CNRS Nantes University UFIP UFIP
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***  3p6h without tail  ***

elNémo ID: 220126105930129012

Job options:

ID        	=	 220126105930129012
JOBID     	=	 3p6h without tail
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3p6h without tail

CRYST1   32.328   53.380   75.031  90.00  90.00  90.00 P 21 21 21    1
ATOM      1  N   MET A   0      12.793  16.822  -2.358  1.00 19.93           N  
ANISOU    1  N   MET A   0     2334   2582   2653   -185   -129    472       N  
ATOM      2  CA  MET A   0      13.357  15.551  -1.916  1.00 19.62           C  
ANISOU    2  CA  MET A   0     2335   2544   2575   -137    -63    376       C  
ATOM      3  C   MET A   0      12.413  14.895  -0.874  1.00 18.50           C  
ANISOU    3  C   MET A   0     2092   2444   2490   -346   -112    272       C  
ATOM      4  O   MET A   0      12.284  13.672  -0.863  1.00 19.52           O  
ANISOU    4  O   MET A   0     2429   2408   2579   -283     51    308       O  
ATOM      5  CB  MET A   0      14.754  15.853  -1.353  1.00 20.57           C  
ANISOU    5  CB  MET A   0     2390   2732   2694     -8   -264    251       C  
ATOM      6  CG  MET A   0      15.792  14.735  -1.353  1.00 23.92           C  
ANISOU    6  CG  MET A   0     2655   3039   3393    505   -268    372       C  
ATOM      7  SD  MET A   0      16.601  14.484   0.260  1.00 34.06           S  
ANISOU    7  SD  MET A   0     4034   4735   4171    346   -158    317       S  
ATOM      8  CE  MET A   0      14.984  14.177   0.907  1.00 17.54           C  
ANISOU    8  CE  MET A   0     2123   2809   1733   1016   -226    111       C  
ATOM      9  N  ACYS A   1      11.764  15.742  -0.070  0.50 19.14           N  
ANISOU    9  N  ACYS A   1     2311   2419   2539   -360    -15    281       N  
ATOM     10  N  BCYS A   1      11.742  15.679  -0.031  0.50 18.03           N  
ANISOU   10  N  BCYS A   1     2153   2293   2401   -387    -71    281       N  
ATOM     11  CA ACYS A   1      10.780  15.337   0.962  0.50 19.93           C  
ANISOU   11  CA ACYS A   1     2442   2540   2589   -303    100    221       C  
ATOM     12  CA BCYS A   1      10.810  15.080   0.978  0.50 17.95           C  
ANISOU   12  CA BCYS A   1     2178   2275   2364   -360      4    224       C  
ATOM     13  C  ACYS A   1       9.584  14.504   0.417  0.50 18.24           C  
ANISOU   13  C  ACYS A   1     2232   2245   2452   -333     96    324       C  
ATOM     14  C  BCYS A   1       9.572  14.405   0.398  0.50 16.84           C  
ANISOU   14  C  BCYS A   1     2023   2069   2304   -364     72    327       C  
ATOM     15  O  ACYS A   1       8.893  13.799   1.176  0.50 17.83           O  
ANISOU   15  O  ACYS A   1     2296   1984   2492   -293    213    401       O  
ATOM     16  O  BCYS A   1       8.807  13.730   1.113  0.50 15.97           O  
ANISOU   16  O  BCYS A   1     1978   1786   2302   -320    270    541       O  
ATOM     17  CB ACYS A   1      10.309  16.612   1.703  0.50 21.22           C  
ANISOU   17  CB ACYS A   1     2559   2689   2815   -299     50    173       C  
ATOM     18  CB BCYS A   1      10.356  16.117   1.984  0.50 18.45           C  
ANISOU   18  CB BCYS A   1     2207   2407   2395   -214    -39    162       C  
ATOM     19  SG ACYS A   1      10.132  16.465   3.549  0.50 28.50           S  
ANISOU   19  SG ACYS A   1     3840   3598   3389   -228    715    177       S  
ATOM     20  SG BCYS A   1      11.671  16.735   2.968  0.50 23.37           S  
ANISOU   20  SG BCYS A   1     2849   3076   2955   -444   -204   -147       S  
ATOM     21  N   ASP A   2       9.357  14.563  -0.891  1.00 17.06           N  
ANISOU   21  N   ASP A   2     1972   2133   2374   -411    -10    498       N  
ATOM     22  CA  ASP A   2       8.322  13.780  -1.544  1.00 17.98           C  
ANISOU   22  CA  ASP A   2     2009   2399   2421   -444    -92    482       C  
ATOM     23  C   ASP A   2       8.510  12.268  -1.380  1.00 16.97           C  
ANISOU   23  C   ASP A   2     1946   2309   2191   -545    -11    468       C  
ATOM     24  O   ASP A   2       7.548  11.561  -1.445  1.00 17.09           O  
ANISOU   24  O   ASP A   2     1752   2501   2238   -718     56    485       O  
ATOM     25  CB  ASP A   2       8.160  14.178  -3.004  1.00 19.37           C  
ANISOU   25  CB  ASP A   2     2040   2641   2677   -543   -165    431       C  
ATOM     26  CG  ASP A   2       7.612  15.593  -3.186  1.00 21.56           C  
ANISOU   26  CG  ASP A   2     2403   2922   2866   -379   -368    680       C  
ATOM     27  OD1 ASP A   2       6.954  16.172  -2.281  1.00 27.62           O  
ANISOU   27  OD1 ASP A   2     3090   3572   3831   -418    339    712       O  
ATOM     28  OD2 ASP A   2       7.901  16.149  -4.238  1.00 25.90           O1-
ANISOU   28  OD2 ASP A   2     3023   3513   3303  -1405   -204    610       O1-
ATOM     29  N   ALA A   3       9.725  11.793  -1.113  1.00 15.87           N  
ANISOU   29  N   ALA A   3     1805   2303   1921   -498    204    456       N  
ATOM     30  CA  ALA A   3       9.971  10.392  -0.845  1.00 16.62           C  
ANISOU   30  CA  ALA A   3     2001   2285   2028   -358    167    270       C  
ATOM     31  C   ALA A   3       9.228   9.902   0.391  1.00 14.50           C  
ANISOU   31  C   ALA A   3     1728   1970   1811   -240    203    225       C  
ATOM     32  O   ALA A   3       9.011   8.692   0.535  1.00 13.67           O  
ANISOU   32  O   ALA A   3     1467   1798   1926   -205    448    -15       O  
ATOM     33  CB  ALA A   3      11.433  10.105  -0.666  1.00 18.46           C  
ANISOU   33  CB  ALA A   3     2057   2632   2322   -296    203    551       C  
ATOM     34  N   PHE A   4       8.927  10.812   1.310  1.00 11.42           N  
ANISOU   34  N   PHE A   4     1098   1608   1633   -144     63    212       N  
ATOM     35  CA  PHE A   4       8.191  10.478   2.537  1.00 10.62           C  
ANISOU   35  CA  PHE A   4     1161   1364   1507    -42     96    105       C  
ATOM     36  C   PHE A   4       6.690  10.526   2.391  1.00  9.73           C  
ANISOU   36  C   PHE A   4     1152   1004   1539      3     75    102       C  
ATOM     37  O   PHE A   4       5.974   9.950   3.181  1.00 11.47           O  
ANISOU   37  O   PHE A   4     1536   1176   1644   -161    160    318       O  
ATOM     38  CB  PHE A   4       8.585  11.435   3.644  1.00 11.14           C  
ANISOU   38  CB  PHE A   4     1106   1474   1653    -91    -47    102       C  
ATOM     39  CG  PHE A   4      10.024  11.274   4.087  1.00 12.02           C  
ANISOU   39  CG  PHE A   4     1055   1868   1644   -154    -35     16       C  
ATOM     40  CD1 PHE A   4      10.429  10.201   4.913  1.00 12.92           C  
ANISOU   40  CD1 PHE A   4     1432   1843   1632     58   -233     24       C  
ATOM     41  CD2 PHE A   4      11.017  12.199   3.748  1.00 13.76           C  
ANISOU   41  CD2 PHE A   4     1103   2052   2073   -235   -158    117       C  
ATOM     42  CE1 PHE A   4      11.721  10.061   5.332  1.00 15.00           C  
ANISOU   42  CE1 PHE A   4     1600   2446   1652    -26   -126    256       C  
ATOM     43  CE2 PHE A   4      12.346  12.014   4.160  1.00 13.60           C  
ANISOU   43  CE2 PHE A   4      907   2255   2003   -622     70    151       C  
ATOM     44  CZ  PHE A   4      12.673  10.959   4.959  1.00 13.58           C  
ANISOU   44  CZ  PHE A   4     1296   2176   1685    154    -22    -85       C  
ATOM     45  N   VAL A   5       6.192  11.234   1.387  1.00 10.11           N  
ANISOU   45  N   VAL A   5     1133   1231   1477     93    103     49       N  
ATOM     46  CA  VAL A   5       4.786  11.513   1.302  1.00 11.18           C  
ANISOU   46  CA  VAL A   5     1295   1304   1646    -21      4     31       C  
ATOM     47  C   VAL A   5       4.039  10.254   0.987  1.00 11.88           C  
ANISOU   47  C   VAL A   5     1496   1275   1740   -145    144    -68       C  
ATOM     48  O   VAL A   5       4.420   9.452   0.130  1.00 14.03           O  
ANISOU   48  O   VAL A   5     1689   1473   2168   -400    354   -310       O  
ATOM     49  CB  VAL A   5       4.475  12.601   0.242  1.00 12.35           C  
ANISOU   49  CB  VAL A   5     1552   1131   2008      9   -170    117       C  
ATOM     50  CG1 VAL A   5       3.001  12.692  -0.169  1.00 15.93           C  
ANISOU   50  CG1 VAL A   5     1691   2021   2340    138   -223    295       C  
ATOM     51  CG2 VAL A   5       5.071  13.959   0.802  1.00 13.01           C  
ANISOU   51  CG2 VAL A   5     1560   1264   2118   -113   -284    184       C  
ATOM     52  N   GLY A   6       2.916  10.089   1.672  1.00 10.94           N  
ANISOU   52  N   GLY A   6     1328   1277   1550   -273     53   -194       N  
ATOM     53  CA  GLY A   6       2.070   8.993   1.421  1.00 11.13           C  
ANISOU   53  CA  GLY A   6      973   1544   1710   -258     81   -167       C  
ATOM     54  C   GLY A   6       1.393   8.479   2.678  1.00 10.57           C  
ANISOU   54  C   GLY A   6     1157   1223   1636   -171     89    -19       C  
ATOM     55  O   GLY A   6       1.335   9.152   3.689  1.00 11.95           O  
ANISOU   55  O   GLY A   6     1513   1360   1664   -372    271   -179       O  
ATOM     56  N   THR A   7       0.918   7.265   2.578  1.00 11.03           N  
ANISOU   56  N   THR A   7     1196   1368   1626   -247   -104    -29       N  
ATOM     57  CA  THR A   7       0.150   6.593   3.640  1.00 11.36           C  
ANISOU   57  CA  THR A   7     1111   1253   1953   -137   -104   -110       C  
ATOM     58  C   THR A   7       0.946   5.319   4.002  1.00 11.19           C  
ANISOU   58  C   THR A   7     1252   1195   1805     78   -161    -37       C  
ATOM     59  O   THR A   7       1.151   4.462   3.141  1.00 12.20           O  
ANISOU   59  O   THR A   7     1613   1351   1670    138   -336    -38       O  
ATOM     60  CB  THR A   7      -1.228   6.245   3.189  1.00 12.31           C  
ANISOU   60  CB  THR A   7     1120   1284   2272   -167   -173    135       C  
ATOM     61  CG2 THR A   7      -2.110   5.792   4.365  1.00 15.54           C  
ANISOU   61  CG2 THR A   7     1576   1736   2592   -655    -70     52       C  
ATOM     62  OG1 THR A   7      -1.839   7.380   2.568  1.00 17.59           O  
ANISOU   62  OG1 THR A   7     1387   1750   3544     96   -511    140       O  
ATOM     63  N   TRP A   8       1.306   5.184   5.268  1.00  9.72           N  
ANISOU   63  N   TRP A   8     1041   1117   1532    167    120    -68       N  
ATOM     64  CA  TRP A   8       2.203   4.159   5.751  1.00  9.14           C  
ANISOU   64  CA  TRP A   8      875    944   1653   -105     34    -49       C  
ATOM     65  C   TRP A   8       1.515   3.415   6.866  1.00 10.62           C  
ANISOU   65  C   TRP A   8     1261   1194   1580    -21    124     -1       C  
ATOM     66  O   TRP A   8       0.752   3.992   7.644  1.00 14.12           O  
ANISOU   66  O   TRP A   8     2209   1322   1831     14    342      0       O  
ATOM     67  CB  TRP A   8       3.457   4.811   6.266  1.00  9.88           C  
ANISOU   67  CB  TRP A   8     1151   1088   1513    -68     76     93       C  
ATOM     68  CG  TRP A   8       4.206   5.641   5.276  1.00  9.18           C  
ANISOU   68  CG  TRP A   8      715   1203   1568   -189    -49    -78       C  
ATOM     69  CD1 TRP A   8       4.070   6.996   5.017  1.00  9.93           C  
ANISOU   69  CD1 TRP A   8      788   1448   1535   -272     37    -82       C  
ATOM     70  CD2 TRP A   8       5.173   5.161   4.337  1.00  8.70           C  
ANISOU   70  CD2 TRP A   8      517   1242   1545    124    -52    153       C  
ATOM     71  CE2 TRP A   8       5.649   6.250   3.589  1.00  9.49           C  
ANISOU   71  CE2 TRP A   8      850   1354   1402     21    169      8       C  
ATOM     72  CE3 TRP A   8       5.737   3.910   4.091  1.00 10.90           C  
ANISOU   72  CE3 TRP A   8     1255   1431   1452    280    121   -100       C  
ATOM     73  NE1 TRP A   8       4.964   7.341   4.042  1.00  9.30           N  
ANISOU   73  NE1 TRP A   8      514   1236   1782   -108    138    130       N  
ATOM     74  CZ2 TRP A   8       6.633   6.111   2.612  1.00 11.42           C  
ANISOU   74  CZ2 TRP A   8     1216   1563   1557     16     10     83       C  
ATOM     75  CZ3 TRP A   8       6.705   3.770   3.134  1.00 10.00           C  
ANISOU   75  CZ3 TRP A   8      614   1407   1778    240   -204   -242       C  
ATOM     76  CH2 TRP A   8       7.154   4.867   2.398  1.00 12.06           C  
ANISOU   76  CH2 TRP A   8     1262   1683   1634     -8      0   -110       C  
ATOM     77  N   LYS A   9       1.868   2.143   7.014  1.00 10.14           N  
ANISOU   77  N   LYS A   9     1031   1248   1572   -228     13    149       N  
ATOM     78  CA  LYS A   9       1.320   1.296   8.108  1.00 10.15           C  
ANISOU   78  CA  LYS A   9      782   1488   1586   -306    -19    100       C  
ATOM     79  C   LYS A   9       2.499   0.635   8.847  1.00  9.84           C  
ANISOU   79  C   LYS A   9      684   1406   1649   -388    -36     78       C  
ATOM     80  O   LYS A   9       3.417   0.144   8.261  1.00 10.69           O  
ANISOU   80  O   LYS A   9     1362   1158   1541   -114     18     44       O  
ATOM     81  CB  LYS A   9       0.308   0.324   7.554  1.00 12.65           C  
ANISOU   81  CB  LYS A   9     1041   1776   1989   -413   -133    358       C  
ATOM     82  CG  LYS A   9       0.836  -0.624   6.614  1.00 19.05           C  
ANISOU   82  CG  LYS A   9     2399   2550   2287   -350   -292    209       C  
ATOM     83  CD  LYS A   9      -0.134  -1.697   6.212  1.00 25.39           C  
ANISOU   83  CD  LYS A   9     3296   2981   3370   -665   -389     64       C  
ATOM     84  CE  LYS A   9       0.562  -2.668   5.247  1.00 27.15           C  
ANISOU   84  CE  LYS A   9     3289   3382   3643   -962   -154    -89       C  
ATOM     85  NZ  LYS A   9       0.302  -2.306   3.809  1.00 33.04           N1+
ANISOU   85  NZ  LYS A   9     4235   4080   4237   -660   -406    260       N1+
ATOM     86  N   LEU A  10       2.407   0.597  10.176  1.00 11.00           N  
ANISOU   86  N   LEU A  10      904   1702   1572   -190     71    270       N  
ATOM     87  CA  LEU A  10       3.458  -0.022  10.979  1.00 10.74           C  
ANISOU   87  CA  LEU A  10      598   1685   1797    -55    -87    234       C  
ATOM     88  C   LEU A  10       3.411  -1.542  10.747  1.00 11.42           C  
ANISOU   88  C   LEU A  10      956   1615   1765   -135    -82    375       C  
ATOM     89  O   LEU A  10       2.332  -2.166  10.962  1.00 14.83           O  
ANISOU   89  O   LEU A  10     1458   1883   2294   -401    -78    540       O  
ATOM     90  CB  LEU A  10       3.210   0.226  12.483  1.00 12.57           C  
ANISOU   90  CB  LEU A  10      899   2052   1823   -201    -78    179       C  
ATOM     91  CG  LEU A  10       4.328  -0.221  13.395  1.00 11.67           C  
ANISOU   91  CG  LEU A  10      398   2214   1820   -187    -93    346       C  
ATOM     92  CD1 LEU A  10       5.569   0.474  13.243  1.00 12.30           C  
ANISOU   92  CD1 LEU A  10      340   2325   2007   -237    -82    260       C  
ATOM     93  CD2 LEU A  10       3.853  -0.156  14.861  1.00 16.79           C  
ANISOU   93  CD2 LEU A  10     1176   3349   1851    -31   -108    187       C  
ATOM     94  N   VAL A  11       4.568  -2.108  10.453  1.00 11.16           N  
ANISOU   94  N   VAL A  11     1045   1268   1924   -269   -240    298       N  
ATOM     95  CA  VAL A  11       4.668  -3.548  10.279  1.00 14.52           C  
ANISOU   95  CA  VAL A  11     1709   1518   2290   -310   -479    261       C  
ATOM     96  C   VAL A  11       5.585  -4.259  11.258  1.00 15.60           C  
ANISOU   96  C   VAL A  11     2097   1578   2251   -312   -594    425       C  
ATOM     97  O   VAL A  11       5.422  -5.465  11.447  1.00 18.47           O  
ANISOU   97  O   VAL A  11     2432   1709   2876   -357   -939    561       O  
ATOM     98  CB  VAL A  11       5.031  -3.942   8.857  1.00 15.84           C  
ANISOU   98  CB  VAL A  11     1782   1727   2509   -312   -470    137       C  
ATOM     99  CG1 VAL A  11       3.883  -3.528   7.929  1.00 18.01           C  
ANISOU   99  CG1 VAL A  11     2396   2149   2297    -50   -668     61       C  
ATOM    100  CG2 VAL A  11       6.428  -3.478   8.409  1.00 17.26           C  
ANISOU  100  CG2 VAL A  11     1927   2046   2584     64   -494     55       C  
ATOM    101  N   SER A  12       6.508  -3.537  11.900  1.00 13.61           N  
ANISOU  101  N   SER A  12     1793   1418   1961    -77   -526    365       N  
ATOM    102  CA  SER A  12       7.379  -4.143  12.907  1.00 14.20           C  
ANISOU  102  CA  SER A  12     1994   1324   2077   -151   -366    335       C  
ATOM    103  C   SER A  12       7.877  -3.122  13.859  1.00 13.01           C  
ANISOU  103  C   SER A  12     1668   1453   1822   -210   -322    225       C  
ATOM    104  O   SER A  12       8.041  -1.960  13.510  1.00 12.29           O  
ANISOU  104  O   SER A  12     1433   1329   1905   -392   -170    388       O  
ATOM    105  CB  SER A  12       8.506  -4.911  12.297  1.00 16.30           C  
ANISOU  105  CB  SER A  12     1978   1922   2291   -107   -445    234       C  
ATOM    106  OG  SER A  12       9.449  -4.095  11.726  1.00 18.77           O  
ANISOU  106  OG  SER A  12     2542   2244   2344     75   -159    326       O  
ATOM    107  N   SER A  13       8.174  -3.578  15.056  1.00 14.13           N  
ANISOU  107  N   SER A  13     2062   1350   1956   -402   -328    270       N  
ATOM    108  CA  SER A  13       8.705  -2.752  16.098  1.00 14.31           C  
ANISOU  108  CA  SER A  13     2118   1521   1799   -274   -393    315       C  
ATOM    109  C   SER A  13       9.667  -3.579  16.934  1.00 14.12           C  
ANISOU  109  C   SER A  13     1983   1522   1859   -227   -341    269       C  
ATOM    110  O   SER A  13       9.378  -4.728  17.260  1.00 17.31           O  
ANISOU  110  O   SER A  13     2624   1483   2469   -365   -604    585       O  
ATOM    111  CB  SER A  13       7.527  -2.223  16.920  1.00 16.64           C  
ANISOU  111  CB  SER A  13     2542   1794   1984   -405   -327    162       C  
ATOM    112  OG  SER A  13       7.907  -1.353  17.952  1.00 17.18           O  
ANISOU  112  OG  SER A  13     2385   1850   2292   -268   -657    105       O  
ATOM    113  N   GLU A  14      10.767  -2.968  17.300  1.00 12.48           N  
ANISOU  113  N   GLU A  14     1837   1183   1720     25   -329     80       N  
ATOM    114  CA  GLU A  14      11.786  -3.561  18.172  1.00 12.08           C  
ANISOU  114  CA  GLU A  14     1589   1181   1817    248   -312     20       C  
ATOM    115  C   GLU A  14      12.155  -2.593  19.275  1.00 11.84           C  
ANISOU  115  C   GLU A  14     1502   1257   1738    182   -205     48       C  
ATOM    116  O   GLU A  14      12.445  -1.436  19.005  1.00 11.54           O  
ANISOU  116  O   GLU A  14     1609   1109   1664    142    -96     37       O  
ATOM    117  CB  GLU A  14      13.054  -3.925  17.387  1.00 14.14           C  
ANISOU  117  CB  GLU A  14     1646   1622   2102    436   -363    -38       C  
ATOM    118  CG  GLU A  14      12.818  -5.092  16.408  1.00 21.74           C  
ANISOU  118  CG  GLU A  14     2883   2413   2961    317   -319   -343       C  
ATOM    119  CD  GLU A  14      12.837  -6.471  17.091  1.00 26.80           C  
ANISOU  119  CD  GLU A  14     3866   2604   3711    377   -519   -389       C  
ATOM    120  OE1 GLU A  14      13.090  -6.551  18.306  1.00 30.29           O  
ANISOU  120  OE1 GLU A  14     4223   3154   4131    291  -1049   -257       O  
ATOM    121  OE2 GLU A  14      12.573  -7.492  16.417  1.00 32.03           O1-
ANISOU  121  OE2 GLU A  14     4453   3063   4654    809   -309  -1091       O1-
ATOM    122  N   ASN A  15      12.160  -3.080  20.492  1.00 10.57           N  
ANISOU  122  N   ASN A  15     1249   1076   1691    171    -44    142       N  
ATOM    123  CA  ASN A  15      12.627  -2.349  21.663  1.00 10.47           C  
ANISOU  123  CA  ASN A  15     1136   1255   1585    168    -52     99       C  
ATOM    124  C   ASN A  15      11.798  -1.117  22.032  1.00 10.24           C  
ANISOU  124  C   ASN A  15      871   1433   1583    192     52    143       C  
ATOM    125  O   ASN A  15      12.248  -0.253  22.758  1.00 10.68           O  
ANISOU  125  O   ASN A  15     1104   1235   1718    -48    -58     29       O  
ATOM    126  CB AASN A  15      14.109  -1.961  21.540  0.50 10.98           C  
ANISOU  126  CB AASN A  15     1190   1380   1600    307    -10     71       C  
ATOM    127  CB BASN A  15      14.093  -1.982  21.519  0.50 11.62           C  
ANISOU  127  CB BASN A  15     1317   1408   1687    341     13     29       C  
ATOM    128  CG AASN A  15      14.834  -1.962  22.883  0.50  9.16           C  
ANISOU  128  CG AASN A  15      255   1535   1688      5    -55    197       C  
ATOM    129  CG BASN A  15      14.930  -3.184  21.333  0.50 12.94           C  
ANISOU  129  CG BASN A  15     1244   1714   1958    453   -176   -130       C  
ATOM    130  ND2AASN A  15      15.682  -0.974  23.101  0.50 10.36           N  
ANISOU  130  ND2AASN A  15      358   1811   1767   -351   -281    400       N  
ATOM    131  ND2BASN A  15      15.434  -3.391  20.148  0.50 18.01           N  
ANISOU  131  ND2BASN A  15     2016   2346   2478    433    425    -67       N  
ATOM    132  OD1AASN A  15      14.692  -2.899  23.682  0.50 11.64           O  
ANISOU  132  OD1AASN A  15     1109   1461   1852   -100    158    320       O  
ATOM    133  OD1BASN A  15      15.026  -3.990  22.238  0.50 17.58           O  
ANISOU  133  OD1BASN A  15     2554   1342   2784    109     17     38       O  
ATOM    134  N   PHE A  16      10.565  -1.017  21.558  1.00 10.27           N  
ANISOU  134  N   PHE A  16      951   1204   1747    -20    -25     44       N  
ATOM    135  CA  PHE A  16       9.722   0.161  21.782  1.00 10.78           C  
ANISOU  135  CA  PHE A  16     1045   1363   1688     17    -77     51       C  
ATOM    136  C   PHE A  16       9.325   0.280  23.230  1.00 10.03           C  
ANISOU  136  C   PHE A  16      707   1460   1642    -93    -58     27       C  
ATOM    137  O   PHE A  16       9.283   1.411  23.769  1.00 10.08           O  
ANISOU  137  O   PHE A  16     1114   1207   1507   -103   -129    -37       O  
ATOM    138  CB  PHE A  16       8.511   0.216  20.846  1.00 10.59           C  
ANISOU  138  CB  PHE A  16     1039   1417   1567    149    -88    -51       C  
ATOM    139  CG  PHE A  16       7.810   1.573  20.781  1.00  9.67           C  
ANISOU  139  CG  PHE A  16      559   1560   1554     88    -73    -62       C  
ATOM    140  CD1 PHE A  16       8.509   2.695  20.380  1.00 12.68           C  
ANISOU  140  CD1 PHE A  16     1456   1454   1907     20    -34    -37       C  
ATOM    141  CD2 PHE A  16       6.527   1.686  21.050  1.00 11.02           C  
ANISOU  141  CD2 PHE A  16      466   1948   1770   -110   -176    -95       C  
ATOM    142  CE1 PHE A  16       7.859   3.893  20.238  1.00 15.03           C  
ANISOU  142  CE1 PHE A  16     2428   1462   1821    321    -79   -196       C  
ATOM    143  CE2 PHE A  16       5.862   2.941  20.928  1.00 12.53           C  
ANISOU  143  CE2 PHE A  16     1287   1786   1686    693    -81    -57       C  
ATOM    144  CZ  PHE A  16       6.593   4.019  20.523  1.00 14.01           C  
ANISOU  144  CZ  PHE A  16     2376   1479   1465    361   -191    -74       C  
ATOM    145  N   ASP A  17       9.084  -0.834  23.927  1.00 10.99           N  
ANISOU  145  N   ASP A  17     1221   1209   1746     56     73    135       N  
ATOM    146  CA  ASP A  17       8.706  -0.715  25.348  1.00 12.61           C  
ANISOU  146  CA  ASP A  17     1450   1441   1899   -181      1    307       C  
ATOM    147  C   ASP A  17       9.905  -0.108  26.158  1.00 11.54           C  
ANISOU  147  C   ASP A  17     1096   1426   1860     87     31    453       C  
ATOM    148  O   ASP A  17       9.758   0.773  26.999  1.00 11.78           O  
ANISOU  148  O   ASP A  17     1448   1407   1618    -36    161    264       O  
ATOM    149  CB  ASP A  17       8.332  -2.078  25.918  1.00 13.92           C  
ANISOU  149  CB  ASP A  17     1644   1523   2120    -39     65    383       C  
ATOM    150  CG  ASP A  17       7.829  -1.978  27.322  1.00 15.99           C  
ANISOU  150  CG  ASP A  17     1876   1766   2430   -116    208    747       C  
ATOM    151  OD1 ASP A  17       8.469  -2.518  28.203  1.00 22.25           O  
ANISOU  151  OD1 ASP A  17     3095   3153   2203    202     49    682       O  
ATOM    152  OD2 ASP A  17       6.798  -1.349  27.565  1.00 18.77           O1-
ANISOU  152  OD2 ASP A  17     2395   2234   2502    117    299    712       O1-
ATOM    153  N   ASP A  18      11.104  -0.580  25.892  1.00 10.98           N  
ANISOU  153  N   ASP A  18      866   1260   2044     33    -72    313       N  
ATOM    154  CA  ASP A  18      12.346  -0.086  26.518  1.00 11.79           C  
ANISOU  154  CA  ASP A  18      745   1690   2044     33     72    327       C  
ATOM    155  C   ASP A  18      12.550   1.404  26.173  1.00 11.81           C  
ANISOU  155  C   ASP A  18     1176   1442   1868     38     31    147       C  
ATOM    156  O   ASP A  18      12.943   2.179  27.049  1.00 10.93           O  
ANISOU  156  O   ASP A  18      923   1465   1766    103   -245    254       O  
ATOM    157  CB  ASP A  18      13.591  -0.918  26.173  1.00 14.49           C  
ANISOU  157  CB  ASP A  18     1065   1966   2475    245     92    344       C  
ATOM    158  CG  ASP A  18      13.633  -2.297  26.941  1.00 22.54           C  
ANISOU  158  CG  ASP A  18     2387   2771   3404    227    221    653       C  
ATOM    159  OD1 ASP A  18      12.853  -2.488  27.872  1.00 29.87           O  
ANISOU  159  OD1 ASP A  18     3316   3438   4594    -48    241   1532       O  
ATOM    160  OD2 ASP A  18      14.464  -3.127  26.632  1.00 30.59           O1-
ANISOU  160  OD2 ASP A  18     3583   3834   4205    627   -477    491       O1-
ATOM    161  N   TYR A  19      12.257   1.824  24.936  1.00 10.45           N  
ANISOU  161  N   TYR A  19     1147   1268   1553     27    115    116       N  
ATOM    162  CA  TYR A  19      12.381   3.250  24.604  1.00  9.35           C  
ANISOU  162  CA  TYR A  19      632   1400   1521     31     97    120       C  
ATOM    163  C   TYR A  19      11.418   4.085  25.427  1.00  8.29           C  
ANISOU  163  C   TYR A  19      276   1458   1413    131    126    267       C  
ATOM    164  O   TYR A  19      11.746   5.107  26.014  1.00 10.13           O  
ANISOU  164  O   TYR A  19     1145   1360   1342    -21    -55     37       O  
ATOM    165  CB  TYR A  19      12.116   3.413  23.084  1.00 10.58           C  
