CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Elnemo is running on a new server.
Should you encounter any unexpected behaviour,
please let us know.


***    ***

elNémo ID: 19101015332028693

Job options:

ID        	=	 19101015332028693
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   SER A   2      -0.987 160.287 265.459  1.00 67.14      A    N  
ANISOU    1  N   SER A   2     6284   8832  10394   2128    289    307  A    N  
ATOM      2  CA  SER A   2      -1.482 161.553 264.932  1.00 71.83      A    C  
ANISOU    2  CA  SER A   2     6937   9324  11032   2369    266    335  A    C  
ATOM      3  C   SER A   2      -0.334 162.461 264.498  1.00 70.02      A    C  
ANISOU    3  C   SER A   2     6977   8746  10883   2404    250    349  A    C  
ATOM      4  O   SER A   2      -0.520 163.656 264.268  1.00 72.20      A    O  
ANISOU    4  O   SER A   2     7370   8861  11203   2607    244    349  A    O  
ATOM      5  CB  SER A   2      -2.357 162.254 265.971  1.00 77.81      A    C  
ANISOU    5  CB  SER A   2     7641  10132  11792   2589    347    221  A    C  
ATOM      6  OG  SER A   2      -3.214 161.327 266.617  1.00 80.46      A    O  
ANISOU    6  OG  SER A   2     7745  10759  12067   2503    394    203  A    O  
ATOM      7  N   THR A   3       0.858 161.883 264.396  1.00 64.33      A    N  
ANISOU    7  N   THR A   3     6353   7897  10193   2188    242    357  A    N  
ATOM      8  CA  THR A   3       2.001 162.585 263.841  1.00 60.55      A    C  
ANISOU    8  CA  THR A   3     6103   7100   9804   2150    218    387  A    C  
ATOM      9  C   THR A   3       2.329 161.809 262.582  1.00 48.54      A    C  
ANISOU    9  C   THR A   3     4523   5649   8270   1971    128    528  A    C  
ATOM     10  O   THR A   3       2.337 160.578 262.603  1.00 41.66      A    O  
ANISOU   10  O   THR A   3     3519   4959   7349   1793    103    534  A    O  
ATOM     11  CB  THR A   3       3.198 162.575 264.800  1.00 63.79      A    C  
ANISOU   11  CB  THR A   3     6670   7295  10272   2029    273    251  A    C  
ATOM     12  CG2 THR A   3       4.352 163.393 264.226  1.00 62.71      A    C  
ANISOU   12  CG2 THR A   3     6765   6832  10232   1970    245    277  A    C  
ATOM     13  OG1 THR A   3       2.798 163.140 266.056  1.00 67.88      A    O  
ANISOU   13  OG1 THR A   3     7228   7798  10766   2194    355    103  A    O  
ATOM     14  N   GLU A   4       2.624 162.510 261.494  1.00 42.90      A    N  
ANISOU   14  N   GLU A   4     3921   4789   7591   2014     78    638  A    N  
ATOM     15  CA  GLU A   4       2.815 161.835 260.216  1.00 44.72      A    C  
ANISOU   15  CA  GLU A   4     4094   5114   7782   1880    -11    774  A    C  
ATOM     16  C   GLU A   4       4.189 162.065 259.623  1.00 43.03      A    C  
ANISOU   16  C   GLU A   4     4058   4655   7636   1748    -28    824  A    C  
ATOM     17  O   GLU A   4       4.739 163.164 259.686  1.00 48.57      A    O  
ANISOU   17  O   GLU A   4     4945   5095   8413   1815      7    817  A    O  
ATOM     18  CB  GLU A   4       1.735 162.204 259.195  1.00 51.35      A    C  
ANISOU   18  CB  GLU A   4     4847   6104   8560   2035    -76    890  A    C  
ATOM     19  CG  GLU A   4       0.402 161.517 259.422  1.00 63.57      A    C  
ANISOU   19  CG  GLU A   4     6153   7979  10021   2071    -98    868  A    C  
ATOM     20  CD  GLU A   4      -0.357 161.298 258.127  1.00 73.17      A    C  
ANISOU   20  CD  GLU A   4     7257   9383  11162   2091   -202    988  A    C  
ATOM     21  OE1 GLU A   4       0.142 161.729 257.065  1.00 77.75      A    O  
ANISOU   21  OE1 GLU A   4     7952   9843  11747   2103   -250   1094  A    O  
ATOM     22  OE2 GLU A   4      -1.446 160.689 258.169  1.00 74.69      A    O1-
ANISOU   22  OE2 GLU A   4     7245   9844  11290   2083   -235    975  A    O1-
ATOM     23  N   ILE A   5       4.726 161.005 259.036  1.00 39.36      A    N  
ANISOU   23  N   ILE A   5     3538   4282   7134   1554    -85    872  A    N  
ATOM     24  CA  ILE A   5       6.021 161.061 258.399  1.00 40.81      A    C  
ANISOU   24  CA  ILE A   5     3857   4286   7362   1419   -105    928  A    C  
ATOM     25  C   ILE A   5       5.882 160.455 257.012  1.00 40.01      A    C  
ANISOU   25  C   ILE A   5     3689   4349   7165   1365   -197   1068  A    C  
ATOM     26  O   ILE A   5       5.054 159.567 256.781  1.00 38.88      A    O  
ANISOU   26  O   ILE A   5     3389   4459   6926   1342   -253   1075  A    O  
ATOM     27  CB  ILE A   5       7.032 160.193 259.220  1.00 58.08      A    C  
ANISOU   27  CB  ILE A   5     6054   6428   9585   1223    -87    811  A    C  
ATOM     28  CG1 ILE A   5       7.342 160.840 260.571  1.00 59.10      A    C  
ANISOU   28  CG1 ILE A   5     6279   6376   9799   1263     -2    655  A    C  
ATOM     29  CG2 ILE A   5       8.325 159.914 258.455  1.00 55.37      A    C  
ANISOU   29  CG2 ILE A   5     5799   5983   9257   1064   -125    876  A    C  
ATOM     30  CD1 ILE A   5       8.102 159.930 261.526  1.00 55.29      A    C  
ANISOU   30  CD1 ILE A   5     5780   5900   9328   1101     15    520  A    C  
ATOM     31  N   LYS A   6       6.709 160.940 256.096  1.00 41.72      A    N  
ANISOU   31  N   LYS A   6     4031   4424   7398   1334   -211   1173  A    N  
ATOM     32  CA  LYS A   6       6.779 160.414 254.752  1.00 47.55      A    C  
ANISOU   32  CA  LYS A   6     4736   5298   8032   1283   -291   1299  A    C  
ATOM     33  C   LYS A   6       8.240 160.076 254.568  1.00 45.41      A    C  
ANISOU   33  C   LYS A   6     4561   4905   7790   1109   -284   1309  A    C  
ATOM     34  O   LYS A   6       9.113 160.905 254.834  1.00 46.32      A    O  
ANISOU   34  O   LYS A   6     4814   4785   8003   1087   -223   1306  A    O  
ATOM     35  CB  LYS A   6       6.347 161.470 253.738  1.00 53.56      A    C  
ANISOU   35  CB  LYS A   6     5562   6019   8767   1445   -304   1437  A    C  
ATOM     36  CG  LYS A   6       6.432 161.008 252.292  1.00 59.86      A    C  
ANISOU   36  CG  LYS A   6     6341   6963   9441   1408   -384   1566  A    C  
ATOM     37  CD  LYS A   6       6.014 162.113 251.332  1.00 68.04      A    C  
ANISOU   37  CD  LYS A   6     7450   7951  10450   1578   -393   1703  A    C  
ATOM     38  CE  LYS A   6       6.290 161.723 249.883  1.00 73.29      A    C  
ANISOU   38  CE  LYS A   6     8122   8740  10985   1537   -462   1830  A    C  
ATOM     39  NZ  LYS A   6       5.465 160.564 249.437  1.00 76.08      A    N1+
ANISOU   39  NZ  LYS A   6     8314   9389  11204   1509   -565   1797  A    N1+
ATOM     40  N   THR A   7       8.510 158.865 254.101  1.00 39.81      A    N  
ANISOU   40  N   THR A   7     3783   4359   6986    982   -352   1314  A    N  
ATOM     41  CA  THR A   7       9.880 158.429 253.892  1.00 33.98      A    C  
ANISOU   41  CA  THR A   7     3118   3543   6252    833   -352   1323  A    C  
ATOM     42  C   THR A   7       9.919 157.531 252.669  1.00 34.55      A    C  
ANISOU   42  C   THR A   7     3151   3809   6167    783   -441   1403  A    C  
ATOM     43  O   THR A   7       8.871 157.094 252.182  1.00 33.98      A    O  
ANISOU   43  O   THR A   7     2989   3930   5992    832   -509   1415  A    O  
ATOM     44  CB  THR A   7      10.439 157.700 255.137  1.00 34.71      A    C  
ANISOU   44  CB  THR A   7     3206   3609   6373    697   -323   1149  A    C  
ATOM     45  CG2 THR A   7       9.672 156.405 255.405  1.00 32.89      A    C  
ANISOU   45  CG2 THR A   7     2849   3606   6042    641   -382   1070  A    C  
ATOM     46  OG1 THR A   7      11.829 157.406 254.952  1.00 35.10      A    O  
ANISOU   46  OG1 THR A   7     3352   3596   6388    549   -308   1134  A    O  
ATOM     47  N   GLN A   8      11.115 157.279 252.150  1.00 32.79      A    N  
ANISOU   47  N   GLN A   8     3001   3544   5915    689   -442   1452  A    N  
ATOM     48  CA  GLN A   8      11.252 156.330 251.054  1.00 32.44      A    C  
ANISOU   48  CA  GLN A   8     2938   3687   5701    644   -525   1501  A    C  
ATOM     49  C   GLN A   8      11.159 154.899 251.571  1.00 30.83      A    C  
ANISOU   49  C   GLN A   8     2682   3620   5413    521   -580   1349  A    C  
ATOM     50  O   GLN A   8      10.324 154.116 251.114  1.00 31.40      A    O  
ANISOU   50  O   GLN A   8     2676   3871   5385    524   -673   1342  A    O  
ATOM     51  CB  GLN A   8      12.570 156.551 250.299  1.00 31.30      A    C  
ANISOU   51  CB  GLN A   8     2896   3478   5516    590   -490   1596  A    C  
ATOM     52  CG  GLN A   8      12.611 157.859 249.490  1.00 34.19      A    C  
ANISOU   52  CG  GLN A   8     3334   3744   5911    688   -439   1761  A    C  
ATOM     53  CD  GLN A   8      13.917 158.040 248.728  1.00 35.70      A    C  
ANISOU   53  CD  GLN A   8     3607   3899   6059    621   -396   1875  A    C  
ATOM     54  NE2 GLN A   8      13.866 157.843 247.416  1.00 37.28      A    N  
ANISOU   54  NE2 GLN A   8     3816   4254   6095    670   -434   1981  A    N  
ATOM     55  OE1 GLN A   8      14.957 158.356 249.312  1.00 36.40      A    O  
ANISOU   55  OE1 GLN A   8     3746   3833   6250    523   -325   1859  A    O  
ATOM     56  N   VAL A   9      12.000 154.571 252.548  1.00 28.23      A    N  
ANISOU   56  N   VAL A   9     2408   3202   5118    406   -522   1221  A    N  
ATOM     57  CA  VAL A   9      12.048 153.220 253.091  1.00 25.18      A    C  
ANISOU   57  CA  VAL A   9     2006   2915   4648    287   -562   1082  A    C  
ATOM     58  C   VAL A   9      11.760 153.190 254.582  1.00 27.26      A    C  
ANISOU   58  C   VAL A   9     2240   3115   5001    251   -506    949  A    C  
ATOM     59  O   VAL A   9      12.351 153.957 255.340  1.00 30.82      A    O  
ANISOU   59  O   VAL A   9     2744   3413   5553    252   -424    910  A    O  
ATOM     60  CB  VAL A   9      13.447 152.593 252.886  1.00 25.57      A    C  
ANISOU   60  CB  VAL A   9     2152   2952   4609    188   -550   1045  A    C  
ATOM     61  CG1 VAL A   9      13.498 151.183 253.462  1.00 22.02      A    C  
ANISOU   61  CG1 VAL A   9     1712   2582   4072     84   -592    906  A    C  
ATOM     62  CG2 VAL A   9      13.839 152.611 251.406  1.00 23.92      A    C  
ANISOU   62  CG2 VAL A   9     1978   2821   4290    232   -591   1176  A    C  
ATOM     63  N   VAL A  10      10.863 152.298 255.002  1.00 25.36      A    N  
ANISOU   63  N   VAL A  10     1918   3000   4719    212   -553    881  A    N  
ATOM     64  CA  VAL A  10      10.710 152.007 256.423  1.00 22.73      A    C  
ANISOU   64  CA  VAL A  10     1566   2638   4433    158   -498    754  A    C  
ATOM     65  C   VAL A  10      11.134 150.559 256.678  1.00 25.45      A    C  
ANISOU   65  C   VAL A  10     1955   3048   4667     17   -540    664  A    C  
ATOM     66  O   VAL A  10      10.750 149.641 255.947  1.00 28.24      A    O  
ANISOU   66  O   VAL A  10     2291   3518   4921    -33   -631    684  A    O  
ATOM     67  CB  VAL A  10       9.278 152.295 256.945  1.00 23.13      A    C  
ANISOU   67  CB  VAL A  10     1477   2768   4542    236   -489    757  A    C  
ATOM     68  CG1 VAL A  10       8.232 151.406 256.263  1.00 23.52      A    C  
ANISOU   68  CG1 VAL A  10     1413   3017   4506    200   -593    799  A    C  
ATOM     69  CG2 VAL A  10       9.221 152.153 258.463  1.00 23.20      A    C  
ANISOU   69  CG2 VAL A  10     1479   2742   4594    199   -410    632  A    C  
ATOM     70  N   VAL A  11      11.921 150.354 257.728  1.00 23.14      A    N  
ANISOU   70  N   VAL A  11     1730   2676   4388    -43   -478    561  A    N  
ATOM     71  CA  VAL A  11      12.400 149.018 258.066  1.00 22.84      A    C  
ANISOU   71  CA  VAL A  11     1755   2677   4246   -157   -509    479  A    C  
ATOM     72  C   VAL A  11      11.783 148.635 259.395  1.00 24.59      A    C  
ANISOU   72  C   VAL A  11     1933   2920   4492   -199   -467    396  A    C  
ATOM     73  O   VAL A  11      11.934 149.352 260.389  1.00 20.21      A    O  
ANISOU   73  O   VAL A  11     1374   2292   4012   -159   -385    343  A    O  
ATOM     74  CB  VAL A  11      13.933 148.986 258.193  1.00 19.90      A    C  
ANISOU   74  CB  VAL A  11     1496   2222   3844   -184   -476    435  A    C  
ATOM     75  CG1 VAL A  11      14.408 147.593 258.582  1.00 17.46      A    C  
ANISOU   75  CG1 VAL A  11     1263   1950   3422   -271   -508    353  A    C  
ATOM     76  CG2 VAL A  11      14.594 149.448 256.892  1.00 21.45      A    C  
ANISOU   76  CG2 VAL A  11     1725   2412   4014   -141   -498    534  A    C  
ATOM     77  N   LEU A  12      11.074 147.511 259.408  1.00 24.16      A    N  
ANISOU   77  N   LEU A  12     1847   2964   4367   -283   -524    386  A    N  
ATOM     78  CA  LEU A  12      10.403 147.066 260.616  1.00 18.75      A    C  
ANISOU   78  CA  LEU A  12     1111   2321   3692   -336   -478    331  A    C  
ATOM     79  C   LEU A  12      11.251 146.025 261.342  1.00 26.36      A    C  
ANISOU   79  C   LEU A  12     2204   3240   4570   -425   -467    250  A    C  
ATOM     80  O   LEU A  12      11.295 144.852 260.952  1.00 22.26      A    O  
ANISOU   80  O   LEU A  12     1765   2747   3945   -509   -531    243  A    O  
ATOM     81  CB  LEU A  12       9.019 146.522 260.268  1.00 19.85      A    C  
ANISOU   81  CB  LEU A  12     1165   2599   3779   -379   -524    373  A    C  
ATOM     82  CG  LEU A  12       8.128 146.072 261.424  1.00 32.71      A    C  
ANISOU   82  CG  LEU A  12     2728   4307   5395   -435   -465    339  A    C  
ATOM     83  CD1 LEU A  12       7.859 147.247 262.352  1.00 31.48      A    C  
ANISOU   83  CD1 LEU A  12     2469   4139   5352   -317   -364    328  A    C  
ATOM     84  CD2 LEU A  12       6.825 145.490 260.904  1.00 28.68      A    C  
ANISOU   84  CD2 LEU A  12     2126   3942   4829   -499   -520    380  A    C  
ATOM     85  N   GLY A  13      11.933 146.469 262.399  1.00 23.42      A    N  
ANISOU   85  N   GLY A  13     1869   2798   4232   -393   -386    181  A    N  
ATOM     86  CA  GLY A  13      12.816 145.602 263.161  1.00 18.38      A    C  
ANISOU   86  CA  GLY A  13     1345   2124   3512   -451   -373    108  A    C  
ATOM     87  C   GLY A  13      14.262 146.042 263.040  1.00 17.48      A    C  
ANISOU   87  C   GLY A  13     1319   1930   3391   -407   -361     69  A    C  
ATOM     88  O   GLY A  13      14.730 146.327 261.934  1.00 19.90      A    O  
ANISOU   88  O   GLY A  13     1642   2221   3697   -382   -401    119  A    O  
ATOM     89  N   ALA A  14      14.970 146.122 264.166  1.00 18.66      A    N  
ANISOU   89  N   ALA A  14     1515   2045   3530   -400   -306    -13  A    N  
ATOM     90  CA  ALA A  14      16.359 146.579 264.145  1.00 14.81      A    C  
ANISOU   90  CA  ALA A  14     1085   1502   3040   -374   -296    -55  A    C  
ATOM     91  C   ALA A  14      17.375 145.486 264.494  1.00 17.28      A    C  
ANISOU   91  C   ALA A  14     1500   1834   3232   -400   -320   -104  A    C  
ATOM     92  O   ALA A  14      18.457 145.773 265.027  1.00 19.66      A    O  
ANISOU   92  O   ALA A  14     1829   2119   3521   -382   -298   -166  A    O  
ATOM     93  CB  ALA A  14      16.537 147.784 265.069  1.00 17.86      A    C  
ANISOU   93  CB  ALA A  14     1439   1829   3517   -331   -227   -121  A    C  
ATOM     94  N   GLY A  15      17.052 144.240 264.159  1.00 14.05      A    N  
ANISOU   94  N   GLY A  15     1150   1456   2732   -440   -371    -78  A    N  
ATOM     95  CA  GLY A  15      18.012 143.162 264.305  1.00 13.63      A    C  
ANISOU   95  CA  GLY A  15     1215   1408   2558   -439   -401   -114  A    C  
ATOM     96  C   GLY A  15      19.029 143.206 263.178  1.00 15.68      A    C  
ANISOU   96  C   GLY A  15     1505   1677   2777   -395   -440    -90  A    C  
ATOM     97  O   GLY A  15      18.996 144.118 262.352  1.00 19.87      A    O  
ANISOU   97  O   GLY A  15     1967   2206   3378   -379   -437    -40  A    O  
ATOM     98  N   PRO A  16      19.933 142.214 263.134  1.00 17.79      A    N  
ANISOU   98  N   PRO A  16     1878   1959   2922   -365   -471   -119  A    N  
ATOM     99  CA  PRO A  16      21.010 142.126 262.136  1.00 18.56      A    C  
ANISOU   99  CA  PRO A  16     2003   2095   2952   -303   -498   -101  A    C  
ATOM    100  C   PRO A  16      20.510 142.407 260.720  1.00 13.41      A    C  
ANISOU  100  C   PRO A  16     1322   1454   2319   -303   -535    -25  A    C  
ATOM    101  O   PRO A  16      21.053 143.255 259.991  1.00 22.98      A    O  
ANISOU  101  O   PRO A  16     2471   2696   3564   -272   -516     21  A    O  
ATOM    102  CB  PRO A  16      21.461 140.664 262.234  1.00 22.79      A    C  
ANISOU  102  CB  PRO A  16     2687   2631   3341   -264   -543   -136  A    C  
ATOM    103  CG  PRO A  16      21.082 140.235 263.591  1.00 17.94      A    C  
ANISOU  103  CG  PRO A  16     2110   1983   2724   -301   -519   -178  A    C  
ATOM    104  CD  PRO A  16      19.869 141.018 263.996  1.00 16.64      A    C  
ANISOU  104  CD  PRO A  16     1840   1797   2684   -379   -483   -157  A    C  
ATOM    105  N   ALA A  17      19.449 141.701 260.353  1.00 16.01      A    N  
ANISOU  105  N   ALA A  17     1695   1764   2625   -347   -591     -7  A    N  
ATOM    106  CA  ALA A  17      18.834 141.866 259.049  1.00 20.22      A    C  
ANISOU  106  CA  ALA A  17     2202   2323   3158   -348   -644     59  A    C  
ATOM    107  C   ALA A  17      18.322 143.297 258.863  1.00 19.05      A    C  
ANISOU  107  C   ALA A  17     1913   2179   3146   -349   -600    122  A    C  
ATOM    108  O   ALA A  17      18.659 143.969 257.879  1.00 19.83      A    O  
ANISOU  108  O   ALA A  17     1976   2307   3252   -303   -600    186  A    O  
ATOM    109  CB  ALA A  17      17.707 140.870 258.875  1.00 14.65      A    C  
ANISOU  109  CB  ALA A  17     1553   1600   2415   -422   -719     54  A    C  
ATOM    110  N   GLY A  18      17.503 143.747 259.810  1.00 19.44      A    N  
ANISOU  110  N   GLY A  18     1891   2200   3296   -390   -560    108  A    N  
ATOM    111  CA  GLY A  18      16.892 145.067 259.745  1.00 14.72      A    C  
ANISOU  111  CA  GLY A  18     1177   1589   2828   -371   -519    159  A    C  
ATOM    112  C   GLY A  18      17.869 146.224 259.705  1.00 22.11      A    C  
ANISOU  112  C   GLY A  18     2085   2486   3830   -328   -461    173  A    C  
ATOM    113  O   GLY A  18      17.786 147.096 258.829  1.00 19.94      A    O  
ANISOU  113  O   GLY A  18     1764   2203   3608   -293   -458    256  A    O  
ATOM    114  N   TYR A  19      18.792 146.263 260.661  1.00 22.02      A    N  
ANISOU  114  N   TYR A  19     2099   2450   3816   -336   -417     97  A    N  
ATOM    115  CA  TYR A  19      19.715 147.389 260.687  1.00 26.09      A    C  
ANISOU  115  CA  TYR A  19     2581   2926   4407   -325   -368    104  A    C  
ATOM    116  C   TYR A  19      20.708 147.297 259.537  1.00 26.27      A    C  
ANISOU  116  C   TYR A  19     2619   3002   4359   -304   -384    170  A    C  
ATOM    117  O   TYR A  19      21.131 148.333 259.016  1.00 22.62      A    O  
ANISOU  117  O   TYR A  19     2115   2512   3970   -304   -352    237  A    O  
ATOM    118  CB  TYR A  19      20.392 147.593 262.058  1.00 21.88      A    C  
ANISOU  118  CB  TYR A  19     2052   2364   3895   -347   -325     -3  A    C  
ATOM    119  CG  TYR A  19      21.566 146.691 262.381  1.00 25.51      A    C  
ANISOU  119  CG  TYR A  19     2565   2892   4236   -344   -341    -60  A    C  
ATOM    120  CD1 TYR A  19      22.797 146.860 261.755  1.00 25.38      A    C  
ANISOU  120  CD1 TYR A  19     2534   2924   4185   -336   -340    -32  A    C  
ATOM    121  CD2 TYR A  19      21.450 145.688 263.338  1.00 19.19      A    C  
ANISOU  121  CD2 TYR A  19     1823   2115   3352   -342   -352   -133  A    C  
ATOM    122  CE1 TYR A  19      23.866 146.039 262.054  1.00 25.90      A    C  
ANISOU  122  CE1 TYR A  19     2634   3074   4135   -309   -354    -82  A    C  
ATOM    123  CE2 TYR A  19      22.516 144.867 263.642  1.00 22.15      A    C  
ANISOU  123  CE2 TYR A  19     2252   2552   3612   -314   -369   -180  A    C  
ATOM    124  CZ  TYR A  19      23.718 145.051 262.998  1.00 30.06      A    C  
ANISOU  124  CZ  TYR A  19     3230   3613   4580   -290   -372   -158  A    C  
ATOM    125  OH  TYR A  19      24.785 144.242 263.300  1.00 44.47      A    O  
ANISOU  125  OH  TYR A  19     5094   5520   6283   -239   -388   -203  A    O  
ATOM    126  N   SER A  20      21.063 146.078 259.111  1.00 21.67      A    N  
ANISOU  126  N   SER A  20     2106   2494   3635   -281   -431    157  A    N  
ATOM    127  CA  SER A  20      21.949 145.990 257.948  1.00 21.13      A    C  
ANISOU  127  CA  SER A  20     2048   2499   3482   -237   -440    221  A    C  
