISOU  237  CG  ARG A  37     6033  11184   8391   1692    387    392  A    C  
ATOM    238  CD  ARG A  37      63.574  -8.896 -25.350  1.00 59.66      A    C  
ANISOU  238  CD  ARG A  37     4921  10331   7417   1844    524    364  A    C  
ATOM    239  NE  ARG A  37      64.477  -7.770 -25.496  1.00 62.80      A    N  
ANISOU  239  NE  ARG A  37     5163  10857   7842   1775    676    530  A    N  
ATOM    240  CZ  ARG A  37      64.316  -6.837 -26.425  1.00 64.38      A    C  
ANISOU  240  CZ  ARG A  37     5395  11175   7890   1751    804    618  A    C  
ATOM    241  NH1 ARG A  37      63.303  -6.941 -27.276  1.00 64.37      A    N1+
ANISOU  241  NH1 ARG A  37     5573  11185   7700   1806    784    550  A    N1+
ATOM    242  NH2 ARG A  37      65.156  -5.813 -26.505  1.00 57.13      A    N  
ANISOU  242  NH2 ARG A  37     4337  10359   7011   1669    944    776  A    N  
ATOM    243  N   HIS A  38      59.023  -6.847 -24.449  1.00 63.02      A    N  
ANISOU  243  N   HIS A  38     5768  10455   7723   1419    174    451  A    N  
ATOM    244  CA  HIS A  38      58.433  -5.833 -25.309  1.00 63.62      A    C  
ANISOU  244  CA  HIS A  38     5904  10613   7655   1403    226    527  A    C  
ATOM    245  C   HIS A  38      59.406  -5.521 -26.452  1.00 65.14      A    C  
ANISOU  245  C   HIS A  38     6046  10983   7719   1504    403    586  A    C  
ATOM    246  O   HIS A  38      60.564  -5.192 -26.215  1.00 67.06      A    O  
ANISOU  246  O   HIS A  38     6154  11284   8042   1481    511    679  A    O  
ATOM    247  CB  HIS A  38      58.100  -4.581 -24.500  1.00 63.94      A    C  
ANISOU  247  CB  HIS A  38     5922  10587   7785   1234    205    670  A    C  
ATOM    248  CG  HIS A  38      57.354  -3.549 -25.276  1.00 66.21      A    C  
ANISOU  248  CG  HIS A  38     6288  10927   7942   1220    230    746  A    C  
ATOM    249  CD2 HIS A  38      56.049  -3.180 -25.251  1.00 58.14      A    C  
ANISOU  249  CD2 HIS A  38     5360   9839   6891   1179    129    728  A    C  
ATOM    250  ND1 HIS A  38      57.956  -2.763 -26.239  1.00 68.87      A    N  
ANISOU  250  ND1 HIS A  38     6610  11399   8157   1255    372    858  A    N  
ATOM    251  CE1 HIS A  38      57.053  -1.955 -26.767  1.00 70.68      A    C  
ANISOU  251  CE1 HIS A  38     6939  11636   8282   1241    345    911  A    C  
ATOM    252  NE2 HIS A  38      55.889  -2.186 -26.185  1.00 56.39      A    N  
ANISOU  252  NE2 HIS A  38     5186   9707   6532   1200    195    830  A    N  
ATOM    253  N   ARG A  39      58.947  -5.637 -27.691  1.00 70.67      A    N  
ANISOU  253  N   ARG A  39     6856  11775   8219   1613    434    531  A    N  
ATOM    254  CA  ARG A  39      59.850  -5.541 -28.846  1.00 70.58      A    C  
ANISOU  254  CA  ARG A  39     6823  11937   8058   1728    615    563  A    C  
ATOM    255  C   ARG A  39      60.608  -4.224 -28.968  1.00 69.95      A    C  
ANISOU  255  C   ARG A  39     6651  11947   7980   1639    770    766  A    C  
ATOM    256  O   ARG A  39      61.611  -4.151 -29.681  1.00 74.34      A    O  
ANISOU  256  O   ARG A  39     7140  12644   8464   1708    948    810  A    O  
ATOM    257  CB  ARG A  39      59.104  -5.824 -30.153  1.00 71.00      A    C  
ANISOU  257  CB  ARG A  39     7043  12064   7868   1851    604    471  A    C  
ATOM    258  CG  ARG A  39      58.752  -7.271 -30.322  1.00 78.54      A    C  
ANISOU  258  CG  ARG A  39     8075  12969   8797   1973    503    257  A    C  
ATOM    259  CD  ARG A  39      58.181  -7.574 -31.689  1.00 93.18      A    C  
ANISOU  259  CD  ARG A  39    10096  14911  10397   2104    499    159  A    C  
ATOM    260  NE  ARG A  39      57.654  -8.931 -31.684  1.00103.10      A    N  
ANISOU  260  NE  ARG A  39    11438  16079  11658   2188    362    -52  A    N  
ATOM    261  CZ  ARG A  39      58.386 -10.011 -31.924  1.00112.01      A    C  
ANISOU  261  CZ  ARG A  39    12558  17225  12776   2322    416   -180  A    C  
ATOM    262  NH1 ARG A  39      59.674  -9.887 -32.222  1.00113.04      A    N1+
ANISOU  262  NH1 ARG A  39    12582  17475  12891   2396    613   -120  A    N1+
ATOM    263  NH2 ARG A  39      57.827 -11.213 -31.876  1.00115.76      A    N  
ANISOU  263  NH2 ARG A  39    13127  17594  13263   2383    276   -369  A    N  
ATOM    264  N   LYS A  40      60.132  -3.194 -28.274  1.00 70.43      A    N  
ANISOU  264  N   LYS A  40     6711  11923   8126   1484    710    886  A    N  
ATOM    265  CA  LYS A  40      60.715  -1.863 -28.391  1.00 66.67      A    C  
ANISOU  265  CA  LYS A  40     6176  11506   7651   1382    840   1083  A    C  
ATOM    266  C   LYS A  40      61.582  -1.453 -27.200  1.00 68.83      A    C  
ANISOU  266  C   LYS A  40     6283  11720   8151   1244    854   1177  A    C  
ATOM    267  O   LYS A  40      62.572  -0.741 -27.373  1.00 73.66      A    O  
ANISOU  267  O   LYS A  40     6786  12415   8788   1189   1001   1309  A    O  
ATOM    268  CB  LYS A  40      59.624  -0.820 -28.653  1.00 65.59      A    C  
ANISOU  268  CB  LYS A  40     6175  11325   7423   1317    779   1169  A    C  
ATOM    269  CG  LYS A  40      59.134  -0.772 -30.103  1.00 64.14      A    C  
ANISOU  269  CG  LYS A  40     6142  11251   6978   1440    823   1152  A    C  
ATOM    270  CD  LYS A  40      58.219   0.411 -30.348  1.00 76.06      A    C  
ANISOU  270  CD  LYS A  40     7768  12718   8411   1377    770   1269  A    C  
ATOM    271  CE  LYS A  40      57.710   0.450 -31.789  1.00 90.58      A    C  
ANISOU  271  CE  LYS A  40     9775  14664   9979   1505    789   1255  A    C  
ATOM    272  NZ  LYS A  40      58.759   0.856 -32.772  1.00 98.75      A    N1+
ANISOU  272  NZ  LYS A  40    10810  15852  10859   1543   1010   1369  A    N1+
ATOM    273  N   THR A  41      61.231  -1.931 -26.008  1.00 70.57      A    N  
ANISOU  273  N   THR A  41     6485  11797   8532   1185    701   1106  A    N  
ATOM    274  CA  THR A  41      61.842  -1.459 -24.766  1.00 67.79      A    C  
ANISOU  274  CA  THR A  41     6012  11362   8383   1039    671   1192  A    C  
ATOM    275  C   THR A  41      62.537  -2.544 -23.962  1.00 66.49      A    C  
ANISOU  275  C   THR A  41     5740  11157   8366   1076    612   1098  A    C  
ATOM    276  O   THR A  41      63.228  -2.258 -22.986  1.00 80.38      A    O  
ANISOU  276  O   THR A  41     7385  12866  10289    971    586   1163  A    O  
ATOM    277  CB  THR A  41      60.775  -0.880 -23.822  1.00 65.33      A    C  
ANISOU  277  CB  THR A  41     5791  10890   8141    909    529   1214  A    C  
ATOM    278  CG2 THR A  41      59.822   0.021 -24.574  1.00 54.34      A    C  
ANISOU  278  CG2 THR A  41     4528   9511   6607    901    542   1275  A    C  
ATOM    279  OG1 THR A  41      60.049  -1.954 -23.208  1.00 61.95      A    O  
ANISOU  279  OG1 THR A  41     5424  10356   7760    945    384   1062  A    O  
ATOM    280  N   GLY A  42      62.319  -3.791 -24.342  1.00 62.17      A    N  
ANISOU  280  N   GLY A  42     5242  10618   7761   1223    574    941  A    N  
ATOM    281  CA  GLY A  42      62.890  -4.909 -23.620  1.00 61.37      A    C  
ANISOU  281  CA  GLY A  42     5067  10460   7791   1278    502    844  A    C  
ATOM    282  C   GLY A  42      62.182  -5.217 -22.317  1.00 60.61      A    C  
ANISOU  282  C   GLY A  42     5037  10178   7815   1180    320    800  A    C  
ATOM    283  O   GLY A  42      62.522  -6.184 -21.634  1.00 61.17      A    O  
ANISOU  283  O   GLY A  42     5080  10174   7989   1220    236    721  A    O  
ATOM    284  N   GLN A  43      61.184  -4.417 -21.967  1.00 54.20      A    N  
ANISOU  284  N   GLN A  43     4320   9287   6987   1058    262    852  A    N  
ATOM    285  CA  GLN A  43      60.432  -4.685 -20.742  1.00 57.48      A    C  
ANISOU  285  CA  GLN A  43     4809   9529   7501    961    109    809  A    C  
ATOM    286  C   GLN A  43      59.934  -6.120 -20.688  1.00 59.80      A    C  
ANISOU  286  C   GLN A  43     5185   9750   7786   1059     13    643  A    C  
ATOM    287  O   GLN A  43      59.254  -6.560 -21.607  1.00 67.72      A    O  
ANISOU  287  O   GLN A  43     6273  10792   8665   1153     17    552  A    O  
ATOM    288  CB  GLN A  43      59.258  -3.718 -20.600  1.00 46.66      A    C  
ANISOU  288  CB  GLN A  43     3539   8098   6092    852     76    860  A    C  
ATOM    289  CG  GLN A  43      58.494  -3.909 -19.317  1.00 65.04      A    C  
ANISOU  289  CG  GLN A  43     5937  10256   8519    744    -53    821  A    C  
ATOM    290  CD  GLN A  43      57.065  -3.434 -19.419  1.00 78.79      A    C  
ANISOU  290  CD  GLN A  43     7789  11945  10204    699    -94    802  A    C  
ATOM    291  NE2 GLN A  43      56.357  -3.442 -18.290  1.00 74.47      A    N  
ANISOU  291  NE2 GLN A  43     7299  11256   9741    592   -180    780  A    N  
ATOM    292  OE1 GLN A  43      56.595  -3.070 -20.504  1.00 79.55      A    O  
ANISOU  292  OE1 GLN A  43     7918  12127  10179    764    -49    806  A    O  
ATOM    293  N   LYS A  44      60.278  -6.848 -19.625  1.00 61.58      A    N  
ANISOU  293  N   LYS A  44     5395   9864   8137   1034    -81    605  A    N  
ATOM    294  CA  LYS A  44      59.808  -8.230 -19.465  1.00 61.13      A    C  
ANISOU  294  CA  LYS A  44     5432   9709   8085   1111   -181    455  A    C  
ATOM    295  C   LYS A  44      58.380  -8.294 -18.913  1.00 65.19      A    C  
ANISOU  295  C   LYS A  44     6085  10089   8596   1008   -281    406  A    C  
ATOM    296  O   LYS A  44      58.017  -7.536 -18.003  1.00 63.26      A    O  
ANISOU  296  O   LYS A  44     5854   9769   8412    862   -312    485  A    O  
ATOM    297  CB  LYS A  44      60.710  -9.054 -18.541  1.00 53.22      A    C  
ANISOU  297  CB  LYS A  44     4379   8625   7215   1134   -253    435  A    C  
ATOM    298  CG  LYS A  44      62.185  -9.066 -18.850  1.00 63.93      A    C  
ANISOU  298  CG  LYS A  44     5569  10101   8622   1229   -171    480  A    C  
ATOM    299  CD  LYS A  44      62.542  -9.331 -20.305  1.00 61.02      A    C  
ANISOU  299  CD  LYS A  44     5159   9890   8135   1397    -40    424  A    C  
ATOM    300  CE  LYS A  44      63.919  -8.746 -20.572  1.00 62.98      A    C  
ANISOU  300  CE  LYS A  44     5209  10285   8437   1425     86    525  A    C  
ATOM    301  NZ  LYS A  44      64.600  -9.307 -21.759  1.00 81.40      A    N1+
ANISOU  301  NZ  LYS A  44     7476  12762  10691   1616    216    455  A    N1+
ATOM    302  N   VAL A  45      57.598  -9.227 -19.456  1.00 64.03      A    N  
ANISOU  302  N   VAL A  45     6035   9911   8382   1085   -329    270  A    N  
ATOM    303  CA  VAL A  45      56.212  -9.444 -19.061  1.00 67.10      A    C  
ANISOU  303  CA  VAL A  45     6538  10184   8773    998   -418    204  A    C  
ATOM    304  C   VAL A  45      55.880 -10.940 -18.967  1.00 65.27      A    C  
ANISOU  304  C   VAL A  45     6399   9843   8559   1056   -510     54  A    C  
ATOM    305  O   VAL A  45      56.572 -11.772 -19.528  1.00 66.57      A    O  
ANISOU  305  O   VAL A  45     6556  10042   8697   1195   -499    -17  A    O  
ATOM    306  CB  VAL A  45      55.229  -8.792 -20.074  1.00 60.82      A    C  
ANISOU  306  CB  VAL A  45     5775   9474   7858   1009   -389    194  A    C  
ATOM    307  CG1 VAL A  45      55.388  -7.270 -20.103  1.00 52.71      A    C  
ANISOU  307  CG1 VAL A  45     4686   8524   6819    938   -309    347  A    C  
ATOM    308  CG2 VAL A  45      55.427  -9.380 -21.453  1.00 58.91      A    C  
ANISOU  308  CG2 VAL A  45     5552   9346   7486   1176   -353    104  A    C  
ATOM    309  N   ALA A  46      54.811 -11.273 -18.257  1.00 65.36      A    N  
ANISOU  309  N   ALA A  46     6499   9718   8617    947   -594      6  A    N  
ATOM    310  CA  ALA A  46      54.262 -12.623 -18.286  1.00 60.03      A    C  
ANISOU  310  CA  ALA A  46     5927   8931   7949    980   -681   -139  A    C  
ATOM    311  C   ALA A  46      52.990 -12.624 -19.140  1.00 58.93      A    C  
ANISOU  311  C   ALA A  46     5837   8824   7729    977   -706   -229  A    C  
ATOM    312  O   ALA A  46      52.099 -11.821 -18.921  1.00 68.05      A    O  
ANISOU  312  O   ALA A  46     6982   9981   8893    871   -705   -186  A    O  
ATOM    313  CB  ALA A  46      53.957 -13.098 -16.876  1.00 47.63      A    C  
ANISOU  313  CB  ALA A  46     4428   7178   6491    848   -756   -132  A    C  
ATOM    314  N   LEU A  47      52.925 -13.509 -20.125  1.00 55.73      A    N  
ANISOU  314  N   LEU A  47     5484   8445   7247   1102   -735   -358  A    N  
ATOM    315  CA  LEU A  47      51.745 -13.648 -20.972  1.00 56.77      A    C  
ANISOU  315  CA  LEU A  47     5667   8601   7300   1106   -786   -461  A    C  
ATOM    316  C   LEU A  47      51.029 -14.924 -20.581  1.00 60.07      A    C  
ANISOU  316  C   LEU A  47     6187   8853   7783   1057   -895   -597  A    C  
ATOM    317  O   LEU A  47      51.594 -16.010 -20.675  1.00 63.83      A    O  
ANISOU  317  O   LEU A  47     6725   9263   8265   1145   -926   -681  A    O  
ATOM    318  CB  LEU A  47      52.141 -13.757 -22.442  1.00 61.84      A    C  
ANISOU  318  CB  LEU A  47     6319   9390   7788   1280   -749   -523  A    C  
ATOM    319  CG  LEU A  47      52.953 -12.645 -23.080  1.00 60.73      A    C  
ANISOU  319  CG  LEU A  47     6094   9424   7556   1351   -625   -401  A    C  
ATOM    320  CD1 LEU A  47      53.175 -12.962 -24.546  1.00 60.89      A    C  
ANISOU  320  CD1 LEU A  47     6159   9571   7404   1519   -593   -489  A    C  
ATOM    321  CD2 LEU A  47      52.225 -11.341 -22.921  1.00 61.46      A    C  
ANISOU  321  CD2 LEU A  47     6144   9559   7651   1240   -611   -290  A    C  
ATOM    322  N   LYS A  48      49.783 -14.796 -20.155  1.00 61.32      A    N  
ANISOU  322  N   LYS A  48     6360   8941   7996    916   -949   -618  A    N  
ATOM    323  CA  LYS A  48      48.988 -15.933 -19.707  1.00 63.94      A    C  
ANISOU  323  CA  LYS A  48     6782   9107   8404    832  -1043   -734  A    C  
ATOM    324  C   LYS A  48      47.741 -16.044 -20.585  1.00 72.59      A    C  
ANISOU  324  C   LYS A  48     7888  10240   9454    818  -1116   -849  A    C  
ATOM    325  O   LYS A  48      46.791 -15.275 -20.425  1.00 75.86      A    O  
ANISOU  325  O   LYS A  48     8239  10684   9899    719  -1118   -814  A    O  
ATOM    326  CB  LYS A  48      48.593 -15.714 -18.252  1.00 61.13      A    C  
ANISOU  326  CB  LYS A  48     6424   8626   8175    652  -1033   -653  A    C  
ATOM    327  CG  LYS A  48      48.129 -16.942 -17.504  1.00 75.32      A    C  
ANISOU  327  CG  LYS A  48     8329  10226  10063    555  -1105   -735  A    C  
ATOM    328  CD  LYS A  48      47.522 -16.525 -16.168  1.00 85.02      A    C  
ANISOU  328  CD  LYS A  48     9554  11359  11391    364  -1074   -652  A    C  
ATOM    329  CE  LYS A  48      46.898 -17.696 -15.439  1.00 96.13      A    C  
ANISOU  329  CE  LYS A  48    11074  12569  12882    241  -1133   -726  A    C  
ATOM    330  NZ  LYS A  48      45.815 -17.227 -14.534  1.00 97.23      A    N1+
ANISOU  330  NZ  LYS A  48    11189  12654  13099     49  -1092   -686  A    N1+
ATOM    331  N   LYS A  49      47.753 -16.986 -21.522  1.00 73.37      A    N  
ANISOU  331  N   LYS A  49     8064  10336   9480    925  -1183   -991  A    N  
ATOM    332  CA  LYS A  49      46.646 -17.154 -22.464  1.00 74.61      A    C  
ANISOU  332  CA  LYS A  49     8237  10532   9578    925  -1275  -1114  A    C  
ATOM    333  C   LYS A  49      45.365 -17.593 -21.759  1.00 71.07      A    C  
ANISOU  333  C   LYS A  49     7793   9947   9265    740  -1355  -1175  A    C  
ATOM    334  O   LYS A  49      45.400 -18.425 -20.850  1.00 74.39      A    O  
ANISOU  334  O   LYS A  49     8275  10200   9791    650  -1369  -1194  A    O  
ATOM    335  CB  LYS A  49      47.030 -18.178 -23.534  1.00 89.69      A    C  
ANISOU  335  CB  LYS A  49    10253  12447  11378   1078  -1332  -1265  A    C  
ATOM    336  CG  LYS A  49      45.997 -18.406 -24.623  1.00 98.31      A    C  
ANISOU  336  CG  LYS A  49    11381  13586  12387   1096  -1447  -1406  A    C  
ATOM    337  CD  LYS A  49      46.190 -19.783 -25.254  1.00110.32      A    C  
ANISOU  337  CD  LYS A  49    13042  15019  13854   1189  -1530  -1586  A    C  
ATOM    338  CE  LYS A  49      45.567 -19.881 -26.637  1.00117.55      A    C  
ANISOU  338  CE  LYS A  49    14011  16033  14620   1272  -1630  -1721  A    C  
ATOM    339  NZ  LYS A  49      46.366 -19.143 -27.661  1.00120.50      A    N1+
ANISOU  339  NZ  LYS A  49    14383  16604  14799   1454  -1542  -1669  A    N1+
ATOM    340  N   VAL A  50      44.239 -17.021 -22.178  1.00 75.47      A    N  
ANISOU  340  N   VAL A  50     8280  10575   9820    685  -1404  -1200  A    N  
ATOM    341  CA  VAL A  50      42.926 -17.421 -21.666  1.00 75.81      A    C  
ANISOU  341  CA  VAL A  50     8299  10511   9996    512  -1478  -1272  A    C  
ATOM    342  C   VAL A  50      42.430 -18.710 -22.326  1.00 84.95      A    C  
ANISOU  342  C   VAL A  50     9549  11585  11145    516  -1611  -1460  A    C  
ATOM    343  O   VAL A  50      42.229 -18.770 -23.551  1.00 81.81      A    O  
ANISOU  343  O   VAL A  50     9171  11284  10629    625  -1695  -1556  A    O  
ATOM    344  CB  VAL A  50      41.866 -16.306 -21.822  1.00 62.60      A    C  
ANISOU  344  CB  VAL A  50     6492   8944   8348    455  -1487  -1231  A    C  
ATOM    345  CG1 VAL A  50      40.483 -16.832 -21.495  1.00 46.74      A    C  
ANISOU  345  CG1 VAL A  50     4439   6843   6477    291  -1571  -1333  A    C  
ATOM    346  CG2 VAL A  50      42.188 -15.159 -20.907  1.00 62.58      A    C  
ANISOU  346  CG2 VAL A  50     6415   8972   8392    408  -1360  -1059  A    C  
ATOM    347  N   LEU A  51      42.234 -19.725 -21.485  1.00 88.38      A    N  
ANISOU  347  N   LEU A  51    10052  11829  11699    391  -1633  -1508  A    N  
ATOM    348  CA  LEU A  51      41.873 -21.074 -21.903  1.00 97.61      A    C  
ANISOU  348  CA  LEU A  51    11334  12871  12884    372  -1754  -1681  A    C  
ATOM    349  C   LEU A  51      40.475 -21.194 -22.490  1.00102.76      A    C  
ANISOU  349  C   LEU A  51    11925  13543  13577    279  -1878  -1805  A    C  
ATOM    350  O   LEU A  51      39.512 -20.672 -21.928  1.00105.22      A    O  
ANISOU  350  O   LEU A  51    12113  13861  14004    129  -1864  -1764  A    O  
ATOM    351  CB  LEU A  51      41.973 -22.010 -20.708  1.00 99.05      A    C  
ANISOU  351  CB  LEU A  51    11606  12832  13198    237  -1734  -1672  A    C  
ATOM    352  CG  LEU A  51      43.376 -22.154 -20.138  1.00 98.19      A    C  
ANISOU  352  CG  LEU A  51    11575  12673  13058    336  -1650  -1575  A    C  
ATOM    353  CD1 LEU A  51      43.329 -22.992 -18.868  1.00 94.61      A    C  
ANISOU  353  CD1 LEU A  51    11219  11995  12735    184  -1642  -1549  A    C  
ATOM    354  CD2 LEU A  51      44.293 -22.768 -21.191  1.00 96.11      A    C  
ANISOU  354  CD2 LEU A  51    11411  12440  12666    550  -1693  -1671  A    C  
ATOM    355  N   MET A  52      40.363 -21.921 -23.598  1.00101.01      A    N  
ANISOU  355  N   MET A  52    11790  13325  13265    367  -2004  -1965  A    N  
ATOM    356  CA  MET A  52      39.074 -22.121 -24.245  1.00106.66      A    C  
ANISOU  356  CA  MET A  52    12453  14057  14014    285  -2153  -2100  A    C  
ATOM    357  C   MET A  52      38.747 -23.601 -24.511  1.00119.32      A    C  
ANISOU  357  C   MET A  52    14193  15485  15658    226  -2286  -2286  A    C  
ATOM    358  O   MET A  52      38.153 -23.939 -25.535  1.00119.30      A    O  
ANISOU  358  O   MET A  52    14214  15519  15595    255  -2437  -2437  A    O  
ATOM    359  CB  MET A  52      39.018 -21.318 -25.546  1.00107.73      A    C  
ANISOU  359  CB  MET A  52    12551  14405  13978    448  -2213  -2120  A    C  
ATOM    360  CG  MET A  52      39.250 -19.823 -25.371  1.00103.42      A    C  
ANISOU  360  CG  MET A  52    11878  14023  13395    501  -2096  -1940  A    C  
ATOM    361  SD  MET A  52      37.736 -18.918 -24.971  1.00134.58      A    S  
ANISOU  361  SD  MET A  52    15613  18025  17496    340  -2134  -1901  A    S  
ATOM    362  CE  MET A  52      38.298 -17.227 -25.176  1.00126.58      A    C  
ANISOU  362  CE  MET A  52    14519  17207  16368    478  -2017  -1711  A    C  
ATOM    363  N   GLU A  53      39.134 -24.479 -23.590  1.00134.07      A    N  
ANISOU  363  N   GLU A  53    16163  17155  17623    142  -2240  -2276  A    N  
ATOM    364  CA  GLU A  53      38.753 -25.887 -23.675  1.00150.09      A    C  
ANISOU  364  CA  GLU A  53    18327  18982  19718     54  -2360  -2439  A    C  
ATOM    365  C   GLU A  53      37.294 -26.052 -23.273  1.00150.29      A    C  
ANISOU  365  C   GLU A  53    18241  18940  19922   -195  -2430  -2490  A    C  
ATOM    366  O   GLU A  53      36.906 -25.684 -22.162  1.00146.92      A    O  
ANISOU  366  O   GLU A  53    17717  18473  19632   -357  -2326  -2374  A    O  
ATOM    367  CB  GLU A  53      39.611 -26.750 -22.748  1.00164.47      A    C  
ANISOU  367  CB  GLU A  53    20300  20598  21595     39  -2290  -2395  A    C  
ATOM    368  CG  GLU A  53      41.092 -26.788 -23.067  1.00175.10      A    C  
ANISOU  368  CG  GLU A  53    21752  21982  22798    281  -2227  -2360  A    C  
ATOM    369  CD  GLU A  53      41.877 -27.550 -22.010  1.00182.59      A    C  
ANISOU  369  CD  GLU A  53    22827  22725  23823    259  -2167  -2297  A    C  
ATOM    370  OE1 GLU A  53      41.245 -28.075 -21.067  1.00183.02      A    O  
ANISOU  370  OE1 GLU A  53    22910  22601  24027     50  -2176  -2281  A    O  
ATOM    371  OE2 GLU A  53      43.120 -27.621 -22.118  1.00185.53      A    O1-
ANISOU  371  OE2 GLU A  53    23268  23115  24109    450  -2112  -2260  A    O1-
ATOM    372  N   ASN A  54      36.491 -26.615 -24.171  1.00154.10      A    N  
ANISOU  372  N   ASN A  54    18738  19410  20403   -229  -2603  -2668  A    N  
ATOM    373  CA  ASN A  54      35.076 -26.849 -23.896  1.00155.63      A    C  
ANISOU  373  CA  ASN A  54    18809  19543  20780   -470  -2686  -2737  A    C  
ATOM    374  C   ASN A  54      34.340 -25.588 -23.440  1.00146.24      A    C  
ANISOU  374  C   ASN A  54    17375  18512  19677   -550  -2605  -2614  A    C  
ATOM    375  O   ASN A  54      33.585 -25.617 -22.465  1.00144.51      A    O  
ANISOU  375  O   ASN A  54    17051  18213  19643   -765  -2540  -2568  A    O  
ATOM    376  CB  ASN A  54      34.899 -27.965 -22.856  1.00157.86      A    C  
ANISOU  376  CB  ASN A  54    19190  19560  21227   -677  -2656  -2750  A    C  
ATOM    377  CG  ASN A  54      35.140 -29.349 -23.433  1.00155.42      A    C  
ANISOU  377  CG  ASN A  54    19103  19067  20883   -651  -2794  -2925  A    C  
ATOM    378  ND2 ASN A  54      36.411 -29.717 -23.587  1.00149.84      A    N  
ANISOU  378  ND2 ASN A  54    18579  18309  20042   -455  -2755  -2914  A    N  
ATOM    379  OD1 ASN A  54      34.194 -30.079 -23.739  1.00155.75      A    O  
ANISOU  379  OD1 ASN A  54    19145  19010  21023   -805  -2937  -3074  A    O  
ATOM    380  N   GLU A  55      34.563 -24.484 -24.146  1.00133.91      A    N  
ANISOU  380  N   GLU A  55    15731  17169  17981   -376  -2602  -2560  A    N  
ATOM    381  CA  GLU A  55      33.894 -23.234 -23.816  1.00119.51      A    C  
ANISOU  381  CA  GLU A  55    13685  15495  16229   -422  -2538  -2449  A    C  
ATOM    382  C   GLU A  55      32.781 -22.929 -24.816  1.00112.23      A    C  
ANISOU  382  C   GLU A  55    12627  14700  15315   -422  -2719  -2565  A    C  
ATOM    383  O   GLU A  55      33.028 -22.464 -25.930  1.00105.10      A    O  
ANISOU  383  O   GLU A  55    11751  13946  14235   -236  -2809  -2595  A    O  
ATOM    384  CB  GLU A  55      34.899 -22.088 -23.718  1.00116.79      A    C  
ANISOU  384  CB  GLU A  55    13335  15290  15751   -248  -2393  -2277  A    C  
ATOM    385  CG  GLU A  55      35.807 -22.178 -22.494  1.00119.37      A    C  
ANISOU  385  CG  GLU A  55    13739  15502  16113   -285  -2212  -2140  A    C  
ATOM    386  CD  GLU A  55      35.034 -22.213 -21.182  1.00126.83      A    C  
ANISOU  386  CD  GLU A  55    14588  16337  17264   -522  -2119  -2082  A    C  
ATOM    387  OE1 GLU A  55      33.869 -21.762 -21.161  1.00132.70      A    O  
ANISOU  387  OE1 GLU A  55    15153  17145  18123   -631  -2150  -2106  A    O  
ATOM    388  OE2 GLU A  55      35.593 -22.687 -20.170  1.00127.78      A    O1-
ANISOU  388  OE2 GLU A  55    14813  16310  17428   -595  -2014  -2011  A    O1-
ATOM    389  N   LYS A  56      31.550 -23.197 -24.392  1.00107.66      A    N  
ANISOU  389  N   LYS A  56    11899  14063  14944   -635  -2771  -2626  A    N  
ATOM    390  CA  LYS A  56      30.396 -23.174 -25.277  1.00104.85      A    C  
ANISOU  390  CA  LYS A  56    11410  13793  14637   -670  -2977  -2765  A    C  
ATOM    391  C   LYS A  56      29.432 -22.057 -24.892  1.00 97.10      A    C  
ANISOU  391  C   LYS A  56    10155  12942  13796   -734  -2934  -2684  A    C  
ATOM    392  O   LYS A  56      28.303 -22.000 -25.371  1.00104.79      A    O  
ANISOU  392  O   LYS A  56    10963  13980  14875   -802  -3091  -2786  A    O  
ATOM    393  CB  LYS A  56      29.701 -24.539 -25.238  1.00112.17      A    C  
ANISOU  393  CB  LYS A  56    12377  14536  15706   -871  -3103  -2935  A    C  
ATOM    394  CG  LYS A  56      30.676 -25.703 -25.444  1.00121.84      A    C  
ANISOU  394  CG  LYS A  56    13886  15594  16813   -815  -3124  -3011  A    C  
ATOM    395  CD  LYS A  56      30.063 -27.067 -25.142  1.00128.95      A    C  
ANISOU  395  CD  LYS A  56    14848  16268  17878  -1043  -3211  -3150  A    C  
ATOM    396  CE  LYS A  56      31.124 -28.167 -25.224  1.00131.78      A    C  
ANISOU  396  CE  LYS A  56    15502  16444  18126   -967  -3211  -3205  A    C  
ATOM    397  NZ  LYS A  56      30.586 -29.527 -24.927  1.00133.60      A    N1+
ANISOU  397  NZ  LYS A  56    15824  16426  18511  -1188  -3297  -3336  A    N1+
ATOM    398  N   GLU A  57      29.900 -21.164 -24.030  1.00 85.35      A    N  
ANISOU  398  N   GLU A  57     8622  11494  12314   -706  -2728  -2505  A    N  
ATOM    399  CA  GLU A  57      29.107 -20.032 -23.583  1.00 74.76      A    C  
ANISOU  399  CA  GLU A  57     7040  10267  11098   -744  -2658  -2417  A    C  
ATOM    400  C   GLU A  57      29.814 -18.714 -23.870  1.00 68.92      A    C  
ANISOU  400  C   GLU A  57     6305   9686  10194   -528  -2586  -2273  A    C  
ATOM    401  O   GLU A  57      29.699 -17.760 -23.101  1.00 65.90      A    O  
ANISOU  401  O   GLU A  57     5805   9349   9885   -544  -2437  -2143  A    O  
ATOM    402  CB  GLU A  57      28.825 -20.143 -22.087  1.00 67.95      A    C  
ANISOU  402  CB  GLU A  57     6105   9285  10428   -952  -2458  -2337  A    C  
ATOM    403  CG  GLU A  57      27.787 -21.179 -21.752  1.00 77.07      A    C  
ANISOU  403  CG  GLU A  57     7179  10311  11792  -1198  -2517  -2464  A    C  
ATOM    404  CD  GLU A  57      26.416 -20.840 -22.314  1.00 93.03      A    C  
ANISOU  404  CD  GLU A  57     8939  12449  13958  -1250  -2668  -2565  A    C  
ATOM    405  OE1 GLU A  57      26.070 -19.640 -22.340  1.00101.12      A    O  
ANISOU  405  OE1 GLU A  57     9793  13628  15001  -1158  -2634  -2489  A    O  
ATOM    406  OE2 GLU A  57      25.683 -21.773 -22.721  1.00 88.96      A    O1-
ANISOU  406  OE2 GLU A  57     8388  11867  13547  -1382  -2829  -2723  A    O1-
ATOM    407  N   GLY A  58      30.546 -18.663 -24.977  1.00 64.32      A    N  
ANISOU  407  N   GLY A  58     5868   9183   9389   -331  -2685  -2297  A    N  
ATOM    408  CA  GLY A  58      31.323 -17.485 -25.313  1.00 62.43      A    C  
ANISOU  408  CA  GLY A  58     5659   9082   8978   -132  -2610  -2156  A    C  
ATOM    409  C   GLY A  58      32.511 -17.298 -24.393  1.00 71.17      A    C  
ANISOU  409  C   GLY A  58     6875  10126  10042   -115  -2390  -2007  A    C  
ATOM    410  O   GLY A  58      33.054 -18.272 -23.857  1.00 71.15      A    O  
ANISOU  410  O   GLY A  58     6998   9976  10058   -191  -2333  -2033  A    O  
ATOM    411  N   PHE A  59      32.912 -16.041 -24.208  1.00 74.74      A    N  
ANISOU  411  N   PHE A  59     7279  10681  10438    -17  -2277  -1851  A    N  
ATOM    412  CA  PHE A  59      34.038 -15.710 -23.338  1.00 67.06      A    C  
ANISOU  412  CA  PHE A  59     6392   9663   9426      1  -2079  -1702  A    C  
ATOM    413  C   PHE A  59      33.776 -16.191 -21.918  1.00 70.03      A    C  
ANISOU  413  C   PHE A  59     6737   9885   9987   -203  -1956  -1680  A    C  
ATOM    414  O   PHE A  59      32.749 -15.868 -21.339  1.00 78.14      A    O  
ANISOU  414  O   PHE A  59     7604  10906  11179   -328  -1930  -1682  A    O  
ATOM    415  CB  PHE A  59      34.320 -14.205 -23.344  1.00 57.82      A    C  
ANISOU  415  CB  PHE A  59     5156   8620   8191    113  -1991  -1545  A    C  
ATOM    416  CG  PHE A  59      35.666 -13.856 -22.796  1.00 64.16      A    C  
ANISOU  416  CG  PHE A  59     6069   9404   8907    170  -1827  -1403  A    C  
ATOM    417  CD1 PHE A  59      36.788 -13.888 -23.607  1.00 61.99      A    C  
ANISOU  417  CD1 PHE A  59     5928   9189   8435    332  -1831  -1380  A    C  
ATOM    418  CD2 PHE A  59      35.821 -13.531 -21.458  1.00 71.18      A    C  
ANISOU  418  CD2 PHE A  59     6925  10210   9908     57  -1668  -1299  A    C  
ATOM    419  CE1 PHE A  59      38.039 -13.584 -23.099  1.00 62.99      A    C  
ANISOU  419  CE1 PHE A  59     6132   9302   8499    377  -1685  -1253  A    C  
ATOM    420  CE2 PHE A  59      37.065 -13.223 -20.945  1.00 70.71      A    C  
ANISOU  420  CE2 PHE A  59     6962  10132   9774    103  -1537  -1174  A    C  
ATOM    421  CZ  PHE A  59      38.180 -13.256 -21.772  1.00 64.34      A    C  
ANISOU  421  CZ  PHE A  59     6266   9391   8790    262  -1549  -1151  A    C  
ATOM    422  N   PRO A  60      34.714 -16.967 -21.355  1.00 68.49      A    N  
ANISOU  422  N   PRO A  60     6698   9564   9761   -231  -1879  -1659  A    N  
ATOM    423  CA  PRO A  60      34.525 -17.678 -20.087  1.00 63.22      A    C  
ANISOU  423  CA  PRO A  60     6053   8725   9242   -427  -1784  -1651  A    C  
ATOM    424  C   PRO A  60      34.226 -16.745 -18.937  1.00 67.10      A    C  
ANISOU  424  C   PRO A  60     6436   9222   9837   -520  -1623  -1524  A    C  
ATOM    425  O   PRO A  60      35.018 -15.845 -18.662  1.00 65.86      A    O  
ANISOU  425  O   PRO A  60     6303   9122   9599   -427  -1522  -1391  A    O  
ATOM    426  CB  PRO A  60      35.865 -18.360 -19.869  1.00 57.40      A    C  
ANISOU  426  CB  PRO A  60     5517   7891   8402   -364  -1737  -1617  A    C  
ATOM    427  CG  PRO A  60      36.446 -18.481 -21.232  1.00 67.80      A    C  
ANISOU  427  CG  PRO A  60     6911   9304   9546   -168  -1851  -1683  A    C  
ATOM    428  CD  PRO A  60      36.024 -17.261 -21.957  1.00 70.60      A    C  
ANISOU  428  CD  PRO A  60     7137   9846   9844    -68  -1883  -1645  A    C  
ATOM    429  N   ILE A  61      33.094 -16.974 -18.275  1.00 70.06      A    N  
ANISOU  429  N   ILE A  61     6694   9534  10390   -706  -1596  -1569  A    N  
ATOM    430  CA  ILE A  61      32.648 -16.127 -17.174  1.00 66.12      A    C  
ANISOU  430  CA  ILE A  61     6085   9039   9998   -802  -1435  -1469  A    C  
ATOM    431  C   ILE A  61      33.685 -16.078 -16.052  1.00 73.14      A    C  
ANISOU  431  C   ILE A  61     7123   9830  10837   -830  -1277  -1338  A    C  
ATOM    432  O   ILE A  61      33.829 -15.061 -15.376  1.00 79.58      A    O  
ANISOU  432  O   ILE A  61     7898  10684  11653   -820  -1151  -1225  A    O  
ATOM    433  CB  ILE A  61      31.269 -16.574 -16.632  1.00 69.35      A    C  
ANISOU  433  CB  ILE A  61     6349   9387  10615  -1014  -1417  -1552  A    C  
ATOM    434  CG1 ILE A  61      30.688 -15.539 -15.675  1.00 68.51      A    C  
ANISOU  434  CG1 ILE A  61     6100   9318  10612  -1080  -1252  -1465  A    C  
ATOM    435  CG2 ILE A  61      31.354 -17.915 -15.934  1.00 75.35      A    C  
ANISOU  435  CG2 ILE A  61     7243   9955  11433  -1190  -1386  -1592  A    C  
ATOM    436  CD1 ILE A  61      29.314 -15.924 -15.178  1.00 66.11      A    C  
ANISOU  436  CD1 ILE A  61     5626   8973  10519  -1282  -1215  -1548  A    C  
ATOM    437  N   THR A  62      34.424 -17.164 -15.863  1.00 69.30      A    N  
ANISOU  437  N   THR A  62     6814   9212  10304   -856  -1296  -1356  A    N  
ATOM    438  CA  THR A  62      35.436 -17.182 -14.812  1.00 68.06      A    C  
ANISOU  438  CA  THR A  62     6803   8959  10099   -876  -1173  -1235  A    C  
ATOM    439  C   THR A  62      36.600 -16.271 -15.152  1.00 66.21      A    C  
ANISOU  439  C   THR A  62     6606   8832   9718   -685  -1153  -1130  A    C  
ATOM    440  O   THR A  62      37.194 -15.679 -14.262  1.00 68.69      A    O  
ANISOU  440  O   THR A  62     6963   9126  10011   -697  -1038  -1008  A    O  
ATOM    441  CB  THR A  62      35.962 -18.594 -14.517  1.00 70.34      A    C  
ANISOU  441  CB  THR A  62     7279   9069  10380   -939  -1210  -1277  A    C  
ATOM    442  CG2 THR A  62      34.819 -19.501 -14.075  1.00 66.09      A    C  
ANISOU  442  CG2 THR A  62     6714   8403   9993  -1157  -1213  -1367  A    C  
ATOM    443  OG1 THR A  62      36.583 -19.129 -15.692  1.00 73.05      A    O  
ANISOU  443  OG1 THR A  62     7694   9443  10618   -781  -1347  -1356  A    O  
ATOM    444  N   ALA A  63      36.914 -16.153 -16.441  1.00 70.95      A    N  
ANISOU  444  N   ALA A  63     7194   9547  10217   -518  -1264  -1179  A    N  
ATOM    445  CA  ALA A  63      37.992 -15.273 -16.898  1.00 63.14      A    C  
ANISOU  445  CA  ALA A  63     6229   8672   9089   -339  -1240  -1080  A    C  
ATOM    446  C   ALA A  63      37.589 -13.814 -16.770  1.00 72.48      A    C  
ANISOU  446  C   ALA A  63     7281   9971  10289   -318  -1170   -990  A    C  
ATOM    447  O   ALA A  63      38.432 -12.962 -16.488  1.00 70.94      A    O  
ANISOU  447  O   ALA A  63     7111   9817  10026   -249  -1089   -867  A    O  
ATOM    448  CB  ALA A  63      38.384 -15.586 -18.328  1.00 56.56      A    C  
ANISOU  448  CB  ALA A  63     5432   7928   8129   -173  -1363  -1160  A    C  
ATOM    449  N   LEU A  64      36.305 -13.525 -16.978  1.00 67.92      A    N  
ANISOU  449  N   LEU A  64     6560   9440   9808   -374  -1207  -1054  A    N  
ATOM    450  CA  LEU A  64      35.802 -12.180 -16.722  1.00 72.68      A    C  
ANISOU  450  CA  LEU A  64     7035  10126  10452   -360  -1135   -976  A    C  
ATOM    451  C   LEU A  64      35.994 -11.794 -15.260  1.00 71.96      A    C  
ANISOU  451  C   LEU A  64     6975   9945  10422   -476   -970   -876  A    C  
ATOM    452  O   LEU A  64      36.452 -10.695 -14.964  1.00 70.97      A    O  
ANISOU  452  O   LEU A  64     6846   9865  10254   -418   -891   -764  A    O  
ATOM    453  CB  LEU A  64      34.328 -12.064 -17.088  1.00 64.02      A    C  
ANISOU  453  CB  LEU A  64     5765   9081   9479   -409  -1205  -1074  A    C  
ATOM    454  CG  LEU A  64      34.069 -12.097 -18.582  1.00 59.78      A    C  
ANISOU  454  CG  LEU A  64     5188   8661   8866   -273  -1382  -1157  A    C  
ATOM    455  CD1 LEU A  64      32.593 -11.992 -18.823  1.00 63.70      A    C  
ANISOU  455  CD1 LEU A  64     5496   9201   9507   -332  -1461  -1253  A    C  
ATOM    456  CD2 LEU A  64      34.824 -10.985 -19.278  1.00 55.63      A    C  
ANISOU  456  CD2 LEU A  64     4692   8255   8188    -88  -1383  -1052  A    C  
ATOM    457  N   ARG A  65      35.629 -12.707 -14.361  1.00 68.81      A    N  
ANISOU  457  N   ARG A  65     6616   9412  10116   -643   -922   -917  A    N  
ATOM    458  CA  ARG A  65      35.774 -12.520 -12.919  1.00 66.62      A    C  
ANISOU  458  CA  ARG A  65     6399   9033   9881   -769   -768   -832  A    C  
ATOM    459  C   ARG A  65      37.225 -12.191 -12.579  1.00 71.10      A    C  
ANISOU  459  C   ARG A  65     7108   9584  10325   -689   -729   -713  A    C  
ATOM    460  O   ARG A  65      37.523 -11.147 -11.996  1.00 69.78      A    O  
ANISOU  460  O   ARG A  65     6938   9440  10137   -675   -637   -612  A    O  
ATOM    461  CB  ARG A  65      35.341 -13.802 -12.201  1.00 72.05      A    C  
ANISOU  461  CB  ARG A  65     7155   9569  10654   -950   -747   -896  A    C  
ATOM    462  CG  ARG A  65      35.004 -13.653 -10.722  1.00 79.26      A    C  
ANISOU  462  CG  ARG A  65     8100  10382  11634  -1117   -580   -835  A    C  
ATOM    463  CD  ARG A  65      34.808 -15.023 -10.059  1.00 90.34      A    C  
ANISOU  463  CD  ARG A  65     9618  11616  13089  -1290   -565   -879  A    C  
ATOM    464  NE  ARG A  65      33.906 -15.895 -10.817  1.00109.49      A    N  
ANISOU  464  NE  ARG A  65    11956  14037  15610  -1348   -668  -1015  A    N  
ATOM    465  CZ  ARG A  65      32.620 -16.100 -10.521  1.00119.81      A    C  
ANISOU  465  CZ  ARG A  65    13131  15325  17065  -1506   -614  -1084  A    C  
ATOM    466  NH1 ARG A  65      32.065 -15.501  -9.469  1.00122.72      A    N1+
ANISOU  466  NH1 ARG A  65    13445  15683  17499  -1617   -441  -1031  A    N1+
ATOM    467  NH2 ARG A  65      31.884 -16.910 -11.277  1.00116.29      A    N  
ANISOU  467  NH2 ARG A  65    12606  14874  16706  -1557   -731  -1212  A    N  
ATOM    468  N   GLU A  66      38.127 -13.091 -12.968  1.00 68.89      A    N  
ANISOU  468  N   GLU A  66     6946   9260   9968   -632   -806   -731  A    N  
ATOM    469  CA  GLU A  66      39.559 -12.911 -12.752  1.00 63.15      A    C  
ANISOU  469  CA  GLU A  66     6333   8525   9136   -546   -788   -630  A    C  
ATOM    470  C   GLU A  66      40.069 -11.573 -13.287  1.00 62.55      A    C  
ANISOU  470  C   GLU A  66     6191   8589   8985   -410   -770   -543  A    C  
ATOM    471  O   GLU A  66      40.769 -10.850 -12.595  1.00 74.42      A    O  
ANISOU  471  O   GLU A  66     7734  10083  10459   -411   -694   -433  A    O  
ATOM    472  CB  GLU A  66      40.336 -14.070 -13.374  1.00 67.78      A    C  
ANISOU  472  CB  GLU A  66     7023   9070   9662   -469   -887   -688  A    C  
ATOM    473  CG  GLU A  66      41.825 -14.014 -13.142  1.00 79.79      A    C  
ANISOU  473  CG  GLU A  66     8643  10580  11095   -378   -873   -594  A    C  
ATOM    474  CD  GLU A  66      42.581 -15.077 -13.915  1.00 92.82      A    C  
ANISOU  474  CD  GLU A  66    10373  12209  12685   -267   -968   -662  A    C  
ATOM    475  OE1 GLU A  66      41.936 -15.893 -14.611  1.00 94.08      A    O  
ANISOU  475  OE1 GLU A  66    10533  12350  12863   -268  -1049   -788  A    O  
ATOM    476  OE2 GLU A  66      43.828 -15.094 -13.825  1.00101.60      A    O1-
ANISOU  476  OE2 GLU A  66    11544  13322  13736   -175   -962   -596  A    O1-
ATOM    477  N   ILE A  67      39.723 -11.245 -14.523  1.00 59.19      A    N  
ANISOU  477  N   ILE A  67     5677   8289   8524   -297   -845   -592  A    N  
ATOM    478  CA  ILE A  67      40.087  -9.953 -15.093  1.00 55.30      A    C  
ANISOU  478  CA  ILE A  67     5128   7923   7959   -175   -828   -505  A    C  
ATOM    479  C   ILE A  67      39.487  -8.795 -14.309  1.00 57.83      A    C  
ANISOU  479  C   ILE A  67     5379   8243   8351   -240   -732   -437  A    C  
ATOM    480  O   ILE A  67      40.132  -7.771 -14.155  1.00 61.83      A    O  
ANISOU  480  O   ILE A  67     5897   8786   8808   -190   -677   -328  A    O  
ATOM    481  CB  ILE A  67      39.643  -9.823 -16.566  1.00 59.51      A    C  
ANISOU  481  CB  ILE A  67     5591   8585   8436    -49   -935   -573  A    C  
ATOM    482  CG1 ILE A  67      40.481 -10.734 -17.457  1.00 63.02      A    C  
ANISOU  482  CG1 ILE A  67     6121   9051   8773     54  -1013   -626  A    C  
ATOM    483  CG2 ILE A  67      39.774  -8.383 -17.042  1.00 52.80      A    C  
ANISOU  483  CG2 ILE A  67     4684   7850   7528     54   -909   -474  A    C  
ATOM    484  CD1 ILE A  67      39.978 -10.807 -18.872  1.00 60.90      A    C  
ANISOU  484  CD1 ILE A  67     5813   8893   8434    165  -1130   -714  A    C  
ATOM    485  N   LYS A  68      38.252  -8.945 -13.826  1.00 58.78      A    N  
ANISOU  485  N   LYS A  68     5425   8321   8590   -351   -707   -504  A    N  
ATOM    486  CA  LYS A  68      37.592  -7.873 -13.080  1.00 54.23      A    C  
ANISOU  486  CA  LYS A  68     4776   7741   8087   -403   -606   -456  A    C  
ATOM    487  C   LYS A  68      38.383  -7.582 -11.820  1.00 61.83      A    C  
ANISOU  487  C   LYS A  68     5854   8612   9028   -479   -493   -357  A    C  
ATOM    488  O   LYS A  68      38.625  -6.432 -11.476  1.00 65.54      A    O  
ANISOU  488  O   LYS A  68     6321   9101   9480   -451   -427   -271  A    O  
ATOM    489  CB  LYS A  68      36.168  -8.265 -12.694  1.00 62.04      A    C  
ANISOU  489  CB  LYS A  68     5659   8695   9220   -523   -582   -556  A    C  
ATOM    490  CG  LYS A  68      35.481  -7.279 -11.750  1.00 74.05      A    C  
ANISOU  490  CG  LYS A  68     7113  10197  10825   -586   -449   -518  A    C  
ATOM    491  CD  LYS A  68      34.356  -7.928 -10.936  1.00 87.05      A    C  
ANISOU  491  CD  LYS A  68     8697  11768  12609   -754   -371   -600  A    C  
ATOM    492  CE  LYS A  68      33.685  -6.897 -10.009  1.00102.29      A    C  
ANISOU  492  CE  LYS A  68    10560  13687  14617   -800   -220   -570  A    C  
ATOM    493  NZ  LYS A  68      33.064  -7.502  -8.780  1.00106.08      A    N1+
ANISOU  493  NZ  LYS A  68    11062  14062  15183   -990    -80   -604  A    N1+
ATOM    494  N   ILE A  69      38.791  -8.653 -11.147  1.00 66.42      A    N  
ANISOU  494  N   ILE A  69     6546   9085   9607   -573   -484   -372  A    N  
ATOM    495  CA  ILE A  69      39.507  -8.574  -9.881  1.00 63.73      A    C  
ANISOU  495  CA  ILE A  69     6333   8641   9240   -658   -398   -287  A    C  
ATOM    496  C   ILE A  69      40.929  -8.017 -10.015  1.00 65.26      A    C  
ANISOU  496  C   ILE A  69     6595   8869   9333   -560   -418   -181  A    C  
ATOM    497  O   ILE A  69      41.329  -7.149  -9.247  1.00 71.94      A    O  
ANISOU  497  O   ILE A  69     7484   9690  10160   -587   -349    -95  A    O  
ATOM    498  CB  ILE A  69      39.522  -9.947  -9.176  1.00 60.44      A    C  
ANISOU  498  CB  ILE A  69     6030   8090   8846   -781   -400   -330  A    C  
ATOM    499  CG1 ILE A  69      38.108 -10.309  -8.705  1.00 58.02      A    C  
ANISOU  499  CG1 ILE A  69     5658   7733   8653   -923   -333   -411  A    C  
ATOM    500  CG2 ILE A  69      40.458  -9.913  -7.999  1.00 59.95      A    C  
ANISOU  500  CG2 ILE A  69     6121   7927   8729   -841   -347   -234  A    C  
ATOM    501  CD1 ILE A  69      37.954 -11.730  -8.164  1.00 55.95      A    C  
ANISOU  501  CD1 ILE A  69     5503   7334   8423  -1056   -340   -460  A    C  
ATOM    502  N   LEU A  70      41.685  -8.522 -10.989  1.00 62.45      A    N  
ANISOU  502  N   LEU A  70     6247   8568   8913   -448   -511   -194  A    N  
ATOM    503  CA  LEU A  70      43.020  -8.011 -11.308  1.00 48.66      A    C  
ANISOU  503  CA  LEU A  70     4530   6878   7080   -345   -527   -100  A    C  
ATOM    504  C   LEU A  70      43.035  -6.508 -11.639  1.00 53.38      A    C  
ANISOU  504  C   LEU A  70     5058   7569   7656   -283   -486    -21  A    C  
ATOM    505  O   LEU A  70      43.973  -5.808 -11.295  1.00 66.14      A    O  
ANISOU  505  O   LEU A  70     6710   9187   9234   -271   -455     79  A    O  
ATOM    506  CB  LEU A  70      43.590  -8.787 -12.488  1.00 48.17      A    C  
ANISOU  506  CB  LEU A  70     4465   6882   6957   -223   -618   -149  A    C  
ATOM    507  CG  LEU A  70      44.469 -10.026 -12.318  1.00 54.95      A    C  
ANISOU  507  CG  LEU A  70     5421   7665   7793   -212   -668   -173  A    C  
ATOM    508  CD1 LEU A  70      44.346 -10.658 -10.943  1.00 63.02      A    C  
ANISOU  508  CD1 LEU A  70     6546   8527   8870   -358   -640   -168  A    C  
ATOM    509  CD2 LEU A  70      44.128 -11.022 -13.419  1.00 54.20      A    C  
ANISOU  509  CD2 LEU A  70     5314   7600   7681   -138   -754   -294  A    C  
ATOM    510  N   GLN A  71      42.001  -6.018 -12.318  1.00 56.17      A    N  
ANISOU  510  N   GLN A  71     5312   7993   8039   -244   -496    -66  A    N  
ATOM    511  CA  GLN A  71      41.924  -4.606 -12.682  1.00 56.49      A    C  
ANISOU  511  CA  GLN A  71     5296   8107   8062   -176   -467      8  A    C  
ATOM    512  C   GLN A  71      41.659  -3.732 -11.469  1.00 59.73      A    C  