ANISOU  165  CB  TYR A  19     1168   1409   1441     61    103    163       C  
ATOM    166  CG  TYR A  19      11.910   4.885  22.697  1.00  8.43           C  
ANISOU  166  CG  TYR A  19      326   1391   1485   -289     33   -114       C  
ATOM    167  CD1 TYR A  19      12.968   5.727  22.597  1.00  8.70           C  
ANISOU  167  CD1 TYR A  19      281   1634   1388   -197    -31    117       C  
ATOM    168  CD2 TYR A  19      10.639   5.340  22.446  1.00  9.78           C  
ANISOU  168  CD2 TYR A  19      370   1597   1747   -373   -168     90       C  
ATOM    169  CE1 TYR A  19      12.757   7.077  22.285  1.00  8.66           C  
ANISOU  169  CE1 TYR A  19      362   1342   1586   -326    150   -102       C  
ATOM    170  CE2 TYR A  19      10.409   6.715  22.148  1.00  9.60           C  
ANISOU  170  CE2 TYR A  19      281   1540   1823     63   -179    297       C  
ATOM    171  CZ  TYR A  19      11.490   7.546  22.077  1.00  9.10           C  
ANISOU  171  CZ  TYR A  19      550   1553   1355   -191    124    -58       C  
ATOM    172  OH  TYR A  19      11.246   8.876  21.753  1.00 11.55           O  
ANISOU  172  OH  TYR A  19     1598   1164   1623     57   -139    214       O  
ATOM    173  N   MET A  20      10.199   3.632  25.478  1.00  7.92           N  
ANISOU  173  N   MET A  20      270   1327   1409     31    103    148       N  
ATOM    174  CA  MET A  20       9.144   4.299  26.224  1.00  9.36           C  
ANISOU  174  CA  MET A  20      566   1436   1555     46    297    229       C  
ATOM    175  C   MET A  20       9.490   4.348  27.718  1.00 10.21           C  
ANISOU  175  C   MET A  20      962   1459   1458    177    190    100       C  
ATOM    176  O   MET A  20       9.268   5.390  28.364  1.00 11.42           O  
ANISOU  176  O   MET A  20     1580   1319   1436   -159    -46     -5       O  
ATOM    177  CB  MET A  20       7.805   3.632  26.051  1.00  9.59           C  
ANISOU  177  CB  MET A  20      655   1584   1402    216    370    204       C  
ATOM    178  CG  MET A  20       7.137   3.912  24.677  1.00 11.51           C  
ANISOU  178  CG  MET A  20     1570   1299   1503     34      2     84       C  
ATOM    179  SD  MET A  20       5.400   3.381  24.561  1.00 12.37           S  
ANISOU  179  SD  MET A  20     1103   1953   1642   -192     75     36       S  
ATOM    180  CE  MET A  20       5.627   1.580  24.654  1.00 13.46           C  
ANISOU  180  CE  MET A  20     1458   1675   1979   -488    116    -35       C  
ATOM    181  N   LYS A  21      10.062   3.256  28.267  1.00 11.81           N  
ANISOU  181  N   LYS A  21     1561   1503   1423   -131    105    111       N  
ATOM    182  CA  LYS A  21      10.510   3.313  29.682  1.00 12.48           C  
ANISOU  182  CA  LYS A  21     1391   1809   1540    -19     59    190       C  
ATOM    183  C   LYS A  21      11.531   4.403  29.870  1.00 13.41           C  
ANISOU  183  C   LYS A  21     1779   1846   1468   -101   -126    151       C  
ATOM    184  O   LYS A  21      11.468   5.150  30.853  1.00 15.51           O  
ANISOU  184  O   LYS A  21     2218   2140   1534    -10   -119     81       O  
ATOM    185  CB  LYS A  21      11.110   1.975  30.113  1.00 13.05           C  
ANISOU  185  CB  LYS A  21     1405   1979   1572      9     49    261       C  
ATOM    186  CG  LYS A  21      10.065   0.899  30.350  1.00 15.56           C  
ANISOU  186  CG  LYS A  21     1788   2221   1903     62     39    425       C  
ATOM    187  CD  LYS A  21      10.738  -0.347  30.866  1.00 19.28           C  
ANISOU  187  CD  LYS A  21     2334   2533   2456    165   -220    677       C  
ATOM    188  CE  LYS A  21       9.819  -1.469  31.103  1.00 23.83           C  
ANISOU  188  CE  LYS A  21     2996   2830   3227    111   -294    629       C  
ATOM    189  NZ  LYS A  21      10.399  -2.449  31.967  1.00 27.26           N1+
ANISOU  189  NZ  LYS A  21     2909   3414   4031    408   -653    791       N1+
ATOM    190  N   GLU A  22      12.487   4.507  28.946  1.00 12.33           N  
ANISOU  190  N   GLU A  22     1415   1708   1559      1   -177    133       N  
ATOM    191  CA  GLU A  22      13.602   5.497  29.053  1.00 13.32           C  
ANISOU  191  CA  GLU A  22     1560   1814   1687    -93   -278     76       C  
ATOM    192  C   GLU A  22      13.029   6.882  28.978  1.00 12.69           C  
ANISOU  192  C   GLU A  22     1739   1689   1391   -181   -234    -31       C  
ATOM    193  O   GLU A  22      13.496   7.766  29.669  1.00 15.74           O  
ANISOU  193  O   GLU A  22     2236   2134   1609   -513   -306    -43       O  
ATOM    194  CB  GLU A  22      14.692   5.217  27.995  1.00 15.07           C  
ANISOU  194  CB  GLU A  22     1783   2089   1851   -102    -98     50       C  
ATOM    195  CG  GLU A  22      16.072   5.721  28.340  1.00 17.96           C  
ANISOU  195  CG  GLU A  22     1965   2441   2416   -196   -427    145       C  
ATOM    196  CD  GLU A  22      16.796   4.879  29.401  1.00 18.57           C  
ANISOU  196  CD  GLU A  22     2160   2427   2468   -363   -381    385       C  
ATOM    197  OE1 GLU A  22      16.263   3.858  29.901  1.00 21.57           O  
ANISOU  197  OE1 GLU A  22     2442   2917   2834   -741   -585    488       O  
ATOM    198  OE2 GLU A  22      17.925   5.266  29.751  1.00 22.85           O1-
ANISOU  198  OE2 GLU A  22     3045   2859   2777   -270   -807    136       O1-
ATOM    199  N   VAL A  23      11.993   7.074  28.159  1.00 12.43           N  
ANISOU  199  N   VAL A  23     1649   1592   1481   -253   -107     34       N  
ATOM    200  CA  VAL A  23      11.298   8.353  28.021  1.00 11.96           C  
ANISOU  200  CA  VAL A  23     1454   1531   1556   -295     29    -41       C  
ATOM    201  C   VAL A  23      10.564   8.748  29.297  1.00 13.02           C  
ANISOU  201  C   VAL A  23     1717   1629   1599   -362     19    -78       C  
ATOM    202  O   VAL A  23      10.459   9.908  29.606  1.00 15.13           O  
ANISOU  202  O   VAL A  23     2285   1630   1833   -336    265   -138       O  
ATOM    203  CB  VAL A  23      10.338   8.341  26.776  1.00 12.31           C  
ANISOU  203  CB  VAL A  23     1643   1463   1569    -85    -53     87       C  
ATOM    204  CG1 VAL A  23       9.339   9.485  26.767  1.00 13.21           C  
ANISOU  204  CG1 VAL A  23     1844   1482   1691    -77    -44      4       C  
ATOM    205  CG2 VAL A  23      11.187   8.315  25.490  1.00 13.06           C  
ANISOU  205  CG2 VAL A  23     1966   1495   1499   -185    169    -84       C  
ATOM    206  N   GLY A  24      10.135   7.754  30.066  1.00 13.31           N  
ANISOU  206  N   GLY A  24     1881   1591   1585   -379     -6    -42       N  
ATOM    207  CA  GLY A  24       9.369   7.984  31.279  1.00 14.22           C  
ANISOU  207  CA  GLY A  24     1998   1841   1563   -265     40    -58       C  
ATOM    208  C   GLY A  24       7.889   7.644  31.196  1.00 13.75           C  
ANISOU  208  C   GLY A  24     2019   1679   1525   -233     55    -71       C  
ATOM    209  O   GLY A  24       7.098   8.034  32.062  1.00 14.49           O  
ANISOU  209  O   GLY A  24     2015   1800   1689   -220    192   -216       O  
ATOM    210  N   VAL A  25       7.476   6.945  30.161  1.00 12.82           N  
ANISOU  210  N   VAL A  25     1971   1318   1580   -212      0    -45       N  
ATOM    211  CA  VAL A  25       6.081   6.556  29.985  1.00 12.36           C  
ANISOU  211  CA  VAL A  25     1845   1334   1515      8     89     11       C  
ATOM    212  C   VAL A  25       5.678   5.534  31.043  1.00 11.59           C  
ANISOU  212  C   VAL A  25     1400   1475   1527    -78     34   -166       C  
ATOM    213  O   VAL A  25       6.434   4.570  31.272  1.00 12.44           O  
ANISOU  213  O   VAL A  25     1686   1453   1588   -311   -163    152       O  
ATOM    214  CB  VAL A  25       5.826   5.994  28.554  1.00 10.92           C  
ANISOU  214  CB  VAL A  25     1273   1239   1635   -212     41    -72       C  
ATOM    215  CG1 VAL A  25       4.373   5.699  28.356  1.00 12.18           C  
ANISOU  215  CG1 VAL A  25     1525   1462   1637    -38    150     74       C  
ATOM    216  CG2 VAL A  25       6.270   6.984  27.477  1.00 12.68           C  
ANISOU  216  CG2 VAL A  25     1782   1262   1771   -195    169    381       C  
ATOM    217  N   GLY A  26       4.512   5.761  31.652  1.00 12.82           N  
ANISOU  217  N   GLY A  26     1749   1669   1451   -353    -73    -40       N  
ATOM    218  CA  GLY A  26       3.983   4.884  32.670  1.00 13.81           C  
ANISOU  218  CA  GLY A  26     1854   1981   1412   -432    136   -169       C  
ATOM    219  C   GLY A  26       3.484   3.555  32.149  1.00 14.13           C  
ANISOU  219  C   GLY A  26     2034   1860   1475   -565    127     19       C  
ATOM    220  O   GLY A  26       3.181   3.402  30.980  1.00 13.33           O  
ANISOU  220  O   GLY A  26     1900   1769   1396   -737    -44    -28       O  
ATOM    221  N   PHE A  27       3.312   2.601  33.069  1.00 13.33           N  
ANISOU  221  N   PHE A  27     1955   1774   1334   -470      1    -19       N  
ATOM    222  CA  PHE A  27       3.031   1.218  32.712  1.00 13.34           C  
ANISOU  222  CA  PHE A  27     1709   1839   1521   -412     54    170       C  
ATOM    223  C   PHE A  27       1.787   1.117  31.806  1.00 11.08           C  
ANISOU  223  C   PHE A  27     1173   1440   1598   -460    199    271       C  
ATOM    224  O   PHE A  27       1.841   0.507  30.745  1.00 12.18           O  
ANISOU  224  O   PHE A  27     1615   1587   1424   -453     46    121       O  
ATOM    225  CB  PHE A  27       2.827   0.392  33.988  1.00 12.73           C  
ANISOU  225  CB  PHE A  27     1453   1816   1567   -280     14    228       C  
ATOM    226  CG  PHE A  27       2.419  -1.023  33.722  1.00 14.62           C  
ANISOU  226  CG  PHE A  27     2084   1882   1589   -619    -65    333       C  
ATOM    227  CD1 PHE A  27       3.351  -2.039  33.583  1.00 15.14           C  
ANISOU  227  CD1 PHE A  27     1695   2020   2035   -806    -35    377       C  
ATOM    228  CD2 PHE A  27       1.077  -1.393  33.619  1.00 15.46           C  
ANISOU  228  CD2 PHE A  27     2090   1822   1961   -623   -165    605       C  
ATOM    229  CE1 PHE A  27       2.922  -3.378  33.311  1.00 17.05           C  
ANISOU  229  CE1 PHE A  27     1857   2352   2268   -792    180    560       C  
ATOM    230  CE2 PHE A  27       0.703  -2.703  33.328  1.00 15.34           C  
ANISOU  230  CE2 PHE A  27     1528   2145   2154   -603   -142    848       C  
ATOM    231  CZ  PHE A  27       1.635  -3.675  33.210  1.00 16.03           C  
ANISOU  231  CZ  PHE A  27     1925   2160   2003   -499   -325    186       C  
ATOM    232  N   ALA A  28       0.651   1.645  32.236  1.00 12.36           N  
ANISOU  232  N   ALA A  28     1134   1809   1751   -452    258     35       N  
ATOM    233  CA  ALA A  28      -0.619   1.405  31.498  1.00 12.85           C  
ANISOU  233  CA  ALA A  28     1190   1758   1932   -179     -9    119       C  
ATOM    234  C   ALA A  28      -0.569   2.063  30.119  1.00 11.97           C  
ANISOU  234  C   ALA A  28      973   1659   1914   -448     29     64       C  
ATOM    235  O   ALA A  28      -0.989   1.462  29.129  1.00 14.12           O  
ANISOU  235  O   ALA A  28     1682   1903   1779   -510   -154    150       O  
ATOM    236  CB  ALA A  28      -1.845   1.911  32.244  1.00 12.87           C  
ANISOU  236  CB  ALA A  28      818   1690   2381    -16    101    122       C  
ATOM    237  N   THR A  29       0.015   3.263  30.035  1.00 12.23           N  
ANISOU  237  N   THR A  29     1360   1616   1667   -456    -48     21       N  
ATOM    238  CA  THR A  29       0.207   3.900  28.749  1.00 12.24           C  
ANISOU  238  CA  THR A  29     1209   1655   1785   -258   -117     97       C  
ATOM    239  C   THR A  29       1.126   3.088  27.865  1.00 11.25           C  
ANISOU  239  C   THR A  29      868   1616   1787    -83   -108    119       C  
ATOM    240  O   THR A  29       0.874   2.917  26.662  1.00 11.60           O  
ANISOU  240  O   THR A  29     1089   1728   1588   -148   -125     -1       O  
ATOM    241  CB  THR A  29       0.716   5.310  28.914  1.00 12.85           C  
ANISOU  241  CB  THR A  29     1654   1389   1836   -270    -53     22       C  
ATOM    242  CG2 THR A  29       0.947   5.994  27.561  1.00 13.82           C  
ANISOU  242  CG2 THR A  29     1813   1468   1967   -297   -391    278       C  
ATOM    243  OG1 THR A  29      -0.251   6.034  29.664  1.00 14.92           O  
ANISOU  243  OG1 THR A  29     1507   1798   2364    -68     34     36       O  
ATOM    244  N   ARG A  30       2.219   2.576  28.405  1.00 10.61           N  
ANISOU  244  N   ARG A  30      921   1498   1612   -334    -64    184       N  
ATOM    245  CA  ARG A  30       3.169   1.772  27.614  1.00 11.13           C  
ANISOU  245  CA  ARG A  30     1143   1599   1484   -159      2    341       C  
ATOM    246  C   ARG A  30       2.474   0.548  27.026  1.00 11.07           C  
ANISOU  246  C   ARG A  30     1215   1525   1464   -118    -66    313       C  
ATOM    247  O   ARG A  30       2.689   0.160  25.870  1.00 11.96           O  
ANISOU  247  O   ARG A  30     1308   1753   1482    -20    -58    171       O  
ATOM    248  CB  ARG A  30       4.352   1.278  28.391  1.00 11.34           C  
ANISOU  248  CB  ARG A  30      884   1756   1665     25   -122    218       C  
ATOM    249  CG  ARG A  30       5.498   2.277  28.716  1.00 12.04           C  
ANISOU  249  CG  ARG A  30     1168   1809   1598   -448    116    210       C  
ATOM    250  CD  ARG A  30       6.811   1.644  28.990  1.00 10.60           C  
ANISOU  250  CD  ARG A  30      313   1937   1775   -244   -216    146       C  
ATOM    251  NE  ARG A  30       6.730   0.497  29.874  1.00 11.89           N  
ANISOU  251  NE  ARG A  30     1326   1582   1609   -256   -106    144       N  
ATOM    252  CZ  ARG A  30       6.581   0.549  31.179  1.00 12.98           C  
ANISOU  252  CZ  ARG A  30     1620   1690   1620   -164      2    113       C  
ATOM    253  NH1 ARG A  30       6.510   1.716  31.858  1.00 13.75           N1+
ANISOU  253  NH1 ARG A  30     2184   1596   1443   -105   -137    326       N1+
ATOM    254  NH2 ARG A  30       6.543  -0.596  31.859  1.00 14.76           N  
ANISOU  254  NH2 ARG A  30     2403   1668   1536   -194    102    184       N  
ATOM    255  N   LYS A  31       1.669  -0.113  27.835  1.00 11.29           N  
ANISOU  255  N   LYS A  31     1268   1600   1418   -275    -20    211       N  
ATOM    256  CA  LYS A  31       1.060  -1.356  27.364  1.00 11.82           C  
ANISOU  256  CA  LYS A  31     1430   1467   1593   -382     19     17       C  
ATOM    257  C   LYS A  31       0.110  -1.064  26.222  1.00 11.89           C  
ANISOU  257  C   LYS A  31     1483   1473   1559   -108    -64     40       C  
ATOM    258  O   LYS A  31       0.106  -1.770  25.223  1.00 13.03           O  
ANISOU  258  O   LYS A  31     1610   1650   1688   -101    -87   -224       O  
ATOM    259  CB  LYS A  31       0.340  -2.066  28.496  1.00 12.53           C  
ANISOU  259  CB  LYS A  31     1441   1525   1793   -516     43     99       C  
ATOM    260  CG  LYS A  31       1.217  -2.608  29.581  1.00 16.28           C  
ANISOU  260  CG  LYS A  31     2341   1910   1933   -323   -131    186       C  
ATOM    261  CD  LYS A  31       2.183  -3.675  29.100  1.00 21.65           C  
ANISOU  261  CD  LYS A  31     3054   2759   2412    269   -345    482       C  
ATOM    262  CE  LYS A  31       3.594  -3.420  29.616  1.00 26.71           C  
ANISOU  262  CE  LYS A  31     3372   3494   3281    -31    -40   -251       C  
ATOM    263  NZ  LYS A  31       4.616  -4.407  29.123  1.00 29.44           N1+
ANISOU  263  NZ  LYS A  31     3897   3705   3582    548   -416   -155       N1+
ATOM    264  N   VAL A  32      -0.730  -0.076  26.382  1.00 11.23           N  
ANISOU  264  N   VAL A  32     1228   1495   1542   -209    -97   -109       N  
ATOM    265  CA  VAL A  32      -1.739   0.262  25.312  1.00 11.62           C  
ANISOU  265  CA  VAL A  32     1061   1718   1635   -203   -179   -157       C  
ATOM    266  C   VAL A  32      -0.999   0.863  24.101  1.00 11.78           C  
ANISOU  266  C   VAL A  32     1328   1547   1598   -199    -75   -148       C  
ATOM    267  O   VAL A  32      -1.358   0.550  22.965  1.00 12.35           O  
ANISOU  267  O   VAL A  32     1319   1899   1474   -398    -76   -111       O  
ATOM    268  CB  VAL A  32      -2.866   1.149  25.884  1.00 12.89           C  
ANISOU  268  CB  VAL A  32     1462   1762   1672    -93    -36   -214       C  
ATOM    269  CG1 VAL A  32      -3.738   1.703  24.804  1.00 16.23           C  
ANISOU  269  CG1 VAL A  32     1773   2251   2140    103    -86   -281       C  
ATOM    270  CG2 VAL A  32      -3.639   0.334  26.937  1.00 14.88           C  
ANISOU  270  CG2 VAL A  32     1525   2158   1968    244     73    -18       C  
ATOM    271  N   ALA A  33      -0.036   1.754  24.328  1.00 11.16           N  
ANISOU  271  N   ALA A  33     1163   1623   1453   -149   -125    -39       N  
ATOM    272  CA  ALA A  33       0.680   2.382  23.215  1.00 10.71           C  
ANISOU  272  CA  ALA A  33      982   1722   1366    -44    -74     82       C  
ATOM    273  C   ALA A  33       1.493   1.353  22.440  1.00 13.06           C  
ANISOU  273  C   ALA A  33     1641   1796   1525      9    -25    125       C  
ATOM    274  O   ALA A  33       1.592   1.437  21.222  1.00 13.42           O  
ANISOU  274  O   ALA A  33     1812   1879   1406    -36     21    185       O  
ATOM    275  CB  ALA A  33       1.529   3.504  23.709  1.00 13.14           C  
ANISOU  275  CB  ALA A  33     1635   1790   1567   -219   -292     93       C  
ATOM    276  N   GLY A  34       2.034   0.347  23.126  1.00 12.11           N  
ANISOU  276  N   GLY A  34     1277   1909   1414    182    153    158       N  
ATOM    277  CA  GLY A  34       2.838  -0.645  22.457  1.00 11.98           C  
ANISOU  277  CA  GLY A  34     1175   1896   1477    259     44    151       C  
ATOM    278  C   GLY A  34       2.067  -1.562  21.571  1.00 12.81           C  
ANISOU  278  C   GLY A  34     1393   1875   1598    149    214    116       C  
ATOM    279  O   GLY A  34       2.592  -2.080  20.622  1.00 14.43           O  
ANISOU  279  O   GLY A  34     1433   2305   1745    117    284   -193       O  
ATOM    280  N   MET A  35       0.789  -1.746  21.857  1.00 11.91           N  
ANISOU  280  N   MET A  35     1319   1543   1663    271    385    193       N  
ATOM    281  CA  MET A  35      -0.079  -2.567  21.029  1.00 12.21           C  
ANISOU  281  CA  MET A  35     1271   1501   1867     51    173    347       C  
ATOM    282  C   MET A  35      -0.494  -1.911  19.696  1.00 12.09           C  
ANISOU  282  C   MET A  35     1349   1417   1826   -225    168    371       C  
ATOM    283  O   MET A  35      -0.812  -2.577  18.738  1.00 14.64           O  
ANISOU  283  O   MET A  35     1922   1507   2133   -343     61    345       O  
ATOM    284  CB  MET A  35      -1.373  -2.912  21.743  1.00 13.40           C  
ANISOU  284  CB  MET A  35     1436   1475   2180    -48    312    426       C  
ATOM    285  CG  MET A  35      -1.200  -3.865  22.865  1.00 14.20           C  
ANISOU  285  CG  MET A  35     1927   1590   1876    146    305     89       C  
ATOM    286  SD  MET A  35      -0.717  -5.479  22.413  1.00 13.73           S  
ANISOU  286  SD  MET A  35     1629   1479   2107     43    103    325       S  
ATOM    287  CE  MET A  35      -2.057  -6.069  21.438  1.00 19.63           C  
ANISOU  287  CE  MET A  35     3026   2180   2252   -434   -750    301       C  
ATOM    288  N   ALA A  36      -0.441  -0.584  19.635  1.00 11.40           N  
ANISOU  288  N   ALA A  36     1151   1419   1760     17    131    392       N  
ATOM    289  CA  ALA A  36      -0.962   0.125  18.482  1.00 13.16           C  
ANISOU  289  CA  ALA A  36     1413   1766   1821     48    135    275       C  
ATOM    290  C   ALA A  36      -0.164  -0.156  17.220  1.00 11.67           C  
ANISOU  290  C   ALA A  36      892   1660   1882   -243     86    171       C  
ATOM    291  O   ALA A  36       1.034  -0.329  17.258  1.00 12.66           O  
ANISOU  291  O   ALA A  36      865   2029   1915    -98     54    195       O  
ATOM    292  CB  ALA A  36      -0.961   1.639  18.769  1.00 13.32           C  
ANISOU  292  CB  ALA A  36     1549   1521   1990    131     23    198       C  
ATOM    293  N   LYS A  37      -0.875  -0.246  16.107  1.00 12.05           N  
ANISOU  293  N   LYS A  37     1054   1613   1911   -250     58    209       N  
ATOM    294  CA ALYS A  37      -0.236  -0.437  14.810  0.50 12.70           C  
ANISOU  294  CA ALYS A  37     1183   1709   1930   -175     35     67       C  
ATOM    295  CA BLYS A  37      -0.272  -0.432  14.782  0.50 12.29           C  
ANISOU  295  CA BLYS A  37     1164   1604   1900   -178     41     60       C  
ATOM    296  C   LYS A  37      -0.754   0.732  13.935  1.00 12.17           C  
ANISOU  296  C   LYS A  37     1169   1636   1818   -370     59    175       C  
ATOM    297  O   LYS A  37      -1.689   0.609  13.146  1.00 13.98           O  
ANISOU  297  O   LYS A  37     1449   1936   1925   -222   -134    189       O  
ATOM    298  CB ALYS A  37      -0.467  -1.876  14.293  0.50 13.70           C  
ANISOU  298  CB ALYS A  37     1298   1819   2087   -221     77     45       C  
ATOM    299  CB BLYS A  37      -0.695  -1.760  14.159  0.50 13.22           C  
ANISOU  299  CB BLYS A  37     1381   1613   2028   -174      8     55       C  
ATOM    300  CG ALYS A  37      -0.388  -2.921  15.463  0.50 16.73           C  
ANISOU  300  CG ALYS A  37     1889   2157   2308    -81    -95     27       C  
ATOM    301  CG BLYS A  37       0.007  -2.930  14.786  0.50 12.67           C  
ANISOU  301  CG BLYS A  37     1401   1377   2033   -155    184     11       C  
ATOM    302  CD ALYS A  37       0.498  -4.114  15.284  0.50 20.03           C  
ANISOU  302  CD ALYS A  37     2321   2545   2745    113   -318    163       C  
ATOM    303  CD BLYS A  37       1.476  -2.935  14.461  0.50 16.54           C  
ANISOU  303  CD BLYS A  37     1650   2289   2342    -67    -47    126       C  
ATOM    304  CE ALYS A  37       0.246  -5.222  16.379  0.50 18.05           C  
ANISOU  304  CE ALYS A  37     1984   2222   2651      6   -114     68       C  
ATOM    305  CE BLYS A  37       2.147  -4.269  14.803  0.50 19.00           C  
ANISOU  305  CE BLYS A  37     2190   2485   2542     87     59    126       C  
ATOM    306  NZ ALYS A  37      -0.633  -4.943  17.609  0.50 14.76           N1+
ANISOU  306  NZ ALYS A  37     1309   1584   2715   -606    312    380       N1+
ATOM    307  NZ BLYS A  37       1.930  -4.675  16.196  0.50 19.75           N1+
ANISOU  307  NZ BLYS A  37     2100   2685   2720    242    149    594       N1+
ATOM    308  N   PRO A  38      -0.129   1.907  14.107  1.00 11.58           N  
ANISOU  308  N   PRO A  38     1227   1470   1701   -355     44    117       N  
ATOM    309  CA  PRO A  38      -0.677   3.073  13.469  1.00 12.40           C  
ANISOU  309  CA  PRO A  38     1337   1674   1699   -119    127    159       C  
ATOM    310  C   PRO A  38      -0.515   3.139  11.978  1.00 12.39           C  
ANISOU  310  C   PRO A  38     1405   1558   1743   -321    472     34       C  
ATOM    311  O   PRO A  38       0.347   2.516  11.416  1.00 12.80           O  
ANISOU  311  O   PRO A  38     1469   1633   1760   -293    377    -17       O  
ATOM    312  CB  PRO A  38       0.085   4.240  14.085  1.00 14.80           C  
ANISOU  312  CB  PRO A  38     2026   1739   1856    -51    219    -61       C  
ATOM    313  CG  PRO A  38       0.764   3.736  15.169  1.00 17.63           C  
ANISOU  313  CG  PRO A  38     2077   2088   2531   -229   -145      2       C  
ATOM    314  CD  PRO A  38       0.959   2.264  15.018  1.00 13.59           C  
ANISOU  314  CD  PRO A  38     1506   1859   1799   -284     57    -70       C  
ATOM    315  N   ASN A  39      -1.417   3.922  11.389  1.00 12.41           N  
ANISOU  315  N   ASN A  39     1710   1404   1601    -94    489     92       N  
ATOM    316  CA  ASN A  39      -1.153   4.482  10.063  1.00 15.16           C  
ANISOU  316  CA  ASN A  39     2227   1611   1921   -208    572     45       C  
ATOM    317  C   ASN A  39      -0.546   5.858  10.202  1.00 16.43           C  
ANISOU  317  C   ASN A  39     2791   1548   1903   -264    732    -52       C  
ATOM    318  O   ASN A  39      -0.952   6.672  11.049  1.00 20.22           O  
ANISOU  318  O   ASN A  39     3429   1801   2451   -506   1266   -197       O  
ATOM    319  CB  ASN A  39      -2.387   4.534   9.254  1.00 17.36           C  
ANISOU  319  CB  ASN A  39     2616   1915   2064     39    325    145       C  
ATOM    320  CG  ASN A  39      -2.701   3.232   8.556  1.00 20.49           C  
ANISOU  320  CG  ASN A  39     2896   2412   2475   -215     -8    280       C  
ATOM    321  ND2 ASN A  39      -3.308   3.359   7.368  1.00 28.62           N  
ANISOU  321  ND2 ASN A  39     3937   4205   2733    276   -407    -85       N  
ATOM    322  OD1 ASN A  39      -2.329   2.155   8.995  1.00 27.12           O  
ANISOU  322  OD1 ASN A  39     4560   2674   3071   -251   -263    200       O  
ATOM    323  N   MET A  40       0.429   6.140   9.372  1.00 15.82           N  
ANISOU  323  N   MET A  40     2680   1463   1866   -264    718    -38       N  
ATOM    324  CA  MET A  40       1.088   7.403   9.377  1.00 15.10           C  
ANISOU  324  CA  MET A  40     2615   1373   1750   -207    645   -133       C  
ATOM    325  C   MET A  40       0.928   8.023   8.001  1.00 14.11           C  
ANISOU  325  C   MET A  40     2410   1176   1774   -221    615    -17       C  
ATOM    326  O   MET A  40       1.197   7.390   6.998  1.00 15.06           O  
ANISOU  326  O   MET A  40     2750   1253   1717    114    739    122       O  
ATOM    327  CB  MET A  40       2.543   7.219   9.733  1.00 15.62           C  
ANISOU  327  CB  MET A  40     2674   1424   1837   -537    551     38       C  
ATOM    328  CG  MET A  40       3.275   8.516   9.702  1.00 19.55           C  
ANISOU  328  CG  MET A  40     3191   1810   2427   -691    660      5       C  
ATOM    329  SD  MET A  40       4.975   8.399  10.157  1.00 23.18           S  
ANISOU  329  SD  MET A  40     4186   1736   2882   -687     33   -123       S  
ATOM    330  CE  MET A  40       5.560   7.080   9.125  1.00 25.39           C  
ANISOU  330  CE  MET A  40     3728   3287   2628   -602    492   -217       C  
ATOM    331  N   ILE A  41       0.366   9.211   7.967  1.00 12.82           N  
ANISOU  331  N   ILE A  41     1905   1222   1744   -101    569    -75       N  
ATOM    332  CA  ILE A  41       0.076   9.954   6.722  1.00 12.27           C  