ATOM    128  C   SER A  20      21.257 146.545 256.707  1.00 22.03      A    C  
ANISOU  128  C   SER A  20     2132   2619   3620   -216   -458    335  A    C  
ATOM    129  O   SER A  20      21.860 147.303 255.928  1.00 25.62      A    O  
ANISOU  129  O   SER A  20     2547   3097   4089   -199   -425    425  A    O  
ATOM    130  CB  SER A  20      22.440 144.563 257.712  1.00 16.36      A    C  
ANISOU  130  CB  SER A  20     1543   1965   2709   -189   -489    174  A    C  
ATOM    131  OG  SER A  20      23.171 144.110 258.843  1.00 18.72      A    O  
ANISOU  131  OG  SER A  20     1867   2268   2978   -189   -470     83  A    O  
ATOM    132  N   ALA A  21      19.981 146.197 256.554  1.00 15.20      A    N  
ANISOU  132  N   ALA A  21     1276   1741   2759   -222   -511    340  A    N  
ATOM    133  CA  ALA A  21      19.172 146.700 255.447  1.00 16.20      A    C  
ANISOU  133  CA  ALA A  21     1365   1888   2903   -192   -542    445  A    C  
ATOM    134  C   ALA A  21      19.069 148.224 255.485  1.00 20.18      A    C  
ANISOU  134  C   ALA A  21     1791   2319   3557   -186   -478    523  A    C  
ATOM    135  O   ALA A  21      19.266 148.899 254.469  1.00 21.50      A    O  
ANISOU  135  O   ALA A  21     1940   2504   3726   -147   -467    638  A    O  
ATOM    136  CB  ALA A  21      17.784 146.085 255.491  1.00 16.05      A    C  
ANISOU  136  CB  ALA A  21     1341   1881   2877   -217   -612    424  A    C  
ATOM    137  N   ALA A  22      18.770 148.758 256.664  1.00 19.82      A    N  
ANISOU  137  N   ALA A  22     1714   2186   3632   -217   -434    463  A    N  
ATOM    138  CA  ALA A  22      18.596 150.196 256.842  1.00 21.94      A    C  
ANISOU  138  CA  ALA A  22     1934   2350   4050   -204   -377    515  A    C  
ATOM    139  C   ALA A  22      19.871 150.973 256.542  1.00 25.95      A    C  
ANISOU  139  C   ALA A  22     2448   2820   4592   -228   -324    566  A    C  
ATOM    140  O   ALA A  22      19.843 151.998 255.841  1.00 23.04      A    O  
ANISOU  140  O   ALA A  22     2065   2395   4295   -206   -297    683  A    O  
ATOM    141  CB  ALA A  22      18.141 150.490 258.257  1.00 16.83      A    C  
ANISOU  141  CB  ALA A  22     1271   1626   3500   -224   -341    411  A    C  
ATOM    142  N   PHE A  23      20.985 150.485 257.082  1.00 20.67      A    N  
ANISOU  142  N   PHE A  23     1796   2186   3870   -275   -308    486  A    N  
ATOM    143  CA  PHE A  23      22.276 151.135 256.884  1.00 21.43      A    C  
ANISOU  143  CA  PHE A  23     1873   2276   3994   -320   -259    527  A    C  
ATOM    144  C   PHE A  23      22.670 151.065 255.408  1.00 25.38      A    C  
ANISOU  144  C   PHE A  23     2369   2873   4402   -282   -261    667  A    C  
ATOM    145  O   PHE A  23      23.228 152.023 254.857  1.00 26.88      A    O  
ANISOU  145  O   PHE A  23     2530   3030   4652   -311   -212    778  A    O  
ATOM    146  CB  PHE A  23      23.359 150.496 257.766  1.00 18.69      A    C  
ANISOU  146  CB  PHE A  23     1525   1989   3587   -362   -253    410  A    C  
ATOM    147  CG  PHE A  23      23.196 150.765 259.245  1.00 22.08      A    C  
ANISOU  147  CG  PHE A  23     1957   2331   4102   -404   -241    278  A    C  
ATOM    148  CD1 PHE A  23      22.165 151.567 259.724  1.00 21.43      A    C  
ANISOU  148  CD1 PHE A  23     1876   2120   4144   -398   -227    264  A    C  
ATOM    149  CD2 PHE A  23      24.073 150.190 260.158  1.00 20.84      A    C  
ANISOU  149  CD2 PHE A  23     1799   2234   3884   -431   -245    166  A    C  
ATOM    150  CE1 PHE A  23      22.019 151.804 261.081  1.00 18.17      A    C  
ANISOU  150  CE1 PHE A  23     1472   1642   3790   -420   -212    135  A    C  
ATOM    151  CE2 PHE A  23      23.935 150.416 261.519  1.00 20.06      A    C  
ANISOU  151  CE2 PHE A  23     1707   2073   3841   -460   -237     42  A    C  
ATOM    152  CZ  PHE A  23      22.909 151.226 261.982  1.00 23.49      A    C  
ANISOU  152  CZ  PHE A  23     2150   2380   4396   -456   -219     23  A    C  
ATOM    153  N   ARG A  24      22.369 149.942 254.758  1.00 17.55      A    N  
ANISOU  153  N   ARG A  24     1412   1995   3260   -219   -318    665  A    N  
ATOM    154  CA  ARG A  24      22.681 149.836 253.335  1.00 21.36      A    C  
ANISOU  154  CA  ARG A  24     1900   2585   3630   -162   -324    788  A    C  
ATOM    155  C   ARG A  24      21.834 150.832 252.525  1.00 20.52      A    C  
ANISOU  155  C   ARG A  24     1777   2422   3598   -131   -321    929  A    C  
ATOM    156  O   ARG A  24      22.349 151.523 251.640  1.00 22.21      A    O  
ANISOU  156  O   ARG A  24     1972   2659   3806   -120   -277   1069  A    O  
ATOM    157  CB  ARG A  24      22.485 148.401 252.836  1.00 22.39      A    C  
ANISOU  157  CB  ARG A  24     2095   2833   3577    -97   -399    733  A    C  
ATOM    158  CG  ARG A  24      22.978 148.167 251.413  1.00 22.71      A    C  
ANISOU  158  CG  ARG A  24     2154   3011   3465    -20   -404    834  A    C  
ATOM    159  CD  ARG A  24      24.435 147.736 251.383  1.00 23.71      A    C  
ANISOU  159  CD  ARG A  24     2273   3247   3489      0   -357    813  A    C  
ATOM    160  NE  ARG A  24      24.928 147.633 250.013  1.00 26.98      A    N  
ANISOU  160  NE  ARG A  24     2692   3807   3751     85   -343    922  A    N  
ATOM    161  CZ  ARG A  24      25.634 148.580 249.402  1.00 28.94      A    C  
ANISOU  161  CZ  ARG A  24     2866   4105   4023     70   -261   1067  A    C  
ATOM    162  NH1 ARG A  24      25.946 149.698 250.046  1.00 21.93      A    N1+
ANISOU  162  NH1 ARG A  24     1904   3111   3315    -39   -194   1112  A    N1+
ATOM    163  NH2 ARG A  24      26.037 148.406 248.151  1.00 30.20      A    N  
ANISOU  163  NH2 ARG A  24     3034   4420   4022    161   -244   1168  A    N  
ATOM    164  N   CYS A  25      20.549 150.937 252.856  1.00 20.68      A    N  
ANISOU  164  N   CYS A  25     1795   2375   3687   -111   -362    903  A    N  
ATOM    165  CA  CYS A  25      19.682 151.932 252.226  1.00 23.98      A    C  
ANISOU  165  CA  CYS A  25     2191   2735   4184    -59   -361   1032  A    C  
ATOM    166  C   CYS A  25      20.240 153.343 252.394  1.00 26.41      A    C  
ANISOU  166  C   CYS A  25     2490   2902   4644    -97   -276   1117  A    C  
ATOM    167  O   CYS A  25      20.272 154.120 251.441  1.00 26.45      A    O  
ANISOU  167  O   CYS A  25     2498   2891   4660    -61   -252   1278  A    O  
ATOM    168  CB  CYS A  25      18.269 151.878 252.814  1.00 22.81      A    C  
ANISOU  168  CB  CYS A  25     2018   2544   4103    -32   -407    973  A    C  
ATOM    169  SG  CYS A  25      17.235 150.551 252.169  1.00 28.04      A    S  
ANISOU  169  SG  CYS A  25     2681   3364   4611      6   -525    942  A    S  
ATOM    170  N   ALA A  26      20.669 153.675 253.610  1.00 25.43      A    N  
ANISOU  170  N   ALA A  26     2363   2668   4630   -175   -235   1008  A    N  
ATOM    171  CA  ALA A  26      21.224 155.000 253.868  1.00 26.90      A    C  
ANISOU  171  CA  ALA A  26     2556   2696   4970   -236   -165   1064  A    C  
ATOM    172  C   ALA A  26      22.483 155.249 253.053  1.00 26.43      A    C  
ANISOU  172  C   ALA A  26     2482   2695   4865   -294   -117   1183  A    C  
ATOM    173  O   ALA A  26      22.636 156.319 252.456  1.00 27.24      A    O  
ANISOU  173  O   ALA A  26     2598   2704   5049   -309    -70   1334  A    O  
ATOM    174  CB  ALA A  26      21.510 155.185 255.349  1.00 29.29      A    C  
ANISOU  174  CB  ALA A  26     2861   2892   5374   -312   -146    899  A    C  
ATOM    175  N   ASP A  27      23.370 154.257 253.008  1.00 26.54      A    N  
ANISOU  175  N   ASP A  27     2470   2871   4744   -318   -124   1126  A    N  
ATOM    176  CA  ASP A  27      24.615 154.388 252.248  1.00 28.38      A    C  
ANISOU  176  CA  ASP A  27     2664   3207   4913   -364    -70   1236  A    C  
ATOM    177  C   ASP A  27      24.335 154.510 250.753  1.00 26.79      A    C  
ANISOU  177  C   ASP A  27     2475   3090   4613   -277    -65   1423  A    C  
ATOM    178  O   ASP A  27      25.147 155.050 250.000  1.00 27.47      A    O  
ANISOU  178  O   ASP A  27     2532   3221   4683   -313      0   1574  A    O  
ATOM    179  CB  ASP A  27      25.535 153.185 252.504  1.00 28.70      A    C  
ANISOU  179  CB  ASP A  27     2673   3427   4806   -365    -83   1127  A    C  
ATOM    180  CG  ASP A  27      26.145 153.189 253.902  1.00 29.32      A    C  
ANISOU  180  CG  ASP A  27     2723   3451   4966   -460    -77    971  A    C  
ATOM    181  OD1 ASP A  27      26.037 154.216 254.608  1.00 26.86      A    O  
ANISOU  181  OD1 ASP A  27     2413   2967   4827   -546    -54    951  A    O  
ATOM    182  OD2 ASP A  27      26.735 152.157 254.293  1.00 27.60      A    O1-
ANISOU  182  OD2 ASP A  27     2490   3364   4632   -439    -98    865  A    O1-
ATOM    183  N   LEU A  28      23.174 154.027 250.326  1.00 23.27      A    N  
ANISOU  183  N   LEU A  28     2067   2678   4099   -166   -135   1420  A    N  
ATOM    184  CA  LEU A  28      22.819 154.088 248.914  1.00 26.61      A    C  
ANISOU  184  CA  LEU A  28     2504   3198   4407    -69   -148   1584  A    C  
ATOM    185  C   LEU A  28      22.006 155.333 248.598  1.00 29.04      A    C  
ANISOU  185  C   LEU A  28     2832   3354   4846    -36   -132   1727  A    C  
ATOM    186  O   LEU A  28      21.542 155.511 247.467  1.00 28.72      A    O  
ANISOU  186  O   LEU A  28     2807   3383   4721     60   -150   1876  A    O  
ATOM    187  CB  LEU A  28      22.071 152.821 248.482  1.00 25.97      A    C  
ANISOU  187  CB  LEU A  28     2452   3262   4155     31   -248   1505  A    C  
ATOM    188  CG  LEU A  28      22.990 151.601 248.358  1.00 29.50      A    C  
ANISOU  188  CG  LEU A  28     2908   3875   4427     41   -258   1413  A    C  
ATOM    189  CD1 LEU A  28      22.203 150.319 248.193  1.00 21.95      A    C  
ANISOU  189  CD1 LEU A  28     2006   3003   3332    111   -368   1296  A    C  
ATOM    190  CD2 LEU A  28      23.943 151.799 247.194  1.00 32.01      A    C  
ANISOU  190  CD2 LEU A  28     3208   4335   4618     79   -195   1567  A    C  
ATOM    191  N   GLY A  29      21.838 156.192 249.602  1.00 27.48      A    N  
ANISOU  191  N   GLY A  29     2644   2950   4846   -102   -102   1679  A    N  
ATOM    192  CA  GLY A  29      21.261 157.507 249.388  1.00 27.25      A    C  
ANISOU  192  CA  GLY A  29     2653   2739   4960    -70    -72   1817  A    C  
ATOM    193  C   GLY A  29      19.760 157.564 249.542  1.00 29.83      A    C  
ANISOU  193  C   GLY A  29     2990   3022   5324     53   -138   1786  A    C  
ATOM    194  O   GLY A  29      19.130 158.525 249.113  1.00 33.28      A    O  
ANISOU  194  O   GLY A  29     3460   3348   5837    134   -127   1922  A    O  
ATOM    195  N   LEU A  30      19.180 156.545 250.167  1.00 29.43      A    N  
ANISOU  195  N   LEU A  30     2906   3057   5217     71   -204   1615  A    N  
ATOM    196  CA  LEU A  30      17.733 156.505 250.363  1.00 28.77      A    C  
ANISOU  196  CA  LEU A  30     2801   2970   5161    175   -267   1581  A    C  
ATOM    197  C   LEU A  30      17.336 157.052 251.734  1.00 28.92      A    C  
ANISOU  197  C   LEU A  30     2824   2815   5350    156   -238   1456  A    C  
ATOM    198  O   LEU A  30      18.035 156.822 252.727  1.00 31.19      A    O  
ANISOU  198  O   LEU A  30     3118   3054   5677     51   -208   1318  A    O  
ATOM    199  CB  LEU A  30      17.229 155.065 250.206  1.00 27.23      A    C  
ANISOU  199  CB  LEU A  30     2566   2973   4805    193   -358   1480  A    C  
ATOM    200  CG  LEU A  30      17.607 154.387 248.885  1.00 28.95      A    C  
ANISOU  200  CG  LEU A  30     2796   3374   4829    226   -399   1568  A    C  
ATOM    201  CD1 LEU A  30      17.331 152.886 248.912  1.00 28.00      A    C  
ANISOU  201  CD1 LEU A  30     2670   3409   4561    212   -489   1429  A    C  
ATOM    202  CD2 LEU A  30      16.860 155.042 247.741  1.00 34.99      A    C  
ANISOU  202  CD2 LEU A  30     3556   4176   5562    349   -428   1749  A    C  
ATOM    203  N   GLU A  31      16.209 157.758 251.793  1.00 31.08      A    N  
ANISOU  203  N   GLU A  31     3091   3010   5709    271   -248   1501  A    N  
ATOM    204  CA  GLU A  31      15.686 158.228 253.074  1.00 34.27      A    C  
ANISOU  204  CA  GLU A  31     3496   3273   6251    288   -222   1373  A    C  
ATOM    205  C   GLU A  31      15.089 157.036 253.810  1.00 33.45      A    C  
ANISOU  205  C   GLU A  31     3320   3316   6074    270   -271   1212  A    C  
ATOM    206  O   GLU A  31      14.188 156.372 253.294  1.00 34.31      A    O  
ANISOU  206  O   GLU A  31     3362   3586   6090    332   -340   1237  A    O  
ATOM    207  CB  GLU A  31      14.602 159.287 252.862  1.00 36.72      A    C  
ANISOU  207  CB  GLU A  31     3815   3479   6658    450   -218   1474  A    C  
ATOM    208  CG  GLU A  31      15.029 160.472 252.013  1.00 54.41      A    C  
ANISOU  208  CG  GLU A  31     6147   5579   8948    479   -171   1651  A    C  
ATOM    209  CD  GLU A  31      13.852 161.351 251.608  1.00 66.36      A    C  
ANISOU  209  CD  GLU A  31     7679   7072  10462    652   -175   1721  A    C  
ATOM    210  OE1 GLU A  31      12.699 160.989 251.934  1.00 69.57      A    O  
ANISOU  210  OE1 GLU A  31     8003   7584  10847    757   -219   1658  A    O  
ATOM    211  OE2 GLU A  31      14.077 162.398 250.962  1.00 68.48      A    O1-
ANISOU  211  OE2 GLU A  31     8044   7230  10747    682   -134   1841  A    O1-
ATOM    212  N   THR A  32      15.576 156.776 255.021  1.00 36.20      A    N  
ANISOU  212  N   THR A  32     3682   3611   6461    180   -239   1050  A    N  
ATOM    213  CA  THR A  32      15.294 155.512 255.698  1.00 30.91      A    C  
ANISOU  213  CA  THR A  32     2963   3080   5703    132   -277    911  A    C  
ATOM    214  C   THR A  32      14.909 155.745 257.150  1.00 28.00      A    C  
ANISOU  214  C   THR A  32     2587   2629   5421    136   -237    766  A    C  
ATOM    215  O   THR A  32      15.550 156.524 257.854  1.00 26.52      A    O  
ANISOU  215  O   THR A  32     2459   2286   5332    103   -182    707  A    O  
ATOM    216  CB  THR A  32      16.533 154.585 255.671  1.00 30.59      A    C  
ANISOU  216  CB  THR A  32     2953   3112   5558     13   -284    855  A    C  
ATOM    217  CG2 THR A  32      16.198 153.200 256.227  1.00 21.98      A    C  
ANISOU  217  CG2 THR A  32     1836   2152   4363    -26   -331    734  A    C  
ATOM    218  OG1 THR A  32      17.013 154.453 254.326  1.00 30.92      A    O  
ANISOU  218  OG1 THR A  32     3008   3232   5508     21   -307    988  A    O  
ATOM    219  N   VAL A  33      13.878 155.037 257.600  1.00 24.07      A    N  
ANISOU  219  N   VAL A  33     2016   2249   4882    168   -265    705  A    N  
ATOM    220  CA  VAL A  33      13.434 155.096 258.986  1.00 24.13      A    C  
ANISOU  220  CA  VAL A  33     2005   2225   4940    180   -222    571  A    C  
ATOM    221  C   VAL A  33      13.364 153.677 259.533  1.00 24.36      A    C  
ANISOU  221  C   VAL A  33     2000   2398   4857     91   -251    478  A    C  
ATOM    222  O   VAL A  33      12.841 152.777 258.872  1.00 20.76      A    O  
ANISOU  222  O   VAL A  33     1494   2081   4311     71   -316    526  A    O  
ATOM    223  CB  VAL A  33      12.030 155.753 259.102  1.00 30.71      A    C  
ANISOU  223  CB  VAL A  33     2762   3067   5841    330   -209    607  A    C  
ATOM    224  CG1 VAL A  33      11.496 155.666 260.530  1.00 30.55      A    C  
ANISOU  224  CG1 VAL A  33     2706   3059   5843    353   -158    469  A    C  
ATOM    225  CG2 VAL A  33      12.055 157.205 258.616  1.00 28.84      A    C  
ANISOU  225  CG2 VAL A  33     2584   2655   5721    441   -178    703  A    C  
ATOM    226  N   ILE A  34      13.883 153.475 260.740  1.00 24.39      A    N  
ANISOU  226  N   ILE A  34     2041   2363   4862     35   -210    346  A    N  
ATOM    227  CA  ILE A  34      13.791 152.169 261.385  1.00 22.56      A    C  
ANISOU  227  CA  ILE A  34     1794   2249   4527    -41   -228    266  A    C  
ATOM    228  C   ILE A  34      12.727 152.203 262.468  1.00 25.97      A    C  
ANISOU  228  C   ILE A  34     2159   2723   4984      8   -184    202  A    C  
ATOM    229  O   ILE A  34      12.674 153.152 263.245  1.00 27.15      A    O  
ANISOU  229  O   ILE A  34     2322   2778   5214     77   -123    141  A    O  
ATOM    230  CB  ILE A  34      15.113 151.788 262.074  1.00 23.15      A    C  
ANISOU  230  CB  ILE A  34     1952   2286   4559   -125   -212    167  A    C  
ATOM    231  CG1 ILE A  34      16.269 151.792 261.081  1.00 28.85      A    C  
ANISOU  231  CG1 ILE A  34     2724   2988   5251   -169   -240    229  A    C  
ATOM    232  CG2 ILE A  34      15.002 150.416 262.722  1.00 29.61      A    C  
ANISOU  232  CG2 ILE A  34     2775   3212   5265   -189   -231    101  A    C  
ATOM    233  CD1 ILE A  34      17.607 151.426 261.707  1.00 29.21      A    C  
ANISOU  233  CD1 ILE A  34     2825   3025   5248   -242   -229    139  A    C  
ATOM    234  N   VAL A  35      11.893 151.168 262.536  1.00 21.59      A    N  
ANISOU  234  N   VAL A  35     1536   2311   4357    -31   -214    213  A    N  
ATOM    235  CA  VAL A  35      10.929 151.046 263.623  1.00 23.19      A    C  
ANISOU  235  CA  VAL A  35     1661   2589   4563     -3   -161    160  A    C  
ATOM    236  C   VAL A  35      11.355 149.874 264.499  1.00 24.05      A    C  
ANISOU  236  C   VAL A  35     1819   2746   4575   -113   -154     82  A    C  
ATOM    237  O   VAL A  35      11.614 148.784 263.993  1.00 23.67      A    O  
ANISOU  237  O   VAL A  35     1806   2744   4443   -210   -217    109  A    O  
ATOM    238  CB  VAL A  35       9.493 150.830 263.092  1.00 25.07      A    C  
ANISOU  238  CB  VAL A  35     1753   2971   4802     30   -192    250  A    C  
ATOM    239  CG1 VAL A  35       8.523 150.604 264.240  1.00 21.62      A    C  
ANISOU  239  CG1 VAL A  35     1216   2644   4356     46   -126    206  A    C  
ATOM    240  CG2 VAL A  35       9.052 152.019 262.250  1.00 22.00      A    C  
ANISOU  240  CG2 VAL A  35     1318   2540   4501    168   -200    336  A    C  
ATOM    241  N   GLU A  36      11.457 150.101 265.805  1.00 19.12      A    N  
ANISOU  241  N   GLU A  36     1212   2102   3950    -86    -80    -16  A    N  
ATOM    242  CA  GLU A  36      11.859 149.034 266.721  1.00 18.43      A    C  
ANISOU  242  CA  GLU A  36     1179   2062   3761   -173    -67    -80  A    C  
ATOM    243  C   GLU A  36      11.139 149.177 268.047  1.00 25.06      A    C  
ANISOU  243  C   GLU A  36     1965   2968   4589   -123     20   -140  A    C  
ATOM    244  O   GLU A  36      11.137 150.254 268.643  1.00 25.36      A    O  
ANISOU  244  O   GLU A  36     2004   2946   4684    -17     78   -209  A    O  
ATOM    245  CB  GLU A  36      13.384 149.033 266.929  1.00 22.45      A    C  
ANISOU  245  CB  GLU A  36     1815   2476   4239   -205    -81   -154  A    C  
ATOM    246  CG  GLU A  36      13.879 148.145 268.081  1.00 22.84      A    C  
ANISOU  246  CG  GLU A  36     1929   2567   4182   -254    -59   -232  A    C  
ATOM    247  CD  GLU A  36      13.607 146.658 267.861  1.00 26.53      A    C  
ANISOU  247  CD  GLU A  36     2418   3112   4550   -348   -101   -174  A    C  
ATOM    248  OE1 GLU A  36      12.979 146.040 268.747  1.00 26.65      A    O  
ANISOU  248  OE1 GLU A  36     2415   3200   4509   -376    -59   -180  A    O  
ATOM    249  OE2 GLU A  36      14.020 146.106 266.814  1.00 27.23      A    O1-
ANISOU  249  OE2 GLU A  36     2550   3183   4611   -394   -174   -123  A    O1-
ATOM    250  N   ARG A  37      10.551 148.079 268.516  1.00 24.77      A    N  
ANISOU  250  N   ARG A  37     1892   3048   4470   -201     31   -114  A    N  
ATOM    251  CA  ARG A  37       9.716 148.113 269.710  1.00 22.61      A    C  
ANISOU  251  CA  ARG A  37     1544   2879   4169   -158    124   -144  A    C  
ATOM    252  C   ARG A  37      10.560 148.220 270.965  1.00 26.04      A    C  
ANISOU  252  C   ARG A  37     2081   3271   4541   -127    179   -263  A    C  
ATOM    253  O   ARG A  37      10.104 148.725 271.984  1.00 32.56      A    O  
ANISOU  253  O   ARG A  37     2869   4149   5355    -37    264   -323  A    O  
ATOM    254  CB  ARG A  37       8.802 146.884 269.771  1.00 25.85      A    C  
ANISOU  254  CB  ARG A  37     1876   3430   4514   -277    121    -58  A    C  
ATOM    255  CG  ARG A  37       9.540 145.559 269.885  1.00 23.86      A    C  
ANISOU  255  CG  ARG A  37     1754   3149   4163   -414     75    -54  A    C  
ATOM    256  CD  ARG A  37       8.595 144.358 269.894  1.00 22.23      A    C  