ANISOU  512  C   GLN A  71     5730   8438   8526   -271   -368     62  A    C  
ATOM    513  O   GLN A  71      41.983  -2.540 -11.462  1.00 57.83      A    O  
ANISOU  513  O   GLN A  71     5489   8219   8263   -234   -333    149  A    O  
ATOM    514  CB  GLN A  71      40.832  -4.370 -13.722  1.00 51.85      A    C  
ANISOU  514  CB  GLN A  71     4599   7607   7493    -98   -523    -58  A    C  
ATOM    515  CG  GLN A  71      41.231  -4.704 -15.150  1.00 54.27      A    C  
ANISOU  515  CG  GLN A  71     4894   8023   7703     35   -619    -79  A    C  
ATOM    516  CD  GLN A  71      40.026  -4.761 -16.063  1.00 61.93      A    C  
ANISOU  516  CD  GLN A  71     5769   9063   8698     91   -703   -171  A    C  
ATOM    517  NE2 GLN A  71      40.263  -4.698 -17.362  1.00 67.66      A    N  
ANISOU  517  NE2 GLN A  71     6492   9895   9320    221   -783   -174  A    N  
ATOM    518  OE1 GLN A  71      38.892  -4.861 -15.599  1.00 63.44      A    O  
ANISOU  518  OE1 GLN A  71     5888   9214   9001     16   -696   -240  A    O  
ATOM    519  N   LEU A  72      41.072  -4.341 -10.443  1.00 62.25      A    N  
ANISOU  519  N   LEU A  72     6082   8659   8910   -396   -318      8  A    N  
ATOM    520  CA  LEU A  72      40.736  -3.644  -9.210  1.00 60.99      A    C  
ANISOU  520  CA  LEU A  72     5964   8417   8793   -494   -211     40  A    C  
ATOM    521  C   LEU A  72      41.909  -3.629  -8.236  1.00 66.17      A    C  
ANISOU  521  C   LEU A  72     6759   8991   9392   -557   -187    123  A    C  
ATOM    522  O   LEU A  72      42.212  -2.600  -7.638  1.00 74.64      A    O  
ANISOU  522  O   LEU A  72     7876  10035  10451   -577   -132    193  A    O  
ATOM    523  CB  LEU A  72      39.517  -4.289  -8.554  1.00 64.68      A    C  
ANISOU  523  CB  LEU A  72     6404   8822   9351   -606   -153    -55  A    C  
ATOM    524  CG  LEU A  72      39.299  -3.946  -7.083  1.00 60.91      A    C  
ANISOU  524  CG  LEU A  72     6013   8237   8894   -733    -26    -32  A    C  
ATOM    525  CD1 LEU A  72      38.724  -2.567  -6.951  1.00 53.26      A    C  
ANISOU  525  CD1 LEU A  72     4982   7292   7962   -693     49    -12  A    C  
ATOM    526  CD2 LEU A  72      38.391  -4.971  -6.458  1.00 47.22      A    C  
ANISOU  526  CD2 LEU A  72     4281   6434   7227   -862     30   -117  A    C  
ATOM    527  N   LEU A  73      42.576  -4.769  -8.095  1.00 60.80      A    N  
ANISOU  527  N   LEU A  73     6152   8270   8681   -585   -239    112  A    N  
ATOM    528  CA  LEU A  73      43.680  -4.905  -7.150  1.00 58.26      A    C  
ANISOU  528  CA  LEU A  73     5959   7866   8310   -643   -240    184  A    C  
ATOM    529  C   LEU A  73      44.989  -4.291  -7.642  1.00 58.85      A    C  
ANISOU  529  C   LEU A  73     6026   8006   8328   -553   -289    276  A    C  
ATOM    530  O   LEU A  73      45.675  -4.868  -8.466  1.00 60.76      A    O  
ANISOU  530  O   LEU A  73     6238   8307   8541   -467   -359    274  A    O  
ATOM    531  CB  LEU A  73      43.880  -6.374  -6.811  1.00 49.01      A    C  
ANISOU  531  CB  LEU A  73     4871   6616   7136   -695   -286    140  A    C  
ATOM    532  CG  LEU A  73      42.632  -6.951  -6.151  1.00 53.29      A    C  
ANISOU  532  CG  LEU A  73     5435   7077   7737   -817   -218     63  A    C  
ATOM    533  CD1 LEU A  73      42.908  -8.330  -5.646  1.00 54.38      A    C  
ANISOU  533  CD1 LEU A  73     5690   7106   7864   -887   -259     39  A    C  
ATOM    534  CD2 LEU A  73      42.178  -6.055  -5.020  1.00 60.91      A    C  
ANISOU  534  CD2 LEU A  73     6449   7984   8708   -913   -103     96  A    C  
ATOM    535  N   LYS A  74      45.329  -3.118  -7.124  1.00 57.70      A    N  
ANISOU  535  N   LYS A  74     5908   7845   8171   -578   -246    354  A    N  
ATOM    536  CA  LYS A  74      46.538  -2.409  -7.537  1.00 53.85      A    C  
ANISOU  536  CA  LYS A  74     5402   7414   7643   -516   -281    449  A    C  
ATOM    537  C   LYS A  74      47.432  -2.140  -6.339  1.00 53.59      A    C  
ANISOU  537  C   LYS A  74     5479   7291   7591   -607   -285    518  A    C  
ATOM    538  O   LYS A  74      47.225  -1.181  -5.594  1.00 61.18      A    O  
ANISOU  538  O   LYS A  74     6495   8197   8555   -672   -233    550  A    O  
ATOM    539  CB  LYS A  74      46.200  -1.083  -8.242  1.00 54.64      A    C  
ANISOU  539  CB  LYS A  74     5427   7587   7748   -452   -244    489  A    C  
ATOM    540  CG  LYS A  74      45.631  -1.220  -9.657  1.00 54.91      A    C  
ANISOU  540  CG  LYS A  74     5352   7735   7776   -334   -272    446  A    C  
ATOM    541  CD  LYS A  74      46.219  -2.430 -10.352  1.00 66.86      A    C  
ANISOU  541  CD  LYS A  74     6848   9301   9255   -274   -340    409  A    C  
ATOM    542  CE  LYS A  74      46.019  -2.409 -11.851  1.00 65.60      A    C  
ANISOU  542  CE  LYS A  74     6602   9267   9055   -143   -375    388  A    C  
ATOM    543  NZ  LYS A  74      46.668  -3.632 -12.382  1.00 66.63      A    N1+
ANISOU  543  NZ  LYS A  74     6737   9432   9148    -88   -433    342  A    N1+
ATOM    544  N   HIS A  75      48.447  -2.973  -6.165  1.00 53.04      A    N  
ANISOU  544  N   HIS A  75     5445   7205   7501   -603   -357    538  A    N  
ATOM    545  CA  HIS A  75      49.251  -2.902  -4.959  1.00 54.31      A    C  
ANISOU  545  CA  HIS A  75     5720   7272   7643   -692   -388    594  A    C  
ATOM    546  C   HIS A  75      50.680  -3.446  -5.154  1.00 58.13      A    C  
ANISOU  546  C   HIS A  75     6182   7785   8119   -639   -485    642  A    C  
ATOM    547  O   HIS A  75      50.912  -4.316  -5.996  1.00 58.97      A    O  
ANISOU  547  O   HIS A  75     6224   7952   8230   -546   -523    607  A    O  
ATOM    548  CB  HIS A  75      48.511  -3.643  -3.850  1.00 52.66      A    C  
ANISOU  548  CB  HIS A  75     5643   6940   7427   -798   -363    540  A    C  
ATOM    549  CG  HIS A  75      49.170  -3.553  -2.515  1.00 58.22      A    C  
ANISOU  549  CG  HIS A  75     6495   7535   8090   -897   -396    591  A    C  
ATOM    550  CD2 HIS A  75      49.034  -2.652  -1.515  1.00 55.53      A    C  
ANISOU  550  CD2 HIS A  75     6256   7123   7721   -990   -350    620  A    C  
ATOM    551  ND1 HIS A  75      50.077  -4.489  -2.070  1.00 54.54      A    N  
ANISOU  551  ND1 HIS A  75     6102   7016   7604   -902   -496    614  A    N  
ATOM    552  CE1 HIS A  75      50.478  -4.164  -0.856  1.00 51.13      A    C  
ANISOU  552  CE1 HIS A  75     5810   6489   7128   -998   -521    660  A    C  
ATOM    553  NE2 HIS A  75      49.863  -3.052  -0.497  1.00 50.76      A    N  
ANISOU  553  NE2 HIS A  75     5787   6429   7070  -1056   -431    661  A    N  
ATOM    554  N   GLU A  76      51.631  -2.930  -4.372  1.00 60.23      A    N  
ANISOU  554  N   GLU A  76     6498   8009   8376   -695   -529    717  A    N  
ATOM    555  CA  GLU A  76      53.036  -3.340  -4.489  1.00 61.25      A    C  
ANISOU  555  CA  GLU A  76     6584   8172   8518   -647   -625    767  A    C  
ATOM    556  C   GLU A  76      53.219  -4.860  -4.324  1.00 59.78      A    C  
ANISOU  556  C   GLU A  76     6447   7935   8330   -610   -697    718  A    C  
ATOM    557  O   GLU A  76      54.160  -5.442  -4.868  1.00 64.85      A    O  
ANISOU  557  O   GLU A  76     7011   8634   8993   -516   -760    728  A    O  
ATOM    558  CB  GLU A  76      53.919  -2.548  -3.506  1.00 71.58      A    C  
ANISOU  558  CB  GLU A  76     7948   9425   9824   -736   -677    848  A    C  
ATOM    559  CG  GLU A  76      55.416  -2.924  -3.461  1.00 97.65      A    C  
ANISOU  559  CG  GLU A  76    11190  12756  13156   -697   -790    903  A    C  
ATOM    560  CD  GLU A  76      56.265  -2.301  -4.583  1.00112.19      A    C  
ANISOU  560  CD  GLU A  76    12848  14741  15039   -618   -772    958  A    C  
ATOM    561  OE1 GLU A  76      55.700  -1.613  -5.461  1.00117.48      A    O  
ANISOU  561  OE1 GLU A  76    13451  15484  15701   -586   -677    959  A    O  
ATOM    562  OE2 GLU A  76      57.504  -2.507  -4.586  1.00107.68      A    O1-
ANISOU  562  OE2 GLU A  76    12196  14207  14509   -587   -851   1004  A    O1-
ATOM    563  N   ASN A  77      52.310  -5.508  -3.606  1.00 50.49      A    N  
ANISOU  563  N   ASN A  77     5400   6651   7133   -683   -679    663  A    N  
ATOM    564  CA  ASN A  77      52.448  -6.940  -3.347  1.00 60.90      A    C  
ANISOU  564  CA  ASN A  77     6797   7893   8449   -664   -750    623  A    C  
ATOM    565  C   ASN A  77      51.389  -7.834  -3.979  1.00 64.11      A    C  
ANISOU  565  C   ASN A  77     7197   8297   8867   -635   -708    527  A    C  
ATOM    566  O   ASN A  77      51.263  -9.007  -3.623  1.00 65.78      A    O  
ANISOU  566  O   ASN A  77     7506   8411   9076   -650   -753    488  A    O  
ATOM    567  CB  ASN A  77      52.547  -7.204  -1.848  1.00 57.76      A    C  
ANISOU  567  CB  ASN A  77     6588   7345   8011   -782   -797    653  A    C  
ATOM    568  CG  ASN A  77      53.709  -6.479  -1.221  1.00 66.43      A    C  
ANISOU  568  CG  ASN A  77     7698   8442   9102   -806   -877    740  A    C  
ATOM    569  ND2 ASN A  77      54.909  -6.737  -1.736  1.00 60.00      A    N  
ANISOU  569  ND2 ASN A  77     6774   7694   8329   -705   -969    773  A    N  
ATOM    570  OD1 ASN A  77      53.537  -5.681  -0.298  1.00 73.59      A    O  
ANISOU  570  OD1 ASN A  77     8704   9288   9969   -915   -855    772  A    O  
ATOM    571  N   VAL A  78      50.623  -7.271  -4.905  1.00 57.89      A    N  
ANISOU  571  N   VAL A  78     6298   7605   8092   -598   -630    490  A    N  
ATOM    572  CA  VAL A  78      49.762  -8.070  -5.756  1.00 56.03      A    C  
ANISOU  572  CA  VAL A  78     6020   7395   7873   -550   -613    395  A    C  
ATOM    573  C   VAL A  78      50.278  -7.949  -7.178  1.00 60.79      A    C  
ANISOU  573  C   VAL A  78     6481   8143   8474   -401   -631    386  A    C  
ATOM    574  O   VAL A  78      50.635  -6.855  -7.634  1.00 64.16      A    O  
ANISOU  574  O   VAL A  78     6820   8668   8892   -365   -598    445  A    O  
ATOM    575  CB  VAL A  78      48.296  -7.600  -5.702  1.00 51.54      A    C  
ANISOU  575  CB  VAL A  78     5439   6821   7321   -625   -517    345  A    C  
ATOM    576  CG1 VAL A  78      47.439  -8.383  -6.699  1.00 44.64      A    C  
ANISOU  576  CG1 VAL A  78     4500   5988   6475   -573   -521    242  A    C  
ATOM    577  CG2 VAL A  78      47.753  -7.770  -4.317  1.00 47.46      A    C  
ANISOU  577  CG2 VAL A  78     5067   6166   6798   -773   -474    347  A    C  
ATOM    578  N   VAL A  79      50.326  -9.080  -7.869  1.00 55.68      A    N  
ANISOU  578  N   VAL A  79     5824   7502   7828   -318   -679    314  A    N  
ATOM    579  CA  VAL A  79      50.778  -9.121  -9.253  1.00 59.99      A    C  
ANISOU  579  CA  VAL A  79     6256   8183   8354   -169   -689    290  A    C  
ATOM    580  C   VAL A  79      50.038  -8.070 -10.102  1.00 62.20      A    C  
ANISOU  580  C   VAL A  79     6441   8578   8615   -148   -622    291  A    C  
ATOM    581  O   VAL A  79      48.904  -7.722  -9.810  1.00 63.97      A    O  
ANISOU  581  O   VAL A  79     6678   8769   8858   -228   -581    263  A    O  
ATOM    582  CB  VAL A  79      50.567 -10.520  -9.819  1.00 57.96      A    C  
ANISOU  582  CB  VAL A  79     6031   7891   8097   -101   -744    184  A    C  
ATOM    583  CG1 VAL A  79      49.113 -10.710 -10.165  1.00 50.78      A    C  
ANISOU  583  CG1 VAL A  79     5123   6971   7199   -152   -718     93  A    C  
ATOM    584  CG2 VAL A  79      51.457 -10.753 -11.005  1.00 66.23      A    C  
ANISOU  584  CG2 VAL A  79     6995   9058   9113     64   -764    167  A    C  
ATOM    585  N   ASN A  80      50.690  -7.547 -11.135  1.00 63.87      A    N  
ANISOU  585  N   ASN A  80     6555   8922   8788    -37   -608    326  A    N  
ATOM    586  CA  ASN A  80      50.151  -6.398 -11.876  1.00 52.64      A    C  
ANISOU  586  CA  ASN A  80     5060   7602   7339    -14   -551    355  A    C  
ATOM    587  C   ASN A  80      49.743  -6.693 -13.301  1.00 57.99      A    C  
ANISOU  587  C   ASN A  80     5683   8388   7963    106   -561    285  A    C  
ATOM    588  O   ASN A  80      50.596  -6.916 -14.152  1.00 59.27      A    O  
ANISOU  588  O   ASN A  80     5805   8640   8074    218   -564    292  A    O  
ATOM    589  CB  ASN A  80      51.166  -5.261 -11.918  1.00 49.85      A    C  
ANISOU  589  CB  ASN A  80     4653   7316   6973     -3   -514    477  A    C  
ATOM    590  CG  ASN A  80      50.641  -4.037 -12.631  1.00 58.85      A    C  
ANISOU  590  CG  ASN A  80     5740   8539   8082     19   -459    522  A    C  
ATOM    591  ND2 ASN A  80      51.410  -3.534 -13.580  1.00 68.99      A    N  
ANISOU  591  ND2 ASN A  80     6956   9940   9316    105   -430    584  A    N  
ATOM    592  OD1 ASN A  80      49.565  -3.538 -12.321  1.00 66.70      A    O  
ANISOU  592  OD1 ASN A  80     6755   9491   9098    -39   -438    503  A    O  
ATOM    593  N   LEU A  81      48.442  -6.676 -13.562  1.00 66.42      A    N  
ANISOU  593  N   LEU A  81     6747   9451   9039     83   -565    215  A    N  
ATOM    594  CA  LEU A  81      47.949  -6.785 -14.925  1.00 60.06      A    C  
ANISOU  594  CA  LEU A  81     5895   8751   8173    192   -590    151  A    C  
ATOM    595  C   LEU A  81      48.210  -5.471 -15.659  1.00 60.04      A    C  
ANISOU  595  C   LEU A  81     5836   8865   8112    254   -543    248  A    C  
ATOM    596  O   LEU A  81      47.714  -4.425 -15.253  1.00 64.40      A    O  
ANISOU  596  O   LEU A  81     6374   9400   8696    195   -507    307  A    O  
ATOM    597  CB  LEU A  81      46.457  -7.109 -14.918  1.00 54.12      A    C  
ANISOU  597  CB  LEU A  81     5139   7957   7465    139   -622     50  A    C  
ATOM    598  CG  LEU A  81      45.839  -7.414 -16.278  1.00 54.22      A    C  
ANISOU  598  CG  LEU A  81     5117   8066   7419    242   -681    -39  A    C  
ATOM    599  CD1 LEU A  81      46.291  -8.787 -16.765  1.00 56.60      A    C  
ANISOU  599  CD1 LEU A  81     5467   8355   7684    307   -740   -135  A    C  
ATOM    600  CD2 LEU A  81      44.343  -7.360 -16.171  1.00 55.48      A    C  
ANISOU  600  CD2 LEU A  81     5237   8196   7646    176   -708   -113  A    C  
ATOM    601  N   ILE A  82      49.000  -5.529 -16.729  1.00 60.23      A    N  
ANISOU  601  N   ILE A  82     5835   9001   8048    374   -536    265  A    N  
ATOM    602  CA  ILE A  82      49.361  -4.347 -17.513  1.00 58.82      A    C  
ANISOU  602  CA  ILE A  82     5616   8933   7798    433   -483    368  A    C  
ATOM    603  C   ILE A  82      48.263  -4.006 -18.507  1.00 60.42      A    C  
ANISOU  603  C   ILE A  82     5812   9203   7940    496   -517    325  A    C  
ATOM    604  O   ILE A  82      47.904  -2.842 -18.700  1.00 63.44      A    O  
ANISOU  604  O   ILE A  82     6180   9614   8310    494   -492    404  A    O  
ATOM    605  CB  ILE A  82      50.635  -4.606 -18.331  1.00 55.71      A    C  
ANISOU  605  CB  ILE A  82     5200   8643   7323    539   -446    399  A    C  
ATOM    606  CG1 ILE A  82      51.815  -4.862 -17.409  1.00 53.14      A    C  
ANISOU  606  CG1 ILE A  82     4858   8265   7067    490   -424    450  A    C  
ATOM    607  CG2 ILE A  82      50.945  -3.440 -19.274  1.00 43.92      A    C  
ANISOU  607  CG2 ILE A  82     3678   7269   5739    597   -382    507  A    C  
ATOM    608  CD1 ILE A  82      53.082  -5.161 -18.169  1.00 56.73      A    C  
ANISOU  608  CD1 ILE A  82     5265   8826   7464    599   -378    474  A    C  
ATOM    609  N   GLU A  83      47.748  -5.045 -19.148  1.00 55.37      A    N  
ANISOU  609  N   GLU A  83     5190   8583   7265    556   -586    198  A    N  
ATOM    610  CA  GLU A  83      46.795  -4.898 -20.234  1.00 63.70      A    C  
ANISOU  610  CA  GLU A  83     6241   9714   8247    634   -645    141  A    C  
ATOM    611  C   GLU A  83      46.352  -6.281 -20.681  1.00 67.23      A    C  
ANISOU  611  C   GLU A  83     6718  10150   8678    671   -733    -18  A    C  
ATOM    612  O   GLU A  83      46.857  -7.298 -20.191  1.00 66.14      A    O  
ANISOU  612  O   GLU A  83     6610   9943   8579    647   -736    -73  A    O  
ATOM    613  CB  GLU A  83      47.419  -4.154 -21.423  1.00 60.72      A    C  
ANISOU  613  CB  GLU A  83     5871   9472   7727    749   -605    227  A    C  
ATOM    614  CG  GLU A  83      48.483  -4.963 -22.185  1.00 64.17      A    C  
ANISOU  614  CG  GLU A  83     6335   9987   8060    852   -579    195  A    C  
ATOM    615  CD  GLU A  83      49.066  -4.197 -23.367  1.00 76.79      A    C  
ANISOU  615  CD  GLU A  83     7948  11725   9505    957   -517    286  A    C  
ATOM    616  OE1 GLU A  83      48.334  -3.411 -24.009  1.00 84.02      A    O  
ANISOU  616  OE1 GLU A  83     8881  12689  10355    991   -548    321  A    O  
ATOM    617  OE2 GLU A  83      50.261  -4.388 -23.660  1.00 73.85      A    O1-
ANISOU  617  OE2 GLU A  83     7568  11414   9078   1009   -434    325  A    O1-
ATOM    618  N   ILE A  84      45.406  -6.306 -21.614  1.00 61.09      A    N  
ANISOU  618  N   ILE A  84     5937   9431   7842    732   -814    -92  A    N  
ATOM    619  CA  ILE A  84      44.919  -7.543 -22.203  1.00 57.31      A    C  
ANISOU  619  CA  ILE A  84     5493   8948   7335    771   -914   -252  A    C  
ATOM    620  C   ILE A  84      45.088  -7.497 -23.731  1.00 63.09      A    C  
ANISOU  620  C   ILE A  84     6269   9816   7887    923   -953   -277  A    C  
ATOM    621  O   ILE A  84      44.773  -6.473 -24.361  1.00 67.88      A    O  
ANISOU  621  O   ILE A  84     6863  10508   8420    975   -958   -204  A    O  
ATOM    622  CB  ILE A  84      43.466  -7.779 -21.786  1.00 53.87      A    C  
ANISOU  622  CB  ILE A  84     5011   8441   7018    676   -998   -344  A    C  
ATOM    623  CG1 ILE A  84      43.439  -8.250 -20.333  1.00 54.78      A    C  
ANISOU  623  CG1 ILE A  84     5121   8411   7283    529   -953   -349  A    C  
ATOM    624  CG2 ILE A  84      42.792  -8.783 -22.699  1.00 53.66      A    C  
ANISOU  624  CG2 ILE A  84     5011   8435   6943    726  -1126   -504  A    C  
ATOM    625  CD1 ILE A  84      42.113  -8.045 -19.649  1.00 59.97      A    C  
ANISOU  625  CD1 ILE A  84     5708   9003   8074    413   -974   -386  A    C  
ATOM    626  N   CYS A  85      45.603  -8.588 -24.314  1.00 57.57      A    N  
ANISOU  626  N   CYS A  85     5634   9132   7108   1000   -977   -378  A    N  
ATOM    627  CA  CYS A  85      45.971  -8.623 -25.743  1.00 65.69      A    C  
ANISOU  627  CA  CYS A  85     6727  10292   7939   1154   -989   -404  A    C  
ATOM    628  C   CYS A  85      45.266  -9.695 -26.587  1.00 71.28      A    C  
ANISOU  628  C   CYS A  85     7502  11003   8578   1211  -1127   -588  A    C  
ATOM    629  O   CYS A  85      44.714 -10.660 -26.058  1.00 75.89      A    O  
ANISOU  629  O   CYS A  85     8086  11474   9274   1133  -1203   -706  A    O  
ATOM    630  CB  CYS A  85      47.487  -8.777 -25.902  1.00 77.14      A    C  
ANISOU  630  CB  CYS A  85     8203  11792   9316   1231   -864   -345  A    C  
ATOM    631  SG  CYS A  85      48.448  -7.299 -25.514  1.00 76.14      A    S  
ANISOU  631  SG  CYS A  85     8011  11723   9195   1205   -709   -120  A    S  
ATOM    632  N   ARG A  86      45.323  -9.527 -27.908  1.00 71.29      A    N  
ANISOU  632  N   ARG A  86     7572  11130   8387   1344  -1157   -609  A    N  
ATOM    633  CA  ARG A  86      44.592 -10.378 -28.850  1.00 62.71      A    C  
ANISOU  633  CA  ARG A  86     6560  10059   7206   1406  -1306   -782  A    C  
ATOM    634  C   ARG A  86      45.486 -10.954 -29.971  1.00 71.49      A    C  
ANISOU  634  C   ARG A  86     7795  11261   8109   1564  -1270   -845  A    C  
ATOM    635  O   ARG A  86      46.696 -10.960 -29.846  1.00 68.32      A    O  
ANISOU  635  O   ARG A  86     7399  10885   7676   1612  -1125   -777  A    O  
ATOM    636  CB  ARG A  86      43.447  -9.569 -29.464  1.00 59.19      A    C  
ANISOU  636  CB  ARG A  86     6094   9682   6714   1417  -1424   -769  A    C  
ATOM    637  CG  ARG A  86      43.919  -8.523 -30.446  1.00 69.00      A    C  
ANISOU  637  CG  ARG A  86     7393  11069   7756   1538  -1366   -644  A    C  
ATOM    638  CD  ARG A  86      42.829  -7.565 -30.864  1.00 85.01      A    C  
ANISOU  638  CD  ARG A  86     9392  13146   9764   1548  -1480   -598  A    C  
ATOM    639  NE  ARG A  86      43.370  -6.547 -31.758  1.00 95.11      A    N  
ANISOU  639  NE  ARG A  86    10747  14548  10843   1658  -1412   -459  A    N  
ATOM    640  CZ  ARG A  86      43.008  -6.405 -33.025  1.00103.62      A    C  
ANISOU  640  CZ  ARG A  86    11930  15727  11714   1775  -1515   -490  A    C  
ATOM    641  NH1 ARG A  86      42.083  -7.207 -33.537  1.00101.04      A    N1+
ANISOU  641  NH1 ARG A  86    11634  15394  11363   1796  -1706   -665  A    N1+
ATOM    642  NH2 ARG A  86      43.556  -5.454 -33.771  1.00108.90      A    N  
ANISOU  642  NH2 ARG A  86    12680  16499  12198   1864  -1433   -344  A    N  
ATOM    643  N   THR A  87      44.860 -11.424 -31.054  1.00 86.62      A    N  
ANISOU  643  N   THR A  87     9802  13225   9884   1643  -1405   -980  A    N  
ATOM    644  CA  THR A  87      45.493 -11.895 -32.295  1.00 94.12      A    C  
ANISOU  644  CA  THR A  87    10892  14273  10597   1806  -1387  -1057  A    C  
ATOM    645  C   THR A  87      44.331 -12.517 -33.016  1.00112.73      A    C  
ANISOU  645  C   THR A  87    13320  16617  12895   1818  -1602  -1233  A    C  
ATOM    646  O   THR A  87      44.068 -12.286 -34.208  1.00120.29      A    O  
ANISOU  646  O   THR A  87    14379  17686  13641   1925  -1677  -1267  A    O  
ATOM    647  CB  THR A  87      46.445 -13.069 -32.070  1.00 97.76      A    C  
ANISOU  647  CB  THR A  87    11400  14667  11078   1849  -1313  -1154  A    C  
ATOM    648  CG2 THR A  87      47.879 -12.599 -31.813  1.00108.77      A    C  
ANISOU  648  CG2 THR A  87    12752  16121  12454   1901  -1097  -1008  A    C  
ATOM    649  OG1 THR A  87      45.975 -13.858 -30.970  1.00 87.40      A    O  
ANISOU  649  OG1 THR A  87    10034  13183   9990   1716  -1384  -1229  A    O  
ATOM    650  N   SER A  98      42.096 -15.311 -30.349  1.00 84.11      A    N  
ANISOU  650  N   SER A  98     9543  12494   9922   1379  -1901  -1584  A    N  
ATOM    651  CA  SER A  98      42.622 -15.663 -29.018  1.00 93.53      A    C  
ANISOU  651  CA  SER A  98    10687  13553  11297   1275  -1788  -1526  A    C  
ATOM    652  C   SER A  98      43.087 -14.483 -28.104  1.00 80.02      A    C  
ANISOU  652  C   SER A  98     8863  11872   9668   1225  -1632  -1315  A    C  
ATOM    653  O   SER A  98      43.516 -13.440 -28.589  1.00 88.51      A    O  
ANISOU  653  O   SER A  98     9924  13080  10625   1311  -1558  -1193  A    O  
ATOM    654  CB  SER A  98      43.749 -16.683 -29.177  1.00 93.75      A    C  
ANISOU  654  CB  SER A  98    10837  13529  11256   1374  -1727  -1599  A    C  
ATOM    655  OG  SER A  98      44.259 -17.069 -27.919  1.00 96.62      A    O  
ANISOU  655  OG  SER A  98    11166  13757  11787   1283  -1641  -1545  A    O  
ATOM    656  N   ILE A  99      43.024 -14.677 -26.785  1.00 67.38      A    N  
ANISOU  656  N   ILE A  99     7200  10141   8262   1082  -1583  -1273  A    N  
ATOM    657  CA  ILE A  99      43.195 -13.584 -25.802  1.00 67.27      A    C  
ANISOU  657  CA  ILE A  99     7081  10131   8347   1003  -1465  -1095  A    C  
ATOM    658  C   ILE A  99      44.271 -13.834 -24.715  1.00 70.02      A    C  
ANISOU  658  C   ILE A  99     7438  10388   8779    964  -1340  -1014  A    C  
ATOM    659  O   ILE A  99      44.275 -14.880 -24.063  1.00 75.35      A    O  
ANISOU  659  O   ILE A  99     8157  10922   9552    893  -1366  -1090  A    O  
ATOM    660  CB  ILE A  99      41.848 -13.291 -25.077  1.00 73.24      A    C  
ANISOU  660  CB  ILE A  99     7731  10823   9272    844  -1526  -1103  A    C  
ATOM    661  CG1 ILE A  99      40.790 -12.805 -26.066  1.00 71.54      A    C  
ANISOU  661  CG1 ILE A  99     7476  10713   8995    888  -1654  -1155  A    C  
ATOM    662  CG2 ILE A  99      42.027 -12.282 -23.956  1.00 68.93      A    C  
ANISOU  662  CG2 ILE A  99     7100  10258   8833    758  -1401   -939  A    C  
ATOM    663  CD1 ILE A  99      41.118 -11.485 -26.714  1.00 72.91      A    C  
ANISOU  663  CD1 ILE A  99     7634  11034   9035   1001  -1605  -1021  A    C  
ATOM    664  N   TYR A 100      45.165 -12.867 -24.508  1.00 68.42      A    N  
ANISOU  664  N   TYR A 100     7196  10259   8540   1004  -1215   -856  A    N  
ATOM    665  CA  TYR A 100      46.240 -12.992 -23.508  1.00 66.07      A    C  
ANISOU  665  CA  TYR A 100     6895   9890   8319    973  -1110   -770  A    C  
ATOM    666  C   TYR A 100      46.160 -11.948 -22.392  1.00 69.64      A    C  
ANISOU  666  C   TYR A 100     7264  10315   8882    852  -1035   -622  A    C  
ATOM    667  O   TYR A 100      45.982 -10.763 -22.661  1.00 76.46      A    O  
ANISOU  667  O   TYR A 100     8073  11274   9706    864   -999   -524  A    O  
ATOM    668  CB  TYR A 100      47.612 -12.858 -24.173  1.00 61.76      A    C  
ANISOU  668  CB  TYR A 100     6371   9452   7644   1125  -1018   -718  A    C  
ATOM    669  CG  TYR A 100      48.013 -14.026 -25.039  1.00 71.10      A    C  
ANISOU  669  CG  TYR A 100     7650  10637   8728   1256  -1059   -864  A    C  
ATOM    670  CD1 TYR A 100      48.871 -15.009 -24.562  1.00 72.49      A    C  
ANISOU  670  CD1 TYR A 100     7868  10717   8958   1288  -1038   -906  A    C  
ATOM    671  CD2 TYR A 100      47.539 -14.146 -26.337  1.00 72.57      A    C  
ANISOU  671  CD2 TYR A 100     7896  10917   8760   1355  -1126   -963  A    C  
ATOM    672  CE1 TYR A 100      49.235 -16.085 -25.355  1.00 77.52      A    C  
ANISOU  672  CE1 TYR A 100     8602  11346   9507   1420  -1073  -1049  A    C  
ATOM    673  CE2 TYR A 100      47.901 -15.214 -27.135  1.00 78.95      A    C  
ANISOU  673  CE2 TYR A 100     8809  11722   9468   1478  -1162  -1108  A    C  
ATOM    674  CZ  TYR A 100      48.747 -16.179 -26.640  1.00 85.46      A    C  
ANISOU  674  CZ  TYR A 100     9671  12444  10355   1513  -1130  -1153  A    C  
ATOM    675  OH  TYR A 100      49.109 -17.237 -27.441  1.00102.08      A    O  
ANISOU  675  OH  TYR A 100    11887  14537  12361   1648  -1162  -1306  A    O  
ATOM    676  N   LEU A 101      46.301 -12.388 -21.145  1.00 62.72      A    N  
ANISOU  676  N   LEU A 101     6394   9300   8135    740  -1015   -604  A    N  
ATOM    677  CA  LEU A 101      46.513 -11.472 -20.026  1.00 57.04      A    C  
ANISOU  677  CA  LEU A 101     5622   8548   7501    639   -933   -463  A    C  
ATOM    678  C   LEU A 101      48.004 -11.125 -19.941  1.00 60.80      A    C  
ANISOU  678  C   LEU A 101     6091   9076   7935    713   -845   -354  A    C  
ATOM    679  O   LEU A 101      48.840 -12.015 -19.993  1.00 66.81      A    O  
ANISOU  679  O   LEU A 101     6897   9807   8683    780   -850   -397  A    O  
ATOM    680  CB  LEU A 101      46.030 -12.102 -18.713  1.00 58.54      A    C  
ANISOU  680  CB  LEU A 101     5842   8570   7832    484   -949   -490  A    C  
ATOM    681  CG  LEU A 101      44.539 -11.998 -18.338  1.00 58.48      A    C  
ANISOU  681  CG  LEU A 101     5795   8509   7915    355   -986   -541  A    C  
ATOM    682  CD1 LEU A 101      43.651 -12.476 -19.442  1.00 64.55      A    C  
ANISOU  682  CD1 LEU A 101     6555   9328   8645    404  -1088   -675  A    C  
ATOM    683  CD2 LEU A 101      44.232 -12.787 -17.087  1.00 54.63      A    C  
ANISOU  683  CD2 LEU A 101     5359   7852   7546    206   -982   -567  A    C  
ATOM    684  N   VAL A 102      48.349  -9.840 -19.838  1.00 59.74      A    N  
ANISOU  684  N   VAL A 102     5897   9017   7785    704   -768   -217  A    N  
ATOM    685  CA  VAL A 102      49.765  -9.450 -19.775  1.00 56.73      A    C  
ANISOU  685  CA  VAL A 102     5488   8692   7377    759   -685   -110  A    C  
ATOM    686  C   VAL A 102      50.146  -8.823 -18.440  1.00 60.39      A    C  
ANISOU  686  C   VAL A 102     5924   9076   7945    637   -641      5  A    C  
ATOM    687  O   VAL A 102      49.638  -7.760 -18.091  1.00 66.28      A    O  
ANISOU  687  O   VAL A 102     6641   9825   8716    560   -613     82  A    O  
ATOM    688  CB  VAL A 102      50.136  -8.449 -20.882  1.00 55.04      A    C  
ANISOU  688  CB  VAL A 102     5234   8639   7040    855   -620    -31  A    C  
ATOM    689  CG1 VAL A 102      51.616  -8.194 -20.880  1.00 56.75      A    C  
ANISOU  689  CG1 VAL A 102     5405   8917   7239    908   -528     65  A    C  
ATOM    690  CG2 VAL A 102      49.691  -8.942 -22.222  1.00 53.18      A    C  
ANISOU  690  CG2 VAL A 102     5042   8488   6677    975   -668   -141  A    C  
ATOM    691  N   PHE A 103      51.048  -9.477 -17.707  1.00 64.13      A    N  
ANISOU  691  N   PHE A 103     6415   9476   8474    627   -643     15  A    N  
ATOM    692  CA  PHE A 103      51.525  -8.969 -16.414  1.00 64.90      A    C  
ANISOU  692  CA  PHE A 103     6504   9497   8660    516   -620    119  A    C  
ATOM    693  C   PHE A 103      52.950  -8.430 -16.457  1.00 66.42      A    C  
ANISOU  693  C   PHE A 103     6626   9767   8845    565   -562    227  A    C  
ATOM    694  O   PHE A 103      53.711  -8.718 -17.376  1.00 72.41      A    O  
ANISOU  694  O   PHE A 103     7345  10626   9543    694   -533    212  A    O  
ATOM    695  CB  PHE A 103      51.503 -10.073 -15.371  1.00 62.70      A    C  
ANISOU  695  CB  PHE A 103     6304   9060   8459    451   -683     64  A    C  
ATOM    696  CG  PHE A 103      50.185 -10.751 -15.233  1.00 56.31      A    C  
ANISOU  696  CG  PHE A 103     5560   8159   7675    383   -735    -44  A    C  
ATOM    697  CD1 PHE A 103      49.264 -10.320 -14.288  1.00 56.39      A    C  
ANISOU  697  CD1 PHE A 103     5593   8086   7748    235   -723    -22  A    C  
ATOM    698  CD2 PHE A 103      49.870 -11.833 -16.030  1.00 50.07      A    C  
ANISOU  698  CD2 PHE A 103     4808   7363   6852    461   -791   -173  A    C  
ATOM    699  CE1 PHE A 103      48.043 -10.952 -14.154  1.00 55.74      A    C  
ANISOU  699  CE1 PHE A 103     5552   7925   7703    161   -758   -121  A    C  
ATOM    700  CE2 PHE A 103      48.647 -12.475 -15.897  1.00 56.20      A    C  
ANISOU  700  CE2 PHE A 103     5636   8051   7667    382   -843   -274  A    C  
ATOM    701  CZ  PHE A 103      47.733 -12.033 -14.959  1.00 50.91      A    C  
ANISOU  701  CZ  PHE A 103     4968   7307   7069    228   -823   -245  A    C  
ATOM    702  N   ASP A 104      53.313  -7.648 -15.449  1.00 64.00      A    N  
ANISOU  702  N   ASP A 104     6303   9414   8601    460   -543    333  A    N  
ATOM    703  CA  ASP A 104      54.721  -7.376 -15.201  1.00 61.43      A    C  
ANISOU  703  CA  ASP A 104     5908   9128   8306    481   -516    424  A    C  
ATOM    704  C   ASP A 104      55.319  -8.702 -14.782  1.00 64.77      A    C  
ANISOU  704  C   ASP A 104     6362   9474   8773    531   -584    357  A    C  
ATOM    705  O   ASP A 104      54.743  -9.401 -13.945  1.00 68.00      A    O  
ANISOU  705  O   ASP A 104     6868   9745   9225    462   -652    304  A    O  
ATOM    706  CB  ASP A 104      54.897  -6.363 -14.078  1.00 61.53      A    C  
ANISOU  706  CB  ASP A 104     5918   9079   8381    341   -509    535  A    C  
ATOM    707  CG  ASP A 104      54.663  -4.940 -14.530  1.00 77.39      A    C  
ANISOU  707  CG  ASP A 104     7884  11167  10354    308   -436    624  A    C  
ATOM    708  OD1 ASP A 104      55.146  -4.569 -15.620  1.00 86.85      A    O  
ANISOU  708  OD1 ASP A 104     9013  12497  11492    397   -374    659  A    O  
ATOM    709  OD2 ASP A 104      54.008  -4.183 -13.780  1.00 84.13      A    O1-
ANISOU  709  OD2 ASP A 104     8783  11945  11239    195   -435    661  A    O1-
ATOM    710  N   PHE A 105      56.465  -9.044 -15.366  1.00 70.60      A    N  
ANISOU  710  N   PHE A 105     7022  10299   9502    655   -560    361  A    N  
ATOM    711  CA  PHE A 105      57.097 -10.342 -15.152  1.00 66.55      A    C  
ANISOU  711  CA  PHE A 105     6533   9722   9032    742   -625    289  A    C  
ATOM    712  C   PHE A 105      57.745 -10.454 -13.791  1.00 67.76      A    C  
ANISOU  712  C   PHE A 105     6699   9763   9284    663   -698    352  A    C  
ATOM    713  O   PHE A 105      58.413  -9.518 -13.335  1.00 72.04      A    O  
ANISOU  713  O   PHE A 105     7163  10344   9866    599   -677    464  A    O  
ATOM    714  CB  PHE A 105      58.146 -10.608 -16.228  1.00 64.99      A    C  
ANISOU  714  CB  PHE A 105     6231   9664   8798    913   -562    271  A    C  
ATOM    715  CG  PHE A 105      58.769 -11.970 -16.141  1.00 65.64      A    C  
ANISOU  715  CG  PHE A 105     6337   9681   8922   1033   -626    182  A    C  
ATOM    716  CD1 PHE A 105      58.063 -13.095 -16.532  1.00 66.51      A    C  
ANISOU  716  CD1 PHE A 105     6563   9715   8993   1098   -678     44  A    C  
ATOM    717  CD2 PHE A 105      60.063 -12.131 -15.675  1.00 62.58      A    C  
ANISOU  717  CD2 PHE A 105     5854   9302   8621   1085   -643    234  A    C  
ATOM    718  CE1 PHE A 105      58.639 -14.354 -16.463  1.00 63.90      A    C  
ANISOU  718  CE1 PHE A 105     6268   9307   8703   1217   -740    -40  A    C  
ATOM    719  CE2 PHE A 105      60.640 -13.394 -15.596  1.00 57.40      A    C  
ANISOU  719  CE2 PHE A 105     5221   8576   8011   1214   -710    151  A    C  
ATOM    720  CZ  PHE A 105      59.928 -14.502 -15.989  1.00 57.77      A    C  
ANISOU  720  CZ  PHE A 105     5399   8537   8013   1282   -755     15  A    C  
ATOM    721  N   CYS A 106      57.539 -11.611 -13.160  1.00 70.53      A    N  
ANISOU  721  N   CYS A 106     7159   9969   9671    665   -792    281  A    N  
ATOM    722  CA  CYS A 106      58.164 -11.959 -11.883  1.00 78.12      A    C  
ANISOU  722  CA  CYS A 106     8164  10807  10712    611   -885    329  A    C  
ATOM    723  C   CYS A 106      59.003 -13.210 -12.080  1.00 82.92      A    C  
ANISOU  723  C   CYS A 106     8768  11381  11357    767   -949    263  A    C  
ATOM    724  O   CYS A 106      58.462 -14.280 -12.358  1.00 78.67      A    O  
ANISOU  724  O   CYS A 106     8333  10760  10798    823   -985    155  A    O  
ATOM    725  CB  CYS A 106      57.103 -12.242 -10.819  1.00 77.85      A    C  
ANISOU  725  CB  CYS A 106     8296  10601  10683    463   -942    313  A    C  
ATOM    726  SG  CYS A 106      55.900 -10.917 -10.558  1.00 76.83      A    S  
ANISOU  726  SG  CYS A 106     8187  10489  10518    293   -864    361  A    S  
ATOM    727  N   GLU A 107      60.317 -13.082 -11.928  1.00 85.70      A    N  
ANISOU  727  N   GLU A 107     8999  11791  11772    838   -966    324  A    N  
ATOM    728  CA  GLU A 107      61.231 -14.171 -12.272  1.00 87.85      A    C  
ANISOU  728  CA  GLU A 107     9231  12060  12087   1020  -1010    261  A    C  
ATOM    729  C   GLU A 107      61.080 -15.447 -11.437  1.00 83.99      A    C  
ANISOU  729  C   GLU A 107     8907  11367  11639   1034  -1148    205  A    C  
ATOM    730  O   GLU A 107      61.273 -16.548 -11.954  1.00 90.89      A    O  
ANISOU  730  O   GLU A 107     9815  12201  12518   1184  -1175    106  A    O  
ATOM    731  CB  GLU A 107      62.685 -13.697 -12.233  1.00 93.14      A    C  
ANISOU  731  CB  GLU A 107     9708  12845  12838   1087  -1000    344  A    C  
ATOM    732  CG  GLU A 107      63.655 -14.669 -12.881  1.00101.38      A    C  
ANISOU  732  CG  GLU A 107    10662  13933  13925   1306  -1003    270  A    C  
ATOM    733  CD  GLU A 107      65.100 -14.275 -12.661  1.00114.84      A    C  
ANISOU  733  CD  GLU A 107    12159  15735  15738   1362  -1010    353  A    C  
ATOM    734  OE1 GLU A 107      65.355 -13.077 -12.403  1.00121.58      A    O  
ANISOU  734  OE1 GLU A 107    12911  16672  16611   1236   -970    464  A    O  
ATOM    735  OE2 GLU A 107      65.978 -15.162 -12.743  1.00114.92      A    O1-
ANISOU  735  OE2 GLU A 107    12106  15736  15823   1530  -1060    305  A    O1-
ATOM    736  N   HIS A 108      60.738 -15.306 -10.160  1.00 72.40      A    N  
ANISOU  736  N   HIS A 108     7555   9761  10192    879  -1231    269  A    N  
ATOM    737  CA  HIS A 108      60.682 -16.460  -9.260  1.00 73.16      A    C  
ANISOU  737  CA  HIS A 108     7823   9653  10321    879  -1366    242  A    C  
ATOM    738  C   HIS A 108      59.287 -16.780  -8.750  1.00 74.13      A    C  
ANISOU  738  C   HIS A 108     8148   9626  10391    728  -1374    206  A    C  
ATOM    739  O   HIS A 108      58.422 -15.909  -8.674  1.00 76.27      A    O  
ANISOU  739  O   HIS A 108     8426   9936  10618    587  -1297    234  A    O  
ATOM    740  CB  HIS A 108      61.602 -16.242  -8.057  1.00 77.90      A    C  
ANISOU  740  CB  HIS A 108     8416  10194  10988    838  -1480    348  A    C  
ATOM    741  CG  HIS A 108      63.014 -15.925  -8.433  1.00 84.57      A    C  
ANISOU  741  CG  HIS A 108     9041  11183  11910    971  -1484    389  A    C  
ATOM    742  CD2 HIS A 108      64.006 -16.710  -8.915  1.00 81.58      A    C  
ANISOU  742  CD2 HIS A 108     8563  10836  11599   1173  -1521    342  A    C  
ATOM    743  ND1 HIS A 108      63.539 -14.653  -8.346  1.00 83.77      A    N  
ANISOU  743  ND1 HIS A 108     8782  11215  11831    896  -1436    486  A    N  
ATOM    744  CE1 HIS A 108      64.796 -14.668  -8.751  1.00 83.62      A    C  
ANISOU  744  CE1 HIS A 108     8566  11310  11895   1035  -1442    502  A    C  
ATOM    745  NE2 HIS A 108      65.102 -15.905  -9.105  1.00 86.24      A    N  
ANISOU  745  NE2 HIS A 108     8923  11587  12256   1212  -1489    413  A    N  
ATOM    746  N   ASP A 109      59.072 -18.043  -8.403  1.00 74.62      A    N  
ANISOU  746  N   ASP A 109     8372   9512  10467    758  -1464    146  A    N  
ATOM    747  CA  ASP A 109      57.924 -18.394  -7.580  1.00 83.09      A    C  
ANISOU  747  CA  ASP A 109     9648  10415  11509    588  -1487    140  A    C  
ATOM    748  C   ASP A 109      58.432 -19.064  -6.304  1.00 85.08      A    C  
ANISOU  748  C   ASP A 109    10053  10481  11792    562  -1626    202  A    C  
ATOM    749  O   ASP A 109      59.450 -19.750  -6.316  1.00 88.82      A    O  
ANISOU  749  O   ASP A 109    10509  10919  12319    717  -1723    197  A    O  
ATOM    750  CB  ASP A 109      56.913 -19.269  -8.331  1.00 89.06      A    C  
ANISOU  750  CB  ASP A 109    10491  11109  12240    601  -1458     11  A    C  
ATOM    751  CG  ASP A 109      57.375 -20.696  -8.481  1.00107.14      A    C  
ANISOU  751  CG  ASP A 109    12880  13263  14566    744  -1558    -65  A    C  
ATOM    752  OD1 ASP A 109      58.599 -20.908  -8.595  1.00114.58      A    O  
ANISOU  752  OD1 ASP A 109    13741  14241  15553    908  -1613    -48  A    O  
ATOM    753  OD2 ASP A 109      56.517 -21.606  -8.490  1.00114.10      A    O1-
ANISOU  753  OD2 ASP A 109    13917  13997  15439    694  -1582   -145  A    O1-
ATOM    754  N   LEU A 110      57.731 -18.834  -5.201  1.00 82.83      A    N  
ANISOU  754  N   LEU A 110     9919  10081  11471    372  -1634    262  A    N  
ATOM    755  CA  LEU A 110      58.149 -19.315  -3.890  1.00 73.90      A    C  
ANISOU  755  CA  LEU A 110     8959   8776  10342    323  -1764    338  A    C  
ATOM    756  C   LEU A 110      58.293 -20.837  -3.813  1.00 73.91      A    C  
ANISOU  756  C   LEU A 110     9120   8591  10370    419  -1874    285  A    C  
ATOM    757  O   LEU A 110      59.039 -21.352  -2.983  1.00 78.34      A    O  
ANISOU  757  O   LEU A 110     9785   9030  10951    462  -2013    345  A    O  
ATOM    758  CB  LEU A 110      57.170 -18.828  -2.824  1.00 70.02      A    C  
ANISOU  758  CB  LEU A 110     8623   8197   9783     93  -1718    396  A    C  
ATOM    759  CG  LEU A 110      57.709 -18.893  -1.402  1.00 69.89      A    C  
ANISOU  759  CG  LEU A 110     8768   8047   9741     24  -1841    501  A    C  
ATOM    760  CD1 LEU A 110      58.926 -17.989  -1.278  1.00 64.46      A    C  
ANISOU  760  CD1 LEU A 110     7916   7491   9087     90  -1902    576  A    C  
ATOM    761  CD2 LEU A 110      56.635 -18.513  -0.401  1.00 67.09      A    C  
ANISOU  761  CD2 LEU A 110     8590   7599   9304   -202  -1770    542  A    C  
ATOM    762  N   ALA A 111      57.576 -21.559  -4.667  1.00 75.40      A    N  
ANISOU  762  N   ALA A 111     9338   8749  10560    454  -1823    171  A    N  
ATOM    763  CA  ALA A 111      57.684 -23.018  -4.692  1.00 76.35      A    C  
ANISOU  763  CA  ALA A 111     9617   8681  10711    550  -1924    108  A    C  
ATOM    764  C   ALA A 111      59.040 -23.449  -5.236  1.00 83.94      A    C  
ANISOU  764  C   ALA A 111    10461   9693  11740    803  -2011     84  A    C  
ATOM    765  O   ALA A 111      59.705 -24.311  -4.663  1.00 89.39      A    O  
ANISOU  765  O   ALA A 111    11268  10228  12468    893  -2151    108  A    O  
ATOM    766  CB  ALA A 111      56.565 -23.627  -5.518  1.00 61.57      A    C  
ANISOU  766  CB  ALA A 111     7798   6768   8827    515  -1852    -17  A    C  
ATOM    767  N   GLY A 112      59.436 -22.838  -6.349  1.00 81.69      A    N  
ANISOU  767  N   GLY A 112     9944   9626  11468    921  -1921     37  A    N  
ATOM    768  CA  GLY A 112      60.701 -23.126  -6.997  1.00 81.88      A    C  
ANISOU  768  CA  GLY A 112     9816   9738  11558   1163  -1963      5  A    C  
ATOM    769  C   GLY A 112      61.913 -22.787  -6.151  1.00 86.42      A    C  
ANISOU  769  C   GLY A 112    10316  10327  12191   1213  -2072    119  A    C  
ATOM    770  O   GLY A 112      62.910 -23.510  -6.187  1.00 89.18      A    O  
ANISOU  770  O   GLY A 112    10636  10632  12616   1403  -2176    103  A    O  
ATOM    771  N   LEU A 113      61.831 -21.687  -5.403  1.00 84.57      A    N  
ANISOU  771  N   LEU A 113    10049  10155  11930   1047  -2055    229  A    N  
ATOM    772  CA  LEU A 113      62.887 -21.304  -4.465  1.00 85.55      A    C  
ANISOU  772  CA  LEU A 113    10124  10280  12102   1057  -2179    342  A    C  
ATOM    773  C   LEU A 113      62.970 -22.279  -3.300  1.00 90.07      A    C  
ANISOU  773  C   LEU A 113    10946  10604  12675   1041  -2356    386  A    C  
ATOM    774  O   LEU A 113      64.053 -22.694  -2.900  1.00 97.38      A    O  
ANISOU  774  O   LEU A 113    11843  11484  13672   1177  -2507    424  A    O  
ATOM    775  CB  LEU A 113      62.633 -19.902  -3.922  1.00 79.71      A    C  
ANISOU  775  CB  LEU A 113     9329   9643  11317    863  -2118    438  A    C  
ATOM    776  CG  LEU A 113      62.755 -18.794  -4.955  1.00 77.51      A    C  
ANISOU  776  CG  LEU A 113     8797   9608  11044    878  -1963    426  A    C  
ATOM    777  CD1 LEU A 113      62.494 -17.467  -4.303  1.00 74.10      A    C  
ANISOU  777  CD1 LEU A 113     8345   9238  10571    685  -1921    521  A    C  
ATOM    778  CD2 LEU A 113      64.135 -18.825  -5.576  1.00 83.25      A    C  
ANISOU  778  CD2 LEU A 113     9289  10471  11871   1082  -1991    421  A    C  
ATOM    779  N   LEU A 114      61.813 -22.637  -2.757  1.00 87.54      A    N  
ANISOU  779  N   LEU A 114    10867  10120  12274    873  -2336    385  A    N  
ATOM    780  CA  LEU A 114      61.743 -23.546  -1.626  1.00 85.78      A    C  
ANISOU  780  CA  LEU A 114    10919   9646  12026    828  -2485    437  A    C  
ATOM    781  C   LEU A 114      62.287 -24.934  -1.952  1.00 92.12      A    C  
ANISOU  781  C   LEU A 114    11795  10306  12899   1039  -2603    371  A    C  
ATOM    782  O   LEU A 114      62.628 -25.686  -1.047  1.00100.41      A    O  
ANISOU  782  O   LEU A 114    13041  11160  13952   1062  -2767    429  A    O  
ATOM    783  CB  LEU A 114      60.306 -23.633  -1.100  1.00 83.77      A    C  
ANISOU  783  CB  LEU A 114    10894   9261  11675    593  -2400    440  A    C  
ATOM    784  CG  LEU A 114      59.999 -22.848   0.183  1.00 82.47      A    C  
ANISOU  784  CG  LEU A 114    10852   9058  11423    382  -2408    558  A    C  
ATOM    785  CD1 LEU A 114      60.916 -21.645   0.348  1.00 79.56      A    C  
ANISOU  785  CD1 LEU A 114    10281   8871  11077    403  -2434    628  A    C  
ATOM    786  CD2 LEU A 114      58.536 -22.439   0.239  1.00 73.05      A    C  
ANISOU  786  CD2 LEU A 114     9740   7861  10154    163  -2236    535  A    C  
ATOM    787  N   SER A 115      62.379 -25.264  -3.239  1.00 93.96      A    N  