ANISOU  332  CA  ILE A  41     1749   1299   1613   -201    435   -217       C  
ATOM    333  C   ILE A  41       0.985  11.162   6.705  1.00 10.91           C  
ANISOU  333  C   ILE A  41     1448   1105   1592   -293    124    -36       C  
ATOM    334  O   ILE A  41       0.898  12.013   7.601  1.00 12.25           O  
ANISOU  334  O   ILE A  41     1754   1308   1590   -327    409   -116       O  
ATOM    335  CB  ILE A  41      -1.412  10.406   6.578  1.00 13.76           C  
ANISOU  335  CB  ILE A  41     1522   1605   2100   -236    464   -325       C  
ATOM    336  CG1 ILE A  41      -2.410   9.207   6.693  1.00 19.15           C  
ANISOU  336  CG1 ILE A  41     2341   2175   2760   -631    621   -332       C  
ATOM    337  CG2 ILE A  41      -1.639  11.173   5.299  1.00 17.54           C  
ANISOU  337  CG2 ILE A  41     2073   2161   2430    -13    194   -296       C  
ATOM    338  CD1 ILE A  41      -3.879   9.650   6.931  1.00 23.86           C  
ANISOU  338  CD1 ILE A  41     2434   2839   3792   -774    565   -349       C  
ATOM    339  N   ILE A  42       1.810  11.264   5.671  1.00  9.98           N  
ANISOU  339  N   ILE A  42     1187   1124   1477   -126    -19   -115       N  
ATOM    340  CA  ILE A  42       2.803  12.357   5.531  1.00  9.28           C  
ANISOU  340  CA  ILE A  42     1098   1044   1383    -95     -5    -36       C  
ATOM    341  C   ILE A  42       2.427  13.113   4.257  1.00  9.20           C  
ANISOU  341  C   ILE A  42      920   1102   1471      1   -124     -2       C  
ATOM    342  O   ILE A  42       2.269  12.492   3.202  1.00 10.71           O  
ANISOU  342  O   ILE A  42     1545   1155   1370   -148   -159    -43       O  
ATOM    343  CB  ILE A  42       4.238  11.839   5.477  1.00  8.75           C  
ANISOU  343  CB  ILE A  42      847   1163   1312    -87    -21    -61       C  
ATOM    344  CG1 ILE A  42       4.594  11.082   6.777  1.00 11.75           C  
ANISOU  344  CG1 ILE A  42     1919   1043   1499    105    -25    -36       C  
ATOM    345  CG2 ILE A  42       5.199  12.990   5.257  1.00 11.39           C  
ANISOU  345  CG2 ILE A  42     1369   1427   1530   -510    -27   -177       C  
ATOM    346  CD1 ILE A  42       6.020  10.463   6.792  1.00 12.63           C  
ANISOU  346  CD1 ILE A  42     1663   1347   1789    209    -94    108       C  
ATOM    347  N   SER A  43       2.194  14.412   4.368  1.00  9.58           N  
ANISOU  347  N   SER A  43     1170   1086   1383    -83   -284      2       N  
ATOM    348  CA  SER A  43       1.920  15.262   3.254  1.00 11.15           C  
ANISOU  348  CA  SER A  43     1346   1399   1488   -105   -322     75       C  
ATOM    349  C   SER A  43       2.712  16.526   3.330  1.00 10.47           C  
ANISOU  349  C   SER A  43     1378   1157   1440   -238   -144     14       C  
ATOM    350  O   SER A  43       3.232  16.929   4.383  1.00 10.53           O  
ANISOU  350  O   SER A  43     1505   1231   1264   -123    -77     58       O  
ATOM    351  CB  SER A  43       0.450  15.548   3.203  1.00 13.19           C  
ANISOU  351  CB  SER A  43     1590   1526   1896   -167   -232    209       C  
ATOM    352  OG  SER A  43       0.056  16.208   4.359  1.00 15.19           O  
ANISOU  352  OG  SER A  43     1567   2008   2196    283   -181     92       O  
ATOM    353  N   VAL A  44       2.845  17.152   2.175  1.00 11.58           N  
ANISOU  353  N   VAL A  44     1818   1250   1329   -100   -295    -68       N  
ATOM    354  CA  VAL A  44       3.529  18.395   2.028  1.00 11.00           C  
ANISOU  354  CA  VAL A  44     1378   1275   1527   -294   -190     -3       C  
ATOM    355  C   VAL A  44       2.722  19.391   1.243  1.00 12.29           C  
ANISOU  355  C   VAL A  44     1880   1328   1459   -126   -294    -37       C  
ATOM    356  O   VAL A  44       2.061  19.030   0.266  1.00 14.85           O  
ANISOU  356  O   VAL A  44     2621   1302   1718    -27   -716     -8       O  
ATOM    357  CB  VAL A  44       4.894  18.233   1.351  1.00 11.93           C  
ANISOU  357  CB  VAL A  44     1210   1553   1768   -303   -224     94       C  
ATOM    358  CG1 VAL A  44       5.732  19.527   1.244  1.00 16.24           C  
ANISOU  358  CG1 VAL A  44      502   2374   3294   -648    267    122       C  
ATOM    359  CG2 VAL A  44       5.766  17.253   2.096  1.00 14.86           C  
ANISOU  359  CG2 VAL A  44     1512   1727   2406   -131   -270    -80       C  
ATOM    360  N   ASN A  45       2.668  20.627   1.700  1.00 11.07           N  
ANISOU  360  N   ASN A  45     1467   1339   1398   -122   -260     57       N  
ATOM    361  CA  ASN A  45       1.935  21.695   1.010  1.00 11.46           C  
ANISOU  361  CA  ASN A  45     1523   1396   1433   -173   -280    110       C  
ATOM    362  C   ASN A  45       2.818  22.930   1.176  1.00 11.99           C  
ANISOU  362  C   ASN A  45     1800   1358   1398    -75   -245    197       C  
ATOM    363  O   ASN A  45       2.923  23.495   2.241  1.00 11.17           O  
ANISOU  363  O   ASN A  45     1559   1337   1348     84   -173    122       O  
ATOM    364  CB  ASN A  45       0.561  21.844   1.636  1.00 11.41           C  
ANISOU  364  CB  ASN A  45     1342   1443   1547    -89   -382    -92       C  
ATOM    365  CG  ASN A  45      -0.341  22.856   0.930  1.00 12.11           C  
ANISOU  365  CG  ASN A  45     1124   1880   1595    108   -329     26       C  
ATOM    366  ND2 ASN A  45       0.270  23.902   0.450  1.00 11.24           N  
ANISOU  366  ND2 ASN A  45     1089   1403   1775    -85   -547    216       N  
ATOM    367  OD1 ASN A  45      -1.599  22.690   0.828  1.00 13.63           O  
ANISOU  367  OD1 ASN A  45     1360   1868   1950    124   -228   -159       O  
ATOM    368  N   GLY A  46       3.486  23.320   0.102  1.00 13.20           N  
ANISOU  368  N   GLY A  46     1972   1598   1443   -196   -181     89       N  
ATOM    369  CA  GLY A  46       4.462  24.380   0.159  1.00 13.02           C  
ANISOU  369  CA  GLY A  46     1692   1591   1664   -150    -43    222       C  
ATOM    370  C   GLY A  46       5.572  24.017   1.112  1.00 12.54           C  
ANISOU  370  C   GLY A  46     1535   1618   1609    -80    149    267       C  
ATOM    371  O   GLY A  46       6.193  22.965   0.993  1.00 14.72           O  
ANISOU  371  O   GLY A  46     1769   1801   2020    141    298     41       O  
ATOM    372  N   ASP A  47       5.825  24.881   2.086  1.00 12.16           N  
ANISOU  372  N   ASP A  47     1298   1738   1583   -229     63    208       N  
ATOM    373  CA  ASP A  47       6.884  24.644   3.084  1.00 12.99           C  
ANISOU  373  CA  ASP A  47     1511   1652   1772   -128   -110    333       C  
ATOM    374  C   ASP A  47       6.389  23.844   4.276  1.00 11.61           C  
ANISOU  374  C   ASP A  47     1439   1393   1576    -52     -7    162       C  
ATOM    375  O   ASP A  47       7.172  23.498   5.147  1.00 11.08           O  
ANISOU  375  O   ASP A  47      827   1589   1791    -86    -85    223       O  
ATOM    376  CB  ASP A  47       7.446  25.984   3.594  1.00 15.24           C  
ANISOU  376  CB  ASP A  47     1997   1887   1905   -337   -188    293       C  
ATOM    377  CG  ASP A  47       8.063  26.839   2.521  1.00 19.64           C  
ANISOU  377  CG  ASP A  47     2420   2371   2670   -532   -321    320       C  
ATOM    378  OD1 ASP A  47       8.580  26.284   1.543  1.00 26.10           O  
ANISOU  378  OD1 ASP A  47     3088   3825   3001   -532    572    485       O  
ATOM    379  OD2 ASP A  47       8.025  28.078   2.693  1.00 27.47           O1-
ANISOU  379  OD2 ASP A  47     4156   2626   3653   -684   -477    402       O1-
ATOM    380  N   VAL A  48       5.100  23.530   4.297  1.00 10.42           N  
ANISOU  380  N   VAL A  48     1344   1236   1376     15   -136    190       N  
ATOM    381  CA  VAL A  48       4.468  22.904   5.485  1.00  8.72           C  
ANISOU  381  CA  VAL A  48      742   1185   1384   -246   -101     64       C  
ATOM    382  C   VAL A  48       4.390  21.408   5.295  1.00  9.78           C  
ANISOU  382  C   VAL A  48     1034   1322   1359   -142   -121    -44       C  
ATOM    383  O   VAL A  48       3.717  20.928   4.381  1.00 10.02           O  
ANISOU  383  O   VAL A  48     1116   1286   1405      2   -233     74       O  
ATOM    384  CB  VAL A  48       3.105  23.507   5.807  1.00 10.03           C  
ANISOU  384  CB  VAL A  48      889   1318   1603     16    -66    163       C  
ATOM    385  CG1 VAL A  48       2.580  22.886   7.122  1.00 12.12           C  
ANISOU  385  CG1 VAL A  48     1753   1241   1609     -9    155     64       C  
ATOM    386  CG2 VAL A  48       3.152  25.042   5.961  1.00 13.09           C  
ANISOU  386  CG2 VAL A  48     1830   1210   1933    316     -9    -22       C  
ATOM    387  N   ILE A  49       5.027  20.673   6.201  1.00  8.42           N  
ANISOU  387  N   ILE A  49      830   1076   1291   -211   -130    -23       N  
ATOM    388  CA  ILE A  49       4.939  19.187   6.252  1.00  7.84           C  
ANISOU  388  CA  ILE A  49      376   1146   1454   -324     77      5       C  
ATOM    389  C   ILE A  49       3.956  18.835   7.344  1.00  7.70           C  
ANISOU  389  C   ILE A  49      262   1181   1480    -94    -16    144       C  
ATOM    390  O   ILE A  49       3.967  19.434   8.440  1.00  8.94           O  
ANISOU  390  O   ILE A  49      829   1181   1383   -176    -19    -54       O  
ATOM    391  CB  ILE A  49       6.336  18.567   6.516  1.00  8.21           C  
ANISOU  391  CB  ILE A  49      284   1266   1570   -175     21     66       C  
ATOM    392  CG1 ILE A  49       7.337  19.054   5.474  1.00 10.25           C  
ANISOU  392  CG1 ILE A  49      716   1533   1645     12    136    -93       C  
ATOM    393  CG2 ILE A  49       6.249  17.035   6.610  1.00 10.89           C  
ANISOU  393  CG2 ILE A  49     1339   1122   1676    111   -142     92       C  
ATOM    394  CD1 ILE A  49       8.795  18.733   5.878  1.00 15.19           C  
ANISOU  394  CD1 ILE A  49      777   2499   2496   -421    393    297       C  
ATOM    395  N   THR A  50       3.028  17.923   7.063  1.00  8.20           N  
ANISOU  395  N   THR A  50      632   1142   1341   -126     59     65       N  
ATOM    396  CA  THR A  50       2.052  17.385   8.033  1.00  9.20           C  
ANISOU  396  CA  THR A  50      895   1203   1396   -251     76     65       C  
ATOM    397  C   THR A  50       2.336  15.885   8.212  1.00  9.04           C  
ANISOU  397  C   THR A  50      781   1220   1430    -62      8    -20       C  
ATOM    398  O   THR A  50       2.415  15.131   7.238  1.00  9.47           O  
ANISOU  398  O   THR A  50      978   1169   1448    -93      1    -28       O  
ATOM    399  CB  THR A  50       0.576  17.691   7.645  1.00  8.79           C  
ANISOU  399  CB  THR A  50      387   1384   1568   -217    -84     21       C  
ATOM    400  CG2 THR A  50      -0.330  17.126   8.652  1.00 10.85           C  
ANISOU  400  CG2 THR A  50      632   1681   1809   -292     47    -43       C  
ATOM    401  OG1 THR A  50       0.453  19.107   7.552  1.00 11.83           O  
ANISOU  401  OG1 THR A  50     1446   1303   1745     65   -230     18       O  
ATOM    402  N   ILE A  51       2.454  15.459   9.472  1.00  8.71           N  
ANISOU  402  N   ILE A  51      805   1142   1361    -95      0    -47       N  
ATOM    403  CA  ILE A  51       2.597  14.028   9.831  1.00  7.99           C  
ANISOU  403  CA  ILE A  51      323   1091   1620   -197    183    -12       C  
ATOM    404  C   ILE A  51       1.430  13.709  10.762  1.00  8.60           C  
ANISOU  404  C   ILE A  51      302   1280   1683   -201     90    126       C  
ATOM    405  O   ILE A  51       1.338  14.264  11.883  1.00 10.05           O  
ANISOU  405  O   ILE A  51     1162   1161   1495     36    164    -79       O  
ATOM    406  CB  ILE A  51       3.937  13.726  10.461  1.00  9.09           C  
ANISOU  406  CB  ILE A  51      272   1391   1790    132     78     45       C  
ATOM    407  CG1 ILE A  51       5.096  14.063   9.575  1.00  9.64           C  
ANISOU  407  CG1 ILE A  51      287   1397   1978    -81    233   -154       C  
ATOM    408  CG2 ILE A  51       3.912  12.211  10.834  1.00 11.77           C  
ANISOU  408  CG2 ILE A  51     1519   1226   1726      5    -54    213       C  
ATOM    409  CD1 ILE A  51       6.418  13.824  10.141  1.00 12.18           C  
ANISOU  409  CD1 ILE A  51      259   2020   2348    -55    103   -294       C  
ATOM    410  N  ALYS A  52       0.502  12.874  10.295  0.50  9.58           N  
ANISOU  410  N  ALYS A  52      383   1467   1787   -341    244    -56       N  
ATOM    411  N  BLYS A  52       0.485  12.896  10.310  0.50  9.43           N  
ANISOU  411  N  BLYS A  52      377   1426   1778   -271    316    -48       N  
ATOM    412  CA ALYS A  52      -0.707  12.446  10.964  0.50 10.26           C  
ANISOU  412  CA ALYS A  52      498   1492   1908   -538    202   -156       C  
ATOM    413  CA BLYS A  52      -0.514  12.324  11.152  0.50  9.98           C  
ANISOU  413  CA BLYS A  52      443   1407   1941   -324    431    -88       C  
ATOM    414  C  ALYS A  52      -0.545  10.937  11.365  0.50 11.02           C  
ANISOU  414  C  ALYS A  52      946   1412   1828   -432    305   -151       C  
ATOM    415  C  BLYS A  52      -0.161  10.915  11.511  0.50 10.77           C  
ANISOU  415  C  BLYS A  52      846   1310   1934   -371    503    -44       C  
ATOM    416  O  ALYS A  52      -0.320  10.119  10.504  0.50  9.29           O  
ANISOU  416  O  ALYS A  52      491   1463   1573   -531    130   -123       O  
ATOM    417  O  BLYS A  52       0.551  10.169  10.813  0.50 10.39           O  
ANISOU  417  O  BLYS A  52      562   1363   2022   -510    388    -55       O  
ATOM    418  CB ALYS A  52      -1.961  12.643  10.066  0.50 10.77           C  
ANISOU  418  CB ALYS A  52      553   1495   2043   -592    217    -89       C  
ATOM    419  CB BLYS A  52      -1.922  12.314  10.563  0.50 10.50           C  
ANISOU  419  CB BLYS A  52      514   1588   1885   -355    552   -124       C  
ATOM    420  CG ALYS A  52      -3.257  12.328  10.707  0.50 13.54           C  
ANISOU  420  CG ALYS A  52      560   2111   2473   -722    229     27       C  
ATOM    421  CG BLYS A  52      -2.303  13.619   9.920  0.50 12.20           C  
ANISOU  421  CG BLYS A  52      305   1977   2354   -228    206     36       C  
ATOM    422  CD ALYS A  52      -4.442  12.624   9.709  0.50 17.29           C  
ANISOU  422  CD ALYS A  52     1133   2523   2913   -733    -60    230       C  
ATOM    423  CD BLYS A  52      -3.571  13.570   9.222  0.50 12.45           C  
ANISOU  423  CD BLYS A  52      283   1904   2541   -184    153    -24       C  
ATOM    424  CE ALYS A  52      -5.847  12.622  10.334  0.50 19.75           C  
ANISOU  424  CE ALYS A  52     1576   2889   3039   -270   -118    232       C  
ATOM    425  CE BLYS A  52      -3.783  14.883   8.420  0.50 18.21           C  
ANISOU  425  CE BLYS A  52     1656   2380   2880    -65     58    312       C  
ATOM    426  NZ ALYS A  52      -6.866  13.257   9.460  0.50 22.56           N1+
ANISOU  426  NZ ALYS A  52     1964   3191   3413    -18   -258    314       N1+
ATOM    427  NZ BLYS A  52      -3.141  14.864   7.064  0.50 20.04           N1+
ANISOU  427  NZ BLYS A  52     2182   2574   2858     15    152    634       N1+
ATOM    428  N   SER A  53      -0.687  10.580  12.655  1.00 12.37           N  
ANISOU  428  N   SER A  53     1614   1286   1797   -325    414      7       N  
ATOM    429  CA  SER A  53      -0.717   9.195  13.107  1.00 13.55           C  
ANISOU  429  CA  SER A  53     1844   1407   1897   -430    490     48       C  
ATOM    430  C   SER A  53      -2.149   8.856  13.539  1.00 13.51           C  
ANISOU  430  C   SER A  53     1931   1497   1703   -413    593     33       C  
ATOM    431  O   SER A  53      -2.721   9.508  14.391  1.00 14.72           O  
ANISOU  431  O   SER A  53     1887   1647   2058   -505    787   -173       O  
ATOM    432  CB  SER A  53       0.245   9.030  14.275  1.00 14.38           C  
ANISOU  432  CB  SER A  53     1670   1531   2262   -248    587     22       C  
ATOM    433  OG  SER A  53       0.266   7.685  14.774  1.00 17.91           O  
ANISOU  433  OG  SER A  53     2777   1648   2378   -403    129    202       O  
ATOM    434  N   GLU A  54      -2.687   7.851  12.890  1.00 13.48           N  
ANISOU  434  N   GLU A  54     1790   1687   1645   -373    362    -72       N  
ATOM    435  CA  GLU A  54      -4.048   7.356  13.198  1.00 14.29           C  
ANISOU  435  CA  GLU A  54     1680   1830   1918   -304    252     37       C  
ATOM    436  C   GLU A  54      -3.914   6.035  13.873  1.00 13.95           C  
ANISOU  436  C   GLU A  54     1413   2093   1790   -213    227    139       C  
ATOM    437  O   GLU A  54      -3.345   5.095  13.298  1.00 13.38           O  
ANISOU  437  O   GLU A  54     1566   1765   1752   -182    359    280       O  
ATOM    438  CB  GLU A  54      -4.820   7.221  11.903  1.00 16.95           C  
ANISOU  438  CB  GLU A  54     2245   2009   2185   -140    164    110       C  
ATOM    439  CG  GLU A  54      -5.031   8.521  11.175  1.00 22.04           C  
ANISOU  439  CG  GLU A  54     2900   2712   2761    -61    112    298       C  
ATOM    440  CD  GLU A  54      -6.065   8.386  10.095  1.00 28.65           C  
ANISOU  440  CD  GLU A  54     3754   3724   3406    105   -263    157       C  
ATOM    441  OE1 GLU A  54      -5.980   7.430   9.292  1.00 30.18           O  
ANISOU  441  OE1 GLU A  54     4167   3922   3377    -82   -667   -145       O  
ATOM    442  OE2 GLU A  54      -6.985   9.230  10.061  1.00 36.17           O1-
ANISOU  442  OE2 GLU A  54     4654   4327   4761    669   -196    149       O1-
ATOM    443  N  ASER A  55      -4.333   5.915  15.123  0.50 14.56           N  
ANISOU  443  N  ASER A  55     1490   2209   1833   -120    192    120       N  
ATOM    444  N  BSER A  55      -4.398   5.956  15.106  0.50 15.35           N  
ANISOU  444  N  BSER A  55     1576   2347   1908    -96    158     91       N  
ATOM    445  CA ASER A  55      -4.286   4.576  15.755  0.50 15.85           C  
ANISOU  445  CA ASER A  55     1832   2274   1914     49    297    234       C  
ATOM    446  CA BSER A  55      -4.153   4.764  15.931  0.50 18.05           C  
ANISOU  446  CA BSER A  55     2199   2533   2123     69    227    130       C  
ATOM    447  C  ASER A  55      -5.409   4.401  16.709  0.50 16.59           C  
ANISOU  447  C  ASER A  55     2208   2223   1873     41    403    188       C  
ATOM    448  C  BSER A  55      -5.262   4.495  16.893  0.50 17.81           C  
ANISOU  448  C  BSER A  55     2399   2374   1992     98    328    141       C  
ATOM    449  O  ASER A  55      -6.250   5.249  16.929  0.50 15.92           O  
ANISOU  449  O  ASER A  55     2086   2104   1857    218    486    470       O  
ATOM    450  O  BSER A  55      -5.914   5.420  17.373  0.50 16.46           O  
ANISOU  450  O  BSER A  55     2358   2041   1855    323    261    327       O  
ATOM    451  CB ASER A  55      -2.934   4.114  16.420  0.50 16.30           C  
ANISOU  451  CB ASER A  55     1972   2159   2059     -2    241    122       C  
ATOM    452  CB BSER A  55      -2.871   4.843  16.752  0.50 20.28           C  
ANISOU  452  CB BSER A  55     2343   2943   2419     29    304     63       C  
ATOM    453  OG ASER A  55      -2.684   4.615  17.747  0.50 10.01           O  
ANISOU  453  OG ASER A  55     1007   1546   1249     29    241    702       O  
ATOM    454  OG BSER A  55      -2.449   6.144  16.925  0.50 24.35           O  
ANISOU  454  OG BSER A  55     3390   3152   2710     35   -147    -95       O  
ATOM    455  N   THR A  56      -5.392   3.224  17.248  1.00 17.34           N  
ANISOU  455  N   THR A  56     2553   2028   2008    208    292     63       N  
ATOM    456  CA  THR A  56      -6.317   2.816  18.249  1.00 18.09           C  
ANISOU  456  CA  THR A  56     2760   2010   2103   -117    354    -41       C  
ATOM    457  C   THR A  56      -5.934   3.369  19.601  1.00 17.62           C  
ANISOU  457  C   THR A  56     2787   1934   1974   -123    485    -66       C  
ATOM    458  O   THR A  56      -6.792   3.393  20.469  1.00 20.53           O  
ANISOU  458  O   THR A  56     3146   2608   2046   -681    694   -191       O  
ATOM    459  CB  THR A  56      -6.272   1.266  18.305  1.00 20.19           C  
ANISOU  459  CB  THR A  56     2909   2175   2588    -97    201   -387       C  
ATOM    460  CG2 THR A  56      -7.093   0.708  17.102  1.00 20.87           C  
ANISOU  460  CG2 THR A  56     3363   2054   2511      0   -239   -407       C  
ATOM    461  OG1 THR A  56      -4.873   0.836  18.239  1.00 19.99           O  
ANISOU  461  OG1 THR A  56     3127   1932   2533    -52     99    -99       O  
ATOM    462  N   PHE A  57      -4.671   3.722  19.814  1.00 16.32           N  
ANISOU  462  N   PHE A  57     2729   1649   1822    -14    462     89       N  
ATOM    463  CA  PHE A  57      -4.217   4.356  21.056  1.00 16.82           C  
ANISOU  463  CA  PHE A  57     2646   1789   1954    -25    466    221       C  
ATOM    464  C   PHE A  57      -4.588   5.827  21.061  1.00 16.42           C  
ANISOU  464  C   PHE A  57     2482   1713   2043    -26    513    203       C  
ATOM    465  O   PHE A  57      -5.497   6.245  21.751  1.00 18.82           O  
ANISOU  465  O   PHE A  57     2682   1886   2581    -19    815    280       O  
ATOM    466  CB  PHE A  57      -2.718   4.104  21.293  1.00 17.84           C  
ANISOU  466  CB  PHE A  57     3021   1825   1929     73    269    295       C  
ATOM    467  CG  PHE A  57      -2.105   4.930  22.380  1.00 20.38           C  
ANISOU  467  CG  PHE A  57     3223   1882   2638    182    -39    407       C  
ATOM    468  CD1 PHE A  57      -2.642   4.961  23.639  1.00 21.99           C  
ANISOU  468  CD1 PHE A  57     3512   2173   2667    172   -257     25       C  
ATOM    469  CD2 PHE A  57      -0.955   5.657  22.133  1.00 19.58           C  
ANISOU  469  CD2 PHE A  57     2831   1941   2664    376     77    307       C  
ATOM    470  CE1 PHE A  57      -2.043   5.753  24.649  1.00 23.48           C  
ANISOU  470  CE1 PHE A  57     3445   2568   2908   -289   -528    215       C  
ATOM    471  CE2 PHE A  57      -0.356   6.442  23.153  1.00 22.53           C  
ANISOU  471  CE2 PHE A  57     3118   2370   3073    478   -358    453       C  
ATOM    472  CZ  PHE A  57      -0.920   6.479  24.384  1.00 22.86           C  
ANISOU  472  CZ  PHE A  57     3366   2383   2935    239   -498    464       C  
ATOM    473  N  ALYS A  58      -3.901   6.578  20.227  0.50 17.18           N  
ANISOU  473  N  ALYS A  58     2377   1831   2319     93    670    220       N  
ATOM    474  N  BLYS A  58      -3.847   6.691  20.364  0.50 14.94           N  
ANISOU  474  N  BLYS A  58     2128   1562   1987     69    660    188       N  
ATOM    475  CA ALYS A  58      -4.181   7.961  20.065  0.50 17.21           C  
ANISOU  475  CA ALYS A  58     2213   1926   2398     79    519    146       C  
ATOM    476  CA BLYS A  58      -4.091   8.160  20.401  0.50 13.60           C  
ANISOU  476  CA BLYS A  58     1696   1543   1926     23    456     41       C  
ATOM    477  C  ALYS A  58      -4.092   8.281  18.618  0.50 16.86           C  
ANISOU  477  C  ALYS A  58     2117   1850   2436    107    545    155       C  
ATOM    478  C  BLYS A  58      -3.679   8.767  19.066  0.50 12.76           C  
ANISOU  478  C  BLYS A  58     1503   1366   1977    -58    517    110       C  
ATOM    479  O  ALYS A  58      -3.608   7.541  17.745  0.50 17.76           O  
ANISOU  479  O  ALYS A  58     2370   1940   2437    -41    667    218       O  
ATOM    480  O  BLYS A  58      -2.487   8.579  18.693  0.50 11.55           O  
ANISOU  480  O  BLYS A  58     1277   1365   1747    260    442    110       O  
ATOM    481  CB ALYS A  58      -3.174   8.816  20.825  0.50 17.58           C  
ANISOU  481  CB ALYS A  58     2097   2023   2558     76    524     82       C  
ATOM    482  CB BLYS A  58      -3.262   8.798  21.525  0.50 12.69           C  
ANISOU  482  CB BLYS A  58     1421   1641   1760   -207    544     90       C  
ATOM    483  CG ALYS A  58      -3.239   8.654  22.334  0.50 20.12           C  
ANISOU  483  CG ALYS A  58     2440   2431   2770     31     97     48       C  
ATOM    484  CG BLYS A  58      -3.391  10.313  21.600  0.50 14.41           C  
ANISOU  484  CG BLYS A  58     1471   1960   2043    -56    346    -72       C  
ATOM    485  CD ALYS A  58      -4.529   9.247  22.858  0.50 22.92           C  
ANISOU  485  CD ALYS A  58     2684   3097   2928    -18    128   -178       C  
ATOM    486  CD BLYS A  58      -4.713  10.780  22.026  0.50 16.70           C  
ANISOU  486  CD BLYS A  58     1453   2416   2476   -276    147   -143       C  
ATOM    487  CE ALYS A  58      -4.937   8.705  24.218  0.50 23.55           C  
ANISOU  487  CE ALYS A  58     2848   3084   3015   -212     12    -47       C  
ATOM    488  CE BLYS A  58      -4.803  12.264  21.783  0.50 20.00           C  
ANISOU  488  CE BLYS A  58     2222   2454   2921   -310    176    -24       C  
ATOM    489  NZ ALYS A  58      -6.363   9.073  24.491  0.50 25.39           N1+
ANISOU  489  NZ ALYS A  58     2971   3339   3334   -115    -51     19       N1+
ATOM    490  NZ BLYS A  58      -5.470  12.556  20.465  0.50 19.64           N1+
ANISOU  490  NZ BLYS A  58     2133   2256   3073   -303    -88     53       N1+
ATOM    491  N   ASN A  59      -4.667   9.400  18.352  1.00 13.54           N  
ANISOU  491  N   ASN A  59     1481   1485   2176     32    627    145       N  
ATOM    492  CA  ASN A  59      -4.393  10.060  17.072  1.00 13.91           C  
ANISOU  492  CA  ASN A  59     1536   1524   2225   -212    647     85       C  
ATOM    493  C   ASN A  59      -3.566  11.300  17.362  1.00 14.28           C  
ANISOU  493  C   ASN A  59     1819   1486   2119   -109    660      5       C  
ATOM    494  O   ASN A  59      -3.799  11.997  18.371  1.00 18.10           O  
ANISOU  494  O   ASN A  59     2629   1680   2565   -110   1138   -183       O  
ATOM    495  CB  ASN A  59      -5.713  10.427  16.368  1.00 15.42           C  
ANISOU  495  CB  ASN A  59     1775   1878   2204    -94    569    289       C  
ATOM    496  CG  ASN A  59      -6.615   9.255  16.075  1.00 16.26           C  
ANISOU  496  CG  ASN A  59      929   2668   2581   -338     -9     33       C  
ATOM    497  ND2 ASN A  59      -7.923   9.429  16.342  1.00 24.83           N  
ANISOU  497  ND2 ASN A  59     1428   4021   3984    -36   -282    129       N  
ATOM    498  OD1 ASN A  59      -6.199   8.217  15.601  1.00 17.11           O  
ANISOU  498  OD1 ASN A  59     1647   2219   2632     58    470    397       O  
ATOM    499  N   THR A  60      -2.597  11.578  16.505  1.00 13.55           N  