ANISOU  256  CD  ARG A  37     1486   3053   3906   -555     65     39  A    C  
ATOM    257  NE  ARG A  37       9.364 143.121 269.773  1.00 25.54      A    N  
ANISOU  257  NE  ARG A  37     2064   3399   4241   -673      3     46  A    N  
ATOM    258  CZ  ARG A  37       8.840 141.908 269.610  1.00 29.99      A    C  
ANISOU  258  CZ  ARG A  37     2641   3995   4759   -826    -35    121  A    C  
ATOM    259  NH1 ARG A  37       7.520 141.737 269.557  1.00 25.15      A    N1+
ANISOU  259  NH1 ARG A  37     1868   3511   4178   -904    -18    200  A    N1+
ATOM    260  NH2 ARG A  37       9.645 140.859 269.503  1.00 25.94      A    N  
ANISOU  260  NH2 ARG A  37     2304   3386   4167   -901    -93    115  A    N  
ATOM    261  N   TYR A  38      11.799 147.754 270.893  1.00 26.61      A    N  
ANISOU  261  N   TYR A  38     2281   3266   4565   -190    127   -301  A    N  
ATOM    262  CA  TYR A  38      12.663 147.845 272.061  1.00 35.04      A    C  
ANISOU  262  CA  TYR A  38     3440   4312   5564   -161    162   -417  A    C  
ATOM    263  C   TYR A  38      13.598 149.054 272.009  1.00 34.79      A    C  
ANISOU  263  C   TYR A  38     3462   4151   5606    -98    146   -515  A    C  
ATOM    264  O   TYR A  38      13.722 149.701 270.968  1.00 31.62      A    O  
ANISOU  264  O   TYR A  38     3047   3662   5304    -90    107   -474  A    O  
ATOM    265  CB  TYR A  38      13.345 146.505 272.347  1.00 43.02      A    C  
ANISOU  265  CB  TYR A  38     4545   5352   6450   -255    128   -404  A    C  
ATOM    266  CG  TYR A  38      12.301 145.472 272.719  1.00 54.06      A    C  
ANISOU  266  CG  TYR A  38     5897   6864   7781   -320    166   -318  A    C  
ATOM    267  CD1 TYR A  38      11.170 145.857 273.434  1.00 57.29      A    C  
ANISOU  267  CD1 TYR A  38     6194   7377   8197   -268    258   -311  A    C  
ATOM    268  CD2 TYR A  38      12.428 144.134 272.360  1.00 54.76      A    C  
ANISOU  268  CD2 TYR A  38     6053   6955   7799   -434    114   -243  A    C  
ATOM    269  CE1 TYR A  38      10.195 144.953 273.783  1.00 58.54      A    C  
ANISOU  269  CE1 TYR A  38     6288   7656   8299   -346    301   -219  A    C  
ATOM    270  CE2 TYR A  38      11.449 143.208 272.713  1.00 57.34      A    C  
ANISOU  270  CE2 TYR A  38     6341   7372   8076   -522    148   -156  A    C  
ATOM    271  CZ  TYR A  38      10.335 143.631 273.426  1.00 64.53      A    C  
ANISOU  271  CZ  TYR A  38     7119   8402   8999   -486    245   -139  A    C  
ATOM    272  OH  TYR A  38       9.346 142.745 273.792  1.00 73.75      A    O  
ANISOU  272  OH  TYR A  38     8225   9676  10120   -590    288    -40  A    O  
ATOM    273  N   ASN A  39      14.230 149.367 273.137  1.00 33.09      A    N  
ANISOU  273  N   ASN A  39     3309   3924   5337    -59    176   -641  A    N  
ATOM    274  CA  ASN A  39      14.966 150.622 273.279  1.00 38.94      A    C  
ANISOU  274  CA  ASN A  39     4099   4540   6157     -9    166   -752  A    C  
ATOM    275  C   ASN A  39      16.391 150.606 272.749  1.00 35.74      A    C  
ANISOU  275  C   ASN A  39     3759   4058   5762    -88     89   -771  A    C  
ATOM    276  O   ASN A  39      17.044 151.648 272.688  1.00 41.13      A    O  
ANISOU  276  O   ASN A  39     4474   4626   6528    -82     71   -844  A    O  
ATOM    277  CB  ASN A  39      14.995 151.017 274.755  1.00 51.34      A    C  
ANISOU  277  CB  ASN A  39     5705   6143   7657     68    223   -898  A    C  
ATOM    278  CG  ASN A  39      15.501 149.887 275.642  1.00 62.54      A    C  
ANISOU  278  CG  ASN A  39     7172   7678   8913     25    221   -922  A    C  
ATOM    279  ND2 ASN A  39      16.071 150.241 276.787  1.00 68.21      A    N  
ANISOU  279  ND2 ASN A  39     7949   8410   9557     71    233  -1066  A    N  
ATOM    280  OD1 ASN A  39      15.379 148.707 275.295  1.00 62.03      A    O  
ANISOU  280  OD1 ASN A  39     7100   7684   8786    -46    205   -813  A    O  
ATOM    281  N   THR A  40      16.880 149.429 272.376  1.00 33.25      A    N  
ANISOU  281  N   THR A  40     3466   3807   5363   -162     45   -706  A    N  
ATOM    282  CA  THR A  40      18.193 149.328 271.742  1.00 29.37      A    C  
ANISOU  282  CA  THR A  40     3014   3275   4871   -222    -23   -705  A    C  
ATOM    283  C   THR A  40      18.079 148.621 270.396  1.00 25.72      A    C  
ANISOU  283  C   THR A  40     2537   2823   4414   -267    -66   -569  A    C  
ATOM    284  O   THR A  40      17.100 147.914 270.142  1.00 26.58      A    O  
ANISOU  284  O   THR A  40     2621   2983   4496   -274    -58   -490  A    O  
ATOM    285  CB  THR A  40      19.238 148.623 272.642  1.00 35.90      A    C  
ANISOU  285  CB  THR A  40     3900   4176   5565   -237    -46   -785  A    C  
ATOM    286  CG2 THR A  40      19.340 149.317 273.991  1.00 39.97      A    C  
ANISOU  286  CG2 THR A  40     4434   4696   6056   -189    -13   -932  A    C  
ATOM    287  OG1 THR A  40      18.863 147.254 272.846  1.00 42.19      A    O  
ANISOU  287  OG1 THR A  40     4726   5063   6241   -246    -42   -720  A    O  
ATOM    288  N   LEU A  41      19.091 148.802 269.551  1.00 25.39      A    N  
ANISOU  288  N   LEU A  41     2507   2742   4397   -303   -113   -546  A    N  
ATOM    289  CA  LEU A  41      19.174 148.132 268.260  1.00 26.59      A    C  
ANISOU  289  CA  LEU A  41     2661   2913   4530   -332   -159   -433  A    C  
ATOM    290  C   LEU A  41      19.903 146.794 268.437  1.00 25.10      A    C  
ANISOU  290  C   LEU A  41     2538   2803   4196   -347   -195   -439  A    C  
ATOM    291  O   LEU A  41      20.385 146.490 269.529  1.00 23.36      A    O  
ANISOU  291  O   LEU A  41     2352   2622   3900   -334   -185   -521  A    O  
ATOM    292  CB  LEU A  41      19.919 149.023 267.258  1.00 25.95      A    C  
ANISOU  292  CB  LEU A  41     2558   2766   4536   -349   -178   -394  A    C  
ATOM    293  CG  LEU A  41      19.443 150.484 267.146  1.00 29.68      A    C  
ANISOU  293  CG  LEU A  41     2996   3124   5158   -327   -144   -393  A    C  
ATOM    294  CD1 LEU A  41      20.279 151.282 266.147  1.00 27.01      A    C  
ANISOU  294  CD1 LEU A  41     2649   2716   4898   -364   -160   -333  A    C  
ATOM    295  CD2 LEU A  41      17.968 150.568 266.782  1.00 25.00      A    C  
ANISOU  295  CD2 LEU A  41     2360   2530   4610   -275   -125   -320  A    C  
ATOM    296  N   GLY A  42      19.953 145.985 267.382  1.00 23.93      A    N  
ANISOU  296  N   GLY A  42     2416   2675   4001   -360   -240   -356  A    N  
ATOM    297  CA  GLY A  42      20.705 144.738 267.413  1.00 22.14      A    C  
ANISOU  297  CA  GLY A  42     2272   2502   3638   -352   -278   -360  A    C  
ATOM    298  C   GLY A  42      19.839 143.503 267.544  1.00 20.44      A    C  
ANISOU  298  C   GLY A  42     2124   2297   3345   -372   -292   -321  A    C  
ATOM    299  O   GLY A  42      20.299 142.386 267.313  1.00 19.98      A    O  
ANISOU  299  O   GLY A  42     2159   2252   3178   -361   -333   -306  A    O  
ATOM    300  N   GLY A  43      18.580 143.707 267.918  1.00 21.07      A    N  
ANISOU  300  N   GLY A  43     2155   2371   3481   -402   -256   -301  A    N  
ATOM    301  CA  GLY A  43      17.621 142.621 267.997  1.00 19.24      A    C  
ANISOU  301  CA  GLY A  43     1963   2151   3195   -455   -266   -249  A    C  
ATOM    302  C   GLY A  43      18.018 141.458 268.891  1.00 14.65      A    C  
ANISOU  302  C   GLY A  43     1499   1583   2486   -457   -266   -269  A    C  
ATOM    303  O   GLY A  43      18.774 141.606 269.873  1.00 16.50      A    O  
ANISOU  303  O   GLY A  43     1757   1843   2669   -406   -238   -336  A    O  
ATOM    304  N   VAL A  44      17.518 140.283 268.522  1.00 16.85      A    N  
ANISOU  304  N   VAL A  44     1858   1837   2708   -517   -306   -210  A    N  
ATOM    305  CA  VAL A  44      17.723 139.086 269.318  1.00 16.90      A    C  
ANISOU  305  CA  VAL A  44     1997   1828   2595   -526   -305   -205  A    C  
ATOM    306  C   VAL A  44      19.201 138.720 269.363  1.00 19.59      A    C  
ANISOU  306  C   VAL A  44     2440   2165   2837   -428   -339   -253  A    C  
ATOM    307  O   VAL A  44      19.745 138.473 270.439  1.00 21.36      A    O  
ANISOU  307  O   VAL A  44     2717   2420   2981   -376   -311   -288  A    O  
ATOM    308  CB  VAL A  44      16.905 137.905 268.777  1.00 18.83      A    C  
ANISOU  308  CB  VAL A  44     2327   2017   2811   -629   -354   -131  A    C  
ATOM    309  CG1 VAL A  44      17.417 136.588 269.350  1.00 15.82      A    C  
ANISOU  309  CG1 VAL A  44     2134   1578   2299   -619   -371   -121  A    C  
ATOM    310  CG2 VAL A  44      15.420 138.095 269.091  1.00 16.12      A    C  
ANISOU  310  CG2 VAL A  44     1868   1715   2542   -736   -309    -76  A    C  
ATOM    311  N  ACYS A  45      19.858 138.730 268.206  0.45 19.31      A    N  
ANISOU  311  N  ACYS A  45     2422   2114   2801   -390   -396   -254  A    N  
ATOM    312  N  BCYS A  45      19.830 138.698 268.187  0.55 19.36      A    N  
ANISOU  312  N  BCYS A  45     2431   2118   2807   -393   -397   -252  A    N  
ATOM    313  CA ACYS A  45      21.261 138.330 268.125  0.45 19.10      A    C  
ANISOU  313  CA ACYS A  45     2475   2110   2674   -285   -427   -292  A    C  
ATOM    314  CA BCYS A  45      21.252 138.390 268.035  0.55 18.28      A    C  
ANISOU  314  CA BCYS A  45     2364   2006   2577   -286   -428   -291  A    C  
ATOM    315  C  ACYS A  45      22.144 139.089 269.107  0.45 22.23      A    C  
ANISOU  315  C  ACYS A  45     2799   2583   3062   -223   -388   -362  A    C  
ATOM    316  C  BCYS A  45      22.133 139.090 269.063  0.55 21.81      A    C  
ANISOU  316  C  BCYS A  45     2746   2529   3011   -224   -389   -360  A    C  
ATOM    317  O  ACYS A  45      22.909 138.484 269.860  0.45 22.23      A    O  
ANISOU  317  O  ACYS A  45     2878   2618   2950   -149   -394   -391  A    O  
ATOM    318  O  BCYS A  45      22.881 138.445 269.801  0.55 22.57      A    O  
ANISOU  318  O  BCYS A  45     2925   2657   2994   -151   -396   -387  A    O  
ATOM    319  CB ACYS A  45      21.796 138.510 266.705  0.45 18.38      A    C  
ANISOU  319  CB ACYS A  45     2367   2024   2592   -249   -475   -279  A    C  
ATOM    320  CB BCYS A  45      21.707 138.769 266.625  0.55 17.95      A    C  
ANISOU  320  CB BCYS A  45     2281   1974   2565   -259   -469   -278  A    C  
ATOM    321  SG ACYS A  45      23.439 137.801 266.451  0.45 23.82      A    S  
ANISOU  321  SG ACYS A  45     3152   2764   3136   -101   -512   -312  A    S  
ATOM    322  SG BCYS A  45      23.491 138.999 266.416  0.55 27.61      A    S  
ANISOU  322  SG BCYS A  45     3486   3288   3717   -133   -479   -323  A    S  
ATOM    323  N   LEU A  46      22.032 140.413 269.113  1.00 21.78      A    N  
ANISOU  323  N   LEU A  46     2603   2550   3121   -250   -354   -391  A    N  
ATOM    324  CA  LEU A  46      22.850 141.203 270.016  1.00 22.07      A    C  
ANISOU  324  CA  LEU A  46     2575   2650   3160   -212   -330   -474  A    C  
ATOM    325  C   LEU A  46      22.369 141.154 271.467  1.00 18.90      A    C  
ANISOU  325  C   LEU A  46     2191   2270   2719   -212   -284   -514  A    C  
ATOM    326  O   LEU A  46      23.183 141.009 272.381  1.00 17.02      A    O  
ANISOU  326  O   LEU A  46     1979   2100   2389   -153   -288   -574  A    O  
ATOM    327  CB  LEU A  46      22.936 142.654 269.533  1.00 25.61      A    C  
ANISOU  327  CB  LEU A  46     2894   3088   3749   -247   -314   -496  A    C  
ATOM    328  CG  LEU A  46      23.828 143.571 270.371  1.00 24.44      A    C  
ANISOU  328  CG  LEU A  46     2679   2989   3618   -234   -303   -594  A    C  
ATOM    329  CD1 LEU A  46      25.166 142.893 270.653  1.00 24.17      A    C  
ANISOU  329  CD1 LEU A  46     2679   3053   3453   -166   -344   -627  A    C  
ATOM    330  CD2 LEU A  46      24.047 144.897 269.657  1.00 23.10      A    C  
ANISOU  330  CD2 LEU A  46     2409   2778   3590   -281   -297   -596  A    C  
ATOM    331  N   ASN A  47      21.064 141.269 271.691  1.00 17.45      A    N  
ANISOU  331  N   ASN A  47     1985   2053   2593   -271   -239   -479  A    N  
ATOM    332  CA  ASN A  47      20.592 141.475 273.065  1.00 19.06      A    C  
ANISOU  332  CA  ASN A  47     2178   2300   2764   -262   -178   -522  A    C  
ATOM    333  C   ASN A  47      20.355 140.209 273.878  1.00 20.00      A    C  
ANISOU  333  C   ASN A  47     2414   2438   2746   -254   -163   -476  A    C  
ATOM    334  O   ASN A  47      20.648 140.168 275.077  1.00 20.52      A    O  
ANISOU  334  O   ASN A  47     2507   2569   2720   -202   -134   -523  A    O  
ATOM    335  CB  ASN A  47      19.337 142.354 273.075  1.00 18.96      A    C  
ANISOU  335  CB  ASN A  47     2063   2271   2871   -305   -121   -513  A    C  
ATOM    336  CG  ASN A  47      19.602 143.757 272.542  1.00 21.25      A    C  
ANISOU  336  CG  ASN A  47     2256   2524   3292   -296   -125   -567  A    C  
ATOM    337  ND2 ASN A  47      19.305 143.976 271.265  1.00 19.07      A    N  
ANISOU  337  ND2 ASN A  47     1942   2198   3108   -330   -153   -500  A    N  
ATOM    338  OD1 ASN A  47      20.091 144.621 273.264  1.00 20.28      A    O  
ANISOU  338  OD1 ASN A  47     2105   2416   3184   -261   -109   -666  A    O  
ATOM    339  N   VAL A  48      19.807 139.186 273.228  1.00 16.38      A    N  
ANISOU  339  N   VAL A  48     2032   1918   2272   -310   -186   -381  A    N  
ATOM    340  CA  VAL A  48      19.430 137.952 273.907  1.00 19.01      A    C  
ANISOU  340  CA  VAL A  48     2493   2237   2495   -331   -169   -313  A    C  
ATOM    341  C   VAL A  48      19.761 136.709 273.075  1.00 22.32      A    C  
ANISOU  341  C   VAL A  48     3063   2563   2855   -338   -241   -253  A    C  
ATOM    342  O   VAL A  48      19.103 135.676 273.218  1.00 26.04      A    O  
ANISOU  342  O   VAL A  48     3642   2971   3282   -408   -237   -173  A    O  
ATOM    343  CB  VAL A  48      17.911 137.938 274.220  1.00 22.35      A    C  
ANISOU  343  CB  VAL A  48     2854   2667   2971   -438   -102   -243  A    C  
ATOM    344  CG1 VAL A  48      17.545 139.074 275.171  1.00 18.88      A    C  
ANISOU  344  CG1 VAL A  48     2288   2323   2564   -400    -21   -308  A    C  
ATOM    345  CG2 VAL A  48      17.101 138.058 272.935  1.00 16.55      A    C  
ANISOU  345  CG2 VAL A  48     2051   1879   2356   -532   -137   -194  A    C  
ATOM    346  N   GLY A  49      20.784 136.798 272.221  1.00 18.60      A    N  
ANISOU  346  N   GLY A  49     2605   2083   2378   -266   -303   -293  A    N  
ATOM    347  CA  GLY A  49      21.106 135.697 271.318  1.00 20.98      A    C  
ANISOU  347  CA  GLY A  49     3054   2298   2619   -248   -373   -253  A    C  
ATOM    348  C   GLY A  49      22.586 135.380 271.143  1.00 20.98      A    C  
ANISOU  348  C   GLY A  49     3123   2333   2516    -97   -420   -298  A    C  
ATOM    349  O   GLY A  49      23.260 135.049 272.118  1.00 22.12      A    O  
ANISOU  349  O   GLY A  49     3325   2527   2554     -6   -410   -317  A    O  
ATOM    350  N  ACYS A  50      23.077 135.515 269.913  0.01 18.65      A    N  
ANISOU  350  N  ACYS A  50     1692   2610   2784     -4   -155   -414  A    N  
ATOM    351  N  BCYS A  50      23.086 135.477 269.906  0.99 15.76      A    N  
ANISOU  351  N  BCYS A  50     1326   2246   2416     -3   -153   -416  A    N  
ATOM    352  CA ACYS A  50      24.451 135.172 269.549  0.01 19.26      A    C  
ANISOU  352  CA ACYS A  50     1798   2769   2751     28   -110   -280  A    C  
ATOM    353  CA BCYS A  50      24.475 135.124 269.570  0.99 20.96      A    C  
ANISOU  353  CA BCYS A  50     2015   2983   2965     26   -107   -282  A    C  
ATOM    354  C  ACYS A  50      25.509 135.697 270.513  0.01 20.16      A    C  
ANISOU  354  C  ACYS A  50     1929   2813   2917    -58    -61   -145  A    C  
ATOM    355  C  BCYS A  50      25.537 135.694 270.510  0.99 21.33      A    C  
ANISOU  355  C  BCYS A  50     2078   2962   3064    -57    -60   -142  A    C  
ATOM    356  O  ACYS A  50      26.292 134.931 271.073  0.01 20.87      A    O  
ANISOU  356  O  ACYS A  50     2050   2893   2989    -93     -5   -140  A    O  
ATOM    357  O  BCYS A  50      26.369 134.957 271.044  0.99 21.92      A    O  
ANISOU  357  O  BCYS A  50     2183   3029   3118    -91     -4   -130  A    O  
ATOM    358  CB ACYS A  50      24.757 135.711 268.152  0.01 19.52      A    C  
ANISOU  358  CB ACYS A  50     1813   2956   2649    164   -148   -154  A    C  
ATOM    359  CB BCYS A  50      24.834 135.571 268.142  0.99 18.80      A    C  
ANISOU  359  CB BCYS A  50     1724   2871   2548    166   -143   -160  A    C  
ATOM    360  SG ACYS A  50      23.311 135.871 267.089  0.01 33.83      A    S  
ANISOU  360  SG ACYS A  50     3590   4854   4411    295   -262   -294  A    S  
ATOM    361  SG BCYS A  50      23.486 135.600 266.972  0.99 33.50      A    S  
ANISOU  361  SG BCYS A  50     3552   4840   4338    312   -254   -304  A    S  
ATOM    362  N   ILE A  51      25.519 137.013 270.697  1.00 16.68      A    N  
ANISOU  362  N   ILE A  51     1456   2315   2568    -80   -101    -51  A    N  
ATOM    363  CA  ILE A  51      26.579 137.676 271.449  1.00 15.34      A    C  
ANISOU  363  CA  ILE A  51     1266   2071   2491   -137    -93     55  A    C  
ATOM    364  C   ILE A  51      26.716 137.281 272.931  1.00 13.46      A    C  
ANISOU  364  C   ILE A  51     1058   1769   2287   -205    -72    -60  A    C  
ATOM    365  O   ILE A  51      27.801 136.866 273.357  1.00 17.22      A    O  
ANISOU  365  O   ILE A  51     1552   2253   2739   -218    -39    -14  A    O  
ATOM    366  CB  ILE A  51      26.535 139.212 271.249  1.00 19.74      A    C  
ANISOU  366  CB  ILE A  51     1745   2546   3209   -137   -162    171  A    C  
ATOM    367  CG1 ILE A  51      26.671 139.541 269.764  1.00 19.72      A    C  
ANISOU  367  CG1 ILE A  51     1712   2644   3137    -41   -151    367  A    C  
ATOM    368  CG2 ILE A  51      27.649 139.872 272.032  1.00 18.34      A    C  
ANISOU  368  CG2 ILE A  51     1512   2263   3193   -190   -180    239  A    C  
ATOM    369  CD1 ILE A  51      27.930 138.935 269.118  1.00 15.60      A    C  
ANISOU  369  CD1 ILE A  51     1193   2243   2491      7    -64    520  A    C  
ATOM    370  N   PRO A  52      25.640 137.429 273.728  1.00 14.60      A    N  
ANISOU  370  N   PRO A  52     1202   1870   2476   -229    -89   -202  A    N  
ATOM    371  CA  PRO A  52      25.786 137.025 275.134  1.00 20.30      A    C  
ANISOU  371  CA  PRO A  52     1952   2585   3178   -253    -51   -283  A    C  
ATOM    372  C   PRO A  52      26.095 135.538 275.295  1.00 18.44      A    C  
ANISOU  372  C   PRO A  52     1774   2394   2838   -255     46   -270  A    C  
ATOM    373  O   PRO A  52      26.908 135.143 276.160  1.00 23.39      A    O  
ANISOU  373  O   PRO A  52     2432   3038   3418   -252     76   -246  A    O  
ATOM    374  CB  PRO A  52      24.409 137.339 275.744  1.00 22.71      A    C  
ANISOU  374  CB  PRO A  52     2232   2872   3525   -257    -56   -422  A    C  
ATOM    375  CG  PRO A  52      23.486 137.511 274.594  1.00 20.91      A    C  
ANISOU  375  CG  PRO A  52     1976   2632   3336   -247    -89   -435  A    C  
ATOM    376  CD  PRO A  52      24.316 138.023 273.464  1.00 16.52      A    C  
ANISOU  376  CD  PRO A  52     1410   2085   2783   -219   -139   -287  A    C  
ATOM    377  N   SER A  53      25.474 134.716 274.453  1.00 15.22      A    N  
ANISOU  377  N   SER A  53     1369   2000   2416   -247     77   -298  A    N  
ATOM    378  CA  SER A  53      25.719 133.287 274.549  1.00 20.82      A    C  
ANISOU  378  CA  SER A  53     2105   2713   3094   -248    153   -299  A    C  
ATOM    379  C   SER A  53      27.187 133.002 274.247  1.00 21.27      A    C  
ANISOU  379  C   SER A  53     2190   2808   3083   -227    152   -200  A    C  
ATOM    380  O   SER A  53      27.822 132.242 274.966  1.00 19.07      A    O  
ANISOU  380  O   SER A  53     1942   2521   2781   -233    202   -167  A    O  
ATOM    381  CB  SER A  53      24.751 132.466 273.673  1.00 20.23      A    C  
ANISOU  381  CB  SER A  53     1992   2621   3075   -230    154   -399  A    C  
ATOM    382  OG  SER A  53      24.919 132.726 272.294  1.00 34.09      A    O  
ANISOU  382  OG  SER A  53     3734   4447   4774   -164     79   -405  A    O  
ATOM    383  N   LYS A  54      27.748 133.665 273.240  1.00 18.69      A    N  
ANISOU  383  N   LYS A  54     1842   2530   2729   -194    103   -130  A    N  
ATOM    384  CA  LYS A  54      29.163 133.469 272.924  1.00 19.75      A    C  
ANISOU  384  CA  LYS A  54     1980   2709   2814   -171    117    -25  A    C  