ANISOU  787  N   SER A 115    11885  10634  13181   1198  -2524    251  A    N  
ATOM    788  CA  SER A 115      62.847 -26.585  -3.670  1.00 97.78      A    C  
ANISOU  788  CA  SER A 115    12437  10983  13732   1414  -2619    166  A    C  
ATOM    789  C   SER A 115      64.321 -26.604  -4.062  1.00 97.36      A    C  
ANISOU  789  C   SER A 115    12158  11047  13788   1672  -2694    159  A    C  
ATOM    790  O   SER A 115      65.014 -27.592  -3.838  1.00104.54      A    O  
ANISOU  790  O   SER A 115    13146  11810  14766   1847  -2843    147  A    O  
ATOM    791  CB  SER A 115      62.010 -27.100  -4.837  1.00101.34      A    C  
ANISOU  791  CB  SER A 115    12905  11437  14163   1441  -2496     18  A    C  
ATOM    792  OG  SER A 115      60.641 -27.104  -4.496  1.00109.91      A    O  
ANISOU  792  OG  SER A 115    14172  12420  15168   1202  -2428     19  A    O  
ATOM    793  N   ASN A 116      64.795 -25.521  -4.666  1.00 94.88      A    N  
ANISOU  793  N   ASN A 116    11560  10995  13496   1698  -2586    167  A    N  
ATOM    794  CA  ASN A 116      66.206 -25.422  -5.001  1.00100.81      A    C  
ANISOU  794  CA  ASN A 116    12062  11880  14360   1920  -2638    170  A    C  
ATOM    795  C   ASN A 116      67.012 -25.502  -3.713  1.00109.82      A    C  
ANISOU  795  C   ASN A 116    13261  12913  15554   1924  -2851    291  A    C  
ATOM    796  O   ASN A 116      66.949 -24.599  -2.874  1.00114.09      A    O  
ANISOU  796  O   ASN A 116    13805  13490  16054   1744  -2879    402  A    O  
ATOM    797  CB  ASN A 116      66.508 -24.125  -5.765  1.00 96.14      A    C  
ANISOU  797  CB  ASN A 116    11169  11584  13775   1899  -2474    180  A    C  
ATOM    798  CG  ASN A 116      67.881 -24.139  -6.446  1.00 99.89      A    C  
ANISOU  798  CG  ASN A 116    11359  12221  14373   2147  -2473    150  A    C  
ATOM    799  ND2 ASN A 116      68.133 -23.141  -7.285  1.00 92.37      A    N  
ANISOU  799  ND2 ASN A 116    10154  11521  13423   2144  -2308    147  A    N  
ATOM    800  OD1 ASN A 116      68.700 -25.034  -6.219  1.00108.03      A    O  
ANISOU  800  OD1 ASN A 116    12398  13150  15499   2340  -2615    131  A    O  
ATOM    801  N   VAL A 117      67.750 -26.596  -3.551  1.00111.27      A    N  
ANISOU  801  N   VAL A 117    13502  12953  15822   2134  -3009    266  A    N  
ATOM    802  CA  VAL A 117      68.549 -26.811  -2.349  1.00117.28      A    C  
ANISOU  802  CA  VAL A 117    14333  13592  16635   2167  -3244    377  A    C  
ATOM    803  C   VAL A 117      69.740 -25.851  -2.260  1.00120.64      A    C  
ANISOU  803  C   VAL A 117    14441  14237  17161   2224  -3284    444  A    C  
ATOM    804  O   VAL A 117      70.354 -25.709  -1.202  1.00117.56      A    O  
ANISOU  804  O   VAL A 117    14081  13787  16800   2201  -3477    550  A    O  
ATOM    805  CB  VAL A 117      69.034 -28.268  -2.256  1.00117.62      A    C  
ANISOU  805  CB  VAL A 117    14521  13415  16753   2399  -3412    329  A    C  
ATOM    806  CG1 VAL A 117      67.841 -29.205  -2.142  1.00119.29      A    C  
ANISOU  806  CG1 VAL A 117    15082  13377  16867   2301  -3396    284  A    C  
ATOM    807  CG2 VAL A 117      69.882 -28.627  -3.467  1.00114.03      A    C  
ANISOU  807  CG2 VAL A 117    13806  13097  16423   2689  -3346    207  A    C  
ATOM    808  N   LEU A 118      70.049 -25.186  -3.371  1.00125.91      A    N  
ANISOU  808  N   LEU A 118    14811  15156  17875   2289  -3104    384  A    N  
ATOM    809  CA  LEU A 118      71.137 -24.208  -3.424  1.00127.95      A    C  
ANISOU  809  CA  LEU A 118    14739  15639  18236   2323  -3107    443  A    C  
ATOM    810  C   LEU A 118      70.704 -22.811  -2.970  1.00120.68      A    C  
ANISOU  810  C   LEU A 118    13785  14831  17235   2049  -3037    539  A    C  
ATOM    811  O   LEU A 118      71.528 -21.901  -2.880  1.00119.63      A    O  
ANISOU  811  O   LEU A 118    13407  14868  17181   2029  -3051    601  A    O  
ATOM    812  CB  LEU A 118      71.708 -24.127  -4.844  1.00132.95      A    C  
ANISOU  812  CB  LEU A 118    15070  16491  18952   2516  -2929    341  A    C  
ATOM    813  CG  LEU A 118      72.497 -25.334  -5.355  1.00136.16      A    C  
ANISOU  813  CG  LEU A 118    15418  16841  19477   2832  -2993    242  A    C  
ATOM    814  CD1 LEU A 118      72.267 -25.535  -6.849  1.00137.68      A    C  
ANISOU  814  CD1 LEU A 118    15506  17162  19645   2961  -2761    100  A    C  
ATOM    815  CD2 LEU A 118      73.982 -25.191  -5.033  1.00132.97      A    C  
ANISOU  815  CD2 LEU A 118    14735  16535  19252   2992  -3131    294  A    C  
ATOM    816  N   VAL A 119      69.413 -22.641  -2.698  1.00116.11      A    N  
ANISOU  816  N   VAL A 119    13449  14157  16509   1839  -2959    546  A    N  
ATOM    817  CA  VAL A 119      68.877 -21.347  -2.276  1.00106.24      A    C  
ANISOU  817  CA  VAL A 119    12196  12994  15174   1585  -2881    625  A    C  
ATOM    818  C   VAL A 119      68.769 -21.286  -0.759  1.00 99.03      A    C  
ANISOU  818  C   VAL A 119    11515  11910  14201   1432  -3068    733  A    C  
ATOM    819  O   VAL A 119      68.280 -22.221  -0.132  1.00101.42      A    O  
ANISOU  819  O   VAL A 119    12102  11989  14442   1420  -3167    735  A    O  
ATOM    820  CB  VAL A 119      67.494 -21.075  -2.906  1.00 96.27      A    C  
ANISOU  820  CB  VAL A 119    11036  11751  13790   1445  -2669    566  A    C  
ATOM    821  CG1 VAL A 119      66.851 -19.848  -2.280  1.00 92.24      A    C  
ANISOU  821  CG1 VAL A 119    10574  11283  13189   1186  -2610    649  A    C  
ATOM    822  CG2 VAL A 119      67.629 -20.901  -4.407  1.00 92.50      A    C  
ANISOU  822  CG2 VAL A 119    10323  11473  13349   1575  -2482    472  A    C  
ATOM    823  N   LYS A 120      69.227 -20.188  -0.168  1.00 90.88      A    N  
ANISOU  823  N   LYS A 120    10375  10977  13178   1310  -3116    823  A    N  
ATOM    824  CA  LYS A 120      69.258 -20.101   1.287  1.00106.29      A    C  
ANISOU  824  CA  LYS A 120    12544  12775  15065   1179  -3310    923  A    C  
ATOM    825  C   LYS A 120      68.593 -18.841   1.829  1.00108.52      A    C  
ANISOU  825  C   LYS A 120    12891  13105  15236    917  -3226    983  A    C  
ATOM    826  O   LYS A 120      68.763 -17.743   1.288  1.00113.04      A    O  
ANISOU  826  O   LYS A 120    13235  13871  15844    860  -3102    987  A    O  
ATOM    827  CB  LYS A 120      70.696 -20.239   1.811  1.00115.98      A    C  
ANISOU  827  CB  LYS A 120    13628  14017  16423   1318  -3552    979  A    C  
ATOM    828  CG  LYS A 120      71.333 -21.598   1.523  1.00113.68      A    C  
ANISOU  828  CG  LYS A 120    13328  13629  16237   1587  -3674    927  A    C  
ATOM    829  CD  LYS A 120      72.680 -21.752   2.211  1.00113.78      A    C  
ANISOU  829  CD  LYS A 120    13223  13633  16377   1716  -3944    991  A    C  
ATOM    830  CE  LYS A 120      73.181 -23.195   2.107  1.00116.83      A    C  
ANISOU  830  CE  LYS A 120    13670  13871  16851   1982  -4090    945  A    C  
ATOM    831  NZ  LYS A 120      74.274 -23.502   3.072  1.00114.53      A    N1+
ANISOU  831  NZ  LYS A 120    13368  13499  16648   2089  -4404   1023  A    N1+
ATOM    832  N   PHE A 121      67.836 -19.017   2.908  1.00104.20      A    N  
ANISOU  832  N   PHE A 121    12666  12373  14551    761  -3288   1031  A    N  
ATOM    833  CA  PHE A 121      67.055 -17.935   3.487  1.00103.08      A    C  
ANISOU  833  CA  PHE A 121    12632  12246  14287    516  -3196   1075  A    C  
ATOM    834  C   PHE A 121      67.579 -17.510   4.854  1.00 96.03      A    C  
ANISOU  834  C   PHE A 121    11870  11276  13343    413  -3403   1174  A    C  
ATOM    835  O   PHE A 121      67.468 -18.257   5.829  1.00 95.39      A    O  
ANISOU  835  O   PHE A 121    12067  10997  13178    396  -3556   1218  A    O  
ATOM    836  CB  PHE A 121      65.593 -18.367   3.644  1.00110.81      A    C  
ANISOU  836  CB  PHE A 121    13890  13085  15129    389  -3061   1043  A    C  
ATOM    837  CG  PHE A 121      64.812 -18.391   2.358  1.00117.01      A    C  
ANISOU  837  CG  PHE A 121    14556  13969  15933    418  -2831    946  A    C  
ATOM    838  CD1 PHE A 121      64.563 -17.212   1.657  1.00122.64      A    C  
ANISOU  838  CD1 PHE A 121    15068  14874  16656    348  -2658    928  A    C  
ATOM    839  CD2 PHE A 121      64.296 -19.586   1.869  1.00113.20      A    C  
ANISOU  839  CD2 PHE A 121    14182  13377  15452    508  -2798    873  A    C  
ATOM    840  CE1 PHE A 121      63.835 -17.228   0.478  1.00120.63      A    C  
ANISOU  840  CE1 PHE A 121    14717  14710  16406    378  -2464    842  A    C  
ATOM    841  CE2 PHE A 121      63.569 -19.612   0.697  1.00114.34      A    C  
ANISOU  841  CE2 PHE A 121    14228  13610  15606    531  -2606    778  A    C  
ATOM    842  CZ  PHE A 121      63.335 -18.431  -0.001  1.00120.27      A    C  
ANISOU  842  CZ  PHE A 121    14775  14562  16359    469  -2442    763  A    C  
ATOM    843  N   THR A 122      68.138 -16.308   4.940  1.00 90.35      A    N  
ANISOU  843  N   THR A 122    10964  10702  12664    337  -3414   1212  A    N  
ATOM    844  CA  THR A 122      68.438 -15.747   6.252  1.00 85.18      A    C  
ANISOU  844  CA  THR A 122    10463   9972  11930    199  -3590   1296  A    C  
ATOM    845  C   THR A 122      67.115 -15.386   6.925  1.00 92.69      A    C  
ANISOU  845  C   THR A 122    11715  10814  12688    -16  -3464   1305  A    C  
ATOM    846  O   THR A 122      66.142 -15.043   6.253  1.00 96.49      A    O  
ANISOU  846  O   THR A 122    12171  11354  13136    -84  -3225   1252  A    O  
ATOM    847  CB  THR A 122      69.410 -14.532   6.199  1.00 89.79      A    C  
ANISOU  847  CB  THR A 122    10771  10730  12616    161  -3648   1330  A    C  
ATOM    848  CG2 THR A 122      69.022 -13.555   5.123  1.00 88.60      A    C  
ANISOU  848  CG2 THR A 122    10396  10762  12506    106  -3392   1288  A    C  
ATOM    849  OG1 THR A 122      69.386 -13.842   7.453  1.00105.74      A    O  
ANISOU  849  OG1 THR A 122    12988  12669  14520    -18  -3777   1395  A    O  
ATOM    850  N   LEU A 123      67.072 -15.502   8.246  1.00 94.92      A    N  
ANISOU  850  N   LEU A 123    12286  10938  12840   -117  -3624   1369  A    N  
ATOM    851  CA  LEU A 123      65.850 -15.252   8.997  1.00 88.50      A    C  
ANISOU  851  CA  LEU A 123    11781  10009  11835   -316  -3504   1379  A    C  
ATOM    852  C   LEU A 123      65.277 -13.850   8.763  1.00 89.84      A    C  
ANISOU  852  C   LEU A 123    11854  10307  11974   -472  -3308   1357  A    C  
ATOM    853  O   LEU A 123      64.064 -13.656   8.805  1.00 97.56      A    O  
ANISOU  853  O   LEU A 123    12976  11246  12846   -595  -3109   1327  A    O  
ATOM    854  CB  LEU A 123      66.100 -15.465  10.483  1.00 82.80      A    C  
ANISOU  854  CB  LEU A 123    11372   9116  10971   -395  -3726   1460  A    C  
ATOM    855  CG  LEU A 123      65.005 -14.909  11.381  1.00 80.46      A    C  
ANISOU  855  CG  LEU A 123    11374   8728  10468   -619  -3602   1476  A    C  
ATOM    856  CD1 LEU A 123      63.846 -15.883  11.459  1.00 78.74      A    C  
ANISOU  856  CD1 LEU A 123    11407   8363  10150   -657  -3460   1458  A    C  
ATOM    857  CD2 LEU A 123      65.563 -14.638  12.747  1.00 84.16      A    C  
ANISOU  857  CD2 LEU A 123    12069   9098  10811   -700  -3836   1553  A    C  
ATOM    858  N   SER A 124      66.144 -12.875   8.520  1.00 83.78      A    N  
ANISOU  858  N   SER A 124    10839   9686  11306   -468  -3363   1371  A    N  
ATOM    859  CA  SER A 124      65.688 -11.509   8.281  1.00 83.03      A    C  
ANISOU  859  CA  SER A 124    10653   9702  11192   -608  -3192   1355  A    C  
ATOM    860  C   SER A 124      65.086 -11.373   6.885  1.00 87.65      A    C  
ANISOU  860  C   SER A 124    11026  10419  11857   -552  -2943   1288  A    C  
ATOM    861  O   SER A 124      64.365 -10.412   6.596  1.00 82.30      A    O  
ANISOU  861  O   SER A 124    10318   9808  11145   -660  -2761   1266  A    O  
ATOM    862  CB  SER A 124      66.844 -10.529   8.421  1.00 74.00      A    C  
ANISOU  862  CB  SER A 124     9309   8665  10141   -628  -3335   1394  A    C  
ATOM    863  OG  SER A 124      67.674 -10.602   7.278  1.00 76.20      A    O  
ANISOU  863  OG  SER A 124     9237   9104  10610   -476  -3323   1377  A    O  
ATOM    864  N   GLU A 125      65.415 -12.330   6.019  1.00 92.40      A    N  
ANISOU  864  N   GLU A 125    11486  11058  12564   -373  -2946   1254  A    N  
ATOM    865  CA  GLU A 125      64.831 -12.414   4.686  1.00 85.44      A    C  
ANISOU  865  CA  GLU A 125    10437  10286  11739   -302  -2729   1184  A    C  
ATOM    866  C   GLU A 125      63.500 -13.162   4.742  1.00 83.92      A    C  
ANISOU  866  C   GLU A 125    10476   9970  11442   -347  -2604   1138  A    C  
ATOM    867  O   GLU A 125      62.543 -12.787   4.064  1.00 90.70      A    O  
ANISOU  867  O   GLU A 125    11293  10890  12280   -396  -2400   1087  A    O  
ATOM    868  CB  GLU A 125      65.806 -13.054   3.695  1.00 92.67      A    C  
ANISOU  868  CB  GLU A 125    11095  11305  12811    -88  -2779   1158  A    C  
ATOM    869  CG  GLU A 125      66.861 -12.069   3.173  1.00108.55      A    C  
ANISOU  869  CG  GLU A 125    12792  13502  14948    -61  -2790   1186  A    C  
ATOM    870  CD  GLU A 125      67.989 -12.727   2.381  1.00118.54      A    C  
ANISOU  870  CD  GLU A 125    13802  14867  16373    155  -2858   1167  A    C  
ATOM    871  OE1 GLU A 125      68.078 -13.977   2.371  1.00120.07      A    O  
ANISOU  871  OE1 GLU A 125    14077  14964  16581    296  -2938   1135  A    O  
ATOM    872  OE2 GLU A 125      68.793 -11.983   1.774  1.00120.16      A    O1-
ANISOU  872  OE2 GLU A 125    13724  15240  16690    183  -2826   1183  A    O1-
ATOM    873  N   ILE A 126      63.425 -14.196   5.573  1.00 75.49      A    N  
ANISOU  873  N   ILE A 126     9654   8722  10306   -340  -2730   1159  A    N  
ATOM    874  CA  ILE A 126      62.142 -14.843   5.831  1.00 75.18      A    C  
ANISOU  874  CA  ILE A 126     9861   8546  10159   -426  -2614   1128  A    C  
ATOM    875  C   ILE A 126      61.138 -13.851   6.414  1.00 75.50      A    C  
ANISOU  875  C   ILE A 126    10031   8577  10078   -630  -2468   1135  A    C  
ATOM    876  O   ILE A 126      59.960 -13.886   6.072  1.00 76.29      A    O  
ANISOU  876  O   ILE A 126    10176   8669  10140   -699  -2279   1083  A    O  
ATOM    877  CB  ILE A 126      62.264 -16.042   6.794  1.00 75.96      A    C  
ANISOU  877  CB  ILE A 126    10241   8432  10187   -410  -2782   1170  A    C  
ATOM    878  CG1 ILE A 126      63.210 -17.101   6.223  1.00 83.73      A    C  
ANISOU  878  CG1 ILE A 126    11111   9406  11297   -188  -2928   1156  A    C  
ATOM    879  CG2 ILE A 126      60.901 -16.656   7.050  1.00 66.10      A    C  
ANISOU  879  CG2 ILE A 126     9238   7045   8832   -524  -2639   1143  A    C  
ATOM    880  CD1 ILE A 126      63.038 -18.468   6.853  1.00 79.32      A    C  
ANISOU  880  CD1 ILE A 126    10836   8622  10681   -156  -3044   1177  A    C  
ATOM    881  N   LYS A 127      61.602 -12.974   7.298  1.00 73.66      A    N  
ANISOU  881  N   LYS A 127     9855   8342   9789   -724  -2559   1193  A    N  
ATOM    882  CA  LYS A 127      60.713 -12.016   7.939  1.00 70.50      A    C  
ANISOU  882  CA  LYS A 127     9597   7921   9269   -909  -2428   1195  A    C  
ATOM    883  C   LYS A 127      60.121 -11.117   6.882  1.00 74.63      A    C  
ANISOU  883  C   LYS A 127     9899   8599   9857   -920  -2217   1139  A    C  
ATOM    884  O   LYS A 127      58.929 -10.805   6.906  1.00 82.95      A    O  
ANISOU  884  O   LYS A 127    11035   9636  10845  -1021  -2033   1101  A    O  
ATOM    885  CB  LYS A 127      61.453 -11.186   8.992  1.00 70.78      A    C  
ANISOU  885  CB  LYS A 127     9719   7934   9241   -994  -2584   1258  A    C  
ATOM    886  CG  LYS A 127      61.807 -11.968  10.237  1.00 85.33      A    C  
ANISOU  886  CG  LYS A 127    11851   9601  10970  -1017  -2784   1318  A    C  
ATOM    887  CD  LYS A 127      62.159 -11.070  11.421  1.00 94.71      A    C  
ANISOU  887  CD  LYS A 127    13202  10743  12040  -1147  -2901   1366  A    C  
ATOM    888  CE  LYS A 127      62.506 -11.924  12.642  1.00100.38      A    C  
ANISOU  888  CE  LYS A 127    14231  11281  12626  -1160  -3113   1432  A    C  
ATOM    889  NZ  LYS A 127      62.701 -11.156  13.903  1.00100.72      A    N1+
ANISOU  889  NZ  LYS A 127    14499  11256  12512  -1299  -3224   1473  A    N1+
ATOM    890  N   ARG A 128      60.962 -10.714   5.938  1.00 75.25      A    N  
ANISOU  890  N   ARG A 128     9693   8831  10068   -810  -2244   1136  A    N  
ATOM    891  CA  ARG A 128      60.540  -9.791   4.902  1.00 69.55      A    C  
ANISOU  891  CA  ARG A 128     8761   8260   9404   -812  -2064   1097  A    C  
ATOM    892  C   ARG A 128      59.567 -10.446   3.922  1.00 68.07      A    C  
ANISOU  892  C   ARG A 128     8529   8098   9238   -752  -1903   1023  A    C  
ATOM    893  O   ARG A 128      58.613  -9.823   3.478  1.00 62.84      A    O  
ANISOU  893  O   ARG A 128     7829   7489   8558   -811  -1729    984  A    O  
ATOM    894  CB  ARG A 128      61.743  -9.240   4.161  1.00 60.37      A    C  
ANISOU  894  CB  ARG A 128     7317   7251   8370   -717  -2130   1122  A    C  
ATOM    895  CG  ARG A 128      61.385  -8.127   3.201  1.00 61.83      A    C  
ANISOU  895  CG  ARG A 128     7314   7582   8598   -737  -1955   1103  A    C  
ATOM    896  CD  ARG A 128      61.059  -6.850   3.943  1.00 68.91      A    C  
ANISOU  896  CD  ARG A 128     8305   8451   9426   -899  -1918   1131  A    C  
ATOM    897  NE  ARG A 128      60.642  -5.823   2.999  1.00 78.18      A    N  
ANISOU  897  NE  ARG A 128     9318   9748  10640   -910  -1751   1116  A    N  
ATOM    898  CZ  ARG A 128      59.381  -5.437   2.814  1.00 73.58      A    C  
ANISOU  898  CZ  ARG A 128     8803   9154  10001   -967  -1580   1073  A    C  
ATOM    899  NH1 ARG A 128      58.398  -5.971   3.529  1.00 71.94      A    N1+
ANISOU  899  NH1 ARG A 128     8812   8824   9698  -1032  -1536   1038  A    N1+
ATOM    900  NH2 ARG A 128      59.106  -4.502   1.916  1.00 65.17      A    N  
ANISOU  900  NH2 ARG A 128     7586   8199   8977   -959  -1452   1068  A    N  
ATOM    901  N   VAL A 129      59.811 -11.706   3.590  1.00 69.42      A    N  
ANISOU  901  N   VAL A 129     8705   8223   9448   -633  -1972    999  A    N  
ATOM    902  CA  VAL A 129      58.909 -12.436   2.716  1.00 69.77      A    C  
ANISOU  902  CA  VAL A 129     8729   8271   9508   -582  -1845    922  A    C  
ATOM    903  C   VAL A 129      57.519 -12.520   3.313  1.00 68.99      A    C  
ANISOU  903  C   VAL A 129     8839   8063   9311   -733  -1722    897  A    C  
ATOM    904  O   VAL A 129      56.533 -12.277   2.616  1.00 71.56      A    O  
ANISOU  904  O   VAL A 129     9095   8450   9646   -758  -1560    837  A    O  
ATOM    905  CB  VAL A 129      59.396 -13.860   2.450  1.00 73.60      A    C  
ANISOU  905  CB  VAL A 129     9239   8684  10042   -439  -1958    899  A    C  
ATOM    906  CG1 VAL A 129      58.228 -14.741   2.032  1.00 61.45      A    C  
ANISOU  906  CG1 VAL A 129     7795   7071   8481   -452  -1848    822  A    C  
ATOM    907  CG2 VAL A 129      60.493 -13.851   1.397  1.00 78.18      A    C  
ANISOU  907  CG2 VAL A 129     9551   9413  10740   -259  -2003    886  A    C  
ATOM    908  N   MET A 130      57.438 -12.870   4.595  1.00 65.84      A    N  
ANISOU  908  N   MET A 130     8694   7505   8816   -832  -1798    943  A    N  
ATOM    909  CA  MET A 130      56.143 -13.011   5.262  1.00 68.37      A    C  
ANISOU  909  CA  MET A 130     9225   7716   9038   -985  -1668    925  A    C  
ATOM    910  C   MET A 130      55.472 -11.666   5.430  1.00 70.21      A    C  
ANISOU  910  C   MET A 130     9425   8022   9231  -1101  -1520    917  A    C  
ATOM    911  O   MET A 130      54.245 -11.560   5.410  1.00 74.86      A    O  
ANISOU  911  O   MET A 130    10058   8596   9790  -1191  -1351    870  A    O  
ATOM    912  CB  MET A 130      56.278 -13.686   6.626  1.00 61.25      A    C  
ANISOU  912  CB  MET A 130     8624   6624   8023  -1065  -1781    987  A    C  
ATOM    913  CG  MET A 130      56.473 -15.173   6.539  1.00 66.81      A    C  
ANISOU  913  CG  MET A 130     9426   7207   8751   -982  -1883    984  A    C  
ATOM    914  SD  MET A 130      55.182 -15.957   5.569  1.00 79.46      A    S  
ANISOU  914  SD  MET A 130    10982   8801  10408   -988  -1704    885  A    S  
ATOM    915  CE  MET A 130      53.731 -15.525   6.530  1.00 65.88      A    C  
ANISOU  915  CE  MET A 130     9464   7001   8565  -1223  -1509    887  A    C  
ATOM    916  N   GLN A 131      56.282 -10.634   5.594  1.00 62.21      A    N  
ANISOU  916  N   GLN A 131     8329   7084   8225  -1098  -1586    961  A    N  
ATOM    917  CA  GLN A 131      55.743  -9.299   5.739  1.00 59.69      A    C  
ANISOU  917  CA  GLN A 131     7983   6823   7874  -1195  -1459    953  A    C  
ATOM    918  C   GLN A 131      55.076  -8.818   4.447  1.00 63.72      A    C  
ANISOU  918  C   GLN A 131     8269   7473   8470  -1143  -1300    893  A    C  
ATOM    919  O   GLN A 131      53.951  -8.331   4.469  1.00 67.30      A    O  
ANISOU  919  O   GLN A 131     8747   7928   8894  -1221  -1140    852  A    O  
ATOM    920  CB  GLN A 131      56.839  -8.345   6.162  1.00 54.90      A    C  
ANISOU  920  CB  GLN A 131     7338   6255   7268  -1206  -1584   1013  A    C  
ATOM    921  CG  GLN A 131      56.318  -7.010   6.552  1.00 62.85      A    C  
ANISOU  921  CG  GLN A 131     8381   7278   8223  -1319  -1474   1008  A    C  
ATOM    922  CD  GLN A 131      57.398  -6.141   7.121  1.00 68.04      A    C  
ANISOU  922  CD  GLN A 131     9039   7943   8871  -1354  -1618   1065  A    C  
ATOM    923  NE2 GLN A 131      57.170  -5.620   8.328  1.00 69.67      A    N  
ANISOU  923  NE2 GLN A 131     9473   8046   8951  -1482  -1628   1078  A    N  
ATOM    924  OE1 GLN A 131      58.433  -5.940   6.488  1.00 65.21      A    O  
ANISOU  924  OE1 GLN A 131     8480   7682   8616  -1269  -1719   1094  A    O  
ATOM    925  N   MET A 132      55.772  -8.956   3.323  1.00 66.58      A    N  
ANISOU  925  N   MET A 132     8413   7952   8933  -1004  -1347    886  A    N  
ATOM    926  CA  MET A 132      55.219  -8.577   2.024  1.00 62.36      A    C  
ANISOU  926  CA  MET A 132     7678   7552   8466   -939  -1216    833  A    C  
ATOM    927  C   MET A 132      53.962  -9.378   1.698  1.00 71.03      A    C  
ANISOU  927  C   MET A 132     8824   8607   9556   -955  -1106    757  A    C  
ATOM    928  O   MET A 132      52.984  -8.828   1.190  1.00 68.27      A    O  
ANISOU  928  O   MET A 132     8402   8317   9218   -981   -968    711  A    O  
ATOM    929  CB  MET A 132      56.259  -8.757   0.915  1.00 47.79      A    C  
ANISOU  929  CB  MET A 132     5617   5831   6712   -783  -1286    839  A    C  
ATOM    930  CG  MET A 132      57.330  -7.682   0.930  1.00 49.68      A    C  
ANISOU  930  CG  MET A 132     5736   6154   6986   -779  -1346    907  A    C  
ATOM    931  SD  MET A 132      58.511  -7.852  -0.413  1.00 73.15      A    S  
ANISOU  931  SD  MET A 132     8436   9289  10067   -602  -1388    915  A    S  
ATOM    932  CE  MET A 132      59.219  -9.443  -0.026  1.00 57.90      A    C  
ANISOU  932  CE  MET A 132     6585   7258   8156   -504  -1552    905  A    C  
ATOM    933  N   LEU A 133      53.995 -10.676   1.991  1.00 66.04      A    N  
ANISOU  933  N   LEU A 133     8314   7865   8912   -939  -1177    744  A    N  
ATOM    934  CA  LEU A 133      52.842 -11.547   1.781  1.00 63.94      A    C  
ANISOU  934  CA  LEU A 133     8111   7537   8646   -975  -1088    674  A    C  
ATOM    935  C   LEU A 133      51.629 -11.121   2.607  1.00 68.83      A    C  
ANISOU  935  C   LEU A 133     8863   8089   9202  -1139   -948    662  A    C  
ATOM    936  O   LEU A 133      50.540 -10.936   2.062  1.00 70.64      A    O  
ANISOU  936  O   LEU A 133     9010   8367   9463  -1166   -814    598  A    O  
ATOM    937  CB  LEU A 133      53.211 -12.999   2.087  1.00 63.91      A    C  
ANISOU  937  CB  LEU A 133     8247   7399   8637   -938  -1205    676  A    C  
ATOM    938  CG  LEU A 133      52.106 -14.037   1.959  1.00 63.71      A    C  
ANISOU  938  CG  LEU A 133     8312   7280   8616   -992  -1132    609  A    C  
ATOM    939  CD1 LEU A 133      52.678 -15.336   1.484  1.00 67.92      A    C  
ANISOU  939  CD1 LEU A 133     8862   7750   9194   -872  -1253    585  A    C  
ATOM    940  CD2 LEU A 133      51.432 -14.215   3.284  1.00 76.75      A    C  
ANISOU  940  CD2 LEU A 133    10205   8779  10176  -1165  -1081    644  A    C  
ATOM    941  N   LEU A 134      51.818 -10.965   3.916  1.00 65.35      A    N  
ANISOU  941  N   LEU A 134     8624   7538   8669  -1243   -980    721  A    N  
ATOM    942  CA  LEU A 134      50.743 -10.514   4.803  1.00 59.23      A    C  
ANISOU  942  CA  LEU A 134     7989   6698   7818  -1398   -834    710  A    C  
ATOM    943  C   LEU A 134      50.214  -9.138   4.443  1.00 60.10      A    C  
ANISOU  943  C   LEU A 134     7959   6923   7953  -1412   -706    684  A    C  
ATOM    944  O   LEU A 134      49.036  -8.842   4.651  1.00 58.38      A    O  
ANISOU  944  O   LEU A 134     7763   6696   7724  -1498   -545    638  A    O  
ATOM    945  CB  LEU A 134      51.195 -10.525   6.264  1.00 54.09      A    C  
ANISOU  945  CB  LEU A 134     7596   5914   7041  -1495   -906    781  A    C  
ATOM    946  CG  LEU A 134      51.164 -11.950   6.807  1.00 53.25      A    C  
ANISOU  946  CG  LEU A 134     7690   5654   6889  -1528   -970    801  A    C  
ATOM    947  CD1 LEU A 134      51.850 -12.058   8.156  1.00 48.13      A    C  
ANISOU  947  CD1 LEU A 134     7302   4876   6109  -1593  -1092    884  A    C  
ATOM    948  CD2 LEU A 134      49.725 -12.440   6.867  1.00 59.44      A    C  
ANISOU  948  CD2 LEU A 134     8532   6384   7670  -1639   -786    744  A    C  
ATOM    949  N   ASN A 135      51.084  -8.286   3.916  1.00 59.32      A    N  
ANISOU  949  N   ASN A 135     7715   6930   7893  -1327   -775    714  A    N  
ATOM    950  CA  ASN A 135      50.653  -6.960   3.498  1.00 54.88      A    C  
ANISOU  950  CA  ASN A 135     7025   6467   7360  -1328   -667    697  A    C  
ATOM    951  C   ASN A 135      49.767  -7.052   2.255  1.00 59.81      A    C  
ANISOU  951  C   ASN A 135     7464   7193   8070  -1261   -568    625  A    C  
ATOM    952  O   ASN A 135      48.889  -6.222   2.045  1.00 68.67      A    O  
ANISOU  952  O   ASN A 135     8519   8362   9211  -1284   -442    591  A    O  
ATOM    953  CB  ASN A 135      51.857  -6.054   3.254  1.00 50.68      A    C  
ANISOU  953  CB  ASN A 135     6395   6010   6849  -1269   -769    756  A    C  
ATOM    954  CG  ASN A 135      51.506  -4.580   3.344  1.00 62.42      A    C  
ANISOU  954  CG  ASN A 135     7849   7537   8330  -1313   -675    759  A    C  
ATOM    955  ND2 ASN A 135      52.103  -3.775   2.474  1.00 55.57      A    N  
ANISOU  955  ND2 ASN A 135     6807   6781   7527  -1237   -700    786  A    N  
ATOM    956  OD1 ASN A 135      50.708  -4.170   4.187  1.00 71.30      A    O  
ANISOU  956  OD1 ASN A 135     9110   8588   9391  -1414   -574    737  A    O  
ATOM    957  N   GLY A 136      50.001  -8.078   1.442  1.00 62.61      A    N  
ANISOU  957  N   GLY A 136     7741   7573   8474  -1172   -633    600  A    N  
ATOM    958  CA  GLY A 136      49.220  -8.307   0.240  1.00 58.09      A    C  
ANISOU  958  CA  GLY A 136     7009   7090   7971  -1105   -567    526  A    C  
ATOM    959  C   GLY A 136      47.836  -8.809   0.580  1.00 64.55      A    C  
ANISOU  959  C   GLY A 136     7893   7839   8793  -1207   -451    461  A    C  
ATOM    960  O   GLY A 136      46.852  -8.370  -0.012  1.00 68.15      A    O  
ANISOU  960  O   GLY A 136     8229   8368   9298  -1204   -350    404  A    O  
ATOM    961  N   LEU A 137      47.755  -9.732   1.535  1.00 58.88      A    N  
ANISOU  961  N   LEU A 137     7364   6981   8027  -1299   -467    471  A    N  
ATOM    962  CA  LEU A 137      46.459 -10.181   2.038  1.00 58.90      A    C  
ANISOU  962  CA  LEU A 137     7446   6906   8028  -1426   -338    420  A    C  
ATOM    963  C   LEU A 137      45.684  -9.048   2.715  1.00 65.18      A    C  
ANISOU  963  C   LEU A 137     8261   7711   8795  -1518   -187    417  A    C  
ATOM    964  O   LEU A 137      44.461  -8.989   2.623  1.00 73.59      A    O  
ANISOU  964  O   LEU A 137     9265   8791   9906  -1577    -50    354  A    O  
ATOM    965  CB  LEU A 137      46.598 -11.376   2.993  1.00 50.03      A    C  
ANISOU  965  CB  LEU A 137     6550   5615   6843  -1516   -381    450  A    C  
ATOM    966  CG  LEU A 137      47.119 -12.663   2.356  1.00 58.30      A    C  
ANISOU  966  CG  LEU A 137     7596   6624   7931  -1433   -512    434  A    C  
ATOM    967  CD1 LEU A 137      47.377 -13.728   3.400  1.00 58.79      A    C  
ANISOU  967  CD1 LEU A 137     7911   6503   7922  -1516   -571    482  A    C  
ATOM    968  CD2 LEU A 137      46.152 -13.167   1.304  1.00 55.28      A    C  
ANISOU  968  CD2 LEU A 137     7067   6293   7644  -1416   -455    336  A    C  
ATOM    969  N   TYR A 138      46.380  -8.146   3.396  1.00 60.76      A    N  
ANISOU  969  N   TYR A 138     7780   7140   8164  -1528   -213    480  A    N  
ATOM    970  CA  TYR A 138      45.670  -7.088   4.088  1.00 61.57      A    C  
ANISOU  970  CA  TYR A 138     7925   7236   8231  -1608    -70    468  A    C  
ATOM    971  C   TYR A 138      44.958  -6.260   3.040  1.00 62.21      A    C  
ANISOU  971  C   TYR A 138     7778   7448   8412  -1532     10    413  A    C  
ATOM    972  O   TYR A 138      43.815  -5.837   3.225  1.00 69.52      A    O  
ANISOU  972  O   TYR A 138     8669   8381   9364  -1584    163    359  A    O  
ATOM    973  CB  TYR A 138      46.627  -6.202   4.880  1.00 61.46      A    C  
ANISOU  973  CB  TYR A 138     8032   7191   8130  -1622   -136    538  A    C  
ATOM    974  CG  TYR A 138      45.959  -4.949   5.398  1.00 61.57      A    C  
ANISOU  974  CG  TYR A 138     8069   7209   8117  -1674      6    515  A    C  
ATOM    975  CD1 TYR A 138      45.198  -4.974   6.559  1.00 62.87      A    C  
ANISOU  975  CD1 TYR A 138     8415   7276   8196  -1801    142    495  A    C  
ATOM    976  CD2 TYR A 138      46.076  -3.744   4.717  1.00 65.89      A    C  
ANISOU  976  CD2 TYR A 138     8463   7852   8720  -1593     13    513  A    C  
ATOM    977  CE1 TYR A 138      44.580  -3.834   7.037  1.00 69.79      A    C  
ANISOU  977  CE1 TYR A 138     9315   8152   9048  -1836    282    463  A    C  
ATOM    978  CE2 TYR A 138      45.458  -2.592   5.185  1.00 69.50      A    C  
ANISOU  978  CE2 TYR A 138     8950   8299   9159  -1629    140    487  A    C  
ATOM    979  CZ  TYR A 138      44.709  -2.643   6.343  1.00 78.77      A    C  
ANISOU  979  CZ  TYR A 138    10299   9377  10252  -1745    275    456  A    C  
ATOM    980  OH  TYR A 138      44.090  -1.503   6.811  1.00 88.82      A    O  
ANISOU  980  OH  TYR A 138    11605  10637  11507  -1768    410    419  A    O  
ATOM    981  N   TYR A 139      45.649  -6.057   1.926  1.00 53.52      A    N  
ANISOU  981  N   TYR A 139     6521   6450   7363  -1403    -94    428  A    N  
ATOM    982  CA  TYR A 139      45.164  -5.206   0.854  1.00 57.35      A    C  
ANISOU  982  CA  TYR A 139     6805   7060   7925  -1313    -48    394  A    C  
ATOM    983  C   TYR A 139      43.970  -5.799   0.128  1.00 60.65      A    C  
ANISOU  983  C   TYR A 139     7098   7522   8425  -1304     18    306  A    C  
ATOM    984  O   TYR A 139      42.962  -5.121  -0.042  1.00 64.92      A    O  
ANISOU  984  O   TYR A 139     7544   8105   9015  -1307    126    260  A    O  
ATOM    985  CB  TYR A 139      46.277  -4.879  -0.159  1.00 51.64      A    C  
ANISOU  985  CB  TYR A 139     5964   6436   7221  -1183   -171    441  A    C  
ATOM    986  CG  TYR A 139      45.748  -4.128  -1.354  1.00 50.27      A    C  
ANISOU  986  CG  TYR A 139     5600   6387   7113  -1086   -132    412  A    C  
ATOM    987  CD1 TYR A 139      45.506  -2.766  -1.284  1.00 49.11      A    C  
ANISOU  987  CD1 TYR A 139     5422   6266   6972  -1080    -66    432  A    C  
ATOM    988  CD2 TYR A 139      45.452  -4.787  -2.543  1.00 52.73      A    C  
ANISOU  988  CD2 TYR A 139     5779   6782   7475   -999   -167    361  A    C  
ATOM    989  CE1 TYR A 139      44.998  -2.076  -2.365  1.00 50.95      A    C  
ANISOU  989  CE1 TYR A 139     5497   6602   7260   -985    -40    412  A    C  
ATOM    990  CE2 TYR A 139      44.946  -4.102  -3.638  1.00 53.30      A    C  
ANISOU  990  CE2 TYR A 139     5693   6966   7592   -907   -144    338  A    C  
ATOM    991  CZ  TYR A 139      44.720  -2.745  -3.538  1.00 56.28      A    C  
ANISOU  991  CZ  TYR A 139     6044   7365   7976   -899    -82    368  A    C  
ATOM    992  OH  TYR A 139      44.213  -2.044  -4.608  1.00 58.04      A    O  
ANISOU  992  OH  TYR A 139     6125   7689   8239   -802    -69    354  A    O  
ATOM    993  N   ILE A 140      44.085  -7.052  -0.316  1.00 63.49      A    N  
ANISOU  993  N   ILE A 140     7452   7867   8805  -1288    -55    280  A    N  
ATOM    994  CA  ILE A 140      43.002  -7.661  -1.094  1.00 67.59      A    C  
ANISOU  994  CA  ILE A 140     7846   8427   9407  -1282    -18    190  A    C  
ATOM    995  C   ILE A 140      41.753  -7.845  -0.249  1.00 67.38      A    C  
ANISOU  995  C   ILE A 140     7868   8329   9405  -1425    131    141  A    C  
ATOM    996  O   ILE A 140      40.641  -7.721  -0.744  1.00 77.79      A    O  
ANISOU  996  O   ILE A 140     9043   9706  10810  -1428    204     68  A    O  
ATOM    997  CB  ILE A 140      43.374  -9.018  -1.761  1.00 54.54      A    C  
ANISOU  997  CB  ILE A 140     6193   6759   7772  -1239   -132    160  A    C  
ATOM    998  CG1 ILE A 140      43.414 -10.136  -0.734  1.00 58.28      A    C  
ANISOU  998  CG1 ILE A 140     6860   7076   8207  -1360   -133    172  A    C  
ATOM    999  CG2 ILE A 140      44.685  -8.931  -2.540  1.00 53.68      A    C  
ANISOU  999  CG2 ILE A 140     6040   6720   7636  -1095   -263    207  A    C  
ATOM   1000  CD1 ILE A 140      43.634 -11.484  -1.356  1.00 70.48      A    C  
ANISOU 1000  CD1 ILE A 140     8417   8584   9781  -1321   -236    131  A    C  
ATOM   1001  N   HIS A 141      41.930  -8.128   1.032  1.00 64.89      A    N  
ANISOU 1001  N   HIS A 141     7753   7889   9012  -1543    176    183  A    N  
ATOM   1002  CA  HIS A 141      40.781  -8.283   1.908  1.00 59.99      A    C  
ANISOU 1002  CA  HIS A 141     7192   7201   8401  -1687    342    143  A    C  
ATOM   1003  C   HIS A 141      40.077  -6.951   2.190  1.00 65.95      A    C  
ANISOU 1003  C   HIS A 141     7874   8009   9174  -1688    483    122  A    C  
ATOM   1004  O   HIS A 141      38.867  -6.912   2.397  1.00 78.20      A    O  
ANISOU 1004  O   HIS A 141     9357   9566  10791  -1759    631     58  A    O  
ATOM   1005  CB  HIS A 141      41.188  -8.962   3.205  1.00 50.67      A    C  
ANISOU 1005  CB  HIS A 141     6273   5869   7110  -1812    353    200  A    C  
ATOM   1006  CG  HIS A 141      41.697 -10.358   3.021  1.00 53.17      A    C  
ANISOU 1006  CG  HIS A 141     6674   6107   7420  -1820    230    214  A    C  
ATOM   1007  CD2 HIS A 141      41.573 -11.224   1.990  1.00 58.52      A    C  
ANISOU 1007  CD2 HIS A 141     7239   6814   8182  -1765    148    162  A    C  
ATOM   1008  ND1 HIS A 141      42.446 -11.011   3.978  1.00 53.95      A    N  
ANISOU 1008  ND1 HIS A 141     7015   6072   7412  -1882    168    286  A    N  
ATOM   1009  CE1 HIS A 141      42.751 -12.223   3.549  1.00 51.33      A    C  
ANISOU 1009  CE1 HIS A 141     6711   5683   7108  -1861     58    279  A    C  
ATOM   1010  NE2 HIS A 141      42.233 -12.378   2.346  1.00 62.94      A    N  
ANISOU 1010  NE2 HIS A 141     7972   7251   8693  -1793     48    201  A    N  
ATOM   1011  N   ARG A 142      40.834  -5.862   2.189  1.00 58.98      A    N  
ANISOU 1011  N   ARG A 142     7003   7162   8244  -1609    438    173  A    N  
ATOM   1012  CA  ARG A 142      40.270  -4.544   2.411  1.00 58.93      A    C  
ANISOU 1012  CA  ARG A 142     6944   7193   8255  -1591    556    155  A    C  
ATOM   1013  C   ARG A 142      39.419  -4.199   1.208  1.00 66.00      A    C  
ANISOU 1013  C   ARG A 142     7588   8209   9280  -1493    570     89  A    C  
ATOM   1014  O   ARG A 142      38.457  -3.440   1.305  1.00 75.79      A    O  
ANISOU 1014  O   ARG A 142     8738   9479  10579  -1489    696     40  A    O  
ATOM   1015  CB  ARG A 142      41.386  -3.515   2.566  1.00 67.10      A    C  
ANISOU 1015  CB  ARG A 142     8050   8229   9217  -1529    475    229  A    C  
ATOM   1016  CG  ARG A 142      41.113  -2.404   3.569  1.00 81.71      A    C  
ANISOU 1016  CG  ARG A 142    10009  10025  11012  -1578    598    229  A    C  
ATOM   1017  CD  ARG A 142      42.146  -1.302   3.417  1.00 91.02      A    C  
ANISOU 1017  CD  ARG A 142    11210  11221  12154  -1505    501    293  A    C  
ATOM   1018  NE  ARG A 142      42.183  -0.861   2.027  1.00108.01      A    N  
ANISOU 1018  NE  ARG A 142    13149  13491  14400  -1370    435    293  A    N  
ATOM   1019  CZ  ARG A 142      43.254  -0.377   1.407  1.00107.20      A    C  
ANISOU 1019  CZ  ARG A 142    13010  13434  14289  -1291    308    360  A    C  
ATOM   1020  NH1 ARG A 142      44.413  -0.262   2.056  1.00101.49      A    N1+
ANISOU 1020  NH1 ARG A 142    12429  12650  13481  -1334    221    429  A    N1+
ATOM   1021  NH2 ARG A 142      43.158  -0.015   0.127  1.00 98.88      A    N  
ANISOU 1021  NH2 ARG A 142    11774  12488  13308  -1173    268    359  A    N  
ATOM   1022  N   ASN A 143      39.783  -4.769   0.066  1.00 66.23      A    N  
ANISOU 1022  N   ASN A 143     7507   8307   9349  -1407    435     85  A    N  
ATOM   1023  CA  ASN A 143      39.058  -4.544  -1.178  1.00 62.58      A    C  
ANISOU 1023  CA  ASN A 143     6821   7962   8994  -1306    414     25  A    C  
ATOM   1024  C   ASN A 143      38.003  -5.603  -1.432  1.00 69.85      A    C  
ANISOU 1024  C   ASN A 143     7652   8885  10004  -1372    448    -63  A    C  
ATOM   1025  O   ASN A 143      37.554  -5.791  -2.560  1.00 68.91      A    O  
ANISOU 1025  O   ASN A 143     7364   8855   9962  -1294    381   -117  A    O  
ATOM   1026  CB  ASN A 143      40.012  -4.469  -2.355  1.00 59.77      A    C  
ANISOU 1026  CB  ASN A 143     6398   7690   8619  -1168    256     65  A    C  
ATOM   1027  CG  ASN A 143      40.756  -3.165  -2.399  1.00 68.16      A    C  
ANISOU 1027  CG  ASN A 143     7478   8783   9638  -1091    237    139  A    C  
ATOM   1028  ND2 ASN A 143      41.802  -3.052  -1.585  1.00 56.94      A    N  
ANISOU 1028  ND2 ASN A 143     6217   7289   8129  -1137    210    212  A    N  
ATOM   1029  OD1 ASN A 143      40.390  -2.257  -3.146  1.00 77.56      A    O  
ANISOU 1029  OD1 ASN A 143     8543  10055  10873   -996    241    133  A    O  
ATOM   1030  N   LYS A 144      37.623  -6.291  -0.362  1.00 74.34      A    N  
ANISOU 1030  N   LYS A 144     8344   9349  10554  -1524    549    -74  A    N  
ATOM   1031  CA  LYS A 144      36.458  -7.159  -0.363  1.00 71.00      A    C  
ANISOU 1031  CA  LYS A 144     7837   8911  10228  -1626    626   -157  A    C  
ATOM   1032  C   LYS A 144      36.685  -8.397  -1.204  1.00 72.43      A    C  
ANISOU 1032  C   LYS A 144     7992   9092  10438  -1614    485   -186  A    C  
ATOM   1033  O   LYS A 144      35.742  -8.980  -1.734  1.00 75.48      A    O  
ANISOU 1033  O   LYS A 144     8239   9507  10931  -1650    491   -269  A    O  
ATOM   1034  CB  LYS A 144      35.219  -6.388  -0.834  1.00 75.40      A    C  
ANISOU 1034  CB  LYS A 144     8167   9569  10914  -1582    713   -234  A    C  
ATOM   1035  CG  LYS A 144      34.704  -5.380   0.181  1.00 84.68      A    C  
ANISOU 1035  CG  LYS A 144     9375  10720  12081  -1623    896   -232  A    C  
ATOM   1036  CD  LYS A 144      34.579  -6.042   1.555  1.00103.72      A    C  
ANISOU 1036  CD  LYS A 144    11982  13004  14423  -1805   1037   -217  A    C  
ATOM   1037  CE  LYS A 144      34.775  -5.036   2.690  1.00111.42      A    C  
ANISOU 1037  CE  LYS A 144    13110  13925  15300  -1827   1167   -177  A    C  
ATOM   1038  NZ  LYS A 144      35.269  -5.694   3.937  1.00111.16      A    N1+
ANISOU 1038  NZ  LYS A 144    13351  13757  15128  -1973   1221   -122  A    N1+
ATOM   1039  N   ILE A 145      37.942  -8.818  -1.304  1.00 70.41      A    N  
ANISOU 1039  N   ILE A 145     7867   8796  10089  -1564    355   -122  A    N  
ATOM   1040  CA  ILE A 145      38.269  -9.980  -2.122  1.00 63.04      A    C  
ANISOU 1040  CA  ILE A 145     6924   7854   9172  -1531    217   -154  A    C  
ATOM   1041  C   ILE A 145      38.974 -11.118  -1.386  1.00 61.75      A    C  
ANISOU 1041  C   ILE A 145     6980   7545   8938  -1615    173   -110  A    C  
ATOM   1042  O   ILE A 145      39.866 -10.886  -0.573  1.00 68.69      A    O  
ANISOU 1042  O   ILE A 145     8022   8361   9717  -1623    165    -25  A    O  
ATOM   1043  CB  ILE A 145      39.043  -9.565  -3.371  1.00 54.31      A    C  
ANISOU 1043  CB  ILE A 145     5720   6865   8050  -1347     75   -143  A    C  
ATOM   1044  CG1 ILE A 145      38.052  -8.994  -4.388  1.00 60.02      A    C  
ANISOU 1044  CG1 ILE A 145     6220   7717   8868  -1275     81   -218  A    C  
ATOM   1045  CG2 ILE A 145      39.772 -10.755  -3.954  1.00 48.40      A    C  
ANISOU 1045  CG2 ILE A 145     5032   6081   7277  -1302    -64   -156  A    C  
ATOM   1046  CD1 ILE A 145      38.663  -8.109  -5.397  1.00 67.58      A    C  
ANISOU 1046  CD1 ILE A 145     7091   8796   9792  -1104     -5   -185  A    C  
ATOM   1047  N   LEU A 146      38.533 -12.344  -1.671  1.00 61.46      A    N  
ANISOU 1047  N   LEU A 146     6947   7448   8956  -1680    138   -170  A    N  
ATOM   1048  CA  LEU A 146      39.164 -13.565  -1.175  1.00 60.01      A    C  
ANISOU 1048  CA  LEU A 146     6966   7115   8718  -1742     72   -136  A    C  
ATOM   1049  C   LEU A 146      40.012 -14.192  -2.272  1.00 67.36      A    C  
ANISOU 1049  C   LEU A 146     7875   8074   9646  -1596   -108   -158  A    C  
ATOM   1050  O   LEU A 146      39.579 -14.265  -3.418  1.00 72.37      A    O  
ANISOU 1050  O   LEU A 146     8345   8802  10349  -1523   -161   -240  A    O  
ATOM   1051  CB  LEU A 146      38.110 -14.576  -0.744  1.00 56.33      A    C  
ANISOU 1051  CB  LEU A 146     6541   6541   8320  -1923    156   -189  A    C  
ATOM   1052  CG  LEU A 146      37.084 -14.168   0.310  1.00 61.19      A    C  
ANISOU 1052  CG  LEU A 146     7168   7126   8955  -2088    364   -185  A    C  
ATOM   1053  CD1 LEU A 146      36.274 -15.382   0.672  1.00 50.96      A    C  
ANISOU 1053  CD1 LEU A 146     5936   5706   7721  -2271    426   -224  A    C  
ATOM   1054  CD2 LEU A 146      37.759 -13.594   1.543  1.00 61.97      A    C  
ANISOU 1054  CD2 LEU A 146     7467   7160   8917  -2119    428    -82  A    C  
ATOM   1055  N   HIS A 147      41.216 -14.644  -1.926  1.00 61.44      A    N  
ANISOU 1055  N   HIS A 147     7288   7243   8813  -1548   -204    -89  A    N  
ATOM   1056  CA  HIS A 147      42.100 -15.252  -2.910  1.00 58.54      A    C  
ANISOU 1056  CA  HIS A 147     6903   6898   8440  -1397   -360   -111  A    C  
ATOM   1057  C   HIS A 147      41.668 -16.672  -3.209  1.00 61.84      A    C  
ANISOU 1057  C   HIS A 147     7380   7206   8912  -1453   -414   -187  A    C  
ATOM   1058  O   HIS A 147      41.491 -17.041  -4.366  1.00 66.46      A    O  
ANISOU 1058  O   HIS A 147     7854   7853   9543  -1368   -489   -275  A    O  
ATOM   1059  CB  HIS A 147      43.555 -15.236  -2.432  1.00 69.76      A    C  
ANISOU 1059  CB  HIS A 147     8458   8276   9773  -1316   -449    -14  A    C  
ATOM   1060  CG  HIS A 147      44.539 -15.667  -3.476  1.00 67.79      A    C  
ANISOU 1060  CG  HIS A 147     8159   8078   9520  -1137   -588    -35  A    C  
ATOM   1061  CD2 HIS A 147      45.326 -14.947  -4.312  1.00 68.93      A    C  
ANISOU 1061  CD2 HIS A 147     8177   8367   9646   -977   -638    -19  A    C  
ATOM   1062  ND1 HIS A 147      44.796 -16.991  -3.760  1.00 64.40      A    N  