ANISOU  499  N   THR A  60     1817   1470   1859   -239    694     73       N  
ATOM    500  CA  THR A  60      -1.831  12.792  16.606  1.00 13.19           C  
ANISOU  500  CA  THR A  60     1785   1340   1886    -30    576     55       C  
ATOM    501  C   THR A  60      -1.707  13.415  15.222  1.00 12.66           C  
ANISOU  501  C   THR A  60     1620   1389   1802    -97    402     52       C  
ATOM    502  O   THR A  60      -1.802  12.739  14.194  1.00 11.69           O  
ANISOU  502  O   THR A  60     1217   1378   1844   -101    379    -37       O  
ATOM    503  CB  THR A  60      -0.467  12.561  17.192  1.00 13.34           C  
ANISOU  503  CB  THR A  60     1853   1356   1858    -34    438    113       C  
ATOM    504  CG2 THR A  60      -0.517  11.970  18.604  1.00 15.48           C  
ANISOU  504  CG2 THR A  60     1808   2085   1987     97    334    315       C  
ATOM    505  OG1 THR A  60       0.299  11.699  16.359  1.00 13.96           O  
ANISOU  505  OG1 THR A  60     1748   1533   2021    153    299     96       O  
ATOM    506  N   GLU A  61      -1.434  14.704  15.206  1.00 12.24           N  
ANISOU  506  N   GLU A  61     1689   1204   1755    -26    452    -19       N  
ATOM    507  CA  GLU A  61      -1.096  15.409  13.990  1.00 11.57           C  
ANISOU  507  CA  GLU A  61     1177   1342   1874    -74    307    -22       C  
ATOM    508  C   GLU A  61      -0.186  16.549  14.313  1.00 11.59           C  
ANISOU  508  C   GLU A  61     1527   1264   1609   -173    349   -111       C  
ATOM    509  O   GLU A  61      -0.452  17.359  15.210  1.00 13.98           O  
ANISOU  509  O   GLU A  61     1809   1535   1967   -138    601   -183       O  
ATOM    510  CB  GLU A  61      -2.345  15.913  13.322  1.00 13.24           C  
ANISOU  510  CB  GLU A  61     1314   1508   2208   -434    133     62       C  
ATOM    511  CG  GLU A  61      -2.084  16.666  12.039  1.00 16.96           C  
ANISOU  511  CG  GLU A  61     1294   2570   2579   -401     -4    413       C  
ATOM    512  CD  GLU A  61      -3.394  17.147  11.445  1.00 22.23           C  
ANISOU  512  CD  GLU A  61     1209   3720   3513   -653    648    755       C  
ATOM    513  OE1 GLU A  61      -3.408  18.231  10.823  1.00 29.51           O  
ANISOU  513  OE1 GLU A  61     2668   4401   4141   -198   -189   1252       O  
ATOM    514  OE2 GLU A  61      -4.433  16.524  11.675  1.00 27.01           O1-
ANISOU  514  OE2 GLU A  61     1177   4934   4150   -431   -209    817       O1-
ATOM    515  N   ILE A  62       0.886  16.640  13.544  1.00 10.42           N  
ANISOU  515  N   ILE A  62     1364   1195   1398   -105    208     15       N  
ATOM    516  CA  ILE A  62       1.814  17.766  13.636  1.00 10.31           C  
ANISOU  516  CA  ILE A  62     1367   1190   1361   -199    185    -70       C  
ATOM    517  C   ILE A  62       2.000  18.377  12.240  1.00  9.70           C  
ANISOU  517  C   ILE A  62     1098   1202   1384   -234     35    127       C  
ATOM    518  O   ILE A  62       2.094  17.644  11.248  1.00 10.99           O  
ANISOU  518  O   ILE A  62     1701   1230   1243   -144    138     -7       O  
ATOM    519  CB  ILE A  62       3.179  17.409  14.291  1.00 10.10           C  
ANISOU  519  CB  ILE A  62     1037   1328   1470   -187     53    143       C  
ATOM    520  CG1 ILE A  62       3.983  16.329  13.511  1.00 12.03           C  
ANISOU  520  CG1 ILE A  62     1495   1596   1478   -381    -12     21       C  
ATOM    521  CG2 ILE A  62       2.957  16.977  15.742  1.00 13.59           C  
ANISOU  521  CG2 ILE A  62     2058   1622   1482    156     63    200       C  
ATOM    522  CD1 ILE A  62       5.383  16.082  13.989  1.00 12.48           C  
ANISOU  522  CD1 ILE A  62      838   1887   2015     51   -422     37       C  
ATOM    523  N   SER A  63       1.997  19.682  12.178  1.00  8.72           N  
ANISOU  523  N   SER A  63      793   1137   1382    -29    119    -15       N  
ATOM    524  CA  SER A  63       2.408  20.450  10.991  1.00  8.57           C  
ANISOU  524  CA  SER A  63      872   1089   1295   -113     81    101       C  
ATOM    525  C   SER A  63       3.545  21.389  11.320  1.00  8.22           C  
ANISOU  525  C   SER A  63      574   1074   1474    -33    -54     95       C  
ATOM    526  O   SER A  63       3.521  22.003  12.379  1.00  9.77           O  
ANISOU  526  O   SER A  63      882   1314   1517   -188     58   -195       O  
ATOM    527  CB  SER A  63       1.217  21.221  10.388  1.00  9.79           C  
ANISOU  527  CB  SER A  63     1153   1193   1374     27    -43    -40       C  
ATOM    528  OG  SER A  63       0.193  20.359   9.966  1.00 12.08           O  
ANISOU  528  OG  SER A  63     1304   1479   1806     35   -425    -47       O  
ATOM    529  N   PHE A  64       4.507  21.501  10.441  1.00  8.15           N  
ANISOU  529  N   PHE A  64      876    934   1287     35     35     -7       N  
ATOM    530  CA  PHE A  64       5.681  22.238  10.741  1.00  8.98           C  
ANISOU  530  CA  PHE A  64      995   1047   1367   -200      0    -29       C  
ATOM    531  C   PHE A  64       6.416  22.649   9.463  1.00  7.69           C  
ANISOU  531  C   PHE A  64      509   1052   1359   -114     68    158       C  
ATOM    532  O   PHE A  64       6.210  22.089   8.405  1.00  9.10           O  
ANISOU  532  O   PHE A  64      956   1278   1222     -6    -57     35       O  
ATOM    533  CB  PHE A  64       6.619  21.367  11.658  1.00 10.08           C  
ANISOU  533  CB  PHE A  64     1220   1229   1379    -51    -51    -63       C  
ATOM    534  CG  PHE A  64       6.993  20.042  11.044  1.00  8.95           C  
ANISOU  534  CG  PHE A  64      307   1536   1556    -79   -119     98       C  
ATOM    535  CD1 PHE A  64       6.150  18.961  11.207  1.00  9.45           C  
ANISOU  535  CD1 PHE A  64      720   1484   1384   -313    -97    159       C  
ATOM    536  CD2 PHE A  64       8.123  19.903  10.317  1.00  9.20           C  
ANISOU  536  CD2 PHE A  64      429   1297   1767   -240     28     96       C  
ATOM    537  CE1 PHE A  64       6.409  17.765  10.533  1.00  9.83           C  
ANISOU  537  CE1 PHE A  64      299   1529   1907    -34    -72    114       C  
ATOM    538  CE2 PHE A  64       8.411  18.691   9.705  1.00 11.18           C  
ANISOU  538  CE2 PHE A  64      929   1946   1371    -38    181     68       C  
ATOM    539  CZ  PHE A  64       7.519  17.658   9.870  1.00  9.64           C  
ANISOU  539  CZ  PHE A  64      394   1473   1794    197   -417    -47       C  
ATOM    540  N   ILE A  65       7.360  23.531   9.645  1.00  7.88           N  
ANISOU  540  N   ILE A  65      409   1183   1402   -110      1      8       N  
ATOM    541  CA  ILE A  65       8.318  23.985   8.668  1.00  8.17           C  
ANISOU  541  CA  ILE A  65      605    950   1546    -74    181     88       C  
ATOM    542  C   ILE A  65       9.689  23.568   9.145  1.00  8.93           C  
ANISOU  542  C   ILE A  65      881   1008   1504    -84    162     93       C  
ATOM    543  O   ILE A  65       9.989  23.682  10.322  1.00  8.38           O  
ANISOU  543  O   ILE A  65      691   1059   1435   -221    -87      7       O  
ATOM    544  CB  ILE A  65       8.199  25.516   8.437  1.00  9.58           C  
ANISOU  544  CB  ILE A  65      905   1084   1649    -64    -72    -44       C  
ATOM    545  CG1 ILE A  65       6.816  25.859   7.890  1.00 10.77           C  
ANISOU  545  CG1 ILE A  65      962   1263   1864    189   -203    268       C  
ATOM    546  CG2 ILE A  65       9.342  25.980   7.552  1.00 11.08           C  
ANISOU  546  CG2 ILE A  65     1096   1142   1969   -170      0    119       C  
ATOM    547  CD1 ILE A  65       6.547  27.395   7.823  1.00 14.05           C  
ANISOU  547  CD1 ILE A  65     1206   1374   2758     95   -246    278       C  
ATOM    548  N   LEU A  66      10.490  23.004   8.271  1.00  8.20           N  
ANISOU  548  N   LEU A  66      610    993   1511     72     97     -2       N  
ATOM    549  CA  LEU A  66      11.752  22.511   8.645  1.00  7.73           C  
ANISOU  549  CA  LEU A  66      588    827   1523    132    187    155       C  
ATOM    550  C   LEU A  66      12.608  23.606   9.304  1.00  9.53           C  
ANISOU  550  C   LEU A  66      944   1095   1581    -33     44    115       C  
ATOM    551  O   LEU A  66      12.679  24.725   8.785  1.00 10.13           O  
ANISOU  551  O   LEU A  66     1087   1177   1584     99     70    156       O  
ATOM    552  CB  LEU A  66      12.519  21.913   7.419  1.00  9.53           C  
ANISOU  552  CB  LEU A  66      598   1311   1713     56     45     49       C  
ATOM    553  CG  LEU A  66      11.914  20.659   6.802  1.00 11.29           C  
ANISOU  553  CG  LEU A  66     1390   1270   1630    -85    -53   -126       C  
ATOM    554  CD1 LEU A  66      12.524  20.372   5.407  1.00 14.48           C  
ANISOU  554  CD1 LEU A  66     1704   1775   2021    255    470   -353       C  
ATOM    555  CD2 LEU A  66      12.039  19.521   7.738  1.00 12.49           C  
ANISOU  555  CD2 LEU A  66     1588   1167   1990   -281   -114    -85       C  
ATOM    556  N   GLY A  67      13.291  23.264  10.398  1.00  9.00           N  
ANISOU  556  N   GLY A  67      847   1031   1539    -22     57    193       N  
ATOM    557  CA  GLY A  67      14.120  24.175  11.124  1.00  9.96           C  
ANISOU  557  CA  GLY A  67     1217   1110   1458    -50     37     -6       C  
ATOM    558  C   GLY A  67      13.450  25.083  12.110  1.00  8.99           C  
ANISOU  558  C   GLY A  67      526   1194   1695   -194    183     64       C  
ATOM    559  O   GLY A  67      14.146  25.836  12.806  1.00  9.62           O  
ANISOU  559  O   GLY A  67      712   1119   1823   -142    -57    -89       O  
ATOM    560  N   GLN A  68      12.132  25.064  12.161  1.00  8.61           N  
ANISOU  560  N   GLN A  68      739    923   1608   -190     91    -91       N  
ATOM    561  CA  GLN A  68      11.304  26.044  12.900  1.00  9.37           C  
ANISOU  561  CA  GLN A  68      988    987   1585   -129     60    -67       C  
ATOM    562  C   GLN A  68      10.573  25.360  14.059  1.00  9.12           C  
ANISOU  562  C   GLN A  68      805    968   1691   -195      9    -10       C  
ATOM    563  O   GLN A  68       9.689  24.532  13.879  1.00  9.37           O  
ANISOU  563  O   GLN A  68      862   1027   1670   -207     12    -63       O  
ATOM    564  CB  GLN A  68      10.316  26.750  11.982  1.00 10.47           C  
ANISOU  564  CB  GLN A  68     1351    925   1701    -59    -33   -236       C  
ATOM    565  CG  GLN A  68      11.130  27.404  10.833  1.00 12.59           C  
ANISOU  565  CG  GLN A  68     1490   1475   1817   -431   -440     52       C  
ATOM    566  CD  GLN A  68      10.432  28.427  10.039  1.00 15.00           C  
ANISOU  566  CD  GLN A  68     1894   1319   2486   -289   -666    -66       C  
ATOM    567  NE2 GLN A  68      11.169  28.981   9.060  1.00 15.42           N  
ANISOU  567  NE2 GLN A  68     2399   1196   2264   -206   -510    396       N  
ATOM    568  OE1 GLN A  68       9.239  28.772  10.274  1.00 17.48           O  
ANISOU  568  OE1 GLN A  68     1848   1609   3182      3   -938    149       O  
ATOM    569  N  AGLU A  69      10.965  25.721  15.280  0.50  8.99           N  
ANISOU  569  N  AGLU A  69     1121    861   1431   -102     32    -43       N  
ATOM    570  N  BGLU A  69      11.007  25.731  15.288  0.50  9.85           N  
ANISOU  570  N  BGLU A  69     1148   1100   1493   -122     81      5       N  
ATOM    571  CA AGLU A  69      10.453  24.986  16.429  0.50  9.33           C  
ANISOU  571  CA AGLU A  69     1194    875   1475   -231      3   -104       C  
ATOM    572  CA BGLU A  69      10.443  25.188  16.558  0.50 11.45           C  
ANISOU  572  CA BGLU A  69     1328   1345   1678   -126    100     -5       C  
ATOM    573  C  AGLU A  69       8.973  25.255  16.704  0.50  9.46           C  
ANISOU  573  C  AGLU A  69     1163   1090   1341     40     55   -159       C  
ATOM    574  C  BGLU A  69       8.935  25.238  16.569  0.50 10.05           C  
ANISOU  574  C  BGLU A  69     1185   1287   1344     91    164   -100       C  
ATOM    575  O  AGLU A  69       8.439  26.362  16.501  0.50  8.09           O  
ANISOU  575  O  AGLU A  69      929    942   1202    186   -171   -194       O  
ATOM    576  O  BGLU A  69       8.360  26.214  16.030  0.50  7.53           O  
ANISOU  576  O  BGLU A  69      665    946   1249    142   -135   -292       O  
ATOM    577  CB AGLU A  69      11.341  25.336  17.639  0.50  9.54           C  
ANISOU  577  CB AGLU A  69     1269    898   1457    -82   -109     86       C  
ATOM    578  CB BGLU A  69      10.986  26.021  17.775  0.50 12.11           C  
ANISOU  578  CB BGLU A  69     1405   1711   1484   -108    158    159       C  
ATOM    579  CG AGLU A  69      10.740  25.075  19.078  0.50 12.46           C  
ANISOU  579  CG AGLU A  69     1806   1245   1684   -375   -123    249       C  
ATOM    580  CG BGLU A  69      10.285  27.325  18.010  0.50 17.91           C  
ANISOU  580  CG BGLU A  69     2300   2244   2259    -51     67   -138       C  
ATOM    581  CD AGLU A  69      11.558  25.709  20.172  0.50 19.19           C  
ANISOU  581  CD AGLU A  69     2843   2465   1980   -462   -372    358       C  
ATOM    582  CD BGLU A  69      10.764  28.129  19.228  0.50 19.00           C  
ANISOU  582  CD BGLU A  69     1765   2737   2717    251   -159   -321       C  
ATOM    583  OE1AGLU A  69      11.359  26.907  20.455  0.50 22.75           O  
ANISOU  583  OE1AGLU A  69     3457   2676   2510  -1141   -573    -38       O  
ATOM    584  OE1BGLU A  69      11.731  27.729  19.900  0.50 16.49           O  
ANISOU  584  OE1BGLU A  69     1157   2311   2794     97   -429    -75       O  
ATOM    585  OE2AGLU A  69      12.386  24.988  20.735  0.50 22.91           O1-
ANISOU  585  OE2AGLU A  69     2795   3499   2411   -808   -711    441       O1-
ATOM    586  OE2BGLU A  69      10.173  29.199  19.489  0.50 24.57           O1-
ANISOU  586  OE2BGLU A  69     3192   2901   3241    599   -187  -1252       O1-
ATOM    587  N   PHE A  70       8.289  24.225  17.191  1.00  9.00           N  
ANISOU  587  N   PHE A  70      849   1137   1433    130     65   -162       N  
ATOM    588  CA  PHE A  70       6.877  24.209  17.449  1.00  8.68           C  
ANISOU  588  CA  PHE A  70      649   1122   1526    227    213    -39       C  
ATOM    589  C   PHE A  70       6.628  23.427  18.725  1.00  9.33           C  
ANISOU  589  C   PHE A  70      901   1020   1624    156    222   -114       C  
ATOM    590  O   PHE A  70       7.401  22.651  19.222  1.00 10.80           O  
ANISOU  590  O   PHE A  70     1284   1244   1575    417    146    168       O  
ATOM    591  CB  PHE A  70       6.130  23.612  16.239  1.00  9.73           C  
ANISOU  591  CB  PHE A  70      969   1318   1410    293    155    -20       C  
ATOM    592  CG  PHE A  70       6.500  22.196  15.895  1.00  8.79           C  
ANISOU  592  CG  PHE A  70      521   1221   1595     97     36     37       C  
ATOM    593  CD1 PHE A  70       7.571  21.925  15.122  1.00  7.57           C  
ANISOU  593  CD1 PHE A  70      277   1072   1524    121    -99    -44       C  
ATOM    594  CD2 PHE A  70       5.709  21.164  16.335  1.00 11.65           C  
ANISOU  594  CD2 PHE A  70     1434   1375   1614     -9    210   -129       C  
ATOM    595  CE1 PHE A  70       7.932  20.611  14.768  1.00  8.56           C  
ANISOU  595  CE1 PHE A  70      459   1355   1436     94     75     35       C  
ATOM    596  CE2 PHE A  70       6.020  19.848  16.007  1.00 12.07           C  
ANISOU  596  CE2 PHE A  70     1506   1419   1659   -247    261      5       C  
ATOM    597  CZ  PHE A  70       7.083  19.578  15.230  1.00 10.88           C  
ANISOU  597  CZ  PHE A  70     1321   1414   1398     -2   -131   -185       C  
ATOM    598  N   ASP A  71       5.443  23.700  19.237  1.00 10.43           N  
ANISOU  598  N   ASP A  71     1063   1157   1743    283     99    245       N  
ATOM    599  CA  ASP A  71       4.871  22.970  20.384  1.00 11.11           C  
ANISOU  599  CA  ASP A  71      988   1497   1736    239    319     99       C  
ATOM    600  C   ASP A  71       4.125  21.730  19.938  1.00 11.85           C  
ANISOU  600  C   ASP A  71     1081   1646   1774    -92    174    257       C  
ATOM    601  O   ASP A  71       3.393  21.732  18.937  1.00 14.10           O  
ANISOU  601  O   ASP A  71     1360   1766   2229    223    210    449       O  
ATOM    602  CB  ASP A  71       3.788  23.834  21.036  1.00 12.52           C  
ANISOU  602  CB  ASP A  71     1287   1689   1780    397    285    245       C  
ATOM    603  CG  ASP A  71       4.320  25.049  21.656  1.00 15.35           C  
ANISOU  603  CG  ASP A  71     1683   2485   1662    411    178   -269       C  
ATOM    604  OD1 ASP A  71       5.271  24.902  22.430  1.00 17.62           O  
ANISOU  604  OD1 ASP A  71     2210   2403   2080    299   -239   -112       O  
ATOM    605  OD2 ASP A  71       3.701  26.139  21.432  1.00 15.76           O1-
ANISOU  605  OD2 ASP A  71     1343   2468   2175    309    -19   -138       O1-
ATOM    606  N   GLU A  72       4.366  20.628  20.664  1.00 12.16           N  
ANISOU  606  N   GLU A  72     1167   1647   1803    -31    121    224       N  
ATOM    607  CA  GLU A  72       3.797  19.336  20.319  1.00 12.62           C  
ANISOU  607  CA  GLU A  72     1171   1681   1939    -62    142    292       C  
ATOM    608  C   GLU A  72       3.304  18.707  21.622  1.00 14.15           C  
ANISOU  608  C   GLU A  72     1667   1674   2033    -45    145    346       C  
ATOM    609  O   GLU A  72       3.948  18.736  22.625  1.00 13.95           O  
ANISOU  609  O   GLU A  72     1506   1902   1889    -81    401    437       O  
ATOM    610  CB  GLU A  72       4.886  18.458  19.649  1.00 12.49           C  
ANISOU  610  CB  GLU A  72     1419   1469   1856   -177    223    216       C  
ATOM    611  CG  GLU A  72       4.485  16.998  19.336  1.00 12.77           C  
ANISOU  611  CG  GLU A  72     1293   1732   1826    -13     38    242       C  
ATOM    612  CD  GLU A  72       5.527  16.195  18.634  1.00 12.41           C  
ANISOU  612  CD  GLU A  72     1377   1581   1757     -6     39    104       C  
ATOM    613  OE1 GLU A  72       6.652  16.639  18.556  1.00 13.72           O  
ANISOU  613  OE1 GLU A  72     1629   1628   1953    -39     98   -169       O  
ATOM    614  OE2 GLU A  72       5.158  15.083  18.191  1.00 16.18           O1-
ANISOU  614  OE2 GLU A  72     2280   1693   2171   -206    -34     47       O1-
ATOM    615  N   VAL A  73       2.137  18.126  21.579  1.00 13.63           N  
ANISOU  615  N   VAL A  73     1439   1587   2152    178     84    480       N  
ATOM    616  CA  VAL A  73       1.621  17.305  22.679  1.00 13.49           C  
ANISOU  616  CA  VAL A  73     1332   1618   2173    151    211    491       C  
ATOM    617  C   VAL A  73       1.684  15.868  22.154  1.00 13.41           C  
ANISOU  617  C   VAL A  73     1320   1754   2020    -54     37    451       C  
ATOM    618  O   VAL A  73       1.015  15.498  21.208  1.00 15.58           O  
ANISOU  618  O   VAL A  73     1609   1806   2504   -178   -313    736       O  
ATOM    619  CB  VAL A  73       0.244  17.718  23.174  1.00 15.87           C  
ANISOU  619  CB  VAL A  73     1660   1992   2377     76    389    283       C  
ATOM    620  CG1 VAL A  73      -0.216  16.734  24.283  1.00 17.44           C  
ANISOU  620  CG1 VAL A  73     1734   2212   2679   -232    690    499       C  
ATOM    621  CG2 VAL A  73       0.273  19.188  23.777  1.00 17.71           C  
ANISOU  621  CG2 VAL A  73     1967   1877   2884    337    703    386       C  
ATOM    622  N   THR A  74       2.590  15.070  22.697  1.00 12.80           N  
ANISOU  622  N   THR A  74     1348   1655   1859    157     42    346       N  
ATOM    623  CA  THR A  74       2.787  13.721  22.192  1.00 12.53           C  
ANISOU  623  CA  THR A  74     1346   1646   1768   -171    125    355       C  
ATOM    624  C   THR A  74       1.649  12.752  22.542  1.00 13.15           C  
ANISOU  624  C   THR A  74     1195   1768   2030     11    105    332       C  
ATOM    625  O   THR A  74       0.780  13.062  23.343  1.00 13.79           O  
ANISOU  625  O   THR A  74     1241   1740   2256    -45    172    391       O  
ATOM    626  CB  THR A  74       4.140  13.167  22.714  1.00 12.69           C  
ANISOU  626  CB  THR A  74     1398   1648   1774    -42   -117    233       C  
ATOM    627  CG2 THR A  74       5.295  14.106  22.406  1.00 11.57           C  
ANISOU  627  CG2 THR A  74      838   1416   2142   -202      9    249       C  
ATOM    628  OG1 THR A  74       3.965  13.002  24.126  1.00 13.57           O  
ANISOU  628  OG1 THR A  74     2042   1573   1539    216    249    224       O  
ATOM    629  N   ALA A  75       1.671  11.572  21.929  1.00 13.76           N  
ANISOU  629  N   ALA A  75     1415   1706   2107   -105    217    302       N  
ATOM    630  CA  ALA A  75       0.580  10.583  22.114  1.00 15.27           C  
ANISOU  630  CA  ALA A  75     1567   1990   2243   -255    178    249       C  
ATOM    631  C   ALA A  75       0.471  10.183  23.591  1.00 14.87           C  
ANISOU  631  C   ALA A  75     1456   1945   2248   -260    170    320       C  
ATOM    632  O   ALA A  75      -0.616   9.890  24.102  1.00 17.27           O  
ANISOU  632  O   ALA A  75     1598   2421   2540   -577    104    336       O  
ATOM    633  CB  ALA A  75       0.809   9.329  21.221  1.00 15.03           C  
ANISOU  633  CB  ALA A  75     1206   2142   2360   -112    211    257       C  
ATOM    634  N   ASP A  76       1.635  10.181  24.270  1.00 14.06           N  
ANISOU  634  N   ASP A  76     1632   1663   2047   -233    178    290       N  
ATOM    635  CA  ASP A  76       1.645   9.888  25.717  1.00 14.28           C  
ANISOU  635  CA  ASP A  76     1821   1776   1827   -244    247    299       C  
ATOM    636  C   ASP A  76       1.475  11.120  26.607  1.00 14.88           C  
ANISOU  636  C   ASP A  76     1814   1875   1963   -103    419    221       C  
ATOM    637  O   ASP A  76       1.623  11.046  27.808  1.00 17.48           O  
ANISOU  637  O   ASP A  76     2561   2148   1929    137    393    302       O  
ATOM    638  CB  ASP A  76       2.904   9.141  26.115  1.00 14.08           C  
ANISOU  638  CB  ASP A  76     1722   1714   1912   -302    151    214       C  
ATOM    639  CG  ASP A  76       4.199   9.933  25.808  1.00 12.79           C  
ANISOU  639  CG  ASP A  76     1387   1484   1985    273    -58     88       C  
ATOM    640  OD1 ASP A  76       4.329  10.438  24.654  1.00 13.77           O  
ANISOU  640  OD1 ASP A  76     1949   1564   1719     27    173    355       O  
ATOM    641  OD2 ASP A  76       5.074  10.129  26.703  1.00 13.70           O1-
ANISOU  641  OD2 ASP A  76     1705   1515   1985    -53    185    291       O1-
ATOM    642  N   ASP A  77       1.112  12.260  26.026  1.00 14.13           N  
ANISOU  642  N   ASP A  77     1765   1751   1851    -15    561    205       N  
ATOM    643  CA  ASP A  77       0.711  13.487  26.735  1.00 16.50           C  
ANISOU  643  CA  ASP A  77     2112   2046   2109    -25    595    174       C  
ATOM    644  C   ASP A  77       1.890  14.232  27.346  1.00 15.84           C  
ANISOU  644  C   ASP A  77     2165   1944   1906     19    544    191       C  
ATOM    645  O   ASP A  77       1.709  14.944  28.340  1.00 18.12           O  
ANISOU  645  O   ASP A  77     2089   2417   2377     29    787   -212       O  
ATOM    646  CB  ASP A  77      -0.427  13.269  27.743  1.00 16.83           C  
ANISOU  646  CB  ASP A  77     2076   2086   2233    -75    670    181       C  
ATOM    647  CG  ASP A  77      -1.287  14.496  27.907  1.00 22.22           C  
ANISOU  647  CG  ASP A  77     2500   2987   2955    163   1007    291       C  
ATOM    648  OD1 ASP A  77      -1.946  14.600  28.963  1.00 28.90           O  
ANISOU  648  OD1 ASP A  77     3185   3937   3855    137   1551    314       O  
ATOM    649  OD2 ASP A  77      -1.357  15.360  26.994  1.00 27.62           O1-
ANISOU  649  OD2 ASP A  77     3256   3565   3669     72   1066    809       O1-
ATOM    650  N   ARG A  78       3.077  14.165  26.733  1.00 14.80           N  
ANISOU  650  N   ARG A  78     2164   1721   1735     78    600     74       N  
ATOM    651  CA  ARG A  78       4.139  15.107  27.102  1.00 14.19           C  
ANISOU  651  CA  ARG A  78     2210   1605   1577     49    406    176       C  
ATOM    652  C   ARG A  78       3.947  16.357  26.269  1.00 14.21           C  
ANISOU  652  C   ARG A  78     2127   1714   1557    201    456    160       C  
ATOM    653  O   ARG A  78       3.617  16.301  25.111  1.00 15.03           O  
ANISOU  653  O   ARG A  78     2310   1544   1857    168    472    152       O  
ATOM    654  CB  ARG A  78       5.526  14.561  26.761  1.00 14.54           C  
ANISOU  654  CB  ARG A  78     2333   1537   1653    120    366    185       C  
ATOM    655  CG  ARG A  78       6.130  13.475  27.702  1.00 14.01           C  
ANISOU  655  CG  ARG A  78     2011   1620   1689     48     69    252       C  
ATOM    656  CD  ARG A  78       7.375  12.868  27.128  1.00 12.51           C  
ANISOU  656  CD  ARG A  78     1649   1462   1640    102    -49     28       C  
ATOM    657  NE  ARG A  78       7.000  11.979  26.032  1.00 12.68           N  
ANISOU  657  NE  ARG A  78     1835   1357   1625    209     19     72       N  
ATOM    658  CZ  ARG A  78       7.593  11.963  24.853  1.00 11.44           C  
ANISOU  658  CZ  ARG A  78     1169   1390   1785    -72    146     36       C  
ATOM    659  NH1 ARG A  78       8.620  12.737  24.586  1.00 10.83           N1+
ANISOU  659  NH1 ARG A  78      989   1448   1675    -67   -121     94       N1+
ATOM    660  NH2 ARG A  78       7.126  11.206  23.906  1.00 13.23           N  
ANISOU  660  NH2 ARG A  78     2130   1213   1683   -112    -37    -20       N  
ATOM    661  N   LYS A  79       4.237  17.480  26.907  1.00 14.49           N  
ANISOU  661  N   LYS A  79     2142   1688   1674     79    464    100       N  
ATOM    662  CA  LYS A  79       4.186  18.779  26.234  1.00 14.58           C  
ANISOU  662  CA  LYS A  79     1953   1688   1896    248    336     77       C  
ATOM    663  C   LYS A  79       5.600  19.143  25.915  1.00 13.38           C  
ANISOU  663  C   LYS A  79     1914   1389   1781    240    331     52       C  
ATOM    664  O   LYS A  79       6.397  19.403  26.821  1.00 16.50           O  
ANISOU  664  O   LYS A  79     2511   2058   1698     58    487    -96       O  
ATOM    665  CB  LYS A  79       3.504  19.835  27.109  1.00 15.80           C  
ANISOU  665  CB  LYS A  79     2208   1653   2140    232    472    170       C  
ATOM    666  CG  LYS A  79       2.028  19.608  27.214  1.00 23.23           C  