ATOM    385  C   LYS A  54      30.098 134.010 274.028  1.00 23.66      A    C  
ANISOU  385  C   LYS A  54     2476   3159   3357   -206    104     27  A    C  
ATOM    386  O   LYS A  54      31.166 133.438 274.294  1.00 21.22      A    O  
ANISOU  386  O   LYS A  54     2179   2862   3020   -198    126     68  A    O  
ATOM    387  CB  LYS A  54      29.501 134.031 271.534  1.00 23.41      A    C  
ANISOU  387  CB  LYS A  54     2401   3263   3230   -106     99     76  A    C  
ATOM    388  CG  LYS A  54      29.562 132.971 270.402  1.00 26.96      A    C  
ANISOU  388  CG  LYS A  54     2852   3831   3561    -13    116     28  A    C  
ATOM    389  CD  LYS A  54      28.203 132.696 269.733  1.00 27.61      A    C  
ANISOU  389  CD  LYS A  54     2923   3943   3623     41     67   -119  A    C  
ATOM    390  CE  LYS A  54      27.432 131.578 270.419  1.00 27.47      A    C  
ANISOU  390  CE  LYS A  54     2914   3819   3704     -8     75   -288  A    C  
ATOM    391  NZ  LYS A  54      26.062 131.373 269.849  1.00 28.07      A    N1+
ANISOU  391  NZ  LYS A  54     2949   3890   3827     34     15   -454  A    N1+
ATOM    392  N   ALA A  55      29.700 135.093 274.690  1.00 19.98      A    N  
ANISOU  392  N   ALA A  55     1982   2639   2971   -229     50     -5  A    N  
ATOM    393  CA  ALA A  55      30.487 135.576 275.832  1.00 18.98      A    C  
ANISOU  393  CA  ALA A  55     1839   2477   2895   -233      3    -24  A    C  
ATOM    394  C   ALA A  55      30.552 134.539 276.973  1.00 18.42      A    C  
ANISOU  394  C   ALA A  55     1837   2444   2718   -211     51    -79  A    C  
ATOM    395  O   ALA A  55      31.650 134.164 277.485  1.00 18.14      A    O  
ANISOU  395  O   ALA A  55     1814   2426   2654   -186     42    -52  A    O  
ATOM    396  CB  ALA A  55      29.918 136.896 276.344  1.00 16.97      A    C  
ANISOU  396  CB  ALA A  55     1526   2161   2762   -238    -86   -102  A    C  
ATOM    397  N   LEU A  56      29.368 134.065 277.362  1.00 12.65      A    N  
ANISOU  397  N   LEU A  56     1137   1727   1940   -213    108   -137  A    N  
ATOM    398  CA  LEU A  56      29.288 133.070 278.431  1.00 13.79      A    C  
ANISOU  398  CA  LEU A  56     1333   1912   1995   -182    186   -132  A    C  
ATOM    399  C   LEU A  56      30.005 131.766 278.051  1.00 21.17      A    C  
ANISOU  399  C   LEU A  56     2301   2836   2908   -182    244    -49  A    C  
ATOM    400  O   LEU A  56      30.650 131.115 278.892  1.00 27.98      A    O  
ANISOU  400  O   LEU A  56     3199   3725   3705   -140    272      0  A    O  
ATOM    401  CB  LEU A  56      27.825 132.825 278.825  1.00 11.95      A    C  
ANISOU  401  CB  LEU A  56     1094   1683   1763   -189    264   -175  A    C  
ATOM    402  CG  LEU A  56      27.117 134.076 279.368  1.00 18.89      A    C  
ANISOU  402  CG  LEU A  56     1934   2588   2654   -168    205   -282  A    C  
ATOM    403  CD1 LEU A  56      25.672 133.790 279.766  1.00 19.28      A    C  
ANISOU  403  CD1 LEU A  56     1962   2654   2710   -171    302   -319  A    C  
ATOM    404  CD2 LEU A  56      27.880 134.660 280.548  1.00 18.67      A    C  
ANISOU  404  CD2 LEU A  56     1911   2638   2547    -86    136   -333  A    C  
ATOM    405  N   LEU A  57      29.908 131.401 276.776  1.00 18.20      A    N  
ANISOU  405  N   LEU A  57     1905   2431   2578   -207    248    -45  A    N  
ATOM    406  CA  LEU A  57      30.557 130.194 276.274  1.00 18.51      A    C  
ANISOU  406  CA  LEU A  57     1955   2458   2619   -193    282    -10  A    C  
ATOM    407  C   LEU A  57      32.074 130.329 276.301  1.00 19.60      A    C  
ANISOU  407  C   LEU A  57     2097   2630   2720   -168    243     49  A    C  
ATOM    408  O   LEU A  57      32.788 129.353 276.591  1.00 14.89      A    O  
ANISOU  408  O   LEU A  57     1523   2024   2112   -143    268     85  A    O  
ATOM    409  CB  LEU A  57      30.088 129.868 274.856  1.00 13.12      A    C  
ANISOU  409  CB  LEU A  57     1234   1778   1973   -186    269    -69  A    C  
ATOM    410  CG  LEU A  57      28.705 129.230 274.726  1.00 19.18      A    C  
ANISOU  410  CG  LEU A  57     1971   2480   2836   -202    300   -158  A    C  
ATOM    411  CD1 LEU A  57      28.212 129.298 273.282  1.00 19.59      A    C  
ANISOU  411  CD1 LEU A  57     1977   2573   2895   -161    238   -261  A    C  
ATOM    412  CD2 LEU A  57      28.770 127.785 275.201  1.00 12.19      A    C  
ANISOU  412  CD2 LEU A  57     1078   1509   2046   -204    364   -141  A    C  
ATOM    413  N   HIS A  58      32.573 131.528 276.006  1.00 16.92      A    N  
ANISOU  413  N   HIS A  58     1719   2310   2399   -174    181     67  A    N  
ATOM    414  CA  HIS A  58      34.008 131.756 276.117  1.00 19.66      A    C  
ANISOU  414  CA  HIS A  58     2038   2668   2764   -156    144    121  A    C  
ATOM    415  C   HIS A  58      34.437 131.593 277.579  1.00 21.81      A    C  
ANISOU  415  C   HIS A  58     2346   2940   3002   -122    113     93  A    C  
ATOM    416  O   HIS A  58      35.462 130.938 277.888  1.00 20.32      A    O  
ANISOU  416  O   HIS A  58     2169   2762   2792    -87    108    122  A    O  
ATOM    417  CB  HIS A  58      34.405 133.138 275.603  1.00 22.49      A    C  
ANISOU  417  CB  HIS A  58     2312   3010   3224   -174     89    167  A    C  
ATOM    418  CG  HIS A  58      35.839 133.471 275.852  1.00 26.34      A    C  
ANISOU  418  CG  HIS A  58     2734   3476   3796   -164     45    211  A    C  
ATOM    419  CD2 HIS A  58      36.973 133.038 275.248  1.00 28.13      A    C  
ANISOU  419  CD2 HIS A  58     2921   3733   4035   -147     78    290  A    C  
ATOM    420  ND1 HIS A  58      36.243 134.339 276.847  1.00 30.71      A    N  
ANISOU  420  ND1 HIS A  58     3237   3972   4459   -159    -55    148  A    N  
ATOM    421  CE1 HIS A  58      37.559 134.429 276.839  1.00 32.68      A    C  
ANISOU  421  CE1 HIS A  58     3411   4197   4808   -148    -87    186  A    C  
ATOM    422  NE2 HIS A  58      38.027 133.652 275.880  1.00 29.96      A    N  
ANISOU  422  NE2 HIS A  58     3074   3908   4403   -146      4    287  A    N  
ATOM    423  N   VAL A  59      33.652 132.176 278.484  1.00 21.54      A    N  
ANISOU  423  N   VAL A  59     2325   2914   2946   -110     89     28  A    N  
ATOM    424  CA  VAL A  59      33.946 131.949 279.909  1.00 23.07      A    C  
ANISOU  424  CA  VAL A  59     2557   3165   3045    -31     65     -3  A    C  
ATOM    425  C   VAL A  59      34.033 130.455 280.283  1.00 22.49      A    C  
ANISOU  425  C   VAL A  59     2552   3111   2884      4    159     87  A    C  
ATOM    426  O   VAL A  59      35.019 129.992 280.912  1.00 21.57      A    O  
ANISOU  426  O   VAL A  59     2455   3027   2712     72    129    116  A    O  
ATOM    427  CB  VAL A  59      32.913 132.669 280.807  1.00 24.15      A    C  
ANISOU  427  CB  VAL A  59     2694   3352   3130      7     47    -94  A    C  
ATOM    428  CG1 VAL A  59      32.954 132.136 282.221  1.00 21.60      A    C  
ANISOU  428  CG1 VAL A  59     2425   3146   2636    126     70    -92  A    C  
ATOM    429  CG2 VAL A  59      33.149 134.177 280.772  1.00 22.67      A    C  
ANISOU  429  CG2 VAL A  59     2418   3125   3069      4    -92   -207  A    C  
ATOM    430  N   ALA A  60      33.025 129.699 279.853  1.00 20.68      A    N  
ANISOU  430  N   ALA A  60     2337   2840   2679    -40    262    128  A    N  
ATOM    431  CA  ALA A  60      32.984 128.254 280.103  1.00 19.46      A    C  
ANISOU  431  CA  ALA A  60     2214   2651   2528    -20    356    227  A    C  
ATOM    432  C   ALA A  60      34.230 127.522 279.567  1.00 18.40      A    C  
ANISOU  432  C   ALA A  60     2078   2482   2433    -10    324    256  A    C  
ATOM    433  O   ALA A  60      34.852 126.679 280.264  1.00 21.98      A    O  
ANISOU  433  O   ALA A  60     2561   2936   2853     51    342    338  A    O  
ATOM    434  CB  ALA A  60      31.719 127.675 279.482  1.00 17.21      A    C  
ANISOU  434  CB  ALA A  60     1900   2284   2355    -83    442    225  A    C  
ATOM    435  N   LYS A  61      34.593 127.861 278.330  1.00 15.95      A    N  
ANISOU  435  N   LYS A  61     1723   2156   2180    -53    282    200  A    N  
ATOM    436  CA  LYS A  61      35.763 127.277 277.679  1.00 17.87      A    C  
ANISOU  436  CA  LYS A  61     1943   2392   2454    -33    258    210  A    C  
ATOM    437  C   LYS A  61      37.037 127.535 278.469  1.00 19.89      A    C  
ANISOU  437  C   LYS A  61     2205   2684   2668     18    193    235  A    C  
ATOM    438  O   LYS A  61      37.839 126.609 278.712  1.00 16.67      A    O  
ANISOU  438  O   LYS A  61     1809   2260   2266     65    191    273  A    O  
ATOM    439  CB  LYS A  61      35.918 127.832 276.257  1.00 17.99      A    C  
ANISOU  439  CB  LYS A  61     1900   2442   2495    -58    240    169  A    C  
ATOM    440  CG  LYS A  61      37.130 127.285 275.506  1.00 20.03      A    C  
ANISOU  440  CG  LYS A  61     2117   2730   2765    -19    232    175  A    C  
ATOM    441  CD  LYS A  61      37.173 127.781 274.054  1.00 19.53      A    C  
ANISOU  441  CD  LYS A  61     1990   2752   2680     -6    243    164  A    C  
ATOM    442  CE  LYS A  61      38.400 127.241 273.335  1.00 18.59      A    C  
ANISOU  442  CE  LYS A  61     1815   2699   2551     55    253    172  A    C  
ATOM    443  NZ  LYS A  61      38.549 127.799 271.969  1.00 19.29      A    N1+
ANISOU  443  NZ  LYS A  61     1832   2921   2576    101    287    203  A    N1+
ATOM    444  N   VAL A  62      37.238 128.789 278.866  1.00 16.86      A    N  
ANISOU  444  N   VAL A  62     1796   2338   2274     19    122    195  A    N  
ATOM    445  CA  VAL A  62      38.428 129.089 279.660  1.00 14.58      A    C  
ANISOU  445  CA  VAL A  62     1487   2076   1978     83     29    174  A    C  
ATOM    446  C   VAL A  62      38.429 128.317 280.989  1.00 15.48      A    C  
ANISOU  446  C   VAL A  62     1677   2238   1965    183     30    207  A    C  
ATOM    447  O   VAL A  62      39.464 127.771 281.386  1.00 18.71      A    O  
ANISOU  447  O   VAL A  62     2091   2659   2358    251    -15    227  A    O  
ATOM    448  CB  VAL A  62      38.641 130.597 279.871  1.00 21.64      A    C  
ANISOU  448  CB  VAL A  62     2304   2968   2948     76    -75     91  A    C  
ATOM    449  CG1 VAL A  62      39.815 130.843 280.816  1.00 19.80      A    C  
ANISOU  449  CG1 VAL A  62     2033   2758   2732    164   -202     20  A    C  
ATOM    450  CG2 VAL A  62      38.886 131.274 278.535  1.00 18.20      A    C  
ANISOU  450  CG2 VAL A  62     1776   2485   2655     -5    -58    130  A    C  
ATOM    451  N   ILE A  63      37.281 128.257 281.670  1.00 18.16      A    N  
ANISOU  451  N   ILE A  63     2070   2618   2213    206     92    232  A    N  
ATOM    452  CA  ILE A  63      37.213 127.477 282.921  1.00 20.93      A    C  
ANISOU  452  CA  ILE A  63     2489   3044   2420    325    130    323  A    C  
ATOM    453  C   ILE A  63      37.659 126.016 282.732  1.00 25.08      A    C  
ANISOU  453  C   ILE A  63     3038   3495   2998    334    196    455  A    C  
ATOM    454  O   ILE A  63      38.564 125.491 283.449  1.00 26.61      A    O  
ANISOU  454  O   ILE A  63     3258   3732   3122    442    150    510  A    O  
ATOM    455  CB  ILE A  63      35.786 127.475 283.518  1.00 19.48      A    C  
ANISOU  455  CB  ILE A  63     2337   2914   2152    340    240    377  A    C  
ATOM    456  CG1 ILE A  63      35.421 128.864 284.054  1.00 19.32      A    C  
ANISOU  456  CG1 ILE A  63     2294   2997   2049    384    153    227  A    C  
ATOM    457  CG2 ILE A  63      35.669 126.446 284.642  1.00 20.13      A    C  
ANISOU  457  CG2 ILE A  63     2476   3071   2102    465    334    555  A    C  
ATOM    458  CD1 ILE A  63      33.961 128.990 284.501  1.00 19.89      A    C  
ANISOU  458  CD1 ILE A  63     2377   3129   2049    392    267    257  A    C  
ATOM    459  N   GLU A  64      37.056 125.366 281.741  1.00 23.93      A    N  
ANISOU  459  N   GLU A  64     2869   3231   2992    234    281    485  A    N  
ATOM    460  CA  GLU A  64      37.419 123.974 281.490  1.00 28.33      A    C  
ANISOU  460  CA  GLU A  64     3422   3686   3658    242    325    576  A    C  
ATOM    461  C   GLU A  64      38.883 123.788 281.068  1.00 27.64      A    C  
ANISOU  461  C   GLU A  64     3308   3590   3602    270    230    523  A    C  
ATOM    462  O   GLU A  64      39.521 122.810 281.458  1.00 28.39      A    O  
ANISOU  462  O   GLU A  64     3416   3647   3726    336    226    606  A    O  
ATOM    463  CB  GLU A  64      36.429 123.290 280.544  1.00 32.74      A    C  
ANISOU  463  CB  GLU A  64     3933   4111   4395    152    406    567  A    C  
ATOM    464  CG  GLU A  64      35.019 123.257 281.135  1.00 44.44      A    C  
ANISOU  464  CG  GLU A  64     5419   5579   5886    134    519    652  A    C  
ATOM    465  CD  GLU A  64      34.905 122.327 282.348  1.00 54.80      A    C  
ANISOU  465  CD  GLU A  64     6757   6879   7188    220    618    875  A    C  
ATOM    466  OE1 GLU A  64      35.813 121.493 282.567  1.00 56.21      A    O  
ANISOU  466  OE1 GLU A  64     6943   7011   7401    281    594    960  A    O  
ATOM    467  OE2 GLU A  64      33.914 122.448 283.099  1.00 58.64      A    O1-
ANISOU  467  OE2 GLU A  64     7246   7411   7622    241    727    984  A    O1-
ATOM    468  N   GLU A  65      39.422 124.714 280.280  1.00 21.66      A    N  
ANISOU  468  N   GLU A  65     2502   2867   2859    224    162    404  A    N  
ATOM    469  CA  GLU A  65      40.837 124.605 279.908  1.00 22.46      A    C  
ANISOU  469  CA  GLU A  65     2555   2973   3005    252     89    364  A    C  
ATOM    470  C   GLU A  65      41.762 124.743 281.121  1.00 22.11      A    C  
ANISOU  470  C   GLU A  65     2533   2988   2879    360     -5    377  A    C  
ATOM    471  O   GLU A  65      42.736 123.976 281.294  1.00 28.85      A    O  
ANISOU  471  O   GLU A  65     3380   3822   3761    425    -46    401  A    O  
ATOM    472  CB  GLU A  65      41.194 125.645 278.838  1.00 23.38      A    C  
ANISOU  472  CB  GLU A  65     2590   3120   3173    188     64    284  A    C  
ATOM    473  CG  GLU A  65      40.632 125.295 277.469  1.00 36.89      A    C  
ANISOU  473  CG  GLU A  65     4268   4814   4934    135    136    259  A    C  
ATOM    474  CD  GLU A  65      41.103 126.230 276.380  1.00 49.65      A    C  
ANISOU  474  CD  GLU A  65     5798   6494   6574    106    136    237  A    C  
ATOM    475  OE1 GLU A  65      41.394 125.735 275.269  1.00 51.88      A    O  
ANISOU  475  OE1 GLU A  65     6030   6816   6868    127    173    213  A    O  
ATOM    476  OE2 GLU A  65      41.171 127.456 276.631  1.00 55.05      A    O1-
ANISOU  476  OE2 GLU A  65     6450   7193   7273     76    101    249  A    O1-
ATOM    477  N   ALA A  66      41.441 125.725 281.962  1.00 21.32      A    N  
ANISOU  477  N   ALA A  66     2452   2970   2678    397    -56    336  A    N  
ATOM    478  CA  ALA A  66      42.189 125.959 283.188  1.00 26.15      A    C  
ANISOU  478  CA  ALA A  66     3079   3675   3182    538   -174    302  A    C  
ATOM    479  C   ALA A  66      42.226 124.683 283.997  1.00 27.92      A    C  
ANISOU  479  C   ALA A  66     3383   3919   3306    651   -129    453  A    C  
ATOM    480  O   ALA A  66      43.298 124.244 284.422  1.00 30.91      A    O  
ANISOU  480  O   ALA A  66     3757   4317   3670    751   -215    456  A    O  
ATOM    481  CB  ALA A  66      41.557 127.079 284.005  1.00 25.51      A    C  
ANISOU  481  CB  ALA A  66     3007   3697   2990    590   -230    212  A    C  
ATOM    482  N   LYS A  67      41.058 124.070 284.187  1.00 27.02      A    N  
ANISOU  482  N   LYS A  67     3326   3788   3152    636     11    593  A    N  
ATOM    483  CA  LYS A  67      41.018 122.792 284.907  1.00 29.13      A    C  
ANISOU  483  CA  LYS A  67     3647   4043   3379    736     84    798  A    C  
ATOM    484  C   LYS A  67      41.824 121.683 284.209  1.00 28.08      A    C  
ANISOU  484  C   LYS A  67     3479   3759   3432    705     76    835  A    C  
ATOM    485  O   LYS A  67      42.510 120.894 284.860  1.00 29.16      A    O  
ANISOU  485  O   LYS A  67     3640   3899   3540    825     45    945  A    O  
ATOM    486  CB  LYS A  67      39.571 122.371 285.148  1.00 35.35      A    C  
ANISOU  486  CB  LYS A  67     4461   4806   4165    706    256    960  A    C  
ATOM    487  CG  LYS A  67      38.884 123.292 286.140  1.00 48.95      A    C  
ANISOU  487  CG  LYS A  67     6222   6722   5654    798    267    948  A    C  
ATOM    488  CD  LYS A  67      37.421 122.948 286.366  1.00 58.07      A    C  
ANISOU  488  CD  LYS A  67     7381   7862   6821    765    456   1113  A    C  
ATOM    489  CE  LYS A  67      36.809 123.927 287.366  1.00 61.47      A    C  
ANISOU  489  CE  LYS A  67     7841   8525   6991    884    460   1070  A    C  
ATOM    490  NZ  LYS A  67      35.328 123.807 287.472  1.00 64.08      A    N1+
ANISOU  490  NZ  LYS A  67     8151   8846   7349    834    647   1195  A    N1+
ATOM    491  N   ALA A  68      41.747 121.628 282.884  1.00 25.79      A    N  
ANISOU  491  N   ALA A  68     3126   3354   3320    567     96    734  A    N  
ATOM    492  CA  ALA A  68      42.451 120.594 282.125  1.00 26.99      A    C  
ANISOU  492  CA  ALA A  68     3226   3379   3650    552     83    723  A    C  
ATOM    493  C   ALA A  68      43.974 120.721 282.217  1.00 27.63      A    C  
ANISOU  493  C   ALA A  68     3278   3509   3713    625    -45    644  A    C  
ATOM    494  O   ALA A  68      44.700 119.750 281.981  1.00 23.27      A    O  
ANISOU  494  O   ALA A  68     2693   2872   3277    663    -71    660  A    O  
ATOM    495  CB  ALA A  68      42.011 120.616 280.670  1.00 25.01      A    C  
ANISOU  495  CB  ALA A  68     2907   3054   3542    429    121    598  A    C  
ATOM    496  N   LEU A  69      44.460 121.916 282.537  1.00 23.36      A    N  
ANISOU  496  N   LEU A  69     2725   3085   3065    647   -135    542  A    N  
ATOM    497  CA  LEU A  69      45.909 122.099 282.704  1.00 26.17      A    C  
ANISOU  497  CA  LEU A  69     3026   3476   3443    720   -267    454  A    C  
ATOM    498  C   LEU A  69      46.528 121.305 283.876  1.00 27.76      A    C  
ANISOU  498  C   LEU A  69     3282   3709   3558    891   -341    550  A    C  
ATOM    499  O   LEU A  69      47.747 121.069 283.905  1.00 23.20      A    O  
ANISOU  499  O   LEU A  69     2652   3124   3041    957   -446    488  A    O  
ATOM    500  CB  LEU A  69      46.230 123.585 282.882  1.00 24.70      A    C  
ANISOU  500  CB  LEU A  69     2784   3376   3226    711   -365    313  A    C  
ATOM    501  CG  LEU A  69      46.462 124.405 281.609  1.00 31.08      A    C  
ANISOU  501  CG  LEU A  69     3478   4146   4187    576   -340    222  A    C  
ATOM    502  CD1 LEU A  69      47.229 125.692 281.912  1.00 29.22      A    C  
ANISOU  502  CD1 LEU A  69     3137   3939   4025    591   -470     95  A    C  
ATOM    503  CD2 LEU A  69      47.172 123.582 280.537  1.00 31.51      A    C  
ANISOU  503  CD2 LEU A  69     3465   4141   4364    544   -292    226  A    C  
ATOM    504  N   ALA A  70      45.703 120.895 284.838  1.00 22.32      A    N  
ANISOU  504  N   ALA A  70     2688   3067   2726    976   -278    716  A    N  
ATOM    505  CA  ALA A  70      46.218 120.306 286.073  1.00 32.96      A    C  
ANISOU  505  CA  ALA A  70     4095   4498   3932   1178   -344    840  A    C  
ATOM    506  C   ALA A  70      47.068 119.049 285.877  1.00 39.27      A    C  
ANISOU  506  C   ALA A  70     4869   5169   4881   1223   -368    922  A    C  
ATOM    507  O   ALA A  70      48.075 118.872 286.564  1.00 37.33      A    O  
ANISOU  507  O   ALA A  70     4629   4992   4564   1379   -499    914  A    O  
ATOM    508  CB  ALA A  70      45.074 120.033 287.058  1.00 33.88      A    C  
ANISOU  508  CB  ALA A  70     4304   4703   3865   1269   -223   1062  A    C  
ATOM    509  N   GLU A  71      46.681 118.185 284.943  1.00 41.99      A    N  
ANISOU  509  N   GLU A  71     5177   5329   5449   1101   -264    975  A    N  
ATOM    510  CA  GLU A  71      47.442 116.956 284.727  1.00 47.14      A    C  
ANISOU  510  CA  GLU A  71     5789   5839   6284   1148   -297   1032  A    C  
ATOM    511  C   GLU A  71      48.762 117.190 283.993  1.00 40.81      A    C  
ANISOU  511  C   GLU A  71     4894   5034   5577   1131   -420    809  A    C  
ATOM    512  O   GLU A  71      49.601 116.293 283.914  1.00 38.61      A    O  
ANISOU  512  O   GLU A  71     4574   4667   5430   1198   -481    818  A    O  
ATOM    513  CB  GLU A  71      46.613 115.882 284.023  1.00 58.08      A    C  