ANISOU 1062  ND1 HIS A 147     7820   7543   9107  -1108   -684    -80  A    N  
ATOM   1063  CE1 HIS A 147      45.700 -17.069  -4.720  1.00 64.00      A    C  
ANISOU 1063  CE1 HIS A 147     7696   7574   9045   -929   -782    -99  A    C  
ATOM   1064  NE2 HIS A 147      46.038 -15.844  -5.072  1.00 68.26      A    N  
ANISOU 1064  NE2 HIS A 147     8102   8270   9563   -851   -751    -59  A    N  
ATOM   1065  N   ARG A 148      41.518 -17.463  -2.153  1.00 62.47      A    N  
ANISOU 1065  N   ARG A 148     7649   7112   8974  -1599   -378   -152  A    N  
ATOM   1066  CA  ARG A 148      40.989 -18.822  -2.244  1.00 67.77      A    C  
ANISOU 1066  CA  ARG A 148     8405   7644   9702  -1694   -409   -215  A    C  
ATOM   1067  C   ARG A 148      41.897 -19.842  -2.943  1.00 74.20      A    C  
ANISOU 1067  C   ARG A 148     9294   8393  10507  -1561   -579   -245  A    C  
ATOM   1068  O   ARG A 148      41.482 -20.973  -3.205  1.00 80.67      A    O  
ANISOU 1068  O   ARG A 148    10175   9095  11379  -1620   -624   -314  A    O  
ATOM   1069  CB  ARG A 148      39.592 -18.819  -2.868  1.00 67.41      A    C  
ANISOU 1069  CB  ARG A 148     8178   7664   9770  -1781   -340   -325  A    C  
ATOM   1070  CG  ARG A 148      38.602 -17.944  -2.123  1.00 75.41      A    C  
ANISOU 1070  CG  ARG A 148     9116   8726  10811  -1918   -158   -306  A    C  
ATOM   1071  CD  ARG A 148      37.164 -18.389  -2.347  1.00 73.22      A    C  
ANISOU 1071  CD  ARG A 148     8717   8440  10663  -2068    -81   -405  A    C  
ATOM   1072  NE  ARG A 148      36.773 -18.363  -3.750  1.00 70.87      A    N  
ANISOU 1072  NE  ARG A 148     8212   8268  10448  -1964   -180   -516  A    N  
ATOM   1073  CZ  ARG A 148      35.587 -18.765  -4.197  1.00 80.38      A    C  
ANISOU 1073  CZ  ARG A 148     9278   9486  11779  -2068   -161   -620  A    C  
ATOM   1074  NH1 ARG A 148      34.673 -19.221  -3.353  1.00 83.25      A    N1+
ANISOU 1074  NH1 ARG A 148     9674   9746  12211  -2285    -28   -624  A    N1+
ATOM   1075  NH2 ARG A 148      35.312 -18.712  -5.489  1.00 82.70      A    N  
ANISOU 1075  NH2 ARG A 148     9399   9895  12127  -1960   -274   -719  A    N  
ATOM   1076  N   ASP A 149      43.135 -19.456  -3.225  1.00 69.51      A    N  
ANISOU 1076  N   ASP A 149     8694   7866   9851  -1384   -669   -197  A    N  
ATOM   1077  CA  ASP A 149      44.104 -20.394  -3.772  1.00 73.83      A    C  
ANISOU 1077  CA  ASP A 149     9317   8348  10385  -1241   -818   -219  A    C  
ATOM   1078  C   ASP A 149      45.502 -20.149  -3.194  1.00 78.48      A    C  
ANISOU 1078  C   ASP A 149    10000   8919  10898  -1135   -887   -110  A    C  
ATOM   1079  O   ASP A 149      46.486 -20.092  -3.924  1.00 84.30      A    O  
ANISOU 1079  O   ASP A 149    10669   9737  11623   -950   -977   -118  A    O  
ATOM   1080  CB  ASP A 149      44.122 -20.310  -5.301  1.00 78.71      A    C  
ANISOU 1080  CB  ASP A 149     9756   9114  11035  -1084   -879   -324  A    C  
ATOM   1081  CG  ASP A 149      44.638 -21.585  -5.952  1.00 88.69      A    C  
ANISOU 1081  CG  ASP A 149    11109  10278  12312   -980  -1009   -398  A    C  
ATOM   1082  OD1 ASP A 149      44.738 -22.614  -5.243  1.00 87.51      A    O  
ANISOU 1082  OD1 ASP A 149    11155   9928  12169  -1055  -1048   -378  A    O  
ATOM   1083  OD2 ASP A 149      44.942 -21.555  -7.170  1.00 92.36      A    O1-
ANISOU 1083  OD2 ASP A 149    11460  10860  12773   -820  -1070   -475  A    O1-
ATOM   1084  N   MET A 150      45.595 -19.997  -1.880  1.00 77.04      A    N  
ANISOU 1084  N   MET A 150     9971   8637  10663  -1252   -843    -10  A    N  
ATOM   1085  CA  MET A 150      46.900 -19.793  -1.264  1.00 77.18      A    C  
ANISOU 1085  CA  MET A 150    10082   8629  10612  -1162   -930     92  A    C  
ATOM   1086  C   MET A 150      47.772 -21.034  -1.385  1.00 83.73      A    C  
ANISOU 1086  C   MET A 150    11043   9322  11448  -1054  -1081     88  A    C  
ATOM   1087  O   MET A 150      47.318 -22.151  -1.135  1.00 90.14      A    O  
ANISOU 1087  O   MET A 150    12010   9960  12280  -1138  -1101     62  A    O  
ATOM   1088  CB  MET A 150      46.748 -19.404   0.202  1.00 75.48      A    C  
ANISOU 1088  CB  MET A 150    10030   8324  10323  -1319   -859    194  A    C  
ATOM   1089  CG  MET A 150      46.244 -18.004   0.371  1.00 78.58      A    C  
ANISOU 1089  CG  MET A 150    10295   8861  10700  -1376   -729    210  A    C  
ATOM   1090  SD  MET A 150      47.433 -16.855  -0.329  1.00 87.18      A    S  
ANISOU 1090  SD  MET A 150    11201  10144  11781  -1181   -801    242  A    S  
ATOM   1091  CE  MET A 150      48.693 -16.929   0.932  1.00 76.62      A    C  
ANISOU 1091  CE  MET A 150    10067   8692  10354  -1176   -913    367  A    C  
ATOM   1092  N   LYS A 151      49.022 -20.830  -1.780  1.00 73.88      A    N  
ANISOU 1092  N   LYS A 151     9728   8151  10191   -867  -1185    114  A    N  
ATOM   1093  CA  LYS A 151      50.000 -21.906  -1.831  1.00 69.09      A    C  
ANISOU 1093  CA  LYS A 151     9233   7423   9594   -735  -1334    117  A    C  
ATOM   1094  C   LYS A 151      51.289 -21.353  -2.400  1.00 74.31      A    C  
ANISOU 1094  C   LYS A 151     9740   8234  10260   -530  -1408    138  A    C  
ATOM   1095  O   LYS A 151      51.283 -20.332  -3.079  1.00 73.45      A    O  
ANISOU 1095  O   LYS A 151     9432   8321  10156   -484  -1341    123  A    O  
ATOM   1096  CB  LYS A 151      49.507 -23.061  -2.690  1.00 65.76      A    C  
ANISOU 1096  CB  LYS A 151     8836   6920   9231   -702  -1366     -2  A    C  
ATOM   1097  CG  LYS A 151      49.404 -22.731  -4.175  1.00 76.58      A    C  
ANISOU 1097  CG  LYS A 151     9983   8476  10638   -571  -1345   -113  A    C  
ATOM   1098  CD  LYS A 151      48.720 -23.861  -4.937  1.00 81.52      A    C  
ANISOU 1098  CD  LYS A 151    10655   9005  11314   -575  -1375   -242  A    C  
ATOM   1099  CE  LYS A 151      48.615 -23.553  -6.417  1.00 84.99      A    C  
ANISOU 1099  CE  LYS A 151    10897   9628  11768   -442  -1365   -355  A    C  
ATOM   1100  NZ  LYS A 151      47.676 -24.477  -7.107  1.00 85.95      A    N1+
ANISOU 1100  NZ  LYS A 151    11055   9667  11935   -493  -1384   -489  A    N1+
ATOM   1101  N   ALA A 152      52.391 -22.033  -2.121  1.00 78.62      A    N  
ANISOU 1101  N   ALA A 152    10376   8686  10810   -407  -1546    177  A    N  
ATOM   1102  CA  ALA A 152      53.705 -21.566  -2.544  1.00 86.36      A    C  
ANISOU 1102  CA  ALA A 152    11203   9800  11808   -217  -1618    205  A    C  
ATOM   1103  C   ALA A 152      53.757 -21.166  -4.022  1.00 85.74      A    C  
ANISOU 1103  C   ALA A 152    10893   9923  11764    -82  -1559    113  A    C  
ATOM   1104  O   ALA A 152      54.340 -20.140  -4.373  1.00 78.12      A    O  
ANISOU 1104  O   ALA A 152     9750   9136  10796    -17  -1527    148  A    O  
ATOM   1105  CB  ALA A 152      54.765 -22.625  -2.242  1.00 90.72      A    C  
ANISOU 1105  CB  ALA A 152    11874  10209  12385    -77  -1782    227  A    C  
ATOM   1106  N   ALA A 153      53.151 -21.973  -4.887  1.00 86.39      A    N  
ANISOU 1106  N   ALA A 153    10985   9969  11870    -47  -1548     -4  A    N  
ATOM   1107  CA  ALA A 153      53.281 -21.759  -6.326  1.00 84.53      A    C  
ANISOU 1107  CA  ALA A 153    10563   9908  11647    102  -1511    -98  A    C  
ATOM   1108  C   ALA A 153      52.622 -20.454  -6.788  1.00 79.81      A    C  
ANISOU 1108  C   ALA A 153     9799   9503  11023     30  -1386    -94  A    C  
ATOM   1109  O   ALA A 153      52.871 -19.978  -7.901  1.00 80.19      A    O  
ANISOU 1109  O   ALA A 153     9682   9724  11062    151  -1348   -138  A    O  
ATOM   1110  CB  ALA A 153      52.732 -22.951  -7.091  1.00 82.92      A    C  
ANISOU 1110  CB  ALA A 153    10436   9605  11466    146  -1542   -233  A    C  
ATOM   1111  N   ASN A 154      51.796 -19.877  -5.920  1.00 65.35      A    N  
ANISOU 1111  N   ASN A 154     8019   7636   9175   -162  -1320    -37  A    N  
ATOM   1112  CA  ASN A 154      51.084 -18.646  -6.237  1.00 66.18      A    C  
ANISOU 1112  CA  ASN A 154     7984   7899   9264   -235  -1205    -30  A    C  
ATOM   1113  C   ASN A 154      51.677 -17.398  -5.569  1.00 74.99      A    C  
ANISOU 1113  C   ASN A 154     9040   9098  10354   -265  -1174     89  A    C  
ATOM   1114  O   ASN A 154      51.152 -16.290  -5.709  1.00 76.32      A    O  
ANISOU 1114  O   ASN A 154     9108   9381  10509   -325  -1082    107  A    O  
ATOM   1115  CB  ASN A 154      49.601 -18.792  -5.890  1.00 66.02      A    C  
ANISOU 1115  CB  ASN A 154     8031   7799   9255   -421  -1132    -73  A    C  
ATOM   1116  CG  ASN A 154      48.852 -19.633  -6.905  1.00 74.00      A    C  
ANISOU 1116  CG  ASN A 154     9024   8795  10297   -394  -1146   -207  A    C  
ATOM   1117  ND2 ASN A 154      47.733 -20.210  -6.490  1.00 73.66      A    N  
ANISOU 1117  ND2 ASN A 154     9075   8627  10285   -556  -1116   -250  A    N  
ATOM   1118  OD1 ASN A 154      49.278 -19.762  -8.052  1.00 76.29      A    O  
ANISOU 1118  OD1 ASN A 154     9219   9185  10581   -234  -1182   -274  A    O  
ATOM   1119  N   VAL A 155      52.764 -17.583  -4.830  1.00 68.32      A    N  
ANISOU 1119  N   VAL A 155     8264   8188   9506   -223  -1262    167  A    N  
ATOM   1120  CA  VAL A 155      53.511 -16.455  -4.318  1.00 65.28      A    C  
ANISOU 1120  CA  VAL A 155     7811   7889   9105   -233  -1259    270  A    C  
ATOM   1121  C   VAL A 155      54.715 -16.246  -5.236  1.00 65.33      A    C  
ANISOU 1121  C   VAL A 155     7644   8039   9139    -44  -1298    273  A    C  
ATOM   1122  O   VAL A 155      55.528 -17.143  -5.423  1.00 71.13      A    O  
ANISOU 1122  O   VAL A 155     8395   8728   9904     86  -1390    251  A    O  
ATOM   1123  CB  VAL A 155      53.953 -16.694  -2.872  1.00 70.15      A    C  
ANISOU 1123  CB  VAL A 155     8606   8352   9697   -317  -1342    359  A    C  
ATOM   1124  CG1 VAL A 155      54.654 -15.461  -2.322  1.00 65.49      A    C  
ANISOU 1124  CG1 VAL A 155     7949   7846   9088   -346  -1347    457  A    C  
ATOM   1125  CG2 VAL A 155      52.747 -17.047  -2.020  1.00 65.97      A    C  
ANISOU 1125  CG2 VAL A 155     8260   7674   9131   -502  -1285    352  A    C  
ATOM   1126  N   LEU A 156      54.808 -15.076  -5.847  1.00 56.28      A    N  
ANISOU 1126  N   LEU A 156     6332   7067   7987    -26  -1218    296  A    N  
ATOM   1127  CA  LEU A 156      55.880 -14.837  -6.793  1.00 62.93      A    C  
ANISOU 1127  CA  LEU A 156     7001   8057   8851    140  -1225    300  A    C  
ATOM   1128  C   LEU A 156      56.822 -13.815  -6.183  1.00 73.36      A    C  
ANISOU 1128  C   LEU A 156     8248   9439  10188    111  -1245    414  A    C  
ATOM   1129  O   LEU A 156      56.452 -13.096  -5.244  1.00 71.46      A    O  
ANISOU 1129  O   LEU A 156     8078   9149   9923    -37  -1231    476  A    O  
ATOM   1130  CB  LEU A 156      55.348 -14.329  -8.141  1.00 58.87      A    C  
ANISOU 1130  CB  LEU A 156     6353   7702   8311    196  -1121    240  A    C  
ATOM   1131  CG  LEU A 156      54.224 -15.084  -8.858  1.00 54.84      A    C  
ANISOU 1131  CG  LEU A 156     5896   7159   7781    202  -1097    120  A    C  
ATOM   1132  CD1 LEU A 156      53.948 -14.452 -10.208  1.00 59.41      A    C  
ANISOU 1132  CD1 LEU A 156     6335   7916   8322    281  -1016     79  A    C  
ATOM   1133  CD2 LEU A 156      54.560 -16.528  -9.042  1.00 48.02      A    C  
ANISOU 1133  CD2 LEU A 156     5118   6189   6939    306  -1182     41  A    C  
ATOM   1134  N   ILE A 157      58.043 -13.772  -6.709  1.00 68.11      A    N  
ANISOU 1134  N   ILE A 157     7439   8876   9563    250  -1276    435  A    N  
ATOM   1135  CA  ILE A 157      59.019 -12.778  -6.311  1.00 62.81      A    C  
ANISOU 1135  CA  ILE A 157     6659   8284   8923    227  -1296    538  A    C  
ATOM   1136  C   ILE A 157      59.729 -12.248  -7.550  1.00 66.24      A    C  
ANISOU 1136  C   ILE A 157     6876   8914   9380    351  -1218    540  A    C  
ATOM   1137  O   ILE A 157      60.084 -13.013  -8.446  1.00 66.68      A    O  
ANISOU 1137  O   ILE A 157     6868   9020   9448    508  -1209    471  A    O  
ATOM   1138  CB  ILE A 157      60.031 -13.357  -5.331  1.00 62.35      A    C  
ANISOU 1138  CB  ILE A 157     6655   8123   8914    254  -1448    586  A    C  
ATOM   1139  CG1 ILE A 157      59.299 -13.998  -4.151  1.00 56.37      A    C  
ANISOU 1139  CG1 ILE A 157     6144   7161   8113    136  -1518    586  A    C  
ATOM   1140  CG2 ILE A 157      60.959 -12.265  -4.852  1.00 65.57      A    C  
ANISOU 1140  CG2 ILE A 157     6950   8606   9357    203  -1480    689  A    C  
ATOM   1141  CD1 ILE A 157      60.183 -14.310  -2.986  1.00 54.86      A    C  
ANISOU 1141  CD1 ILE A 157     6039   6860   7944    126  -1679    657  A    C  
ATOM   1142  N   THR A 158      59.913 -10.935  -7.614  1.00 64.90      A    N  
ANISOU 1142  N   THR A 158     6602   8848   9208    279  -1153    617  A    N  
ATOM   1143  CA  THR A 158      60.564 -10.331  -8.769  1.00 67.73      A    C  
ANISOU 1143  CA  THR A 158     6764   9393   9579    374  -1061    635  A    C  
ATOM   1144  C   THR A 158      62.085 -10.410  -8.664  1.00 74.35      A    C  
ANISOU 1144  C   THR A 158     7454  10290  10505    459  -1123    686  A    C  
ATOM   1145  O   THR A 158      62.628 -10.762  -7.619  1.00 68.18      A    O  
ANISOU 1145  O   THR A 158     6723   9407   9775    431  -1253    719  A    O  
ATOM   1146  CB  THR A 158      60.145  -8.864  -8.963  1.00 60.59      A    C  
ANISOU 1146  CB  THR A 158     5810   8571   8642    262   -961    703  A    C  
ATOM   1147  CG2 THR A 158      58.658  -8.769  -9.271  1.00 53.54      A    C  
ANISOU 1147  CG2 THR A 158     5022   7647   7675    209   -893    644  A    C  
ATOM   1148  OG1 THR A 158      60.429  -8.122  -7.772  1.00 62.84      A    O  
ANISOU 1148  OG1 THR A 158     6133   8785   8957    121  -1023    789  A    O  
ATOM   1149  N   ARG A 159      62.760 -10.086  -9.761  1.00 85.16      A    N  
ANISOU 1149  N   ARG A 159     8640  11828  11889    564  -1029    693  A    N  
ATOM   1150  CA  ARG A 159      64.214 -10.040  -9.797  1.00 86.54      A    C  
ANISOU 1150  CA  ARG A 159     8629  12091  12162    643  -1059    743  A    C  
ATOM   1151  C   ARG A 159      64.732  -9.097  -8.703  1.00 84.64      A    C  
ANISOU 1151  C   ARG A 159     8360  11818  11982    490  -1138    854  A    C  
ATOM   1152  O   ARG A 159      65.734  -9.385  -8.045  1.00 81.44      A    O  
ANISOU 1152  O   ARG A 159     7888  11386  11669    515  -1259    886  A    O  
ATOM   1153  CB  ARG A 159      64.667  -9.567 -11.178  1.00 88.70      A    C  
ANISOU 1153  CB  ARG A 159     8718  12564  12421    739   -901    748  A    C  
ATOM   1154  CG  ARG A 159      66.142  -9.711 -11.470  1.00 98.84      A    C  
ANISOU 1154  CG  ARG A 159     9782  13963  13811    855   -897    774  A    C  
ATOM   1155  CD  ARG A 159      66.474  -9.100 -12.828  1.00113.58      A    C  
ANISOU 1155  CD  ARG A 159    11486  16029  15639    920   -709    791  A    C  
ATOM   1156  NE  ARG A 159      67.910  -8.924 -13.029  1.00128.45      A    N  
ANISOU 1156  NE  ARG A 159    13125  18041  17638    986   -678    843  A    N  
ATOM   1157  CZ  ARG A 159      68.730  -9.883 -13.452  1.00134.47      A    C  
ANISOU 1157  CZ  ARG A 159    13774  18857  18460   1177   -674    777  A    C  
ATOM   1158  NH1 ARG A 159      68.256 -11.097 -13.716  1.00128.75      A    N1+
ANISOU 1158  NH1 ARG A 159    13180  18056  17684   1318   -708    654  A    N1+
ATOM   1159  NH2 ARG A 159      70.027  -9.631 -13.608  1.00136.32      A    N  
ANISOU 1159  NH2 ARG A 159    13761  19220  18816   1225   -637    829  A    N  
ATOM   1160  N   ASP A 160      64.027  -7.986  -8.501  1.00 79.64      A    N  
ANISOU 1160  N   ASP A 160     7785  11178  11296    334  -1080    905  A    N  
ATOM   1161  CA  ASP A 160      64.410  -6.981  -7.514  1.00 80.82      A    C  
ANISOU 1161  CA  ASP A 160     7930  11289  11488    176  -1146   1001  A    C  
ATOM   1162  C   ASP A 160      63.947  -7.317  -6.093  1.00 77.31      A    C  
ANISOU 1162  C   ASP A 160     7697  10657  11021     72  -1285    998  A    C  
ATOM   1163  O   ASP A 160      64.038  -6.479  -5.194  1.00 77.23      A    O  
ANISOU 1163  O   ASP A 160     7735  10592  11016    -72  -1341   1063  A    O  
ATOM   1164  CB  ASP A 160      63.872  -5.602  -7.918  1.00100.03      A    C  
ANISOU 1164  CB  ASP A 160    10348  13785  13875     63  -1020   1057  A    C  
ATOM   1165  CG  ASP A 160      64.463  -5.096  -9.229  1.00115.80      A    C  
ANISOU 1165  CG  ASP A 160    12144  15967  15888    139   -882   1089  A    C  
ATOM   1166  OD1 ASP A 160      65.529  -5.606  -9.644  1.00120.02      A    O  
ANISOU 1166  OD1 ASP A 160    12516  16593  16495    255   -887   1086  A    O  
ATOM   1167  OD2 ASP A 160      63.861  -4.181  -9.841  1.00116.83      A    O1-
ANISOU 1167  OD2 ASP A 160    12282  16149  15957     87   -764   1120  A    O1-
ATOM   1168  N   GLY A 161      63.438  -8.532  -5.896  1.00 73.93      A    N  
ANISOU 1168  N   GLY A 161     7406  10124  10558    141  -1338    921  A    N  
ATOM   1169  CA  GLY A 161      63.060  -9.016  -4.574  1.00 73.37      A    C  
ANISOU 1169  CA  GLY A 161     7548   9871  10457     54  -1466    921  A    C  
ATOM   1170  C   GLY A 161      61.744  -8.542  -3.966  1.00 73.85      A    C  
ANISOU 1170  C   GLY A 161     7804   9832  10425   -102  -1413    915  A    C  
ATOM   1171  O   GLY A 161      61.592  -8.530  -2.746  1.00 79.49      A    O  
ANISOU 1171  O   GLY A 161     8681  10415  11108   -212  -1504    943  A    O  
ATOM   1172  N   VAL A 162      60.793  -8.151  -4.807  1.00 66.71      A    N  
ANISOU 1172  N   VAL A 162     6883   8990   9473   -108  -1268    877  A    N  
ATOM   1173  CA  VAL A 162      59.469  -7.778  -4.339  1.00 64.85      A    C  
ANISOU 1173  CA  VAL A 162     6807   8669   9164   -234  -1204    857  A    C  
ATOM   1174  C   VAL A 162      58.507  -8.943  -4.553  1.00 64.98      A    C  
ANISOU 1174  C   VAL A 162     6936   8610   9143   -191  -1185    763  A    C  
ATOM   1175  O   VAL A 162      58.378  -9.448  -5.665  1.00 64.06      A    O  
ANISOU 1175  O   VAL A 162     6737   8572   9032    -73  -1134    702  A    O  
ATOM   1176  CB  VAL A 162      58.928  -6.554  -5.076  1.00 68.16      A    C  
ANISOU 1176  CB  VAL A 162     7142   9193   9563   -273  -1068    875  A    C  
ATOM   1177  CG1 VAL A 162      57.698  -6.028  -4.368  1.00 72.58      A    C  
ANISOU 1177  CG1 VAL A 162     7856   9657  10065   -409  -1016    863  A    C  
ATOM   1178  CG2 VAL A 162      59.977  -5.473  -5.151  1.00 69.27      A    C  
ANISOU 1178  CG2 VAL A 162     7144   9424   9754   -299  -1074    965  A    C  
ATOM   1179  N   LEU A 163      57.849  -9.364  -3.474  1.00 55.17      A    N  
ANISOU 1179  N   LEU A 163     5891   7214   7860   -294  -1225    753  A    N  
ATOM   1180  CA  LEU A 163      56.910 -10.474  -3.497  1.00 52.49      A    C  
ANISOU 1180  CA  LEU A 163     5676   6777   7492   -289  -1212    672  A    C  
ATOM   1181  C   LEU A 163      55.544 -10.052  -4.056  1.00 59.53      A    C  
ANISOU 1181  C   LEU A 163     6562   7706   8352   -341  -1075    617  A    C  
ATOM   1182  O   LEU A 163      54.998  -9.017  -3.672  1.00 66.13      A    O  
ANISOU 1182  O   LEU A 163     7414   8548   9163   -448  -1005    647  A    O  
ATOM   1183  CB  LEU A 163      56.742 -11.037  -2.082  1.00 57.38      A    C  
ANISOU 1183  CB  LEU A 163     6515   7213   8072   -394  -1296    695  A    C  
ATOM   1184  CG  LEU A 163      55.605 -12.044  -1.862  1.00 56.95      A    C  
ANISOU 1184  CG  LEU A 163     6622   7033   7984   -445  -1263    627  A    C  
ATOM   1185  CD1 LEU A 163      55.884 -12.947  -0.675  1.00 61.10      A    C  
ANISOU 1185  CD1 LEU A 163     7356   7380   8479   -491  -1382    659  A    C  
ATOM   1186  CD2 LEU A 163      54.278 -11.345  -1.700  1.00 46.21      A    C  
ANISOU 1186  CD2 LEU A 163     5302   5670   6584   -577  -1126    604  A    C  
ATOM   1187  N   LYS A 164      54.998 -10.867  -4.954  1.00 51.87      A    N  
ANISOU 1187  N   LYS A 164     5567   6755   7386   -262  -1045    530  A    N  
ATOM   1188  CA  LYS A 164      53.702 -10.592  -5.570  1.00 50.46      A    C  
ANISOU 1188  CA  LYS A 164     5367   6616   7189   -297   -939    467  A    C  
ATOM   1189  C   LYS A 164      52.762 -11.763  -5.377  1.00 55.18      A    C  
ANISOU 1189  C   LYS A 164     6090   7093   7785   -338   -947    384  A    C  
ATOM   1190  O   LYS A 164      53.084 -12.882  -5.761  1.00 69.63      A    O  
ANISOU 1190  O   LYS A 164     7942   8884   9630   -248  -1012    332  A    O  
ATOM   1191  CB  LYS A 164      53.835 -10.365  -7.077  1.00 46.52      A    C  
ANISOU 1191  CB  LYS A 164     4702   6279   6693   -163   -894    431  A    C  
ATOM   1192  CG  LYS A 164      54.842  -9.322  -7.506  1.00 51.59      A    C  
ANISOU 1192  CG  LYS A 164     5205   7055   7343   -109   -874    512  A    C  
ATOM   1193  CD  LYS A 164      54.520  -7.950  -6.981  1.00 54.09      A    C  
ANISOU 1193  CD  LYS A 164     5521   7382   7650   -226   -816    583  A    C  
ATOM   1194  CE  LYS A 164      55.056  -6.899  -7.942  1.00 61.09      A    C  
ANISOU 1194  CE  LYS A 164     6253   8423   8535   -163   -758    637  A    C  
ATOM   1195  NZ  LYS A 164      55.441  -5.625  -7.253  1.00 67.13      A    N1+
ANISOU 1195  NZ  LYS A 164     7012   9182   9312   -264   -746    734  A    N1+
ATOM   1196  N   LEU A 165      51.601 -11.501  -4.790  1.00 56.15      A    N  
ANISOU 1196  N   LEU A 165     6290   7152   7893   -474   -875    369  A    N  
ATOM   1197  CA  LEU A 165      50.495 -12.458  -4.777  1.00 60.94      A    C  
ANISOU 1197  CA  LEU A 165     6979   7666   8510   -534   -853    283  A    C  
ATOM   1198  C   LEU A 165      49.888 -12.587  -6.168  1.00 56.90      A    C  
ANISOU 1198  C   LEU A 165     6339   7262   8018   -447   -823    192  A    C  
ATOM   1199  O   LEU A 165      49.547 -11.580  -6.785  1.00 60.47      A    O  
ANISOU 1199  O   LEU A 165     6670   7839   8466   -426   -759    196  A    O  
ATOM   1200  CB  LEU A 165      49.417 -11.976  -3.827  1.00 63.24      A    C  
ANISOU 1200  CB  LEU A 165     7354   7887   8789   -702   -761    293  A    C  
ATOM   1201  CG  LEU A 165      49.465 -12.618  -2.465  1.00 68.62      A    C  
ANISOU 1201  CG  LEU A 165     8239   8394   9438   -817   -790    331  A    C  
ATOM   1202  CD1 LEU A 165      48.582 -11.833  -1.526  1.00 77.39      A    C  
ANISOU 1202  CD1 LEU A 165     9417   9468  10521   -971   -675    353  A    C  
ATOM   1203  CD2 LEU A 165      48.980 -14.050  -2.637  1.00 73.26      A    C  
ANISOU 1203  CD2 LEU A 165     8911   8875  10051   -829   -822    259  A    C  
ATOM   1204  N   ALA A 166      49.741 -13.820  -6.650  1.00 53.44      A    N  
ANISOU 1204  N   ALA A 166     5940   6768   7596   -397   -876    109  A    N  
ATOM   1205  CA  ALA A 166      49.352 -14.053  -8.038  1.00 57.75      A    C  
ANISOU 1205  CA  ALA A 166     6380   7416   8146   -294   -875     15  A    C  
ATOM   1206  C   ALA A 166      48.319 -15.162  -8.220  1.00 66.10      A    C  
ANISOU 1206  C   ALA A 166     7505   8375   9234   -351   -893    -95  A    C  
ATOM   1207  O   ALA A 166      48.030 -15.913  -7.296  1.00 64.96      A    O  
ANISOU 1207  O   ALA A 166     7501   8071   9110   -460   -907    -95  A    O  
ATOM   1208  CB  ALA A 166      50.580 -14.340  -8.885  1.00 62.59      A    C  
ANISOU 1208  CB  ALA A 166     6931   8109   8741   -113   -934     12  A    C  
ATOM   1209  N   ASP A 167      47.788 -15.250  -9.438  1.00 77.65      A    N  
ANISOU 1209  N   ASP A 167     8875   9933  10695   -278   -896   -187  A    N  
ATOM   1210  CA  ASP A 167      46.782 -16.244  -9.821  1.00 80.46      A    C  
ANISOU 1210  CA  ASP A 167     9268  10215  11086   -327   -926   -307  A    C  
ATOM   1211  C   ASP A 167      45.471 -16.051  -9.074  1.00 73.76      A    C  
ANISOU 1211  C   ASP A 167     8433   9303  10290   -515   -856   -316  A    C  
ATOM   1212  O   ASP A 167      45.243 -16.664  -8.035  1.00 65.64      A    O  
ANISOU 1212  O   ASP A 167     7533   8118   9288   -644   -845   -297  A    O  
ATOM   1213  CB  ASP A 167      47.297 -17.678  -9.647  1.00 85.59      A    C  
ANISOU 1213  CB  ASP A 167    10061  10712  11748   -295  -1014   -352  A    C  
ATOM   1214  CG  ASP A 167      46.557 -18.675 -10.529  1.00 94.39      A    C  
ANISOU 1214  CG  ASP A 167    11191  11788  12885   -282  -1068   -495  A    C  
ATOM   1215  OD1 ASP A 167      45.497 -18.313 -11.083  1.00 99.56      A    O  
ANISOU 1215  OD1 ASP A 167    11752  12519  13557   -332  -1041   -557  A    O  
ATOM   1216  OD2 ASP A 167      47.033 -19.820 -10.677  1.00 94.81      A    O1-
ANISOU 1216  OD2 ASP A 167    11351  11731  12941   -217  -1148   -550  A    O1-
ATOM   1217  N   PHE A 168      44.609 -15.202  -9.626  1.00 74.51      A    N  
ANISOU 1217  N   PHE A 168     8393   9518  10399   -526   -806   -343  A    N  
ATOM   1218  CA  PHE A 168      43.334 -14.889  -9.002  1.00 66.87      A    C  
ANISOU 1218  CA  PHE A 168     7398   8517   9494   -688   -725   -356  A    C  
ATOM   1219  C   PHE A 168      42.188 -15.623  -9.675  1.00 66.84      A    C  
ANISOU 1219  C   PHE A 168     7342   8499   9552   -735   -760   -486  A    C  
ATOM   1220  O   PHE A 168      41.034 -15.226  -9.557  1.00 77.21      A    O  
ANISOU 1220  O   PHE A 168     8566   9840  10931   -833   -701   -519  A    O  
ATOM   1221  CB  PHE A 168      43.114 -13.374  -8.980  1.00 66.48      A    C  
ANISOU 1221  CB  PHE A 168     7232   8593   9435   -676   -645   -292  A    C  
ATOM   1222  CG  PHE A 168      43.903 -12.676  -7.907  1.00 67.74      A    C  
ANISOU 1222  CG  PHE A 168     7465   8717   9557   -708   -592   -171  A    C  
ATOM   1223  CD1 PHE A 168      43.305 -12.315  -6.706  1.00 60.08      A    C  
ANISOU 1223  CD1 PHE A 168     6550   7669   8610   -858   -496   -133  A    C  
ATOM   1224  CD2 PHE A 168      45.261 -12.431  -8.072  1.00 68.43      A    C  
ANISOU 1224  CD2 PHE A 168     7569   8846   9584   -594   -640    -99  A    C  
ATOM   1225  CE1 PHE A 168      44.040 -11.692  -5.694  1.00 54.84      A    C  
ANISOU 1225  CE1 PHE A 168     5974   6964   7898   -891   -461    -29  A    C  
ATOM   1226  CE2 PHE A 168      46.005 -11.808  -7.061  1.00 62.14      A    C  
ANISOU 1226  CE2 PHE A 168     6841   8012   8758   -633   -611      8  A    C  
ATOM   1227  CZ  PHE A 168      45.392 -11.439  -5.874  1.00 51.29      A    C  
ANISOU 1227  CZ  PHE A 168     5539   6554   7395   -782   -529     41  A    C  
ATOM   1228  N   GLY A 169      42.528 -16.717 -10.353  1.00 66.38      A    N  
ANISOU 1228  N   GLY A 169     7344   8396   9482   -665   -861   -565  A    N  
ATOM   1229  CA  GLY A 169      41.579 -17.539 -11.083  1.00 62.50      A    C  
ANISOU 1229  CA  GLY A 169     6822   7881   9044   -701   -923   -700  A    C  
ATOM   1230  C   GLY A 169      40.449 -18.144 -10.268  1.00 70.82      A    C  
ANISOU 1230  C   GLY A 169     7911   8800  10199   -914   -877   -738  A    C  
ATOM   1231  O   GLY A 169      39.373 -18.417 -10.807  1.00 85.77      A    O  
ANISOU 1231  O   GLY A 169     9714  10712  12163   -977   -904   -842  A    O  
ATOM   1232  N   LEU A 170      40.690 -18.374  -8.981  1.00 65.57      A    N  
ANISOU 1232  N   LEU A 170     7377   7998   9538  -1029   -810   -654  A    N  
ATOM   1233  CA  LEU A 170      39.654 -18.869  -8.076  1.00 68.24      A    C  
ANISOU 1233  CA  LEU A 170     7760   8208   9961  -1247   -732   -669  A    C  
ATOM   1234  C   LEU A 170      39.153 -17.754  -7.177  1.00 69.95      A    C  
ANISOU 1234  C   LEU A 170     7912   8475  10192  -1342   -585   -591  A    C  
ATOM   1235  O   LEU A 170      38.251 -17.954  -6.370  1.00 72.85      A    O  
ANISOU 1235  O   LEU A 170     8294   8761  10624  -1523   -485   -594  A    O  
ATOM   1236  CB  LEU A 170      40.177 -20.001  -7.194  1.00 76.89      A    C  
ANISOU 1236  CB  LEU A 170     9082   9091  11040  -1326   -752   -630  A    C  
ATOM   1237  CG  LEU A 170      39.879 -21.444  -7.593  1.00 97.90      A    C  
ANISOU 1237  CG  LEU A 170    11837  11608  13754  -1377   -846   -733  A    C  
ATOM   1238  CD1 LEU A 170      40.806 -21.910  -8.719  1.00 97.84      A    C  
ANISOU 1238  CD1 LEU A 170    11849  11634  13692  -1166   -989   -796  A    C  
ATOM   1239  CD2 LEU A 170      39.996 -22.351  -6.366  1.00104.16      A    C  
ANISOU 1239  CD2 LEU A 170    12854  12174  14549  -1527   -814   -669  A    C  
ATOM   1240  N   ALA A 171      39.757 -16.581  -7.301  1.00 66.96      A    N  
ANISOU 1240  N   ALA A 171     7467   8224   9750  -1221   -565   -520  A    N  
ATOM   1241  CA  ALA A 171      39.420 -15.476  -6.423  1.00 63.90      A    C  
ANISOU 1241  CA  ALA A 171     7042   7872   9363  -1293   -430   -445  A    C  
ATOM   1242  C   ALA A 171      37.940 -15.110  -6.549  1.00 69.06      A    C  
ANISOU 1242  C   ALA A 171     7530   8586  10125  -1390   -348   -518  A    C  
ATOM   1243  O   ALA A 171      37.294 -15.418  -7.548  1.00 77.24      A    O  
ANISOU 1243  O   ALA A 171     8442   9683  11224  -1361   -420   -619  A    O  
ATOM   1244  CB  ALA A 171      40.291 -14.290  -6.734  1.00 57.88      A    C  
ANISOU 1244  CB  ALA A 171     6227   7238   8528  -1141   -441   -370  A    C  
ATOM   1245  N   ARG A 172      37.414 -14.444  -5.531  1.00 69.96      A    N  
ANISOU 1245  N   ARG A 172     7640   8683  10258  -1500   -201   -470  A    N  
ATOM   1246  CA  ARG A 172      36.003 -14.086  -5.487  1.00 74.27      A    C  
ANISOU 1246  CA  ARG A 172     8020   9279  10920  -1597   -101   -536  A    C  
ATOM   1247  C   ARG A 172      35.758 -12.942  -4.510  1.00 71.84      A    C  
ANISOU 1247  C   ARG A 172     7703   8994  10600  -1640     60   -469  A    C  
ATOM   1248  O   ARG A 172      36.397 -12.869  -3.464  1.00 73.36      A    O  
ANISOU 1248  O   ARG A 172     8071   9095  10705  -1691    123   -382  A    O  
ATOM   1249  CB  ARG A 172      35.169 -15.294  -5.056  1.00 76.66      A    C  
ANISOU 1249  CB  ARG A 172     8363   9454  11309  -1788    -60   -597  A    C  
ATOM   1250  CG  ARG A 172      33.875 -14.911  -4.390  1.00 82.44      A    C  
ANISOU 1250  CG  ARG A 172     8979  10198  12148  -1939    111   -626  A    C  
ATOM   1251  CD  ARG A 172      33.144 -16.106  -3.833  1.00 98.46      A    C  
ANISOU 1251  CD  ARG A 172    11068  12087  14254  -2153    174   -667  A    C  
ATOM   1252  NE  ARG A 172      31.760 -15.769  -3.506  1.00113.73      A    N  
ANISOU 1252  NE  ARG A 172    12818  14068  16325  -2284    327   -723  A    N  
ATOM   1253  CZ  ARG A 172      30.788 -15.629  -4.405  1.00123.97      A    C  
ANISOU 1253  CZ  ARG A 172    13864  15478  17762  -2265    281   -829  A    C  
ATOM   1254  NH1 ARG A 172      31.036 -15.790  -5.702  1.00125.76      A    N1+
ANISOU 1254  NH1 ARG A 172    14011  15780  17991  -2123     84   -892  A    N1+
ATOM   1255  NH2 ARG A 172      29.562 -15.323  -4.008  1.00129.11      A    N  
ANISOU 1255  NH2 ARG A 172    14338  16169  18548  -2385    432   -875  A    N  
ATOM   1256  N   ALA A 173      34.822 -12.058  -4.842  1.00 69.93      A    N  
ANISOU 1256  N   ALA A 173     7263   8865  10442  -1614    119   -514  A    N  
ATOM   1257  CA  ALA A 173      34.433 -10.990  -3.924  1.00 70.83      A    C  
ANISOU 1257  CA  ALA A 173     7360   8993  10559  -1655    285   -470  A    C  
ATOM   1258  C   ALA A 173      33.601 -11.515  -2.753  1.00 72.61      A    C  
ANISOU 1258  C   ALA A 173     7641   9112  10836  -1864    456   -485  A    C  
ATOM   1259  O   ALA A 173      32.876 -12.503  -2.882  1.00 75.68      A    O  
ANISOU 1259  O   ALA A 173     7983   9456  11316  -1981    458   -555  A    O  
ATOM   1260  CB  ALA A 173      33.676  -9.912  -4.660  1.00 42.56      A    C  
ANISOU 1260  CB  ALA A 173     3550   5558   7063  -1548    290   -517  A    C  
ATOM   1261  N   PHE A 174      33.711 -10.847  -1.610  1.00 73.21      A    N  
ANISOU 1261  N   PHE A 174     7825   9143  10847  -1917    604   -420  A    N  
ATOM   1262  CA  PHE A 174      32.907 -11.203  -0.450  1.00 78.64      A    C  
ANISOU 1262  CA  PHE A 174     8574   9741  11565  -2112    798   -428  A    C  
ATOM   1263  C   PHE A 174      32.269  -9.961   0.170  1.00 90.46      A    C  
ANISOU 1263  C   PHE A 174     9992  11295  13085  -2107    978   -431  A    C  
ATOM   1264  O   PHE A 174      32.490  -8.837  -0.290  1.00 91.34      A    O  
ANISOU 1264  O   PHE A 174    10014  11503  13189  -1953    938   -422  A    O  
ATOM   1265  CB  PHE A 174      33.734 -11.990   0.578  1.00 81.14      A    C  
ANISOU 1265  CB  PHE A 174     9189   9896  11746  -2220    811   -343  A    C  
ATOM   1266  CG  PHE A 174      34.683 -11.144   1.384  1.00 80.84      A    C  
ANISOU 1266  CG  PHE A 174     9329   9830  11558  -2168    836   -247  A    C  
ATOM   1267  CD1 PHE A 174      35.935 -10.815   0.890  1.00 81.41      A    C  
ANISOU 1267  CD1 PHE A 174     9457   9932  11545  -2014    668   -190  A    C  
ATOM   1268  CD2 PHE A 174      34.329 -10.692   2.644  1.00 74.00      A    C  
ANISOU 1268  CD2 PHE A 174     8576   8907  10632  -2278   1028   -216  A    C  
ATOM   1269  CE1 PHE A 174      36.809 -10.039   1.634  1.00 82.09      A    C  
ANISOU 1269  CE1 PHE A 174     9697   9989  11504  -1979    678   -105  A    C  
ATOM   1270  CE2 PHE A 174      35.193  -9.921   3.389  1.00 76.23      A    C  
ANISOU 1270  CE2 PHE A 174     9034   9157  10772  -2236   1036   -137  A    C  
ATOM   1271  CZ  PHE A 174      36.437  -9.589   2.884  1.00 79.52      A    C  
ANISOU 1271  CZ  PHE A 174     9493   9601  11118  -2090    853    -81  A    C  
ATOM   1272  N   SER A 175      31.457 -10.177   1.200  1.00105.61      A    N  
ANISOU 1272  N   SER A 175    11945  13150  15031  -2277   1182   -446  A    N  
ATOM   1273  CA  SER A 175      30.737  -9.101   1.877  1.00110.75      A    C  
ANISOU 1273  CA  SER A 175    12524  13846  15711  -2283   1384   -465  A    C  
ATOM   1274  C   SER A 175      30.096  -9.645   3.143  1.00119.77      A    C  
ANISOU 1274  C   SER A 175    13782  14886  16838  -2498   1612   -463  A    C  
ATOM   1275  O   SER A 175      30.421 -10.746   3.592  1.00113.36      A    O  
ANISOU 1275  O   SER A 175    13156  13954  15960  -2632   1599   -421  A    O  
ATOM   1276  CB  SER A 175      29.659  -8.523   0.963  1.00103.85      A    C  
ANISOU 1276  CB  SER A 175    11320  13114  15023  -2195   1386   -564  A    C  
ATOM   1277  OG  SER A 175      28.807  -9.554   0.490  1.00 99.98      A    O  
ANISOU 1277  OG  SER A 175    10677  12633  14677  -2303   1369   -641  A    O  
ATOM   1278  N   LEU A 176      29.173  -8.880   3.716  1.00136.33      A    N  
ANISOU 1278  N   LEU A 176    15774  17028  18995  -2527   1828   -507  A    N  
ATOM   1279  CA  LEU A 176      28.512  -9.323   4.936  1.00146.85      A    C  
ANISOU 1279  CA  LEU A 176    17212  18276  20307  -2732   2078   -506  A    C  
ATOM   1280  C   LEU A 176      27.011  -9.016   4.994  1.00148.70      A    C  
ANISOU 1280  C   LEU A 176    17168  18600  20732  -2790   2290   -609  A    C  
ATOM   1281  O   LEU A 176      26.594  -8.079   5.670  1.00158.02      A    O  
ANISOU 1281  O   LEU A 176    18333  19809  21899  -2766   2482   -628  A    O  
ATOM   1282  CB  LEU A 176      29.233  -8.760   6.174  1.00147.97      A    C  
ANISOU 1282  CB  LEU A 176    17658  18330  20236  -2749   2184   -424  A    C  
ATOM   1283  CG  LEU A 176      28.928  -9.366   7.554  1.00146.66      A    C  
ANISOU 1283  CG  LEU A 176    17719  18042  19965  -2966   2412   -388  A    C  
ATOM   1284  CD1 LEU A 176      29.085 -10.889   7.563  1.00142.11      A    C  
ANISOU 1284  CD1 LEU A 176    17265  17353  19378  -3125   2341   -348  A    C  
ATOM   1285  CD2 LEU A 176      29.801  -8.725   8.631  1.00142.36      A    C  
ANISOU 1285  CD2 LEU A 176    17487  17416  19187  -2949   2456   -308  A    C  
ATOM   1286  N   ALA A 177      26.207  -9.795   4.272  0.75139.80      A    N  
ANISOU 1286  N   ALA A 177    15814  17516  19789  -2861   2249   -681  A    N  
ATOM   1287  CA  ALA A 177      24.804  -9.967   4.639  0.75134.68      A    C  
ANISOU 1287  CA  ALA A 177    14953  16906  19312  -3006   2483   -762  A    C  
ATOM   1288  C   ALA A 177      24.963 -10.883   5.842  0.75130.62      A    C  
ANISOU 1288  C   ALA A 177    14727  16237  18666  -3236   2647   -692  A    C  
ATOM   1289  O   ALA A 177      25.496 -10.460   6.868  0.75127.84      A    O  
ANISOU 1289  O   ALA A 177    14636  15814  18125  -3248   2766   -622  A    O  
ATOM   1290  CB  ALA A 177      24.049 -10.654   3.531  0.75131.93      A    C  
ANISOU 1290  CB  ALA A 177    14314  16630  19183  -3034   2355   -851  A    C  
ATOM   1291  N   PRO A 182      23.184 -15.410   5.514  1.00136.90      A    N  
ANISOU 1291  N   PRO A 182    15425  16771  19820  -3960   2674   -756  A    N  
ATOM   1292  CA  PRO A 182      24.176 -16.438   5.823  1.00137.77      A    C  
ANISOU 1292  CA  PRO A 182    15893  16695  19758  -4040   2557   -655  A    C  
ATOM   1293  C   PRO A 182      24.794 -16.682   4.450  1.00139.37      A    C  
ANISOU 1293  C   PRO A 182    16015  16933  20005  -3868   2216   -694  A    C  
ATOM   1294  O   PRO A 182      24.051 -16.976   3.513  1.00142.07      A    O  
ANISOU 1294  O   PRO A 182    16078  17351  20550  -3882   2128   -798  A    O  
ATOM   1295  CB  PRO A 182      23.333 -17.641   6.261  1.00137.89      A    C  
ANISOU 1295  CB  PRO A 182    15916  16598  19877  -4337   2709   -662  A    C  
ATOM   1296  CG  PRO A 182      21.926 -17.111   6.439  1.00141.01      A    C  
ANISOU 1296  CG  PRO A 182    15975  17129  20474  -4425   2966   -754  A    C  
ATOM   1297  CD  PRO A 182      21.819 -15.955   5.486  1.00139.22      A    C  
ANISOU 1297  CD  PRO A 182    15453  17097  20348  -4164   2834   -841  A    C  
ATOM   1298  N   ASN A 183      26.102 -16.509   4.301  1.00134.34      A    N  
ANISOU 1298  N   ASN A 183    15601  16255  19186  -3701   2029   -621  A    N  
ATOM   1299  CA  ASN A 183      26.708 -16.522   2.968  1.00124.09      A    C  
ANISOU 1299  CA  ASN A 183    14209  15021  17918  -3505   1731   -662  A    C  
ATOM   1300  C   ASN A 183      26.561 -17.848   2.225  1.00121.34      A    C  
ANISOU 1300  C   ASN A 183    13842  14589  17671  -3601   1570   -713  A    C  
ATOM   1301  O   ASN A 183      26.564 -18.917   2.829  1.00117.96      A    O  
ANISOU 1301  O   ASN A 183    13612  13994  17214  -3792   1624   -669  A    O  
ATOM   1302  CB  ASN A 183      28.179 -16.104   3.030  1.00118.72      A    C  
ANISOU 1302  CB  ASN A 183    13772  14311  17027  -3322   1584   -568  A    C  
ATOM   1303  CG  ASN A 183      28.356 -14.599   3.069  1.00117.12      A    C  
ANISOU 1303  CG  ASN A 183    13479  14243  16776  -3142   1628   -560  A    C  
ATOM   1304  ND2 ASN A 183      29.486 -14.150   3.613  1.00114.64      A    N  
ANISOU 1304  ND2 ASN A 183    13409  13881  16268  -3052   1591   -463  A    N  
ATOM   1305  OD1 ASN A 183      27.491 -13.847   2.610  1.00115.34      A    O  
ANISOU 1305  OD1 ASN A 183    12970  14160  16693  -3084   1686   -642  A    O  
ATOM   1306  N   ARG A 184      26.434 -17.768   0.906  1.00122.81      A    N  
ANISOU 1306  N   ARG A 184    13804  14887  17970  -3465   1367   -807  A    N  
ATOM   1307  CA  ARG A 184      26.282 -18.959   0.079  1.00125.97      A    C  
ANISOU 1307  CA  ARG A 184    14177  15218  18468  -3536   1192   -876  A    C  
ATOM   1308  C   ARG A 184      27.490 -19.182  -0.823  1.00120.34      A    C  
ANISOU 1308  C   ARG A 184    13592  14490  17641  -3333    917   -865  A    C  
ATOM   1309  O   ARG A 184      27.337 -19.379  -2.032  1.00113.20      A    O  
ANISOU 1309  O   ARG A 184    12528  13658  16825  -3243    728   -961  A    O  
ATOM   1310  CB  ARG A 184      25.013 -18.859  -0.768  1.00134.52      A    C  
ANISOU 1310  CB  ARG A 184    14887  16436  19789  -3570   1171  -1014  A    C  
ATOM   1311  CG  ARG A 184      23.733 -18.989   0.039  1.00143.55      A    C  
ANISOU 1311  CG  ARG A 184    15884  17573  21086  -3813   1435  -1042  A    C  
ATOM   1312  CD  ARG A 184      22.518 -19.147  -0.858  1.00149.35      A    C  
ANISOU 1312  CD  ARG A 184    16251  18418  22077  -3870   1374  -1185  A    C  
ATOM   1313  NE  ARG A 184      21.410 -19.786  -0.154  1.00153.40      A    N  
ANISOU 1313  NE  ARG A 184    16667  18868  22749  -4163   1592  -1211  A    N  
ATOM   1314  CZ  ARG A 184      21.274 -21.102  -0.017  1.00154.02      A    C  
ANISOU 1314  CZ  ARG A 184    16872  18777  22870  -4387   1576  -1213  A    C  
ATOM   1315  NH1 ARG A 184      22.181 -21.922  -0.536  1.00152.88      A    N1+
ANISOU 1315  NH1 ARG A 184    16960  18507  22622  -4336   1345  -1197  A    N1+
ATOM   1316  NH2 ARG A 184      20.235 -21.601   0.640  1.00153.59      A    N  
ANISOU 1316  NH2 ARG A 184    16714  18675  22967  -4662   1796  -1231  A    N  
ATOM   1317  N   TYR A 185      28.687 -19.150  -0.235  1.00121.82      A    N  
ANISOU 1317  N   TYR A 185    14067  14587  17634  -3261    897   -751  A    N  
ATOM   1318  CA  TYR A 185      29.926 -19.293  -1.010  1.00117.76      A    C  
ANISOU 1318  CA  TYR A 185    13671  14066  17008  -3057    659   -732  A    C  
ATOM   1319  C   TYR A 185      30.282 -20.768  -1.206  1.00115.01      A    C  
ANISOU 1319  C   TYR A 185    13507  13536  16654  -3140    528   -743  A    C  
ATOM   1320  O   TYR A 185      29.861 -21.629  -0.426  1.00121.52      A    O  
ANISOU 1320  O   TYR A 185    14463  14203  17506  -3359    636   -718  A    O  
ATOM   1321  CB  TYR A 185      31.103 -18.518  -0.380  1.00109.23      A    C  
ANISOU 1321  CB  TYR A 185    12780  12986  15736  -2921    672   -612  A    C  
ATOM   1322  CG  TYR A 185      30.858 -17.027  -0.181  1.00101.59      A    C  
ANISOU 1322  CG  TYR A 185    11662  12177  14760  -2827    790   -599  A    C  
ATOM   1323  CD1 TYR A 185      30.151 -16.289  -1.117  1.00100.71      A    C  
ANISOU 1323  CD1 TYR A 185    11252  12239  14773  -2727    758   -690  A    C  
ATOM   1324  CD2 TYR A 185      31.350 -16.359   0.939  1.00 96.52      A    C  
ANISOU 1324  CD2 TYR A 185    11191  11502  13982  -2831    920   -498  A    C  
ATOM   1325  CE1 TYR A 185      29.925 -14.934  -0.940  1.00102.96      A    C  
ANISOU 1325  CE1 TYR A 185    11412  12652  15057  -2632    859   -678  A    C  
ATOM   1326  CE2 TYR A 185      31.128 -15.004   1.124  1.00 94.94      A    C  
ANISOU 1326  CE2 TYR A 185    10869  11429  13776  -2744   1024   -494  A    C  
ATOM   1327  CZ  TYR A 185      30.413 -14.298   0.180  1.00100.09      A    C  
ANISOU 1327  CZ  TYR A 185    11224  12245  14563  -2642    997   -583  A    C  
ATOM   1328  OH  TYR A 185      30.178 -12.953   0.344  1.00102.50      A    O  
ANISOU 1328  OH  TYR A 185    11414  12662  14868  -2545   1095   -580  A    O  
HETATM 1329  N   TPO A 186      31.062 -21.045  -2.249  1.00 99.52      A    N  
ANISOU 1329  N   TPO A 186    11565  11594  14655  -2962    303   -781  A    N  
HETATM 1330  CA  TPO A 186      31.340 -22.445  -2.700  1.00 95.56      A    C  
ANISOU 1330  CA  TPO A 186    11208  10931  14171  -3008    148   -825  A    C  
HETATM 1331  C   TPO A 186      32.407 -23.149  -1.894  1.00104.54      A    C  
ANISOU 1331  C   TPO A 186    12681  11872  15166  -3019    125   -714  A    C  
HETATM 1332  O   TPO A 186      33.351 -22.515  -1.439  1.00107.32      A    O  
ANISOU 1332  O   TPO A 186    13147  12251  15380  -2893    131   -616  A    O  
HETATM 1333  CB  TPO A 186      31.618 -22.334  -4.197  1.00 82.34      A    C  
ANISOU 1333  CB  TPO A 186     9388   9380  12515  -2801    -66   -927  A    C  
HETATM 1334  CG2 TPO A 186      32.717 -23.281  -4.669  1.00 64.29      A    C  
ANISOU 1334  CG2 TPO A 186     7316   6970  10141  -2690   -252   -930  A    C  
HETATM 1335  OG1 TPO A 186      31.945 -20.960  -4.437  1.00 93.97      A    O  
ANISOU 1335  OG1 TPO A 186    10731  11046  13928  -2617    -49   -894  A    O  
HETATM 1336  P   TPO A 186      31.797 -20.223  -5.866  1.00106.58      A    P  
ANISOU 1336  P   TPO A 186    12084  12852  15560  -2418   -187   -988  A    P  
HETATM 1337  O1P TPO A 186      33.107 -20.492  -6.569  1.00100.14      A    O  
ANISOU 1337  O1P TPO A 186    11409  12025  14613  -2216   -361   -973  A    O  