ANISOU  666  CG  LYS A  79     2900   2735   3191    262    299    -42       C  
ATOM    667  CD  LYS A  79       1.601  18.462  28.079  1.00 29.98           C  
ANISOU  667  CD  LYS A  79     3780   3570   4038    -46    302    166       C  
ATOM    668  CE  LYS A  79       0.129  18.607  28.515  1.00 33.43           C  
ANISOU  668  CE  LYS A  79     4034   4235   4432     50    273    208       C  
ATOM    669  NZ  LYS A  79      -0.611  17.325  28.423  1.00 34.82           N1+
ANISOU  669  NZ  LYS A  79     4389   4187   4651     85    347     83       N1+
ATOM    670  N   VAL A  80       5.991  19.037  24.633  1.00 12.30           N  
ANISOU  670  N   VAL A  80     1725   1445   1501    289    243     15       N  
ATOM    671  CA  VAL A  80       7.394  19.138  24.229  1.00 11.71           C  
ANISOU  671  CA  VAL A  80     1597   1422   1428    198    204     40       C  
ATOM    672  C   VAL A  80       7.548  20.298  23.257  1.00 11.07           C  
ANISOU  672  C   VAL A  80     1459   1272   1473    284     41    -23       C  
ATOM    673  O   VAL A  80       6.597  20.784  22.643  1.00 11.56           O  
ANISOU  673  O   VAL A  80     1313   1367   1709     67    145    119       O  
ATOM    674  CB  VAL A  80       7.882  17.810  23.574  1.00 11.15           C  
ANISOU  674  CB  VAL A  80     1413   1209   1614    108    293     32       C  
ATOM    675  CG1 VAL A  80       7.627  16.588  24.519  1.00 12.58           C  
ANISOU  675  CG1 VAL A  80     1632   1260   1886    344    331    351       C  
ATOM    676  CG2 VAL A  80       7.216  17.556  22.233  1.00 12.41           C  
ANISOU  676  CG2 VAL A  80     1983   1417   1314    259    360     60       C  
ATOM    677  N  ALYS A  81       8.795  20.739  23.166  0.50 10.51           N  
ANISOU  677  N  ALYS A  81     1393   1143   1454    305    160    -11       N  
ATOM    678  N  BLYS A  81       8.793  20.725  23.151  0.50 10.72           N  
ANISOU  678  N  BLYS A  81     1464   1158   1449    305    158    -29       N  
ATOM    679  CA ALYS A  81       9.221  21.686  22.136  0.50 10.16           C  
ANISOU  679  CA ALYS A  81     1201   1144   1515    132     96     -8       C  
ATOM    680  CA BLYS A  81       9.188  21.672  22.124  0.50 10.71           C  
ANISOU  680  CA BLYS A  81     1401   1180   1488    150     80    -13       C  
ATOM    681  C  ALYS A  81       9.983  20.883  21.101  0.50 10.42           C  
ANISOU  681  C  ALYS A  81     1223   1288   1449    185    171    -27       C  
ATOM    682  C  BLYS A  81      10.005  20.919  21.094  0.50 10.64           C  
ANISOU  682  C  BLYS A  81     1364   1246   1431    191    150    -46       C  
ATOM    683  O  ALYS A  81      10.929  20.181  21.428  0.50 10.59           O  
ANISOU  683  O  ALYS A  81     1043   1429   1552      7    -36      6       O  
ATOM    684  O  BLYS A  81      11.017  20.306  21.415  0.50 11.05           O  
ANISOU  684  O  BLYS A  81     1537   1258   1403    115    -28    -75       O  
ATOM    685  CB ALYS A  81      10.135  22.769  22.734  0.50 12.47           C  
ANISOU  685  CB ALYS A  81     1653   1355   1728     25     96    -71       C  
ATOM    686  CB BLYS A  81      10.027  22.793  22.722  0.50 13.13           C  
ANISOU  686  CB BLYS A  81     1801   1435   1750     96     92   -124       C  
ATOM    687  CG ALYS A  81       9.490  23.598  23.812  0.50 14.37           C  
ANISOU  687  CG ALYS A  81     1730   1641   2086     95    201   -202       C  
ATOM    688  CG BLYS A  81      10.170  23.933  21.779  0.50 16.29           C  
ANISOU  688  CG BLYS A  81     2275   1935   1979    -90     14    -20       C  
ATOM    689  CD ALYS A  81       8.508  24.588  23.255  0.50 16.59           C  
ANISOU  689  CD ALYS A  81     2142   2088   2072      6    -84    -15       C  
ATOM    690  CD BLYS A  81       9.203  24.987  22.185  0.50 22.02           C  
ANISOU  690  CD BLYS A  81     2861   2573   2930     24    148    -76       C  
ATOM    691  CE ALYS A  81       7.856  25.366  24.406  0.50 17.10           C  
ANISOU  691  CE ALYS A  81     2233   2049   2214    -82   -236   -230       C  
ATOM    692  CE BLYS A  81       9.538  25.513  23.571  0.50 24.06           C  
ANISOU  692  CE BLYS A  81     3210   2786   3145   -159     -2    -49       C  
ATOM    693  NZ ALYS A  81       6.858  26.389  23.958  0.50 17.49           N1+
ANISOU  693  NZ ALYS A  81     2216   2280   2148    -88   -671    -20       N1+
ATOM    694  NZ BLYS A  81       8.409  26.317  24.055  0.50 25.57           N1+
ANISOU  694  NZ BLYS A  81     3236   2709   3770   -180    -10    -36       N1+
ATOM    695  N   SER A  82       9.544  20.945  19.854  1.00  9.38           N  
ANISOU  695  N   SER A  82      855   1266   1441    331    115     55       N  
ATOM    696  CA  SER A  82      10.074  20.104  18.795  1.00  9.49           C  
ANISOU  696  CA  SER A  82     1039   1121   1444    157    195      5       C  
ATOM    697  C   SER A  82      10.665  20.950  17.676  1.00  8.43           C  
ANISOU  697  C   SER A  82      704   1154   1342    183   -108    -37       C  
ATOM    698  O   SER A  82      10.141  22.013  17.320  1.00  9.18           O  
ANISOU  698  O   SER A  82      953   1025   1510    325     28     39       O  
ATOM    699  CB  SER A  82       8.895  19.299  18.236  1.00 10.14           C  
ANISOU  699  CB  SER A  82     1143   1201   1506    -12    156    -49       C  
ATOM    700  OG  SER A  82       8.555  18.303  19.185  1.00 12.58           O  
ANISOU  700  OG  SER A  82     1758   1215   1806    -19    349    304       O  
ATOM    701  N   THR A  83      11.732  20.416  17.103  1.00  8.37           N  
ANISOU  701  N   THR A  83      755   1009   1414    117     17     54       N  
ATOM    702  CA  THR A  83      12.310  20.949  15.877  1.00  8.69           C  
ANISOU  702  CA  THR A  83      937    900   1462     83     19     56       C  
ATOM    703  C   THR A  83      12.584  19.782  14.953  1.00  9.18           C  
ANISOU  703  C   THR A  83     1125   1047   1315    242    209     64       C  
ATOM    704  O   THR A  83      13.160  18.778  15.374  1.00  9.92           O  
ANISOU  704  O   THR A  83     1269   1108   1390    287   -104     61       O  
ATOM    705  CB  THR A  83      13.540  21.750  16.136  1.00 10.13           C  
ANISOU  705  CB  THR A  83      837   1194   1816     15    104    -61       C  
ATOM    706  CG2 THR A  83      13.952  22.478  14.894  1.00 13.49           C  
ANISOU  706  CG2 THR A  83     1480   1532   2113   -440    354    -48       C  
ATOM    707  OG1 THR A  83      13.360  22.665  17.200  1.00 13.08           O  
ANISOU  707  OG1 THR A  83     1401   1418   2151   -186    -11   -433       O  
ATOM    708  N   ILE A  84      12.152  19.904  13.697  1.00  9.17           N  
ANISOU  708  N   ILE A  84     1250   1009   1222    159    -35    -26       N  
ATOM    709  CA  ILE A  84      12.393  18.895  12.685  1.00  8.83           C  
ANISOU  709  CA  ILE A  84      969    993   1393    211    165     28       C  
ATOM    710  C   ILE A  84      13.211  19.480  11.560  1.00  8.34           C  
ANISOU  710  C   ILE A  84      781   1128   1257     46    -15     38       C  
ATOM    711  O   ILE A  84      12.867  20.563  11.055  1.00  9.63           O  
ANISOU  711  O   ILE A  84     1264   1097   1298    115     -9     93       O  
ATOM    712  CB  ILE A  84      11.049  18.266  12.175  1.00  8.41           C  
ANISOU  712  CB  ILE A  84      965    919   1311    330    136    137       C  
ATOM    713  CG1 ILE A  84      10.213  17.651  13.330  1.00  8.58           C  
ANISOU  713  CG1 ILE A  84      839    943   1476     92    129    251       C  
ATOM    714  CG2 ILE A  84      11.354  17.200  11.132  1.00  9.86           C  
ANISOU  714  CG2 ILE A  84      931   1283   1532    168     65    -71       C  
ATOM    715  CD1 ILE A  84       8.911  17.077  13.038  1.00  8.98           C  
ANISOU  715  CD1 ILE A  84      398   1315   1700   -207     61    109       C  
ATOM    716  N   THR A  85      14.314  18.817  11.211  1.00  8.48           N  
ANISOU  716  N   THR A  85      788   1030   1404     43     74    184       N  
ATOM    717  CA  THR A  85      15.185  19.204  10.138  1.00 10.01           C  
ANISOU  717  CA  THR A  85     1062   1101   1639      7    228    112       C  
ATOM    718  C   THR A  85      15.408  18.028   9.216  1.00 10.66           C  
ANISOU  718  C   THR A  85     1348   1224   1479    -27    395    102       C  
ATOM    719  O   THR A  85      15.086  16.912   9.541  1.00 10.95           O  
ANISOU  719  O   THR A  85     1503   1157   1499    -57    438     27       O  
ATOM    720  CB  THR A  85      16.479  19.760  10.679  1.00  9.76           C  
ANISOU  720  CB  THR A  85      506   1233   1969    274    214    -82       C  
ATOM    721  CG2 THR A  85      16.295  21.003  11.501  1.00 14.40           C  
ANISOU  721  CG2 THR A  85     1534   1614   2321   -357    178   -536       C  
ATOM    722  OG1 THR A  85      17.087  18.720  11.472  1.00 13.98           O  
ANISOU  722  OG1 THR A  85     1260   1612   2437    188   -229   -142       O  
ATOM    723  N  ALEU A  86      16.208  18.257   8.185  0.50 10.43           N  
ANISOU  723  N  ALEU A  86     1069   1283   1607   -150    331    113       N  
ATOM    724  N  BLEU A  86      15.756  18.334   7.970  0.50 11.44           N  
ANISOU  724  N  BLEU A  86     1606   1190   1549     26    309    122       N  
ATOM    725  CA ALEU A  86      16.745  17.164   7.378  0.50 11.48           C  
ANISOU  725  CA ALEU A  86     1388   1328   1645   -193    124     23       C  
ATOM    726  CA BLEU A  86      16.146  17.338   6.980  0.50 11.87           C  
ANISOU  726  CA BLEU A  86     1502   1373   1634   -119    186     93       C  
ATOM    727  C  ALEU A  86      18.236  17.048   7.628  0.50 11.54           C  
ANISOU  727  C  ALEU A  86     1368   1270   1744   -239     77     10       C  
ATOM    728  C  BLEU A  86      17.645  17.350   6.892  0.50 13.07           C  
ANISOU  728  C  BLEU A  86     1553   1537   1876   -175    311    -17       C  
ATOM    729  O  ALEU A  86      18.921  18.096   7.630  0.50 13.08           O  
ANISOU  729  O  ALEU A  86     1661   1400   1908   -423    207   -105       O  
ATOM    730  O  BLEU A  86      18.267  18.364   6.509  0.50 15.98           O  
ANISOU  730  O  BLEU A  86     1801   1778   2493   -113    519     83       O  
ATOM    731  CB ALEU A  86      16.518  17.383   5.909  0.50 11.85           C  
ANISOU  731  CB ALEU A  86     1330   1513   1660   -210    135      5       C  
ATOM    732  CB BLEU A  86      15.544  17.629   5.591  0.50 13.17           C  
ANISOU  732  CB BLEU A  86     1849   1521   1632   -101    139     38       C  
ATOM    733  CG ALEU A  86      15.120  17.088   5.409  0.50 11.86           C  
ANISOU  733  CG ALEU A  86      937   1718   1851   -483   -260     66       C  
ATOM    734  CG BLEU A  86      14.304  16.892   5.064  0.50 16.13           C  
ANISOU  734  CG BLEU A  86     2064   2012   2051   -134    -90     89       C  
ATOM    735  CD1ALEU A  86      14.873  17.781   4.045  0.50 14.01           C  
ANISOU  735  CD1ALEU A  86     1487   1857   1976    -21    -59     65       C  
ATOM    736  CD1BLEU A  86      13.942  17.403   3.671  0.50 16.42           C  
ANISOU  736  CD1BLEU A  86     2508   2037   1690     49     80   -213       C  
ATOM    737  CD2ALEU A  86      14.928  15.556   5.301  0.50 10.47           C  
ANISOU  737  CD2ALEU A  86      273   1671   2031    -25   -181   -254       C  
ATOM    738  CD2BLEU A  86      14.468  15.374   5.037  0.50 14.89           C  
ANISOU  738  CD2BLEU A  86     2497   1574   1583   -443     65    -71       C  
ATOM    739  N  AASP A  87      18.731  15.811   7.816  0.50 11.45           N  
ANISOU  739  N  AASP A  87     1214   1360   1776   -236    195    -37       N  
ATOM    740  N  BASP A  87      18.244  16.227   7.257  0.50 12.72           N  
ANISOU  740  N  BASP A  87     1281   1708   1842   -233    189     11       N  
ATOM    741  CA AASP A  87      20.162  15.456   7.844  0.50 12.75           C  
ANISOU  741  CA AASP A  87     1234   1611   1996   -234    111      8       C  
ATOM    742  CA BASP A  87      19.668  16.094   7.321  0.50 14.13           C  
ANISOU  742  CA BASP A  87     1462   1863   2044   -197    122    -63       C  
ATOM    743  C  AASP A  87      20.402  14.512   6.687  0.50 12.25           C  
ANISOU  743  C  AASP A  87     1008   1667   1977   -292    130     75       C  
ATOM    744  C  BASP A  87      20.074  14.955   6.413  0.50 13.66           C  
ANISOU  744  C  BASP A  87     1365   1844   1980   -153    244    -17       C  
ATOM    745  O  AASP A  87      20.192  13.302   6.795  0.50 13.26           O  
ANISOU  745  O  AASP A  87      947   1753   2335   -172    -12    -25       O  
ATOM    746  O  BASP A  87      19.761  13.791   6.687  0.50 14.09           O  
ANISOU  746  O  BASP A  87     1715   1644   1991    -56     83     16       O  
ATOM    747  CB AASP A  87      20.606  14.797   9.174  0.50 13.76           C  
ANISOU  747  CB AASP A  87     1260   1820   2148   -200    139    -33       C  
ATOM    748  CB BASP A  87      20.126  15.824   8.756  0.50 15.00           C  
ANISOU  748  CB BASP A  87     1490   2071   2136   -166    131     11       C  
ATOM    749  CG AASP A  87      22.085  14.373   9.175  0.50 17.26           C  
ANISOU  749  CG AASP A  87     1774   2186   2597    -29   -140   -100       C  
ATOM    750  CG BASP A  87      21.650  15.690   8.877  0.50 19.14           C  
ANISOU  750  CG BASP A  87     1943   2604   2723   -188     47   -118       C  
ATOM    751  OD1AASP A  87      22.835  14.798   8.285  0.50 21.11           O  
ANISOU  751  OD1AASP A  87     1957   2922   3141   -295    -74    228       O  
ATOM    752  OD1BASP A  87      22.384  16.270   8.046  0.50 23.57           O  
ANISOU  752  OD1BASP A  87     2261   3417   3276   -385    170   -107       O  
ATOM    753  OD2AASP A  87      22.503  13.618  10.088  0.50 22.85           O1-
ANISOU  753  OD2AASP A  87     2404   2851   3423     37   -540    213       O1-
ATOM    754  OD2BASP A  87      22.121  15.008   9.807  0.50 23.64           O1-
ANISOU  754  OD2BASP A  87     2580   2857   3545   -306   -513   -100       O1-
ATOM    755  N  AGLY A  88      20.888  15.074   5.583  0.50 13.79           N  
ANISOU  755  N  AGLY A  88     1334   1858   2045   -171    282      4       N  
ATOM    756  N  BGLY A  88      20.748  15.281   5.309  0.50 14.15           N  
ANISOU  756  N  BGLY A  88     1475   1891   2009    -28    205    -45       N  
ATOM    757  CA AGLY A  88      20.819  14.377   4.320  0.50 14.22           C  
ANISOU  757  CA AGLY A  88     1636   1799   1966   -175    295    -22       C  
ATOM    758  CA BGLY A  88      21.167  14.225   4.421  0.50 14.56           C  
ANISOU  758  CA BGLY A  88     1671   1905   1955    -33     97    -76       C  
ATOM    759  C  AGLY A  88      19.402  14.064   3.899  0.50 13.69           C  
ANISOU  759  C  AGLY A  88     1639   1745   1817   -152    310    -21       C  
ATOM    760  C  BGLY A  88      19.997  13.304   4.094  0.50 13.92           C  
ANISOU  760  C  BGLY A  88     1506   1912   1870     59    153    -73       C  
ATOM    761  O  AGLY A  88      18.577  14.962   3.749  0.50 13.34           O  
ANISOU  761  O  AGLY A  88     1502   1692   1874   -360    382      0       O  
ATOM    762  O  BGLY A  88      20.157  12.098   4.065  0.50 13.61           O  
ANISOU  762  O  BGLY A  88     1347   1812   2009    167     43     35       O  
ATOM    763  N  AGLY A  89      19.138  12.778   3.704  0.50 12.99           N  
ANISOU  763  N  AGLY A  89     1519   1688   1729   -180    305    -83       N  
ATOM    764  N  BGLY A  89      18.815  13.854   3.837  0.50 12.94           N  
ANISOU  764  N  BGLY A  89     1515   1776   1626     68    204     -2       N  
ATOM    765  CA AGLY A  89      17.801  12.247   3.440  0.50 13.41           C  
ANISOU  765  CA AGLY A  89     1584   1792   1718   -138    245   -217       C  
ATOM    766  CA BGLY A  89      17.680  13.039   3.489  0.50 12.62           C  
ANISOU  766  CA BGLY A  89     1337   1825   1634    126    251    -88       C  
ATOM    767  C  AGLY A  89      17.054  11.798   4.680  0.50 12.30           C  
ANISOU  767  C  AGLY A  89     1339   1653   1680   -111    306   -328       C  
ATOM    768  C  BGLY A  89      16.897  12.315   4.610  0.50 12.41           C  
ANISOU  768  C  BGLY A  89     1344   1767   1603   -144    204    -56       C  
ATOM    769  O  AGLY A  89      16.122  10.984   4.603  0.50 12.67           O  
ANISOU  769  O  AGLY A  89     1652   1338   1822     34     57   -502       O  
ATOM    770  O  BGLY A  89      15.815  11.774   4.345  0.50 12.29           O  
ANISOU  770  O  BGLY A  89     1357   1695   1614    -12     90     13       O  
ATOM    771  N   VAL A  90      17.436  12.312   5.852  1.00 12.43           N  
ANISOU  771  N   VAL A  90     1236   1840   1643   -224    202   -222       N  
ATOM    772  CA  VAL A  90      16.771  11.818   7.092  1.00 11.27           C  
ANISOU  772  CA  VAL A  90     1101   1499   1681   -298    224   -230       C  
ATOM    773  C   VAL A  90      16.018  12.979   7.745  1.00  8.87           C  
ANISOU  773  C   VAL A  90      478   1472   1418   -127     14    -89       C  
ATOM    774  O   VAL A  90      16.589  14.049   7.964  1.00 10.53           O  
ANISOU  774  O   VAL A  90     1220   1271   1506   -402    224   -106       O  
ATOM    775  CB  VAL A  90      17.853  11.241   8.069  1.00 11.50           C  
ANISOU  775  CB  VAL A  90     1127   1336   1906   -163    323   -174       C  
ATOM    776  CG1 VAL A  90      17.212  10.718   9.341  1.00 14.08           C  
ANISOU  776  CG1 VAL A  90     1795   1547   2007   -184    410    -39       C  
ATOM    777  CG2 VAL A  90      18.692  10.195   7.388  1.00 14.86           C  
ANISOU  777  CG2 VAL A  90     1582   1599   2462    434    189   -256       C  
ATOM    778  N   LEU A  91      14.758  12.761   8.037  1.00  9.22           N  
ANISOU  778  N   LEU A  91      772   1336   1394    -42     29    -37       N  
ATOM    779  CA  LEU A  91      13.980  13.715   8.837  1.00  9.25           C  
ANISOU  779  CA  LEU A  91     1016   1151   1346     64    156    126       C  
ATOM    780  C   LEU A  91      14.401  13.453  10.282  1.00  9.71           C  
ANISOU  780  C   LEU A  91     1179   1310   1200    241    383    -10       C  
ATOM    781  O   LEU A  91      14.209  12.359  10.816  1.00  9.87           O  
ANISOU  781  O   LEU A  91     1394   1016   1338    109    252    148       O  
ATOM    782  CB  LEU A  91      12.490  13.527   8.649  1.00 11.51           C  
ANISOU  782  CB  LEU A  91     1268   1433   1670      8    252    266       C  
ATOM    783  CG  LEU A  91      11.905  14.123   7.397  1.00 13.13           C  
ANISOU  783  CG  LEU A  91     1654   1605   1727   -264     24     -1       C  
ATOM    784  CD1 LEU A  91      10.555  13.551   7.232  1.00 16.50           C  
ANISOU  784  CD1 LEU A  91     1753   1958   2555   -206    -37    258       C  
ATOM    785  CD2 LEU A  91      11.863  15.662   7.565  1.00 13.84           C  
ANISOU  785  CD2 LEU A  91     2125   1165   1968    412      5    149       C  
ATOM    786  N   VAL A  92      14.903  14.482  10.949  1.00  9.55           N  
ANISOU  786  N   VAL A  92     1334   1035   1257    148    188    -14       N  
ATOM    787  CA  VAL A  92      15.364  14.375  12.327  1.00  9.26           C  
ANISOU  787  CA  VAL A  92     1111   1041   1363    184    178     73       C  
ATOM    788  C   VAL A  92      14.491  15.245  13.200  1.00  9.21           C  
ANISOU  788  C   VAL A  92     1008   1109   1383    404     67    157       C  
ATOM    789  O   VAL A  92      14.436  16.465  13.013  1.00 11.21           O  
ANISOU  789  O   VAL A  92     1615   1176   1465    287    114    151       O  
ATOM    790  CB  VAL A  92      16.831  14.833  12.412  1.00 10.89           C  
ANISOU  790  CB  VAL A  92     1384   1257   1496    141    259      8       C  
ATOM    791  CG1 VAL A  92      17.353  14.745  13.848  1.00 14.02           C  
ANISOU  791  CG1 VAL A  92     1688   2028   1609    218     83    -64       C  
ATOM    792  CG2 VAL A  92      17.735  14.022  11.475  1.00 11.95           C  
ANISOU  792  CG2 VAL A  92     1146   1681   1713    183    216   -171       C  
ATOM    793  N   HIS A  93      13.784  14.608  14.114  1.00  9.02           N  
ANISOU  793  N   HIS A  93     1037   1030   1359    298    151     46       N  
ATOM    794  CA  HIS A  93      12.777  15.226  14.997  1.00  8.07           C  
ANISOU  794  CA  HIS A  93      593   1075   1396    245    149    136       C  
ATOM    795  C   HIS A  93      13.298  15.178  16.402  1.00  9.19           C  
ANISOU  795  C   HIS A  93     1110   1202   1181    244     86      6       C  
ATOM    796  O   HIS A  93      13.416  14.127  17.000  1.00 10.40           O  
ANISOU  796  O   HIS A  93     1671   1020   1259    157    -35     79       O  
ATOM    797  CB  HIS A  93      11.480  14.493  14.794  1.00  8.54           C  
ANISOU  797  CB  HIS A  93      613   1142   1487    302   -144    213       C  
ATOM    798  CG  HIS A  93      10.297  14.929  15.557  1.00  8.38           C  
ANISOU  798  CG  HIS A  93      520   1082   1578    254    249    199       C  
ATOM    799  CD2 HIS A  93      10.087  15.908  16.479  1.00 11.66           C  
ANISOU  799  CD2 HIS A  93     1353   1263   1815    197     41    393       C  
ATOM    800  ND1 HIS A  93       9.137  14.228  15.425  1.00 11.75           N  
ANISOU  800  ND1 HIS A  93      669   1665   2130    131    317    615       N  
ATOM    801  CE1 HIS A  93       8.230  14.757  16.216  1.00 13.51           C  
ANISOU  801  CE1 HIS A  93      767   2066   2299    141    343    820       C  
ATOM    802  NE2 HIS A  93       8.775  15.788  16.855  1.00 13.23           N  
ANISOU  802  NE2 HIS A  93     1264   1574   2186    467    407    898       N  
ATOM    803  N   VAL A  94      13.610  16.350  16.988  1.00  8.55           N  
ANISOU  803  N   VAL A  94      821   1134   1292    215    -36    -19       N  
ATOM    804  CA  VAL A  94      14.079  16.454  18.371  1.00  9.19           C  
ANISOU  804  CA  VAL A  94     1039    996   1455    271    162     31       C  
ATOM    805  C   VAL A  94      13.012  17.035  19.210  1.00  9.02           C  
ANISOU  805  C   VAL A  94      870   1138   1418    159     14   -174       C  
ATOM    806  O   VAL A  94      12.454  18.087  18.902  1.00 10.76           O  
ANISOU  806  O   VAL A  94     1239   1327   1523    596    148     97       O  
ATOM    807  CB  VAL A  94      15.391  17.278  18.445  1.00 10.67           C  
ANISOU  807  CB  VAL A  94     1123   1148   1780    107    147     39       C  
ATOM    808  CG1 VAL A  94      15.892  17.318  19.841  1.00 13.35           C  
ANISOU  808  CG1 VAL A  94     1497   1689   1885     57   -251    -88       C  
ATOM    809  CG2 VAL A  94      16.415  16.687  17.471  1.00 11.19           C  
ANISOU  809  CG2 VAL A  94      264   1701   2287    -49    135     31       C  
ATOM    810  N   GLN A  95      12.701  16.337  20.307  1.00  9.77           N  
ANISOU  810  N   GLN A  95     1556    882   1274    159   -115    -29       N  
ATOM    811  CA  GLN A  95      11.718  16.764  21.283  1.00 10.38           C  
ANISOU  811  CA  GLN A  95     1588    978   1377    313    -97     54       C  
ATOM    812  C   GLN A  95      12.389  17.062  22.589  1.00 10.05           C  
ANISOU  812  C   GLN A  95     1449   1019   1347    136    -31     48       C  
ATOM    813  O   GLN A  95      13.132  16.237  23.115  1.00 11.34           O  
ANISOU  813  O   GLN A  95     1629   1292   1384    211   -172    -12       O  
ATOM    814  CB  GLN A  95      10.673  15.664  21.554  1.00 10.27           C  
ANISOU  814  CB  GLN A  95     1567    976   1358    195     92     35       C  
ATOM    815  CG  GLN A  95       9.817  15.231  20.364  1.00 10.26           C  
ANISOU  815  CG  GLN A  95     1210   1283   1405    -59    105    -96       C  
ATOM    816  CD  GLN A  95       8.909  14.058  20.629  1.00  9.85           C  
ANISOU  816  CD  GLN A  95      550   1396   1794   -116     81     53       C  
ATOM    817  NE2 GLN A  95       7.829  13.944  19.864  1.00 10.38           N  
ANISOU  817  NE2 GLN A  95      734   1472   1735     19     29    187       N  
ATOM    818  OE1 GLN A  95       9.179  13.234  21.515  1.00 11.78           O  
ANISOU  818  OE1 GLN A  95     1259   1397   1817    -15     40    255       O  
ATOM    819  N   LYS A  96      12.092  18.244  23.145  1.00 11.46           N  
ANISOU  819  N   LYS A  96     1798   1177   1377    177   -196    -49       N  
ATOM    820  CA  LYS A  96      12.643  18.720  24.431  1.00 13.12           C  
ANISOU  820  CA  LYS A  96     2049   1393   1540     -5   -186    -59       C  
ATOM    821  C   LYS A  96      11.542  18.970  25.433  1.00 12.66           C  
ANISOU  821  C   LYS A  96     2217   1188   1403    138   -209    -66       C  
ATOM    822  O   LYS A  96      10.560  19.627  25.135  1.00 13.08           O  
ANISOU  822  O   LYS A  96     2204   1285   1479     88    -66    -61       O  
ATOM    823  CB  LYS A  96      13.411  20.031  24.223  1.00 14.15           C  
ANISOU  823  CB  LYS A  96     2067   1630   1680    -86   -249   -238       C  
ATOM    824  CG  LYS A  96      14.453  20.008  23.182  1.00 17.80           C  
ANISOU  824  CG  LYS A  96     2300   2217   2246     81   -253   -147       C  
ATOM    825  CD  LYS A  96      15.648  19.199  23.521  1.00 19.29           C  
ANISOU  825  CD  LYS A  96     2506   2135   2685    207     50    -46       C  
ATOM    826  CE  LYS A  96      16.863  19.453  22.623  1.00 19.90           C  
ANISOU  826  CE  LYS A  96     2129   2523   2909   -299   -120   -157       C  
ATOM    827  NZ  LYS A  96      18.046  18.643  22.945  1.00 21.99           N1+
ANISOU  827  NZ  LYS A  96     2603   2059   3691   -353    -89   -109       N1+
ATOM    828  N   TRP A  97      11.731  18.445  26.650  1.00 13.48           N  
ANISOU  828  N   TRP A  97     2407   1256   1456    118   -115    -96       N  
ATOM    829  CA  TRP A  97      10.747  18.665  27.728  1.00 14.51           C  
ANISOU  829  CA  TRP A  97     2415   1611   1484    294   -134   -144       C  
ATOM    830  C   TRP A  97      11.409  18.349  29.036  1.00 15.77           C  
ANISOU  830  C   TRP A  97     2664   1881   1444    360   -101    -95       C  
ATOM    831  O   TRP A  97      12.211  17.445  29.128  1.00 16.76           O  
ANISOU  831  O   TRP A  97     3045   1842   1480    537   -309   -119       O  
ATOM    832  CB  TRP A  97       9.490  17.787  27.539  1.00 14.41           C  
ANISOU  832  CB  TRP A  97     2251   1668   1556    216    151      0       C  
ATOM    833  CG  TRP A  97       9.658  16.361  27.936  1.00 14.91           C  