ANISOU  513  CB  GLU A  71     7137   7011   7921   1051   -173   1126  A    C  
ATOM    514  CG  GLU A  71      46.218 116.208 282.604  1.00 66.87      A    C  
ANISOU  514  CG  GLU A  71     8174   8067   9168    886   -135    921  A    C  
ATOM    515  CD  GLU A  71      45.384 115.102 281.989  1.00 77.81      A    C  
ANISOU  515  CD  GLU A  71     9502   9237  10827    821    -51    968  A    C  
ATOM    516  OE1 GLU A  71      45.313 114.006 282.591  1.00 81.80      A    O  
ANISOU  516  OE1 GLU A  71    10003   9595  11483    891    -28   1167  A    O  
ATOM    517  OE2 GLU A  71      44.808 115.325 280.902  1.00 81.06      A    O1-
ANISOU  517  OE2 GLU A  71     9857   9619  11323    712    -17    807  A    O1-
ATOM    518  N   HIS A  72      48.947 118.394 283.461  1.00 33.37      A    N  
ANISOU  518  N   HIS A  72     3902   4182   4594   1047   -449    626  A    N  
ATOM    519  CA  HIS A  72      50.174 118.708 282.741  1.00 28.74      A    C  
ANISOU  519  CA  HIS A  72     3199   3601   4119   1026   -533    446  A    C  
ATOM    520  C   HIS A  72      51.121 119.535 283.603  1.00 26.48      A    C  
ANISOU  520  C   HIS A  72     2888   3430   3744   1133   -690    356  A    C  
ATOM    521  O   HIS A  72      52.141 120.025 283.117  1.00 31.11      A    O  
ANISOU  521  O   HIS A  72     3351   4022   4447   1111   -761    208  A    O  
ATOM    522  CB  HIS A  72      49.858 119.443 281.437  1.00 31.54      A    C  
ANISOU  522  CB  HIS A  72     3476   3964   4545    870   -448    330  A    C  
ATOM    523  CG  HIS A  72      48.937 118.691 280.530  1.00 34.02      A    C  
ANISOU  523  CG  HIS A  72     3795   4186   4945    791   -328    357  A    C  
ATOM    524  CD2 HIS A  72      48.028 119.125 279.621  1.00 31.16      A    C  
ANISOU  524  CD2 HIS A  72     3420   3837   4583    681   -232    315  A    C  
ATOM    525  ND1 HIS A  72      48.862 117.312 280.516  1.00 32.05      A    N  
ANISOU  525  ND1 HIS A  72     3551   3803   4822    837   -317    420  A    N  
ATOM    526  CE1 HIS A  72      47.962 116.932 279.630  1.00 32.79      A    C  
ANISOU  526  CE1 HIS A  72     3622   3826   5012    759   -231    385  A    C  
ATOM    527  NE2 HIS A  72      47.441 118.009 279.071  1.00 35.31      A    N  
ANISOU  527  NE2 HIS A  72     3937   4247   5233    670   -179    320  A    N  
ATOM    528  N   GLY A  73      50.768 119.714 284.874  1.00 30.02      A    N  
ANISOU  528  N   GLY A  73     3435   3978   3994   1262   -746    435  A    N  
ATOM    529  CA  GLY A  73      51.652 120.376 285.821  1.00 29.99      A    C  
ANISOU  529  CA  GLY A  73     3404   4096   3896   1415   -935    315  A    C  
ATOM    530  C   GLY A  73      51.287 121.798 286.223  1.00 32.34      A    C  
ANISOU  530  C   GLY A  73     3684   4507   4097   1411   -999    176  A    C  
ATOM    531  O   GLY A  73      52.045 122.451 286.941  1.00 35.80      A    O  
ANISOU  531  O   GLY A  73     4063   5033   4504   1541  -1188     13  A    O  
ATOM    532  N   ILE A  74      50.137 122.287 285.770  1.00 24.71      A    N  
ANISOU  532  N   ILE A  74     2750   3530   3108   1274   -864    213  A    N  
ATOM    533  CA  ILE A  74      49.662 123.609 286.180  1.00 29.92      A    C  
ANISOU  533  CA  ILE A  74     3393   4284   3692   1276   -925     83  A    C  
ATOM    534  C   ILE A  74      48.348 123.511 286.944  1.00 24.93      A    C  
ANISOU  534  C   ILE A  74     2899   3762   2812   1341   -832    218  A    C  
ATOM    535  O   ILE A  74      47.291 123.314 286.345  1.00 26.15      A    O  
ANISOU  535  O   ILE A  74     3096   3851   2987   1204   -659    333  A    O  
ATOM    536  CB  ILE A  74      49.443 124.520 284.963  1.00 30.66      A    C  
ANISOU  536  CB  ILE A  74     3380   4279   3989   1063   -854      1  A    C  
ATOM    537  CG1 ILE A  74      50.615 124.391 283.984  1.00 38.32      A    C  
ANISOU  537  CG1 ILE A  74     4209   5147   5203    985   -866    -55  A    C  
ATOM    538  CG2 ILE A  74      49.207 125.965 285.406  1.00 28.51      A    C  
ANISOU  538  CG2 ILE A  74     3046   4064   3721   1075   -963   -167  A    C  
ATOM    539  CD1 ILE A  74      51.393 125.666 283.781  1.00 44.87      A    C  
ANISOU  539  CD1 ILE A  74     4859   5946   6245    945   -979   -226  A    C  
ATOM    540  N   VAL A  75      48.406 123.687 288.261  1.00 27.60      A    N  
ANISOU  540  N   VAL A  75     3290   4284   2912   1566   -950    190  A    N  
ATOM    541  CA  VAL A  75      47.237 123.446 289.102  1.00 29.49      A    C  
ANISOU  541  CA  VAL A  75     3655   4670   2881   1672   -838    361  A    C  
ATOM    542  C   VAL A  75      46.643 124.746 289.637  1.00 34.43      A    C  
ANISOU  542  C   VAL A  75     4263   5446   3373   1728   -914    174  A    C  
ATOM    543  O   VAL A  75      47.189 125.361 290.551  1.00 37.09      A    O  
ANISOU  543  O   VAL A  75     4577   5907   3610   1870  -1068    -28  A    O  
ATOM    544  CB  VAL A  75      47.570 122.508 290.287  1.00 33.31      A    C  
ANISOU  544  CB  VAL A  75     4230   5281   3145   1893   -847    520  A    C  
ATOM    545  CG1 VAL A  75      46.337 122.269 291.144  1.00 33.71      A    C  
ANISOU  545  CG1 VAL A  75     4384   5477   2948   1971   -673    720  A    C  
ATOM    546  CG2 VAL A  75      48.133 121.182 289.783  1.00 32.45      A    C  
ANISOU  546  CG2 VAL A  75     4126   5007   3197   1861   -795    711  A    C  
ATOM    547  N   PHE A  76      45.527 125.165 289.053  1.00 36.80      A    N  
ANISOU  547  N   PHE A  76     4570   5684   3727   1557   -769    205  A    N  
ATOM    548  CA  PHE A  76      44.750 126.266 289.599  1.00 40.31      A    C  
ANISOU  548  CA  PHE A  76     5008   6270   4037   1616   -812     59  A    C  
ATOM    549  C   PHE A  76      43.837 125.634 290.642  1.00 48.94      A    C  
ANISOU  549  C   PHE A  76     6224   7572   4800   1798   -680    278  A    C  
ATOM    550  O   PHE A  76      43.523 124.448 290.553  1.00 52.22      A    O  
ANISOU  550  O   PHE A  76     6710   7928   5204   1773   -503    571  A    O  
ATOM    551  CB  PHE A  76      43.896 126.913 288.504  1.00 38.25      A    C  
ANISOU  551  CB  PHE A  76     4703   5854   3977   1363   -700     29  A    C  
ATOM    552  CG  PHE A  76      44.681 127.736 287.507  1.00 36.40      A    C  
ANISOU  552  CG  PHE A  76     4329   5447   4055   1203   -806   -152  A    C  
ATOM    553  CD1 PHE A  76      45.077 129.034 287.809  1.00 39.72      A    C  
ANISOU  553  CD1 PHE A  76     4630   5887   4574   1251  -1003   -418  A    C  
ATOM    554  CD2 PHE A  76      45.002 127.216 286.258  1.00 34.00      A    C  
ANISOU  554  CD2 PHE A  76     3991   4963   3963   1018   -703    -51  A    C  
ATOM    555  CE1 PHE A  76      45.791 129.794 286.889  1.00 40.38      A    C  
ANISOU  555  CE1 PHE A  76     4558   5792   4994   1100  -1073   -531  A    C  
ATOM    556  CE2 PHE A  76      45.713 127.970 285.334  1.00 36.75      A    C  
ANISOU  556  CE2 PHE A  76     4199   5183   4581    889   -763   -166  A    C  
ATOM    557  CZ  PHE A  76      46.108 129.259 285.649  1.00 38.97      A    C  
ANISOU  557  CZ  PHE A  76     4356   5462   4989    921   -936   -381  A    C  
ATOM    558  N   GLY A  77      43.401 126.401 291.632  1.00 56.60      A    N  
ANISOU  558  N   GLY A  77     7200   8739   5565   1943   -723    132  A    N  
ATOM    559  CA  GLY A  77      42.424 125.872 292.566  1.00 62.54      A    C  
ANISOU  559  CA  GLY A  77     8037   9662   6064   2065   -526    342  A    C  
ATOM    560  C   GLY A  77      41.089 125.706 291.861  1.00 58.15      A    C  
ANISOU  560  C   GLY A  77     7506   9030   5557   1903   -320    540  A    C  
ATOM    561  O   GLY A  77      41.006 125.784 290.630  1.00 48.26      A    O  
ANISOU  561  O   GLY A  77     6217   7551   4570   1667   -298    524  A    O  
ATOM    562  N   GLU A  78      40.034 125.455 292.624  1.00 57.59      A    N  
ANISOU  562  N   GLU A  78     7467   9091   5324   1979   -131    699  A    N  
ATOM    563  CA  GLU A  78      38.704 125.595 292.067  1.00 56.81      A    C  
ANISOU  563  CA  GLU A  78     7366   8932   5287   1829     43    803  A    C  
ATOM    564  C   GLU A  78      38.453 127.094 292.084  1.00 45.56      A    C  
ANISOU  564  C   GLU A  78     5889   7610   3811   1850   -116    466  A    C  
ATOM    565  O   GLU A  78      38.768 127.766 293.064  1.00 46.08      A    O  
ANISOU  565  O   GLU A  78     5921   7853   3735   2042   -248    250  A    O  
ATOM    566  CB  GLU A  78      37.671 124.825 292.887  1.00 70.42      A    C  
ANISOU  566  CB  GLU A  78     9097  10734   6924   1895    291   1079  A    C  
ATOM    567  CG  GLU A  78      36.463 124.381 292.080  1.00 78.20      A    C  
ANISOU  567  CG  GLU A  78    10066  11534   8114   1680    508   1274  A    C  
ATOM    568  CD  GLU A  78      35.161 124.901 292.647  1.00 88.79      A    C  
ANISOU  568  CD  GLU A  78    11368  13008   9359   1719    625   1269  A    C  
ATOM    569  OE1 GLU A  78      35.146 125.338 293.820  1.00 94.76      A    O  
ANISOU  569  OE1 GLU A  78    12113  14016   9875   1943    579   1191  A    O  
ATOM    570  OE2 GLU A  78      34.153 124.888 291.910  1.00 89.48      A    O1-
ANISOU  570  OE2 GLU A  78    11426  12948   9624   1534    755   1326  A    O1-
ATOM    571  N   PRO A  79      37.884 127.631 291.004  1.00 43.37      A    N  
ANISOU  571  N   PRO A  79     5570   7148   3760   1615    -91    383  A    N  
ATOM    572  CA  PRO A  79      37.687 129.082 290.932  1.00 44.66      A    C  
ANISOU  572  CA  PRO A  79     5657   7339   3972   1600   -251     54  A    C  
ATOM    573  C   PRO A  79      36.658 129.606 291.932  1.00 46.47      A    C  
ANISOU  573  C   PRO A  79     5893   7842   3923   1788   -203      0  A    C  
ATOM    574  O   PRO A  79      35.725 128.896 292.304  1.00 47.31      A    O  
ANISOU  574  O   PRO A  79     6035   8002   3938   1801     33    256  A    O  
ATOM    575  CB  PRO A  79      37.199 129.291 289.496  1.00 38.35      A    C  
ANISOU  575  CB  PRO A  79     4815   6250   3506   1288   -175     60  A    C  
ATOM    576  CG  PRO A  79      36.562 128.005 289.123  1.00 39.71      A    C  
ANISOU  576  CG  PRO A  79     5045   6327   3716   1187     69    377  A    C  
ATOM    577  CD  PRO A  79      37.372 126.940 289.808  1.00 41.06      A    C  
ANISOU  577  CD  PRO A  79     5275   6581   3746   1345     82    560  A    C  
ATOM    578  N   LYS A  80      36.852 130.837 292.389  1.00 45.96      A    N  
ANISOU  578  N   LYS A  80     5745   7857   3861   1892   -413   -344  A    N  
ATOM    579  CA  LYS A  80      35.835 131.498 293.190  1.00 50.23      A    C  
ANISOU  579  CA  LYS A  80     6241   8562   4282   2012   -370   -446  A    C  
ATOM    580  C   LYS A  80      34.993 132.326 292.225  1.00 47.96      A    C  
ANISOU  580  C   LYS A  80     5913   8146   4165   1815   -373   -573  A    C  
ATOM    581  O   LYS A  80      35.510 133.206 291.534  1.00 46.79      A    O  
ANISOU  581  O   LYS A  80     5684   7818   4277   1697   -567   -808  A    O  
ATOM    582  CB  LYS A  80      36.481 132.354 294.284  1.00 59.15      A    C  
ANISOU  582  CB  LYS A  80     7280   9836   5357   2259   -588   -759  A    C  
ATOM    583  CG  LYS A  80      35.503 132.976 295.277  1.00 67.04      A    C  
ANISOU  583  CG  LYS A  80     8215  11054   6204   2444   -564   -859  A    C  
ATOM    584  CD  LYS A  80      36.241 133.680 296.415  1.00 74.74      A    C  
ANISOU  584  CD  LYS A  80     9093  12190   7113   2736   -773  -1163  A    C  
ATOM    585  CE  LYS A  80      35.316 133.971 297.594  1.00 78.54      A    C  
ANISOU  585  CE  LYS A  80     9516  12966   7358   2986   -725  -1185  A    C  
ATOM    586  NZ  LYS A  80      34.258 134.967 297.265  1.00 77.72      A    N1+
ANISOU  586  NZ  LYS A  80     9332  12821   7377   2891   -752  -1340  A    N1+
ATOM    587  N   THR A  81      33.703 132.015 292.147  1.00 45.71      A    N  
ANISOU  587  N   THR A  81     5655   7889   3822   1748   -141   -389  A    N  
ATOM    588  CA  THR A  81      32.854 132.596 291.114  1.00 39.41      A    C  
ANISOU  588  CA  THR A  81     4811   6888   3275   1512    -97   -451  A    C  
ATOM    589  C   THR A  81      31.791 133.544 291.678  1.00 40.35      A    C  
ANISOU  589  C   THR A  81     4868   7171   3290   1619   -110   -644  A    C  
ATOM    590  O   THR A  81      31.142 133.246 292.685  1.00 39.82      A    O  
ANISOU  590  O   THR A  81     4801   7283   3045   1762      3   -521  A    O  
ATOM    591  CB  THR A  81      32.169 131.481 290.298  1.00 42.54      A    C  
ANISOU  591  CB  THR A  81     5255   7104   3802   1299    168   -118  A    C  
ATOM    592  CG2 THR A  81      31.420 132.059 289.105  1.00 42.44      A    C  
ANISOU  592  CG2 THR A  81     5187   6852   4085   1051    181   -193  A    C  
ATOM    593  OG1 THR A  81      33.159 130.555 289.828  1.00 45.27      A    O  
ANISOU  593  OG1 THR A  81     5648   7308   4245   1223    171     42  A    O  
ATOM    594  N   ASP A  82      31.636 134.691 291.021  1.00 38.91      A    N  
ANISOU  594  N   ASP A  82     4597   6818   3367   1494   -264   -897  A    N  
ATOM    595  CA  ASP A  82      30.627 135.685 291.377  1.00 34.30      A    C  
ANISOU  595  CA  ASP A  82     3934   6324   2774   1559   -304  -1106  A    C  
ATOM    596  C   ASP A  82      29.732 135.909 290.159  1.00 33.91      A    C  
ANISOU  596  C   ASP A  82     3860   6017   3006   1287   -205  -1044  A    C  
ATOM    597  O   ASP A  82      30.122 136.607 289.218  1.00 33.98      A    O  
ANISOU  597  O   ASP A  82     3809   5771   3330   1119   -348  -1151  A    O  
ATOM    598  CB  ASP A  82      31.308 136.989 291.808  1.00 33.80      A    C  
ANISOU  598  CB  ASP A  82     3740   6233   2869   1670   -619  -1464  A    C  
ATOM    599  CG  ASP A  82      30.320 138.056 292.271  1.00 39.84      A    C  
ANISOU  599  CG  ASP A  82     4391   7057   3688   1741   -684  -1661  A    C  
ATOM    600  OD1 ASP A  82      29.108 137.935 291.992  1.00 42.64      A    O  
ANISOU  600  OD1 ASP A  82     4771   7423   4007   1650   -513  -1557  A    O  
ATOM    601  OD2 ASP A  82      30.765 139.025 292.924  1.00 43.71      A    O1-
ANISOU  601  OD2 ASP A  82     4750   7572   4287   1899   -903  -1927  A    O1-
ATOM    602  N   ILE A  83      28.534 135.327 290.193  1.00 28.30      A    N  
ANISOU  602  N   ILE A  83     3523   4206   3026   1010    214  -1116  A    N  
ATOM    603  CA  ILE A  83      27.622 135.329 289.049  1.00 34.03      A    C  
ANISOU  603  CA  ILE A  83     4082   4990   3857    872    280   -985  A    C  
ATOM    604  C   ILE A  83      27.176 136.743 288.664  1.00 31.12      A    C  
ANISOU  604  C   ILE A  83     3734   4577   3513    986    240  -1033  A    C  
ATOM    605  O   ILE A  83      26.999 137.053 287.477  1.00 26.29      A    O  
ANISOU  605  O   ILE A  83     3026   3926   3039    823    209  -1002  A    O  
ATOM    606  CB  ILE A  83      26.370 134.468 289.354  1.00 39.51      A    C  
ANISOU  606  CB  ILE A  83     4623   5902   4487    875    430   -735  A    C  
ATOM    607  CG1 ILE A  83      26.789 133.053 289.748  1.00 41.46      A    C  
ANISOU  607  CG1 ILE A  83     4913   6150   4691    752    442   -688  A    C  
ATOM    608  CG2 ILE A  83      25.436 134.416 288.158  1.00 42.83      A    C  
ANISOU  608  CG2 ILE A  83     4870   6380   5022    660    424   -543  A    C  
ATOM    609  CD1 ILE A  83      27.610 132.347 288.686  1.00 33.94      A    C  
ANISOU  609  CD1 ILE A  83     4061   5017   3818    507    356   -740  A    C  
ATOM    610  N   ASP A  84      27.019 137.599 289.671  1.00 29.81      A    N  
ANISOU  610  N   ASP A  84     3760   4389   3178   1294    234  -1114  A    N  
ATOM    611  CA  ASP A  84      26.641 138.990 289.444  1.00 36.69      A    C  
ANISOU  611  CA  ASP A  84     4773   5164   4004   1472    185  -1176  A    C  
ATOM    612  C   ASP A  84      27.680 139.709 288.582  1.00 33.59      A    C  
ANISOU  612  C   ASP A  84     4450   4530   3780   1230    -58  -1320  A    C  
ATOM    613  O   ASP A  84      27.332 140.514 287.708  1.00 35.59      A    O  
ANISOU  613  O   ASP A  84     4673   4733   4118   1199    -82  -1314  A    O  
ATOM    614  CB  ASP A  84      26.457 139.724 290.778  1.00 47.52      A    C  
ANISOU  614  CB  ASP A  84     6477   6444   5133   1781    162  -1171  A    C  
ATOM    615  CG  ASP A  84      25.297 139.177 291.596  1.00 56.86      A    C  
ANISOU  615  CG  ASP A  84     7549   7890   6166   2030    417   -920  A    C  
ATOM    616  OD1 ASP A  84      24.266 138.808 290.994  1.00 55.52      A    O  
ANISOU  616  OD1 ASP A  84     7057   7978   6058   2037    608   -695  A    O  
ATOM    617  OD2 ASP A  84      25.411 139.132 292.842  1.00 65.38      A    O1-
ANISOU  617  OD2 ASP A  84     8845   8931   7064   2214    405   -904  A    O1-
ATOM    618  N   LYS A  85      28.954 139.406 288.818  1.00 33.61      A    N  
ANISOU  618  N   LYS A  85     4510   4420   3840   1060   -233  -1397  A    N  
ATOM    619  CA  LYS A  85      30.031 140.002 288.029  1.00 33.21      A    C  
ANISOU  619  CA  LYS A  85     4441   4209   3970    815   -463  -1421  A    C  
ATOM    620  C   LYS A  85      30.096 139.483 286.590  1.00 27.92      A    C  
ANISOU  620  C   LYS A  85     3484   3622   3504    600   -354  -1309  A    C  
ATOM    621  O   LYS A  85      30.324 140.255 285.657  1.00 24.05      A    O  
ANISOU  621  O   LYS A  85     2947   3045   3145    487   -449  -1292  A    O  
ATOM    622  CB  LYS A  85      31.393 139.875 288.732  1.00 26.69      A    C  
ANISOU  622  CB  LYS A  85     3701   3292   3146    702   -699  -1429  A    C  
ATOM    623  CG  LYS A  85      31.626 140.923 289.812  1.00 37.99      A    C  
ANISOU  623  CG  LYS A  85     5550   4489   4394    816   -994  -1552  A    C  
ATOM    624  CD  LYS A  85      33.108 141.049 290.142  1.00 43.52      A    C  
ANISOU  624  CD  LYS A  85     6275   5081   5178    557  -1352  -1472  A    C  
ATOM    625  CE  LYS A  85      33.362 142.189 291.114  1.00 55.86      A    C  
ANISOU  625  CE  LYS A  85     8324   6340   6560    584  -1713  -1526  A    C  
ATOM    626  NZ  LYS A  85      33.173 141.794 292.539  1.00 59.73      A    N1+
ANISOU  626  NZ  LYS A  85     9075   6819   6800    818  -1656  -1574  A    N1+
ATOM    627  N   ILE A  86      29.902 138.180 286.415  1.00 27.57      A    N  
ANISOU  627  N   ILE A  86     3310   3713   3453    557   -174  -1225  A    N  
ATOM    628  CA  ILE A  86      29.823 137.603 285.078  1.00 25.61      A    C  
ANISOU  628  CA  ILE A  86     2932   3487   3310    403    -84  -1128  A    C  
ATOM    629  C   ILE A  86      28.693 138.277 284.295  1.00 25.84      A    C  
ANISOU  629  C   ILE A  86     2905   3528   3384    388    -49  -1106  A    C  
ATOM    630  O   ILE A  86      28.887 138.726 283.151  1.00 28.62      A    O  
ANISOU  630  O   ILE A  86     3207   3815   3853    284    -88  -1084  A    O  
ATOM    631  CB  ILE A  86      29.584 136.076 285.135  1.00 22.70      A    C  
ANISOU  631  CB  ILE A  86     2576   3193   2855    366     52  -1046  A    C  
ATOM    632  CG1 ILE A  86      30.669 135.394 285.973  1.00 26.53      A    C  
ANISOU  632  CG1 ILE A  86     3113   3689   3278    425     45  -1055  A    C  
ATOM    633  CG2 ILE A  86      29.532 135.479 283.727  1.00 18.21      A    C  
ANISOU  633  CG2 ILE A  86     2033   2565   2322    231     93   -959  A    C  
ATOM    634  CD1 ILE A  86      30.518 133.879 286.051  1.00 30.54      A    C  
ANISOU  634  CD1 ILE A  86     3708   4225   3673    407    163   -980  A    C  
ATOM    635  N   ARG A  87      27.524 138.361 284.929  1.00 24.09      A    N  
ANISOU  635  N   ARG A  87     2672   3421   3062    523     38  -1067  A    N  
ATOM    636  CA  ARG A  87      26.358 138.996 284.321  1.00 28.99      A    C  
ANISOU  636  CA  ARG A  87     3192   4116   3708    554     93   -974  A    C  
ATOM    637  C   ARG A  87      26.686 140.450 283.947  1.00 28.10      A    C  
ANISOU  637  C   ARG A  87     3174   3851   3651    621    -21  -1095  A    C  
ATOM    638  O   ARG A  87      26.391 140.907 282.832  1.00 29.25      A    O  
ANISOU  638  O   ARG A  87     3234   3974   3907    519    -33  -1054  A    O  
ATOM    639  CB  ARG A  87      25.161 138.933 285.282  1.00 30.41      A    C  
ANISOU  639  CB  ARG A  87     3309   4506   3740    786    239   -829  A    C  
ATOM    640  CG  ARG A  87      23.824 139.293 284.654  1.00 34.04      A    C  
ANISOU  640  CG  ARG A  87     3562   5145   4227    810    330   -598  A    C  
ATOM    641  CD  ARG A  87      22.712 139.434 285.696  1.00 35.80      A    C  
ANISOU  641  CD  ARG A  87     3688   5638   4277   1157    522   -372  A    C  