HETATM 1338  O2P TPO A 186      30.607 -20.866  -6.539  1.00115.91      A    O1-
ANISOU 1338  O2P TPO A 186    13092  14040  16909  -2539   -243  -1125  A    O1-
HETATM 1339  O3P TPO A 186      31.567 -18.793  -5.452  1.00 98.56      A    O  
ANISOU 1339  O3P TPO A 186    10933  11981  14533  -2364    -50   -930  A    O  
ATOM   1340  N   ASN A 187      32.262 -24.463  -1.711  1.00113.05      A    N  
ANISOU 1340  N   ASN A 187    13924  12748  16283  -3170     90   -727  A    N  
ATOM   1341  CA  ASN A 187      33.069 -25.215  -0.740  1.00112.11      A    C  
ANISOU 1341  CA  ASN A 187    14143  12412  16042  -3225     93   -609  A    C  
ATOM   1342  C   ASN A 187      34.423 -25.761  -1.225  1.00115.90      A    C  
ANISOU 1342  C   ASN A 187    14805  12810  16422  -3020   -123   -592  A    C  
ATOM   1343  O   ASN A 187      35.430 -25.631  -0.526  1.00112.22      A    O  
ANISOU 1343  O   ASN A 187    14539  12282  15818  -2940   -136   -477  A    O  
ATOM   1344  CB  ASN A 187      32.245 -26.353  -0.136  1.00111.88      A    C  
ANISOU 1344  CB  ASN A 187    14235  12177  16096  -3507    185   -609  A    C  
ATOM   1345  CG  ASN A 187      32.885 -26.938   1.108  1.00116.22      A    C  
ANISOU 1345  CG  ASN A 187    15138  12510  16509  -3596    239   -463  A    C  
ATOM   1346  ND2 ASN A 187      33.661 -26.124   1.808  1.00111.45      A    N  
ANISOU 1346  ND2 ASN A 187    14634  11958  15753  -3488    283   -354  A    N  
ATOM   1347  OD1 ASN A 187      32.682 -28.109   1.438  1.00126.41      A    O  
ANISOU 1347  OD1 ASN A 187    16618  13581  17830  -3764    233   -448  A    O  
ATOM   1348  N   ARG A 188      34.447 -26.382  -2.402  1.00120.52      A    N  
ANISOU 1348  N   ARG A 188    15322  13393  17076  -2935   -294   -711  A    N  
ATOM   1349  CA  ARG A 188      35.683 -26.968  -2.928  1.00123.48      A    C  
ANISOU 1349  CA  ARG A 188    15858  13690  17370  -2734   -489   -713  A    C  
ATOM   1350  C   ARG A 188      36.684 -25.916  -3.427  1.00114.25      A    C  
ANISOU 1350  C   ARG A 188    14594  12714  16101  -2465   -555   -687  A    C  
ATOM   1351  O   ARG A 188      36.952 -25.816  -4.625  1.00112.07      A    O  
ANISOU 1351  O   ARG A 188    14194  12552  15837  -2291   -683   -781  A    O  
ATOM   1352  CB  ARG A 188      35.381 -27.977  -4.046  1.00134.94      A    C  
ANISOU 1352  CB  ARG A 188    17281  15072  18917  -2725   -644   -861  A    C  
ATOM   1353  CG  ARG A 188      34.721 -29.282  -3.594  1.00147.45      A    C  
ANISOU 1353  CG  ARG A 188    19031  16404  20588  -2971   -627   -879  A    C  
ATOM   1354  CD  ARG A 188      34.342 -30.142  -4.804  1.00155.85      A    C  
ANISOU 1354  CD  ARG A 188    20037  17423  21755  -2961   -789  -1047  A    C  
ATOM   1355  NE  ARG A 188      33.207 -31.028  -4.545  1.00160.60      A    N  
ANISOU 1355  NE  ARG A 188    20659  17863  22497  -3250   -735  -1097  A    N  
ATOM   1356  CZ  ARG A 188      32.354 -31.444  -5.480  1.00162.85      A    C  
ANISOU 1356  CZ  ARG A 188    20789  18169  22918  -3325   -820  -1253  A    C  
ATOM   1357  NH1 ARG A 188      32.497 -31.048  -6.739  1.00158.20      A    N1+
ANISOU 1357  NH1 ARG A 188    20028  17755  22324  -3124   -962  -1374  A    N1+
ATOM   1358  NH2 ARG A 188      31.350 -32.251  -5.158  1.00167.14      A    N  
ANISOU 1358  NH2 ARG A 188    21352  18557  23598  -3609   -763  -1288  A    N  
ATOM   1359  N   VAL A 189      37.241 -25.134  -2.507  1.00110.55      A    N  
ANISOU 1359  N   VAL A 189    14194  12280  15531  -2437   -467   -559  A    N  
ATOM   1360  CA  VAL A 189      38.275 -24.166  -2.868  1.00107.95      A    C  
ANISOU 1360  CA  VAL A 189    13795  12112  15109  -2202   -528   -519  A    C  
ATOM   1361  C   VAL A 189      39.565 -24.381  -2.076  1.00101.84      A    C  
ANISOU 1361  C   VAL A 189    13260  11222  14213  -2119   -585   -396  A    C  
ATOM   1362  O   VAL A 189      39.554 -24.976  -0.998  1.00 93.27      A    O  
ANISOU 1362  O   VAL A 189    12394   9952  13091  -2261   -538   -315  A    O  
ATOM   1363  CB  VAL A 189      37.792 -22.703  -2.713  1.00102.74      A    C  
ANISOU 1363  CB  VAL A 189    12933  11655  14449  -2203   -392   -495  A    C  
ATOM   1364  CG1 VAL A 189      37.021 -22.254  -3.955  1.00 99.97      A    C  
ANISOU 1364  CG1 VAL A 189    12306  11483  14194  -2145   -420   -621  A    C  
ATOM   1365  CG2 VAL A 189      36.956 -22.544  -1.455  1.00 95.97      A    C  
ANISOU 1365  CG2 VAL A 189    12135  10727  13602  -2432   -198   -432  A    C  
ATOM   1366  N   VAL A 190      40.671 -23.888  -2.625  1.00102.76      A    N  
ANISOU 1366  N   VAL A 190    13329  11449  14267  -1890   -689   -381  A    N  
ATOM   1367  CA  VAL A 190      41.994 -24.085  -2.040  1.00 99.44      A    C  
ANISOU 1367  CA  VAL A 190    13094  10939  13748  -1779   -776   -278  A    C  
ATOM   1368  C   VAL A 190      42.467 -25.511  -2.286  1.00 93.82      A    C  
ANISOU 1368  C   VAL A 190    12562  10032  13053  -1732   -917   -314  A    C  
ATOM   1369  O   VAL A 190      41.732 -26.463  -2.041  1.00 91.76      A    O  
ANISOU 1369  O   VAL A 190    12417   9601  12845  -1895   -899   -346  A    O  
ATOM   1370  CB  VAL A 190      42.016 -23.815  -0.512  1.00 76.56      A    C  
ANISOU 1370  CB  VAL A 190    10374   7945  10771  -1924   -673   -143  A    C  
ATOM   1371  CG1 VAL A 190      43.448 -23.702  -0.023  1.00 76.59      A    C  
ANISOU 1371  CG1 VAL A 190    10512   7914  10673  -1777   -782    -39  A    C  
ATOM   1372  CG2 VAL A 190      41.233 -22.555  -0.164  1.00 71.63      A    C  
ANISOU 1372  CG2 VAL A 190     9595   7474  10146  -2018   -502   -128  A    C  
ATOM   1373  N   THR A 191      43.693 -25.655  -2.781  1.00 94.37      A    N  
ANISOU 1373  N   THR A 191    12649  10123  13084  -1508  -1054   -311  A    N  
ATOM   1374  CA  THR A 191      44.304 -26.971  -2.905  1.00 88.76      A    C  
ANISOU 1374  CA  THR A 191    12128   9214  12383  -1432  -1194   -335  A    C  
ATOM   1375  C   THR A 191      44.334 -27.632  -1.548  1.00 91.63      A    C  
ANISOU 1375  C   THR A 191    12767   9343  12707  -1582  -1183   -221  A    C  
ATOM   1376  O   THR A 191      44.550 -26.984  -0.527  1.00 94.84      A    O  
ANISOU 1376  O   THR A 191    13235   9762  13038  -1642  -1119   -101  A    O  
ATOM   1377  CB  THR A 191      45.732 -26.904  -3.444  1.00 94.78      A    C  
ANISOU 1377  CB  THR A 191    12862  10043  13105  -1159  -1324   -329  A    C  
ATOM   1378  CG2 THR A 191      45.739 -27.185  -4.929  1.00101.52      A    C  
ANISOU 1378  CG2 THR A 191    13577  10991  14005  -1007  -1391   -478  A    C  
ATOM   1379  OG1 THR A 191      46.268 -25.593  -3.211  1.00101.31      A    O  
ANISOU 1379  OG1 THR A 191    13556  11061  13876  -1092  -1274   -246  A    O  
ATOM   1380  N   LEU A 192      44.122 -28.936  -1.556  1.00 99.25      A    N  
ANISOU 1380  N   LEU A 192    13913  10084  13715  -1642  -1251   -261  A    N  
ATOM   1381  CA  LEU A 192      43.967 -29.718  -0.342  1.00 97.65      A    C  
ANISOU 1381  CA  LEU A 192    13996   9628  13478  -1813  -1235   -159  A    C  
ATOM   1382  C   LEU A 192      44.942 -29.353   0.780  1.00 97.06      A    C  
ANISOU 1382  C   LEU A 192    14076   9514  13287  -1761  -1266      0  A    C  
ATOM   1383  O   LEU A 192      44.528 -29.149   1.921  1.00 98.95      A    O  
ANISOU 1383  O   LEU A 192    14452   9684  13463  -1945  -1161    104  A    O  
ATOM   1384  CB  LEU A 192      44.097 -31.196  -0.686  1.00 94.74      A    C  
ANISOU 1384  CB  LEU A 192    13815   9017  13163  -1788  -1366   -220  A    C  
ATOM   1385  CG  LEU A 192      43.628 -32.162   0.386  1.00 90.44      A    C  
ANISOU 1385  CG  LEU A 192    13568   8186  12607  -2009  -1337   -135  A    C  
ATOM   1386  CD1 LEU A 192      42.273 -31.714   0.911  1.00 87.87      A    C  
ANISOU 1386  CD1 LEU A 192    13177   7905  12304  -2297  -1129   -119  A    C  
ATOM   1387  CD2 LEU A 192      43.568 -33.543  -0.228  1.00 87.25      A    C  
ANISOU 1387  CD2 LEU A 192    13302   7564  12284  -1989  -1460   -232  A    C  
ATOM   1388  N   TRP A 193      46.229 -29.270   0.454  1.00 93.59      A    N  
ANISOU 1388  N   TRP A 193    13614   9123  12821  -1512  -1411     14  A    N  
ATOM   1389  CA  TRP A 193      47.268 -29.109   1.471  1.00 92.00      A    C  
ANISOU 1389  CA  TRP A 193    13573   8858  12523  -1444  -1489    156  A    C  
ATOM   1390  C   TRP A 193      47.199 -27.780   2.221  1.00 94.03      A    C  
ANISOU 1390  C   TRP A 193    13754   9275  12698  -1524  -1374    246  A    C  
ATOM   1391  O   TRP A 193      47.553 -27.702   3.401  1.00 95.51      A    O  
ANISOU 1391  O   TRP A 193    14139   9365  12788  -1587  -1389    373  A    O  
ATOM   1392  CB  TRP A 193      48.658 -29.310   0.867  1.00 90.77      A    C  
ANISOU 1392  CB  TRP A 193    13369   8736  12382  -1153  -1669    137  A    C  
ATOM   1393  CG  TRP A 193      48.858 -30.667   0.272  1.00 94.63      A    C  
ANISOU 1393  CG  TRP A 193    13978   9038  12939  -1054  -1793     56  A    C  
ATOM   1394  CD1 TRP A 193      48.040 -31.755   0.411  1.00 98.36      A    C  
ANISOU 1394  CD1 TRP A 193    14642   9282  13448  -1212  -1783     23  A    C  
ATOM   1395  CD2 TRP A 193      49.961 -31.095  -0.533  1.00 96.49      A    C  
ANISOU 1395  CD2 TRP A 193    14159   9287  13215   -776  -1944     -6  A    C  
ATOM   1396  CE2 TRP A 193      49.739 -32.451  -0.860  1.00101.10      A    C  
ANISOU 1396  CE2 TRP A 193    14918   9639  13857   -769  -2024    -82  A    C  
ATOM   1397  CE3 TRP A 193      51.113 -30.466  -1.013  1.00 96.03      A    C  
ANISOU 1397  CE3 TRP A 193    13917   9413  13155   -535  -2011     -7  A    C  
ATOM   1398  NE1 TRP A 193      48.559 -32.827  -0.273  1.00100.26      A    N  
ANISOU 1398  NE1 TRP A 193    14961   9385  13749  -1045  -1927    -60  A    N  
ATOM   1399  CZ2 TRP A 193      50.629 -33.186  -1.646  1.00 99.33      A    C  
ANISOU 1399  CZ2 TRP A 193    14697   9362  13683   -514  -2167   -165  A    C  
ATOM   1400  CZ3 TRP A 193      51.997 -31.199  -1.796  1.00 99.67      A    C  
ANISOU 1400  CZ3 TRP A 193    14366   9833  13670   -287  -2143    -86  A    C  
ATOM   1401  CH2 TRP A 193      51.748 -32.544  -2.105  1.00 96.34      A    C  
ANISOU 1401  CH2 TRP A 193    14127   9179  13300   -271  -2218   -168  A    C  
ATOM   1402  N   TYR A 194      46.737 -26.737   1.542  1.00 89.80      A    N  
ANISOU 1402  N   TYR A 194    12948   8976  12197  -1518  -1268    179  A    N  
ATOM   1403  CA  TYR A 194      46.609 -25.443   2.187  1.00 84.96      A    C  
ANISOU 1403  CA  TYR A 194    12257   8508  11514  -1589  -1153    250  A    C  
ATOM   1404  C   TYR A 194      45.173 -25.137   2.565  1.00 86.06      A    C  
ANISOU 1404  C   TYR A 194    12375   8657  11665  -1831   -952    232  A    C  
ATOM   1405  O   TYR A 194      44.883 -24.047   3.060  1.00 92.07      A    O  
ANISOU 1405  O   TYR A 194    13066   9539  12378  -1900   -832    272  A    O  
ATOM   1406  CB  TYR A 194      47.157 -24.339   1.294  1.00 76.09      A    C  
ANISOU 1406  CB  TYR A 194    10856   7639  10414  -1412  -1167    208  A    C  
ATOM   1407  CG  TYR A 194      48.564 -24.596   0.838  1.00 78.39      A    C  
ANISOU 1407  CG  TYR A 194    11128   7946  10711  -1171  -1344    217  A    C  
ATOM   1408  CD1 TYR A 194      49.640 -23.963   1.450  1.00 82.11      A    C  
ANISOU 1408  CD1 TYR A 194    11617   8464  11118  -1085  -1418    318  A    C  
ATOM   1409  CD2 TYR A 194      48.821 -25.482  -0.197  1.00 78.51      A    C  
ANISOU 1409  CD2 TYR A 194    11105   7928  10798  -1029  -1439    118  A    C  
ATOM   1410  CE1 TYR A 194      50.938 -24.198   1.033  1.00 85.54      A    C  
ANISOU 1410  CE1 TYR A 194    12006   8922  11575   -863  -1575    324  A    C  
ATOM   1411  CE2 TYR A 194      50.109 -25.726  -0.620  1.00 84.94      A    C  
ANISOU 1411  CE2 TYR A 194    11888   8762  11624   -798  -1585    120  A    C  
ATOM   1412  CZ  TYR A 194      51.165 -25.082  -0.004  1.00 90.10      A    C  
ANISOU 1412  CZ  TYR A 194    12536   9471  12227   -716  -1650    224  A    C  
ATOM   1413  OH  TYR A 194      52.450 -25.324  -0.435  1.00 93.84      A    O  
ANISOU 1413  OH  TYR A 194    12950   9974  12730   -485  -1790    223  A    O  
ATOM   1414  N   ARG A 195      44.274 -26.088   2.331  1.00 81.84      A    N  
ANISOU 1414  N   ARG A 195    11895   7996  11202  -1959   -914    166  A    N  
ATOM   1415  CA  ARG A 195      42.880 -25.872   2.687  1.00 83.73      A    C  
ANISOU 1415  CA  ARG A 195    12095   8246  11474  -2196   -716    145  A    C  
ATOM   1416  C   ARG A 195      42.735 -25.888   4.193  1.00 90.82      A    C  
ANISOU 1416  C   ARG A 195    13247   9005  12257  -2373   -620    276  A    C  
ATOM   1417  O   ARG A 195      43.330 -26.731   4.865  1.00 91.87      A    O  
ANISOU 1417  O   ARG A 195    13651   8935  12321  -2378   -718    361  A    O  
ATOM   1418  CB  ARG A 195      41.961 -26.909   2.056  1.00 85.06      A    C  
ANISOU 1418  CB  ARG A 195    12250   8310  11760  -2304   -706     41  A    C  
ATOM   1419  CG  ARG A 195      40.485 -26.577   2.221  1.00 93.17      A    C  
ANISOU 1419  CG  ARG A 195    13156   9392  12854  -2534   -501     -3  A    C  
ATOM   1420  CD  ARG A 195      39.605 -27.565   1.484  1.00 98.61      A    C  
ANISOU 1420  CD  ARG A 195    13797   9993  13677  -2637   -514   -119  A    C  
ATOM   1421  NE  ARG A 195      40.055 -27.764   0.113  1.00 98.89      A    N  
ANISOU 1421  NE  ARG A 195    13687  10110  13775  -2430   -677   -236  A    N  
ATOM   1422  CZ  ARG A 195      39.761 -28.834  -0.615  1.00100.39      A    C  
ANISOU 1422  CZ  ARG A 195    13906  10184  14056  -2448   -770   -338  A    C  
ATOM   1423  NH1 ARG A 195      39.016 -29.803  -0.096  1.00101.03      A    N1+
ANISOU 1423  NH1 ARG A 195    14146  10054  14186  -2674   -718   -331  A    N1+
ATOM   1424  NH2 ARG A 195      40.217 -28.936  -1.856  1.00 97.50      A    N  
ANISOU 1424  NH2 ARG A 195    13417   9906  13724  -2245   -910   -447  A    N  
ATOM   1425  N   PRO A 196      41.951 -24.938   4.726  1.00 92.07      A    N  
ANISOU 1425  N   PRO A 196    13323   9272  12388  -2508   -428    292  A    N  
ATOM   1426  CA  PRO A 196      41.712 -24.766   6.160  1.00 95.44      A    C  
ANISOU 1426  CA  PRO A 196    13977   9600  12688  -2682   -299    407  A    C  
ATOM   1427  C   PRO A 196      40.569 -25.659   6.627  1.00103.05      A    C  
ANISOU 1427  C   PRO A 196    15069  10399  13687  -2935   -154    406  A    C  
ATOM   1428  O   PRO A 196      39.754 -26.069   5.800  1.00105.63      A    O  
ANISOU 1428  O   PRO A 196    15230  10746  14157  -2992   -118    298  A    O  
ATOM   1429  CB  PRO A 196      41.308 -23.298   6.257  1.00 87.87      A    C  
ANISOU 1429  CB  PRO A 196    12817   8857  11713  -2688   -149    389  A    C  
ATOM   1430  CG  PRO A 196      40.642 -23.007   4.955  1.00 79.64      A    C  
ANISOU 1430  CG  PRO A 196    11450   7981  10829  -2634   -123    253  A    C  
ATOM   1431  CD  PRO A 196      41.239 -23.927   3.925  1.00 82.33      A    C  
ANISOU 1431  CD  PRO A 196    11767   8271  11243  -2488   -323    194  A    C  
ATOM   1432  N   PRO A 197      40.508 -25.945   7.938  1.00105.86      A    N  
ANISOU 1432  N   PRO A 197    15720  10593  13909  -3092    -72    525  A    N  
ATOM   1433  CA  PRO A 197      39.556 -26.873   8.569  1.00106.76      A    C  
ANISOU 1433  CA  PRO A 197    16018  10517  14029  -3350     71    556  A    C  
ATOM   1434  C   PRO A 197      38.099 -26.583   8.224  1.00108.70      A    C  
ANISOU 1434  C   PRO A 197    16017  10874  14411  -3525    297    456  A    C  
ATOM   1435  O   PRO A 197      37.346 -27.514   7.960  1.00117.66      A    O  
ANISOU 1435  O   PRO A 197    17158  11894  15655  -3675    338    412  A    O  
ATOM   1436  CB  PRO A 197      39.779 -26.639  10.062  1.00106.22      A    C  
ANISOU 1436  CB  PRO A 197    16252  10350  13755  -3457    159    702  A    C  
ATOM   1437  CG  PRO A 197      41.157 -26.120  10.160  1.00106.90      A    C  
ANISOU 1437  CG  PRO A 197    16394  10487  13736  -3228    -42    758  A    C  
ATOM   1438  CD  PRO A 197      41.386 -25.303   8.929  1.00101.69      A    C  
ANISOU 1438  CD  PRO A 197    15371  10064  13201  -3032   -110    642  A    C  
ATOM   1439  N   GLU A 198      37.709 -25.315   8.240  1.00105.72      A    N  
ANISOU 1439  N   GLU A 198    15425  10710  14033  -3507    435    421  A    N  
ATOM   1440  CA  GLU A 198      36.342 -24.926   7.917  1.00108.46      A    C  
ANISOU 1440  CA  GLU A 198    15507  11182  14519  -3648    644    323  A    C  
ATOM   1441  C   GLU A 198      35.855 -25.586   6.637  1.00113.34      A    C  
ANISOU 1441  C   GLU A 198    15910  11818  15336  -3633    553    194  A    C  
ATOM   1442  O   GLU A 198      34.808 -26.229   6.610  1.00120.46      A    O  
ANISOU 1442  O   GLU A 198    16770  12650  16349  -3836    669    149  A    O  
ATOM   1443  CB  GLU A 198      36.250 -23.410   7.743  1.00108.79      A    C  
ANISOU 1443  CB  GLU A 198    15305  11471  14558  -3536    726    280  A    C  
ATOM   1444  CG  GLU A 198      37.011 -22.617   8.778  1.00108.03      A    C  
ANISOU 1444  CG  GLU A 198    15402  11381  14265  -3484    747    388  A    C  
ATOM   1445  CD  GLU A 198      38.322 -22.062   8.262  1.00104.77      A    C  
ANISOU 1445  CD  GLU A 198    14949  11056  13804  -3224    520    401  A    C  
ATOM   1446  OE1 GLU A 198      38.310 -21.001   7.598  1.00 96.00      A    O  
ANISOU 1446  OE1 GLU A 198    13579  10145  12751  -3095    523    335  A    O  
ATOM   1447  OE2 GLU A 198      39.369 -22.675   8.546  1.00112.69      A    O1-
ANISOU 1447  OE2 GLU A 198    16180  11924  14712  -3149    342    481  A    O1-
ATOM   1448  N   LEU A 199      36.619 -25.405   5.568  1.00110.34      A    N  
ANISOU 1448  N   LEU A 199    15391  11537  14996  -3396    347    132  A    N  
ATOM   1449  CA  LEU A 199      36.228 -25.904   4.259  1.00108.17      A    C  
ANISOU 1449  CA  LEU A 199    14907  11303  14889  -3350    244     -3  A    C  
ATOM   1450  C   LEU A 199      36.084 -27.426   4.238  1.00105.44      A    C  
ANISOU 1450  C   LEU A 199    14757  10713  14595  -3475    170     -8  A    C  
ATOM   1451  O   LEU A 199      35.221 -27.973   3.552  1.00107.04      A    O  
ANISOU 1451  O   LEU A 199    14820  10902  14950  -3577    179   -114  A    O  
ATOM   1452  CB  LEU A 199      37.234 -25.436   3.208  1.00102.13      A    C  
ANISOU 1452  CB  LEU A 199    14006  10678  14119  -3060     41    -52  A    C  
ATOM   1453  CG  LEU A 199      37.321 -23.913   3.144  1.00 97.55      A    C  
ANISOU 1453  CG  LEU A 199    13225  10335  13505  -2947    112    -50  A    C  
ATOM   1454  CD1 LEU A 199      38.245 -23.464   2.025  1.00 96.73      A    C  
ANISOU 1454  CD1 LEU A 199    12974  10374  13405  -2679    -71    -98  A    C  
ATOM   1455  CD2 LEU A 199      35.930 -23.324   2.969  1.00 91.08      A    C  
ANISOU 1455  CD2 LEU A 199    12154   9649  12805  -3079    299   -131  A    C  
ATOM   1456  N   LEU A 200      36.935 -28.102   4.994  1.00 98.40      A    N  
ANISOU 1456  N   LEU A 200    14193   9619  13577  -3465     87    107  A    N  
ATOM   1457  CA  LEU A 200      36.898 -29.548   5.053  1.00102.35      A    C  
ANISOU 1457  CA  LEU A 200    14920   9857  14111  -3572      7    119  A    C  
ATOM   1458  C   LEU A 200      35.649 -30.009   5.795  1.00107.89      A    C  
ANISOU 1458  C   LEU A 200    15692  10442  14859  -3897    229    145  A    C  
ATOM   1459  O   LEU A 200      35.053 -31.024   5.436  1.00109.56      A    O  
ANISOU 1459  O   LEU A 200    15928  10509  15190  -4038    212     88  A    O  
ATOM   1460  CB  LEU A 200      38.167 -30.077   5.715  1.00103.55      A    C  
ANISOU 1460  CB  LEU A 200    15408   9825  14112  -3459   -148    246  A    C  
ATOM   1461  CG  LEU A 200      39.431 -29.698   4.944  1.00103.12      A    C  
ANISOU 1461  CG  LEU A 200    15265   9884  14032  -3139   -365    215  A    C  
ATOM   1462  CD1 LEU A 200      40.685 -30.022   5.738  1.00107.28      A    C  
ANISOU 1462  CD1 LEU A 200    16092  10260  14408  -3024   -507    351  A    C  
ATOM   1463  CD2 LEU A 200      39.451 -30.388   3.588  1.00102.64      A    C  
ANISOU 1463  CD2 LEU A 200    15073   9816  14110  -3026   -518     73  A    C  
ATOM   1464  N   LEU A 201      35.248 -29.251   6.814  1.00105.54      A    N  
ANISOU 1464  N   LEU A 201    15422  10208  14471  -4019    444    226  A    N  
ATOM   1465  CA  LEU A 201      34.030 -29.545   7.564  1.00110.14      A    C  
ANISOU 1465  CA  LEU A 201    16044  10713  15092  -4330    697    253  A    C  
ATOM   1466  C   LEU A 201      32.775 -29.176   6.781  1.00116.50      A    C  
ANISOU 1466  C   LEU A 201    16466  11694  16105  -4426    820    106  A    C  
ATOM   1467  O   LEU A 201      31.659 -29.334   7.279  1.00124.23      A    O  
ANISOU 1467  O   LEU A 201    17403  12646  17154  -4683   1046    107  A    O  
ATOM   1468  CB  LEU A 201      34.032 -28.832   8.918  1.00109.65      A    C  
ANISOU 1468  CB  LEU A 201    16146  10666  14848  -4416    897    380  A    C  
ATOM   1469  CG  LEU A 201      34.948 -29.431   9.988  1.00111.15      A    C  
ANISOU 1469  CG  LEU A 201    16778  10626  14830  -4425    823    546  A    C  
ATOM   1470  CD1 LEU A 201      34.663 -28.823  11.357  1.00108.25      A    C  
ANISOU 1470  CD1 LEU A 201    16582  10263  14287  -4570   1062    659  A    C  
ATOM   1471  CD2 LEU A 201      34.790 -30.948  10.028  1.00106.31      A    C  
ANISOU 1471  CD2 LEU A 201    16399   9729  14265  -4578    760    579  A    C  
ATOM   1472  N   GLY A 202      32.965 -28.677   5.562  1.00110.44      A    N  
ANISOU 1472  N   GLY A 202    15419  11110  15434  -4218    672    -16  A    N  
ATOM   1473  CA  GLY A 202      31.862 -28.419   4.652  1.00107.58      A    C  
ANISOU 1473  CA  GLY A 202    14694  10908  15274  -4276    726   -164  A    C  
ATOM   1474  C   GLY A 202      31.329 -26.999   4.686  1.00108.56      A    C  
ANISOU 1474  C   GLY A 202    14536  11293  15419  -4231    887   -198  A    C  
ATOM   1475  O   GLY A 202      30.250 -26.726   4.156  1.00103.02      A    O  
ANISOU 1475  O   GLY A 202    13533  10721  14888  -4313    974   -307  A    O  
ATOM   1476  N   GLU A 203      32.092 -26.093   5.293  1.00115.33      A    N  
ANISOU 1476  N   GLU A 203    15488  12222  16110  -4095    913   -109  A    N  
ATOM   1477  CA  GLU A 203      31.687 -24.693   5.444  1.00113.34      A    C  
ANISOU 1477  CA  GLU A 203    15014  12195  15856  -4041   1067   -130  A    C  
ATOM   1478  C   GLU A 203      31.343 -23.994   4.125  1.00109.99      A    C  
ANISOU 1478  C   GLU A 203    14216  11995  15580  -3882    976   -268  A    C  
ATOM   1479  O   GLU A 203      31.946 -24.267   3.085  1.00107.62      A    O  
ANISOU 1479  O   GLU A 203    13868  11715  15309  -3713    749   -325  A    O  
ATOM   1480  CB  GLU A 203      32.775 -23.901   6.171  1.00109.79      A    C  
ANISOU 1480  CB  GLU A 203    14752  11767  15196  -3892   1047    -19  A    C  
ATOM   1481  CG  GLU A 203      32.420 -22.442   6.395  1.00114.89      A    C  
ANISOU 1481  CG  GLU A 203    15206  12620  15827  -3832   1203    -37  A    C  
ATOM   1482  CD  GLU A 203      31.274 -22.267   7.372  1.00124.17      A    C  
ANISOU 1482  CD  GLU A 203    16374  13787  17018  -4068   1509    -23  A    C  
ATOM   1483  OE1 GLU A 203      31.437 -22.638   8.553  1.00129.08      A    O  
ANISOU 1483  OE1 GLU A 203    17299  14257  17491  -4206   1622     88  A    O  
ATOM   1484  OE2 GLU A 203      30.214 -21.751   6.963  1.00125.75      A    O1-
ANISOU 1484  OE2 GLU A 203    16266  14135  17377  -4110   1639   -122  A    O1-
ATOM   1485  N   ARG A 204      30.369 -23.088   4.184  1.00106.82      A    N  
ANISOU 1485  N   ARG A 204    13559  11761  15269  -3933   1159   -322  A    N  
ATOM   1486  CA  ARG A 204      29.968 -22.305   3.021  1.00104.83      A    C  
ANISOU 1486  CA  ARG A 204    12955  11726  15150  -3782   1085   -442  A    C  
ATOM   1487  C   ARG A 204      29.873 -20.825   3.381  1.00105.99      A    C  
ANISOU 1487  C   ARG A 204    12975  12049  15249  -3681   1221   -424  A    C  
ATOM   1488  O   ARG A 204      29.788 -19.964   2.503  1.00102.70      A    O  
ANISOU 1488  O   ARG A 204    12311  11813  14898  -3510   1146   -496  A    O  
ATOM   1489  CB  ARG A 204      28.639 -22.814   2.454  1.00107.94      A    C  
ANISOU 1489  CB  ARG A 204    13096  12148  15769  -3948   1134   -562  A    C  
ATOM   1490  CG  ARG A 204      28.725 -24.222   1.883  1.00118.37      A    C  
ANISOU 1490  CG  ARG A 204    14518  13303  17156  -4027    965   -605  A    C  
ATOM   1491  CD  ARG A 204      27.405 -24.688   1.289  1.00132.56      A    C  
ANISOU 1491  CD  ARG A 204    16049  15133  19186  -4198    996   -733  A    C  
ATOM   1492  NE  ARG A 204      26.971 -23.848   0.175  1.00139.20      A    N  
ANISOU 1492  NE  ARG A 204    16542  16203  20144  -4039    904   -852  A    N  
ATOM   1493  CZ  ARG A 204      27.448 -23.937  -1.064  1.00138.42      A    C  
ANISOU 1493  CZ  ARG A 204    16375  16164  20055  -3848    651   -931  A    C  
ATOM   1494  NH1 ARG A 204      28.390 -24.828  -1.358  1.00134.13      A    N1+
ANISOU 1494  NH1 ARG A 204    16073  15470  19421  -3783    470   -913  A    N1+
ATOM   1495  NH2 ARG A 204      26.987 -23.129  -2.011  1.00137.08      A    N  
ANISOU 1495  NH2 ARG A 204    15901  16202  19980  -3713    580  -1029  A    N  
ATOM   1496  N   ASP A 205      29.895 -20.539   4.680  1.00108.77      A    N  
ANISOU 1496  N   ASP A 205    13514  12336  15476  -3785   1418   -329  A    N  
ATOM   1497  CA  ASP A 205      29.868 -19.165   5.174  1.00109.52      A    C  
ANISOU 1497  CA  ASP A 205    13542  12566  15503  -3698   1556   -308  A    C  
ATOM   1498  C   ASP A 205      31.223 -18.768   5.762  1.00108.80      A    C  
ANISOU 1498  C   ASP A 205    13729  12422  15188  -3567   1470   -194  A    C  
ATOM   1499  O   ASP A 205      31.448 -18.861   6.969  1.00111.26      A    O  
ANISOU 1499  O   ASP A 205    14305  12619  15349  -3674   1593    -98  A    O  
ATOM   1500  CB  ASP A 205      28.774 -18.994   6.228  1.00110.92      A    C  
ANISOU 1500  CB  ASP A 205    13702  12733  15707  -3912   1871   -302  A    C  
ATOM   1501  CG  ASP A 205      28.588 -17.552   6.642  1.00116.98      A    C  
ANISOU 1501  CG  ASP A 205    14367  13646  16432  -3815   2024   -308  A    C  
ATOM   1502  OD1 ASP A 205      29.064 -16.654   5.916  1.00122.68      A    O  
ANISOU 1502  OD1 ASP A 205    14957  14499  17157  -3592   1884   -337  A    O  
ATOM   1503  OD2 ASP A 205      27.962 -17.315   7.694  1.00121.20      A    O1-
ANISOU 1503  OD2 ASP A 205    14963  14161  16928  -3961   2289   -284  A    O1-
ATOM   1504  N   TYR A 206      32.126 -18.322   4.901  1.00101.87      A    N  
ANISOU 1504  N   TYR A 206    12790  11629  14286  -3338   1255   -204  A    N  
ATOM   1505  CA  TYR A 206      33.465 -17.975   5.343  1.00102.00      A    C  
ANISOU 1505  CA  TYR A 206    13037  11602  14116  -3209   1145   -104  A    C  
ATOM   1506  C   TYR A 206      33.944 -16.650   4.753  1.00 97.18      A    C  
ANISOU 1506  C   TYR A 206    12261  11168  13495  -2991   1072   -123  A    C  
ATOM   1507  O   TYR A 206      33.204 -15.940   4.060  1.00 91.17      A    O  
ANISOU 1507  O   TYR A 206    11220  10559  12859  -2934   1117   -209  A    O  
ATOM   1508  CB  TYR A 206      34.443 -19.088   4.969  1.00 98.58      A    C  
ANISOU 1508  CB  TYR A 206    12778  11037  13639  -3155    918    -67  A    C  
ATOM   1509  CG  TYR A 206      34.462 -19.375   3.487  1.00 95.00      A    C  
ANISOU 1509  CG  TYR A 206    12108  10669  13320  -3024    738   -166  A    C  
ATOM   1510  CD1 TYR A 206      33.964 -20.567   2.982  1.00 93.63      A    C  
ANISOU 1510  CD1 TYR A 206    11917  10402  13257  -3124    683   -228  A    C  
ATOM   1511  CD2 TYR A 206      34.959 -18.443   2.590  1.00 90.98      A    C  
ANISOU 1511  CD2 TYR A 206    11420  10328  12820  -2808    625   -199  A    C  
ATOM   1512  CE1 TYR A 206      33.975 -20.825   1.625  1.00 88.72      A    C  
ANISOU 1512  CE1 TYR A 206    11113   9857  12742  -3003    513   -329  A    C  
ATOM   1513  CE2 TYR A 206      34.975 -18.692   1.238  1.00 87.65      A    C  
ANISOU 1513  CE2 TYR A 206    10819   9987  12497  -2687    466   -289  A    C  
ATOM   1514  CZ  TYR A 206      34.481 -19.881   0.758  1.00 84.92      A    C  
ANISOU 1514  CZ  TYR A 206    10465   9550  12251  -2781    408   -358  A    C  
ATOM   1515  OH  TYR A 206      34.498 -20.121  -0.596  1.00 79.17      A    O  
ANISOU 1515  OH  TYR A 206     9574   8901  11605  -2657    245   -456  A    O  
ATOM   1516  N   GLY A 207      35.199 -16.333   5.036  1.00 93.36      A    N  
ANISOU 1516  N   GLY A 207    11954  10657  12863  -2871    951    -39  A    N  
ATOM   1517  CA  GLY A 207      35.815 -15.130   4.519  1.00 97.87      A    C  
ANISOU 1517  CA  GLY A 207    12403  11371  13411  -2675    870    -40  A    C  
ATOM   1518  C   GLY A 207      37.325 -15.167   4.619  1.00 91.45      A    C  
ANISOU 1518  C   GLY A 207    11773  10508  12465  -2550    683     48  A    C  
ATOM   1519  O   GLY A 207      37.946 -16.229   4.481  1.00 88.99      A    O  
ANISOU 1519  O   GLY A 207    11593  10089  12132  -2543    543     75  A    O  
ATOM   1520  N   PRO A 208      37.924 -14.000   4.885  1.00 81.67      A    N  
ANISOU 1520  N   PRO A 208    10543   9342  11145  -2452    679     90  A    N  
ATOM   1521  CA  PRO A 208      39.377 -13.788   4.868  1.00 83.00      A    C  
ANISOU 1521  CA  PRO A 208    10824   9501  11212  -2317    497    165  A    C  
ATOM   1522  C   PRO A 208      40.192 -14.824   5.651  1.00 83.50      A    C  
ANISOU 1522  C   PRO A 208    11175   9388  11162  -2373    399    250  A    C  
ATOM   1523  O   PRO A 208      41.303 -15.142   5.236  1.00 81.24      A    O  
ANISOU 1523  O   PRO A 208    10924   9089  10853  -2247    208    285  A    O  
ATOM   1524  CB  PRO A 208      39.529 -12.400   5.482  1.00 78.86      A    C  
ANISOU 1524  CB  PRO A 208    10315   9038  10610  -2291    581    197  A    C  
ATOM   1525  CG  PRO A 208      38.262 -11.709   5.123  1.00 80.33      A    C  
ANISOU 1525  CG  PRO A 208    10277   9334  10910  -2313    748    110  A    C  
ATOM   1526  CD  PRO A 208      37.190 -12.765   5.198  1.00 75.38      A    C  
ANISOU 1526  CD  PRO A 208     9633   8643  10364  -2465    854     59  A    C  
ATOM   1527  N   PRO A 209      39.655 -15.348   6.762  1.00 82.46      A    N  
ANISOU 1527  N   PRO A 209    11249   9123  10960  -2554    531    286  A    N  
ATOM   1528  CA  PRO A 209      40.490 -16.261   7.551  1.00 80.69      A    C  
ANISOU 1528  CA  PRO A 209    11323   8723  10611  -2595    421    380  A    C  
ATOM   1529  C   PRO A 209      41.004 -17.485   6.795  1.00 82.36      A    C  
ANISOU 1529  C   PRO A 209    11545   8860  10887  -2526    237    372  A    C  
ATOM   1530  O   PRO A 209      42.010 -18.059   7.211  1.00 81.61      A    O  
ANISOU 1530  O   PRO A 209    11656   8649  10703  -2484     86    451  A    O  
ATOM   1531  CB  PRO A 209      39.560 -16.671   8.689  1.00 74.43      A    C  
ANISOU 1531  CB  PRO A 209    10719   7809   9751  -2817    627    406  A    C  
ATOM   1532  CG  PRO A 209      38.698 -15.473   8.882  1.00 69.50      A    C  
ANISOU 1532  CG  PRO A 209     9946   7312   9149  -2853    834    354  A    C  
ATOM   1533  CD  PRO A 209      38.436 -14.960   7.493  1.00 75.29      A    C  
ANISOU 1533  CD  PRO A 209    10337   8217  10052  -2714    784    258  A    C  
ATOM   1534  N   ILE A 210      40.352 -17.877   5.706  1.00 85.59      A    N  
ANISOU 1534  N   ILE A 210    11743   9330  11447  -2507    238    276  A    N  
ATOM   1535  CA  ILE A 210      40.816 -19.055   4.977  1.00 86.63      A    C  
ANISOU 1535  CA  ILE A 210    11899   9381  11636  -2439     67    255  A    C  
ATOM   1536  C   ILE A 210      42.172 -18.804   4.319  1.00 80.48      A    C  
ANISOU 1536  C   ILE A 210    11070   8672  10837  -2214   -138    274  A    C  
ATOM   1537  O   ILE A 210      43.002 -19.708   4.213  1.00 79.16      A    O  
ANISOU 1537  O   ILE A 210    11028   8397  10651  -2140   -298    303  A    O  
ATOM   1538  CB  ILE A 210      39.789 -19.561   3.929  1.00 84.58      A    C  
ANISOU 1538  CB  ILE A 210    11433   9167  11539  -2475    102    135  A    C  
ATOM   1539  CG1 ILE A 210      39.736 -18.639   2.712  1.00 80.25      A    C  
ANISOU 1539  CG1 ILE A 210    10583   8833  11075  -2315     67     53  A    C  
ATOM   1540  CG2 ILE A 210      38.417 -19.702   4.552  1.00 87.17      A    C  
ANISOU 1540  CG2 ILE A 210    11762   9449  11908  -2702    321    111  A    C  
ATOM   1541  CD1 ILE A 210      39.027 -19.258   1.524  1.00 73.55      A    C  
ANISOU 1541  CD1 ILE A 210     9552   8024  10369  -2306     26    -65  A    C  
ATOM   1542  N   ASP A 211      42.401 -17.569   3.888  1.00 74.32      A    N  
ANISOU 1542  N   ASP A 211    10106   8067  10064  -2104   -129    260  A    N  
ATOM   1543  CA  ASP A 211      43.656 -17.228   3.233  1.00 75.03      A    C  
ANISOU 1543  CA  ASP A 211    10122   8243  10145  -1902   -299    280  A    C  
ATOM   1544  C   ASP A 211      44.823 -17.188   4.216  1.00 77.33      A    C  
ANISOU 1544  C   ASP A 211    10626   8443  10311  -1876   -401    392  A    C  
ATOM   1545  O   ASP A 211      45.955 -17.505   3.854  1.00 74.81      A    O  
ANISOU 1545  O   ASP A 211    10314   8121   9990  -1732   -572    418  A    O  
ATOM   1546  CB  ASP A 211      43.528 -15.910   2.463  1.00 72.88      A    C  
ANISOU 1546  CB  ASP A 211     9598   8175   9918  -1804   -254    239  A    C  
ATOM   1547  CG  ASP A 211      42.672 -16.047   1.215  1.00 74.10      A    C  
ANISOU 1547  CG  ASP A 211     9527   8430  10195  -1769   -227    128  A    C  
ATOM   1548  OD1 ASP A 211      42.454 -17.196   0.771  1.00 83.67      A    O  
ANISOU 1548  OD1 ASP A 211    10765   9564  11460  -1784   -285     76  A    O  
ATOM   1549  OD2 ASP A 211      42.221 -15.013   0.678  1.00 65.19      A    O1-
ANISOU 1549  OD2 ASP A 211     8207   7452   9110  -1725   -161     90  A    O1-
ATOM   1550  N   LEU A 212      44.538 -16.823   5.462  1.00 81.41      A    N  
ANISOU 1550  N   LEU A 212    11317   8890  10726  -2015   -298    453  A    N  
ATOM   1551  CA  LEU A 212      45.570 -16.720   6.491  1.00 77.88      A    C  
ANISOU 1551  CA  LEU A 212    11089   8355  10146  -2006   -401    559  A    C  
ATOM   1552  C   LEU A 212      46.055 -18.089   6.935  1.00 79.86      A    C  
ANISOU 1552  C   LEU A 212    11575   8414  10355  -2022   -528    613  A    C  
ATOM   1553  O   LEU A 212      47.217 -18.256   7.310  1.00 81.41      A    O  
ANISOU 1553  O   LEU A 212    11890   8553  10487  -1934   -700    685  A    O  
ATOM   1554  CB  LEU A 212      45.046 -15.944   7.688  1.00 76.32      A    C  
ANISOU 1554  CB  LEU A 212    11031   8133   9834  -2153   -245    599  A    C  
ATOM   1555  CG  LEU A 212      44.688 -14.496   7.379  1.00 81.51      A    C  
ANISOU 1555  CG  LEU A 212    11487   8961  10523  -2123   -134    554  A    C  
ATOM   1556  CD1 LEU A 212      43.658 -13.997   8.393  1.00 97.88      A    C  
ANISOU 1556  CD1 LEU A 212    13669  10999  12520  -2293     87    552  A    C  
ATOM   1557  CD2 LEU A 212      45.941 -13.654   7.391  1.00 70.74      A    C  
ANISOU 1557  CD2 LEU A 212    10100   7663   9113  -1999   -281    606  A    C  
ATOM   1558  N   TRP A 213      45.151 -19.062   6.908  1.00 78.07      A    N  
ANISOU 1558  N   TRP A 213    11413   8079  10169  -2138   -446    578  A    N  
ATOM   1559  CA  TRP A 213      45.528 -20.447   7.125  1.00 74.35      A    C  
ANISOU 1559  CA  TRP A 213    11151   7416   9684  -2143   -570    617  A    C  
ATOM   1560  C   TRP A 213      46.592 -20.856   6.104  1.00 78.96      A    C  
ANISOU 1560  C   TRP A 213    11617   8037  10346  -1923   -778    588  A    C  
ATOM   1561  O   TRP A 213      47.604 -21.450   6.461  1.00 90.54      A    O  
ANISOU 1561  O   TRP A 213    13242   9393  11765  -1838   -950    655  A    O  
ATOM   1562  CB  TRP A 213      44.302 -21.351   7.023  1.00 76.30      A    C  
ANISOU 1562  CB  TRP A 213    11433   7561   9995  -2305   -440    564  A    C  
ATOM   1563  CG  TRP A 213      44.608 -22.796   7.218  1.00 82.04      A    C  
ANISOU 1563  CG  TRP A 213    12388   8069  10715  -2322   -560    602  A    C  
ATOM   1564  CD1 TRP A 213      44.946 -23.694   6.255  1.00 87.36      A    C  
ANISOU 1564  CD1 TRP A 213    13003   8700  11492  -2202   -700    542  A    C  
ATOM   1565  CD2 TRP A 213      44.607 -23.516   8.459  1.00 87.56      A    C  
ANISOU 1565  CD2 TRP A 213    13429   8550  11289  -2462   -553    709  A    C  
ATOM   1566  CE2 TRP A 213      44.958 -24.848   8.166  1.00 89.88      A    C  
ANISOU 1566  CE2 TRP A 213    13854   8667  11628  -2416   -700    712  A    C  
ATOM   1567  CE3 TRP A 213      44.348 -23.161   9.788  1.00 90.10      A    C  
ANISOU 1567  CE3 TRP A 213    13974   8804  11455  -2619   -436    802  A    C  
ATOM   1568  NE1 TRP A 213      45.160 -24.930   6.814  1.00 94.19      A    N  
ANISOU 1568  NE1 TRP A 213    14147   9325  12316  -2255   -786    603  A    N  
ATOM   1569  CZ2 TRP A 213      45.055 -25.830   9.152  1.00 90.32      A    C  
ANISOU 1569  CZ2 TRP A 213    14256   8476  11584  -2523   -740    815  A    C  
ATOM   1570  CZ3 TRP A 213      44.443 -24.134  10.766  1.00 91.89      A    C  
ANISOU 1570  CZ3 TRP A 213    14548   8796  11571  -2729   -469    904  A    C  
ATOM   1571  CH2 TRP A 213      44.792 -25.456  10.442  1.00 93.36      A    C  
ANISOU 1571  CH2 TRP A 213    14859   8804  11811  -2682   -623    914  A    C  
ATOM   1572  N   GLY A 214      46.370 -20.525   4.835  1.00 72.41      A    N  
ANISOU 1572  N   GLY A 214    10510   7369   9634  -1823   -761    488  A    N  
ATOM   1573  CA  GLY A 214      47.359 -20.783   3.806  1.00 69.76      A    C  
ANISOU 1573  CA  GLY A 214    10044   7097   9365  -1607   -928    453  A    C  
ATOM   1574  C   GLY A 214      48.682 -20.090   4.095  1.00 75.14      A    C  
ANISOU 1574  C   GLY A 214    10714   7845   9989  -1474  -1053    529  A    C  
ATOM   1575  O   GLY A 214      49.750 -20.682   3.945  1.00 80.58      A    O  
ANISOU 1575  O   GLY A 214    11447   8482  10689  -1332  -1224    555  A    O  
ATOM   1576  N   ALA A 215      48.612 -18.826   4.504  1.00 72.49      A    N  
ANISOU 1576  N   ALA A 215    10316   7623   9604  -1520   -969    562  A    N  
ATOM   1577  CA  ALA A 215      49.804 -18.063   4.866  1.00 71.89      A    C  
ANISOU 1577  CA  ALA A 215    10229   7608   9476  -1426  -1082    635  A    C  
ATOM   1578  C   ALA A 215      50.578 -18.761   5.979  1.00 78.47      A    C  
ANISOU 1578  C   ALA A 215    11336   8262  10217  -1441  -1227    733  A    C  
ATOM   1579  O   ALA A 215      51.811 -18.781   5.974  1.00 81.05      A    O  
ANISOU 1579  O   ALA A 215    11647   8600  10547  -1303  -1402    778  A    O  
ATOM   1580  CB  ALA A 215      49.429 -16.645   5.292  1.00 65.24      A    C  
ANISOU 1580  CB  ALA A 215     9326   6877   8585  -1510   -956    651  A    C  
ATOM   1581  N   GLY A 216      49.845 -19.322   6.937  1.00 77.22      A    N  
ANISOU 1581  N   GLY A 216    11424   7940   9974  -1609  -1153    769  A    N  
ATOM   1582  CA  GLY A 216      50.449 -20.116   7.989  1.00 77.44      A    C  
ANISOU 1582  CA  GLY A 216    11749   7774   9902  -1632  -1290    866  A    C  
ATOM   1583  C   GLY A 216      51.247 -21.284   7.435  1.00 79.45      A    C  
ANISOU 1583  C   GLY A 216    12019   7938  10231  -1472  -1478    860  A    C  
ATOM   1584  O   GLY A 216      52.414 -21.462   7.786  1.00 80.53      A    O  
ANISOU 1584  O   GLY A 216    12227   8029  10341  -1355  -1672    926  A    O  
ATOM   1585  N   CYS A 217      50.620 -22.074   6.563  1.00 73.32      A    N  
ANISOU 1585  N   CYS A 217    11171   7134   9554  -1462  -1426    774  A    N  
ATOM   1586  CA  CYS A 217      51.284 -23.207   5.924  1.00 73.44      A    C  
ANISOU 1586  CA  CYS A 217    11197   7059   9649  -1302  -1588    746  A    C  
ATOM   1587  C   CYS A 217      52.513 -22.783   5.128  1.00 79.88      A    C  
ANISOU 1587  C   CYS A 217    11784   8029  10536  -1068  -1724    726  A    C  
ATOM   1588  O   CYS A 217      53.573 -23.418   5.204  1.00 83.79      A    O  
ANISOU 1588  O   CYS A 217    12344   8445  11048   -919  -1911    762  A    O  
ATOM   1589  CB  CYS A 217      50.310 -23.948   5.012  1.00 75.93      A    C  
ANISOU 1589  CB  CYS A 217    11443   7344  10060  -1340  -1494    636  A    C  
ATOM   1590  SG  CYS A 217      48.842 -24.569   5.853  1.00 93.88      A    S  
ANISOU 1590  SG  CYS A 217    13956   9432  12280  -1626  -1324    655  A    S  
ATOM   1591  N   ILE A 218      52.367 -21.712   4.355  1.00 76.79      A    N  
ANISOU 1591  N   ILE A 218    11125   7859  10192  -1035  -1626    669  A    N  
ATOM   1592  CA  ILE A 218      53.479 -21.182   3.580  1.00 73.67      A    C  
ANISOU 1592  CA  ILE A 218    10500   7631   9863   -836  -1721    655  A    C  
ATOM   1593  C   ILE A 218      54.607 -20.719   4.492  1.00 76.35      A    C  
ANISOU 1593  C   ILE A 218    10905   7960  10143   -796  -1863    762  A    C  
ATOM   1594  O   ILE A 218      55.780 -20.938   4.201  1.00 79.58      A    O  
ANISOU 1594  O   ILE A 218    11231   8398  10608   -619  -2018    776  A    O  
ATOM   1595  CB  ILE A 218      53.039 -20.008   2.707  1.00 70.35      A    C  
ANISOU 1595  CB  ILE A 218     9811   7437   9483   -836  -1578    594  A    C  
ATOM   1596  CG1 ILE A 218      52.066 -20.489   1.633  1.00 68.26      A    C  
ANISOU 1596  CG1 ILE A 218     9449   7199   9287   -839  -1476    477  A    C  
ATOM   1597  CG2 ILE A 218      54.251 -19.316   2.087  1.00 63.29      A    C  
ANISOU 1597  CG2 ILE A 218     8697   6712   8638   -660  -1662    605  A    C  
ATOM   1598  CD1 ILE A 218      51.342 -19.367   0.965  1.00 66.02      A    C  
ANISOU 1598  CD1 ILE A 218     8953   7106   9024   -879  -1325    427  A    C  
ATOM   1599  N   MET A 219      54.255 -20.077   5.598  1.00 76.43      A    N  
ANISOU 1599  N   MET A 219    11062   7934  10044   -960  -1810    832  A    N  
ATOM   1600  CA  MET A 219      55.267 -19.581   6.524  1.00 80.40      A    C  
ANISOU 1600  CA  MET A 219    11644   8426  10479   -942  -1955    930  A    C  
ATOM   1601  C   MET A 219      56.112 -20.717   7.106  1.00 81.48      A    C  
ANISOU 1601  C   MET A 219    11982   8380  10598   -853  -2171    994  A    C  
ATOM   1602  O   MET A 219      57.335 -20.631   7.132  1.00 78.86      A    O  
ANISOU 1602  O   MET A 219    11573   8085  10304   -710  -2350   1032  A    O  
ATOM   1603  CB  MET A 219      54.627 -18.765   7.645  1.00 79.20      A    C  
ANISOU 1603  CB  MET A 219    11655   8246  10190  -1142  -1851    983  A    C  
ATOM   1604  CG  MET A 219      55.634 -18.094   8.560  1.00 78.48      A    C  
ANISOU 1604  CG  MET A 219    11636   8160  10023  -1134  -2003   1071  A    C  
ATOM   1605  SD  MET A 219      54.832 -17.210   9.898  1.00 88.71      A    S  
ANISOU 1605  SD  MET A 219    13164   9406  11137  -1367  -1871   1119  A    S  
ATOM   1606  CE  MET A 219      56.221 -16.334  10.599  1.00 94.82      A    C  
ANISOU 1606  CE  MET A 219    13939  10227  11862  -1314  -2087   1196  A    C  
ATOM   1607  N   ALA A 220      55.455 -21.774   7.576  1.00 82.54      A    N  
ANISOU 1607  N   ALA A 220    12370   8313  10679   -941  -2155   1007  A    N  
ATOM   1608  CA  ALA A 220      56.163 -22.949   8.074  1.00 86.40      A    C  
ANISOU 1608  CA  ALA A 220    13072   8603  11153   -851  -2359   1068  A    C  
ATOM   1609  C   ALA A 220      57.045 -23.504   6.967  1.00 95.60      A    C  
ANISOU 1609  C   ALA A 220    14031   9823  12470   -606  -2480   1005  A    C  
ATOM   1610  O   ALA A 220      58.204 -23.863   7.188  1.00 99.02      A    O  
ANISOU 1610  O   ALA A 220    14479  10212  12933   -450  -2690   1052  A    O  
ATOM   1611  CB  ALA A 220      55.175 -24.007   8.546  1.00 82.25      A    C  
ANISOU 1611  CB  ALA A 220    12832   7855  10564   -994  -2287   1081  A    C  
ATOM   1612  N   GLU A 221      56.475 -23.556   5.769  1.00 96.19      A    N  
ANISOU 1612  N   GLU A 221    13909   9999  12639   -571  -2344    892  A    N  