ANISOU  833  CG  TRP A  97     2378   1661   1626    326    283    118       C  
ATOM    834  CD1 TRP A  97       9.149  15.763  29.032  1.00 14.27           C  
ANISOU  834  CD1 TRP A  97     1553   2175   1692    473    491     32       C  
ATOM    835  CD2 TRP A  97      10.447  15.379  27.279  1.00 13.56           C  
ANISOU  835  CD2 TRP A  97     2269   1388   1493    101    285   -143       C  
ATOM    836  CE2 TRP A  97      10.340  14.197  28.027  1.00 13.97           C  
ANISOU  836  CE2 TRP A  97     2183   1581   1542    -97    228    120       C  
ATOM    837  CE3 TRP A  97      11.175  15.358  26.104  1.00 13.79           C  
ANISOU  837  CE3 TRP A  97     2025   1648   1565   -198    -10    -92       C  
ATOM    838  NE1 TRP A  97       9.519  14.465  29.093  1.00 14.22           N  
ANISOU  838  NE1 TRP A  97     2017   1617   1767    111    211     -1       N  
ATOM    839  CZ2 TRP A  97      10.994  13.013  27.657  1.00 14.22           C  
ANISOU  839  CZ2 TRP A  97     2244   1540   1617   -331    -30    177       C  
ATOM    840  CZ3 TRP A  97      11.819  14.181  25.738  1.00 11.88           C  
ANISOU  840  CZ3 TRP A  97     1598   1451   1465   -128     59    -55       C  
ATOM    841  CH2 TRP A  97      11.711  13.026  26.513  1.00 13.84           C  
ANISOU  841  CH2 TRP A  97     2059   1399   1798   -136     32   -242       C  
ATOM    842  N   ASP A  98      11.130  19.154  30.058  1.00 18.37           N  
ANISOU  842  N   ASP A  98     3341   2119   1518    353   -140   -280       N  
ATOM    843  CA  ASP A  98      11.592  18.804  31.434  1.00 20.86           C  
ANISOU  843  CA  ASP A  98     3500   2578   1846    253   -277   -344       C  
ATOM    844  C   ASP A  98      13.092  18.567  31.522  1.00 20.52           C  
ANISOU  844  C   ASP A  98     3493   2471   1832    146   -389   -437       C  
ATOM    845  O   ASP A  98      13.575  17.703  32.280  1.00 23.26           O  
ANISOU  845  O   ASP A  98     4076   2885   1875    178   -489   -393       O  
ATOM    846  CB  ASP A  98      10.840  17.563  31.896  1.00 22.87           C  
ANISOU  846  CB  ASP A  98     3734   3081   1872    203   -296   -226       C  
ATOM    847  CG  ASP A  98       9.773  17.880  32.853  1.00 30.14           C  
ANISOU  847  CG  ASP A  98     4338   4068   3044    199   -126   -350       C  
ATOM    848  OD1 ASP A  98      10.163  18.130  34.028  1.00 35.16           O  
ANISOU  848  OD1 ASP A  98     5484   5005   2869    162   -480     87       O  
ATOM    849  OD2 ASP A  98       8.581  17.863  32.429  1.00 37.63           O1-
ANISOU  849  OD2 ASP A  98     4625   5616   4056     71   -429   -435       O1-
ATOM    850  N   GLY A  99      13.864  19.313  30.746  1.00 19.97           N  
ANISOU  850  N   GLY A  99     3303   2411   1873     80   -481   -622       N  
ATOM    851  CA  GLY A  99      15.292  19.082  30.701  1.00 20.72           C  
ANISOU  851  CA  GLY A  99     3219   2502   2152     -3   -488   -454       C  
ATOM    852  C   GLY A  99      15.788  17.825  30.024  1.00 20.14           C  
ANISOU  852  C   GLY A  99     3053   2422   2175     28   -518   -419       C  
ATOM    853  O   GLY A  99      16.987  17.581  30.013  1.00 22.96           O  
ANISOU  853  O   GLY A  99     3307   2727   2690     17   -843   -508       O  
ATOM    854  N   LYS A 100      14.884  17.072  29.389  1.00 17.66           N  
ANISOU  854  N   LYS A 100     2776   2173   1758     32   -614   -371       N  
ATOM    855  CA  LYS A 100      15.160  15.808  28.680  1.00 16.27           C  
ANISOU  855  CA  LYS A 100     2548   1988   1646    172   -538   -159       C  
ATOM    856  C   LYS A 100      15.085  16.056  27.175  1.00 14.11           C  
ANISOU  856  C   LYS A 100     2246   1645   1469     58   -551    -46       C  
ATOM    857  O   LYS A 100      14.541  17.059  26.737  1.00 13.56           O  
ANISOU  857  O   LYS A 100     2058   1439   1653     89   -482   -158       O  
ATOM    858  CB  LYS A 100      14.104  14.774  29.083  1.00 16.38           C  
ANISOU  858  CB  LYS A 100     2715   1871   1636    271   -501     11       C  
ATOM    859  CG  LYS A 100      14.098  14.453  30.591  1.00 21.53           C  
ANISOU  859  CG  LYS A 100     3393   2720   2066     63   -338    -59       C  
ATOM    860  CD  LYS A 100      12.903  13.570  30.959  1.00 24.79           C  
ANISOU  860  CD  LYS A 100     3586   3220   2610     43    103    184       C  
ATOM    861  CE  LYS A 100      12.641  13.444  32.459  1.00 28.25           C  
ANISOU  861  CE  LYS A 100     4106   3730   2896     43     72     75       C  
ATOM    862  NZ  LYS A 100      11.237  13.007  32.696  1.00 34.69           N1+
ANISOU  862  NZ  LYS A 100     4885   4717   3578   -267    380    470       N1+
ATOM    863  N   SER A 101      15.611  15.119  26.402  1.00 13.56           N  
ANISOU  863  N   SER A 101     2244   1480   1428    190   -467    -75       N  
ATOM    864  CA  SER A 101      15.546  15.217  24.948  1.00 13.73           C  
ANISOU  864  CA  SER A 101     2149   1459   1605     39   -321    -19       C  
ATOM    865  C   SER A 101      15.461  13.818  24.374  1.00 11.67           C  
ANISOU  865  C   SER A 101     1705   1272   1457    113   -186     38       C  
ATOM    866  O   SER A 101      16.096  12.920  24.864  1.00 13.04           O  
ANISOU  866  O   SER A 101     2002   1204   1745    118   -606     30       O  
ATOM    867  CB  SER A 101      16.831  15.893  24.452  1.00 15.77           C  
ANISOU  867  CB  SER A 101     2363   1686   1940   -102   -235     19       C  
ATOM    868  OG  SER A 101      16.902  16.052  23.072  1.00 17.66           O  
ANISOU  868  OG  SER A 101     2505   1974   2228   -458   -259     49       O  
ATOM    869  N   THR A 102      14.705  13.662  23.294  1.00 10.41           N  
ANISOU  869  N   THR A 102     1504   1151   1297     55   -245     14       N  
ATOM    870  CA  THR A 102      14.654  12.423  22.527  1.00  9.08           C  
ANISOU  870  CA  THR A 102      984   1060   1404    319    -13    -47       C  
ATOM    871  C   THR A 102      14.639  12.802  21.051  1.00  9.78           C  
ANISOU  871  C   THR A 102     1357   1135   1224    134    -76     44       C  
ATOM    872  O   THR A 102      14.140  13.869  20.685  1.00 10.72           O  
ANISOU  872  O   THR A 102     1523   1101   1447    202    -17     71       O  
ATOM    873  CB  THR A 102      13.417  11.590  22.919  1.00 10.49           C  
ANISOU  873  CB  THR A 102     1357   1289   1339   -282     -5   -123       C  
ATOM    874  CG2 THR A 102      12.057  12.231  22.567  1.00 10.16           C  
ANISOU  874  CG2 THR A 102      649   1366   1845    -46   -153    -19       C  
ATOM    875  OG1 THR A 102      13.512  10.288  22.301  1.00 11.22           O  
ANISOU  875  OG1 THR A 102     1426   1037   1800    -24     -2   -107       O  
ATOM    876  N   THR A 103      15.175  11.902  20.226  1.00  9.77           N  
ANISOU  876  N   THR A 103     1442    944   1325    294   -173     54       N  
ATOM    877  CA  THR A 103      15.286  12.140  18.799  1.00 10.26           C  
ANISOU  877  CA  THR A 103     1346   1060   1491    282   -163     21       C  
ATOM    878  C   THR A 103      14.608  10.970  18.059  1.00 10.20           C  
ANISOU  878  C   THR A 103     1380   1126   1370    356    -78    -13       C  
ATOM    879  O   THR A 103      14.892   9.806  18.345  1.00 12.30           O  
ANISOU  879  O   THR A 103     2180   1035   1455    323   -304    116       O  
ATOM    880  CB  THR A 103      16.765  12.284  18.369  1.00 11.57           C  
ANISOU  880  CB  THR A 103     1228   1467   1699    259    -69    115       C  
ATOM    881  CG2 THR A 103      16.856  12.527  16.885  1.00 13.08           C  
ANISOU  881  CG2 THR A 103     1161   1914   1893     28     60    -29       C  
ATOM    882  OG1 THR A 103      17.339  13.405  19.047  1.00 15.15           O  
ANISOU  882  OG1 THR A 103     1709   1876   2169    -15   -197      5       O  
ATOM    883  N   ILE A 104      13.754  11.333  17.117  1.00  9.52           N  
ANISOU  883  N   ILE A 104     1478    877   1262    247   -182     52       N  
ATOM    884  CA  ILE A 104      13.072  10.417  16.220  1.00 10.89           C  
ANISOU  884  CA  ILE A 104     1758   1029   1351    165    -51     45       C  
ATOM    885  C   ILE A 104      13.578  10.708  14.832  1.00  9.97           C  
ANISOU  885  C   ILE A 104     1670   1014   1104    144     25    -29       C  
ATOM    886  O   ILE A 104      13.448  11.829  14.349  1.00  9.87           O  
ANISOU  886  O   ILE A 104     1538    965   1246    343    100     73       O  
ATOM    887  CB  ILE A 104      11.537  10.617  16.306  1.00 11.48           C  
ANISOU  887  CB  ILE A 104     1800   1252   1308      5    167    104       C  
ATOM    888  CG1 ILE A 104      11.037  10.328  17.731  1.00 11.24           C  
ANISOU  888  CG1 ILE A 104     1278   1457   1533    -87    -18    -21       C  
ATOM    889  CG2 ILE A 104      10.860   9.681  15.308  1.00 12.78           C  
ANISOU  889  CG2 ILE A 104     1770   1533   1551   -115    -83   -133       C  
ATOM    890  CD1 ILE A 104       9.621  10.774  17.930  1.00 16.03           C  
ANISOU  890  CD1 ILE A 104     1384   2575   2129     42   -107    -17       C  
ATOM    891  N   LYS A 105      14.149   9.714  14.178  1.00  9.37           N  
ANISOU  891  N   LYS A 105     1309    936   1315     43     93     18       N  
ATOM    892  CA  LYS A 105      14.609   9.804  12.815  1.00  9.66           C  
ANISOU  892  CA  LYS A 105     1331   1063   1275     97     93     20       C  
ATOM    893  C   LYS A 105      13.763   9.001  11.897  1.00  9.35           C  
ANISOU  893  C   LYS A 105     1246   1025   1280    185     -1    -52       C  
ATOM    894  O   LYS A 105      13.343   7.888  12.257  1.00 11.11           O  
ANISOU  894  O   LYS A 105     1757   1084   1378     31   -117     82       O  
ATOM    895  CB  LYS A 105      16.066   9.306  12.726  1.00 10.55           C  
ANISOU  895  CB  LYS A 105     1236   1406   1365    -36    200    -98       C  
ATOM    896  CG  LYS A 105      17.084  10.219  13.470  1.00 14.19           C  
ANISOU  896  CG  LYS A 105     1422   1949   2020     27   -331   -179       C  
ATOM    897  CD  LYS A 105      18.531   9.781  13.314  1.00 18.35           C  
ANISOU  897  CD  LYS A 105     1065   3113   2792   -228   -350   -164       C  
ATOM    898  CE  LYS A 105      19.472  10.821  14.027  1.00 20.88           C  
ANISOU  898  CE  LYS A 105     1401   3080   3450   -387    -30   -131       C  
ATOM    899  NZ  LYS A 105      20.941  10.563  13.931  1.00 25.97           N1+
ANISOU  899  NZ  LYS A 105     2190   3268   4408   -170   -110   -317       N1+
ATOM    900  N   ARG A 106      13.418   9.547  10.732  1.00  9.33           N  
ANISOU  900  N   ARG A 106     1328    909   1305     48     13    -26       N  
ATOM    901  CA  ARG A 106      12.612   8.870   9.747  1.00  9.43           C  
ANISOU  901  CA  ARG A 106     1174   1119   1288   -155    111      9       C  
ATOM    902  C   ARG A 106      13.461   8.858   8.458  1.00  9.69           C  
ANISOU  902  C   ARG A 106     1199   1248   1234    -75     35    -14       C  
ATOM    903  O   ARG A 106      13.914   9.894   7.999  1.00 10.33           O  
ANISOU  903  O   ARG A 106     1401   1220   1303    -97     12     14       O  
ATOM    904  CB  ARG A 106      11.286   9.628   9.540  1.00  9.59           C  
ANISOU  904  CB  ARG A 106      719   1218   1706   -173     21     41       C  
ATOM    905  CG  ARG A 106      10.381   9.595  10.802  1.00 11.84           C  
ANISOU  905  CG  ARG A 106     1406   1310   1783   -274    283    150       C  
ATOM    906  CD  ARG A 106       9.154  10.542  10.629  1.00 14.84           C  
ANISOU  906  CD  ARG A 106     1245   2067   2325   -263    457     34       C  
ATOM    907  NE  ARG A 106       8.127  10.473  11.714  1.00 17.76           N  
ANISOU  907  NE  ARG A 106     1647   2203   2897    -51    734    249       N  
ATOM    908  CZ  ARG A 106       8.139  11.262  12.788  1.00 16.06           C  
ANISOU  908  CZ  ARG A 106      998   2541   2562    446    264    531       C  
ATOM    909  NH1 ARG A 106       9.126  12.113  13.027  1.00 15.51           N1+
ANISOU  909  NH1 ARG A 106     1221   2559   2110    601    252    428       N1+
ATOM    910  NH2 ARG A 106       7.183  11.130  13.689  1.00 20.48           N  
ANISOU  910  NH2 ARG A 106     2359   3038   2385    -50   1002     77       N  
ATOM    911  N   LYS A 107      13.592   7.679   7.846  1.00  9.84           N  
ANISOU  911  N   LYS A 107     1311   1232   1195   -197     58    -34       N  
ATOM    912  CA  LYS A 107      14.414   7.504   6.664  1.00 11.43           C  
ANISOU  912  CA  LYS A 107     1672   1381   1290    -76    -11    -74       C  
ATOM    913  C   LYS A 107      13.790   6.472   5.720  1.00 12.09           C  
ANISOU  913  C   LYS A 107     1716   1503   1372   -338     63    -37       C  
ATOM    914  O   LYS A 107      13.271   5.454   6.151  1.00 12.79           O  
ANISOU  914  O   LYS A 107     1973   1549   1336   -484     22    -10       O  
ATOM    915  CB  LYS A 107      15.800   7.011   7.071  1.00 13.51           C  
ANISOU  915  CB  LYS A 107     1761   1938   1433      1    103   -242       C  
ATOM    916  CG  LYS A 107      16.870   7.105   5.956  1.00 16.52           C  
ANISOU  916  CG  LYS A 107     1969   2107   2201    -73      3   -146       C  
ATOM    917  CD  LYS A 107      18.247   6.659   6.387  1.00 18.80           C  
ANISOU  917  CD  LYS A 107     1799   2759   2584    259     89   -300       C  
ATOM    918  CE  LYS A 107      19.322   7.172   5.392  1.00 22.67           C  
ANISOU  918  CE  LYS A 107     2209   3404   2999     20    545   -597       C  
ATOM    919  NZ  LYS A 107      20.665   6.704   5.708  1.00 28.61           N1+
ANISOU  919  NZ  LYS A 107     2493   4495   3882    -66    574   -402       N1+
ATOM    920  N   ARG A 108      13.897   6.726   4.424  1.00 10.97           N  
ANISOU  920  N   ARG A 108     1451   1368   1347    -36     32     -5       N  
ATOM    921  CA  ARG A 108      13.480   5.742   3.446  1.00 10.43           C  
ANISOU  921  CA  ARG A 108     1081   1421   1460    -92     62     14       C  
ATOM    922  C   ARG A 108      14.592   4.695   3.285  1.00 10.69           C  
ANISOU  922  C   ARG A 108      936   1568   1557   -117    -35   -204       C  
ATOM    923  O   ARG A 108      15.748   5.037   3.084  1.00 12.95           O  
ANISOU  923  O   ARG A 108     1187   1656   2076    -32    235   -481       O  
ATOM    924  CB  ARG A 108      13.180   6.421   2.105  1.00 11.35           C  
ANISOU  924  CB  ARG A 108      866   1788   1656   -400    127     48       C  
ATOM    925  CG  ARG A 108      11.835   7.076   2.086  1.00 13.56           C  
ANISOU  925  CG  ARG A 108     1345   2077   1727   -167    -15    364       C  
ATOM    926  CD  ARG A 108      10.600   6.132   2.156  1.00 15.61           C  
ANISOU  926  CD  ARG A 108     1017   2721   2193   -240    217    424       C  
ATOM    927  NE  ARG A 108      10.718   5.044   1.158  1.00 17.96           N  
ANISOU  927  NE  ARG A 108     1463   2467   2892   -305   -149    402       N  
ATOM    928  CZ  ARG A 108      10.470   5.179  -0.138  1.00 17.53           C  
ANISOU  928  CZ  ARG A 108     1805   1985   2870   -330   -169    136       C  
ATOM    929  NH1 ARG A 108       9.914   6.276  -0.607  1.00 16.98           N1+
ANISOU  929  NH1 ARG A 108     1951   2213   2284    -37   -162    274       N1+
ATOM    930  NH2 ARG A 108      10.680   4.183  -0.979  1.00 21.52           N  
ANISOU  930  NH2 ARG A 108     2014   3001   3161    297   -233    -99       N  
ATOM    931  N   GLU A 109      14.195   3.435   3.295  1.00 11.35           N  
ANISOU  931  N   GLU A 109     1410   1374   1526    -38    156   -211       N  
ATOM    932  CA  GLU A 109      15.095   2.313   3.064  1.00 12.30           C  
ANISOU  932  CA  GLU A 109     1394   1642   1637    154     54   -213       C  
ATOM    933  C   GLU A 109      14.349   1.353   2.213  1.00 10.88           C  
ANISOU  933  C   GLU A 109     1072   1439   1623     68    136    -60       C  
ATOM    934  O   GLU A 109      13.374   0.781   2.658  1.00 11.24           O  
ANISOU  934  O   GLU A 109     1107   1573   1589   -194    175    -73       O  
ATOM    935  CB  GLU A 109      15.454   1.610   4.382  1.00 15.35           C  
ANISOU  935  CB  GLU A 109     2006   1866   1959    262     -8   -205       C  
ATOM    936  CG  GLU A 109      16.132   2.475   5.396  1.00 20.36           C  
ANISOU  936  CG  GLU A 109     2986   2507   2241    226   -304   -145       C  
ATOM    937  CD  GLU A 109      17.554   2.702   5.075  1.00 24.23           C  
ANISOU  937  CD  GLU A 109     3309   3117   2777    -34   -151   -467       C  
ATOM    938  OE1 GLU A 109      18.226   3.427   5.846  1.00 29.11           O  
ANISOU  938  OE1 GLU A 109     3589   3677   3794   -111   -772   -799       O  
ATOM    939  OE2 GLU A 109      18.033   2.143   4.054  1.00 30.27           O1-
ANISOU  939  OE2 GLU A 109     3778   4117   3604    180     77  -1013       O1-
ATOM    940  N   ASP A 110      14.775   1.134   0.982  1.00 11.40           N  
ANISOU  940  N   ASP A 110     1261   1686   1384    -21    112    -77       N  
ATOM    941  CA  ASP A 110      14.025   0.333   0.031  1.00 11.85           C  
ANISOU  941  CA  ASP A 110     1421   1619   1460   -109    244     32       C  
ATOM    942  C   ASP A 110      12.626   0.901  -0.053  1.00 10.96           C  
ANISOU  942  C   ASP A 110     1038   1754   1371   -151     18   -160       C  
ATOM    943  O   ASP A 110      12.458   2.103  -0.161  1.00 11.98           O  
ANISOU  943  O   ASP A 110     1327   1674   1548     -7    183   -137       O  
ATOM    944  CB  ASP A 110      14.156  -1.174   0.348  1.00 12.66           C  
ANISOU  944  CB  ASP A 110     1668   1552   1589    -35    222    -89       C  
ATOM    945  CG  ASP A 110      15.592  -1.666   0.282  1.00 16.74           C  
ANISOU  945  CG  ASP A 110     2095   2330   1934    214    343    239       C  
ATOM    946  OD1 ASP A 110      16.344  -1.172  -0.571  1.00 17.69           O  
ANISOU  946  OD1 ASP A 110     2001   2166   2552    568    589    157       O  
ATOM    947  OD2 ASP A 110      15.955  -2.535   1.102  1.00 21.71           O1-
ANISOU  947  OD2 ASP A 110     2465   2923   2858    623    402    660       O1-
ATOM    948  N   ASP A 111      11.568   0.078  -0.025  1.00 11.42           N  
ANISOU  948  N   ASP A 111     1132   1819   1386    -20    -87   -204       N  
ATOM    949  CA  ASP A 111      10.201   0.540  -0.089  1.00 11.18           C  
ANISOU  949  CA  ASP A 111      988   1769   1489   -176      3   -192       C  
ATOM    950  C   ASP A 111       9.594   0.868   1.281  1.00 10.94           C  
ANISOU  950  C   ASP A 111      729   1736   1688    -52     12   -304       C  
ATOM    951  O   ASP A 111       8.428   1.169   1.359  1.00 13.22           O  
ANISOU  951  O   ASP A 111      920   2323   1779    188   -118   -635       O  
ATOM    952  CB  ASP A 111       9.300  -0.489  -0.817  1.00 11.88           C  
ANISOU  952  CB  ASP A 111     1212   1884   1418   -184     -1   -212       C  
ATOM    953  CG  ASP A 111       9.634  -0.584  -2.283  1.00 13.73           C  
ANISOU  953  CG  ASP A 111     1766   1775   1674     72    143    -99       C  
ATOM    954  OD1 ASP A 111       9.849   0.478  -2.893  1.00 15.76           O  
ANISOU  954  OD1 ASP A 111     2381   2041   1565   -426     50   -168       O  
ATOM    955  OD2 ASP A 111       9.692  -1.705  -2.816  1.00 16.46           O1-
ANISOU  955  OD2 ASP A 111     2623   1954   1677      6    324   -326       O1-
ATOM    956  N   LYS A 112      10.457   0.874   2.318  1.00 11.69           N  
ANISOU  956  N   LYS A 112     1345   1608   1487   -127    248   -167       N  
ATOM    957  CA ALYS A 112      10.043   1.069   3.715  0.50 11.53           C  
ANISOU  957  CA ALYS A 112     1435   1510   1435   -187    226   -138       C  
ATOM    958  CA BLYS A 112       9.929   1.119   3.649  0.50 11.52           C  
ANISOU  958  CA BLYS A 112     1404   1567   1405    -92    210   -143       C  
ATOM    959  C   LYS A 112      10.332   2.467   4.175  1.00 10.86           C  
ANISOU  959  C   LYS A 112     1320   1458   1347    -81    142    -68       C  
ATOM    960  O   LYS A 112      11.163   3.143   3.621  1.00 11.84           O  
ANISOU  960  O   LYS A 112     1646   1405   1445   -191    307    -22       O  
ATOM    961  CB ALYS A 112      10.832   0.118   4.630  0.50 11.52           C  
ANISOU  961  CB ALYS A 112     1410   1458   1507    -96    401   -133       C  
ATOM    962  CB BLYS A 112      10.403  -0.007   4.550  0.50 12.25           C  
ANISOU  962  CB BLYS A 112     1565   1657   1431      9    179   -124       C  
ATOM    963  CG ALYS A 112      10.562  -1.387   4.425  0.50 13.14           C  
ANISOU  963  CG ALYS A 112     1723   1511   1758   -334    276   -118       C  
ATOM    964  CG BLYS A 112      10.060  -1.380   3.995  0.50 13.58           C  
ANISOU  964  CG BLYS A 112     1602   1859   1696      4    245   -195       C  
ATOM    965  CD ALYS A 112       9.081  -1.741   4.359  0.50 17.07           C  
ANISOU  965  CD ALYS A 112     2005   2266   2214   -234    214    -41       C  
ATOM    966  CD BLYS A 112      10.460  -2.488   4.924  0.50 18.53           C  
ANISOU  966  CD BLYS A 112     2424   2333   2282    265    145    -95       C  
ATOM    967  CE ALYS A 112       8.892  -3.235   4.622  0.50 19.47           C  
ANISOU  967  CE ALYS A 112     2139   2504   2752   -270    202     38       C  
ATOM    968  CE BLYS A 112      10.170  -3.862   4.336  0.50 20.43           C  
ANISOU  968  CE BLYS A 112     2536   2427   2799    212     19   -147       C  
ATOM    969  NZ ALYS A 112       7.526  -3.675   4.388  0.50 20.22           N1+
ANISOU  969  NZ ALYS A 112     2215   2390   3078   -824    189     71       N1+
ATOM    970  NZ BLYS A 112      10.305  -4.937   5.373  0.50 22.95           N1+
ANISOU  970  NZ BLYS A 112     2791   2667   3260    457    -90    -46       N1+
ATOM    971  N   LEU A 113       9.619   2.854   5.218  1.00  9.26           N  
ANISOU  971  N   LEU A 113      888   1248   1379   -182     37   -123       N  
ATOM    972  CA ALEU A 113       9.949   4.059   5.985  0.50  9.19           C  
ANISOU  972  CA ALEU A 113      880   1276   1334   -300    -16    -72       C  
ATOM    973  CA BLEU A 113       9.937   4.037   5.996  0.50  9.78           C  
ANISOU  973  CA BLEU A 113     1100   1259   1355   -308    -68    -70       C  
ATOM    974  C   LEU A 113      10.365   3.504   7.371  1.00  9.36           C  
ANISOU  974  C   LEU A 113     1119   1098   1336   -219    -69   -134       C  
ATOM    975  O   LEU A 113       9.558   2.920   8.072  1.00 11.23           O  
ANISOU  975  O   LEU A 113     1434   1386   1446   -132     79    155       O  
ATOM    976  CB ALEU A 113       8.776   5.057   5.996  0.50 10.41           C  
ANISOU  976  CB ALEU A 113     1156   1388   1411   -213     65   -136       C  
ATOM    977  CB BLEU A 113       8.713   4.929   6.078  0.50 11.09           C  
ANISOU  977  CB BLEU A 113     1379   1338   1493   -255    -49   -159       C  
ATOM    978  CG ALEU A 113       9.031   6.495   6.481  0.50  9.35           C  
ANISOU  978  CG ALEU A 113      319   1616   1615     62    239    -95       C  
ATOM    979  CG BLEU A 113       8.953   6.171   6.906  0.50 12.81           C  
ANISOU  979  CG BLEU A 113     1916   1350   1599   -159   -212    -77       C  
ATOM    980  CD1ALEU A 113       7.856   7.376   6.119  0.50 10.07           C  
ANISOU  980  CD1ALEU A 113      346   1593   1886   -176    290    300       C  
ATOM    981  CD1BLEU A 113      10.220   6.936   6.328  0.50 13.95           C  
ANISOU  981  CD1BLEU A 113     1399   1522   2378    -32   -379   -170       C  
ATOM    982  CD2ALEU A 113       9.271   6.458   7.989  0.50 12.31           C  
ANISOU  982  CD2ALEU A 113     1281   1645   1748    343    503    220       C  
ATOM    983  CD2BLEU A 113       7.685   6.982   6.922  0.50 16.96           C  
ANISOU  983  CD2BLEU A 113     2234   1855   2353   -115   -109   -394       C  
ATOM    984  N   VAL A 114      11.631   3.731   7.722  1.00  9.00           N  
ANISOU  984  N   VAL A 114     1020   1122   1275   -338     63      9       N  
ATOM    985  CA  VAL A 114      12.232   3.232   8.961  1.00 10.12           C  
ANISOU  985  CA  VAL A 114     1348   1078   1418   -140    128     99       C  
ATOM    986  C   VAL A 114      12.292   4.389   9.929  1.00 10.02           C  
ANISOU  986  C   VAL A 114     1256   1248   1301   -206    -11    -32       C  
ATOM    987  O   VAL A 114      12.722   5.505   9.589  1.00 11.11           O  
ANISOU  987  O   VAL A 114     1618   1271   1331   -344    206    -10       O  
ATOM    988  CB  VAL A 114      13.576   2.565   8.719  1.00 10.74           C  
ANISOU  988  CB  VAL A 114     1234   1189   1655    -76     58     26       C  
ATOM    989  CG1 VAL A 114      14.151   2.027  10.042  1.00 13.12           C  
ANISOU  989  CG1 VAL A 114     1540   1763   1681     33    136    113       C  
ATOM    990  CG2 VAL A 114      13.431   1.431   7.695  1.00 13.44           C  
ANISOU  990  CG2 VAL A 114     1840   1418   1846    321    117   -268       C  
ATOM    991  N   VAL A 115      11.830   4.122  11.145  1.00 10.05           N  
ANISOU  991  N   VAL A 115     1496   1001   1319   -117     53     65       N  
ATOM    992  CA  VAL A 115      11.769   5.108  12.216  1.00  9.91           C  
ANISOU  992  CA  VAL A 115     1286   1052   1427   -140    -56     40       C  
ATOM    993  C   VAL A 115      12.690   4.629  13.335  1.00 10.12           C  
ANISOU  993  C   VAL A 115     1258   1190   1397    -73   -199    201       C  
ATOM    994  O   VAL A 115      12.542   3.530  13.846  1.00 13.28           O  
ANISOU  994  O   VAL A 115     1812   1459   1774   -317   -326    363       O  
ATOM    995  CB  VAL A 115      10.316   5.346  12.685  1.00 11.13           C  
ANISOU  995  CB  VAL A 115     1346   1281   1603     27     91   -111       C  
ATOM    996  CG1 VAL A 115      10.211   6.479  13.734  1.00 14.22           C  
ANISOU  996  CG1 VAL A 115     1482   1951   1970   -315     94   -440       C  
ATOM    997  CG2 VAL A 115       9.438   5.695  11.506  1.00 13.58           C  
ANISOU  997  CG2 VAL A 115     1485   1509   2166   -148   -112     18       C  
ATOM    998  N  AGLU A 116      13.645   5.459  13.700  0.50  9.09           N  
ANISOU  998  N  AGLU A 116      977   1122   1353    100   -214    183       N  
ATOM    999  N  BGLU A 116      13.619   5.466  13.748  0.50  9.98           N  
ANISOU  999  N  BGLU A 116     1180   1208   1403    -33   -181    178       N  
ATOM   1000  CA AGLU A 116      14.565   5.202  14.815  0.50  8.94           C  