ATOM    642  NE  ARG A  87      22.628 138.277 286.585  1.00 40.38      A    N  
ANISOU  642  NE  ARG A  87     4202   6358   4781   1140    588   -244  A    N  
ATOM    643  CZ  ARG A  87      22.932 138.296 287.882  1.00 41.17      A    C  
ANISOU  643  CZ  ARG A  87     4479   6465   4700   1443    665   -336  A    C  
ATOM    644  NH1 ARG A  87      23.324 139.423 288.463  1.00 41.87      A    N1+
ANISOU  644  NH1 ARG A  87     4883   6391   4636   1782    648   -559  A    N1+
ATOM    645  NH2 ARG A  87      22.827 137.188 288.603  1.00 38.21      A    N  
ANISOU  645  NH2 ARG A  87     4017   6229   4273   1401    728   -196  A    N  
ATOM    646  N   THR A  88      27.334 141.158 284.867  1.00 27.89      A    N  
ANISOU  646  N   THR A  88     3369   3690   3538    766   -144  -1234  A    N  
ATOM    647  CA  THR A  88      27.722 142.545 284.620  1.00 31.08      A    C  
ANISOU  647  CA  THR A  88     3953   3885   3971    788   -333  -1335  A    C  
ATOM    648  C   THR A  88      28.639 142.656 283.394  1.00 28.90      A    C  
ANISOU  648  C   THR A  88     3529   3530   3924    496   -451  -1298  A    C  
ATOM    649  O   THR A  88      28.473 143.554 282.562  1.00 26.92      A    O  
ANISOU  649  O   THR A  88     3273   3196   3759    454   -510  -1295  A    O  
ATOM    650  CB  THR A  88      28.410 143.166 285.858  1.00 31.74      A    C  
ANISOU  650  CB  THR A  88     4396   3768   3895    917   -552  -1470  A    C  
ATOM    651  CG2 THR A  88      28.931 144.566 285.548  1.00 29.85      A    C  
ANISOU  651  CG2 THR A  88     4407   3245   3689    847   -848  -1543  A    C  
ATOM    652  OG1 THR A  88      27.469 143.251 286.937  1.00 35.00      A    O  
ANISOU  652  OG1 THR A  88     5019   4243   4038   1299   -408  -1492  A    O  
ATOM    653  N   TRP A  89      29.579 141.725 283.262  1.00 27.74      A    N  
ANISOU  653  N   TRP A  89     3259   3429   3853    341   -452  -1237  A    N  
ATOM    654  CA  TRP A  89      30.469 141.718 282.100  1.00 27.55      A    C  
ANISOU  654  CA  TRP A  89     3076   3386   4004    158   -495  -1127  A    C  
ATOM    655  C   TRP A  89      29.723 141.462 280.781  1.00 21.28      A    C  
ANISOU  655  C   TRP A  89     2175   2647   3265    115   -338  -1070  A    C  
ATOM    656  O   TRP A  89      29.936 142.166 279.778  1.00 27.10      A    O  
ANISOU  656  O   TRP A  89     2849   3327   4121     40   -389  -1021  A    O  
ATOM    657  CB  TRP A  89      31.586 140.692 282.289  1.00 26.09      A    C  
ANISOU  657  CB  TRP A  89     2803   3279   3831    111   -467  -1018  A    C  
ATOM    658  CG  TRP A  89      32.407 140.502 281.053  1.00 31.08      A    C  
ANISOU  658  CG  TRP A  89     3272   3953   4583     40   -415   -834  A    C  
ATOM    659  CD1 TRP A  89      33.241 141.419 280.466  1.00 30.91      A    C  
ANISOU  659  CD1 TRP A  89     3120   3904   4720    -64   -565   -683  A    C  
ATOM    660  CD2 TRP A  89      32.472 139.323 280.244  1.00 28.89      A    C  
ANISOU  660  CD2 TRP A  89     2990   3745   4241    105   -197   -743  A    C  
ATOM    661  CE2 TRP A  89      33.366 139.592 279.187  1.00 28.84      A    C  
ANISOU  661  CE2 TRP A  89     2851   3774   4334    112   -173   -537  A    C  
ATOM    662  CE3 TRP A  89      31.862 138.069 280.311  1.00 30.73      A    C  
ANISOU  662  CE3 TRP A  89     3368   3990   4317    163    -45   -790  A    C  
ATOM    663  NE1 TRP A  89      33.818 140.875 279.341  1.00 33.86      A    N  
ANISOU  663  NE1 TRP A  89     3357   4377   5132    -16   -398   -480  A    N  
ATOM    664  CZ2 TRP A  89      33.657 138.650 278.206  1.00 35.23      A    C  
ANISOU  664  CZ2 TRP A  89     3729   4617   5040    256     36   -406  A    C  
ATOM    665  CZ3 TRP A  89      32.154 137.138 279.336  1.00 34.26      A    C  
ANISOU  665  CZ3 TRP A  89     3931   4419   4668    240     99   -682  A    C  
ATOM    666  CH2 TRP A  89      33.045 137.429 278.300  1.00 35.65      A    C  
ANISOU  666  CH2 TRP A  89     4031   4617   4897    326    157   -505  A    C  
ATOM    667  N   LYS A  90      28.850 140.457 280.792  1.00 20.93      A    N  
ANISOU  667  N   LYS A  90     2124   2701   3126    135   -186  -1049  A    N  
ATOM    668  CA  LYS A  90      27.998 140.158 279.633  1.00 25.05      A    C  
ANISOU  668  CA  LYS A  90     2602   3248   3667     46   -112   -972  A    C  
ATOM    669  C   LYS A  90      27.257 141.418 279.172  1.00 19.58      A    C  
ANISOU  669  C   LYS A  90     1855   2542   3044     74   -149   -984  A    C  
ATOM    670  O   LYS A  90      27.245 141.798 277.968  1.00 20.58      A    O  
ANISOU  670  O   LYS A  90     1942   2618   3259    -11   -166   -945  A    O  
ATOM    671  CB  LYS A  90      26.968 139.099 280.033  1.00 26.25      A    C  
ANISOU  671  CB  LYS A  90     2759   3509   3707     14    -38   -892  A    C  
ATOM    672  CG  LYS A  90      26.118 138.593 278.888  1.00 24.52      A    C  
ANISOU  672  CG  LYS A  90     2545   3286   3486   -161    -53   -761  A    C  
ATOM    673  CD  LYS A  90      24.743 138.123 279.362  1.00 28.86      A    C  
ANISOU  673  CD  LYS A  90     2983   4005   3980   -231    -47   -579  A    C  
ATOM    674  CE  LYS A  90      23.858 139.291 279.783  1.00 27.79      A    C  
ANISOU  674  CE  LYS A  90     2649   4035   3876    -57     18   -519  A    C  
ATOM    675  NZ  LYS A  90      22.428 138.886 279.923  1.00 28.86      A    N1+
ANISOU  675  NZ  LYS A  90     2573   4410   3982   -132     37   -202  A    N1+
ATOM    676  N   GLU A  91      26.637 142.060 280.158  1.00 18.88      A    N  
ANISOU  676  N   GLU A  91     1801   2494   2877    244   -145  -1030  A    N  
ATOM    677  CA  GLU A  91      25.923 143.303 279.925  1.00 31.75      A    C  
ANISOU  677  CA  GLU A  91     3447   4105   4512    367   -156  -1037  A    C  
ATOM    678  C   GLU A  91      26.853 144.372 279.366  1.00 31.10      A    C  
ANISOU  678  C   GLU A  91     3448   3821   4545    297   -323  -1120  A    C  
ATOM    679  O   GLU A  91      26.429 145.181 278.553  1.00 28.68      A    O  
ANISOU  679  O   GLU A  91     3117   3479   4302    296   -334  -1098  A    O  
ATOM    680  CB  GLU A  91      25.214 143.784 281.197  1.00 33.72      A    C  
ANISOU  680  CB  GLU A  91     3822   4414   4576    680    -93  -1055  A    C  
ATOM    681  CG  GLU A  91      24.033 142.902 281.593  1.00 37.49      A    C  
ANISOU  681  CG  GLU A  91     4113   5169   4964    761     96   -850  A    C  
ATOM    682  CD  GLU A  91      23.521 143.172 282.997  1.00 44.69      A    C  
ANISOU  682  CD  GLU A  91     5155   6175   5649   1147    211   -826  A    C  
ATOM    683  OE1 GLU A  91      24.113 144.012 283.712  1.00 47.99      A    O  
ANISOU  683  OE1 GLU A  91     5907   6383   5944   1351    111  -1021  A    O  
ATOM    684  OE2 GLU A  91      22.524 142.529 283.388  1.00 46.95      A    O1-
ANISOU  684  OE2 GLU A  91     5235   6742   5863   1246    381   -577  A    O1-
ATOM    685  N   LYS A  92      28.111 144.383 279.805  1.00 28.42      A    N  
ANISOU  685  N   LYS A  92     3185   3371   4243    219   -470  -1165  A    N  
ATOM    686  CA  LYS A  92      29.074 145.357 279.294  1.00 30.87      A    C  
ANISOU  686  CA  LYS A  92     3520   3519   4690     87   -678  -1143  A    C  
ATOM    687  C   LYS A  92      29.391 145.140 277.814  1.00 28.28      A    C  
ANISOU  687  C   LYS A  92     2980   3246   4518    -55   -603  -1012  A    C  
ATOM    688  O   LYS A  92      29.388 146.100 277.029  1.00 24.59      A    O  
ANISOU  688  O   LYS A  92     2497   2694   4151   -107   -682   -980  A    O  
ATOM    689  CB  LYS A  92      30.361 145.356 280.122  1.00 32.97      A    C  
ANISOU  689  CB  LYS A  92     3853   3701   4973    -12   -894  -1116  A    C  
ATOM    690  CG  LYS A  92      31.384 146.387 279.659  1.00 40.76      A    C  
ANISOU  690  CG  LYS A  92     4824   4540   6122   -217  -1179   -991  A    C  
ATOM    691  CD  LYS A  92      32.643 146.345 280.515  1.00 50.68      A    C  
ANISOU  691  CD  LYS A  92     6100   5747   7408   -373  -1450   -875  A    C  
ATOM    692  CE  LYS A  92      33.630 147.425 280.094  1.00 60.05      A    C  
ANISOU  692  CE  LYS A  92     7268   6843   8704   -597  -1693   -608  A    C  
ATOM    693  NZ  LYS A  92      34.911 147.344 280.858  1.00 64.90      A    N1+
ANISOU  693  NZ  LYS A  92     7848   7475   9334   -770  -1916   -380  A    N1+
ATOM    694  N   VAL A  93      29.662 143.894 277.417  1.00 24.75      A    N  
ANISOU  694  N   VAL A  93     2430   2916   4058    -82   -451   -931  A    N  
ATOM    695  CA  VAL A  93      29.874 143.647 275.980  1.00 26.58      A    C  
ANISOU  695  CA  VAL A  93     2570   3172   4358   -130   -357   -808  A    C  
ATOM    696  C   VAL A  93      28.634 144.044 275.151  1.00 25.82      A    C  
ANISOU  696  C   VAL A  93     2486   3064   4259   -139   -311   -847  A    C  
ATOM    697  O   VAL A  93      28.742 144.746 274.104  1.00 27.52      A    O  
ANISOU  697  O   VAL A  93     2649   3235   4573   -176   -333   -787  A    O  
ATOM    698  CB  VAL A  93      30.467 142.226 275.642  1.00 28.46      A    C  
ANISOU  698  CB  VAL A  93     2833   3480   4503    -82   -206   -705  A    C  
ATOM    699  CG1 VAL A  93      30.954 141.517 276.889  1.00 30.72      A    C  
ANISOU  699  CG1 VAL A  93     3143   3814   4713    -41   -210   -729  A    C  
ATOM    700  CG2 VAL A  93      29.494 141.375 274.859  1.00 19.19      A    C  
ANISOU  700  CG2 VAL A  93     1802   2286   3204    -89   -103   -724  A    C  
ATOM    701  N   ILE A  94      27.458 143.630 275.635  1.00 25.37      A    N  
ANISOU  701  N   ILE A  94     2463   3077   4099   -106   -253   -896  A    N  
ATOM    702  CA  ILE A  94      26.226 144.012 274.941  1.00 24.44      A    C  
ANISOU  702  CA  ILE A  94     2296   3004   3986   -123   -226   -854  A    C  
ATOM    703  C   ILE A  94      26.074 145.542 274.798  1.00 27.50      A    C  
ANISOU  703  C   ILE A  94     2676   3320   4451    -44   -293   -898  A    C  
ATOM    704  O   ILE A  94      25.885 146.050 273.696  1.00 26.55      A    O  
ANISOU  704  O   ILE A  94     2509   3168   4409    -97   -301   -851  A    O  
ATOM    705  CB  ILE A  94      24.981 143.433 275.638  1.00 24.95      A    C  
ANISOU  705  CB  ILE A  94     2313   3225   3943    -92   -164   -785  A    C  
ATOM    706  CG1 ILE A  94      24.973 141.905 275.544  1.00 25.43      A    C  
ANISOU  706  CG1 ILE A  94     2434   3307   3920   -237   -156   -710  A    C  
ATOM    707  CG2 ILE A  94      23.711 143.985 275.013  1.00 21.81      A    C  
ANISOU  707  CG2 ILE A  94     1791   2932   3565    -93   -146   -656  A    C  
ATOM    708  CD1 ILE A  94      23.847 141.264 276.334  1.00 25.73      A    C  
ANISOU  708  CD1 ILE A  94     2379   3524   3875   -257   -129   -567  A    C  
ATOM    709  N   ASN A  95      26.193 146.270 275.903  1.00 23.52      A    N  
ANISOU  709  N   ASN A  95     2287   2754   3897     95   -360   -991  A    N  
ATOM    710  CA  ASN A  95      26.032 147.730 275.909  1.00 24.39      A    C  
ANISOU  710  CA  ASN A  95     2528   2724   4014    204   -461  -1047  A    C  
ATOM    711  C   ASN A  95      27.051 148.412 275.004  1.00 28.07      A    C  
ANISOU  711  C   ASN A  95     2973   3040   4651     29   -613  -1014  A    C  
ATOM    712  O   ASN A  95      26.743 149.402 274.336  1.00 31.40      A    O  
ANISOU  712  O   ASN A  95     3425   3379   5125     44   -659  -1005  A    O  
ATOM    713  CB  ASN A  95      26.101 148.300 277.332  1.00 28.11      A    C  
ANISOU  713  CB  ASN A  95     3282   3074   4323    408   -558  -1163  A    C  
ATOM    714  CG  ASN A  95      24.914 147.876 278.199  1.00 38.27      A    C  
ANISOU  714  CG  ASN A  95     4577   4551   5414    685   -357  -1130  A    C  
ATOM    715  ND2 ASN A  95      25.070 147.990 279.520  1.00 35.29      A    N  
ANISOU  715  ND2 ASN A  95     4464   4094   4852    892   -400  -1223  A    N  
ATOM    716  OD1 ASN A  95      23.877 147.450 277.689  1.00 43.14      A    O  
ANISOU  716  OD1 ASN A  95     4961   5392   6038    708   -183   -979  A    O  
ATOM    717  N   GLN A  96      28.278 147.894 275.008  1.00 25.94      A    N  
ANISOU  717  N   GLN A  96     2629   2762   4466   -118   -683   -949  A    N  
ATOM    718  CA  GLN A  96      29.293 148.377 274.079  1.00 31.67      A    C  
ANISOU  718  CA  GLN A  96     3236   3433   5364   -273   -786   -800  A    C  
ATOM    719  C   GLN A  96      28.791 148.253 272.638  1.00 30.37      A    C  
ANISOU  719  C   GLN A  96     2949   3342   5247   -272   -626   -731  A    C  
ATOM    720  O   GLN A  96      28.804 149.234 271.867  1.00 31.83      A    O  
ANISOU  720  O   GLN A  96     3133   3459   5503   -301   -681   -663  A    O  
ATOM    721  CB  GLN A  96      30.602 147.605 274.270  1.00 34.91      A    C  
ANISOU  721  CB  GLN A  96     3516   3927   5820   -356   -798   -638  A    C  
ATOM    722  CG  GLN A  96      31.799 148.211 273.553  1.00 49.45      A    C  
ANISOU  722  CG  GLN A  96     5231   5786   7773   -468   -882   -350  A    C  
ATOM    723  CD  GLN A  96      33.105 147.542 273.948  1.00 63.39      A    C  
ANISOU  723  CD  GLN A  96     6829   7680   9575   -517   -905   -122  A    C  
ATOM    724  NE2 GLN A  96      34.151 147.781 273.166  1.00 72.64      A    N  
ANISOU  724  NE2 GLN A  96     7807   8962  10831   -560   -891    210  A    N  
ATOM    725  OE1 GLN A  96      33.171 146.819 274.947  1.00 63.48      A    O  
ANISOU  725  OE1 GLN A  96     6872   7715   9534   -494   -922   -215  A    O  
ATOM    726  N   LEU A  97      28.311 147.061 272.280  1.00 24.67      A    N  
ANISOU  726  N   LEU A  97     2201   2739   4431   -236   -446   -728  A    N  
ATOM    727  CA  LEU A  97      27.843 146.874 270.899  1.00 24.90      A    C  
ANISOU  727  CA  LEU A  97     2206   2794   4461   -251   -349   -660  A    C  
ATOM    728  C   LEU A  97      26.594 147.699 270.504  1.00 26.65      A    C  
ANISOU  728  C   LEU A  97     2423   3009   4695   -238   -364   -704  A    C  
ATOM    729  O   LEU A  97      26.539 148.271 269.400  1.00 25.43      A    O  
ANISOU  729  O   LEU A  97     2233   2819   4609   -262   -365   -642  A    O  
ATOM    730  CB  LEU A  97      27.664 145.384 270.592  1.00 25.30      A    C  
ANISOU  730  CB  LEU A  97     2355   2895   4363   -246   -236   -632  A    C  
ATOM    731  CG  LEU A  97      29.019 144.660 270.585  1.00 31.15      A    C  
ANISOU  731  CG  LEU A  97     3114   3651   5072   -171   -165   -526  A    C  
ATOM    732  CD1 LEU A  97      28.878 143.159 270.750  1.00 28.53      A    C  
ANISOU  732  CD1 LEU A  97     2984   3318   4539   -130    -83   -541  A    C  
ATOM    733  CD2 LEU A  97      29.789 144.992 269.310  1.00 31.39      A    C  
ANISOU  733  CD2 LEU A  97     3100   3677   5149    -96    -96   -347  A    C  
ATOM    734  N   THR A  98      25.610 147.780 271.400  1.00 21.32      A    N  
ANISOU  734  N   THR A  98     1769   2395   3938   -161   -353   -769  A    N  
ATOM    735  CA  THR A  98      24.400 148.562 271.145  1.00 24.49      A    C  
ANISOU  735  CA  THR A  98     2132   2849   4325    -76   -328   -740  A    C  
ATOM    736  C   THR A  98      24.747 150.046 271.020  1.00 27.50      A    C  
ANISOU  736  C   THR A  98     2600   3068   4781     -4   -425   -795  A    C  
ATOM    737  O   THR A  98      24.155 150.773 270.208  1.00 21.51      A    O  
ANISOU  737  O   THR A  98     1805   2307   4060     27   -411   -748  A    O  
ATOM    738  CB  THR A  98      23.318 148.366 272.236  1.00 24.88      A    C  
ANISOU  738  CB  THR A  98     2158   3054   4241     85   -248   -710  A    C  
ATOM    739  CG2 THR A  98      22.823 146.930 272.259  1.00 24.79      A    C  
ANISOU  739  CG2 THR A  98     2047   3202   4172    -54   -204   -592  A    C  
ATOM    740  OG1 THR A  98      23.864 148.690 273.519  1.00 32.55      A    O  
ANISOU  740  OG1 THR A  98     3295   3932   5140    233   -288   -837  A    O  
ATOM    741  N   GLY A  99      25.692 150.489 271.849  1.00 26.37      A    N  
ANISOU  741  N   GLY A  99     2599   2770   4648      1   -562   -874  A    N  
ATOM    742  CA  GLY A  99      26.214 151.840 271.756  1.00 28.94      A    C  
ANISOU  742  CA  GLY A  99     3078   2874   5043    -15   -753   -894  A    C  
ATOM    743  C   GLY A  99      26.804 152.055 270.376  1.00 28.94      A    C  
ANISOU  743  C   GLY A  99     2906   2867   5221   -186   -770   -762  A    C  
ATOM    744  O   GLY A  99      26.550 153.083 269.726  1.00 24.54      A    O  
ANISOU  744  O   GLY A  99     2393   2212   4720   -175   -827   -740  A    O  
ATOM    745  N   GLY A 100      27.585 151.074 269.918  1.00 23.43      A    N  
ANISOU  745  N   GLY A 100     2061   2291   4551   -277   -680   -637  A    N  
ATOM    746  CA  GLY A 100      28.117 151.135 268.567  1.00 19.98      A    C  
ANISOU  746  CA  GLY A 100     1530   1901   4159   -318   -604   -454  A    C  
ATOM    747  C   GLY A 100      27.056 151.296 267.487  1.00 23.59      A    C  
ANISOU  747  C   GLY A 100     1964   2387   4611   -278   -508   -476  A    C  
ATOM    748  O   GLY A 100      27.167 152.168 266.604  1.00 25.98      A    O  
ANISOU  748  O   GLY A 100     2245   2638   4989   -293   -537   -393  A    O  
ATOM    749  N   LEU A 101      26.002 150.484 267.571  1.00 21.61      A    N  
ANISOU  749  N   LEU A 101     1710   2228   4273   -250   -420   -552  A    N  
ATOM    750  CA  LEU A 101      24.938 150.537 266.569  1.00 19.35      A    C  
ANISOU  750  CA  LEU A 101     1393   1996   3964   -255   -371   -514  A    C  
ATOM    751  C   LEU A 101      24.206 151.879 266.587  1.00 24.42      A    C  
ANISOU  751  C   LEU A 101     2002   2598   4680   -178   -420   -547  A    C  
ATOM    752  O   LEU A 101      23.900 152.450 265.530  1.00 23.55      A    O  
ANISOU  752  O   LEU A 101     1852   2473   4622   -188   -415   -484  A    O  
ATOM    753  CB  LEU A 101      23.935 149.397 266.766  1.00 20.50      A    C  
ANISOU  753  CB  LEU A 101     1528   2265   3995   -304   -336   -500  A    C  
ATOM    754  CG  LEU A 101      24.403 147.973 266.443  1.00 22.90      A    C  
ANISOU  754  CG  LEU A 101     1949   2550   4200   -388   -320   -474  A    C  
ATOM    755  CD1 LEU A 101      23.290 146.995 266.721  1.00 20.71      A    C  
ANISOU  755  CD1 LEU A 101     1700   2367   3803   -501   -366   -414  A    C  
ATOM    756  CD2 LEU A 101      24.871 147.833 265.008  1.00 23.58      A    C  
ANISOU  756  CD2 LEU A 101     2154   2548   4256   -388   -300   -401  A    C  
ATOM    757  N   ALA A 102      23.915 152.379 267.784  1.00 23.68      A    N  
ANISOU  757  N   ALA A 102     1996   2474   4525    -45   -450   -631  A    N  
ATOM    758  CA  ALA A 102      23.269 153.682 267.902  1.00 26.97      A    C  
ANISOU  758  CA  ALA A 102     2519   2816   4913    133   -473   -653  A    C  
ATOM    759  C   ALA A 102      24.146 154.754 267.262  1.00 24.24      A    C  
ANISOU  759  C   ALA A 102     2258   2250   4701     41   -622   -651  A    C  
ATOM    760  O   ALA A 102      23.655 155.639 266.542  1.00 28.25      A    O  
ANISOU  760  O   ALA A 102     2783   2715   5236    105   -619   -614  A    O  
ATOM    761  CB  ALA A 102      22.992 154.017 269.358  1.00 25.52      A    C  
ANISOU  761  CB  ALA A 102     2548   2580   4569    365   -484   -747  A    C  
ATOM    762  N   GLY A 103      25.445 154.672 267.538  1.00 22.94      A    N  
ANISOU  762  N   GLY A 103     2120   1967   4629   -119   -764   -641  A    N  
ATOM    763  CA  GLY A 103      26.399 155.598 266.953  1.00 24.48      A    C  
ANISOU  763  CA  GLY A 103     2326   1993   4983   -272   -944   -535  A    C  
ATOM    764  C   GLY A 103      26.371 155.565 265.436  1.00 29.47      A    C  
ANISOU  764  C   GLY A 103     2772   2743   5683   -302   -808   -388  A    C  
ATOM    765  O   GLY A 103      26.360 156.615 264.787  1.00 27.40      A    O  
ANISOU  765  O   GLY A 103     2539   2368   5503   -324   -891   -329  A    O  
ATOM    766  N   MET A 104      26.335 154.362 264.865  1.00 25.34      A    N  
ANISOU  766  N   MET A 104     2143   2411   5075   -283   -613   -331  A    N  
ATOM    767  CA  MET A 104      26.327 154.234 263.406  1.00 26.34      A    C  
ANISOU  767  CA  MET A 104     2201   2604   5202   -277   -501   -207  A    C  
ATOM    768  C   MET A 104      25.028 154.716 262.769  1.00 26.38      A    C  
ANISOU  768  C   MET A 104     2188   2616   5219   -235   -478   -262  A    C  
ATOM    769  O   MET A 104      25.041 155.299 261.682  1.00 27.78      A    O  
ANISOU  769  O   MET A 104     2335   2769   5452   -235   -465   -172  A    O  
ATOM    770  CB  MET A 104      26.651 152.799 262.973  1.00 25.96      A    C  