ATOM   1613  CA  GLU A 221      57.161 -24.051   4.586  1.00 90.57      A    C  
ANISOU 1613  CA  GLU A 221    12997   9356  12061   -345  -2416    811  A    C  
ATOM   1614  C   GLU A 221      58.515 -23.366   4.348  1.00 86.67      A    C  
ANISOU 1614  C   GLU A 221    12277   9026  11628   -170  -2537    836  A    C  
ATOM   1615  O   GLU A 221      59.422 -23.977   3.794  1.00 87.84      A    O  
ANISOU 1615  O   GLU A 221    12331   9174  11870     39  -2661    806  A    O  
ATOM   1616  CB  GLU A 221      56.245 -23.879   3.377  1.00 89.21      A    C  
ANISOU 1616  CB  GLU A 221    12638   9309  11950   -365  -2230    688  A    C  
ATOM   1617  CG  GLU A 221      56.639 -24.668   2.154  1.00 95.96      A    C  
ANISOU 1617  CG  GLU A 221    13362  10183  12915   -161  -2276    584  A    C  
ATOM   1618  CD  GLU A 221      55.425 -25.114   1.369  1.00 99.29      A    C  
ANISOU 1618  CD  GLU A 221    13780  10585  13362   -240  -2136    474  A    C  
ATOM   1619  OE1 GLU A 221      54.382 -25.365   2.012  1.00 98.44      A    O  
ANISOU 1619  OE1 GLU A 221    13859  10347  13196   -444  -2055    495  A    O  
ATOM   1620  OE2 GLU A 221      55.512 -25.212   0.124  1.00101.11      A    O1-
ANISOU 1620  OE2 GLU A 221    13822  10930  13665   -104  -2105    367  A    O1-
ATOM   1621  N   MET A 222      58.650 -22.107   4.772  1.00 79.89      A    N  
ANISOU 1621  N   MET A 222    11329   8302  10721   -259  -2498    887  A    N  
ATOM   1622  CA  MET A 222      59.903 -21.361   4.607  1.00 80.15      A    C  
ANISOU 1622  CA  MET A 222    11141   8493  10818   -128  -2607    918  A    C  
ATOM   1623  C   MET A 222      61.070 -22.001   5.363  1.00 92.81      A    C  
ANISOU 1623  C   MET A 222    12857   9974  12433     -8  -2861    995  A    C  
ATOM   1624  O   MET A 222      62.238 -21.727   5.069  1.00 97.63      A    O  
ANISOU 1624  O   MET A 222    13261  10697  13137    149  -2979   1005  A    O  
ATOM   1625  CB  MET A 222      59.750 -19.918   5.088  1.00 70.69      A    C  
ANISOU 1625  CB  MET A 222     9881   7423   9555   -276  -2529    964  A    C  
ATOM   1626  CG  MET A 222      58.660 -19.128   4.410  1.00 72.63      A    C  
ANISOU 1626  CG  MET A 222    10004   7800   9794   -385  -2292    898  A    C  
ATOM   1627  SD  MET A 222      59.069 -18.685   2.717  1.00 79.53      A    S  
ANISOU 1627  SD  MET A 222    10502   8914  10803   -213  -2211    809  A    S  
ATOM   1628  CE  MET A 222      60.584 -17.775   2.935  1.00 80.87      A    C  
ANISOU 1628  CE  MET A 222    10484   9216  11026   -126  -2351    883  A    C  
ATOM   1629  N   TRP A 223      60.751 -22.834   6.350  1.00 90.42      A    N  
ANISOU 1629  N   TRP A 223    12880   9439  12036    -84  -2946   1055  A    N  
ATOM   1630  CA  TRP A 223      61.775 -23.502   7.137  1.00 93.20      A    C  
ANISOU 1630  CA  TRP A 223    13378   9648  12384     28  -3205   1136  A    C  
ATOM   1631  C   TRP A 223      61.870 -24.986   6.807  1.00 93.78      A    C  
ANISOU 1631  C   TRP A 223    13573   9540  12519    174  -3294   1102  A    C  
ATOM   1632  O   TRP A 223      62.966 -25.552   6.804  1.00 90.33      A    O  
ANISOU 1632  O   TRP A 223    13098   9058  12165    376  -3498   1121  A    O  
ATOM   1633  CB  TRP A 223      61.522 -23.310   8.632  1.00 95.00      A    C  
ANISOU 1633  CB  TRP A 223    13921   9734  12441   -154  -3274   1249  A    C  
ATOM   1634  CG  TRP A 223      61.931 -21.967   9.122  1.00 96.30      A    C  
ANISOU 1634  CG  TRP A 223    13981  10049  12561   -234  -3292   1295  A    C  
ATOM   1635  CD1 TRP A 223      63.202 -21.548   9.405  1.00 96.53      A    C  
ANISOU 1635  CD1 TRP A 223    13885  10150  12641   -125  -3500   1344  A    C  
ATOM   1636  CD2 TRP A 223      61.072 -20.852   9.382  1.00 91.81      A    C  
ANISOU 1636  CD2 TRP A 223    13418   9571  11896   -439  -3099   1291  A    C  
ATOM   1637  CE2 TRP A 223      61.891 -19.786   9.822  1.00 90.98      A    C  
ANISOU 1637  CE2 TRP A 223    13206   9580  11780   -448  -3205   1337  A    C  
ATOM   1638  CE3 TRP A 223      59.694 -20.649   9.288  1.00 82.83      A    C  
ANISOU 1638  CE3 TRP A 223    12357   8426  10687   -613  -2851   1248  A    C  
ATOM   1639  NE1 TRP A 223      63.185 -20.238   9.826  1.00 93.06      A    N  
ANISOU 1639  NE1 TRP A 223    13385   9835  12139   -261  -3452   1370  A    N  
ATOM   1640  CZ2 TRP A 223      61.374 -18.536  10.164  1.00 83.67      A    C  
ANISOU 1640  CZ2 TRP A 223    12269   8750  10770   -620  -3069   1340  A    C  
ATOM   1641  CZ3 TRP A 223      59.183 -19.406   9.632  1.00 86.30      A    C  
ANISOU 1641  CZ3 TRP A 223    12771   8971  11048   -773  -2713   1252  A    C  
ATOM   1642  CH2 TRP A 223      60.023 -18.365  10.064  1.00 82.68      A    C  
ANISOU 1642  CH2 TRP A 223    12226   8614  10576   -772  -2822   1296  A    C  
ATOM   1643  N   THR A 224      60.725 -25.608   6.532  1.00 86.54      A    N  
ANISOU 1643  N   THR A 224    12798   8515  11570     72  -3145   1050  A    N  
ATOM   1644  CA  THR A 224      60.678 -27.042   6.275  1.00 89.38      A    C  
ANISOU 1644  CA  THR A 224    13315   8669  11976    180  -3221   1016  A    C  
ATOM   1645  C   THR A 224      60.981 -27.393   4.819  1.00 96.90      A    C  
ANISOU 1645  C   THR A 224    14006   9731  13081    387  -3180    883  A    C  
ATOM   1646  O   THR A 224      61.248 -28.553   4.503  1.00103.63      A    O  
ANISOU 1646  O   THR A 224    14947  10431  13998    537  -3278    843  A    O  
ATOM   1647  CB  THR A 224      59.313 -27.656   6.662  1.00 88.10      A    C  
ANISOU 1647  CB  THR A 224    13440   8316  11718    -35  -3089   1018  A    C  
ATOM   1648  CG2 THR A 224      59.000 -27.403   8.123  1.00 82.98      A    C  
ANISOU 1648  CG2 THR A 224    13082   7544  10900   -237  -3114   1149  A    C  
ATOM   1649  OG1 THR A 224      58.276 -27.088   5.855  1.00 96.12      A    O  
ANISOU 1649  OG1 THR A 224    14288   9481  12751   -153  -2847    922  A    O  
ATOM   1650  N   ARG A 225      60.936 -26.393   3.943  1.00 92.80      A    N  
ANISOU 1650  N   ARG A 225    13181   9470  12609    396  -3036    816  A    N  
ATOM   1651  CA  ARG A 225      61.112 -26.595   2.497  1.00 94.51      A    C  
ANISOU 1651  CA  ARG A 225    13150   9817  12943    572  -2962    686  A    C  
ATOM   1652  C   ARG A 225      59.998 -27.417   1.835  1.00 98.74      A    C  
ANISOU 1652  C   ARG A 225    13793  10245  13477    516  -2842    583  A    C  
ATOM   1653  O   ARG A 225      59.866 -27.432   0.611  1.00100.11      A    O  
ANISOU 1653  O   ARG A 225    13779  10543  13716    614  -2744    465  A    O  
ATOM   1654  CB  ARG A 225      62.480 -27.205   2.176  1.00 92.98      A    C  
ANISOU 1654  CB  ARG A 225    12848   9616  12865    856  -3143    672  A    C  
ATOM   1655  CG  ARG A 225      63.653 -26.308   2.525  1.00 89.41      A    C  
ANISOU 1655  CG  ARG A 225    12196   9324  12453    932  -3249    747  A    C  
ATOM   1656  CD  ARG A 225      63.300 -24.861   2.304  1.00 85.19      A    C  
ANISOU 1656  CD  ARG A 225    11465   9023  11882    782  -3082    754  A    C  
ATOM   1657  NE  ARG A 225      64.475 -24.001   2.325  1.00 89.44      A    N  
ANISOU 1657  NE  ARG A 225    11751   9741  12490    873  -3161    800  A    N  
ATOM   1658  CZ  ARG A 225      65.126 -23.605   1.235  1.00 96.36      A    C  
ANISOU 1658  CZ  ARG A 225    12310  10828  13476   1025  -3095    736  A    C  
ATOM   1659  NH1 ARG A 225      64.720 -23.994   0.030  1.00 95.45      A    N1+
ANISOU 1659  NH1 ARG A 225    12102  10769  13394   1114  -2953    620  A    N1+
ATOM   1660  NH2 ARG A 225      66.183 -22.815   1.347  1.00 97.04      A    N  
ANISOU 1660  NH2 ARG A 225    12171  11067  13631   1081  -3168    789  A    N  
ATOM   1661  N   SER A 226      59.188 -28.086   2.644  1.00101.71      A    N  
ANISOU 1661  N   SER A 226    14477  10393  13777    352  -2848    627  A    N  
ATOM   1662  CA  SER A 226      58.141 -28.940   2.116  1.00108.68      A    C  
ANISOU 1662  CA  SER A 226    15476  11147  14668    280  -2753    535  A    C  
ATOM   1663  C   SER A 226      56.803 -28.573   2.747  1.00108.09      A    C  
ANISOU 1663  C   SER A 226    15544  11029  14496    -19  -2597    572  A    C  
ATOM   1664  O   SER A 226      56.747 -28.296   3.944  1.00108.27      A    O  
ANISOU 1664  O   SER A 226    15744  10973  14421   -157  -2625    692  A    O  
ATOM   1665  CB  SER A 226      58.482 -30.406   2.402  1.00118.33      A    C  
ANISOU 1665  CB  SER A 226    16954  12087  15920    387  -2921    542  A    C  
ATOM   1666  OG  SER A 226      57.710 -31.288   1.603  1.00125.21      A    O  
ANISOU 1666  OG  SER A 226    17886  12853  16836    378  -2853    422  A    O  
ATOM   1667  N   PRO A 227      55.723 -28.552   1.940  1.00105.16      A    N  
ANISOU 1667  N   PRO A 227    15092  10715  14148   -116  -2432    466  A    N  
ATOM   1668  CA  PRO A 227      54.377 -28.389   2.500  1.00 97.38      A    C  
ANISOU 1668  CA  PRO A 227    14240   9667  13093   -395  -2278    488  A    C  
ATOM   1669  C   PRO A 227      54.222 -29.336   3.679  1.00 94.54      A    C  
ANISOU 1669  C   PRO A 227    14240   9016  12665   -508  -2360    587  A    C  
ATOM   1670  O   PRO A 227      54.627 -30.490   3.593  1.00 92.50      A    O  
ANISOU 1670  O   PRO A 227    14133   8565  12448   -394  -2495    575  A    O  
ATOM   1671  CB  PRO A 227      53.471 -28.807   1.344  1.00 86.72      A    C  
ANISOU 1671  CB  PRO A 227    12792   8342  11815   -416  -2172    341  A    C  
ATOM   1672  CG  PRO A 227      54.241 -28.440   0.139  1.00 86.72      A    C  
ANISOU 1672  CG  PRO A 227    12516   8547  11887   -182  -2199    252  A    C  
ATOM   1673  CD  PRO A 227      55.694 -28.659   0.471  1.00 95.85      A    C  
ANISOU 1673  CD  PRO A 227    13689   9669  13059     28  -2380    318  A    C  
ATOM   1674  N   ILE A 228      53.649 -28.848   4.768  1.00 92.92      A    N  
ANISOU 1674  N   ILE A 228    14181   8774  12350   -725  -2277    686  A    N  
ATOM   1675  CA  ILE A 228      53.764 -29.533   6.047  1.00 95.93      A    C  
ANISOU 1675  CA  ILE A 228    14913   8905  12632   -814  -2373    814  A    C  
ATOM   1676  C   ILE A 228      52.663 -30.552   6.312  1.00 99.91      A    C  
ANISOU 1676  C   ILE A 228    15665   9176  13121  -1007  -2290    810  A    C  
ATOM   1677  O   ILE A 228      52.824 -31.447   7.144  1.00105.37      A    O  
ANISOU 1677  O   ILE A 228    16671   9615  13752  -1044  -2394    903  A    O  
ATOM   1678  CB  ILE A 228      53.793 -28.516   7.181  1.00 97.70      A    C  
ANISOU 1678  CB  ILE A 228    15205   9195  12722   -946  -2333    930  A    C  
ATOM   1679  CG1 ILE A 228      52.584 -27.585   7.064  1.00101.82      A    C  
ANISOU 1679  CG1 ILE A 228    15596   9870  13220  -1152  -2080    884  A    C  
ATOM   1680  CG2 ILE A 228      55.094 -27.724   7.128  1.00 93.77      A    C  
ANISOU 1680  CG2 ILE A 228    14525   8864  12239   -753  -2476    960  A    C  
ATOM   1681  CD1 ILE A 228      52.304 -26.771   8.306  1.00103.90      A    C  
ANISOU 1681  CD1 ILE A 228    16003  10142  13332  -1331  -2000    990  A    C  
ATOM   1682  N   MET A 229      51.547 -30.412   5.605  1.00101.19      A    N  
ANISOU 1682  N   MET A 229    15687   9419  13341  -1134  -2107    705  A    N  
ATOM   1683  CA  MET A 229      50.417 -31.321   5.760  1.00101.87      A    C  
ANISOU 1683  CA  MET A 229    15964   9304  13436  -1339  -2010    687  A    C  
ATOM   1684  C   MET A 229      49.967 -31.875   4.408  1.00105.36      A    C  
ANISOU 1684  C   MET A 229    16243   9770  14019  -1279  -1989    523  A    C  
ATOM   1685  O   MET A 229      49.021 -31.362   3.808  1.00107.32      A    O  
ANISOU 1685  O   MET A 229    16294  10168  14314  -1389  -1828    432  A    O  
ATOM   1686  CB  MET A 229      49.260 -30.603   6.454  1.00 93.78      A    C  
ANISOU 1686  CB  MET A 229    14959   8339  12335  -1619  -1785    727  A    C  
ATOM   1687  CG  MET A 229      49.533 -30.275   7.916  1.00 86.05      A    C  
ANISOU 1687  CG  MET A 229    14227   7278  11190  -1719  -1794    889  A    C  
ATOM   1688  SD  MET A 229      48.173 -29.387   8.705  1.00115.26      A    S  
ANISOU 1688  SD  MET A 229    17939  11059  14796  -2031  -1502    922  A    S  
ATOM   1689  CE  MET A 229      48.587 -27.687   8.309  1.00107.41      A    C  
ANISOU 1689  CE  MET A 229    16602  10404  13803  -1914  -1460    880  A    C  
ATOM   1690  N   GLN A 230      50.642 -32.927   3.945  1.00106.56      A    N  
ANISOU 1690  N   GLN A 230    16485   9767  14235  -1097  -2159    482  A    N  
ATOM   1691  CA  GLN A 230      50.444 -33.453   2.589  1.00102.91      A    C  
ANISOU 1691  CA  GLN A 230    15874   9333  13895   -989  -2172    314  A    C  
ATOM   1692  C   GLN A 230      49.356 -34.530   2.476  1.00107.52      A    C  
ANISOU 1692  C   GLN A 230    16632   9692  14530  -1178  -2120    256  A    C  
ATOM   1693  O   GLN A 230      49.635 -35.656   2.061  1.00111.09      A    O  
ANISOU 1693  O   GLN A 230    17218   9948  15043  -1073  -2245    198  A    O  
ATOM   1694  CB  GLN A 230      51.768 -33.988   2.022  1.00 95.80      A    C  
ANISOU 1694  CB  GLN A 230    14953   8400  13048   -670  -2372    275  A    C  
ATOM   1695  CG  GLN A 230      52.924 -32.996   2.091  1.00 98.13      A    C  
ANISOU 1695  CG  GLN A 230    15059   8912  13315   -479  -2436    330  A    C  
ATOM   1696  CD  GLN A 230      54.017 -33.281   1.073  1.00104.24      A    C  
ANISOU 1696  CD  GLN A 230    15674   9757  14174   -162  -2563    235  A    C  
ATOM   1697  NE2 GLN A 230      55.151 -32.601   1.210  1.00101.34      A    N  
ANISOU 1697  NE2 GLN A 230    15164   9540  13799     12  -2643    292  A    N  
ATOM   1698  OE1 GLN A 230      53.839 -34.095   0.170  1.00111.90      A    O  
ANISOU 1698  OE1 GLN A 230    16647  10650  15218    -77  -2585    107  A    O  
ATOM   1699  N   GLY A 231      48.119 -34.170   2.816  1.00106.75      A    N  
ANISOU 1699  N   GLY A 231    16520   9624  14415  -1455  -1933    266  A    N  
ATOM   1700  CA  GLY A 231      46.997 -35.096   2.778  1.00112.24      A    C  
ANISOU 1700  CA  GLY A 231    17356  10121  15168  -1676  -1863    218  A    C  
ATOM   1701  C   GLY A 231      46.695 -35.722   1.422  1.00119.09      A    C  
ANISOU 1701  C   GLY A 231    18101  10985  16163  -1596  -1910     34  A    C  
ATOM   1702  O   GLY A 231      47.078 -35.195   0.374  1.00120.74      A    O  
ANISOU 1702  O   GLY A 231    18051  11412  16411  -1403  -1938    -76  A    O  
ATOM   1703  N   ASN A 232      45.993 -36.854   1.450  1.00122.59      A    N  
ANISOU 1703  N   ASN A 232    18743  11173  16663  -1755  -1915      0  A    N  
ATOM   1704  CA  ASN A 232      45.643 -37.588   0.238  1.00126.33      A    C  
ANISOU 1704  CA  ASN A 232    19150  11598  17253  -1706  -1974   -181  A    C  
ATOM   1705  C   ASN A 232      44.194 -37.335  -0.188  1.00126.70      A    C  
ANISOU 1705  C   ASN A 232    19025  11739  17374  -1959  -1814   -276  A    C  
ATOM   1706  O   ASN A 232      43.903 -37.128  -1.370  1.00121.29      A    O  
ANISOU 1706  O   ASN A 232    18110  11214  16760  -1883  -1821   -436  A    O  
ATOM   1707  CB  ASN A 232      45.883 -39.084   0.440  1.00135.33      A    C  
ANISOU 1707  CB  ASN A 232    20624  12370  18425  -1697  -2115   -173  A    C  
ATOM   1708  CG  ASN A 232      45.769 -39.871  -0.851  1.00149.27      A    C  
ANISOU 1708  CG  ASN A 232    22344  14074  20300  -1589  -2211   -370  A    C  
ATOM   1709  ND2 ASN A 232      45.716 -41.196  -0.737  1.00153.99      A    N  
ANISOU 1709  ND2 ASN A 232    23232  14335  20943  -1631  -2314   -385  A    N  
ATOM   1710  OD1 ASN A 232      45.729 -39.294  -1.941  1.00151.96      A    O  
ANISOU 1710  OD1 ASN A 232    22405  14659  20674  -1468  -2196   -509  A    O  
ATOM   1711  N   THR A 233      43.289 -37.369   0.786  1.00129.14      A    N  
ANISOU 1711  N   THR A 233    19452  11950  17668  -2257  -1670   -178  A    N  
ATOM   1712  CA  THR A 233      41.896 -36.991   0.569  1.00125.48      A    C  
ANISOU 1712  CA  THR A 233    18800  11598  17279  -2512  -1496   -248  A    C  
ATOM   1713  C   THR A 233      41.457 -36.029   1.663  1.00119.62      A    C  
ANISOU 1713  C   THR A 233    18025  10971  16455  -2689  -1304   -111  A    C  
ATOM   1714  O   THR A 233      42.223 -35.737   2.586  1.00114.21      A    O  
ANISOU 1714  O   THR A 233    17491  10257  15646  -2625  -1319     35  A    O  
ATOM   1715  CB  THR A 233      40.948 -38.211   0.550  1.00130.28      A    C  
ANISOU 1715  CB  THR A 233    19577  11936  17989  -2756  -1486   -300  A    C  
ATOM   1716  CG2 THR A 233      40.947 -38.867  -0.830  1.00130.50      A    C  
ANISOU 1716  CG2 THR A 233    19521  11938  18125  -2626  -1632   -497  A    C  
ATOM   1717  OG1 THR A 233      41.357 -39.166   1.543  1.00127.03      A    O  
ANISOU 1717  OG1 THR A 233    19545  11203  17519  -2817  -1544   -162  A    O  
ATOM   1718  N   GLU A 234      40.225 -35.542   1.561  1.00118.35      A    N  
ANISOU 1718  N   GLU A 234    17668  10938  16363  -2905  -1128   -163  A    N  
ATOM   1719  CA  GLU A 234      39.715 -34.564   2.513  1.00119.89      A    C  
ANISOU 1719  CA  GLU A 234    17802  11262  16488  -3066   -924    -57  A    C  
ATOM   1720  C   GLU A 234      39.758 -35.059   3.961  1.00125.31      A    C  
ANISOU 1720  C   GLU A 234    18835  11710  17065  -3242   -856    121  A    C  
ATOM   1721  O   GLU A 234      39.935 -34.269   4.886  1.00124.16      A    O  
ANISOU 1721  O   GLU A 234    18731  11646  16798  -3270   -754    240  A    O  
ATOM   1722  CB  GLU A 234      38.296 -34.144   2.137  1.00124.39      A    C  
ANISOU 1722  CB  GLU A 234    18109  11976  17177  -3279   -750   -154  A    C  
ATOM   1723  CG  GLU A 234      38.154 -33.681   0.698  1.00134.45      A    C  
ANISOU 1723  CG  GLU A 234    19057  13477  18551  -3120   -824   -328  A    C  
ATOM   1724  CD  GLU A 234      36.816 -33.014   0.434  1.00147.12      A    C  
ANISOU 1724  CD  GLU A 234    20372  15265  20262  -3303   -655   -407  A    C  
ATOM   1725  OE1 GLU A 234      36.232 -32.453   1.390  1.00147.93      A    O  
ANISOU 1725  OE1 GLU A 234    20465  15408  20333  -3481   -457   -316  A    O  
ATOM   1726  OE2 GLU A 234      36.352 -33.048  -0.727  1.00152.37      A    O1-
ANISOU 1726  OE2 GLU A 234    20820  16033  21039  -3262   -722   -562  A    O1-
ATOM   1727  N   GLN A 235      39.602 -36.366   4.153  1.00131.71      A    N  
ANISOU 1727  N   GLN A 235    19912  12220  17913  -3359   -917    139  A    N  
ATOM   1728  CA  GLN A 235      39.590 -36.948   5.496  1.00130.05      A    C  
ANISOU 1728  CA  GLN A 235    20063  11757  17594  -3541   -856    313  A    C  
ATOM   1729  C   GLN A 235      40.991 -37.283   6.018  1.00124.11      A    C  
ANISOU 1729  C   GLN A 235    19590  10859  16709  -3319  -1052    432  A    C  
ATOM   1730  O   GLN A 235      41.225 -37.260   7.227  1.00117.46      A    O  
ANISOU 1730  O   GLN A 235    19003   9905  15721  -3402  -1006    598  A    O  
ATOM   1731  CB  GLN A 235      38.694 -38.183   5.527  1.00133.87      A    C  
ANISOU 1731  CB  GLN A 235    20716  11969  18181  -3801   -816    291  A    C  
ATOM   1732  CG  GLN A 235      38.715 -38.964   4.228  1.00139.99      A    C  
ANISOU 1732  CG  GLN A 235    21404  12677  19108  -3693   -988    118  A    C  
ATOM   1733  CD  GLN A 235      37.988 -40.288   4.330  1.00146.21      A    C  
ANISOU 1733  CD  GLN A 235    22414  13149  19992  -3943   -982    108  A    C  
ATOM   1734  NE2 GLN A 235      37.767 -40.930   3.185  1.00142.74      A    N  
ANISOU 1734  NE2 GLN A 235    21879  12658  19699  -3900  -1106    -64  A    N  
ATOM   1735  OE1 GLN A 235      37.630 -40.733   5.425  1.00148.58      A    O  
ANISOU 1735  OE1 GLN A 235    22979  13245  20230  -4178   -867    253  A    O  
ATOM   1736  N   HIS A 236      41.915 -37.597   5.110  1.00123.55      A    N  
ANISOU 1736  N   HIS A 236    19468  10789  16686  -3035  -1270    344  A    N  
ATOM   1737  CA  HIS A 236      43.316 -37.792   5.483  1.00121.87      A    C  
ANISOU 1737  CA  HIS A 236    19450  10484  16372  -2783  -1469    439  A    C  
ATOM   1738  C   HIS A 236      43.999 -36.444   5.726  1.00120.91      A    C  
ANISOU 1738  C   HIS A 236    19149  10642  16151  -2626  -1453    489  A    C  
ATOM   1739  O   HIS A 236      44.960 -36.354   6.494  1.00121.28      A    O  
ANISOU 1739  O   HIS A 236    19374  10629  16077  -2508  -1558    617  A    O  
ATOM   1740  CB  HIS A 236      44.071 -38.603   4.422  1.00122.58      A    C  
ANISOU 1740  CB  HIS A 236    19537  10482  16556  -2525  -1692    320  A    C  
ATOM   1741  CG  HIS A 236      45.523 -38.809   4.736  1.00129.34      A    C  
ANISOU 1741  CG  HIS A 236    20554  11255  17334  -2246  -1901    405  A    C  
ATOM   1742  CD2 HIS A 236      46.145 -39.196   5.876  1.00133.45      A    C  
ANISOU 1742  CD2 HIS A 236    21397  11571  17737  -2240  -1986    578  A    C  
ATOM   1743  ND1 HIS A 236      46.524 -38.601   3.808  1.00129.08      A    N  
ANISOU 1743  ND1 HIS A 236    20336  11363  17345  -1922  -2053    308  A    N  
ATOM   1744  CE1 HIS A 236      47.696 -38.854   4.362  1.00129.16      A    C  
ANISOU 1744  CE1 HIS A 236    20528  11264  17285  -1728  -2221    414  A    C  
ATOM   1745  NE2 HIS A 236      47.495 -39.217   5.617  1.00132.29      A    N  
ANISOU 1745  NE2 HIS A 236    21237  11447  17579  -1912  -2196    578  A    N  
ATOM   1746  N   GLN A 237      43.501 -35.397   5.068  1.00113.28      A    N  
ANISOU 1746  N   GLN A 237    17832   9971  15237  -2627  -1332    389  A    N  
ATOM   1747  CA  GLN A 237      43.946 -34.042   5.368  1.00106.21      A    C  
ANISOU 1747  CA  GLN A 237    16769   9333  14252  -2533  -1281    439  A    C  
ATOM   1748  C   GLN A 237      43.488 -33.674   6.777  1.00108.32      A    C  
ANISOU 1748  C   GLN A 237    17225   9547  14386  -2762  -1119    590  A    C  
ATOM   1749  O   GLN A 237      44.305 -33.372   7.642  1.00112.00      A    O  
ANISOU 1749  O   GLN A 237    17855   9988  14714  -2688  -1185    717  A    O  
ATOM   1750  CB  GLN A 237      43.403 -33.038   4.342  1.00104.70      A    C  
ANISOU 1750  CB  GLN A 237    16181   9448  14151  -2499  -1180    301  A    C  
ATOM   1751  CG  GLN A 237      43.868 -31.586   4.537  1.00 98.20      A    C  
ANISOU 1751  CG  GLN A 237    15170   8891  13248  -2393  -1131    342  A    C  
ATOM   1752  CD  GLN A 237      45.340 -31.374   4.196  1.00 98.60      A    C  
ANISOU 1752  CD  GLN A 237    15186   9011  13267  -2088  -1330    356  A    C  
ATOM   1753  NE2 GLN A 237      45.942 -30.334   4.773  1.00 94.03      A    N  
ANISOU 1753  NE2 GLN A 237    14564   8573  12589  -2024  -1320    442  A    N  
ATOM   1754  OE1 GLN A 237      45.926 -32.135   3.425  1.00101.76      A    O  
ANISOU 1754  OE1 GLN A 237    15595   9337  13734  -1914  -1487    286  A    O  
ATOM   1755  N   LEU A 238      42.180 -33.713   7.012  1.00107.84      A    N  
ANISOU 1755  N   LEU A 238    17141   9469  14363  -3040   -906    573  A    N  
ATOM   1756  CA  LEU A 238      41.642 -33.422   8.337  1.00109.16      A    C  
ANISOU 1756  CA  LEU A 238    17494   9580  14400  -3274   -720    707  A    C  
ATOM   1757  C   LEU A 238      42.372 -34.198   9.427  1.00115.24      A    C  
ANISOU 1757  C   LEU A 238    18689  10078  15021  -3280   -834    873  A    C  
ATOM   1758  O   LEU A 238      42.608 -33.687  10.523  1.00111.45      A    O  
ANISOU 1758  O   LEU A 238    18375   9599  14372  -3331   -778   1003  A    O  
ATOM   1759  CB  LEU A 238      40.155 -33.744   8.389  1.00106.23      A    C  
ANISOU 1759  CB  LEU A 238    17081   9163  14120  -3582   -493    663  A    C  
ATOM   1760  CG  LEU A 238      39.247 -32.531   8.249  1.00109.18      A    C  
ANISOU 1760  CG  LEU A 238    17134   9815  14536  -3676   -270    595  A    C  
ATOM   1761  CD1 LEU A 238      37.848 -32.974   7.882  1.00113.55      A    C  
ANISOU 1761  CD1 LEU A 238    17555  10343  15247  -3926   -103    504  A    C  
ATOM   1762  CD2 LEU A 238      39.243 -31.730   9.540  1.00107.38      A    C  
ANISOU 1762  CD2 LEU A 238    17043   9631  14127  -3771   -113    727  A    C  
ATOM   1763  N   ALA A 239      42.720 -35.441   9.124  1.00119.38      A    N  
ANISOU 1763  N   ALA A 239    19398  10358  15602  -3224  -1002    868  A    N  
ATOM   1764  CA  ALA A 239      43.465 -36.256  10.066  1.00117.95      A    C  
ANISOU 1764  CA  ALA A 239    19625   9898  15291  -3201  -1145   1024  A    C  
ATOM   1765  C   ALA A 239      44.820 -35.616  10.319  1.00115.06      A    C  
ANISOU 1765  C   ALA A 239    19261   9637  14819  -2929  -1328   1086  A    C  
ATOM   1766  O   ALA A 239      45.189 -35.366  11.462  1.00119.23      A    O  
ANISOU 1766  O   ALA A 239    20023  10107  15171  -2968  -1333   1235  A    O  
ATOM   1767  CB  ALA A 239      43.629 -37.669   9.535  1.00119.32      A    C  
ANISOU 1767  CB  ALA A 239    19966   9799  15571  -3154  -1309    984  A    C  
ATOM   1768  N   LEU A 240      45.554 -35.344   9.246  1.00112.12      A    N  
ANISOU 1768  N   LEU A 240    18625   9423  14551  -2658  -1477    971  A    N  
ATOM   1769  CA  LEU A 240      46.887 -34.761   9.359  1.00113.18      A    C  
ANISOU 1769  CA  LEU A 240    18719   9668  14617  -2391  -1659   1017  A    C  
ATOM   1770  C   LEU A 240      46.879 -33.441  10.121  1.00113.43      A    C  
ANISOU 1770  C   LEU A 240    18680   9903  14516  -2454  -1541   1089  A    C  
ATOM   1771  O   LEU A 240      47.856 -33.102  10.800  1.00109.06      A    O  
ANISOU 1771  O   LEU A 240    18243   9352  13845  -2332  -1677   1191  A    O  
ATOM   1772  CB  LEU A 240      47.511 -34.565   7.978  1.00111.94      A    C  
ANISOU 1772  CB  LEU A 240    18239   9688  14604  -2120  -1781    866  A    C  
ATOM   1773  CG  LEU A 240      48.405 -35.698   7.486  1.00117.27      A    C  
ANISOU 1773  CG  LEU A 240    19036  10169  15351  -1896  -2021    839  A    C  
ATOM   1774  CD1 LEU A 240      48.798 -35.457   6.044  1.00116.44      A    C  
ANISOU 1774  CD1 LEU A 240    18595  10262  15384  -1664  -2082    670  A    C  
ATOM   1775  CD2 LEU A 240      49.639 -35.811   8.372  1.00122.43      A    C  
ANISOU 1775  CD2 LEU A 240    19910  10716  15892  -1737  -2222    983  A    C  
ATOM   1776  N   ILE A 241      45.773 -32.706  10.000  1.00114.51      A    N  
ANISOU 1776  N   ILE A 241    18624  10206  14678  -2639  -1295   1029  A    N  
ATOM   1777  CA  ILE A 241      45.597 -31.426  10.684  1.00107.28      A    C  
ANISOU 1777  CA  ILE A 241    17636   9480  13646  -2716  -1150   1077  A    C  
ATOM   1778  C   ILE A 241      45.449 -31.626  12.186  1.00104.91      A    C  
ANISOU 1778  C   ILE A 241    17715   8999  13148  -2902  -1085   1242  A    C  
ATOM   1779  O   ILE A 241      45.918 -30.806  12.976  1.00103.77      A    O  
ANISOU 1779  O   ILE A 241    17639   8935  12855  -2878  -1093   1323  A    O  
ATOM   1780  CB  ILE A 241      44.355 -30.663  10.169  1.00104.30      A    C  
ANISOU 1780  CB  ILE A 241    16961   9309  13359  -2868   -895    966  A    C  
ATOM   1781  CG1 ILE A 241      44.589 -30.120   8.757  1.00104.55      A    C  
ANISOU 1781  CG1 ILE A 241    16605   9573  13544  -2666   -957    815  A    C  
ATOM   1782  CG2 ILE A 241      44.009 -29.520  11.103  1.00100.20      A    C  
ANISOU 1782  CG2 ILE A 241    16450   8920  12702  -2990   -715   1030  A    C  
ATOM   1783  CD1 ILE A 241      43.440 -29.273   8.231  1.00100.48      A    C  
ANISOU 1783  CD1 ILE A 241    15787   9273  13116  -2785   -735    709  A    C  
ATOM   1784  N   SER A 242      44.788 -32.717  12.572  1.00102.94      A    N  
ANISOU 1784  N   SER A 242    17721   8501  12891  -3094  -1020   1291  A    N  
ATOM   1785  CA  SER A 242      44.587 -33.044  13.978  1.00102.39      A    C  
ANISOU 1785  CA  SER A 242    18048   8232  12623  -3287   -947   1456  A    C  
ATOM   1786  C   SER A 242      45.888 -33.476  14.642  1.00110.89      A    C  
ANISOU 1786  C   SER A 242    19427   9142  13564  -3114  -1223   1588  A    C  
ATOM   1787  O   SER A 242      46.151 -33.111  15.786  1.00112.33      A    O  
ANISOU 1787  O   SER A 242    19852   9287  13542  -3172  -1218   1716  A    O  
ATOM   1788  CB  SER A 242      43.530 -34.134  14.134  1.00106.95      A    C  
ANISOU 1788  CB  SER A 242    18810   8581  13244  -3546   -801   1475  A    C  
ATOM   1789  OG  SER A 242      42.253 -33.653  13.763  1.00112.48      A    O  
ANISOU 1789  OG  SER A 242    19250   9439  14047  -3740   -524   1373  A    O  
ATOM   1790  N   GLN A 243      46.699 -34.247  13.922  1.00116.61      A    N  
ANISOU 1790  N   GLN A 243    20137   9767  14403  -2895  -1469   1551  A    N  
ATOM   1791  CA  GLN A 243      47.985 -34.718  14.440  1.00120.77      A    C  
ANISOU 1791  CA  GLN A 243    20916  10135  14835  -2698  -1759   1663  A    C  
ATOM   1792  C   GLN A 243      49.026 -33.591  14.493  1.00119.53      A    C  
ANISOU 1792  C   GLN A 243    20579  10210  14629  -2486  -1891   1664  A    C  
ATOM   1793  O   GLN A 243      50.216 -33.835  14.722  1.00117.44      A    O  
ANISOU 1793  O   GLN A 243    20424   9870  14327  -2275  -2157   1730  A    O  
ATOM   1794  CB  GLN A 243      48.510 -35.881  13.595  1.00120.46      A    C  
ANISOU 1794  CB  GLN A 243    20892   9924  14953  -2514  -1969   1607  A    C  
ATOM   1795  CG  GLN A 243      47.462 -36.930  13.265  1.00128.97      A    C  
ANISOU 1795  CG  GLN A 243    22074  10802  16129  -2712  -1844   1565  A    C  
ATOM   1796  CD  GLN A 243      47.904 -37.862  12.151  1.00128.77      A    C  
ANISOU 1796  CD  GLN A 243    21969  10670  16288  -2510  -2027   1454  A    C  
ATOM   1797  NE2 GLN A 243      47.154 -38.944  11.947  1.00122.98      A    N  
ANISOU 1797  NE2 GLN A 243    21392   9703  15633  -2668  -1973   1431  A    N  
ATOM   1798  OE1 GLN A 243      48.909 -37.610  11.482  1.00127.29      A    O  
ANISOU 1798  OE1 GLN A 243    21583  10609  16173  -2219  -2209   1386  A    O  
ATOM   1799  N   LEU A 244      48.568 -32.360  14.273  1.00115.80      A    N  
ANISOU 1799  N   LEU A 244    19821  10012  14165  -2543  -1708   1590  A    N  
ATOM   1800  CA  LEU A 244      49.421 -31.179  14.386  1.00111.89      A    C  
ANISOU 1800  CA  LEU A 244    19158   9738  13618  -2389  -1799   1593  A    C  
ATOM   1801  C   LEU A 244      48.749 -30.088  15.220  1.00110.53      A    C  
ANISOU 1801  C   LEU A 244    19010   9693  13293  -2586  -1574   1629  A    C  
ATOM   1802  O   LEU A 244      49.410 -29.394  15.987  1.00114.50      A    O  
ANISOU 1802  O   LEU A 244    19607  10248  13650  -2541  -1662   1704  A    O  
ATOM   1803  CB  LEU A 244      49.775 -30.625  13.002  1.00103.53      A    C  
ANISOU 1803  CB  LEU A 244    17659   8923  12754  -2186  -1838   1440  A    C  
ATOM   1804  CG  LEU A 244      50.720 -29.422  12.954  1.00 95.46      A    C  
ANISOU 1804  CG  LEU A 244    16425   8133  11711  -2017  -1939   1434  A    C  
ATOM   1805  CD1 LEU A 244      52.156 -29.851  13.216  1.00 95.24      A    C  
ANISOU 1805  CD1 LEU A 244    16517   8008  11662  -1789  -2254   1510  A    C  
ATOM   1806  CD2 LEU A 244      50.612 -28.703  11.618  1.00 89.53      A    C  
ANISOU 1806  CD2 LEU A 244    15239   7645  11135  -1907  -1865   1281  A    C  
ATOM   1807  N   CYS A 245      47.433 -29.955  15.079  1.00107.72      A    N  
ANISOU 1807  N   CYS A 245    18571   9382  12975  -2804  -1289   1569  A    N  
ATOM   1808  CA  CYS A 245      46.707 -28.838  15.681  1.00111.84      A    C  
ANISOU 1808  CA  CYS A 245    19048  10057  13388  -2971  -1046   1569  A    C  
ATOM   1809  C   CYS A 245      45.840 -29.215  16.885  1.00118.23      A    C  
ANISOU 1809  C   CYS A 245    20210  10692  14019  -3248   -846   1677  A    C  
ATOM   1810  O   CYS A 245      45.273 -28.343  17.550  1.00116.91      A    O  
ANISOU 1810  O   CYS A 245    20062  10627  13732  -3387   -639   1689  A    O  
ATOM   1811  CB  CYS A 245      45.852 -28.139  14.616  1.00111.20      A    C  
ANISOU 1811  CB  CYS A 245    18553  10211  13487  -2994   -850   1411  A    C  
ATOM   1812  SG  CYS A 245      46.814 -27.391  13.275  1.00119.13      A    S  
ANISOU 1812  SG  CYS A 245    19138  11465  14661  -2689  -1033   1292  A    S  
ATOM   1813  N   GLY A 246      45.748 -30.508  17.171  1.00124.07      A    N  
ANISOU 1813  N   GLY A 246    21240  11163  14738  -3325   -903   1757  A    N  
ATOM   1814  CA  GLY A 246      44.862 -30.989  18.212  1.00128.16      A    C  
ANISOU 1814  CA  GLY A 246    22092  11501  15102  -3605   -695   1861  A    C  
ATOM   1815  C   GLY A 246      43.556 -31.447  17.599  1.00134.84      A    C  
ANISOU 1815  C   GLY A 246    22778  12337  16116  -3800   -450   1771  A    C  
ATOM   1816  O   GLY A 246      43.338 -31.289  16.400  1.00136.12      A    O  
ANISOU 1816  O   GLY A 246    22574  12647  16497  -3712   -449   1625  A    O  
ATOM   1817  N   SER A 247      42.686 -32.024  18.417  1.00140.55      A    N  
ANISOU 1817  N   SER A 247    23779  12887  16737  -4071   -245   1859  A    N  
ATOM   1818  CA  SER A 247      41.397 -32.490  17.928  1.00142.22      A    C  
ANISOU 1818  CA  SER A 247    23846  13078  17112  -4288     -4   1781  A    C  
ATOM   1819  C   SER A 247      40.439 -31.316  17.762  1.00132.03      A    C  
ANISOU 1819  C   SER A 247    22226  12063  15877  -4390    285   1672  A    C  
ATOM   1820  O   SER A 247      40.665 -30.237  18.314  1.00128.77      A    O  
ANISOU 1820  O   SER A 247    21800  11803  15324  -4346    342   1689  A    O  
ATOM   1821  CB  SER A 247      40.813 -33.545  18.871  1.00155.71      A    C  
ANISOU 1821  CB  SER A 247    25967  14496  18700  -4554    123   1921  A    C  
ATOM   1822  OG  SER A 247      40.958 -33.165  20.229  1.00162.68      A    O  
ANISOU 1822  OG  SER A 247    27186  15330  19295  -4646    205   2066  A    O  
ATOM   1823  N   ILE A 248      39.376 -31.533  16.997  1.00127.69      A    N  
ANISOU 1823  N   ILE A 248    21412  11570  15537  -4520    457   1558  A    N  
ATOM   1824  CA  ILE A 248      38.418 -30.478  16.691  1.00125.85      A    C  
ANISOU 1824  CA  ILE A 248    20823  11597  15396  -4598    715   1439  A    C  
ATOM   1825  C   ILE A 248      37.181 -30.569  17.585  1.00136.31      A    C  
ANISOU 1825  C   ILE A 248    22274  12867  16650  -4921   1068   1490  A    C  
ATOM   1826  O   ILE A 248      36.138 -31.054  17.154  1.00144.28      A    O  
ANISOU 1826  O   ILE A 248    23130  13856  17832  -5103   1233   1424  A    O  
ATOM   1827  CB  ILE A 248      37.971 -30.562  15.219  1.00117.59      A    C  
ANISOU 1827  CB  ILE A 248    19360  10679  14638  -4530    681   1266  A    C  
ATOM   1828  CG1 ILE A 248      39.187 -30.592  14.294  1.00111.44      A    C  
ANISOU 1828  CG1 ILE A 248    18471   9941  13929  -4217    348   1216  A    C  
ATOM   1829  CG2 ILE A 248      37.054 -29.407  14.864  1.00113.56      A    C  
ANISOU 1829  CG2 ILE A 248    18472  10447  14230  -4576    915   1145  A    C  
ATOM   1830  CD1 ILE A 248      38.865 -31.056  12.895  1.00106.52      A    C  
ANISOU 1830  CD1 ILE A 248    17552   9362  13557  -4156    270   1067  A    C  
ATOM   1831  N   THR A 249      37.293 -30.097  18.823  1.00132.55      A    N  
ANISOU 1831  N   THR A 249    22074  12368  15920  -4995   1187   1603  A    N  
ATOM   1832  CA  THR A 249      36.187 -30.190  19.774  1.00130.50      A    C  
ANISOU 1832  CA  THR A 249    21973  12050  15560  -5300   1539   1664  A    C  
ATOM   1833  C   THR A 249      35.679 -28.814  20.192  1.00126.85      A    C  
ANISOU 1833  C   THR A 249    21341  11830  15026  -5321   1790   1606  A    C  
ATOM   1834  O   THR A 249      36.437 -27.852  20.189  1.00127.20      A    O  
ANISOU 1834  O   THR A 249    21323  12018  14990  -5114   1660   1582  A    O  
ATOM   1835  CB  THR A 249      36.597 -30.982  21.023  1.00132.31      A    C  
ANISOU 1835  CB  THR A 249    22753  12001  15519  -5418   1510   1863  A    C  
ATOM   1836  CG2 THR A 249      36.826 -32.448  20.669  1.00136.12      A    C  
ANISOU 1836  CG2 THR A 249    23416  12211  16092  -5451   1324   1921  A    C  
ATOM   1837  OG1 THR A 249      37.801 -30.429  21.567  1.00126.36      A    O  
ANISOU 1837  OG1 THR A 249    22201  11261  14548  -5211   1288   1936  A    O  
ATOM   1838  N   PRO A 250      34.388 -28.721  20.554  1.00126.73      A    N  
ANISOU 1838  N   PRO A 250    21249  11856  15046  -5574   2155   1581  A    N  
ATOM   1839  CA  PRO A 250      33.723 -27.468  20.940  1.00129.72      A    C  
ANISOU 1839  CA  PRO A 250    21449  12459  15380  -5611   2438   1511  A    C  
ATOM   1840  C   PRO A 250      34.394 -26.776  22.121  1.00138.29      A    C  
ANISOU 1840  C   PRO A 250    22870  13534  16139  -5558   2442   1611  A    C  
ATOM   1841  O   PRO A 250      33.992 -25.673  22.498  1.00135.02      A    O  
ANISOU 1841  O   PRO A 250    22349  13294  15659  -5559   2650   1553  A    O  
ATOM   1842  CB  PRO A 250      32.317 -27.927  21.341  1.00130.76      A    C  
ANISOU 1842  CB  PRO A 250    21564  12544  15573  -5933   2816   1515  A    C  
ATOM   1843  CG  PRO A 250      32.113 -29.198  20.609  1.00126.26      A    C  
ANISOU 1843  CG  PRO A 250    20955  11814  15206  -6021   2701   1512  A    C  
ATOM   1844  CD  PRO A 250      33.456 -29.861  20.560  1.00123.45      A    C  
ANISOU 1844  CD  PRO A 250    20894  11271  14740  -5844   2320   1610  A    C  
ATOM   1845  N   GLU A 251      35.395 -27.427  22.703  1.00151.25      A    N  
ANISOU 1845  N   GLU A 251    24922  14968  17579  -5510   2206   1756  A    N  
ATOM   1846  CA  GLU A 251      36.167 -26.847  23.795  1.00160.65      A    C  
ANISOU 1846  CA  GLU A 251    26456  16132  18451  -5444   2145   1854  A    C  
ATOM   1847  C   GLU A 251      37.226 -25.908  23.226  1.00155.17      A    C  
ANISOU 1847  C   GLU A 251    25565  15602  17791  -5141   1858   1781  A    C  
ATOM   1848  O   GLU A 251      37.641 -24.943  23.871  1.00149.61      A    O  
ANISOU 1848  O   GLU A 251    24964  14983  16896  -5067   1859   1790  A    O  
ATOM   1849  CB  GLU A 251      36.827 -27.958  24.616  1.00169.97      A    C  
ANISOU 1849  CB  GLU A 251    28151  17017  19411  -5506   1980   2043  A    C  
ATOM   1850  CG  GLU A 251      37.630 -27.472  25.810  1.00176.14      A    C  
ANISOU 1850  CG  GLU A 251    29335  17749  19843  -5451   1892   2157  A    C  
ATOM   1851  CD  GLU A 251      38.141 -28.615  26.664  1.00184.48      A    C  
ANISOU 1851  CD  GLU A 251    30917  18502  20675  -5534   1752   2352  A    C  
ATOM   1852  OE1 GLU A 251      37.990 -29.785  26.245  1.00184.39      A    O  
ANISOU 1852  OE1 GLU A 251    30946  18314  20799  -5606   1688   2396  A    O  
ATOM   1853  OE2 GLU A 251      38.691 -28.344  27.755  1.00188.38      A    O1-
ANISOU 1853  OE2 GLU A 251    31794  18927  20854  -5527   1697   2461  A    O1-
ATOM   1854  N   VAL A 252      37.644 -26.205  21.999  1.00154.78      A    N  
ANISOU 1854  N   VAL A 252    25232  15593  17985  -4974   1621   1706  A    N  
ATOM   1855  CA  VAL A 252      38.663 -25.441  21.289  1.00147.36      A    C  
ANISOU 1855  CA  VAL A 252    24072  14804  17115  -4690   1343   1637  A    C  
ATOM   1856  C   VAL A 252      38.010 -24.529  20.244  1.00136.51      A    C  
ANISOU 1856  C   VAL A 252    22194  13690  15984  -4623   1469   1463  A    C  
ATOM   1857  O   VAL A 252      38.486 -23.422  19.977  1.00134.35      A    O  
ANISOU 1857  O   VAL A 252    21739  13593  15715  -4451   1390   1398  A    O  
ATOM   1858  CB  VAL A 252      39.685 -26.400  20.616  1.00119.18      A    C  
ANISOU 1858  CB  VAL A 252    20544  11100  13637  -4524    979   1675  A    C  
ATOM   1859  CG1 VAL A 252      40.573 -25.665  19.645  1.00114.06      A    C  
ANISOU 1859  CG1 VAL A 252    19582  10634  13121  -4244    735   1581  A    C  
ATOM   1860  CG2 VAL A 252      40.528 -27.101  21.673  1.00124.17      A    C  
ANISOU 1860  CG2 VAL A 252    21672  11493  14015  -4533    801   1850  A    C  
ATOM   1861  N   TRP A 253      36.895 -24.994  19.687  1.00128.00      A    N  
ANISOU 1861  N   TRP A 253    20902  12627  15105  -4770   1664   1391  A    N  
ATOM   1862  CA  TRP A 253      36.224 -24.330  18.575  1.00122.03      A    C  
ANISOU 1862  CA  TRP A 253    19663  12096  14606  -4708   1752   1227  A    C  
ATOM   1863  C   TRP A 253      34.716 -24.280  18.824  1.00125.96      A    C  
ANISOU 1863  C   TRP A 253    20034  12642  15181  -4951   2132   1175  A    C  
ATOM   1864  O   TRP A 253      33.964 -25.064  18.247  1.00126.05      A    O  
ANISOU 1864  O   TRP A 253    19898  12611  15386  -5075   2201   1131  A    O  
ATOM   1865  CB  TRP A 253      36.510 -25.112  17.290  1.00118.61      A    C  
ANISOU 1865  CB  TRP A 253    19026  11638  14403  -4596   1517   1167  A    C  
ATOM   1866  CG  TRP A 253      35.965 -24.535  16.005  1.00113.29      A    C  
ANISOU 1866  CG  TRP A 253    17871  11185  13991  -4503   1542   1002  A    C  
ATOM   1867  CD1 TRP A 253      35.073 -23.509  15.864  1.00113.65      A    C  
ANISOU 1867  CD1 TRP A 253    17631  11433  14118  -4535   1773    903  A    C  
ATOM   1868  CD2 TRP A 253      36.255 -24.997  14.681  1.00104.25      A    C  
ANISOU 1868  CD2 TRP A 253    16489  10068  13052  -4361   1323    919  A    C  
ATOM   1869  CE2 TRP A 253      35.518 -24.193  13.784  1.00107.64      A    C  
ANISOU 1869  CE2 TRP A 253    16501  10724  13672  -4316   1425    775  A    C  
ATOM   1870  CE3 TRP A 253      37.076 -26.005  14.167  1.00 92.70      A    C  
ANISOU 1870  CE3 TRP A 253    15136   8458  11627  -4258   1049    948  A    C  
ATOM   1871  NE1 TRP A 253      34.808 -23.289  14.529  1.00108.23      A    N  
ANISOU 1871  NE1 TRP A 253    16547  10900  13674  -4419   1695    770  A    N  
ATOM   1872  CZ2 TRP A 253      35.578 -24.368  12.404  1.00108.09      A    C  
ANISOU 1872  CZ2 TRP A 253    16264  10868  13937  -4180   1261    665  A    C  
ATOM   1873  CZ3 TRP A 253      37.134 -26.179  12.801  1.00 97.93      A    C  
ANISOU 1873  CZ3 TRP A 253    15501   9207  12499  -4121    900    831  A    C  
ATOM   1874  CH2 TRP A 253      36.390 -25.365  11.932  1.00105.75      A    C  
ANISOU 1874  CH2 TRP A 253    16092  10428  13661  -4087   1005    692  A    C  
ATOM   1875  N   PRO A 254      34.269 -23.350  19.682  1.00130.55      A    N  
ANISOU 1875  N   PRO A 254    20668  13314  15619  -5020   2383   1174  A    N  
ATOM   1876  CA  PRO A 254      32.856 -23.256  20.067  1.00134.86      A    C  
ANISOU 1876  CA  PRO A 254    21110  13910  16220  -5252   2774   1130  A    C  
ATOM   1877  C   PRO A 254      31.893 -23.470  18.896  1.00137.82      A    C  
ANISOU 1877  C   PRO A 254    21042  14395  16928  -5292   2846    996  A    C  
ATOM   1878  O   PRO A 254      32.083 -22.901  17.822  1.00131.38      A    O  
ANISOU 1878  O   PRO A 254    19889  13741  16289  -5099   2692    886  A    O  
ATOM   1879  CB  PRO A 254      32.743 -21.826  20.595  1.00132.19      A    C  
ANISOU 1879  CB  PRO A 254    20718  13744  15764  -5180   2938   1079  A    C  
ATOM   1880  CG  PRO A 254      34.089 -21.545  21.159  1.00130.74      A    C  
ANISOU 1880  CG  PRO A 254    20853  13489  15333  -5028   2685   1173  A    C  
ATOM   1881  CD  PRO A 254      35.075 -22.272  20.280  1.00130.17      A    C  
ANISOU 1881  CD  PRO A 254    20753  13341  15366  -4872   2308   1197  A    C  
ATOM   1882  N   ASN A 255      30.875 -24.296  19.115  1.00146.68      A    N  
ANISOU 1882  N   ASN A 255    22177  15425  18131  -5550   3073   1011  A    N  
ATOM   1883  CA  ASN A 255      29.845 -24.569  18.111  1.00148.33      A    C  
ANISOU 1883  CA  ASN A 255    21976  15725  18656  -5629   3158    885  A    C  
ATOM   1884  C   ASN A 255      30.335 -25.234  16.828  1.00145.93      A    C  
ANISOU 1884  C   ASN A 255    21509  15390  18546  -5496   2830    832  A    C  
ATOM   1885  O   ASN A 255      29.656 -25.180  15.803  1.00148.46      A    O  
ANISOU 1885  O   ASN A 255    21444  15836  19127  -5486   2834    701  A    O  
ATOM   1886  CB  ASN A 255      29.060 -23.301  17.770  1.00147.24      A    C  
ANISOU 1886  CB  ASN A 255    21437  15853  18653  -5562   3351    744  A    C  
ATOM   1887  CG  ASN A 255      27.970 -23.007  18.776  1.00152.25      A    C  
ANISOU 1887  CG  ASN A 255    22104  16517  19226  -5784   3770    751  A    C  