ANISOU 1000  CA AGLU A 116      848    954   1592    294   -107     85       C  
ATOM   1001  CA BGLU A 116      14.539   5.151  14.849  0.50 10.63           C  
ANISOU 1001  CA BGLU A 116     1189   1198   1651     57   -111     93       C  
ATOM   1002  C  AGLU A 116      14.167   6.201  15.918  0.50  9.28           C  
ANISOU 1002  C  AGLU A 116     1091   1102   1330    155   -154    -34       C  
ATOM   1003  C  BGLU A 116      14.364   6.159  15.950  0.50 10.02           C  
ANISOU 1003  C  BGLU A 116     1191   1205   1408     22   -197     -4       C  
ATOM   1004  O  AGLU A 116      13.976   7.388  15.667  0.50  9.49           O  
ANISOU 1004  O  AGLU A 116     1257   1002   1344    243   -245    117       O  
ATOM   1005  O  BGLU A 116      14.691   7.330  15.748  0.50  8.42           O  
ANISOU 1005  O  BGLU A 116      898    939   1360     64   -267    101       O  
ATOM   1006  CB AGLU A 116      16.020   5.321  14.372  0.50 10.70           C  
ANISOU 1006  CB AGLU A 116      900   1404   1760    217   -244     82       C  
ATOM   1007  CB BGLU A 116      15.967   5.245  14.417  0.50 12.57           C  
ANISOU 1007  CB BGLU A 116     1317   1577   1879    -45   -174    109       C  
ATOM   1008  CG AGLU A 116      17.059   4.986  15.431  0.50 11.21           C  
ANISOU 1008  CG AGLU A 116      739   1468   2051    754    -71    170       C  
ATOM   1009  CG BGLU A 116      16.569   4.042  13.908  0.50 16.34           C  
ANISOU 1009  CG BGLU A 116     1706   2085   2417     14     -5     -2       C  
ATOM   1010  CD AGLU A 116      18.467   5.601  15.167  0.50 14.00           C  
ANISOU 1010  CD AGLU A 116     1041   2145   2131    460   -216   -183       C  
ATOM   1011  CD BGLU A 116      18.066   4.111  14.055  0.50 19.18           C  
ANISOU 1011  CD BGLU A 116     1530   2645   3109    495   -157   -174       C  
ATOM   1012  OE1AGLU A 116      18.624   6.844  15.197  0.50 17.67           O  
ANISOU 1012  OE1AGLU A 116     2307   2341   2063    -19     90     51       O  
ATOM   1013  OE1BGLU A 116      18.599   5.125  14.567  0.50 20.86           O  
ANISOU 1013  OE1BGLU A 116     1387   3322   3216    756   -888   -705       O  
ATOM   1014  OE2AGLU A 116      19.433   4.837  14.957  0.50 13.83           O1-
ANISOU 1014  OE2AGLU A 116      270   2128   2857    178     -3    163       O1-
ATOM   1015  OE2BGLU A 116      18.710   3.146  13.682  0.50 20.25           O1-
ANISOU 1015  OE2BGLU A 116      703   3414   3574   1051   -317   -253       O1-
ATOM   1016  N   CYS A 117      13.918   5.683  17.105  1.00  9.72           N  
ANISOU 1016  N   CYS A 117     1326   1028   1339    211   -159     34       N  
ATOM   1017  CA  CYS A 117      13.614   6.492  18.268  1.00 10.54           C  
ANISOU 1017  CA  CYS A 117     1432   1042   1529    321   -200     51       C  
ATOM   1018  C   CYS A 117      14.704   6.259  19.277  1.00 10.71           C  
ANISOU 1018  C   CYS A 117     1429   1264   1374    130   -245     45       C  
ATOM   1019  O   CYS A 117      14.942   5.142  19.709  1.00 11.16           O  
ANISOU 1019  O   CYS A 117     1748   1027   1465     99   -306    125       O  
ATOM   1020  CB  CYS A 117      12.237   6.040  18.873  1.00 12.06           C  
ANISOU 1020  CB  CYS A 117     1412   1570   1600    337   -305     -3       C  
ATOM   1021  SG  CYS A 117      10.872   6.014  17.707  1.00 15.75           S  
ANISOU 1021  SG  CYS A 117     1737   2445   1799    386   -192    152       S  
ATOM   1022  N   VAL A 118      15.311   7.345  19.710  1.00 10.36           N  
ANISOU 1022  N   VAL A 118     1289   1096   1550    143   -165     83       N  
ATOM   1023  CA  VAL A 118      16.474   7.278  20.549  1.00 10.36           C  
ANISOU 1023  CA  VAL A 118      975   1200   1760     97   -104      4       C  
ATOM   1024  C   VAL A 118      16.280   8.127  21.813  1.00 10.98           C  
ANISOU 1024  C   VAL A 118     1327   1192   1651    154   -176     56       C  
ATOM   1025  O   VAL A 118      15.929   9.317  21.738  1.00 11.54           O  
ANISOU 1025  O   VAL A 118     1569   1151   1665    434   -183      7       O  
ATOM   1026  CB  VAL A 118      17.800   7.751  19.849  1.00 12.12           C  
ANISOU 1026  CB  VAL A 118     1082   1363   2158   -163   -175    -78       C  
ATOM   1027  CG1 VAL A 118      18.888   7.839  20.794  1.00 15.73           C  
ANISOU 1027  CG1 VAL A 118      498   2321   3158    -80   -102   -229       C  
ATOM   1028  CG2 VAL A 118      18.182   6.871  18.725  1.00 16.34           C  
ANISOU 1028  CG2 VAL A 118     1780   1894   2533    185    331   -217       C  
ATOM   1029  N   MET A 119      16.519   7.498  22.952  1.00 11.35           N  
ANISOU 1029  N   MET A 119     1552   1073   1685    159   -244     53       N  
ATOM   1030  CA AMET A 119      16.561   8.219  24.217  0.50 12.68           C  
ANISOU 1030  CA AMET A 119     1728   1391   1697    242   -338     74       C  
ATOM   1031  CA BMET A 119      16.487   8.175  24.259  0.50 12.57           C  
ANISOU 1031  CA BMET A 119     1726   1338   1710    174   -303    136       C  
ATOM   1032  C   MET A 119      17.751   7.650  24.955  1.00 13.24           C  
ANISOU 1032  C   MET A 119     1749   1512   1768    304   -341     56       C  
ATOM   1033  O   MET A 119      17.795   6.502  25.349  1.00 12.56           O  
ANISOU 1033  O   MET A 119     1496   1543   1730    514   -310    -13       O  
ATOM   1034  CB AMET A 119      15.257   8.032  24.983  0.50 12.55           C  
ANISOU 1034  CB AMET A 119     1503   1536   1728    438   -432    -76       C  
ATOM   1035  CB BMET A 119      15.172   7.788  24.995  0.50 12.40           C  
ANISOU 1035  CB BMET A 119     1443   1484   1784    265   -403     16       C  
ATOM   1036  CG AMET A 119      15.296   8.500  26.427  0.50 14.81           C  
ANISOU 1036  CG AMET A 119     1863   1925   1837    225   -384   -115       C  
ATOM   1037  CG BMET A 119      14.862   8.498  26.328  0.50 13.24           C  
ANISOU 1037  CG BMET A 119     1663   1485   1880     -5   -359    224       C  
ATOM   1038  SD AMET A 119      14.360  10.003  26.582  0.50 16.05           S  
ANISOU 1038  SD AMET A 119     2019   1741   2337    248   -128   -322       S  
ATOM   1039  SD BMET A 119      15.103  10.279  26.176  0.50 12.07           S  
ANISOU 1039  SD BMET A 119     1488   1424   1673     13     70    213       S  
ATOM   1040  CE AMET A 119      15.338  10.869  27.839  0.50 15.38           C  
ANISOU 1040  CE AMET A 119     1148   1895   2799   -547   -579   -284       C  
ATOM   1041  CE BMET A 119      14.629  10.798  27.892  0.50 12.20           C  
ANISOU 1041  CE BMET A 119     1411   1513   1710    -41   -384    151       C  
ATOM   1042  N   LYS A 120      18.737   8.516  25.088  1.00 15.78           N  
ANISOU 1042  N   LYS A 120     2146   1598   2249    259   -334    113       N  
ATOM   1043  CA  LYS A 120      19.979   8.191  25.692  1.00 18.12           C  
ANISOU 1043  CA  LYS A 120     2208   2134   2540     69   -241    109       C  
ATOM   1044  C   LYS A 120      20.554   6.986  24.930  1.00 16.34           C  
ANISOU 1044  C   LYS A 120     1776   2007   2425   -169   -382    124       C  
ATOM   1045  O   LYS A 120      20.728   7.001  23.701  1.00 18.09           O  
ANISOU 1045  O   LYS A 120     1959   2149   2764    -47   -199    326       O  
ATOM   1046  CB  LYS A 120      19.794   8.005  27.214  1.00 17.44           C  
ANISOU 1046  CB  LYS A 120     2260   1875   2491    231   -474    101       C  
ATOM   1047  CG  LYS A 120      19.443   9.318  27.926  1.00 22.82           C  
ANISOU 1047  CG  LYS A 120     3078   2606   2987    210   -148   -131       C  
ATOM   1048  CD  LYS A 120      18.593   9.124  29.160  1.00 27.51           C  
ANISOU 1048  CD  LYS A 120     3684   3412   3353    168      0   -279       C  
ATOM   1049  CE  LYS A 120      19.329   8.414  30.270  1.00 32.21           C  
ANISOU 1049  CE  LYS A 120     4257   4149   3832    214      9    -68       C  
ATOM   1050  NZ  LYS A 120      18.361   7.996  31.345  1.00 35.26           N1+
ANISOU 1050  NZ  LYS A 120     4569   4932   3896    372    311   -418       N1+
ATOM   1051  N   GLY A 121      20.829   5.908  25.629  1.00 14.75           N  
ANISOU 1051  N   GLY A 121     1260   1847   2496   -224   -321    195       N  
ATOM   1052  CA  GLY A 121      21.447   4.748  24.978  1.00 14.33           C  
ANISOU 1052  CA  GLY A 121     1320   1761   2363   -146   -167    195       C  
ATOM   1053  C   GLY A 121      20.447   3.761  24.475  1.00 13.23           C  
ANISOU 1053  C   GLY A 121     1352   1586   2087   -176   -250    198       C  
ATOM   1054  O   GLY A 121      20.805   2.701  24.020  1.00 13.79           O  
ANISOU 1054  O   GLY A 121     1210   1701   2326    153     29    380       O  
ATOM   1055  N   VAL A 122      19.155   4.079  24.577  1.00 12.36           N  
ANISOU 1055  N   VAL A 122     1441   1254   2000    -44   -217    235       N  
ATOM   1056  CA  VAL A 122      18.103   3.166  24.134  1.00 10.74           C  
ANISOU 1056  CA  VAL A 122     1053   1200   1828    224   -143    168       C  
ATOM   1057  C   VAL A 122      17.555   3.578  22.803  1.00 12.28           C  
ANISOU 1057  C   VAL A 122     1515   1407   1742    239   -247    223       C  
ATOM   1058  O   VAL A 122      17.098   4.721  22.627  1.00 13.43           O  
ANISOU 1058  O   VAL A 122     2067   1216   1819    537   -501     90       O  
ATOM   1059  CB  VAL A 122      16.988   3.053  25.163  1.00 11.46           C  
ANISOU 1059  CB  VAL A 122     1023   1382   1948    238    -17    154       C  
ATOM   1060  CG1 VAL A 122      15.870   2.112  24.689  1.00 13.80           C  
ANISOU 1060  CG1 VAL A 122     1145   1652   2443    107     74    256       C  
ATOM   1061  CG2 VAL A 122      17.538   2.577  26.520  1.00 13.35           C  
ANISOU 1061  CG2 VAL A 122     1171   1847   2054    217     48    491       C  
ATOM   1062  N   THR A 123      17.568   2.661  21.850  1.00 11.41           N  
ANISOU 1062  N   THR A 123     1268   1189   1876    340   -196    204       N  
ATOM   1063  CA  THR A 123      17.057   2.868  20.520  1.00 12.72           C  
ANISOU 1063  CA  THR A 123     1670   1299   1864    164   -143    151       C  
ATOM   1064  C   THR A 123      15.914   1.872  20.255  1.00 11.69           C  
ANISOU 1064  C   THR A 123     1466   1130   1845    233   -432     44       C  
ATOM   1065  O   THR A 123      16.045   0.646  20.534  1.00 16.03           O  
ANISOU 1065  O   THR A 123     2086   1451   2550    240   -437    334       O  
ATOM   1066  CB  THR A 123      18.131   2.668  19.473  1.00 13.62           C  
ANISOU 1066  CB  THR A 123     1524   1649   1999    135   -125    -31       C  
ATOM   1067  CG2 THR A 123      17.623   2.925  18.046  1.00 16.59           C  
ANISOU 1067  CG2 THR A 123     2330   2053   1918    171     59    122       C  
ATOM   1068  OG1 THR A 123      19.202   3.535  19.781  1.00 17.23           O  
ANISOU 1068  OG1 THR A 123     1922   2062   2562   -123    136   -118       O  
ATOM   1069  N   SER A 124      14.871   2.326  19.640  1.00 10.48           N  
ANISOU 1069  N   SER A 124     1204   1159   1618   -132   -319    284       N  
ATOM   1070  CA  SER A 124      13.826   1.491  19.093  1.00 10.04           C  
ANISOU 1070  CA  SER A 124      987   1183   1643     53   -205    288       C  
ATOM   1071  C   SER A 124      13.687   1.727  17.616  1.00 11.10           C  
ANISOU 1071  C   SER A 124     1354   1367   1494    126   -159    242       C  
ATOM   1072  O   SER A 124      13.750   2.853  17.160  1.00 12.60           O  
ANISOU 1072  O   SER A 124     2119   1164   1503     32    -61    256       O  
ATOM   1073  CB  SER A 124      12.468   1.779  19.758  1.00 10.85           C  
ANISOU 1073  CB  SER A 124     1181   1242   1700     51   -222    197       C  
ATOM   1074  OG  SER A 124      11.375   1.187  19.103  1.00 12.01           O  
ANISOU 1074  OG  SER A 124     1259   1557   1744     30     51    121       O  
ATOM   1075  N   THR A 125      13.494   0.657  16.848  1.00  9.73           N  
ANISOU 1075  N   THR A 125     1131   1085   1478    101   -128    245       N  
ATOM   1076  CA  THR A 125      13.352   0.725  15.411  1.00 10.88           C  
ANISOU 1076  CA  THR A 125     1221   1357   1555    266     33    189       C  
ATOM   1077  C   THR A 125      11.986   0.251  15.017  1.00 10.41           C  
ANISOU 1077  C   THR A 125     1197   1353   1402    -32     35    110       C  
ATOM   1078  O   THR A 125      11.534  -0.836  15.420  1.00 11.49           O  
ANISOU 1078  O   THR A 125     1320   1367   1678   -209   -134    251       O  
ATOM   1079  CB  THR A 125      14.381  -0.168  14.704  1.00 12.04           C  
ANISOU 1079  CB  THR A 125      908   1892   1773    302     10     99       C  
ATOM   1080  CG2 THR A 125      14.253  -0.111  13.214  1.00 16.00           C  
ANISOU 1080  CG2 THR A 125     1524   2709   1844    410    160    -32       C  
ATOM   1081  OG1 THR A 125      15.670   0.297  15.063  1.00 16.37           O  
ANISOU 1081  OG1 THR A 125     1411   2266   2541    608    187      2       O  
ATOM   1082  N   ARG A 126      11.273   1.090  14.293  1.00 10.54           N  
ANISOU 1082  N   ARG A 126     1380   1271   1353   -229   -286    149       N  
ATOM   1083  CA  ARG A 126       9.942   0.792  13.839  1.00 11.41           C  
ANISOU 1083  CA  ARG A 126     1534   1426   1374   -342    -71    204       C  
ATOM   1084  C   ARG A 126       9.922   0.847  12.333  1.00 11.01           C  
ANISOU 1084  C   ARG A 126     1333   1507   1343   -304   -207    247       C  
ATOM   1085  O   ARG A 126      10.499   1.728  11.758  1.00 15.21           O  
ANISOU 1085  O   ARG A 126     2380   1916   1481   -986   -119    288       O  
ATOM   1086  CB  ARG A 126       8.963   1.747  14.458  1.00 12.45           C  
ANISOU 1086  CB  ARG A 126     1422   1869   1439   -359    -62     33       C  
ATOM   1087  CG  ARG A 126       8.781   1.420  15.960  1.00 17.05           C  
ANISOU 1087  CG  ARG A 126     2054   2525   1897    232   -285     90       C  
ATOM   1088  CD  ARG A 126       8.161   2.465  16.734  1.00 19.63           C  
ANISOU 1088  CD  ARG A 126     2340   3098   2017    225   -318     25       C  
ATOM   1089  NE  ARG A 126       6.733   2.681  16.577  1.00 20.24           N  
ANISOU 1089  NE  ARG A 126     2313   3517   1858   -201   -178   -218       N  
ATOM   1090  CZ  ARG A 126       5.746   2.055  17.220  1.00 18.10           C  
ANISOU 1090  CZ  ARG A 126     2234   3004   1639   -542   -378    -50       C  
ATOM   1091  NH1 ARG A 126       5.932   0.901  17.837  1.00 18.51           N1+
ANISOU 1091  NH1 ARG A 126     2079   3258   1693     76   -363   -196       N1+
ATOM   1092  NH2 ARG A 126       4.509   2.482  17.049  1.00 19.96           N  
ANISOU 1092  NH2 ARG A 126     2199   3004   2379   -600     68    118       N  
ATOM   1093  N   VAL A 127       9.227  -0.074  11.687  1.00 10.65           N  
ANISOU 1093  N   VAL A 127     1386   1359   1302   -370   -158    147       N  
ATOM   1094  CA  VAL A 127       9.316  -0.164  10.251  1.00 10.49           C  
ANISOU 1094  CA  VAL A 127     1129   1432   1422   -281   -101     -9       C  
ATOM   1095  C   VAL A 127       7.893  -0.046   9.734  1.00  9.31           C  
ANISOU 1095  C   VAL A 127     1034   1258   1245   -179    -48    -68       C  
ATOM   1096  O   VAL A 127       6.986  -0.770  10.160  1.00  9.95           O  
ANISOU 1096  O   VAL A 127      845   1469   1464   -258    -17    133       O  
ATOM   1097  CB  VAL A 127       9.875  -1.481   9.760  1.00 11.59           C  
ANISOU 1097  CB  VAL A 127     1100   1656   1648    -28      0    -43       C  
ATOM   1098  CG1 VAL A 127       9.867  -1.479   8.213  1.00 13.70           C  
ANISOU 1098  CG1 VAL A 127     1532   2086   1585    490   -106   -179       C  
ATOM   1099  CG2 VAL A 127      11.292  -1.674  10.308  1.00 13.67           C  
ANISOU 1099  CG2 VAL A 127     1140   1846   2205     23      9     69       C  
ATOM   1100  N   TYR A 128       7.693   0.931   8.816  1.00  9.25           N  
ANISOU 1100  N   TYR A 128      907   1279   1327   -225     80    110       N  
ATOM   1101  CA  TYR A 128       6.451   1.140   8.129  1.00  9.22           C  
ANISOU 1101  CA  TYR A 128      754   1275   1472   -207    -64     77       C  
ATOM   1102  C   TYR A 128       6.547   0.730   6.676  1.00  8.41           C  
ANISOU 1102  C   TYR A 128      253   1335   1606     11    -10      1       C  
ATOM   1103  O   TYR A 128       7.582   0.955   6.058  1.00 10.57           O  
ANISOU 1103  O   TYR A 128     1050   1467   1496   -341     95   -100       O  
ATOM   1104  CB  TYR A 128       6.038   2.636   8.192  1.00 10.18           C  
ANISOU 1104  CB  TYR A 128     1105   1232   1529   -104    -55    -31       C  
ATOM   1105  CG  TYR A 128       5.563   3.097   9.572  1.00  9.18           C  
ANISOU 1105  CG  TYR A 128      422   1350   1715   -319   -348     51       C  
ATOM   1106  CD1 TYR A 128       6.506   3.374  10.559  1.00 11.40           C  
ANISOU 1106  CD1 TYR A 128      441   1733   2153   -524    -40    -78       C  
ATOM   1107  CD2 TYR A 128       4.271   3.309   9.836  1.00  9.33           C  
ANISOU 1107  CD2 TYR A 128      306   1442   1796   -173   -218     85       C  
ATOM   1108  CE1 TYR A 128       6.077   3.826  11.870  1.00 13.51           C  
ANISOU 1108  CE1 TYR A 128     1473   1835   1824    -81   -228   -278       C  
ATOM   1109  CE2 TYR A 128       3.823   3.744  11.095  1.00 12.42           C  
ANISOU 1109  CE2 TYR A 128     1534   1530   1653   -180     31    -37       C  
ATOM   1110  CZ  TYR A 128       4.739   4.024  12.075  1.00 12.43           C  
ANISOU 1110  CZ  TYR A 128     1319   1728   1673   -450   -155   -145       C  
ATOM   1111  OH  TYR A 128       4.173   4.384  13.287  1.00 15.69           O  
ANISOU 1111  OH  TYR A 128     2003   2338   1618    140     57   -359       O  
ATOM   1112  N   GLU A 129       5.434   0.225   6.160  1.00  9.80           N  
ANISOU 1112  N   GLU A 129      646   1468   1607   -104    -20    -26       N  
ATOM   1113  CA AGLU A 129       5.299  -0.134   4.759  0.50 10.84           C  
ANISOU 1113  CA AGLU A 129      923   1540   1654   -123    -28   -142       C  
ATOM   1114  CA BGLU A 129       5.350  -0.027   4.721  0.50 11.54           C  
ANISOU 1114  CA BGLU A 129     1038   1618   1726    -13    -76    -91       C  
ATOM   1115  C   GLU A 129       4.203   0.735   4.152  1.00 10.91           C  
ANISOU 1115  C   GLU A 129     1147   1406   1592      1   -153   -182       C  
ATOM   1116  O   GLU A 129       3.336   1.226   4.855  1.00 10.51           O  
ANISOU 1116  O   GLU A 129     1121   1363   1508   -167    -74      2       O  
ATOM   1117  CB AGLU A 129       5.025  -1.665   4.632  0.50 10.28           C  
ANISOU 1117  CB AGLU A 129      469   1675   1762   -246    -54    -97       C  
ATOM   1118  CB BGLU A 129       5.275  -1.527   4.369  0.50 12.59           C  
ANISOU 1118  CB BGLU A 129     1100   1784   1899    143   -184    -54       C  
ATOM   1119  CG AGLU A 129       6.282  -2.526   4.906  0.50 13.56           C  
ANISOU 1119  CG AGLU A 129      995   2053   2102    206   -287   -100       C  
ATOM   1120  CG BGLU A 129       3.914  -2.167   4.386  0.50 14.68           C  
ANISOU 1120  CG BGLU A 129      605   2355   2617    487   -311    231       C  
ATOM   1121  CD AGLU A 129       5.955  -4.045   4.835  0.50 16.47           C  
ANISOU 1121  CD AGLU A 129     1270   2244   2742   -112   -295   -144       C  
ATOM   1122  CD BGLU A 129       4.068  -3.657   4.072  0.50 21.19           C  
ANISOU 1122  CD BGLU A 129     2395   2627   3028    236    -78     17       C  
ATOM   1123  OE1AGLU A 129       4.759  -4.403   4.648  0.50 19.18           O  
ANISOU 1123  OE1AGLU A 129     2187   2016   3084   -403   -369   -100       O  
ATOM   1124  OE1BGLU A 129       3.074  -4.379   4.064  0.50 23.96           O  
ANISOU 1124  OE1BGLU A 129     2766   2686   3651     45   -211     80       O  
ATOM   1125  OE2AGLU A 129       6.867  -4.863   5.025  0.50 23.44           O1-
ANISOU 1125  OE2AGLU A 129     2845   2667   3393     61   -260    122       O1-
ATOM   1126  OE2BGLU A 129       5.225  -4.100   3.847  0.50 24.22           O1-
ANISOU 1126  OE2BGLU A 129     2957   3157   3088    374    282    -23       O1-
ATOM   1127  N   ARG A 130       4.194   0.866   2.842  1.00 10.76           N  
ANISOU 1127  N   ARG A 130     1097   1483   1506    -14   -205   -221       N  
ATOM   1128  CA  ARG A 130       3.089   1.570   2.192  1.00 13.21           C  
ANISOU 1128  CA  ARG A 130     1574   1734   1710      8   -318   -156       C  
ATOM   1129  C   ARG A 130       1.766   0.891   2.475  1.00 14.34           C  
ANISOU 1129  C   ARG A 130     1607   1741   2099    -16   -399   -248       C  
ATOM   1130  O   ARG A 130       1.622  -0.358   2.410  1.00 15.66           O  
ANISOU 1130  O   ARG A 130     1869   1603   2478   -197   -544   -289       O  
ATOM   1131  CB  ARG A 130       3.303   1.582   0.701  1.00 14.70           C  
ANISOU 1131  CB  ARG A 130     1805   2082   1696     69   -411    -77       C  
ATOM   1132  CG  ARG A 130       4.465   2.316   0.277  1.00 16.88           C  
ANISOU 1132  CG  ARG A 130     2342   2219   1851     44   -135    187       C  
ATOM   1133  CD  ARG A 130       4.184   3.763   0.142  1.00 18.08           C  
ANISOU 1133  CD  ARG A 130     2013   2260   2595    237   -115     86       C  
ATOM   1134  NE  ARG A 130       5.349   4.478  -0.383  1.00 18.32           N  
ANISOU 1134  NE  ARG A 130     2384   2033   2541    -28    -33    227       N  
ATOM   1135  CZ  ARG A 130       5.411   5.790  -0.544  1.00 16.56           C  
ANISOU 1135  CZ  ARG A 130     2289   1898   2104   -169   -238    185       C  
ATOM   1136  NH1 ARG A 130       4.386   6.540  -0.286  1.00 16.38           N1+
ANISOU 1136  NH1 ARG A 130     2218   1943   2063   -238   -314    136       N1+
ATOM   1137  NH2 ARG A 130       6.542   6.343  -0.949  1.00 18.46           N  
ANISOU 1137  NH2 ARG A 130     2442   2149   2422   -344    127     42       N  
ATOM   1138  N   ALA A 131       0.768   1.689   2.794  1.00 15.38           N  
ANISOU 1138  N   ALA A 131     1519   1879   2444   -184   -316   -174       N  
ATOM   1139  CA  ALA A 131      -0.516   1.151   3.150  1.00 18.11           C  
ANISOU 1139  CA  ALA A 131     1716   2271   2893   -196   -288    -58       C  
ATOM   1140  C   ALA A 131      -1.245   0.582   1.912  1.00 20.22           C  
ANISOU 1140  C   ALA A 131     1855   2613   3213   -359   -421    -77       C  
ATOM   1141  O   ALA A 131      -0.903   0.943   0.800  1.00 22.45           O  
ANISOU 1141  O   ALA A 131     2227   2975   3328   -392   -800   -114       O  
ATOM   1142  CB  ALA A 131      -1.346   2.232   3.825  1.00 19.20           C  
ANISOU 1142  CB  ALA A 131     1798   2391   3104   -176    -67   -170       C  
TER   
HETATM 1143  C1  IBP A 133       5.912   6.100  15.533  1.00 23.49           C  
ANISOU 1143  C1  IBP A 133     3022   2729   3173    919   -547   -318       C  
HETATM 1144  O1  IBP A 133       5.828   4.891  15.301  1.00 21.01           O  
ANISOU 1144  O1  IBP A 133     3376   2420   2183    550   -544   -155       O  
HETATM 1145  C2  IBP A 133       4.998   8.580  21.675  1.00 21.54           C  
ANISOU 1145  C2  IBP A 133     2827   2760   2598   -137    253    245       C  
HETATM 1146  O2  IBP A 133       5.119   6.949  15.023  1.00 25.39           O  
ANISOU 1146  O2  IBP A 133     3606   2662   3379    877  -1068   -531       O  
HETATM 1147  C3  IBP A 133       4.916   7.519  22.769  1.00 24.21           C  
ANISOU 1147  C3  IBP A 133     3530   2628   3038   -210    392    479       C  
HETATM 1148  C4  IBP A 133       6.354   7.260  23.229  1.00 26.19           C  
ANISOU 1148  C4  IBP A 133     3967   2705   3277    340    435    367       C  
HETATM 1149  C5  IBP A 133       4.046   6.332  22.271  1.00 24.79           C  
ANISOU 1149  C5  IBP A 133     3087   2594   3736     34    302    596       C  
HETATM 1150  C6  IBP A 133       6.959   6.541  16.556  1.00 22.44           C  
ANISOU 1150  C6  IBP A 133     3058   2521   2946    488   -142   -584       C  
HETATM 1151  C7  IBP A 133       7.564   7.849  16.044  1.00 21.52           C  
ANISOU 1151  C7  IBP A 133     2304   2934   2937    346   -436    -34       C  
HETATM 1152  C8  IBP A 133       6.383   6.991  17.891  1.00 19.38           C  
ANISOU 1152  C8  IBP A 133     2528   2350   2484    417   -161   -421       C  
HETATM 1153  C9  IBP A 133       7.295   7.487  18.806  1.00 16.50           C  
ANISOU 1153  C9  IBP A 133     1824   1983   2461    196    158      0       C  
HETATM 1154  C10 IBP A 133       6.818   7.993  20.007  1.00 17.91           C  
ANISOU 1154  C10 IBP A 133     2511   2209   2083    412   -343     57       C  
HETATM 1155  C11 IBP A 133       5.466   7.995  20.324  1.00 18.98           C  
ANISOU 1155  C11 IBP A 133     2493   2423   2294    314   -299     15       C  
HETATM 1156  C12 IBP A 133       4.558   7.493  19.381  1.00 20.07           C  
ANISOU 1156  C12 IBP A 133     2004   2946   2675    300   -259   -279       C  
HETATM 1157  C13 IBP A 133       5.011   7.006  18.157  1.00 21.23           C  
ANISOU 1157  C13 IBP A 133     2346   3047   2674    196   -104   -483       C  
HETATM 1158  O   HOH A 134      -3.992   6.125   7.622  1.00 34.54           O  
ANISOU 1158  O   HOH A 134     2547   3557   7018   -606    975   -361       O  
HETATM 1159  O   HOH A 135      10.423  22.071  12.751  1.00  8.95           O  
ANISOU 1159  O   HOH A 135      908   1004   1488     89    -50     45       O  
HETATM 1160  O   HOH A 136       7.234  24.913  12.333  1.00 11.14           O  
ANISOU 1160  O   HOH A 136     1125   1580   1527   -138    140   -263       O  
HETATM 1161  O   HOH A 137       4.675  24.380  13.250  1.00 10.77           O  
ANISOU 1161  O   HOH A 137      783   1463   1844    -83    -90   -327       O  
HETATM 1162  O   HOH A 138      -2.667   5.959  32.846  1.00 40.24           O  
ANISOU 1162  O   HOH A 138     6076   3644   5566   -429    936    936       O  
HETATM 1163  O   HOH A 139       1.006  20.272   5.118  1.00 13.35           O  
ANISOU 1163  O   HOH A 139     1144   1946   1981   -288   -175    382       O  
HETATM 1164  O   HOH A 140       5.443  -1.126  -1.029  1.00 65.24           O  
ANISOU 1164  O   HOH A 140     7751   8863   8173  -2620  -1448  -3171       O  
HETATM 1165  O   HOH A 141      -2.744  18.850  20.448  1.00 33.54           O  
ANISOU 1165  O   HOH A 141     2830   4986   4927   -343    583   -393       O  
HETATM 1166  O   HOH A 142       9.184  21.330   2.493  1.00 47.27           O  
ANISOU 1166  O   HOH A 142    10914   2967   4078   1331    490   -961       O  
HETATM 1167  O   HOH A 143      13.731  26.627  15.364  1.00 11.65           O  