ANISOU  770  CB  MET A 104     2127   2664   5073   -266   -371   -155  A    C  
ATOM    771  CG  MET A 104      28.145 152.524 262.984  1.00 32.07      A    C  
ANISOU  771  CG  MET A 104     2807   3468   5911   -268   -351     27  A    C  
ATOM    772  SD  MET A 104      28.608 150.993 262.169  1.00 30.75      A    S  
ANISOU  772  SD  MET A 104     2654   3391   5640   -126   -149    143  A    S  
ATOM    773  CE  MET A 104      27.806 149.783 263.226  1.00 27.85      A    C  
ANISOU  773  CE  MET A 104     2465   3019   5097   -164   -164    -88  A    C  
ATOM    774  N   ALA A 105      23.910 154.463 263.439  1.00 24.84      A    N  
ANISOU  774  N   ALA A 105     1976   2490   4972   -184   -464   -364  A    N  
ATOM    775  CA  ALA A 105      22.628 154.957 262.965  1.00 24.25      A    C  
ANISOU  775  CA  ALA A 105     1864   2494   4855   -100   -423   -329  A    C  
ATOM    776  C   ALA A 105      22.665 156.477 262.953  1.00 28.52      A    C  
ANISOU  776  C   ALA A 105     2499   2878   5459      5   -490   -351  A    C  
ATOM    777  O   ALA A 105      22.224 157.116 261.993  1.00 21.24      A    O  
ANISOU  777  O   ALA A 105     1537   1957   4574     31   -472   -282  A    O  
ATOM    778  CB  ALA A 105      21.498 154.456 263.845  1.00 20.22      A    C  
ANISOU  778  CB  ALA A 105     1307   2158   4217     -7   -363   -319  A    C  
ATOM    779  N   LYS A 106      23.189 157.056 264.027  1.00 21.97      A    N  
ANISOU  779  N   LYS A 106     1852   1879   4616     59   -600   -444  A    N  
ATOM    780  CA  LYS A 106      23.284 158.503 264.096  1.00 37.00      A    C  
ANISOU  780  CA  LYS A 106     3981   3544   6534    142   -735   -471  A    C  
ATOM    781  C   LYS A 106      24.159 159.026 262.952  1.00 35.50      A    C  
ANISOU  781  C   LYS A 106     3701   3254   6535    -56   -832   -347  A    C  
ATOM    782  O   LYS A 106      23.795 159.981 262.272  1.00 28.07      A    O  
ANISOU  782  O   LYS A 106     2815   2228   5621      1   -852   -308  A    O  
ATOM    783  CB  LYS A 106      23.864 158.931 265.437  1.00 39.80      A    C  
ANISOU  783  CB  LYS A 106     4652   3661   6811    175   -926   -582  A    C  
ATOM    784  CG  LYS A 106      23.933 160.419 265.609  1.00 47.49      A    C  
ANISOU  784  CG  LYS A 106     6013   4299   7733    259  -1137   -620  A    C  
ATOM    785  CD  LYS A 106      24.581 160.758 266.922  1.00 57.55      A    C  
ANISOU  785  CD  LYS A 106     7697   5277   8893    245  -1406   -724  A    C  
ATOM    786  CE  LYS A 106      26.069 160.993 266.739  1.00 64.64      A    C  
ANISOU  786  CE  LYS A 106     8520   6121   9921   -155  -1667   -547  A    C  
ATOM    787  NZ  LYS A 106      26.301 162.403 266.276  1.00 70.07      A    N1+
ANISOU  787  NZ  LYS A 106     9447   6603  10573   -225  -1873   -452  A    N1+
ATOM    788  N   GLY A 107      25.311 158.391 262.744  1.00 37.11      A    N  
ANISOU  788  N   GLY A 107     3749   3493   6857   -253   -869   -243  A    N  
ATOM    789  CA  GLY A 107      26.239 158.800 261.700  1.00 30.96      A    C  
ANISOU  789  CA  GLY A 107     2858   2718   6188   -366   -898    -25  A    C  
ATOM    790  C   GLY A 107      25.674 158.724 260.294  1.00 25.28      A    C  
ANISOU  790  C   GLY A 107     2007   2108   5492   -308   -733     40  A    C  
ATOM    791  O   GLY A 107      26.035 159.517 259.421  1.00 27.90      A    O  
ANISOU  791  O   GLY A 107     2303   2388   5910   -341   -769    187  A    O  
ATOM    792  N   ARG A 108      24.772 157.776 260.074  1.00 22.44      A    N  
ANISOU  792  N   ARG A 108     1599   1901   5026   -232   -579    -44  A    N  
ATOM    793  CA  ARG A 108      24.159 157.592 258.761  1.00 22.68      A    C  
ANISOU  793  CA  ARG A 108     1577   2026   5014   -192   -468     22  A    C  
ATOM    794  C   ARG A 108      22.853 158.376 258.658  1.00 26.14      A    C  
ANISOU  794  C   ARG A 108     2031   2474   5428    -99   -474    -30  A    C  
ATOM    795  O   ARG A 108      22.128 158.266 257.665  1.00 27.57      A    O  
ANISOU  795  O   ARG A 108     2161   2746   5566    -84   -418     35  A    O  
ATOM    796  CB  ARG A 108      23.922 156.104 258.474  1.00 20.67      A    C  
ANISOU  796  CB  ARG A 108     1345   1902   4607   -200   -371     16  A    C  
ATOM    797  CG  ARG A 108      25.197 155.336 258.114  1.00 23.89      A    C  
ANISOU  797  CG  ARG A 108     1739   2316   5021   -192   -301    131  A    C  
ATOM    798  CD  ARG A 108      24.937 153.846 258.039  1.00 19.43      A    C  
ANISOU  798  CD  ARG A 108     1334   1802   4247   -173   -243     88  A    C  
ATOM    799  NE  ARG A 108      25.924 153.137 257.227  1.00 21.88      A    N  
ANISOU  799  NE  ARG A 108     1755   2111   4446    -35   -117    233  A    N  
ATOM    800  CZ  ARG A 108      26.956 152.461 257.723  1.00 25.63      A    C  
ANISOU  800  CZ  ARG A 108     2227   2626   4887     47    -33    308  A    C  
ATOM    801  NH1 ARG A 108      27.153 152.404 259.036  1.00 26.79      A    N1+
ANISOU  801  NH1 ARG A 108     2264   2795   5122    -52   -101    224  A    N1+
ATOM    802  NH2 ARG A 108      27.787 151.831 256.907  1.00 21.94      A    N  
ANISOU  802  NH2 ARG A 108     1887   2182   4266    273    132    490  A    N  
ATOM    803  N   LYS A 109      22.547 159.134 259.710  1.00 28.93      A    N  
ANISOU  803  N   LYS A 109     2840   2714   5439   -299  -1068    806  A    N  
ATOM    804  CA  LYS A 109      21.362 159.992 259.749  1.00 30.38      A    C  
ANISOU  804  CA  LYS A 109     3002   2824   5717   -226  -1086    791  A    C  
ATOM    805  C   LYS A 109      20.083 159.194 259.588  1.00 30.31      A    C  
ANISOU  805  C   LYS A 109     2951   2915   5650   -180  -1026    741  A    C  
ATOM    806  O   LYS A 109      19.123 159.655 258.967  1.00 33.01      A    O  
ANISOU  806  O   LYS A 109     3238   3256   6049   -133  -1046    783  A    O  
ATOM    807  CB  LYS A 109      21.441 161.068 258.663  1.00 30.26      A    C  
ANISOU  807  CB  LYS A 109     2941   2761   5796   -230  -1160    938  A    C  
ATOM    808  CG  LYS A 109      22.639 162.010 258.799  1.00 29.13      A    C  
ANISOU  808  CG  LYS A 109     2829   2500   5741   -279  -1227   1001  A    C  
ATOM    809  CD  LYS A 109      22.751 162.920 257.571  1.00 32.08      A    C  
ANISOU  809  CD  LYS A 109     3150   2848   6190   -294  -1291   1172  A    C  
ATOM    810  CE  LYS A 109      23.884 163.921 257.723  1.00 40.11      A    C  
ANISOU  810  CE  LYS A 109     4185   3770   7283   -350  -1344   1215  A    C  
ATOM    811  NZ  LYS A 109      25.198 163.236 257.813  1.00 45.18      A    N1+
ANISOU  811  NZ  LYS A 109     4838   4477   7852   -422  -1324   1229  A    N1+
ATOM    812  N   VAL A 110      20.055 158.006 260.177  1.00 26.96      A    N  
ANISOU  812  N   VAL A 110     2551   2570   5122   -194   -958    651  A    N  
ATOM    813  CA  VAL A 110      18.862 157.184 260.118  1.00 24.28      A    C  
ANISOU  813  CA  VAL A 110     2168   2320   4736   -158   -900    599  A    C  
ATOM    814  C   VAL A 110      18.017 157.397 261.362  1.00 24.78      A    C  
ANISOU  814  C   VAL A 110     2260   2316   4841    -96   -851    474  A    C  
ATOM    815  O   VAL A 110      18.478 157.164 262.479  1.00 27.19      A    O  
ANISOU  815  O   VAL A 110     2637   2584   5109   -104   -818    385  A    O  
ATOM    816  CB  VAL A 110      19.204 155.687 259.993  1.00 26.73      A    C  
ANISOU  816  CB  VAL A 110     2484   2760   4914   -208   -851    577  A    C  
ATOM    817  CG1 VAL A 110      17.936 154.846 260.120  1.00 24.03      A    C  
ANISOU  817  CG1 VAL A 110     2098   2491   4539   -175   -791    513  A    C  
ATOM    818  CG2 VAL A 110      19.894 155.409 258.665  1.00 21.86      A    C  
ANISOU  818  CG2 VAL A 110     1831   2229   4245   -256   -889    695  A    C  
ATOM    819  N   LYS A 111      16.783 157.845 261.154  1.00 26.33      A    N  
ANISOU  819  N   LYS A 111     2396   2499   5110    -31   -846    469  A    N  
ATOM    820  CA  LYS A 111      15.836 158.075 262.236  1.00 28.35      A    C  
ANISOU  820  CA  LYS A 111     2661   2701   5409     40   -789    355  A    C  
ATOM    821  C   LYS A 111      15.307 156.762 262.800  1.00 24.54      A    C  
ANISOU  821  C   LYS A 111     2174   2320   4832     32   -693    275  A    C  
ATOM    822  O   LYS A 111      14.904 155.868 262.058  1.00 23.33      A    O  
ANISOU  822  O   LYS A 111     1959   2275   4630      6   -679    313  A    O  
ATOM    823  CB  LYS A 111      14.658 158.893 261.692  1.00 29.31      A    C  
ANISOU  823  CB  LYS A 111     2701   2790   5646    113   -816    386  A    C  
ATOM    824  CG  LYS A 111      13.485 159.094 262.651  1.00 33.90      A    C  
ANISOU  824  CG  LYS A 111     3265   3335   6280    198   -746    275  A    C  
ATOM    825  CD  LYS A 111      13.788 159.949 263.866  1.00 38.48      A    C  
ANISOU  825  CD  LYS A 111     3931   3786   6904    243   -739    181  A    C  
ATOM    826  CE  LYS A 111      12.480 160.347 264.541  1.00 43.26      A    C  
ANISOU  826  CE  LYS A 111     4497   4358   7582    345   -677     89  A    C  
ATOM    827  NZ  LYS A 111      12.694 161.041 265.840  1.00 48.58      A    N1+
ANISOU  827  NZ  LYS A 111     5264   4919   8274    400   -655    -26  A    N1+
ATOM    828  N   VAL A 112      15.277 156.673 264.125  1.00 22.39      A    N  
ANISOU  828  N   VAL A 112     1968   2005   4533     56   -631    165  A    N  
ATOM    829  CA  VAL A 112      14.738 155.509 264.806  1.00 25.02      A    C  
ANISOU  829  CA  VAL A 112     2303   2421   4783     51   -532     91  A    C  
ATOM    830  C   VAL A 112      13.461 155.884 265.547  1.00 27.31      A    C  
ANISOU  830  C   VAL A 112     2560   2683   5133    136   -460     11  A    C  
ATOM    831  O   VAL A 112      13.474 156.753 266.419  1.00 26.87      A    O  
ANISOU  831  O   VAL A 112     2562   2530   5119    192   -453    -58  A    O  
ATOM    832  CB  VAL A 112      15.738 154.936 265.828  1.00 27.01      A    C  
ANISOU  832  CB  VAL A 112     2665   2665   4933      8   -504     28  A    C  
ATOM    833  CG1 VAL A 112      15.129 153.747 266.559  1.00 26.16      A    C  
ANISOU  833  CG1 VAL A 112     2561   2638   4741      3   -400    -38  A    C  
ATOM    834  CG2 VAL A 112      17.033 154.531 265.146  1.00 24.70      A    C  
ANISOU  834  CG2 VAL A 112     2397   2403   4586    -73   -569    102  A    C  
ATOM    835  N   VAL A 113      12.363 155.231 265.181  1.00 23.02      A    N  
ANISOU  835  N   VAL A 113     1922   2224   4599    147   -410     19  A    N  
ATOM    836  CA  VAL A 113      11.085 155.375 265.871  1.00 25.42      A    C  
ANISOU  836  CA  VAL A 113     2176   2525   4956    223   -323    -54  A    C  
ATOM    837  C   VAL A 113      10.851 154.149 266.752  1.00 29.16      A    C  
ANISOU  837  C   VAL A 113     2673   3076   5329    195   -212   -116  A    C  
ATOM    838  O   VAL A 113      10.893 152.994 266.287  1.00 28.22      A    O  
ANISOU  838  O   VAL A 113     2524   3050   5150    127   -203    -78  A    O  
ATOM    839  CB  VAL A 113       9.909 155.576 264.890  1.00 26.21      A    C  
ANISOU  839  CB  VAL A 113     2139   2659   5160    261   -345      0  A    C  
ATOM    840  CG1 VAL A 113       8.590 155.680 265.640  1.00 28.60      A    C  
ANISOU  840  CG1 VAL A 113     2377   2964   5524    340   -245    -76  A    C  
ATOM    841  CG2 VAL A 113      10.140 156.814 264.027  1.00 25.03      A    C  
ANISOU  841  CG2 VAL A 113     1973   2429   5109    290   -458     71  A    C  
ATOM    842  N   ASN A 114      10.673 154.404 268.043  1.00 27.54      A    N  
ANISOU  842  N   ASN A 114     2532   2829   5103    245   -131   -211  A    N  
ATOM    843  CA  ASN A 114      10.502 153.327 269.003  1.00 32.58      A    C  
ANISOU  843  CA  ASN A 114     3208   3532   5640    221    -21   -266  A    C  
ATOM    844  C   ASN A 114       9.038 153.005 269.288  1.00 31.58      A    C  
ANISOU  844  C   ASN A 114     2977   3462   5559    268     89   -294  A    C  
ATOM    845  O   ASN A 114       8.268 153.879 269.677  1.00 32.70      A    O  
ANISOU  845  O   ASN A 114     3085   3558   5781    358    129   -342  A    O  
ATOM    846  CB  ASN A 114      11.302 153.609 270.274  1.00 38.48      A    C  
ANISOU  846  CB  ASN A 114     4102   4216   6304    237      4   -348  A    C  
ATOM    847  CG  ASN A 114      12.804 153.470 270.049  1.00 44.45      A    C  
ANISOU  847  CG  ASN A 114     4950   4944   6995    164    -92   -314  A    C  
ATOM    848  ND2 ASN A 114      13.488 154.598 269.897  1.00 42.28      A    N  
ANISOU  848  ND2 ASN A 114     4719   4569   6775    186   -183   -310  A    N  
ATOM    849  OD1 ASN A 114      13.336 152.360 269.996  1.00 45.78      A    O  
ANISOU  849  OD1 ASN A 114     5145   5178   7073     89    -85   -289  A    O  
ATOM    850  N   GLY A 115       8.654 151.749 269.073  1.00 28.15      A    N  
ANISOU  850  N   GLY A 115     2487   3124   5084    207    136   -263  A    N  
ATOM    851  CA  GLY A 115       7.284 151.337 269.314  1.00 28.26      A    C  
ANISOU  851  CA  GLY A 115     2390   3197   5151    237    240   -279  A    C  
ATOM    852  C   GLY A 115       6.886 150.139 268.475  1.00 26.65      A    C  
ANISOU  852  C   GLY A 115     2091   3084   4952    160    227   -213  A    C  
ATOM    853  O   GLY A 115       7.698 149.581 267.734  1.00 26.64      A    O  
ANISOU  853  O   GLY A 115     2119   3104   4899     87    142   -162  A    O  
ATOM    854  N   LEU A 116       5.632 149.728 268.615  1.00 28.19      A    N  
ANISOU  854  N   LEU A 116     2170   3331   5211    178    313   -218  A    N  
ATOM    855  CA  LEU A 116       5.107 148.589 267.879  1.00 26.09      A    C  
ANISOU  855  CA  LEU A 116     1802   3144   4965    108    300   -163  A    C  
ATOM    856  C   LEU A 116       4.603 149.032 266.512  1.00 26.19      A    C  
ANISOU  856  C   LEU A 116     1698   3161   5093    125    190   -106  A    C  
ATOM    857  O   LEU A 116       3.670 149.829 266.424  1.00 26.41      A    O  
ANISOU  857  O   LEU A 116     1631   3167   5236    201    204   -115  A    O  
ATOM    858  CB  LEU A 116       3.934 147.975 268.644  1.00 28.00      A    C  
ANISOU  858  CB  LEU A 116     1959   3439   5242    117    441   -186  A    C  
ATOM    859  CG  LEU A 116       4.078 146.581 269.242  1.00 33.51      A    C  
ANISOU  859  CG  LEU A 116     2693   4192   5846     33    516   -181  A    C  
ATOM    860  CD1 LEU A 116       2.708 146.044 269.611  1.00 26.98      A    C  
ANISOU  860  CD1 LEU A 116     1731   3420   5099     37    633   -177  A    C  
ATOM    861  CD2 LEU A 116       4.788 145.647 268.282  1.00 24.55      A    C  
ANISOU  861  CD2 LEU A 116     1577   3085   4666    -62    404   -128  A    C  
ATOM    862  N   GLY A 117       5.190 148.502 265.445  1.00 27.21      A    N  
ANISOU  862  N   GLY A 117     1833   3319   5188     58     81    -48  A    N  
ATOM    863  CA  GLY A 117       4.748 148.866 264.112  1.00 31.14      A    C  
ANISOU  863  CA  GLY A 117     2230   3826   5774     72    -31     10  A    C  
ATOM    864  C   GLY A 117       3.780 147.837 263.550  1.00 34.48      A    C  
ANISOU  864  C   GLY A 117     2527   4324   6249     29    -34     36  A    C  
ATOM    865  O   GLY A 117       4.003 146.628 263.673  1.00 31.47      A    O  
ANISOU  865  O   GLY A 117     2168   3990   5799    -46    -12     36  A    O  
ATOM    866  N   LYS A 118       2.692 148.314 262.950  1.00 34.95      A    N  
ANISOU  866  N   LYS A 118     2476   4389   6416     78    -67     56  A    N  
ATOM    867  CA  LYS A 118       1.748 147.444 262.247  1.00 35.16      A    C  
ANISOU  867  CA  LYS A 118     2459   4478   6422     39    -96     81  A    C  
ATOM    868  C   LYS A 118       1.252 148.125 260.979  1.00 34.63      A    C  
ANISOU  868  C   LYS A 118     2365   4407   6386     76   -213    125  A    C  
ATOM    869  O   LYS A 118       1.015 149.338 260.965  1.00 35.40      A    O  
ANISOU  869  O   LYS A 118     2431   4451   6567    152   -228    128  A    O  
ATOM    870  CB  LYS A 118       0.587 147.032 263.159  1.00 36.64      A    C  
ANISOU  870  CB  LYS A 118     2559   4688   6673     50     30     47  A    C  
ATOM    871  CG  LYS A 118       1.032 146.062 264.250  1.00 41.94      A    C  
ANISOU  871  CG  LYS A 118     3267   5379   7287     -8    141     17  A    C  
ATOM    872  CD  LYS A 118      -0.015 145.804 265.306  1.00 44.64      A    C  
ANISOU  872  CD  LYS A 118     3532   5743   7687     10    289    -12  A    C  
ATOM    873  CE  LYS A 118       0.500 144.779 266.312  1.00 45.91      A    C  
ANISOU  873  CE  LYS A 118     3746   5925   7774    -57    395    -30  A    C  
ATOM    874  NZ  LYS A 118      -0.332 144.733 267.549  1.00 51.05      A    N1+
ANISOU  874  NZ  LYS A 118     4339   6591   8465    -26    568    -60  A    N1+
ATOM    875  N   PHE A 119       1.114 147.347 259.910  1.00 30.67      A    N  
ANISOU  875  N   PHE A 119     1881   3959   5815     26   -296    157  A    N  
ATOM    876  CA  PHE A 119       0.644 147.900 258.647  1.00 35.85      A    C  
ANISOU  876  CA  PHE A 119     2515   4618   6488     57   -406    199  A    C  
ATOM    877  C   PHE A 119      -0.822 148.285 258.761  1.00 36.28      A    C  
ANISOU  877  C   PHE A 119     2455   4668   6662    109   -379    189  A    C  
ATOM    878  O   PHE A 119      -1.597 147.622 259.454  1.00 39.05      A    O  
ANISOU  878  O   PHE A 119     2743   5044   7050     92   -294    159  A    O  
ATOM    879  CB  PHE A 119       0.845 146.902 257.501  1.00 33.33      A    C  
ANISOU  879  CB  PHE A 119     2242   4361   6062     -3   -493    221  A    C  
ATOM    880  CG  PHE A 119       2.288 146.694 257.117  1.00 28.67      A    C  
ANISOU  880  CG  PHE A 119     1763   3778   5350    -40   -537    238  A    C  
ATOM    881  CD1 PHE A 119       2.902 147.523 256.190  1.00 29.75      A    C  
ANISOU  881  CD1 PHE A 119     1948   3902   5456    -14   -623    285  A    C  
ATOM    882  CD2 PHE A 119       3.028 145.664 257.683  1.00 28.23      A    C  
ANISOU  882  CD2 PHE A 119     1766   3744   5216   -101   -490    210  A    C  
ATOM    883  CE1 PHE A 119       4.236 147.332 255.833  1.00 27.97      A    C  
ANISOU  883  CE1 PHE A 119     1819   3689   5119    -48   -655    305  A    C  
ATOM    884  CE2 PHE A 119       4.356 145.466 257.336  1.00 31.12      A    C  
ANISOU  884  CE2 PHE A 119     2231   4119   5472   -132   -527    223  A    C  
ATOM    885  CZ  PHE A 119       4.962 146.305 256.409  1.00 31.08      A    C  
ANISOU  885  CZ  PHE A 119     2268   4106   5437   -105   -607    270  A    C  
ATOM    886  N   THR A 120      -1.184 149.374 258.092  1.00 36.92      A    N  
ANISOU  886  N   THR A 120     2509   4716   6805    171   -449    219  A    N  
ATOM    887  CA  THR A 120      -2.570 149.808 258.005  1.00 36.28      A    C  
ANISOU  887  CA  THR A 120     2318   4629   6836    224   -445    215  A    C  
ATOM    888  C   THR A 120      -2.948 149.905 256.535  1.00 37.01      A    C  
ANISOU  888  C   THR A 120     2406   4745   6911    224   -578    263  A    C  
ATOM    889  O   THR A 120      -4.126 149.944 256.191  1.00 43.17      A    O  
ANISOU  889  O   THR A 120     3098   5538   7765    247   -600    265  A    O  
ATOM    890  CB  THR A 120      -2.798 151.169 258.699  1.00 34.69      A    C  
ANISOU  890  CB  THR A 120     2078   4354   6747    316   -399    198  A    C  
ATOM    891  CG2 THR A 120      -2.629 151.041 260.200  1.00 31.42      A    C  
ANISOU  891  CG2 THR A 120     1656   3925   6357    328   -253    138  A    C  
ATOM    892  OG1 THR A 120      -1.846 152.118 258.207  1.00 37.74      A    O  
ANISOU  892  OG1 THR A 120     2541   4687   7112    341   -478    234  A    O  
ATOM    893  N   GLY A 121      -1.938 149.958 255.668  1.00 36.25      A    N  
ANISOU  893  N   GLY A 121     2404   4655   6715    199   -664    302  A    N  
ATOM    894  CA  GLY A 121      -2.197 149.982 254.237  1.00 34.35      A    C  
ANISOU  894  CA  GLY A 121     2171   4446   6437    198   -785    346  A    C  
ATOM    895  C   GLY A 121      -0.989 149.574 253.410  1.00 36.00      A    C  
ANISOU  895  C   GLY A 121     2489   4688   6503    152   -850    375  A    C  
ATOM    896  O   GLY A 121       0.116 149.435 253.948  1.00 35.84      A    O  
ANISOU  896  O   GLY A 121     2540   4657   6421    124   -807    368  A    O  
ATOM    897  N   ALA A 122      -1.178 149.458 252.096  1.00 32.81      A    N  
ANISOU  897  N   ALA A 122     2097   4324   6047    149   -953    410  A    N  
ATOM    898  CA  ALA A 122      -0.119 148.996 251.200  1.00 33.47      A    C  
ANISOU  898  CA  ALA A 122     2276   4452   5987    111  -1012    434  A    C  