ATOM   1888  ND2 ASN A 255      27.307 -21.868  18.609  1.00150.08      A    N  
ANISOU 1888  ND2 ASN A 255    21511  16462  19051  -5715   3951    632  A    N  
ATOM   1889  OD1 ASN A 255      27.721 -23.796  19.693  1.00155.19      A    O  
ANISOU 1889  OD1 ASN A 255    22788  16715  19461  -6014   3936    863  A    O  
ATOM   1890  N   VAL A 256      31.505 -25.864  16.885  1.00141.08      A    N  
ANISOU 1890  N   VAL A 256    21190  14609  17803  -5389   2545    928  A    N  
ATOM   1891  CA  VAL A 256      32.009 -26.613  15.738  1.00134.64      A    C  
ANISOU 1891  CA  VAL A 256    20267  13738  17152  -5266   2244    882  A    C  
ATOM   1892  C   VAL A 256      31.100 -27.797  15.433  1.00142.31      A    C  
ANISOU 1892  C   VAL A 256    21197  14573  18301  -5502   2331    862  A    C  
ATOM   1893  O   VAL A 256      30.975 -28.208  14.282  1.00144.86      A    O  
ANISOU 1893  O   VAL A 256    21278  14922  18840  -5443   2177    759  A    O  
ATOM   1894  CB  VAL A 256      33.448 -27.123  15.956  1.00122.21      A    C  
ANISOU 1894  CB  VAL A 256    19035  11994  15404  -5107   1933    996  A    C  
ATOM   1895  CG1 VAL A 256      33.489 -28.153  17.070  1.00122.77      A    C  
ANISOU 1895  CG1 VAL A 256    19563  11791  15295  -5312   1998   1156  A    C  
ATOM   1896  CG2 VAL A 256      33.995 -27.712  14.669  1.00114.72      A    C  
ANISOU 1896  CG2 VAL A 256    17926  11027  14634  -4937   1633    922  A    C  
ATOM   1897  N   ASP A 257      30.461 -28.331  16.471  1.00150.60      A    N  
ANISOU 1897  N   ASP A 257    22493  15476  19252  -5776   2582    960  A    N  
ATOM   1898  CA  ASP A 257      29.576 -29.490  16.338  1.00153.20      A    C  
ANISOU 1898  CA  ASP A 257    22823  15650  19737  -6042   2690    960  A    C  
ATOM   1899  C   ASP A 257      28.252 -29.130  15.665  1.00158.02      A    C  
ANISOU 1899  C   ASP A 257    22965  16452  20622  -6157   2897    805  A    C  
ATOM   1900  O   ASP A 257      27.409 -29.994  15.432  1.00161.01      A    O  
ANISOU 1900  O   ASP A 257    23267  16735  21173  -6385   2990    779  A    O  
ATOM   1901  CB  ASP A 257      29.313 -30.130  17.705  1.00145.78      A    C  
ANISOU 1901  CB  ASP A 257    22304  14493  18591  -6310   2914   1126  A    C  
ATOM   1902  CG  ASP A 257      28.608 -29.187  18.671  1.00141.58      A    C  
ANISOU 1902  CG  ASP A 257    21754  14103  17938  -6427   3279   1140  A    C  
ATOM   1903  OD1 ASP A 257      28.851 -27.965  18.608  1.00135.94      A    O  
ANISOU 1903  OD1 ASP A 257    20871  13601  17178  -6233   3281   1074  A    O  
ATOM   1904  OD2 ASP A 257      27.810 -29.671  19.501  1.00144.71      A    O1-
ANISOU 1904  OD2 ASP A 257    22312  14390  18281  -6716   3572   1216  A    O1-
ATOM   1905  N   ASN A 258      28.080 -27.850  15.354  1.00156.80      A    N  
ANISOU 1905  N   ASN A 258    22499  16563  20514  -5998   2957    703  A    N  
ATOM   1906  CA  ASN A 258      26.877 -27.361  14.692  1.00155.17      A    C  
ANISOU 1906  CA  ASN A 258    21825  16562  20568  -6064   3129    551  A    C  
ATOM   1907  C   ASN A 258      26.866 -27.735  13.205  1.00148.25      A    C  
ANISOU 1907  C   ASN A 258    20646  15736  19945  -5951   2864    419  A    C  
ATOM   1908  O   ASN A 258      25.924 -27.416  12.479  1.00142.44      A    O  
ANISOU 1908  O   ASN A 258    19507  15166  19447  -5984   2941    283  A    O  
ATOM   1909  CB  ASN A 258      26.786 -25.840  14.862  1.00158.22      A    C  
ANISOU 1909  CB  ASN A 258    22012  17198  20905  -5903   3257    492  A    C  
ATOM   1910  CG  ASN A 258      25.359 -25.329  14.854  1.00160.26      A    C  
ANISOU 1910  CG  ASN A 258    21908  17629  21355  -6053   3577    387  A    C  
ATOM   1911  ND2 ASN A 258      25.174 -24.097  14.384  1.00156.03      A    N  
ANISOU 1911  ND2 ASN A 258    21051  17335  20901  -5862   3593    277  A    N  
ATOM   1912  OD1 ASN A 258      24.436 -26.025  15.275  1.00162.13      A    O  
ANISOU 1912  OD1 ASN A 258    22152  17779  21670  -6336   3810    407  A    O  
ATOM   1913  N   TYR A 259      27.921 -28.414  12.759  1.00148.67      A    N  
ANISOU 1913  N   TYR A 259    20900  15644  19943  -5811   2548    457  A    N  
ATOM   1914  CA  TYR A 259      28.073 -28.772  11.348  1.00155.35      A    C  
ANISOU 1914  CA  TYR A 259    21508  16528  20990  -5674   2276    334  A    C  
ATOM   1915  C   TYR A 259      27.876 -30.263  11.097  1.00151.71      A    C  
ANISOU 1915  C   TYR A 259    21192  15821  20630  -5857   2186    346  A    C  
ATOM   1916  O   TYR A 259      28.411 -31.103  11.821  1.00150.26      A    O  
ANISOU 1916  O   TYR A 259    21409  15391  20293  -5941   2150    481  A    O  
ATOM   1917  CB  TYR A 259      29.447 -28.341  10.819  1.00168.88      A    C  
ANISOU 1917  CB  TYR A 259    23282  18291  22593  -5338   1970    337  A    C  
ATOM   1918  CG  TYR A 259      29.656 -26.845  10.823  1.00178.49      A    C  
ANISOU 1918  CG  TYR A 259    24312  19758  23748  -5141   2018    303  A    C  
ATOM   1919  CD1 TYR A 259      29.113 -26.049   9.824  1.00182.89      A    C  
ANISOU 1919  CD1 TYR A 259    24447  20553  24491  -5030   2009    157  A    C  
ATOM   1920  CD2 TYR A 259      30.389 -26.229  11.829  1.00179.40      A    C  
ANISOU 1920  CD2 TYR A 259    24684  19861  23618  -5068   2062    417  A    C  
ATOM   1921  CE1 TYR A 259      29.292 -24.684   9.826  1.00183.63      A    C  
ANISOU 1921  CE1 TYR A 259    24384  20856  24532  -4852   2052    129  A    C  
ATOM   1922  CE2 TYR A 259      30.574 -24.866  11.841  1.00180.55      A    C  
ANISOU 1922  CE2 TYR A 259    24671  20218  23712  -4898   2103    382  A    C  
ATOM   1923  CZ  TYR A 259      30.024 -24.097  10.838  1.00184.32      A    C  
ANISOU 1923  CZ  TYR A 259    24733  20920  24381  -4790   2102    240  A    C  
ATOM   1924  OH  TYR A 259      30.209 -22.735  10.847  1.00186.44      A    O  
ANISOU 1924  OH  TYR A 259    24858  21381  24600  -4620   2140    210  A    O  
ATOM   1925  N   GLU A 260      27.125 -30.582  10.047  1.00151.71      A    N  
ANISOU 1925  N   GLU A 260    20874  15882  20887  -5912   2132    202  A    N  
ATOM   1926  CA  GLU A 260      26.781 -31.965   9.733  1.00157.39      A    C  
ANISOU 1926  CA  GLU A 260    21690  16374  21736  -6109   2056    189  A    C  
ATOM   1927  C   GLU A 260      27.887 -32.707   8.986  1.00151.14      A    C  
ANISOU 1927  C   GLU A 260    21079  15434  20914  -5907   1698    179  A    C  
ATOM   1928  O   GLU A 260      27.642 -33.348   7.963  1.00156.28      A    O  
ANISOU 1928  O   GLU A 260    21586  16047  21747  -5913   1534     61  A    O  
ATOM   1929  CB  GLU A 260      25.476 -32.031   8.932  1.00165.17      A    C  
ANISOU 1929  CB  GLU A 260    22259  17480  23018  -6268   2138     31  A    C  
ATOM   1930  CG  GLU A 260      24.962 -33.448   8.714  1.00172.69      A    C  
ANISOU 1930  CG  GLU A 260    23306  18190  24119  -6527   2098     16  A    C  
ATOM   1931  CD  GLU A 260      24.032 -33.567   7.523  1.00176.67      A    C  
ANISOU 1931  CD  GLU A 260    23393  18814  24920  -6584   2024   -174  A    C  
ATOM   1932  OE1 GLU A 260      23.636 -32.521   6.965  1.00175.78      A    O  
ANISOU 1932  OE1 GLU A 260    22904  18982  24903  -6450   2046   -284  A    O  
ATOM   1933  OE2 GLU A 260      23.697 -34.711   7.144  1.00178.47      A    O1-
ANISOU 1933  OE2 GLU A 260    23679  18847  25284  -6763   1934   -213  A    O1-
ATOM   1934  N   LEU A 261      29.107 -32.626   9.496  1.00137.22      A    N  
ANISOU 1934  N   LEU A 261    19628  13588  18923  -5726   1574    297  A    N  
ATOM   1935  CA  LEU A 261      30.185 -33.429   8.940  1.00131.54      A    C  
ANISOU 1935  CA  LEU A 261    19115  12698  18166  -5545   1256    303  A    C  
ATOM   1936  C   LEU A 261      31.207 -33.760  10.009  1.00133.75      A    C  
ANISOU 1936  C   LEU A 261    19848  12777  18195  -5500   1207    487  A    C  
ATOM   1937  O   LEU A 261      32.211 -34.408   9.732  1.00134.63      A    O  
ANISOU 1937  O   LEU A 261    20169  12732  18251  -5335    950    515  A    O  
ATOM   1938  CB  LEU A 261      30.831 -32.728   7.736  1.00125.65      A    C  
ANISOU 1938  CB  LEU A 261    18104  12167  17472  -5214   1026    177  A    C  
ATOM   1939  CG  LEU A 261      30.020 -32.735   6.428  1.00121.96      A    C  
ANISOU 1939  CG  LEU A 261    17249  11840  17253  -5220    967    -14  A    C  
ATOM   1940  CD1 LEU A 261      30.579 -31.749   5.415  1.00114.37      A    C  
ANISOU 1940  CD1 LEU A 261    16021  11134  16302  -4903    804   -116  A    C  
ATOM   1941  CD2 LEU A 261      29.963 -34.132   5.848  1.00122.39      A    C  
ANISOU 1941  CD2 LEU A 261    17428  11654  17421  -5311    800    -67  A    C  
ATOM   1942  N   TYR A 262      30.935 -33.328  11.237  1.00136.15      A    N  
ANISOU 1942  N   TYR A 262    20304  13081  18346  -5647   1452    608  A    N  
ATOM   1943  CA  TYR A 262      31.770 -33.699  12.374  1.00143.48      A    C  
ANISOU 1943  CA  TYR A 262    21693  13801  19022  -5648   1423    794  A    C  
ATOM   1944  C   TYR A 262      31.660 -35.212  12.611  1.00153.61      A    C  
ANISOU 1944  C   TYR A 262    23295  14744  20327  -5846   1374    871  A    C  
ATOM   1945  O   TYR A 262      32.363 -35.779  13.452  1.00156.40      A    O  
ANISOU 1945  O   TYR A 262    24066  14870  20489  -5851   1305   1028  A    O  
ATOM   1946  CB  TYR A 262      31.375 -32.902  13.627  1.00147.68      A    C  
ANISOU 1946  CB  TYR A 262    22321  14413  19380  -5783   1720    896  A    C  
ATOM   1947  CG  TYR A 262      32.282 -33.124  14.821  1.00160.56      A    C  
ANISOU 1947  CG  TYR A 262    24427  15857  20721  -5761   1675   1086  A    C  
ATOM   1948  CD1 TYR A 262      33.527 -32.518  14.897  1.00163.26      A    C  
ANISOU 1948  CD1 TYR A 262    24860  16263  20906  -5474   1462   1124  A    C  
ATOM   1949  CD2 TYR A 262      31.891 -33.940  15.872  1.00173.84      A    C  
ANISOU 1949  CD2 TYR A 262    26468  17298  22287  -6034   1842   1230  A    C  
ATOM   1950  CE1 TYR A 262      34.360 -32.724  15.987  1.00171.70      A    C  
ANISOU 1950  CE1 TYR A 262    26362  17164  21713  -5450   1396   1295  A    C  
ATOM   1951  CE2 TYR A 262      32.715 -34.154  16.970  1.00179.71      A    C  
ANISOU 1951  CE2 TYR A 262    27666  17864  22750  -6011   1785   1409  A    C  
ATOM   1952  CZ  TYR A 262      33.948 -33.543  17.024  1.00179.01      A    C  
ANISOU 1952  CZ  TYR A 262    27655  17848  22513  -5715   1553   1438  A    C  
ATOM   1953  OH  TYR A 262      34.767 -33.756  18.114  1.00181.20      A    O  
ANISOU 1953  OH  TYR A 262    28380  17952  22516  -5689   1474   1613  A    O  
ATOM   1954  N   GLU A 263      30.782 -35.851  11.839  1.00157.51      A    N  
ANISOU 1954  N   GLU A 263    23589  15199  21058  -6005   1396    756  A    N  
ATOM   1955  CA  GLU A 263      30.520 -37.289  11.925  1.00161.28      A    C  
ANISOU 1955  CA  GLU A 263    24324  15354  21600  -6220   1358    804  A    C  
ATOM   1956  C   GLU A 263      31.778 -38.156  11.810  1.00168.01      A    C  
ANISOU 1956  C   GLU A 263    25524  15958  22355  -6021   1039    871  A    C  
ATOM   1957  O   GLU A 263      32.064 -38.963  12.698  1.00174.22      A    O  
ANISOU 1957  O   GLU A 263    26730  16463  23002  -6138   1041   1032  A    O  
ATOM   1958  CB  GLU A 263      29.515 -37.694  10.844  1.00156.17      A    C  
ANISOU 1958  CB  GLU A 263    23340  14750  21248  -6356   1362    628  A    C  
ATOM   1959  CG  GLU A 263      29.989 -37.393   9.428  1.00148.95      A    C  
ANISOU 1959  CG  GLU A 263    22133  14000  20460  -6058   1091    452  A    C  
ATOM   1960  CD  GLU A 263      28.884 -37.515   8.403  1.00148.69      A    C  
ANISOU 1960  CD  GLU A 263    21717  14075  20705  -6190   1118    268  A    C  
ATOM   1961  OE1 GLU A 263      27.704 -37.604   8.806  1.00149.18      A    O  
ANISOU 1961  OE1 GLU A 263    21667  14141  20875  -6501   1375    269  A    O  
ATOM   1962  OE2 GLU A 263      29.196 -37.516   7.192  1.00145.90      A    O1-
ANISOU 1962  OE2 GLU A 263    21170  13805  20458  -5982    883    120  A    O1-
ATOM   1963  N   LYS A 264      32.512 -37.998  10.710  1.00163.48      A    N  
ANISOU 1963  N   LYS A 264    24774  15485  21855  -5720    769    748  A    N  
ATOM   1964  CA  LYS A 264      33.728 -38.771  10.465  1.00162.18      A    C  
ANISOU 1964  CA  LYS A 264    24884  15112  21626  -5493    459    785  A    C  
ATOM   1965  C   LYS A 264      34.705 -37.939   9.644  1.00160.18      A    C  
ANISOU 1965  C   LYS A 264    24408  15094  21359  -5115    251    692  A    C  
ATOM   1966  O   LYS A 264      34.293 -37.221   8.735  1.00155.38      A    O  
ANISOU 1966  O   LYS A 264    23407  14745  20884  -5043    272    539  A    O  
ATOM   1967  CB  LYS A 264      33.394 -40.081   9.737  1.00163.55      A    C  
ANISOU 1967  CB  LYS A 264    25120  15041  21979  -5599    333    703  A    C  
ATOM   1968  CG  LYS A 264      32.528 -41.045  10.551  1.00159.74      A    C  
ANISOU 1968  CG  LYS A 264    24903  14279  21512  -5982    518    811  A    C  
ATOM   1969  CD  LYS A 264      32.186 -42.324   9.794  1.00153.30      A    C  
ANISOU 1969  CD  LYS A 264    24146  13213  20887  -6095    383    719  A    C  
ATOM   1970  CE  LYS A 264      31.203 -43.177  10.599  1.00150.58      A    C  
ANISOU 1970  CE  LYS A 264    24023  12614  20576  -6513    603    825  A    C  
ATOM   1971  NZ  LYS A 264      31.006 -44.549  10.046  1.00145.83      A    N1+
ANISOU 1971  NZ  LYS A 264    23580  11697  20132  -6634    453    769  A    N1+
ATOM   1972  N   LEU A 265      35.998 -38.026   9.954  1.00167.71      A    N  
ANISOU 1972  N   LEU A 265    25607  15959  22156  -4876     48    785  A    N  
ATOM   1973  CA  LEU A 265      36.521 -38.912  10.992  1.00176.53      A    C  
ANISOU 1973  CA  LEU A 265    27201  16757  23116  -4941    -10    967  A    C  
ATOM   1974  C   LEU A 265      36.881 -38.144  12.267  1.00182.90      A    C  
ANISOU 1974  C   LEU A 265    28191  17622  23680  -4950    104   1133  A    C  
ATOM   1975  O   LEU A 265      37.603 -37.146  12.219  1.00178.35      A    O  
ANISOU 1975  O   LEU A 265    27481  17262  23021  -4719     33   1123  A    O  
ATOM   1976  CB  LEU A 265      37.774 -39.619  10.473  1.00175.87      A    C  
ANISOU 1976  CB  LEU A 265    27280  16514  23027  -4649   -345    958  A    C  
ATOM   1977  CG  LEU A 265      37.811 -39.948   8.978  1.00173.54      A    C  
ANISOU 1977  CG  LEU A 265    26725  16274  22940  -4492   -512    756  A    C  
ATOM   1978  CD1 LEU A 265      39.240 -39.897   8.452  1.00167.57      A    C  
ANISOU 1978  CD1 LEU A 265    25981  15547  22142  -4105   -797    730  A    C  
ATOM   1979  CD2 LEU A 265      37.161 -41.301   8.697  1.00177.34      A    C  
ANISOU 1979  CD2 LEU A 265    27365  16458  23558  -4699   -533    717  A    C  
ATOM   1980  N   GLU A 266      36.391 -38.619  13.407  1.00191.78      A    N  
ANISOU 1980  N   GLU A 266    29636  18547  24685  -5220    278   1285  A    N  
ATOM   1981  CA  GLU A 266      36.694 -37.986  14.690  1.00198.12      A    C  
ANISOU 1981  CA  GLU A 266    30667  19375  25232  -5249    389   1446  A    C  
ATOM   1982  C   GLU A 266      38.049 -38.436  15.239  1.00201.45      A    C  
ANISOU 1982  C   GLU A 266    31471  19598  25471  -5040    116   1586  A    C  
ATOM   1983  O   GLU A 266      38.606 -39.441  14.794  1.00207.36      A    O  
ANISOU 1983  O   GLU A 266    32371  20129  26289  -4930   -119   1584  A    O  
ATOM   1984  CB  GLU A 266      35.601 -38.297  15.713  1.00202.15      A    C  
ANISOU 1984  CB  GLU A 266    31379  19759  25670  -5628    706   1557  A    C  
ATOM   1985  CG  GLU A 266      34.226 -37.775  15.348  1.00200.63      A    C  
ANISOU 1985  CG  GLU A 266    30806  19774  25650  -5848   1004   1432  A    C  
ATOM   1986  CD  GLU A 266      33.134 -38.382  16.208  1.00202.80      A    C  
ANISOU 1986  CD  GLU A 266    31280  19876  25900  -6241   1302   1533  A    C  
ATOM   1987  OE1 GLU A 266      33.357 -39.477  16.770  1.00202.89      A    O  
ANISOU 1987  OE1 GLU A 266    31703  19562  25822  -6356   1240   1671  A    O  
ATOM   1988  OE2 GLU A 266      32.054 -37.767  16.319  1.00202.93      A    O1-
ANISOU 1988  OE2 GLU A 266    31038  20077  25989  -6433   1602   1475  A    O1-
ATOM   1989  N   LEU A 267      38.561 -37.688  16.214  1.00194.46      A    N  
ANISOU 1989  N   LEU A 267    30743  18787  24356  -4985    144   1704  A    N  
ATOM   1990  CA  LEU A 267      39.828 -37.993  16.874  1.00186.34      A    C  
ANISOU 1990  CA  LEU A 267    30075  17590  23135  -4797   -112   1848  A    C  
ATOM   1991  C   LEU A 267      39.928 -37.141  18.135  1.00187.60      A    C  
ANISOU 1991  C   LEU A 267    30420  17831  23029  -4861     23   1979  A    C  
ATOM   1992  O   LEU A 267      39.420 -36.020  18.159  1.00190.13      A    O  
ANISOU 1992  O   LEU A 267    30477  18420  23344  -4906    227   1910  A    O  
ATOM   1993  CB  LEU A 267      41.006 -37.668  15.950  1.00174.08      A    C  
ANISOU 1993  CB  LEU A 267    28304  16171  21668  -4419   -418   1750  A    C  
ATOM   1994  CG  LEU A 267      41.264 -38.543  14.719  1.00163.73      A    C  
ANISOU 1994  CG  LEU A 267    26869  14763  20579  -4272   -622   1627  A    C  
ATOM   1995  CD1 LEU A 267      41.991 -37.760  13.636  1.00156.81      A    C  
ANISOU 1995  CD1 LEU A 267    25607  14159  19814  -3958   -781   1478  A    C  
ATOM   1996  CD2 LEU A 267      42.028 -39.806  15.094  1.00161.62      A    C  
ANISOU 1996  CD2 LEU A 267    27020  14137  20249  -4198   -861   1748  A    C  
ATOM   1997  N   VAL A 268      40.565 -37.661  19.183  1.00183.40      A    N  
ANISOU 1997  N   VAL A 268    30350  17063  22272  -4864    -93   2164  A    N  
ATOM   1998  CA  VAL A 268      40.836 -36.848  20.375  1.00175.11      A    C  
ANISOU 1998  CA  VAL A 268    29507  16083  20943  -4887    -17   2285  A    C  
ATOM   1999  C   VAL A 268      42.261 -37.044  20.896  1.00169.21      A    C  
ANISOU 1999  C   VAL A 268    29065  15206  20023  -4642   -360   2409  A    C  
ATOM   2000  O   VAL A 268      42.579 -38.073  21.485  1.00168.06      A    O  
ANISOU 2000  O   VAL A 268    29335  14754  19768  -4682   -486   2556  A    O  
ATOM   2001  CB  VAL A 268      39.827 -37.109  21.513  1.00169.88      A    C  
ANISOU 2001  CB  VAL A 268    29156  15285  20108  -5243    304   2415  A    C  
ATOM   2002  CG1 VAL A 268      40.020 -36.084  22.627  1.00164.93      A    C  
ANISOU 2002  CG1 VAL A 268    28683  14784  19198  -5257    411   2501  A    C  
ATOM   2003  CG2 VAL A 268      38.401 -37.059  20.987  1.00165.16      A    C  
ANISOU 2003  CG2 VAL A 268    28249  14793  19711  -5496    634   2295  A    C  
ATOM   2004  N   LYS A 274      49.007 -29.140  19.134  1.00118.41      A    N  
ANISOU 2004  N   LYS A 274    20929  10482  13579  -2916  -1528   2002  A    N  
ATOM   2005  CA  LYS A 274      50.413 -29.204  19.511  1.00123.30      A    C  
ANISOU 2005  CA  LYS A 274    21678  11046  14125  -2708  -1869   2084  A    C  
ATOM   2006  C   LYS A 274      51.377 -28.941  18.326  1.00129.69      A    C  
ANISOU 2006  C   LYS A 274    22099  12020  15156  -2427  -2075   1980  A    C  
ATOM   2007  O   LYS A 274      52.135 -29.818  17.901  1.00120.69      A    O  
ANISOU 2007  O   LYS A 274    20976  10763  14118  -2247  -2308   1993  A    O  
ATOM   2008  CB  LYS A 274      50.689 -30.520  20.223  1.00136.08      A    C  
ANISOU 2008  CB  LYS A 274    23728  12344  15630  -2729  -2029   2228  A    C  
ATOM   2009  CG  LYS A 274      49.799 -30.685  21.451  1.00156.09      A    C  
ANISOU 2009  CG  LYS A 274    26659  14729  17918  -3011  -1815   2343  A    C  
ATOM   2010  CD  LYS A 274      50.347 -31.706  22.448  1.00170.70      A    C  
ANISOU 2010  CD  LYS A 274    29003  16276  19581  -3011  -2028   2522  A    C  
ATOM   2011  CE  LYS A 274      49.653 -31.589  23.805  1.00174.89      A    C  
ANISOU 2011  CE  LYS A 274    29941  16698  19811  -3274  -1829   2646  A    C  
ATOM   2012  NZ  LYS A 274      50.036 -32.675  24.751  1.00177.88      A    N1+
ANISOU 2012  NZ  LYS A 274    30831  16758  19997  -3301  -2009   2830  A    N1+
ATOM   2013  N   VAL A 275      51.342 -27.698  17.834  1.00127.84      A    N  
ANISOU 2013  N   VAL A 275    21528  12057  14989  -2391  -1980   1880  A    N  
ATOM   2014  CA  VAL A 275      52.042 -27.262  16.620  1.00119.52      A    C  
ANISOU 2014  CA  VAL A 275    20065  11202  14147  -2164  -2096   1768  A    C  
ATOM   2015  C   VAL A 275      53.492 -26.839  16.850  1.00118.79      A    C  
ANISOU 2015  C   VAL A 275    19940  11166  14029  -1956  -2393   1815  A    C  
ATOM   2016  O   VAL A 275      54.369 -27.134  16.038  1.00114.39      A    O  
ANISOU 2016  O   VAL A 275    19181  10649  13632  -1733  -2583   1773  A    O  
ATOM   2017  CB  VAL A 275      51.320 -26.051  15.974  1.00107.42      A    C  
ANISOU 2017  CB  VAL A 275    18184   9934  12695  -2226  -1853   1647  A    C  
ATOM   2018  CG1 VAL A 275      52.147 -25.473  14.834  1.00102.33      A    C  
ANISOU 2018  CG1 VAL A 275    17147   9500  12233  -1996  -1978   1552  A    C  
ATOM   2019  CG2 VAL A 275      49.933 -26.432  15.495  1.00105.13      A    C  
ANISOU 2019  CG2 VAL A 275    17830   9628  12488  -2397  -1579   1573  A    C  
ATOM   2020  N   LYS A 276      53.737 -26.118  17.940  1.00122.32      A    N  
ANISOU 2020  N   LYS A 276    20572  11623  14279  -2031  -2426   1895  A    N  
ATOM   2021  CA  LYS A 276      55.084 -25.642  18.248  1.00120.54      A    C  
ANISOU 2021  CA  LYS A 276    20317  11456  14026  -1860  -2714   1940  A    C  
ATOM   2022  C   LYS A 276      56.083 -26.798  18.371  1.00119.97      A    C  
ANISOU 2022  C   LYS A 276    20411  11191  13981  -1682  -3028   2021  A    C  
ATOM   2023  O   LYS A 276      57.247 -26.666  17.989  1.00116.52      A    O  
ANISOU 2023  O   LYS A 276    19785  10833  13656  -1464  -3271   2009  A    O  
ATOM   2024  CB  LYS A 276      55.087 -24.789  19.523  1.00120.09      A    C  
ANISOU 2024  CB  LYS A 276    20501  11404  13722  -1996  -2704   2016  A    C  
ATOM   2025  CG  LYS A 276      54.394 -23.430  19.388  1.00113.83      A    C  
ANISOU 2025  CG  LYS A 276    19503  10828  12919  -2116  -2448   1927  A    C  
ATOM   2026  CD  LYS A 276      54.662 -22.534  20.600  1.00111.03      A    C  
ANISOU 2026  CD  LYS A 276    19373  10484  12330  -2205  -2495   1990  A    C  
ATOM   2027  CE  LYS A 276      53.962 -21.178  20.465  1.00113.29      A    C  
ANISOU 2027  CE  LYS A 276    19465  10970  12610  -2313  -2239   1895  A    C  
ATOM   2028  NZ  LYS A 276      54.640 -20.061  21.212  1.00107.75      A    N1+
ANISOU 2028  NZ  LYS A 276    18825  10345  11771  -2312  -2364   1914  A    N1+
ATOM   2029  N   ASP A 277      55.615 -27.930  18.892  1.00121.55      A    N  
ANISOU 2029  N   ASP A 277    20958  11136  14088  -1775  -3016   2103  A    N  
ATOM   2030  CA  ASP A 277      56.458 -29.112  19.072  1.00125.97      A    C  
ANISOU 2030  CA  ASP A 277    21723  11475  14664  -1613  -3306   2188  A    C  
ATOM   2031  C   ASP A 277      57.036 -29.662  17.766  1.00119.66      A    C  
ANISOU 2031  C   ASP A 277    20610  10721  14134  -1371  -3422   2090  A    C  
ATOM   2032  O   ASP A 277      58.245 -29.875  17.652  1.00114.78      A    O  
ANISOU 2032  O   ASP A 277    19923  10097  13592  -1138  -3709   2111  A    O  
ATOM   2033  CB  ASP A 277      55.682 -30.227  19.784  1.00137.24      A    C  
ANISOU 2033  CB  ASP A 277    23584  12612  15950  -1785  -3227   2291  A    C  
ATOM   2034  CG  ASP A 277      55.477 -29.950  21.261  1.00145.64      A    C  
ANISOU 2034  CG  ASP A 277    25055  13571  16710  -1968  -3211   2426  A    C  
ATOM   2035  OD1 ASP A 277      55.474 -28.760  21.645  1.00151.28      A    O  
ANISOU 2035  OD1 ASP A 277    25688  14466  17326  -2033  -3141   2406  A    O  
ATOM   2036  OD2 ASP A 277      55.315 -30.923  22.035  1.00142.80      A    O1-
ANISOU 2036  OD2 ASP A 277    25111  12943  16204  -2047  -3268   2553  A    O1-
ATOM   2037  N   ARG A 278      56.171 -29.905  16.787  1.00114.07      A    N  
ANISOU 2037  N   ARG A 278    19715  10059  13569  -1424  -3199   1979  A    N  
ATOM   2038  CA  ARG A 278      56.593 -30.589  15.572  1.00111.41      A    C  
ANISOU 2038  CA  ARG A 278    19142   9727  13461  -1210  -3290   1883  A    C  
ATOM   2039  C   ARG A 278      57.569 -29.746  14.732  1.00112.62      A    C  
ANISOU 2039  C   ARG A 278    18876  10146  13770   -989  -3394   1794  A    C  
ATOM   2040  O   ARG A 278      58.362 -30.294  13.968  1.00116.96      A    O  
ANISOU 2040  O   ARG A 278    19267  10691  14481   -753  -3556   1744  A    O  
ATOM   2041  CB  ARG A 278      55.365 -31.028  14.760  1.00112.37      A    C  
ANISOU 2041  CB  ARG A 278    19183   9831  13683  -1341  -3029   1781  A    C  
ATOM   2042  CG  ARG A 278      55.547 -32.314  13.930  1.00120.45      A    C  
ANISOU 2042  CG  ARG A 278    20207  10691  14867  -1189  -3133   1726  A    C  
ATOM   2043  CD  ARG A 278      54.185 -32.876  13.487  1.00124.79      A    C  
ANISOU 2043  CD  ARG A 278    20798  11155  15463  -1390  -2886   1659  A    C  
ATOM   2044  NE  ARG A 278      54.200 -33.533  12.176  1.00125.36      A    N  
ANISOU 2044  NE  ARG A 278    20662  11229  15740  -1242  -2903   1522  A    N  
ATOM   2045  CZ  ARG A 278      54.245 -32.890  11.005  1.00125.80      A    C  
ANISOU 2045  CZ  ARG A 278    20320  11540  15941  -1133  -2831   1378  A    C  
ATOM   2046  NH1 ARG A 278      54.309 -31.564  10.962  1.00116.37      A    N1+
ANISOU 2046  NH1 ARG A 278    18880  10613  14720  -1150  -2741   1357  A    N1+
ATOM   2047  NH2 ARG A 278      54.244 -33.572   9.865  1.00127.84      A    N  
ANISOU 2047  NH2 ARG A 278    20436  11776  16361  -1002  -2852   1255  A    N  
ATOM   2048  N   LEU A 279      57.528 -28.422  14.899  1.00107.93      A    N  
ANISOU 2048  N   LEU A 279    18113   9773  13123  -1065  -3299   1777  A    N  
ATOM   2049  CA  LEU A 279      58.320 -27.506  14.070  1.00101.03      A    C  
ANISOU 2049  CA  LEU A 279    16830   9163  12395   -896  -3352   1694  A    C  
ATOM   2050  C   LEU A 279      59.575 -26.967  14.749  1.00106.72      A    C  
ANISOU 2050  C   LEU A 279    17551   9932  13066   -782  -3613   1772  A    C  
ATOM   2051  O   LEU A 279      60.327 -26.199  14.141  1.00 97.96      A    O  
ANISOU 2051  O   LEU A 279    16108   9035  12079   -649  -3671   1716  A    O  
ATOM   2052  CB  LEU A 279      57.462 -26.324  13.624  1.00101.41      A    C  
ANISOU 2052  CB  LEU A 279    16642   9439  12452  -1042  -3073   1608  A    C  
ATOM   2053  CG  LEU A 279      56.212 -26.638  12.798  1.00103.54      A    C  
ANISOU 2053  CG  LEU A 279    16824   9719  12799  -1150  -2811   1509  A    C  
ATOM   2054  CD1 LEU A 279      55.340 -25.405  12.666  1.00101.03      A    C  
ANISOU 2054  CD1 LEU A 279    16334   9599  12452  -1311  -2555   1451  A    C  
ATOM   2055  CD2 LEU A 279      56.574 -27.192  11.428  1.00 98.32      A    C  
ANISOU 2055  CD2 LEU A 279    15896   9114  12346   -944  -2858   1400  A    C  
ATOM   2056  N   LYS A 280      59.785 -27.359  16.006  1.00119.58      A    N  
ANISOU 2056  N   LYS A 280    19557  11364  14514   -843  -3769   1903  A    N  
ATOM   2057  CA  LYS A 280      60.949 -26.944  16.800  1.00119.80      A    C  
ANISOU 2057  CA  LYS A 280    19640  11406  14473   -749  -4051   1988  A    C  
ATOM   2058  C   LYS A 280      62.265 -27.031  16.031  1.00115.14      A    C  
ANISOU 2058  C   LYS A 280    18728  10922  14098   -462  -4284   1945  A    C  
ATOM   2059  O   LYS A 280      63.070 -26.095  16.047  1.00107.01      A    O  
ANISOU 2059  O   LYS A 280    17477  10071  13110   -399  -4392   1937  A    O  
ATOM   2060  CB  LYS A 280      61.095 -27.838  18.034  1.00124.29      A    C  
ANISOU 2060  CB  LYS A 280    20681  11691  14853   -784  -4242   2134  A    C  
ATOM   2061  CG  LYS A 280      60.232 -27.506  19.237  1.00120.11      A    C  
ANISOU 2061  CG  LYS A 280    20521  11068  14048  -1054  -4104   2220  A    C  
ATOM   2062  CD  LYS A 280      60.473 -28.562  20.325  1.00113.47      A    C  
ANISOU 2062  CD  LYS A 280    20153   9928  13031  -1057  -4315   2371  A    C  
ATOM   2063  CE  LYS A 280      59.402 -28.539  21.402  1.00105.90      A    C  
ANISOU 2063  CE  LYS A 280    19604   8835  11798  -1340  -4118   2455  A    C  
ATOM   2064  NZ  LYS A 280      59.290 -29.873  22.052  1.00106.12      A    N1+
ANISOU 2064  NZ  LYS A 280    20067   8546  11709  -1358  -4228   2582  A    N1+
ATOM   2065  N   ALA A 281      62.488 -28.179  15.393  1.00113.92      A    N  
ANISOU 2065  N   ALA A 281    18558  10647  14078   -292  -4360   1917  A    N  
ATOM   2066  CA  ALA A 281      63.757 -28.481  14.734  1.00110.66      A    C  
ANISOU 2066  CA  ALA A 281    17881  10297  13866      2  -4589   1881  A    C  
ATOM   2067  C   ALA A 281      64.097 -27.508  13.604  1.00111.73      A    C  
ANISOU 2067  C   ALA A 281    17532  10740  14180     86  -4476   1762  A    C  
ATOM   2068  O   ALA A 281      65.200 -26.958  13.555  1.00110.14      A    O  
ANISOU 2068  O   ALA A 281    17101  10680  14068    225  -4651   1767  A    O  
ATOM   2069  CB  ALA A 281      63.748 -29.911  14.216  1.00110.01      A    C  
ANISOU 2069  CB  ALA A 281    17898  10014  13887    154  -4645   1857  A    C  
ATOM   2070  N   TYR A 282      63.142 -27.299  12.701  1.00106.20      A    N  
ANISOU 2070  N   TYR A 282    16681  10141  13530     -2  -4189   1659  A    N  
ATOM   2071  CA  TYR A 282      63.364 -26.469  11.527  1.00 93.41      A    C  
ANISOU 2071  CA  TYR A 282    14625   8797  12069     78  -4062   1546  A    C  
ATOM   2072  C   TYR A 282      63.354 -25.001  11.892  1.00 91.75      A    C  
ANISOU 2072  C   TYR A 282    14291   8780  11789    -65  -3990   1563  A    C  
ATOM   2073  O   TYR A 282      64.208 -24.235  11.443  1.00 90.86      A    O  
ANISOU 2073  O   TYR A 282    13867   8867  11790     40  -4051   1535  A    O  
ATOM   2074  CB  TYR A 282      62.290 -26.741  10.478  1.00 93.66      A    C  
ANISOU 2074  CB  TYR A 282    14565   8860  12160     25  -3795   1433  A    C  
ATOM   2075  CG  TYR A 282      61.939 -28.200  10.344  1.00105.11      A    C  
ANISOU 2075  CG  TYR A 282    16241  10065  13629     80  -3828   1423  A    C  
ATOM   2076  CD1 TYR A 282      60.902 -28.754  11.084  1.00113.15      A    C  
ANISOU 2076  CD1 TYR A 282    17619  10871  14501   -125  -3741   1479  A    C  
ATOM   2077  CD2 TYR A 282      62.647 -29.027   9.483  1.00107.54      A    C  
ANISOU 2077  CD2 TYR A 282    16409  10348  14102    336  -3939   1355  A    C  
ATOM   2078  CE1 TYR A 282      60.577 -30.088  10.966  1.00117.15      A    C  
ANISOU 2078  CE1 TYR A 282    18343  11138  15031    -89  -3773   1474  A    C  
ATOM   2079  CE2 TYR A 282      62.329 -30.364   9.359  1.00112.84      A    C  
ANISOU 2079  CE2 TYR A 282    17303  10777  14793    388  -3976   1340  A    C  
ATOM   2080  CZ  TYR A 282      61.294 -30.888  10.103  1.00117.68      A    C  
ANISOU 2080  CZ  TYR A 282    18277  11174  15264    169  -3897   1402  A    C  
ATOM   2081  OH  TYR A 282      60.976 -32.217   9.985  1.00123.06      A    O  
ANISOU 2081  OH  TYR A 282    19188  11599  15969    206  -3936   1391  A    O  
ATOM   2082  N   VAL A 283      62.382 -24.607  12.706  1.00 97.98      A    N  
ANISOU 2082  N   VAL A 283    15328   9506  12393   -309  -3853   1608  A    N  
ATOM   2083  CA  VAL A 283      62.241 -23.207  13.088  1.00106.09      A    C  
ANISOU 2083  CA  VAL A 283    16273  10696  13340   -458  -3764   1615  A    C  
ATOM   2084  C   VAL A 283      62.833 -22.932  14.466  1.00116.60      A    C  
ANISOU 2084  C   VAL A 283    17854  11936  14512   -515  -3984   1730  A    C  
ATOM   2085  O   VAL A 283      62.355 -23.450  15.477  1.00114.58      A    O  
ANISOU 2085  O   VAL A 283    17982  11481  14074   -635  -4008   1811  A    O  
ATOM   2086  CB  VAL A 283      60.773 -22.768  13.091  1.00101.73      A    C  
ANISOU 2086  CB  VAL A 283    15804  10161  12687   -688  -3451   1576  A    C  
ATOM   2087  CG1 VAL A 283      60.686 -21.272  13.317  1.00 98.34      A    C  
ANISOU 2087  CG1 VAL A 283    15249   9912  12204   -807  -3356   1565  A    C  
ATOM   2088  CG2 VAL A 283      60.101 -23.157  11.785  1.00 98.76      A    C  
ANISOU 2088  CG2 VAL A 283    15221   9849  12453   -641  -3255   1464  A    C  
ATOM   2089  N   ARG A 284      63.868 -22.104  14.507  1.00124.23      A    N  
ANISOU 2089  N   ARG A 284    18609  13051  15543   -438  -4143   1738  A    N  
ATOM   2090  CA  ARG A 284      64.510 -21.780  15.774  1.00131.99      A    C  
ANISOU 2090  CA  ARG A 284    19808  13962  16382   -486  -4381   1838  A    C  
ATOM   2091  C   ARG A 284      63.900 -20.563  16.472  1.00132.30      A    C  
ANISOU 2091  C   ARG A 284    19954  14066  16249   -716  -4242   1845  A    C  
ATOM   2092  O   ARG A 284      63.614 -20.620  17.668  1.00134.60      A    O  
ANISOU 2092  O   ARG A 284    20613  14210  16320   -848  -4298   1923  A    O  
ATOM   2093  CB  ARG A 284      66.018 -21.624  15.589  1.00137.96      A    C  
ANISOU 2093  CB  ARG A 284    20303  14816  17297   -284  -4669   1850  A    C  
ATOM   2094  CG  ARG A 284      66.726 -22.957  15.537  1.00150.21      A    C  
ANISOU 2094  CG  ARG A 284    21920  16217  18937    -66  -4901   1886  A    C  
ATOM   2095  CD  ARG A 284      67.918 -22.935  14.617  1.00156.21      A    C  
ANISOU 2095  CD  ARG A 284    22263  17136  19954    174  -5035   1835  A    C  
ATOM   2096  NE  ARG A 284      68.243 -24.284  14.169  1.00162.49      A    N  
ANISOU 2096  NE  ARG A 284    23077  17799  20863    391  -5139   1826  A    N  
ATOM   2097  CZ  ARG A 284      69.171 -24.563  13.262  1.00164.46      A    C  
ANISOU 2097  CZ  ARG A 284    22990  18156  21343    632  -5224   1768  A    C  
ATOM   2098  NH1 ARG A 284      69.866 -23.578  12.710  1.00164.02      A    N1+
ANISOU 2098  NH1 ARG A 284    22546  18346  21428    673  -5212   1723  A    N1+
ATOM   2099  NH2 ARG A 284      69.402 -25.822  12.908  1.00163.00      A    N  
ANISOU 2099  NH2 ARG A 284    22858  17826  21247    830  -5313   1754  A    N  
ATOM   2100  N   ASP A 285      63.688 -19.477  15.731  1.00124.86      A    N  
ANISOU 2100  N   ASP A 285    18707  13334  15399   -759  -4057   1764  A    N  
ATOM   2101  CA  ASP A 285      63.125 -18.258  16.314  1.00122.97      A    C  
ANISOU 2101  CA  ASP A 285    18547  13159  15016   -961  -3919   1757  A    C  
ATOM   2102  C   ASP A 285      61.791 -18.531  17.016  1.00117.98      A    C  
ANISOU 2102  C   ASP A 285    18271  12381  14174  -1154  -3708   1776  A    C  
ATOM   2103  O   ASP A 285      60.883 -19.105  16.422  1.00117.63      A    O  
ANISOU 2103  O   ASP A 285    18216  12307  14170  -1176  -3498   1732  A    O  
ATOM   2104  CB  ASP A 285      62.964 -17.169  15.245  1.00125.72      A    C  
ANISOU 2104  CB  ASP A 285    18514  13741  15514   -966  -3723   1664  A    C  
ATOM   2105  CG  ASP A 285      62.616 -15.805  15.837  1.00128.90      A    C  
ANISOU 2105  CG  ASP A 285    18970  14213  15794  -1144  -3626   1655  A    C  
ATOM   2106  OD1 ASP A 285      61.679 -15.727  16.658  1.00129.71      A    O  
ANISOU 2106  OD1 ASP A 285    19376  14209  15698  -1310  -3494   1671  A    O  
ATOM   2107  OD2 ASP A 285      63.272 -14.803  15.474  1.00130.78      A    O1-
ANISOU 2107  OD2 ASP A 285    18947  14609  16135  -1120  -3674   1630  A    O1-
ATOM   2108  N   PRO A 286      61.675 -18.116  18.289  1.00117.08      A    N  
ANISOU 2108  N   PRO A 286    18475  12178  13834  -1299  -3763   1838  A    N  
ATOM   2109  CA  PRO A 286      60.473 -18.339  19.104  1.00116.19      A    C  
ANISOU 2109  CA  PRO A 286    18726  11924  13498  -1492  -3562   1865  A    C  
ATOM   2110  C   PRO A 286      59.298 -17.470  18.668  1.00116.54      A    C  
ANISOU 2110  C   PRO A 286    18644  12090  13547  -1632  -3210   1775  A    C  
ATOM   2111  O   PRO A 286      58.165 -17.956  18.673  1.00118.92      A    O  
ANISOU 2111  O   PRO A 286    19080  12315  13790  -1737  -2977   1762  A    O  
ATOM   2112  CB  PRO A 286      60.919 -17.931  20.516  1.00111.30      A    C  
ANISOU 2112  CB  PRO A 286    18434  11213  12643  -1580  -3751   1946  A    C  
ATOM   2113  CG  PRO A 286      62.408 -17.834  20.455  1.00111.08      A    C  
ANISOU 2113  CG  PRO A 286    18236  11238  12730  -1412  -4103   1975  A    C  
ATOM   2114  CD  PRO A 286      62.732 -17.443  19.056  1.00113.87      A    C  
ANISOU 2114  CD  PRO A 286    18106  11794  13364  -1286  -4033   1886  A    C  
ATOM   2115  N   TYR A 287      59.561 -16.207  18.322  1.00112.67      A    N  
ANISOU 2115  N   TYR A 287    17904  11778  13127  -1635  -3177   1717  A    N  
ATOM   2116  CA  TYR A 287      58.523 -15.318  17.799  1.00105.12      A    C  
ANISOU 2116  CA  TYR A 287    16792  10947  12203  -1738  -2862   1628  A    C  
ATOM   2117  C   TYR A 287      57.955 -15.892  16.496  1.00 97.09      A    C  
ANISOU 2117  C   TYR A 287    15518   9995  11377  -1661  -2693   1561  A    C  
ATOM   2118  O   TYR A 287      56.756 -15.821  16.243  1.00 95.64      A    O  
ANISOU 2118  O   TYR A 287    15332   9824  11181  -1763  -2421   1508  A    O  
ATOM   2119  CB  TYR A 287      59.058 -13.900  17.550  1.00100.71      A    C  
ANISOU 2119  CB  TYR A 287    15995  10559  11712  -1731  -2892   1584  A    C  
ATOM   2120  CG  TYR A 287      59.512 -13.125  18.777  1.00109.77      A    C  
ANISOU 2120  CG  TYR A 287    17379  11658  12672  -1827  -3035   1625  A    C  
ATOM   2121  CD1 TYR A 287      58.620 -12.787  19.793  1.00113.14      A    C  
ANISOU 2121  CD1 TYR A 287    18129  11994  12864  -2001  -2877   1628  A    C  
ATOM   2122  CD2 TYR A 287      60.832 -12.695  18.898  1.00114.59      A    C  
ANISOU 2122  CD2 TYR A 287    17877  12321  13343  -1746  -3325   1654  A    C  
ATOM   2123  CE1 TYR A 287      59.043 -12.060  20.909  1.00118.01      A    C  
ANISOU 2123  CE1 TYR A 287    18979  12565  13295  -2086  -3013   1655  A    C  
ATOM   2124  CE2 TYR A 287      61.264 -11.972  20.006  1.00115.48      A    C  
ANISOU 2124  CE2 TYR A 287    18206  12387  13284  -1839  -3477   1683  A    C  
ATOM   2125  CZ  TYR A 287      60.369 -11.658  21.008  1.00117.74      A    C  
ANISOU 2125  CZ  TYR A 287    18837  12576  13323  -2006  -3324   1682  A    C  
ATOM   2126  OH  TYR A 287      60.808 -10.941  22.102  1.00113.47      A    O  
ANISOU 2126  OH  TYR A 287    18529  11986  12599  -2095  -3481   1702  A    O  
ATOM   2127  N   ALA A 288      58.827 -16.465  15.673  1.00 89.31      A    N  
ANISOU 2127  N   ALA A 288    14313   9050  10569  -1478  -2860   1559  A    N  
ATOM   2128  CA  ALA A 288      58.401 -17.109  14.436  1.00 82.84      A    C  
ANISOU 2128  CA  ALA A 288    13274   8281   9921  -1388  -2733   1493  A    C  
ATOM   2129  C   ALA A 288      57.446 -18.273  14.706  1.00 84.33      A    C  
ANISOU 2129  C   ALA A 288    13718   8292  10033  -1466  -2622   1508  A    C  
ATOM   2130  O   ALA A 288      56.362 -18.349  14.127  1.00 89.99      A    O  
ANISOU 2130  O   ALA A 288    14358   9039  10793  -1535  -2381   1442  A    O  
ATOM   2131  CB  ALA A 288      59.606 -17.570  13.639  1.00 78.83      A    C  
ANISOU 2131  CB  ALA A 288    12526   7832   9594  -1168  -2946   1491  A    C  
ATOM   2132  N   LEU A 289      57.857 -19.177  15.587  1.00 84.89      A    N  
ANISOU 2132  N   LEU A 289    14090   8172   9993  -1458  -2806   1599  A    N  
ATOM   2133  CA  LEU A 289      57.009 -20.284  16.017  1.00 86.27      A    C  
ANISOU 2133  CA  LEU A 289    14558   8149  10072  -1555  -2714   1635  A    C  
ATOM   2134  C   LEU A 289      55.678 -19.800  16.575  1.00 92.40      A    C  
ANISOU 2134  C   LEU A 289    15493   8911  10703  -1784  -2425   1620  A    C  
ATOM   2135  O   LEU A 289      54.636 -20.382  16.300  1.00100.49      A    O  
ANISOU 2135  O   LEU A 289    16558   9877  11747  -1873  -2224   1588  A    O  
ATOM   2136  CB  LEU A 289      57.731 -21.128  17.064  1.00 88.50      A    C  
ANISOU 2136  CB  LEU A 289    15181   8224  10220  -1523  -2975   1755  A    C  
ATOM   2137  CG  LEU A 289      58.641 -22.206  16.479  1.00 99.83      A    C  
ANISOU 2137  CG  LEU A 289    16535   9589  11806  -1305  -3207   1769  A    C  
ATOM   2138  CD1 LEU A 289      59.752 -22.573  17.456  1.00107.94      A    C  
ANISOU 2138  CD1 LEU A 289    17794  10484  12732  -1222  -3538   1882  A    C  
ATOM   2139  CD2 LEU A 289      57.826 -23.431  16.087  1.00 97.09      A    C  
ANISOU 2139  CD2 LEU A 289    16299   9091  11499  -1330  -3087   1754  A    C  
ATOM   2140  N   ASP A 290      55.710 -18.731  17.358  1.00 95.73      A    N  
ANISOU 2140  N   ASP A 290    16001   9386  10986  -1879  -2402   1636  A    N  
ATOM   2141  CA  ASP A 290      54.490 -18.217  17.962  1.00101.70      A    C  
ANISOU 2141  CA  ASP A 290    16915  10131  11596  -2085  -2122   1617  A    C  
ATOM   2142  C   ASP A 290      53.488 -17.735  16.908  1.00100.61      A    C  
ANISOU 2142  C   ASP A 290    16470  10146  11612  -2115  -1845   1502  A    C  
ATOM   2143  O   ASP A 290      52.296 -18.041  16.991  1.00100.18      A    O  
ANISOU 2143  O   ASP A 290    16497  10042  11524  -2252  -1603   1477  A    O  
ATOM   2144  CB  ASP A 290      54.809 -17.093  18.950  1.00105.25      A    C  
ANISOU 2144  CB  ASP A 290    17507  10613  11872  -2160  -2166   1642  A    C  
ATOM   2145  CG  ASP A 290      53.591 -16.649  19.732  1.00110.78      A    C  
ANISOU 2145  CG  ASP A 290    18422  11278  12393  -2366  -1880   1628  A    C  
ATOM   2146  OD1 ASP A 290      52.862 -17.521  20.257  1.00110.76      A    O  
ANISOU 2146  OD1 ASP A 290    18680  11124  12279  -2479  -1763   1674  A    O  
ATOM   2147  OD2 ASP A 290      53.363 -15.426  19.818  1.00113.57      A    O1-
ANISOU 2147  OD2 ASP A 290    18682  11750  12720  -2415  -1766   1569  A    O1-
ATOM   2148  N   LEU A 291      53.972 -16.981  15.922  1.00 93.87      A    N  
ANISOU 2148  N   LEU A 291    15262   9476  10926  -1991  -1882   1435  A    N  
ATOM   2149  CA  LEU A 291      53.108 -16.474  14.860  1.00 82.92      A    C  
ANISOU 2149  CA  LEU A 291    13578   8243   9686  -1998  -1651   1330  A    C  
ATOM   2150  C   LEU A 291      52.519 -17.624  14.055  1.00 88.99      A    C  
ANISOU 2150  C   LEU A 291    14277   8960  10575  -1972  -1578   1293  A    C  
ATOM   2151  O   LEU A 291      51.325 -17.636  13.763  1.00 95.13      A    O  
ANISOU 2151  O   LEU A 291    15003   9758  11383  -2076  -1340   1233  A    O  
ATOM   2152  CB  LEU A 291      53.871 -15.531  13.932  1.00 71.17      A    C  
ANISOU 2152  CB  LEU A 291    11746   6948   8347  -1858  -1731   1282  A    C  
ATOM   2153  CG  LEU A 291      53.073 -14.988  12.747  1.00 66.73      A    C  
ANISOU 2153  CG  LEU A 291    10871   6548   7934  -1842  -1522   1180  A    C  
ATOM   2154  CD1 LEU A 291      51.790 -14.336  13.229  1.00 64.28      A    C  
ANISOU 2154  CD1 LEU A 291    10643   6244   7536  -2011  -1256   1141  A    C  
ATOM   2155  CD2 LEU A 291      53.915 -14.006  11.941  1.00 66.74      A    C  
ANISOU 2155  CD2 LEU A 291    10573   6728   8057  -1716  -1608   1152  A    C  
ATOM   2156  N   ILE A 292      53.355 -18.595  13.699  1.00 86.69      A    N  
ANISOU 2156  N   ILE A 292    13983   8598  10358  -1832  -1788   1324  A    N  
ATOM   2157  CA  ILE A 292      52.868 -19.761  12.973  1.00 85.95      A    C  
ANISOU 2157  CA  ILE A 292    13856   8430  10371  -1804  -1744   1286  A    C  
ATOM   2158  C   ILE A 292      51.724 -20.438  13.721  1.00 86.88      A    C  
ANISOU 2158  C   ILE A 292    14256   8379  10374  -2003  -1572   1315  A    C  
ATOM   2159  O   ILE A 292      50.792 -20.962  13.109  1.00 89.41      A    O  
ANISOU 2159  O   ILE A 292    14500   8687  10784  -2060  -1416   1253  A    O  
ATOM   2160  CB  ILE A 292      53.983 -20.774  12.697  1.00 86.54      A    C  
ANISOU 2160  CB  ILE A 292    13953   8414  10517  -1623  -2008   1325  A    C  
ATOM   2161  CG1 ILE A 292      55.087 -20.125  11.870  1.00 90.77      A    C  
ANISOU 2161  CG1 ILE A 292    14174   9130  11185  -1429  -2150   1290  A    C  
ATOM   2162  CG2 ILE A 292      53.445 -21.957  11.931  1.00 83.19      A    C  
ANISOU 2162  CG2 ILE A 292    13508   7900  10201  -1597  -1959   1274  A    C  