ANISOU 1167  O   HOH A 143     1275   1298   1854   -405    -29   -169       O  
HETATM 1168  O   HOH A 144      17.988  27.310   5.841  1.00 28.11           O  
ANISOU 1168  O   HOH A 144     2846   4754   3078    166   -286   -282       O  
HETATM 1169  O   HOH A 145      11.705  12.318  12.131  1.00 11.66           O  
ANISOU 1169  O   HOH A 145     1651   1229   1547     98    234    -64       O  
HETATM 1170  O   HOH A 146       0.800   7.512  -1.831  1.00 29.47           O  
ANISOU 1170  O   HOH A 146     4281   4253   2662   -380   -951    756       O  
HETATM 1171  O   HOH A 147       8.697  -3.773   1.127  1.00 40.87           O  
ANISOU 1171  O   HOH A 147     4975   3849   6705  -1958   -893   2275       O  
HETATM 1172  O   HOH A 148       3.755  25.550  17.914  1.00 15.09           O  
ANISOU 1172  O   HOH A 148     1827   1905   2002    768   -144   -385       O  
HETATM 1173  O   HOH A 149      25.608   5.028  23.797  1.00 38.92           O  
ANISOU 1173  O   HOH A 149     5662   4388   4736  -2178   2092    277       O  
HETATM 1174  O   HOH A 150      16.255  23.270   8.777  1.00 29.96           O  
ANISOU 1174  O   HOH A 150     2388   3297   5698   -107   1403  -1337       O  
HETATM 1175  O   HOH A 151       3.956  10.317  13.579  1.00 34.56           O  
ANISOU 1175  O   HOH A 151     3502   5861   3767   -876    186   2545       O  
HETATM 1176  O   HOH A 152       8.450  21.628  26.746  1.00 46.68           O  
ANISOU 1176  O   HOH A 152     7330   4339   6066  -2734   1903  -3159       O  
HETATM 1177  O   HOH A 153      12.687  10.186  31.674  1.00 43.73           O  
ANISOU 1177  O   HOH A 153     8195   5032   3389  -2315  -1509   -667       O  
HETATM 1178  O   HOH A 154       7.294  26.307  -0.920  1.00 37.20           O  
ANISOU 1178  O   HOH A 154     4509   6540   3085  -1925   -141    684       O  
HETATM 1179  O   HOH A 155       6.366  23.729  -4.256  1.00 40.71           O  
ANISOU 1179  O   HOH A 155     4422   6942   4101    367  -1091    -95       O  
HETATM 1180  O   HOH A 156       6.542  21.629  -1.321  1.00 41.76           O  
ANISOU 1180  O   HOH A 156     9217   4045   2603   1492   1426   -257       O  
HETATM 1181  O   HOH A 157      21.528   7.690   8.286  1.00 38.94           O  
ANISOU 1181  O   HOH A 157     4359   6088   4346   1990   -584    668       O  
HETATM 1182  O   HOH A 158      -3.825  -0.547  22.306  1.00 12.31           O  
ANISOU 1182  O   HOH A 158     1231   1428   2016   -344   -261    276       O  
HETATM 1183  O   HOH A 159      -3.150  14.373  19.842  1.00 36.92           O  
ANISOU 1183  O   HOH A 159     4848   5567   3610   -940   1665   -412       O  
HETATM 1184  O   HOH A 160       9.810  23.002   5.422  1.00 14.24           O  
ANISOU 1184  O   HOH A 160     1402   2434   1574    484    -78     81       O  
HETATM 1185  O   HOH A 161       8.926   6.448  -3.435  1.00 49.79           O  
ANISOU 1185  O   HOH A 161     6084   9073   3759   1640   -648    693       O  
HETATM 1186  O   HOH A 162      -3.588   3.265  29.040  1.00 33.01           O  
ANISOU 1186  O   HOH A 162     4058   3243   5240    628  -2311  -1146       O  
HETATM 1187  O   HOH A 163      10.071  -7.071  15.724  1.00 42.92           O  
ANISOU 1187  O   HOH A 163     4620   2468   9219    113    910    938       O  
HETATM 1188  O   HOH A 164       3.311  21.412  23.987  1.00 35.39           O  
ANISOU 1188  O   HOH A 164     6924   2778   3743    752   -245   -508       O  
HETATM 1189  O   HOH A 165       3.820  16.593  -2.153  1.00 40.96           O  
ANISOU 1189  O   HOH A 165     6885   4478   4200  -3205   1228   -860       O  
HETATM 1190  O   HOH A 166      21.097   7.829  15.270  1.00 57.17           O  
ANISOU 1190  O   HOH A 166     4709   3858  13154   -204   2892   1578       O  
HETATM 1191  O   HOH A 167      15.313   8.986   3.214  1.00 18.51           O  
ANISOU 1191  O   HOH A 167     2871   1831   2331   -578    689     21       O  
HETATM 1192  O   HOH A 168      20.541   4.489  17.500  1.00 40.40           O  
ANISOU 1192  O   HOH A 168     5269   3983   6095    764   3091   1850       O  
HETATM 1193  O   HOH A 169       7.646   3.133  -0.720  1.00 27.85           O  
ANISOU 1193  O   HOH A 169     3477   3700   3402   1272   1171    686       O  
HETATM 1194  O   HOH A 170      20.844  11.472  10.863  1.00 67.95           O  
ANISOU 1194  O   HOH A 170     1301  14509  10004   1256   1482   4976       O  
HETATM 1195  O   HOH A 171       1.574   5.786   0.136  1.00 16.50           O  
ANISOU 1195  O   HOH A 171     2229   1951   2089   -275   -442   -223       O  
HETATM 1196  O   HOH A 172       8.812  10.516  21.631  1.00 14.30           O  
ANISOU 1196  O   HOH A 172     1937   1440   2057   -146    373     89       O  
HETATM 1197  O   HOH A 173       2.180   9.830  17.486  1.00 14.66           O  
ANISOU 1197  O   HOH A 173     1521   1798   2250   -129   -212   -102       O  
HETATM 1198  O   HOH A 174       8.783  -3.053  20.098  1.00 17.94           O  
ANISOU 1198  O   HOH A 174     2634   1901   2279    295   -456   -185       O  
HETATM 1199  O   HOH A 175       1.605  15.783  -0.137  1.00 19.58           O  
ANISOU 1199  O   HOH A 175     3340   2532   1564    215   -593   -280       O  
HETATM 1200  O   HOH A 176       7.141  27.732  11.818  1.00 16.84           O  
ANISOU 1200  O   HOH A 176     1089   2056   3250    226   -225   -242       O  
HETATM 1201  O   HOH A 177       4.081  27.142   2.431  1.00 18.67           O  
ANISOU 1201  O   HOH A 177     2401   1994   2696    216   -482    -22       O  
HETATM 1202  O   HOH A 178      -0.526  14.348   6.471  1.00 15.64           O  
ANISOU 1202  O   HOH A 178     1883   1844   2213    -75     48   -101       O  
HETATM 1203  O   HOH A 179      13.318  21.244  28.359  1.00 22.55           O  
ANISOU 1203  O   HOH A 179     3109   2444   3014     -1   -505   -302       O  
HETATM 1204  O   HOH A 180       1.909  12.782  14.317  1.00 18.70           O  
ANISOU 1204  O   HOH A 180     2864   2126   2114   -194    260    660       O  
HETATM 1205  O   HOH A 181      16.127  18.703  14.205  1.00 20.44           O  
ANISOU 1205  O   HOH A 181     3142   2321   2302   -489   -303    178       O  
HETATM 1206  O   HOH A 182      18.010  -3.727   1.242  1.00 58.32           O  
ANISOU 1206  O   HOH A 182     4620   9405   8131   2964    654   3028       O  
HETATM 1207  O   HOH A 183       7.466   5.197  -4.908  1.00 47.01           O  
ANISOU 1207  O   HOH A 183     3918   8777   5163  -1483  -2004    570       O  
HETATM 1208  O   HOH A 184      16.322  21.104   7.262  1.00 17.56           O  
ANISOU 1208  O   HOH A 184     2600   1348   2723   -316    332    270       O  
HETATM 1209  O   HOH A 185       7.274   3.982  35.526  1.00 39.14           O  
ANISOU 1209  O   HOH A 185     7188   4246   3435  -2687   -789     57       O  
HETATM 1210  O   HOH A 186      21.912  11.752   7.606  1.00 64.78           O  
ANISOU 1210  O   HOH A 186     3742   9358  11514    224  -2284    705       O  
HETATM 1211  O   HOH A 187       1.676  26.193   2.181  1.00 19.36           O  
ANISOU 1211  O   HOH A 187     2364   1596   3392    -75     23   -269       O  
HETATM 1212  O   HOH A 188      15.816  -5.815  18.965  1.00 74.67           O  
ANISOU 1212  O   HOH A 188     6075   1382  20912    212  -8190    663       O  
HETATM 1213  O   HOH A 189       3.351  11.444  19.520  1.00 13.84           O  
ANISOU 1213  O   HOH A 189     1215   1786   2256   -174    134    149       O  
HETATM 1214  O   HOH A 190      21.197   9.414  22.582  1.00 54.10           O  
ANISOU 1214  O   HOH A 190    10056   6567   3929  -4926  -1036   1202       O  
HETATM 1215  O   HOH A 191       8.390   2.651  -3.043  1.00 93.12           O  
ANISOU 1215  O   HOH A 191    25407   5760   4212   4036  -1569   2369       O  
HETATM 1216  O   HOH A 192      11.330  -2.802   0.844  1.00 18.62           O  
ANISOU 1216  O   HOH A 192     2864   1788   2421   -259     76    -90       O  
HETATM 1217  O   HOH A 193      20.366  10.967  20.271  1.00 37.49           O  
ANISOU 1217  O   HOH A 193     4037   3067   7138  -1184    748   -420       O  
HETATM 1218  O   HOH A 194      10.358  29.887   6.556  1.00134.64           O  
ANISOU 1218  O   HOH A 194    21199  15094  14860 -13091 -12638   7689       O  
HETATM 1219  O   HOH A 195      11.322  27.956   4.972  1.00 44.57           O  
ANISOU 1219  O   HOH A 195     7731   3425   5777   -540   3102   -134       O  
HETATM 1220  O   HOH A 196       6.323   8.596  12.540  1.00 98.13           O  
ANISOU 1220  O   HOH A 196     7637  23676   5972  -2283  -1358   5370       O  
HETATM 1221  O   HOH A 197       2.884   1.007  18.772  1.00 18.47           O  
ANISOU 1221  O   HOH A 197     1620   3421   1976   -679    161    -41       O  
HETATM 1222  O   HOH A 198      19.744  10.008  17.616  1.00 35.30           O  
ANISOU 1222  O   HOH A 198     4405   3072   5933    783      0    953       O  
HETATM 1223  O   HOH A 199      20.319   4.935  28.471  1.00 21.46           O  
ANISOU 1223  O   HOH A 199     3342   2019   2791    605   -294    250       O  
HETATM 1224  O   HOH A 200       1.973  30.486  -7.078  1.00 40.95           O  
ANISOU 1224  O   HOH A 200     7950   3982   3626  -2682    575    -25       O  
HETATM 1225  O   HOH A 201      12.184  28.507  22.429  1.00 41.70           O  
ANISOU 1225  O   HOH A 201     7549   5320   2974   -234   -841  -1434       O  
HETATM 1226  O   HOH A 202      13.177  21.556  19.833  1.00 18.21           O  
ANISOU 1226  O   HOH A 202     1625   3231   2061  -1031   -217    119       O  
HETATM 1227  O   HOH A 203      -2.830   0.787  -1.295  1.00 37.83           O  
ANISOU 1227  O   HOH A 203     3913   5224   5236     71  -2113   -572       O  
HETATM 1228  O   HOH A 204       2.819  13.910  18.424  1.00 19.48           O  
ANISOU 1228  O   HOH A 204     2852   2101   2448   -366     16     65       O  
HETATM 1229  O   HOH A 205      13.215  -3.910   2.499  1.00 52.18           O  
ANISOU 1229  O   HOH A 205     9635   4171   6019   -631  -3592   2538       O  
HETATM 1230  O   HOH A 206      13.079  -7.594  20.050  1.00 39.13           O  
ANISOU 1230  O   HOH A 206     4891   3073   6903   1227  -1503   -564       O  
HETATM 1231  O   HOH A 207      11.533  -5.809  21.050  1.00 23.95           O  
ANISOU 1231  O   HOH A 207     3955   1306   3837   -484   -136    845       O  
HETATM 1232  O   HOH A 208       6.266  -0.418   1.370  1.00 18.08           O  
ANISOU 1232  O   HOH A 208     1634   2431   2805    160    270   -350       O  
HETATM 1233  O   HOH A 209       6.179  11.389  19.548  1.00 16.45           O  
ANISOU 1233  O   HOH A 209     1203   2142   2904   -394    -27    139       O  
HETATM 1234  O   HOH A 210       2.575   6.713  13.634  1.00 20.46           O  
ANISOU 1234  O   HOH A 210     2265   2080   3428   -214    -14    -12       O  
HETATM 1235  O   HOH A 211      18.219   0.754   1.603  1.00 46.03           O  
ANISOU 1235  O   HOH A 211     3173  10820   3496  -1839    597    427       O  
HETATM 1236  O   HOH A 212       0.636  18.547  18.968  1.00 27.19           O  
ANISOU 1236  O   HOH A 212     2115   3204   5012  -1067  -1042   2086       O  
HETATM 1237  O   HOH A 213       6.067  27.560  15.398  1.00 18.23           O  
ANISOU 1237  O   HOH A 213     1920   1797   3210    401   -955   -472       O  
HETATM 1238  O   HOH A 214      11.461  -3.150  13.676  1.00 19.07           O  
ANISOU 1238  O   HOH A 214     2791   1993   2461    289     -6    -75       O  
HETATM 1239  O   HOH A 215      17.601  -1.636  20.052  1.00 22.09           O  
ANISOU 1239  O   HOH A 215     2831   2174   3385    551   -694   -205       O  
HETATM 1240  O   HOH A 216      13.993  -1.973   4.255  1.00 48.29           O  
ANISOU 1240  O   HOH A 216     7790   5213   5345  -3056    183   1591       O  
HETATM 1241  O   HOH A 217      -0.710  18.743   3.750  1.00 17.96           O  
ANISOU 1241  O   HOH A 217     2425   1742   2654   -207   -744     92       O  
HETATM 1242  O   HOH A 218      17.754  13.818  21.739  1.00 21.78           O  
ANISOU 1242  O   HOH A 218     2174   3715   2387   -584   -213   -349       O  
HETATM 1243  O   HOH A 219      14.644   1.498  29.177  1.00 18.82           O  
ANISOU 1243  O   HOH A 219     1981   2959   2208    324   -355    323       O  
HETATM 1244  O   HOH A 220       0.484   5.071  32.379  1.00 24.92           O  
ANISOU 1244  O   HOH A 220     4441   2841   2185   -269      8   -151       O  
HETATM 1245  O   HOH A 221       6.346   9.135  -1.814  1.00 21.09           O  
ANISOU 1245  O   HOH A 221     2552   2264   3194   -274    472   -471       O  
HETATM 1246  O   HOH A 222       3.588   3.666  35.764  1.00 27.42           O  
ANISOU 1246  O   HOH A 222     5413   3042   1962  -1939   -722    312       O  
HETATM 1247  O   HOH A 223      12.329 -10.063  16.818  1.00 76.29           O  
ANISOU 1247  O   HOH A 223     9617   9035  10334   2058  -3039  -4026       O  
HETATM 1248  O   HOH A 224      17.441  13.356  27.957  1.00 25.00           O  
ANISOU 1248  O   HOH A 224     2710   2959   3828    -71  -1158    864       O  
HETATM 1249  O  AHOH A 225       8.301  -3.472  22.743  0.50 18.86           O  
ANISOU 1249  O  AHOH A 225     1875   2526   2765  -1464    131   -639       O  
HETATM 1250  O  BHOH A 225       9.578  -3.670  23.125  0.50 25.79           O  
ANISOU 1250  O  BHOH A 225     4157   3213   2429  -2552    358   -425       O  
HETATM 1251  O  AHOH A 226       8.984  28.788  16.689  0.50 18.49           O  
ANISOU 1251  O  AHOH A 226     1745   1424   3854    218    360   -153       O  
HETATM 1252  O  BHOH A 226       9.569  28.810  15.333  0.50 11.64           O  
ANISOU 1252  O  BHOH A 226      436   1357   2629    -31    278    203       O  
HETATM 1253  O   HOH A 227       4.805  -1.710  25.584  1.00 24.44           O  
ANISOU 1253  O   HOH A 227     2623   3076   3585    234    535   -591       O  
HETATM 1254  O   HOH A 228       0.936  15.794  18.524  1.00 29.28           O  
ANISOU 1254  O   HOH A 228     4942   3940   2241  -1190    441    -81       O  
HETATM 1255  O   HOH A 229      18.259  11.294  24.327  1.00 29.49           O  
ANISOU 1255  O   HOH A 229     2975   1769   6460   -120  -1137    498       O  
HETATM 1256  O   HOH A 230      -1.894  15.910  17.823  1.00 27.26           O  
ANISOU 1256  O   HOH A 230     5569   2206   2582   -313   1372   -409       O  
HETATM 1257  O   HOH A 231      15.520  19.709  27.307  1.00 25.63           O  
ANISOU 1257  O   HOH A 231     4693   2352   2690   -700  -1055   -317       O  
HETATM 1258  O   HOH A 232       2.145  -3.552  24.701  1.00 21.51           O  
ANISOU 1258  O   HOH A 232     2376   2961   2835    685   -394   -650       O  
HETATM 1259  O   HOH A 233      -7.183  10.048  19.684  1.00 33.27           O  
ANISOU 1259  O   HOH A 233     2655   7094   2892    999   1020    772       O  
HETATM 1260  O   HOH A 234      11.422  -3.234  24.670  1.00 33.28           O  
ANISOU 1260  O   HOH A 234     6737   1595   4310    501   2397    510       O  
HETATM 1261  O   HOH A 235       5.131  -1.564  19.561  1.00 25.53           O  
ANISOU 1261  O   HOH A 235     1653   3277   4767   -355    644   -294       O  
HETATM 1262  O   HOH A 236      -2.257   3.886  -2.960  1.00 42.17           O  
ANISOU 1262  O   HOH A 236     7039   3903   5079    928  -1998    560       O  
HETATM 1263  O   HOH A 237      -5.246  14.054  14.828  1.00 45.50           O  
ANISOU 1263  O   HOH A 237     3967   3070  10249    402    359  -1077       O  
HETATM 1264  O   HOH A 238      15.440  26.836   5.358  1.00101.85           O  
ANISOU 1264  O   HOH A 238     8165  21803   8728   -114  -1565  -7201       O  
HETATM 1265  O   HOH A 239      18.854  17.712  14.756  1.00 36.19           O  
ANISOU 1265  O   HOH A 239     2970   4066   6715    123  -1612   -183       O  
HETATM 1266  O   HOH A 240      -2.374   4.680  -0.248  1.00 38.97           O  
ANISOU 1266  O   HOH A 240     5071   3855   5878  -1222  -1672    973       O  
HETATM 1267  O   HOH A 241      12.219  -6.532  23.435  1.00 34.99           O  
ANISOU 1267  O   HOH A 241     4163   3892   5239    -32    919  -1311       O  
HETATM 1268  O   HOH A 242      20.016  16.782  16.573  1.00 38.55           O  
ANISOU 1268  O   HOH A 242     3420   4958   6267   -820    738   2208       O  
HETATM 1269  O   HOH A 243      16.009  -3.013  -2.764  1.00 23.44           O  
ANISOU 1269  O   HOH A 243     4518   2534   1852    666    -63    276       O  
HETATM 1270  O   HOH A 244      16.093  25.760  19.903  1.00 46.78           O  
ANISOU 1270  O   HOH A 244     9479   5317   2977  -3226  -2562   1751       O  
HETATM 1271  O   HOH A 245       4.692  14.676  30.993  1.00 48.32           O  
ANISOU 1271  O   HOH A 245    12109   3934   2316  -1026    924   -427       O  
HETATM 1272  O   HOH A 246      17.397  12.417  30.185  1.00 40.43           O  
ANISOU 1272  O   HOH A 246     6023   5214   4123   1555   -757  -1307       O  
HETATM 1273  O   HOH A 247       7.336  -6.308  15.515  1.00 31.73           O  
ANISOU 1273  O   HOH A 247     5685   2508   3862  -1812  -1772   1557       O  
HETATM 1274  O   HOH A 248      -0.211  21.682  29.375  1.00 39.65           O  
ANISOU 1274  O   HOH A 248     6338   4480   4245   3169  -1866   -650       O  
HETATM 1275  O   HOH A 249      11.488  24.737   4.293  1.00 34.53           O  
ANISOU 1275  O   HOH A 249     2073   7082   3965  -1600    -79   2405       O  
HETATM 1276  O   HOH A 250      -1.856  20.273  11.551  1.00 30.53           O  
ANISOU 1276  O   HOH A 250     3182   2791   5627   -674   2070     -7       O  
HETATM 1277  O   HOH A 251      -9.417   4.066  20.751  1.00 18.52           O  
ANISOU 1277  O   HOH A 251     2695   1593   2748    500    782    153       O  
HETATM 1278  O   HOH A 252      20.837   5.062  21.561  1.00 24.38           O  
ANISOU 1278  O   HOH A 252     3748   2405   3110    913    451    372       O  
HETATM 1279  O   HOH A 253       4.790  10.136  29.453  1.00 24.62           O  
ANISOU 1279  O   HOH A 253     4677   2601   2075   -510    332    666       O  
HETATM 1280  O   HOH A 254       0.100   3.438  -0.144  1.00 23.52           O  
ANISOU 1280  O   HOH A 254     2238   2460   4235   -105  -1293   -486       O  
HETATM 1281  O   HOH A 255      17.234   8.923  16.421  1.00 26.74           O  
ANISOU 1281  O   HOH A 255     4231   2892   3035    580   -656    410       O  
HETATM 1282  O   HOH A 256       5.279  22.709  24.138  1.00 29.22           O  
ANISOU 1282  O   HOH A 256     4709   3266   3126   1529    194   -719       O  
HETATM 1283  O   HOH A 257       2.846  12.279  30.066  1.00 28.06           O  
ANISOU 1283  O   HOH A 257     4681   3386   2594    488   -109    130       O  
HETATM 1284  O   HOH A 258       8.996  12.016  30.690  1.00 25.01           O  
ANISOU 1284  O   HOH A 258     4514   2521   2466   -197   1063    363       O  
HETATM 1285  O   HOH A 259      -4.623  12.006  13.313  1.00 33.35           O  
ANISOU 1285  O   HOH A 259     2228   7652   2789   -482   -480    637       O  
HETATM 1286  O   HOH A 260       0.135   7.956  17.689  1.00 25.16           O  
ANISOU 1286  O   HOH A 260     3781   2634   3143   -357    664     57       O  
HETATM 1287  O   HOH A 261       9.252  21.217  29.718  1.00 30.11           O  
ANISOU 1287  O   HOH A 261     5350   2812   3278   1712    238   -878       O  
HETATM 1288  O   HOH A 262       3.133   8.309  30.990  1.00 23.85           O  
ANISOU 1288  O   HOH A 262     3213   2246   3601    124   1217    288       O  
HETATM 1289  O   HOH A 263       6.120  -2.059  22.807  1.00 32.16           O  
ANISOU 1289  O   HOH A 263     3324   4631   4262    248   -610     63       O  
HETATM 1290  O   HOH A 264       8.818   4.901  32.802  1.00 23.88           O  
ANISOU 1290  O   HOH A 264     2365   3110   3595   -666  -1148    544       O  
HETATM 1291  O   HOH A 265       7.084  -3.066  30.469  1.00 26.25           O  
ANISOU 1291  O   HOH A 265     5675   1930   2369   -374    499    -13       O  
HETATM 1292  O   HOH A 266      19.516  14.703  18.187  1.00 31.72           O  
ANISOU 1292  O   HOH A 266     2250   4187   5614   -215    803   1953       O  
HETATM 1293  O   HOH A 267      -1.838   7.861  -0.396  1.00 32.71           O  
ANISOU 1293  O   HOH A 267     7129   3083   2215  -1826    776   -156       O  
HETATM 1294  O   HOH A 268      10.994  22.250  26.587  1.00 29.94           O  
ANISOU 1294  O   HOH A 268     5646   3024   2705    249   -302    103       O  
HETATM 1295  O   HOH A 269       7.174  29.357  13.914  1.00 24.05           O  
ANISOU 1295  O   HOH A 269     3588   2173   3377     36   -150    193       O  
HETATM 1296  O   HOH A 270      12.795  25.544   6.189  1.00 28.88           O  
ANISOU 1296  O   HOH A 270     4717   2629   3628   1031   1592    784       O  
HETATM 1297  O   HOH A 271      10.519  -3.729  28.305  1.00 48.81           O  
ANISOU 1297  O   HOH A 271     4284   4818   9441    884   1009   5315       O  
HETATM 1298  O   HOH A 272      10.225  -5.248   9.287  1.00 36.20           O  
ANISOU 1298  O   HOH A 272     7249   2438   4065   -434   1398   -663       O  
HETATM 1299  O   HOH A 273      18.882  17.172   2.637  1.00 32.00           O  
ANISOU 1299  O   HOH A 273     4497   3929   3730    648    771   -647       O  
HETATM 1300  O   HOH A 274      18.402   4.568   2.415  1.00 24.43           O  
ANISOU 1300  O   HOH A 274     2879   4334   2067     65   -168   -418       O  
HETATM 1301  O   HOH A 275       0.744  19.538  -2.000  1.00 37.61           O  
ANISOU 1301  O   HOH A 275     5903   2937   5447   1705  -3086   -415       O  
HETATM 1302  O   HOH A 276       6.174  11.822  16.636  1.00 35.53           O  
ANISOU 1302  O   HOH A 276     2412   7990   3094  -2271    583   -299       O  
HETATM 1303  O   HOH A 277       8.035  30.717   8.506  1.00 28.04           O  
ANISOU 1303  O   HOH A 277     3209   2344   5101    385   -603    642       O  
HETATM 1304  O   HOH A 278      -3.931   1.782  15.029  1.00 26.55           O  
ANISOU 1304  O   HOH A 278     3198   2688   4202   1050   1604    342       O  
HETATM 1305  O   HOH A 279       4.400   9.395  15.920  1.00 22.84           O  
ANISOU 1305  O   HOH A 279     2744   2534   3399    -94   -223   -140       O  
HETATM 1306  O   HOH A 280       4.958  17.179  29.767  1.00 31.47           O  
ANISOU 1306  O   HOH A 280     6262   3532   2163   -466    547   -312       O  
HETATM 1307  O   HOH A 281       4.210  13.313  15.693  1.00 26.10           O  
ANISOU 1307  O   HOH A 281     4309   2965   2641    376    -24    178       O  
HETATM 1308  O   HOH A 282       0.071   5.226  18.666  1.00 34.88           O  
ANISOU 1308  O   HOH A 282     3940   3727   5585  -1545  -2195   2148       O  
HETATM 1309  O   HOH A 283      -7.686   6.574  19.109  1.00 30.84           O  
ANISOU 1309  O   HOH A 283     2881   4593   4242   1069    326   -774       O  
HETATM 1310  O   HOH A 284       5.948  29.957  10.091  1.00 27.66           O  
ANISOU 1310  O   HOH A 284     2383   3835   4289   -731    327   -897       O  
HETATM 1311  O   HOH A 285      19.427  20.386   7.524  1.00 35.54           O  
ANISOU 1311  O   HOH A 285     3679   3146   6677  -1023   2103  -2005       O  
HETATM 1312  O   HOH A 286      13.392   6.636  -1.554  1.00 24.53           O  
ANISOU 1312  O   HOH A 286     3803   3062   2455   1940     66    205       O  
HETATM 1313  O   HOH A 287      -5.099   2.361  33.319  1.00 30.83           O  
ANISOU 1313  O   HOH A 287     2808   2473   6433     17   -789   1522       O  
HETATM 1314  O   HOH A 288      15.885  26.116   8.695  1.00 26.29           O  
ANISOU 1314  O   HOH A 288     2915   3877   3196  -1531   -209   -226       O  
HETATM 1315  O   HOH A 289       1.565  25.781 -13.149  1.00 27.43           O  
ANISOU 1315  O   HOH A 289     2893   3259   4267    -17  -1218    163       O  
HETATM 1316  O   HOH A 290      -1.089  18.297   0.720  1.00 30.47           O  
ANISOU 1316  O   HOH A 290     3119   2904   5552    755  -1175    514       O  
HETATM 1317  O   HOH A 291      16.500  23.207  21.642  1.00 41.04           O  
ANISOU 1317  O   HOH A 291     3445   2523   9623   -602   2125   1994       O  
HETATM 1318  O   HOH A 292       2.432  -5.391  19.901  1.00 30.93           O  
ANISOU 1318  O   HOH A 292     3123   4561   4066    367    752   -988       O  
HETATM 1319  O   HOH A 293      -7.975   6.242  14.915  1.00 39.00           O  
ANISOU 1319  O   HOH A 293     3091   5496   6228   -217   -990   2942       O  
HETATM 1320  O   HOH A 294       5.475  16.588  -5.323  1.00 38.23           O  
ANISOU 1320  O   HOH A 294     3974   4346   6204    927  -2464  -1380       O  
HETATM 1321  O   HOH A 295      13.558  28.145   7.942  1.00 34.29           O  
ANISOU 1321  O   HOH A 295     3765   6034   3226    908   -542  -1748       O  
HETATM 1322  O   HOH A 296       2.798  -2.394  17.741  1.00 29.61           O  
ANISOU 1322  O   HOH A 296     4165   4224   2860   1925    -89    -72       O  
HETATM 1323  O   HOH A 297      18.350  11.463  21.646  1.00 46.45           O  
ANISOU 1323  O   HOH A 297     1632   9277   6739    698  -1401  -1938       O  
HETATM 1324  O   HOH A 298       8.789  -5.975  20.148  1.00 33.13           O  
ANISOU 1324  O   HOH A 298     3678   4108   4801     27    720   -595       O  
HETATM 1325  O   HOH A 299      -2.253  19.573   6.723  1.00 33.29           O  
ANISOU 1325  O   HOH A 299     3573   3578   5498    881  -1322    710       O  
HETATM 1326  O   HOH A 300      -2.782   5.917  28.952  1.00 41.08           O  
ANISOU 1326  O   HOH A 300     5103   3722   6783   -275  -1885  -1716       O  
HETATM 1327  O   HOH A 301       0.109  -2.634   9.576  1.00 34.90           O  
ANISOU 1327  O   HOH A 301     3135   4372   5752  -1624   -900   1937       O  
HETATM 1328  O   HOH A 302       3.026  -4.579  22.480  1.00 34.92           O  
ANISOU 1328  O   HOH A 302     5209   4462   3596   2654   1589   1553       O  
HETATM 1329  O   HOH A 303      12.922  12.132  -3.047  1.00 44.94           O  
ANISOU 1329  O   HOH A 303     6638   4310   6125  -2010   2374   -176       O  
HETATM 1330  O   HOH A 304      -2.062   9.409  26.363  1.00 43.71           O  
ANISOU 1330  O   HOH A 304     4987   5535   6083  -1083   3226   -462       O  
HETATM 1331  O   HOH A 305       2.894  -2.373   1.131  1.00 35.03           O  
ANISOU 1331  O   HOH A 305     5263   3156   4890    184   -181  -1823       O  
CONECT 1143 1144 1146 1150
CONECT 1144 1143
CONECT 1145 1147 1155
CONECT 1146 1143
CONECT 1147 1145 1148 1149
CONECT 1148 1147
CONECT 1149 1147
CONECT 1150 1143 1151 1152
CONECT 1151 1150
CONECT 1152 1150 1153 1157
CONECT 1153 1152 1154
CONECT 1154 1153 1155
CONECT 1155 1145 1154 1156
CONECT 1156 1155 1157
CONECT 1157 1152 1156
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.