ATOM   2163  CD1 ILE A 292      56.056 -21.121  11.286  1.00 91.25      A    C  
ANISOU 2163  CD1 ILE A 292    14171   9137  11362  -1224  -2363   1292  A    C  
ATOM   2164  N   ASP A 293      51.782 -20.406  15.046  1.00 89.43      A    N  
ANISOU 2164  N   ASP A 293    14906   8578  10496  -2116  -1598   1409  A    N  
ATOM   2165  CA  ASP A 293      50.754 -21.048  15.856  1.00 98.83      A    C  
ANISOU 2165  CA  ASP A 293    16393   9603  11556  -2316  -1426   1453  A    C  
ATOM   2166  C   ASP A 293      49.448 -20.252  15.896  1.00 96.83      A    C  
ANISOU 2166  C   ASP A 293    16052   9451  11286  -2484  -1105   1383  A    C  
ATOM   2167  O   ASP A 293      48.386 -20.816  16.144  1.00100.76      A    O  
ANISOU 2167  O   ASP A 293    16672   9857  11757  -2645   -908   1382  A    O  
ATOM   2168  CB  ASP A 293      51.267 -21.317  17.277  1.00109.50      A    C  
ANISOU 2168  CB  ASP A 293    18152  10780  12674  -2378  -1562   1583  A    C  
ATOM   2169  CG  ASP A 293      50.293 -22.144  18.110  1.00122.41      A    C  
ANISOU 2169  CG  ASP A 293    20123  12220  14166  -2583  -1394   1646  A    C  
ATOM   2170  OD1 ASP A 293      49.789 -23.184  17.615  1.00124.82      A    O  
ANISOU 2170  OD1 ASP A 293    20429  12424  14572  -2610  -1341   1633  A    O  
ATOM   2171  OD2 ASP A 293      50.040 -21.750  19.270  1.00126.03      A    O1-
ANISOU 2171  OD2 ASP A 293    20857  12622  14406  -2722  -1312   1708  A    O1-
ATOM   2172  N   LYS A 294      49.516 -18.947  15.655  1.00 92.13      A    N  
ANISOU 2172  N   LYS A 294    15244   9043  10717  -2448  -1049   1325  A    N  
ATOM   2173  CA  LYS A 294      48.308 -18.130  15.700  1.00 92.04      A    C  
ANISOU 2173  CA  LYS A 294    15142   9130  10700  -2585   -752   1254  A    C  
ATOM   2174  C   LYS A 294      47.645 -18.078  14.336  1.00 91.33      A    C  
ANISOU 2174  C   LYS A 294    14692   9178  10833  -2534   -634   1141  A    C  
ATOM   2175  O   LYS A 294      46.504 -17.645  14.213  1.00 97.95      A    O  
ANISOU 2175  O   LYS A 294    15425  10085  11705  -2642   -387   1075  A    O  
ATOM   2176  CB  LYS A 294      48.610 -16.727  16.223  1.00 95.03      A    C  
ANISOU 2176  CB  LYS A 294    15513   9616  10979  -2585   -738   1248  A    C  
ATOM   2177  CG  LYS A 294      49.303 -16.746  17.573  1.00101.14      A    C  
ANISOU 2177  CG  LYS A 294    16652  10257  11519  -2632   -879   1354  A    C  
ATOM   2178  CD  LYS A 294      49.425 -15.367  18.188  1.00102.60      A    C  
ANISOU 2178  CD  LYS A 294    16867  10528  11588  -2665   -836   1335  A    C  
ATOM   2179  CE  LYS A 294      49.968 -15.472  19.608  1.00108.30      A    C  
ANISOU 2179  CE  LYS A 294    17996  11102  12050  -2735   -963   1436  A    C  
ATOM   2180  NZ  LYS A 294      50.446 -14.158  20.132  1.00111.91      A    N1+
ANISOU 2180  NZ  LYS A 294    18479  11637  12406  -2730  -1015   1418  A    N1+
ATOM   2181  N   LEU A 295      48.371 -18.532  13.318  1.00 89.12      A    N  
ANISOU 2181  N   LEU A 295    14226   8936  10700  -2365   -815   1118  A    N  
ATOM   2182  CA  LEU A 295      47.833 -18.638  11.963  1.00 86.66      A    C  
ANISOU 2182  CA  LEU A 295    13599   8740  10587  -2302   -739   1013  A    C  
ATOM   2183  C   LEU A 295      47.209 -20.007  11.755  1.00 92.41      A    C  
ANISOU 2183  C   LEU A 295    14420   9323  11370  -2373   -702   1003  A    C  
ATOM   2184  O   LEU A 295      46.152 -20.126  11.141  1.00 98.62      A    O  
ANISOU 2184  O   LEU A 295    15052  10157  12262  -2444   -533    921  A    O  
ATOM   2185  CB  LEU A 295      48.925 -18.415  10.914  1.00 75.09      A    C  
ANISOU 2185  CB  LEU A 295    11887   7398   9246  -2081   -935    984  A    C  
ATOM   2186  CG  LEU A 295      49.387 -16.989  10.616  1.00 75.63      A    C  
ANISOU 2186  CG  LEU A 295    11746   7656   9336  -2001   -943    960  A    C  
ATOM   2187  CD1 LEU A 295      50.675 -17.008   9.809  1.00 73.47      A    C  
ANISOU 2187  CD1 LEU A 295    11296   7461   9159  -1794  -1163    963  A    C  
ATOM   2188  CD2 LEU A 295      48.305 -16.219   9.885  1.00 76.03      A    C  
ANISOU 2188  CD2 LEU A 295    11554   7855   9479  -2041   -726    864  A    C  
ATOM   2189  N   LEU A 296      47.874 -21.041  12.261  1.00 88.87      A    N  
ANISOU 2189  N   LEU A 296    14223   8690  10853  -2350   -873   1088  A    N  
ATOM   2190  CA  LEU A 296      47.356 -22.400  12.163  1.00 88.08      A    C  
ANISOU 2190  CA  LEU A 296    14258   8415  10794  -2425   -856   1092  A    C  
ATOM   2191  C   LEU A 296      46.446 -22.713  13.343  1.00 92.80      A    C  
ANISOU 2191  C   LEU A 296    15153   8864  11245  -2665   -673   1158  A    C  
ATOM   2192  O   LEU A 296      46.598 -23.736  14.007  1.00 89.74      A    O  
ANISOU 2192  O   LEU A 296    15066   8262  10769  -2727   -745   1246  A    O  
ATOM   2193  CB  LEU A 296      48.496 -23.413  12.080  1.00 81.33      A    C  
ANISOU 2193  CB  LEU A 296    13533   7418   9948  -2271  -1129   1149  A    C  
ATOM   2194  CG  LEU A 296      49.314 -23.282  10.798  1.00 82.03      A    C  
ANISOU 2194  CG  LEU A 296    13318   7650  10200  -2035  -1282   1071  A    C  
ATOM   2195  CD1 LEU A 296      50.534 -24.190  10.811  1.00 82.79      A    C  
ANISOU 2195  CD1 LEU A 296    13538   7613  10304  -1864  -1554   1128  A    C  
ATOM   2196  CD2 LEU A 296      48.435 -23.559   9.588  1.00 78.67      A    C  
ANISOU 2196  CD2 LEU A 296    12654   7299   9939  -2042  -1157    946  A    C  
ATOM   2197  N   VAL A 297      45.514 -21.804  13.604  1.00 93.88      A    N  
ANISOU 2197  N   VAL A 297    15205   9112  11353  -2795   -431   1117  A    N  
ATOM   2198  CA  VAL A 297      44.489 -22.003  14.616  1.00 89.48      A    C  
ANISOU 2198  CA  VAL A 297    14878   8448  10673  -3033   -200   1160  A    C  
ATOM   2199  C   VAL A 297      43.275 -22.642  13.945  1.00 97.04      A    C  
ANISOU 2199  C   VAL A 297    15687   9394  11789  -3153    -21   1079  A    C  
ATOM   2200  O   VAL A 297      43.019 -22.394  12.768  1.00 99.99      A    O  
ANISOU 2200  O   VAL A 297    15732   9913  12346  -3065    -16    968  A    O  
ATOM   2201  CB  VAL A 297      44.097 -20.659  15.262  1.00 79.31      A    C  
ANISOU 2201  CB  VAL A 297    13568   7290   9278  -3102    -20   1145  A    C  
ATOM   2202  CG1 VAL A 297      42.765 -20.765  15.981  1.00 68.33      A    C  
ANISOU 2202  CG1 VAL A 297    12298   5844   7821  -3343    289   1146  A    C  
ATOM   2203  CG2 VAL A 297      45.195 -20.175  16.203  1.00 76.91      A    C  
ANISOU 2203  CG2 VAL A 297    13498   6947   8779  -3038   -189   1239  A    C  
ATOM   2204  N   LEU A 298      42.536 -23.467  14.681  1.00101.81      A    N  
ANISOU 2204  N   LEU A 298    16537   9824  12321  -3360    120   1136  A    N  
ATOM   2205  CA  LEU A 298      41.415 -24.201  14.098  1.00101.65      A    C  
ANISOU 2205  CA  LEU A 298    16395   9768  12459  -3495    271   1066  A    C  
ATOM   2206  C   LEU A 298      40.159 -23.345  13.924  1.00102.58      A    C  
ANISOU 2206  C   LEU A 298    16257  10058  12659  -3613    560    969  A    C  
ATOM   2207  O   LEU A 298      39.561 -23.322  12.848  1.00106.04      A    O  
ANISOU 2207  O   LEU A 298    16384  10610  13297  -3589    599    853  A    O  
ATOM   2208  CB  LEU A 298      41.112 -25.465  14.906  1.00104.72      A    C  
ANISOU 2208  CB  LEU A 298    17139   9893  12757  -3681    311   1168  A    C  
ATOM   2209  CG  LEU A 298      42.186 -26.560  14.868  1.00103.33      A    C  
ANISOU 2209  CG  LEU A 298    17190   9517  12554  -3562     20   1247  A    C  
ATOM   2210  CD1 LEU A 298      41.924 -27.616  15.937  1.00112.85      A    C  
ANISOU 2210  CD1 LEU A 298    18813  10451  13615  -3758     73   1379  A    C  
ATOM   2211  CD2 LEU A 298      42.302 -27.205  13.485  1.00 90.49      A    C  
ANISOU 2211  CD2 LEU A 298    15324   7906  11153  -3432   -121   1143  A    C  
ATOM   2212  N   ASP A 299      39.755 -22.644  14.975  1.00100.87      A    N  
ANISOU 2212  N   ASP A 299    16174   9863  12288  -3734    756   1011  A    N  
ATOM   2213  CA  ASP A 299      38.594 -21.769  14.877  1.00105.39      A    C  
ANISOU 2213  CA  ASP A 299    16504  10600  12938  -3828   1034    918  A    C  
ATOM   2214  C   ASP A 299      38.941 -20.468  14.142  1.00108.68      A    C  
ANISOU 2214  C   ASP A 299    16616  11247  13431  -3631    972    831  A    C  
ATOM   2215  O   ASP A 299      39.751 -19.675  14.620  1.00113.34      A    O  
ANISOU 2215  O   ASP A 299    17304  11875  13884  -3532    885    874  A    O  
ATOM   2216  CB  ASP A 299      38.028 -21.472  16.267  1.00107.54      A    C  
ANISOU 2216  CB  ASP A 299    17036  10813  13012  -4019   1285    985  A    C  
ATOM   2217  CG  ASP A 299      36.799 -20.582  16.220  1.00111.67      A    C  
ANISOU 2217  CG  ASP A 299    17307  11503  13621  -4110   1589    884  A    C  
ATOM   2218  OD1 ASP A 299      36.247 -20.382  15.120  1.00109.24      A    O  
ANISOU 2218  OD1 ASP A 299    16634  11332  13539  -4056   1610    769  A    O  
ATOM   2219  OD2 ASP A 299      36.382 -20.082  17.286  1.00118.33      A    O1-
ANISOU 2219  OD2 ASP A 299    18320  12338  14303  -4229   1807    918  A    O1-
ATOM   2220  N   PRO A 300      38.325 -20.254  12.968  1.00 99.64      A    N  
ANISOU 2220  N   PRO A 300    15108  10247  12504  -3579   1007    710  A    N  
ATOM   2221  CA  PRO A 300      38.470 -19.061  12.122  1.00 93.70      A    C  
ANISOU 2221  CA  PRO A 300    14040   9712  11848  -3405    969    622  A    C  
ATOM   2222  C   PRO A 300      38.235 -17.771  12.896  1.00101.07      A    C  
ANISOU 2222  C   PRO A 300    14992  10740  12671  -3425   1139    622  A    C  
ATOM   2223  O   PRO A 300      38.885 -16.763  12.630  1.00104.71      A    O  
ANISOU 2223  O   PRO A 300    15351  11317  13116  -3268   1041    607  A    O  
ATOM   2224  CB  PRO A 300      37.347 -19.218  11.102  1.00 89.04      A    C  
ANISOU 2224  CB  PRO A 300    13128   9221  11483  -3445   1077    503  A    C  
ATOM   2225  CG  PRO A 300      37.076 -20.654  11.054  1.00 88.34      A    C  
ANISOU 2225  CG  PRO A 300    13162   8962  11442  -3571   1049    523  A    C  
ATOM   2226  CD  PRO A 300      37.414 -21.246  12.378  1.00 94.58      A    C  
ANISOU 2226  CD  PRO A 300    14354   9551  12029  -3700   1078    654  A    C  
ATOM   2227  N   ALA A 301      37.298 -17.806  13.836  1.00103.32      A    N  
ANISOU 2227  N   ALA A 301    15405  10971  12882  -3621   1400    636  A    N  
ATOM   2228  CA  ALA A 301      36.999 -16.644  14.660  1.00 98.98      A    C  
ANISOU 2228  CA  ALA A 301    14903  10493  12213  -3650   1587    628  A    C  
ATOM   2229  C   ALA A 301      38.169 -16.307  15.575  1.00100.57      A    C  
ANISOU 2229  C   ALA A 301    15418  10616  12179  -3593   1443    727  A    C  
ATOM   2230  O   ALA A 301      38.317 -15.158  15.992  1.00101.68      A    O  
ANISOU 2230  O   ALA A 301    15568  10836  12230  -3542   1497    710  A    O  
ATOM   2231  CB  ALA A 301      35.740 -16.881  15.474  1.00 97.41      A    C  
ANISOU 2231  CB  ALA A 301    14782  10246  11983  -3877   1912    621  A    C  
ATOM   2232  N   GLN A 302      38.996 -17.307  15.879  1.00102.22      A    N  
ANISOU 2232  N   GLN A 302    15884  10664  12292  -3598   1250    828  A    N  
ATOM   2233  CA  GLN A 302      40.151 -17.122  16.765  1.00106.13      A    C  
ANISOU 2233  CA  GLN A 302    16689  11071  12565  -3547   1078    929  A    C  
ATOM   2234  C   GLN A 302      41.472 -17.060  16.000  1.00 99.43      A    C  
ANISOU 2234  C   GLN A 302    15741  10261  11776  -3330    748    942  A    C  
ATOM   2235  O   GLN A 302      42.537 -16.890  16.594  1.00102.34      A    O  
ANISOU 2235  O   GLN A 302    16318  10573  11994  -3264    563   1020  A    O  
ATOM   2236  CB  GLN A 302      40.216 -18.229  17.828  1.00109.33      A    C  
ANISOU 2236  CB  GLN A 302    17498  11256  12788  -3701   1086   1049  A    C  
ATOM   2237  CG  GLN A 302      39.413 -17.957  19.100  1.00111.83      A    C  
ANISOU 2237  CG  GLN A 302    18060  11520  12912  -3896   1375   1079  A    C  
ATOM   2238  CD  GLN A 302      39.074 -19.231  19.865  1.00116.15      A    C  
ANISOU 2238  CD  GLN A 302    18932  11858  13344  -4088   1453   1182  A    C  
ATOM   2239  NE2 GLN A 302      37.953 -19.851  19.515  1.00115.50      A    N  
ANISOU 2239  NE2 GLN A 302    18712  11764  13408  -4233   1662   1139  A    N  
ATOM   2240  OE1 GLN A 302      39.816 -19.656  20.750  1.00120.15      A    O  
ANISOU 2240  OE1 GLN A 302    19809  12209  13633  -4108   1319   1301  A    O  
ATOM   2241  N   ARG A 303      41.405 -17.201  14.682  1.00 89.18      A    N  
ANISOU 2241  N   ARG A 303    14124   9064  10698  -3221    675    865  A    N  
ATOM   2242  CA  ARG A 303      42.606 -17.122  13.861  1.00 86.80      A    C  
ANISOU 2242  CA  ARG A 303    13695   8818  10466  -3013    394    869  A    C  
ATOM   2243  C   ARG A 303      43.065 -15.673  13.710  1.00 87.05      A    C  
ANISOU 2243  C   ARG A 303    13576   9008  10489  -2895    365    835  A    C  
ATOM   2244  O   ARG A 303      42.253 -14.773  13.482  1.00 85.57      A    O  
ANISOU 2244  O   ARG A 303    13202   8945  10364  -2916    550    757  A    O  
ATOM   2245  CB  ARG A 303      42.357 -17.745  12.489  1.00 85.57      A    C  
ANISOU 2245  CB  ARG A 303    13265   8718  10530  -2936    337    792  A    C  
ATOM   2246  CG  ARG A 303      43.610 -17.977  11.652  1.00 85.15      A    C  
ANISOU 2246  CG  ARG A 303    13118   8691  10542  -2729     54    802  A    C  
ATOM   2247  CD  ARG A 303      43.272 -18.801  10.422  1.00 82.21      A    C  
ANISOU 2247  CD  ARG A 303    12543   8337  10356  -2678     14    725  A    C  
ATOM   2248  NE  ARG A 303      42.537 -19.993  10.822  1.00 89.20      A    N  
ANISOU 2248  NE  ARG A 303    13604   9051  11236  -2846    101    744  A    N  
ATOM   2249  CZ  ARG A 303      41.634 -20.611  10.074  1.00 85.98      A    C  
ANISOU 2249  CZ  ARG A 303    13046   8645  10977  -2909    182    664  A    C  
ATOM   2250  NH1 ARG A 303      41.336 -20.154   8.867  1.00 90.47      A    N1+
ANISOU 2250  NH1 ARG A 303    13287   9383  11702  -2808    182    556  A    N1+
ATOM   2251  NH2 ARG A 303      41.025 -21.684  10.545  1.00 77.72      A    N  
ANISOU 2251  NH2 ARG A 303    12186   7425   9919  -3080    259    693  A    N  
ATOM   2252  N   ILE A 304      44.371 -15.461  13.833  1.00 86.10      A    N  
ANISOU 2252  N   ILE A 304    13534   8878  10301  -2772    126    895  A    N  
ATOM   2253  CA  ILE A 304      44.957 -14.132  13.704  1.00 86.34      A    C  
ANISOU 2253  CA  ILE A 304    13441   9041  10325  -2667     68    874  A    C  
ATOM   2254  C   ILE A 304      44.738 -13.551  12.307  1.00 82.20      A    C  
ANISOU 2254  C   ILE A 304    12533   8696  10005  -2544     84    781  A    C  
ATOM   2255  O   ILE A 304      44.768 -14.274  11.308  1.00 80.31      A    O  
ANISOU 2255  O   ILE A 304    12132   8479   9903  -2471      9    751  A    O  
ATOM   2256  CB  ILE A 304      46.466 -14.144  14.043  1.00 78.01      A    C  
ANISOU 2256  CB  ILE A 304    12523   7937   9182  -2562   -216    958  A    C  
ATOM   2257  CG1 ILE A 304      46.961 -12.725  14.310  1.00 66.15      A    C  
ANISOU 2257  CG1 ILE A 304    10979   6531   7624  -2517   -243    949  A    C  
ATOM   2258  CG2 ILE A 304      47.264 -14.804  12.933  1.00 79.84      A    C  
ANISOU 2258  CG2 ILE A 304    12570   8202   9565  -2401   -424    955  A    C  
ATOM   2259  CD1 ILE A 304      48.381 -12.668  14.816  1.00 60.22      A    C  
ANISOU 2259  CD1 ILE A 304    10375   5729   6777  -2444   -514   1031  A    C  
ATOM   2260  N   ASP A 305      44.499 -12.245  12.242  1.00 77.01      A    N  
ANISOU 2260  N   ASP A 305    11746   8157   9357  -2521    182    735  A    N  
ATOM   2261  CA  ASP A 305      44.254 -11.595  10.958  1.00 76.35      A    C  
ANISOU 2261  CA  ASP A 305    11319   8241   9450  -2406    202    655  A    C  
ATOM   2262  C   ASP A 305      45.505 -10.878  10.413  1.00 80.50      A    C  
ANISOU 2262  C   ASP A 305    11729   8855  10004  -2248     -1    680  A    C  
ATOM   2263  O   ASP A 305      46.515 -10.756  11.116  1.00 89.51      A    O  
ANISOU 2263  O   ASP A 305    13044   9933  11031  -2237   -149    751  A    O  
ATOM   2264  CB  ASP A 305      43.020 -10.676  11.032  1.00 74.68      A    C  
ANISOU 2264  CB  ASP A 305    10996   8108   9272  -2471    455    578  A    C  
ATOM   2265  CG  ASP A 305      43.244  -9.430  11.882  1.00 93.03      A    C  
ANISOU 2265  CG  ASP A 305    13437  10440  11472  -2487    505    590  A    C  
ATOM   2266  OD1 ASP A 305      44.411  -9.080  12.152  1.00104.11      A    O  
ANISOU 2266  OD1 ASP A 305    14937  11824  12797  -2427    321    649  A    O  
ATOM   2267  OD2 ASP A 305      42.243  -8.783  12.271  1.00 92.00      A    O1-
ANISOU 2267  OD2 ASP A 305    13294  10334  11329  -2558    728    535  A    O1-
ATOM   2268  N   SER A 306      45.448 -10.435   9.159  1.00 69.72      A    N  
ANISOU 2268  N   SER A 306    10071   7632   8789  -2131    -13    624  A    N  
ATOM   2269  CA  SER A 306      46.572  -9.726   8.533  1.00 72.24      A    C  
ANISOU 2269  CA  SER A 306    10253   8046   9148  -1990   -178    648  A    C  
ATOM   2270  C   SER A 306      47.131  -8.576   9.365  1.00 74.58      A    C  
ANISOU 2270  C   SER A 306    10662   8336   9338  -2013   -202    687  A    C  
ATOM   2271  O   SER A 306      48.349  -8.421   9.478  1.00 68.09      A    O  
ANISOU 2271  O   SER A 306     9875   7510   8486  -1952   -390    746  A    O  
ATOM   2272  CB  SER A 306      46.176  -9.178   7.159  1.00 73.95      A    C  
ANISOU 2272  CB  SER A 306    10160   8420   9516  -1885   -131    580  A    C  
ATOM   2273  OG  SER A 306      46.416 -10.130   6.146  1.00 82.59      A    O  
ANISOU 2273  OG  SER A 306    11130   9544  10706  -1795   -229    562  A    O  
ATOM   2274  N   ASP A 307      46.233  -7.756   9.910  1.00 76.35      A    N  
ANISOU 2274  N   ASP A 307    10931   8562   9516  -2097    -14    647  A    N  
ATOM   2275  CA  ASP A 307      46.621  -6.595  10.702  1.00 75.62      A    C  
ANISOU 2275  CA  ASP A 307    10957   8455   9321  -2125    -17    666  A    C  
ATOM   2276  C   ASP A 307      47.407  -7.015  11.937  1.00 79.53      A    C  
ANISOU 2276  C   ASP A 307    11759   8816   9643  -2198   -143    741  A    C  
ATOM   2277  O   ASP A 307      48.547  -6.599  12.128  1.00 85.45      A    O  
ANISOU 2277  O   ASP A 307    12548   9563  10356  -2154   -328    791  A    O  
ATOM   2278  CB  ASP A 307      45.386  -5.791  11.112  1.00 80.92      A    C  
ANISOU 2278  CB  ASP A 307    11640   9135   9970  -2200    231    597  A    C  
ATOM   2279  CG  ASP A 307      45.665  -4.298  11.213  1.00 96.66      A    C  
ANISOU 2279  CG  ASP A 307    13604  11172  11948  -2164    236    583  A    C  
ATOM   2280  OD1 ASP A 307      46.293  -3.726  10.281  1.00 97.08      A    O  
ANISOU 2280  OD1 ASP A 307    13462  11320  12106  -2054    124    593  A    O  
ATOM   2281  OD2 ASP A 307      45.242  -3.700  12.229  1.00102.38      A    O1-
ANISOU 2281  OD2 ASP A 307    14514  11834  12554  -2248    359    561  A    O1-
ATOM   2282  N   ASP A 308      46.805  -7.856  12.767  1.00 77.19      A    N  
ANISOU 2282  N   ASP A 308    11681   8407   9243  -2312    -49    753  A    N  
ATOM   2283  CA  ASP A 308      47.451  -8.269  14.001  1.00 82.02      A    C  
ANISOU 2283  CA  ASP A 308    12617   8880   9667  -2387   -162    828  A    C  
ATOM   2284  C   ASP A 308      48.707  -9.089  13.740  1.00 74.87      A    C  
ANISOU 2284  C   ASP A 308    11719   7942   8787  -2298   -438    901  A    C  
ATOM   2285  O   ASP A 308      49.607  -9.127  14.569  1.00 84.59      A    O  
ANISOU 2285  O   ASP A 308    13157   9092   9891  -2312   -610    968  A    O  
ATOM   2286  CB  ASP A 308      46.469  -9.030  14.895  1.00 91.98      A    C  
ANISOU 2286  CB  ASP A 308    14114  10024  10808  -2535     19    832  A    C  
ATOM   2287  CG  ASP A 308      45.355  -8.139  15.429  1.00 96.75      A    C  
ANISOU 2287  CG  ASP A 308    14757  10648  11354  -2627    291    764  A    C  
ATOM   2288  OD1 ASP A 308      45.619  -6.943  15.676  1.00 96.55      A    O  
ANISOU 2288  OD1 ASP A 308    14736  10662  11285  -2602    288    740  A    O  
ATOM   2289  OD2 ASP A 308      44.219  -8.632  15.606  1.00 97.71      A    O1-
ANISOU 2289  OD2 ASP A 308    14903  10744  11479  -2724    510    731  A    O1-
ATOM   2290  N   ALA A 309      48.770  -9.737  12.586  1.00 73.23      A    N  
ANISOU 2290  N   ALA A 309    11285   7798   8742  -2200   -485    884  A    N  
ATOM   2291  CA  ALA A 309      49.934 -10.548  12.236  1.00 75.57      A    C  
ANISOU 2291  CA  ALA A 309    11561   8071   9083  -2094   -732    940  A    C  
ATOM   2292  C   ALA A 309      51.120  -9.664  11.872  1.00 81.08      A    C  
ANISOU 2292  C   ALA A 309    12110   8864   9832  -1988   -906    961  A    C  
ATOM   2293  O   ALA A 309      52.250  -9.931  12.268  1.00 88.86      A    O  
ANISOU 2293  O   ALA A 309    13185   9801  10776  -1945  -1126   1026  A    O  
ATOM   2294  CB  ALA A 309      49.603 -11.491  11.096  1.00 66.96      A    C  
ANISOU 2294  CB  ALA A 309    10281   7017   8144  -2020   -716    902  A    C  
ATOM   2295  N   LEU A 310      50.852  -8.609  11.111  1.00 77.64      A    N  
ANISOU 2295  N   LEU A 310    11444   8564   9493  -1947   -810    907  A    N  
ATOM   2296  CA  LEU A 310      51.872  -7.632  10.747  1.00 69.62      A    C  
ANISOU 2296  CA  LEU A 310    10282   7641   8531  -1870   -941    927  A    C  
ATOM   2297  C   LEU A 310      52.407  -6.909  11.990  1.00 75.10      A    C  
ANISOU 2297  C   LEU A 310    11201   8258   9076  -1954  -1025    967  A    C  
ATOM   2298  O   LEU A 310      53.498  -6.328  11.969  1.00 72.99      A    O  
ANISOU 2298  O   LEU A 310    10871   8029   8833  -1911  -1196   1003  A    O  
ATOM   2299  CB  LEU A 310      51.305  -6.629   9.730  1.00 57.72      A    C  
ANISOU 2299  CB  LEU A 310     8516   6272   7140  -1825   -796    865  A    C  
ATOM   2300  CG  LEU A 310      51.346  -7.086   8.269  1.00 58.01      A    C  
ANISOU 2300  CG  LEU A 310     8279   6424   7338  -1697   -804    838  A    C  
ATOM   2301  CD1 LEU A 310      50.616  -6.124   7.345  1.00 55.37      A    C  
ANISOU 2301  CD1 LEU A 310     7730   6213   7096  -1662   -652    780  A    C  
ATOM   2302  CD2 LEU A 310      52.782  -7.262   7.831  1.00 55.93      A    C  
ANISOU 2302  CD2 LEU A 310     7909   6207   7135  -1587  -1019    891  A    C  
ATOM   2303  N   ASN A 311      51.627  -6.960  13.069  1.00 75.13      A    N  
ANISOU 2303  N   ASN A 311    11466   8154   8924  -2081   -903    959  A    N  
ATOM   2304  CA  ASN A 311      51.976  -6.301  14.317  1.00 70.96      A    C  
ANISOU 2304  CA  ASN A 311    11195   7543   8225  -2172   -961    985  A    C  
ATOM   2305  C   ASN A 311      52.640  -7.234  15.326  1.00 80.02      A    C  
ANISOU 2305  C   ASN A 311    12624   8553   9227  -2209  -1146   1062  A    C  
ATOM   2306  O   ASN A 311      53.159  -6.791  16.353  1.00 86.09      A    O  
ANISOU 2306  O   ASN A 311    13615   9249   9845  -2271  -1257   1093  A    O  
ATOM   2307  CB  ASN A 311      50.746  -5.671  14.955  1.00 69.58      A    C  
ANISOU 2307  CB  ASN A 311    11158   7334   7945  -2284   -704    925  A    C  
ATOM   2308  CG  ASN A 311      51.086  -4.940  16.232  1.00 81.38      A    C  
ANISOU 2308  CG  ASN A 311    12935   8740   9248  -2375   -758    939  A    C  
ATOM   2309  ND2 ASN A 311      50.594  -5.453  17.364  1.00 81.31      A    N  
ANISOU 2309  ND2 ASN A 311    13242   8608   9045  -2485   -680    954  A    N  
ATOM   2310  OD1 ASN A 311      51.814  -3.940  16.209  1.00 76.51      A    O  
ANISOU 2310  OD1 ASN A 311    12261   8160   8649  -2351   -873    937  A    O  
ATOM   2311  N   HIS A 312      52.611  -8.527  15.028  1.00 81.20      A    N  
ANISOU 2311  N   HIS A 312    12775   8660   9418  -2169  -1185   1091  A    N  
ATOM   2312  CA  HIS A 312      53.229  -9.531  15.878  1.00 85.76      A    C  
ANISOU 2312  CA  HIS A 312    13614   9098   9873  -2186  -1371   1172  A    C  
ATOM   2313  C   HIS A 312      54.710  -9.236  16.078  1.00 85.81      A    C  
ANISOU 2313  C   HIS A 312    13604   9114   9885  -2112  -1671   1227  A    C  
ATOM   2314  O   HIS A 312      55.375  -8.747  15.167  1.00 79.14      A    O  
ANISOU 2314  O   HIS A 312    12470   8395   9204  -2009  -1752   1211  A    O  
ATOM   2315  CB  HIS A 312      53.051 -10.915  15.262  1.00 86.93      A    C  
ANISOU 2315  CB  HIS A 312    13709   9209  10114  -2125  -1380   1187  A    C  
ATOM   2316  CG  HIS A 312      53.509 -12.029  16.145  1.00 86.69      A    C  
ANISOU 2316  CG  HIS A 312    13974   9011   9953  -2146  -1546   1272  A    C  
ATOM   2317  CD2 HIS A 312      52.827 -12.825  17.000  1.00 89.99      A    C  
ANISOU 2317  CD2 HIS A 312    14697   9277  10218  -2261  -1457   1310  A    C  
ATOM   2318  ND1 HIS A 312      54.826 -12.428  16.213  1.00 87.44      A    N  
ANISOU 2318  ND1 HIS A 312    14074   9078  10072  -2037  -1843   1336  A    N  
ATOM   2319  CE1 HIS A 312      54.935 -13.425  17.072  1.00 93.43      A    C  
ANISOU 2319  CE1 HIS A 312    15137   9668  10694  -2075  -1943   1411  A    C  
ATOM   2320  NE2 HIS A 312      53.735 -13.688  17.562  1.00 94.43      A    N  
ANISOU 2320  NE2 HIS A 312    15459   9714  10705  -2216  -1709   1400  A    N  
ATOM   2321  N   ASP A 313      55.229  -9.542  17.265  1.00 93.38      A    N  
ANISOU 2321  N   ASP A 313    14871   9944  10666  -2166  -1836   1294  A    N  
ATOM   2322  CA  ASP A 313      56.604  -9.175  17.591  1.00101.16      A    C  
ANISOU 2322  CA  ASP A 313    15852  10936  11648  -2113  -2133   1341  A    C  
ATOM   2323  C   ASP A 313      57.623  -9.812  16.640  1.00 91.98      A    C  
ANISOU 2323  C   ASP A 313    14421   9840  10686  -1947  -2332   1369  A    C  
ATOM   2324  O   ASP A 313      58.762  -9.364  16.551  1.00 87.15      A    O  
ANISOU 2324  O   ASP A 313    13678   9287  10146  -1884  -2547   1392  A    O  
ATOM   2325  CB  ASP A 313      56.924  -9.479  19.060  1.00116.29      A    C  
ANISOU 2325  CB  ASP A 313    18173  12692  13322  -2199  -2289   1409  A    C  
ATOM   2326  CG  ASP A 313      56.167  -8.569  20.024  1.00124.49      A    C  
ANISOU 2326  CG  ASP A 313    19461  13684  14156  -2352  -2120   1372  A    C  
ATOM   2327  OD1 ASP A 313      55.810  -7.438  19.626  1.00125.40      A    O  
ANISOU 2327  OD1 ASP A 313    19411  13899  14337  -2374  -1973   1299  A    O  
ATOM   2328  OD2 ASP A 313      55.933  -8.986  21.182  1.00126.99      A    O1-
ANISOU 2328  OD2 ASP A 313    20151  13860  14241  -2447  -2132   1415  A    O1-
ATOM   2329  N   PHE A 314      57.201 -10.840  15.914  1.00 92.59      A    N  
ANISOU 2329  N   PHE A 314    14409   9912  10858  -1879  -2251   1361  A    N  
ATOM   2330  CA  PHE A 314      58.054 -11.474  14.912  1.00 91.77      A    C  
ANISOU 2330  CA  PHE A 314    14043   9877  10947  -1708  -2400   1370  A    C  
ATOM   2331  C   PHE A 314      58.644 -10.448  13.937  1.00 86.07      A    C  
ANISOU 2331  C   PHE A 314    12965   9339  10398  -1633  -2410   1332  A    C  
ATOM   2332  O   PHE A 314      59.802 -10.560  13.531  1.00 84.06      A    O  
ANISOU 2332  O   PHE A 314    12530   9146  10264  -1514  -2610   1359  A    O  
ATOM   2333  CB  PHE A 314      57.269 -12.560  14.163  1.00 96.44      A    C  
ANISOU 2333  CB  PHE A 314    14585  10444  11615  -1664  -2256   1340  A    C  
ATOM   2334  CG  PHE A 314      57.989 -13.135  12.963  1.00101.92      A    C  
ANISOU 2334  CG  PHE A 314    14989  11224  12511  -1481  -2357   1324  A    C  
ATOM   2335  CD1 PHE A 314      59.031 -14.030  13.121  1.00102.41      A    C  
ANISOU 2335  CD1 PHE A 314    15091  11216  12606  -1362  -2609   1381  A    C  
ATOM   2336  CD2 PHE A 314      57.596 -12.802  11.674  1.00100.71      A    C  
ANISOU 2336  CD2 PHE A 314    14534  11220  12510  -1421  -2197   1251  A    C  
ATOM   2337  CE1 PHE A 314      59.680 -14.566  12.017  1.00 99.52      A    C  
ANISOU 2337  CE1 PHE A 314    14459  10929  12424  -1184  -2684   1357  A    C  
ATOM   2338  CE2 PHE A 314      58.246 -13.331  10.573  1.00 93.72      A    C  
ANISOU 2338  CE2 PHE A 314    13401  10417  11793  -1251  -2275   1230  A    C  
ATOM   2339  CZ  PHE A 314      59.286 -14.214  10.745  1.00 91.74      A    C  
ANISOU 2339  CZ  PHE A 314    13184  10096  11575  -1132  -2510   1280  A    C  
ATOM   2340  N   PHE A 315      57.853  -9.440  13.581  1.00 84.06      A    N  
ANISOU 2340  N   PHE A 315    12611   9171  10156  -1702  -2191   1272  A    N  
ATOM   2341  CA  PHE A 315      58.271  -8.449  12.587  1.00 79.12      A    C  
ANISOU 2341  CA  PHE A 315    11661   8712   9688  -1641  -2167   1240  A    C  
ATOM   2342  C   PHE A 315      58.969  -7.246  13.203  1.00 83.45      A    C  
ANISOU 2342  C   PHE A 315    12234   9278  10193  -1709  -2282   1260  A    C  
ATOM   2343  O   PHE A 315      59.455  -6.380  12.482  1.00 80.98      A    O  
ANISOU 2343  O   PHE A 315    11670   9090  10007  -1673  -2287   1248  A    O  
ATOM   2344  CB  PHE A 315      57.066  -7.960  11.784  1.00 75.37      A    C  
ANISOU 2344  CB  PHE A 315    11052   8319   9264  -1666  -1886   1167  A    C  
ATOM   2345  CG  PHE A 315      56.413  -9.026  10.959  1.00 73.93      A    C  
ANISOU 2345  CG  PHE A 315    10787   8146   9158  -1596  -1778   1134  A    C  
ATOM   2346  CD1 PHE A 315      55.257  -9.645  11.394  1.00 65.51      A    C  
ANISOU 2346  CD1 PHE A 315     9913   6979   7998  -1683  -1624   1112  A    C  
ATOM   2347  CD2 PHE A 315      56.954  -9.404   9.745  1.00 74.95      A    C  
ANISOU 2347  CD2 PHE A 315    10645   8382   9451  -1449  -1827   1122  A    C  
ATOM   2348  CE1 PHE A 315      54.662 -10.623  10.637  1.00 65.71      A    C  
ANISOU 2348  CE1 PHE A 315     9862   7004   8100  -1631  -1538   1077  A    C  
ATOM   2349  CE2 PHE A 315      56.364 -10.380   8.987  1.00 71.15      A    C  
ANISOU 2349  CE2 PHE A 315    10101   7900   9031  -1386  -1740   1081  A    C  
ATOM   2350  CZ  PHE A 315      55.214 -10.990   9.436  1.00 72.50      A    C  
ANISOU 2350  CZ  PHE A 315    10466   7963   9116  -1481  -1603   1058  A    C  
ATOM   2351  N   TRP A 316      59.010  -7.202  14.534  1.00 94.10      A    N  
ANISOU 2351  N   TRP A 316    13898  10498  11358  -1813  -2375   1291  A    N  
ATOM   2352  CA  TRP A 316      59.476  -6.028  15.274  1.00 91.45      A    C  
ANISOU 2352  CA  TRP A 316    13650  10153  10945  -1905  -2468   1295  A    C  
ATOM   2353  C   TRP A 316      60.535  -6.367  16.328  1.00 99.38      A    C  
ANISOU 2353  C   TRP A 316    14851  11060  11849  -1918  -2774   1361  A    C  
ATOM   2354  O   TRP A 316      60.623  -5.728  17.379  1.00 99.17      A    O  
ANISOU 2354  O   TRP A 316    15059  10957  11664  -2028  -2846   1364  A    O  
ATOM   2355  CB  TRP A 316      58.280  -5.313  15.914  1.00 82.32      A    C  
ANISOU 2355  CB  TRP A 316    12709   8938   9631  -2041  -2238   1243  A    C  
ATOM   2356  CG  TRP A 316      57.297  -4.887  14.895  1.00 79.96      A    C  
ANISOU 2356  CG  TRP A 316    12200   8738   9442  -2021  -1967   1178  A    C  
ATOM   2357  CD1 TRP A 316      56.146  -5.531  14.542  1.00 78.69      A    C  
ANISOU 2357  CD1 TRP A 316    12047   8569   9281  -2018  -1749   1143  A    C  
ATOM   2358  CD2 TRP A 316      57.396  -3.745  14.038  1.00 80.93      A    C  
ANISOU 2358  CD2 TRP A 316    12064   8984   9702  -1997  -1898   1144  A    C  
ATOM   2359  CE2 TRP A 316      56.261  -3.749  13.205  1.00 72.91      A    C  
ANISOU 2359  CE2 TRP A 316    10917   8029   8754  -1970  -1643   1089  A    C  
ATOM   2360  CE3 TRP A 316      58.330  -2.713  13.902  1.00 77.65      A    C  
ANISOU 2360  CE3 TRP A 316    11518   8626   9359  -2002  -2030   1158  A    C  
ATOM   2361  NE1 TRP A 316      55.513  -4.849  13.535  1.00 71.65      A    N  
ANISOU 2361  NE1 TRP A 316    10916   7792   8515  -1987  -1559   1085  A    N  
ATOM   2362  CZ2 TRP A 316      56.033  -2.759  12.251  1.00 68.37      A    C  
ANISOU 2362  CZ2 TRP A 316    10103   7568   8305  -1937  -1524   1053  A    C  
ATOM   2363  CZ3 TRP A 316      58.100  -1.731  12.959  1.00 76.02      A    C  
ANISOU 2363  CZ3 TRP A 316    11078   8526   9279  -1981  -1896   1124  A    C  
ATOM   2364  CH2 TRP A 316      56.962  -1.761  12.143  1.00 73.96      A    C  
ANISOU 2364  CH2 TRP A 316    10707   8322   9073  -1943  -1649   1075  A    C  
ATOM   2365  N   SER A 317      61.341  -7.378  16.029  1.00105.35      A    N  
ANISOU 2365  N   SER A 317    15511  11818  12700  -1795  -2960   1409  A    N  
ATOM   2366  CA  SER A 317      62.436  -7.787  16.896  1.00106.28      A    C  
ANISOU 2366  CA  SER A 317    15771  11855  12757  -1775  -3281   1476  A    C  
ATOM   2367  C   SER A 317      63.608  -8.198  16.012  1.00112.74      A    C  
ANISOU 2367  C   SER A 317    16255  12777  13803  -1612  -3463   1501  A    C  
ATOM   2368  O   SER A 317      63.419  -8.492  14.832  1.00117.03      A    O  
ANISOU 2368  O   SER A 317    16537  13421  14507  -1512  -3324   1472  A    O  
ATOM   2369  CB  SER A 317      61.996  -8.950  17.773  1.00100.09      A    C  
ANISOU 2369  CB  SER A 317    15339  10901  11790  -1793  -3315   1521  A    C  
ATOM   2370  OG  SER A 317      61.451  -9.981  16.975  1.00101.27      A    O  
ANISOU 2370  OG  SER A 317    15397  11053  12029  -1704  -3178   1512  A    O  
ATOM   2371  N   ASP A 318      64.818  -8.211  16.563  1.00111.00      A    N  
ANISOU 2371  N   ASP A 318    16037  12538  13600  -1582  -3772   1551  A    N  
ATOM   2372  CA  ASP A 318      65.989  -8.510  15.743  1.00110.71      A    C  
ANISOU 2372  CA  ASP A 318    15654  12614  13795  -1426  -3939   1570  A    C  
ATOM   2373  C   ASP A 318      66.133 -10.009  15.488  1.00106.07      A    C  
ANISOU 2373  C   ASP A 318    15080  11967  13253  -1268  -4011   1599  A    C  
ATOM   2374  O   ASP A 318      65.761 -10.822  16.328  1.00 98.23      A    O  
ANISOU 2374  O   ASP A 318    14414  10813  12094  -1289  -4071   1636  A    O  
ATOM   2375  CB  ASP A 318      67.262  -7.904  16.346  1.00115.93      A    C  
ANISOU 2375  CB  ASP A 318    16259  13295  14494  -1450  -4245   1606  A    C  
ATOM   2376  CG  ASP A 318      67.330  -6.383  16.165  1.00119.19      A    C  
ANISOU 2376  CG  ASP A 318    16529  13805  14952  -1574  -4167   1569  A    C  
ATOM   2377  OD1 ASP A 318      67.201  -5.901  15.013  1.00113.50      A    O  
ANISOU 2377  OD1 ASP A 318    15507  13224  14393  -1541  -3977   1535  A    O  
ATOM   2378  OD2 ASP A 318      67.515  -5.668  17.177  1.00118.79      A    O1-
ANISOU 2378  OD2 ASP A 318    16682  13684  14769  -1705  -4300   1574  A    O1-
ATOM   2379  N   PRO A 319      66.617 -10.379  14.293  1.00110.14      A    N  
ANISOU 2379  N   PRO A 319    15252  12606  13989  -1111  -3987   1581  A    N  
ATOM   2380  CA  PRO A 319      66.964  -9.468  13.191  1.00106.15      A    C  
ANISOU 2380  CA  PRO A 319    14366  12294  13672  -1088  -3876   1542  A    C  
ATOM   2381  C   PRO A 319      65.717  -8.832  12.587  1.00100.24      A    C  
ANISOU 2381  C   PRO A 319    13604  11597  12886  -1176  -3544   1484  A    C  
ATOM   2382  O   PRO A 319      64.676  -9.477  12.520  1.00107.30      A    O  
ANISOU 2382  O   PRO A 319    14657  12419  13694  -1181  -3378   1460  A    O  
ATOM   2383  CB  PRO A 319      67.615 -10.394  12.151  1.00108.88      A    C  
ANISOU 2383  CB  PRO A 319    14431  12722  14215   -877  -3915   1536  A    C  
ATOM   2384  CG  PRO A 319      67.837 -11.716  12.852  1.00111.85      A    C  
ANISOU 2384  CG  PRO A 319    15038  12937  14522   -786  -4113   1579  A    C  
ATOM   2385  CD  PRO A 319      66.807 -11.792  13.927  1.00108.40      A    C  
ANISOU 2385  CD  PRO A 319    15020  12332  13836   -941  -4054   1595  A    C  
ATOM   2386  N   MET A 320      65.816  -7.585  12.153  1.00 97.46      A    N  
ANISOU 2386  N   MET A 320    13064  11364  12604  -1246  -3454   1463  A    N  
ATOM   2387  CA  MET A 320      64.685  -6.925  11.509  1.00 96.21      A    C  
ANISOU 2387  CA  MET A 320    12869  11260  12427  -1311  -3154   1409  A    C  
ATOM   2388  C   MET A 320      64.541  -7.413  10.076  1.00 99.72      A    C  
ANISOU 2388  C   MET A 320    13039  11826  13024  -1169  -3002   1376  A    C  
ATOM   2389  O   MET A 320      65.507  -7.907   9.495  1.00109.38      A    O  
ANISOU 2389  O   MET A 320    14040  13126  14393  -1032  -3119   1393  A    O  
ATOM   2390  CB  MET A 320      64.861  -5.406  11.532  1.00 91.03      A    C  
ANISOU 2390  CB  MET A 320    12123  10673  11793  -1430  -3120   1403  A    C  
ATOM   2391  CG  MET A 320      64.746  -4.801  12.913  1.00 88.10      A    C  
ANISOU 2391  CG  MET A 320    12058  10173  11241  -1586  -3221   1413  A    C  
ATOM   2392  SD  MET A 320      63.104  -4.993  13.622  1.00103.24      A    S  
ANISOU 2392  SD  MET A 320    14345  11953  12927  -1688  -2995   1372  A    S  
ATOM   2393  CE  MET A 320      62.289  -3.522  12.989  1.00 63.16      A    C  
ANISOU 2393  CE  MET A 320     9148   6962   7886  -1772  -2727   1313  A    C  
ATOM   2394  N   PRO A 321      63.330  -7.289   9.505  1.00 90.61      A    N  
ANISOU 2394  N   PRO A 321    11900  10692  11836  -1196  -2743   1325  A    N  
ATOM   2395  CA  PRO A 321      63.106  -7.680   8.110  1.00 84.93      A    C  
ANISOU 2395  CA  PRO A 321    10937  10089  11242  -1070  -2594   1286  A    C  
ATOM   2396  C   PRO A 321      64.094  -6.969   7.210  1.00 87.26      A    C  
ANISOU 2396  C   PRO A 321    10902  10552  11702  -1007  -2619   1301  A    C  
ATOM   2397  O   PRO A 321      64.276  -5.762   7.355  1.00 87.68      A    O  
ANISOU 2397  O   PRO A 321    10905  10647  11761  -1109  -2606   1317  A    O  
ATOM   2398  CB  PRO A 321      61.695  -7.168   7.828  1.00 81.64      A    C  
ANISOU 2398  CB  PRO A 321    10590   9676  10755  -1155  -2335   1234  A    C  
ATOM   2399  CG  PRO A 321      61.032  -7.145   9.155  1.00 85.91      A    C  
ANISOU 2399  CG  PRO A 321    11465  10060  11118  -1293  -2341   1241  A    C  
ATOM   2400  CD  PRO A 321      62.101  -6.798  10.149  1.00 85.59      A    C  
ANISOU 2400  CD  PRO A 321    11511   9968  11040  -1342  -2581   1297  A    C  
ATOM   2401  N   SER A 322      64.734  -7.702   6.307  1.00 86.37      A    N  
ANISOU 2401  N   SER A 322    10572  10526  11719   -844  -2650   1295  A    N  
ATOM   2402  CA  SER A 322      65.691  -7.094   5.390  1.00 82.78      A    C  
ANISOU 2402  CA  SER A 322     9789  10241  11423   -780  -2650   1311  A    C  
ATOM   2403  C   SER A 322      65.351  -7.402   3.936  1.00 80.39      A    C  
ANISOU 2403  C   SER A 322     9288  10062  11195   -656  -2460   1264  A    C  
ATOM   2404  O   SER A 322      64.664  -8.374   3.647  1.00 83.30      A    O  
ANISOU 2404  O   SER A 322     9746  10380  11524   -582  -2393   1217  A    O  
ATOM   2405  CB  SER A 322      67.124  -7.544   5.711  1.00 82.22      A    C  
ANISOU 2405  CB  SER A 322     9597  10184  11458   -693  -2898   1354  A    C  
ATOM   2406  OG  SER A 322      67.345  -8.903   5.367  1.00 80.13      A    O  
ANISOU 2406  OG  SER A 322     9309   9897  11239   -519  -2952   1331  A    O  
ATOM   2407  N   ASP A 323      65.850  -6.580   3.023  1.00 80.55      A    N  
ANISOU 2407  N   ASP A 323     9047  10240  11320   -638  -2378   1277  A    N  
ATOM   2408  CA  ASP A 323      65.590  -6.783   1.607  1.00 88.96      A    C  
ANISOU 2408  CA  ASP A 323     9927  11433  12441   -520  -2200   1236  A    C  
ATOM   2409  C   ASP A 323      66.137  -8.117   1.090  1.00 91.13      A    C  
ANISOU 2409  C   ASP A 323    10109  11729  12787   -327  -2261   1203  A    C  
ATOM   2410  O   ASP A 323      67.003  -8.731   1.705  1.00 93.30      A    O  
ANISOU 2410  O   ASP A 323    10388  11952  13111   -269  -2454   1226  A    O  
ATOM   2411  CB  ASP A 323      66.101  -5.590   0.801  1.00105.40      A    C  
ANISOU 2411  CB  ASP A 323    11766  13673  14610   -551  -2105   1272  A    C  
ATOM   2412  CG  ASP A 323      65.292  -4.319   1.073  1.00123.23      A    C  
ANISOU 2412  CG  ASP A 323    14132  15900  16789   -719  -2000   1287  A    C  
ATOM   2413  OD1 ASP A 323      64.087  -4.436   1.418  1.00120.36      A    O  
ANISOU 2413  OD1 ASP A 323    13981  15440  16311   -771  -1921   1247  A    O  
ATOM   2414  OD2 ASP A 323      65.859  -3.209   0.946  1.00130.74      A    O1-
ANISOU 2414  OD2 ASP A 323    14953  16920  17801   -799  -1994   1338  A    O1-
ATOM   2415  N   LEU A 324      65.598  -8.577  -0.032  1.00 94.33      A    N  
ANISOU 2415  N   LEU A 324    10444  12202  13194   -222  -2105   1144  A    N  
ATOM   2416  CA  LEU A 324      65.934  -9.894  -0.555  1.00 89.96      A    C  
ANISOU 2416  CA  LEU A 324     9842  11648  12692    -35  -2143   1093  A    C  
ATOM   2417  C   LEU A 324      67.065  -9.847  -1.583  1.00105.30      A    C  
ANISOU 2417  C   LEU A 324    11474  13767  14770    110  -2118   1096  A    C  
ATOM   2418  O   LEU A 324      67.020  -9.076  -2.551  1.00 98.51      A    O  
ANISOU 2418  O   LEU A 324    10449  13053  13929    105  -1957   1098  A    O  
ATOM   2419  CB  LEU A 324      64.690 -10.572  -1.145  1.00 78.38      A    C  
ANISOU 2419  CB  LEU A 324     8500  10137  11144      1  -2004   1013  A    C  
ATOM   2420  CG  LEU A 324      63.901 -11.532  -0.245  1.00 75.42      A    C  
ANISOU 2420  CG  LEU A 324     8415   9563  10679    -40  -2076    988  A    C  
ATOM   2421  CD1 LEU A 324      63.480 -10.887   1.061  1.00 72.93      A    C  
ANISOU 2421  CD1 LEU A 324     8304   9134  10271   -230  -2128   1042  A    C  
ATOM   2422  CD2 LEU A 324      62.688 -12.086  -0.971  1.00 72.25      A    C  
ANISOU 2422  CD2 LEU A 324     8090   9140  10221    -18  -1926    905  A    C  
ATOM   2423  N   LYS A 325      68.083 -10.675  -1.349  1.00124.48      A    N  
ANISOU 2423  N   LYS A 325    13827  16179  17291    241  -2276   1098  A    N  
ATOM   2424  CA  LYS A 325      69.214 -10.821  -2.267  1.00129.51      A    C  
ANISOU 2424  CA  LYS A 325    14162  16977  18068    403  -2255   1091  A    C  
ATOM   2425  C   LYS A 325      69.779 -12.254  -2.255  1.00121.48      A    C  
ANISOU 2425  C   LYS A 325    13145  15896  17116    609  -2381   1042  A    C  
ATOM   2426  O   LYS A 325      70.830 -12.527  -2.837  1.00112.10      A    O  
ANISOU 2426  O   LYS A 325    11711  14823  16058    765  -2394   1031  A    O  
ATOM   2427  CB  LYS A 325      70.293  -9.774  -1.965  1.00134.63      A    C  
ANISOU 2427  CB  LYS A 325    14602  17727  18823    320  -2326   1173  A    C  
ATOM   2428  CG  LYS A 325      69.837  -8.343  -2.268  1.00141.89      A    C  
ANISOU 2428  CG  LYS A 325    15485  18728  19699    147  -2171   1215  A    C  
ATOM   2429  CD  LYS A 325      70.848  -7.295  -1.818  1.00149.28      A    C  
ANISOU 2429  CD  LYS A 325    16252  19730  20739     32  -2262   1298  A    C  
ATOM   2430  CE  LYS A 325      70.339  -5.878  -2.088  1.00150.59      A    C  
ANISOU 2430  CE  LYS A 325    16413  19947  20855   -143  -2112   1341  A    C  
ATOM   2431  NZ  LYS A 325      71.383  -4.837  -1.832  1.00151.43      A    N1+
ANISOU 2431  NZ  LYS A 325    16326  20129  21080   -257  -2182   1419  A    N1+
ATOM   2432  N   GLY A 326      69.055 -13.160  -1.599  1.00118.06      A    N  
ANISOU 2432  N   GLY A 326    12990  15275  16593    608  -2465   1013  A    N  
ATOM   2433  CA  GLY A 326      69.365 -14.579  -1.616  1.00112.18      A    C  
ANISOU 2433  CA  GLY A 326    12300  14433  15889    798  -2572    961  A    C  
ATOM   2434  C   GLY A 326      68.224 -15.393  -2.209  1.00104.30      A    C  
ANISOU 2434  C   GLY A 326    11475  13357  14798    841  -2448    872  A    C  
ATOM   2435  O   GLY A 326      67.155 -15.529  -1.606  1.00 92.37      A    O  
ANISOU 2435  O   GLY A 326    10225  11703  13169    710  -2443    872  A    O  
TER   
CONECT 1319 1329
CONECT 1329 1319 1330
CONECT 1330 1329 1331 1333
CONECT 1331 1330 1332 1340
CONECT 1332 1331
CONECT 1333 1330 1334 1335
CONECT 1334 1333
CONECT 1335 1333 1336
CONECT 1336 1335 1337 1338 1339
CONECT 1337 1336
CONECT 1338 1336
CONECT 1339 1336
CONECT 1340 1331
END



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