ATOM    899  C   ALA A 122       1.078 149.937 251.213  1.00 31.98      A    C  
ANISOU  899  C   ALA A 122     2164   4222   5765    126  -1018    481  A    C  
ATOM    900  O   ALA A 122       2.188 149.554 250.833  1.00 33.19      A    O  
ANISOU  900  O   ALA A 122     2402   4407   5803     90  -1032    496  A    O  
ATOM    901  CB  ALA A 122      -0.653 148.854 249.788  1.00 33.54      A    C  
ANISOU  901  CB  ALA A 122     2275   4509   5960    121  -1121    461  A    C  
ATOM    902  N   ASN A 123       0.849 151.162 251.672  1.00 28.99      A    N  
ANISOU  902  N   ASN A 123     1753   3770   5493    179  -1006    503  A    N  
ATOM    903  CA  ASN A 123       1.918 152.142 251.779  1.00 35.30      A    C  
ANISOU  903  CA  ASN A 123     2616   4513   6283    193  -1014    551  A    C  
ATOM    904  C   ASN A 123       1.885 152.836 253.130  1.00 33.28      A    C  
ANISOU  904  C   ASN A 123     2330   4175   6139    228   -935    518  A    C  
ATOM    905  O   ASN A 123       2.418 153.938 253.278  1.00 32.60      A    O  
ANISOU  905  O   ASN A 123     2271   4017   6098    260   -951    554  A    O  
ATOM    906  CB  ASN A 123       1.851 153.179 250.651  1.00 36.39      A    C  
ANISOU  906  CB  ASN A 123     2766   4631   6430    232  -1113    631  A    C  
ATOM    907  CG  ASN A 123       2.178 152.583 249.299  1.00 39.48      A    C  
ANISOU  907  CG  ASN A 123     3205   5104   6690    202  -1189    668  A    C  
ATOM    908  ND2 ASN A 123       3.451 152.643 248.917  1.00 39.06      A    N  
ANISOU  908  ND2 ASN A 123     3240   5066   6537    173  -1202    713  A    N  
ATOM    909  OD1 ASN A 123       1.308 152.030 248.627  1.00 40.09      A    O  
ANISOU  909  OD1 ASN A 123     3242   5234   6757    205  -1234    652  A    O  
ATOM    910  N   THR A 124       1.254 152.202 254.117  1.00 31.22      A    N  
ANISOU  910  N   THR A 124     2011   3923   5926    223   -848    448  A    N  
ATOM    911  CA  THR A 124       1.159 152.848 255.425  1.00 38.03      A    C  
ANISOU  911  CA  THR A 124     2840   4714   6895    266   -764    407  A    C  
ATOM    912  C   THR A 124       1.402 151.903 256.591  1.00 36.60      A    C  
ANISOU  912  C   THR A 124     2661   4556   6691    227   -656    341  A    C  
ATOM    913  O   THR A 124       0.738 150.856 256.714  1.00 37.89      A    O  
ANISOU  913  O   THR A 124     2783   4777   6836    193   -617    309  A    O  
ATOM    914  CB  THR A 124      -0.199 153.566 255.620  1.00 42.68      A    C  
ANISOU  914  CB  THR A 124     3327   5267   7623    340   -753    390  A    C  
ATOM    915  CG2 THR A 124      -0.175 154.414 256.877  1.00 42.63      A    C  
ANISOU  915  CG2 THR A 124     3298   5178   7720    401   -672    344  A    C  
ATOM    916  OG1 THR A 124      -0.455 154.423 254.500  1.00 47.42      A    O  
ANISOU  916  OG1 THR A 124     3928   5847   8245    374   -860    454  A    O  
ATOM    917  N   LEU A 125       2.343 152.304 257.447  1.00 32.29      A    N  
ANISOU  917  N   LEU A 125     2162   3957   6151    233   -612    324  A    N  
ATOM    918  CA  LEU A 125       2.681 151.564 258.660  1.00 31.10      A    C  
ANISOU  918  CA  LEU A 125     2018   3816   5984    202   -506    263  A    C  
ATOM    919  C   LEU A 125       2.428 152.461 259.868  1.00 28.27      A    C  
ANISOU  919  C   LEU A 125     1617   3380   5745    278   -424    210  A    C  
ATOM    920  O   LEU A 125       2.859 153.608 259.894  1.00 27.89      A    O  
ANISOU  920  O   LEU A 125     1592   3253   5751    330   -463    225  A    O  
ATOM    921  CB  LEU A 125       4.154 151.142 258.637  1.00 27.64      A    C  
ANISOU  921  CB  LEU A 125     1680   3386   5435    141   -526    278  A    C  
ATOM    922  CG  LEU A 125       4.685 150.351 259.839  1.00 29.53      A    C  
ANISOU  922  CG  LEU A 125     1941   3634   5644    101   -429    220  A    C  
ATOM    923  CD1 LEU A 125       4.252 148.902 259.737  1.00 32.67      A    C  
ANISOU  923  CD1 LEU A 125     2331   4113   5968     36   -397    202  A    C  
ATOM    924  CD2 LEU A 125       6.193 150.422 259.936  1.00 30.57      A    C  
ANISOU  924  CD2 LEU A 125     2166   3744   5706     64   -459    236  A    C  
ATOM    925  N   GLU A 126       1.738 151.933 260.871  1.00 29.81      A    N  
ANISOU  925  N   GLU A 126     1753   3596   5978    285   -308    148  A    N  
ATOM    926  CA  GLU A 126       1.375 152.713 262.049  1.00 32.45      A    C  
ANISOU  926  CA  GLU A 126     2046   3868   6416    370   -209     83  A    C  
ATOM    927  C   GLU A 126       2.153 152.216 263.261  1.00 34.65      A    C  
ANISOU  927  C   GLU A 126     2397   4144   6625    342   -103     23  A    C  
ATOM    928  O   GLU A 126       2.184 151.016 263.539  1.00 27.47      A    O  
ANISOU  928  O   GLU A 126     1492   3301   5645    271    -47     15  A    O  
ATOM    929  CB  GLU A 126      -0.132 152.621 262.305  1.00 33.71      A    C  
ANISOU  929  CB  GLU A 126     2100   4058   6652    410   -138     56  A    C  
ATOM    930  CG  GLU A 126      -0.644 153.553 263.385  1.00 39.94      A    C  
ANISOU  930  CG  GLU A 126     2846   4785   7543    515    -37    -13  A    C  
ATOM    931  CD  GLU A 126      -2.155 153.699 263.362  1.00 47.89      A    C  
ANISOU  931  CD  GLU A 126     3744   5818   8633    563      3    -23  A    C  
ATOM    932  OE1 GLU A 126      -2.800 153.365 264.379  1.00 53.21      A    O  
ANISOU  932  OE1 GLU A 126     4368   6522   9330    586    143    -78  A    O  
ATOM    933  OE2 GLU A 126      -2.700 154.133 262.325  1.00 47.97      A    O1-
ANISOU  933  OE2 GLU A 126     3720   5824   8684    577   -103     27  A    O1-
ATOM    934  N   VAL A 127       2.804 153.138 263.967  1.00 32.80      A    N  
ANISOU  934  N   VAL A 127     2268   3829   6366    390    -80    -18  A    N  
ATOM    935  CA  VAL A 127       3.643 152.765 265.099  1.00 32.77      A    C  
ANISOU  935  CA  VAL A 127     2396   3816   6237    359      6    -76  A    C  
ATOM    936  C   VAL A 127       3.046 153.261 266.407  1.00 37.82      A    C  
ANISOU  936  C   VAL A 127     3041   4422   6909    442    138   -165  A    C  
ATOM    937  O   VAL A 127       2.688 154.436 266.529  1.00 36.03      A    O  
ANISOU  937  O   VAL A 127     2794   4122   6774    536    127   -193  A    O  
ATOM    938  CB  VAL A 127       5.060 153.337 264.970  1.00 29.66      A    C  
ANISOU  938  CB  VAL A 127     2144   3357   5769    338    -77    -60  A    C  
ATOM    939  CG1 VAL A 127       5.944 152.821 266.107  1.00 26.25      A    C  
ANISOU  939  CG1 VAL A 127     1847   2923   5205    299      0   -118  A    C  
ATOM    940  CG2 VAL A 127       5.655 152.982 263.619  1.00 27.75      A    C  
ANISOU  940  CG2 VAL A 127     1896   3152   5497    269   -202     32  A    C  
ATOM    941  N   GLU A 128       2.900 152.356 267.371  1.00 37.92      A    N  
ANISOU  941  N   GLU A 128     3077   4488   6845    411    263   -209  A    N  
ATOM    942  CA  GLU A 128       2.396 152.735 268.684  1.00 38.74      A    C  
ANISOU  942  CA  GLU A 128     3198   4572   6949    489    403   -296  A    C  
ATOM    943  C   GLU A 128       3.566 152.666 269.671  1.00 37.05      A    C  
ANISOU  943  C   GLU A 128     3166   4325   6585    467    435   -347  A    C  
ATOM    944  O   GLU A 128       4.103 151.585 269.944  1.00 34.97      A    O  
ANISOU  944  O   GLU A 128     2965   4114   6209    382    463   -334  A    O  
ATOM    945  CB  GLU A 128       1.264 151.788 269.072  1.00 39.91      A    C  
ANISOU  945  CB  GLU A 128     3229   4810   7126    474    530   -299  A    C  
ATOM    946  CG  GLU A 128       0.554 152.092 270.368  1.00 48.94      A    C  
ANISOU  946  CG  GLU A 128     4364   5956   8274    559    695   -380  A    C  
ATOM    947  CD  GLU A 128      -0.733 151.297 270.488  1.00 53.75      A    C  
ANISOU  947  CD  GLU A 128     4812   6652   8958    548    807   -361  A    C  
ATOM    948  OE1 GLU A 128      -0.965 150.404 269.642  1.00 54.21      A    O  
ANISOU  948  OE1 GLU A 128     4783   6764   9049    463    749   -290  A    O  
ATOM    949  OE2 GLU A 128      -1.517 151.575 271.415  1.00 54.25      A    O1-
ANISOU  949  OE2 GLU A 128     4832   6729   9050    625    950   -418  A    O1-
ATOM    950  N   GLY A 129       3.992 153.826 270.167  1.00 36.02      A    N  
ANISOU  950  N   GLY A 129     3124   4103   6460    543    417   -405  A    N  
ATOM    951  CA  GLY A 129       5.161 153.899 271.028  1.00 32.87      A    C  
ANISOU  951  CA  GLY A 129     2901   3659   5931    526    419   -455  A    C  
ATOM    952  C   GLY A 129       5.182 155.021 272.050  1.00 33.24      A    C  
ANISOU  952  C   GLY A 129     3030   3619   5980    633    462   -556  A    C  
ATOM    953  O   GLY A 129       4.150 155.607 272.385  1.00 31.45      A    O  
ANISOU  953  O   GLY A 129     2728   3383   5840    730    536   -605  A    O  
ATOM    954  N   GLU A 130       6.387 155.309 272.542  1.00 30.16      A    N  
ANISOU  954  N   GLU A 130     2797   3165   5497    615    409   -591  A    N  
ATOM    955  CA  GLU A 130       6.620 156.315 273.573  1.00 35.49      A    C  
ANISOU  955  CA  GLU A 130     3581   3748   6153    708    430   -696  A    C  
ATOM    956  C   GLU A 130       6.075 157.681 273.159  1.00 36.69      A    C  
ANISOU  956  C   GLU A 130     3669   3808   6462    809    373   -716  A    C  
ATOM    957  O   GLU A 130       5.594 158.445 273.998  1.00 33.04      A    O  
ANISOU  957  O   GLU A 130     3234   3296   6024    919    437   -815  A    O  
ATOM    958  CB  GLU A 130       8.106 156.416 273.941  1.00 40.36      A    C  
ANISOU  958  CB  GLU A 130     4367   4302   6667    657    344   -715  A    C  
ATOM    959  CG  GLU A 130       9.036 156.691 272.771  1.00 54.05      A    C  
ANISOU  959  CG  GLU A 130     6098   5988   8452    588    182   -624  A    C  
ATOM    960  CD  GLU A 130      10.502 156.459 273.120  1.00 67.83      A    C  
ANISOU  960  CD  GLU A 130     7987   7698  10086    517    113   -629  A    C  
ATOM    961  OE1 GLU A 130      10.802 156.156 274.299  1.00 70.46      A    O  
ANISOU  961  OE1 GLU A 130     8433   8036  10304    527    179   -707  A    O  
ATOM    962  OE2 GLU A 130      11.356 156.581 272.214  1.00 69.36      A    O1-
ANISOU  962  OE2 GLU A 130     8181   7864  10309    452     -7   -551  A    O1-
ATOM    963  N   ASN A 131       6.167 157.990 271.869  1.00 32.62      A    N  
ANISOU  963  N   ASN A 131     3075   3268   6050    777    250   -623  A    N  
ATOM    964  CA  ASN A 131       5.721 159.286 271.380  1.00 36.43      A    C  
ANISOU  964  CA  ASN A 131     3500   3653   6687    866    177   -625  A    C  
ATOM    965  C   ASN A 131       4.308 159.201 270.830  1.00 39.27      A    C  
ANISOU  965  C   ASN A 131     3681   4072   7166    914    227   -595  A    C  
ATOM    966  O   ASN A 131       3.921 160.012 269.987  1.00 43.03      A    O  
ANISOU  966  O   ASN A 131     4077   4492   7780    958    138   -551  A    O  
ATOM    967  CB  ASN A 131       6.636 159.749 270.240  1.00 38.66      A    C  
ANISOU  967  CB  ASN A 131     3799   3872   7017    804      8   -528  A    C  
ATOM    968  CG  ASN A 131       8.056 160.041 270.696  1.00 45.80      A    C  
ANISOU  968  CG  ASN A 131     4864   4698   7840    762    -62   -552  A    C  
ATOM    969  ND2 ASN A 131       8.972 160.131 269.740  1.00 41.70      A    N  
ANISOU  969  ND2 ASN A 131     4359   4154   7333    683   -187   -454  A    N  
ATOM    970  OD1 ASN A 131       8.331 160.161 271.889  1.00 53.31      A    O  
ANISOU  970  OD1 ASN A 131     5925   5616   8716    800     -4   -656  A    O  
ATOM    971  N   GLY A 132       3.528 158.232 271.304  1.00 38.25      A    N  
ANISOU  971  N   GLY A 132     3488   4053   6991    905    364   -614  A    N  
ATOM    972  CA  GLY A 132       2.154 158.117 270.852  1.00 33.97      A    C  
ANISOU  972  CA  GLY A 132     2767   3569   6573    949    416   -589  A    C  
ATOM    973  C   GLY A 132       2.087 157.331 269.558  1.00 39.10      A    C  
ANISOU  973  C   GLY A 132     3318   4288   7250    851    333   -469  A    C  
ATOM    974  O   GLY A 132       2.827 156.358 269.360  1.00 37.79      A    O  
ANISOU  974  O   GLY A 132     3208   4178   6973    741    313   -423  A    O  
ATOM    975  N   LYS A 133       1.185 157.757 268.679  1.00 36.68      A    N  
ANISOU  975  N   LYS A 133     2867   3978   7093    895    280   -423  A    N  
ATOM    976  CA  LYS A 133       0.940 157.071 267.422  1.00 38.82      A    C  
ANISOU  976  CA  LYS A 133     3033   4317   7401    817    197   -317  A    C  
ATOM    977  C   LYS A 133       1.680 157.845 266.337  1.00 39.97      A    C  
ANISOU  977  C   LYS A 133     3217   4388   7583    803     24   -242  A    C  
ATOM    978  O   LYS A 133       1.549 159.068 266.242  1.00 40.44      A    O  
ANISOU  978  O   LYS A 133     3274   4347   7743    890    -33   -256  A    O  
ATOM    979  CB  LYS A 133      -0.563 157.088 267.122  1.00 40.83      A    C  
ANISOU  979  CB  LYS A 133     3098   4613   7803    880    238   -310  A    C  
ATOM    980  CG  LYS A 133      -0.955 156.594 265.733  1.00 43.23      A    C  
ANISOU  980  CG  LYS A 133     3282   4972   8170    820    127   -206  A    C  
ATOM    981  CD  LYS A 133      -2.466 156.671 265.553  1.00 53.10      A    C  
ANISOU  981  CD  LYS A 133     4418   6267   9489    858    162   -202  A    C  
ATOM    982  CE  LYS A 133      -3.182 155.785 266.563  1.00 57.16      A    C  
ANISOU  982  CE  LYS A 133     4878   6864   9978    851    334   -255  A    C  
ATOM    983  NZ  LYS A 133      -4.660 155.809 266.379  1.00 60.21      A    N1+
ANISOU  983  NZ  LYS A 133     5143   7297  10436    883    365   -244  A    N1+
ATOM    984  N   THR A 134       2.426 157.132 265.498  1.00 31.04      A    N  
ANISOU  984  N   THR A 134     2116   3304   6373    697    -59   -161  A    N  
ATOM    985  CA  THR A 134       3.156 157.757 264.398  1.00 33.50      A    C  
ANISOU  985  CA  THR A 134     2460   3562   6705    673   -214    -74  A    C  
ATOM    986  C   THR A 134       2.764 157.065 263.106  1.00 36.90      A    C  
ANISOU  986  C   THR A 134     2788   4079   7154    616   -291     21  A    C  
ATOM    987  O   THR A 134       2.960 155.853 262.965  1.00 32.98      A    O  
ANISOU  987  O   THR A 134     2293   3674   6564    530   -266     38  A    O  
ATOM    988  CB  THR A 134       4.688 157.620 264.563  1.00 33.78      A    C  
ANISOU  988  CB  THR A 134     2653   3573   6610    596   -252    -63  A    C  
ATOM    989  CG2 THR A 134       5.413 158.365 263.458  1.00 29.04      A    C  
ANISOU  989  CG2 THR A 134     2079   2915   6041    577   -400     33  A    C  
ATOM    990  OG1 THR A 134       5.102 158.153 265.829  1.00 33.52      A    O  
ANISOU  990  OG1 THR A 134     2727   3464   6545    643   -185   -160  A    O  
ATOM    991  N   VAL A 135       2.256 157.834 262.147  1.00 35.69      A    N  
ANISOU  991  N   VAL A 135     2553   3889   7117    663   -395     84  A    N  
ATOM    992  CA  VAL A 135       1.843 157.261 260.874  1.00 35.45      A    C  
ANISOU  992  CA  VAL A 135     2489   3945   7037    598   -470    168  A    C  
ATOM    993  C   VAL A 135       2.959 157.463 259.859  1.00 35.84      A    C  
ANISOU  993  C   VAL A 135     2622   3983   7014    539   -592    260  A    C  
ATOM    994  O   VAL A 135       3.364 158.594 259.572  1.00 35.28      A    O  
ANISOU  994  O   VAL A 135     2592   3821   6991    576   -666    298  A    O  
ATOM    995  CB  VAL A 135       0.549 157.908 260.353  1.00 38.86      A    C  
ANISOU  995  CB  VAL A 135     2842   4366   7556    659   -500    182  A    C  
ATOM    996  CG1 VAL A 135       0.178 157.324 259.000  1.00 32.01      A    C  
ANISOU  996  CG1 VAL A 135     1955   3581   6626    596   -586    261  A    C  
ATOM    997  CG2 VAL A 135      -0.582 157.687 261.339  1.00 38.09      A    C  
ANISOU  997  CG2 VAL A 135     2656   4291   7524    715   -371     96  A    C  
ATOM    998  N   ILE A 136       3.470 156.354 259.336  1.00 33.36      A    N  
ANISOU  998  N   ILE A 136     2337   3759   6580    447   -607    295  A    N  
ATOM    999  CA  ILE A 136       4.581 156.396 258.404  1.00 31.59      A    C  
ANISOU  999  CA  ILE A 136     2195   3543   6265    387   -702    380  A    C  
ATOM   1000  C   ILE A 136       4.118 155.983 257.019  1.00 32.95      A    C  
ANISOU 1000  C   ILE A 136     2357   3795   6368    351   -773    447  A    C  
ATOM   1001  O   ILE A 136       3.752 154.820 256.798  1.00 31.74      A    O  
ANISOU 1001  O   ILE A 136     2185   3733   6142    304   -747    429  A    O  
ATOM   1002  CB  ILE A 136       5.724 155.455 258.847  1.00 34.54      A    C  
ANISOU 1002  CB  ILE A 136     2629   3957   6537    313   -668    363  A    C  
ATOM   1003  CG1 ILE A 136       6.215 155.814 260.251  1.00 29.03      A    C  
ANISOU 1003  CG1 ILE A 136     2000   3185   5847    338   -583    279  A    C  
ATOM   1004  CG2 ILE A 136       6.878 155.498 257.854  1.00 29.50      A    C  
ANISOU 1004  CG2 ILE A 136     2075   3336   5800    253   -756    451  A    C  
ATOM   1005  CD1 ILE A 136       7.428 155.010 260.698  1.00 27.48      A    C  
ANISOU 1005  CD1 ILE A 136     1916   3019   5506    256   -547    259  A    C  
ATOM   1006  N   ASN A 137       4.147 156.945 256.096  1.00 35.75      A    N  
ANISOU 1006  N   ASN A 137     2730   4108   6745    374   -864    522  A    N  
ATOM   1007  CA  ASN A 137       3.829 156.708 254.695  1.00 33.66      A    C  
ANISOU 1007  CA  ASN A 137     2467   3912   6411    349   -942    591  A    C  
ATOM   1008  C   ASN A 137       5.140 156.417 253.969  1.00 34.05      A    C  
ANISOU 1008  C   ASN A 137     2607   3998   6331    282   -987    658  A    C  
ATOM   1009  O   ASN A 137       6.067 157.224 254.014  1.00 32.60      A    O  
ANISOU 1009  O   ASN A 137     2478   3748   6160    280  -1015    705  A    O  
ATOM   1010  CB  ASN A 137       3.166 157.950 254.087  1.00 36.93      A    C  
ANISOU 1010  CB  ASN A 137     2852   4261   6919    412  -1014    641  A    C  
ATOM   1011  CG  ASN A 137       1.844 158.307 254.757  1.00 43.85      A    C  
ANISOU 1011  CG  ASN A 137     3634   5101   7928    485   -969    575  A    C  
ATOM   1012  ND2 ASN A 137       1.733 159.545 255.228  1.00 44.95      A    N  
ANISOU 1012  ND2 ASN A 137     3766   5131   8183    554   -976    568  A    N  
ATOM   1013  OD1 ASN A 137       0.943 157.475 254.864  1.00 48.89      A    O  
ANISOU 1013  OD1 ASN A 137     4205   5806   8563    481   -927    529  A    O  
ATOM   1014  N   PHE A 138       5.213 155.272 253.294  1.00 33.31      A    N  
ANISOU 1014  N   PHE A 138     2532   4010   6117    229   -993    660  A    N  
ATOM   1015  CA  PHE A 138       6.462 154.825 252.680  1.00 31.41      A    C  
ANISOU 1015  CA  PHE A 138     2374   3818   5742    168  -1017    708  A    C  
ATOM   1016  C   PHE A 138       6.296 154.493 251.198  1.00 31.45      A    C  
ANISOU 1016  C   PHE A 138     2394   3904   5651    154  -1087    763  A    C  
ATOM   1017  O   PHE A 138       5.181 154.238 250.729  1.00 34.75      A    O  
ANISOU 1017  O   PHE A 138     2757   4356   6088    177  -1113    746  A    O  
ATOM   1018  CB  PHE A 138       7.023 153.607 253.423  1.00 25.29      A    C  
ANISOU 1018  CB  PHE A 138     1625   3092   4892    115   -945    641  A    C  
ATOM   1019  CG  PHE A 138       6.075 152.444 253.480  1.00 25.30      A    C  
ANISOU 1019  CG  PHE A 138     1579   3164   4869    102   -911    575  A    C  
ATOM   1020  CD1 PHE A 138       5.996 151.539 252.428  1.00 25.17      A    C  
ANISOU 1020  CD1 PHE A 138     1581   3238   4745     71   -950    584  A    C  
ATOM   1021  CD2 PHE A 138       5.269 152.245 254.595  1.00 25.53      A    C  
ANISOU 1021  CD2 PHE A 138     1543   3169   4989    123   -837    503  A    C  
ATOM   1022  CE1 PHE A 138       5.115 150.467 252.480  1.00 33.61      A    C  
ANISOU 1022  CE1 PHE A 138     2606   4361   5802     56   -927    525  A    C  
ATOM   1023  CE2 PHE A 138       4.396 151.171 254.663  1.00 25.64      A    C  
ANISOU 1023  CE2 PHE A 138     1511   3244   4988    103   -803    452  A    C  
ATOM   1024  CZ  PHE A 138       4.318 150.279 253.603  1.00 31.37      A    C  
ANISOU 1024  CZ  PHE A 138     2256   4050   5612     67   -854    464  A    C  
ATOM   1025  N   ASP A 139       7.407 154.508 250.465  1.00 27.98      A    N  
ANISOU 1025  N   ASP A 139     2025   3495   5109    118  -1119    830  A    N  
ATOM   1026  CA  ASP A 139       7.423 153.999 249.099  1.00 31.36      A    C  
ANISOU 1026  CA  ASP A 139     2478   4016   5423    103  -1175    870  A    C  
ATOM   1027  C   ASP A 139       7.772 152.516 249.140  1.00 31.71      A    C  
ANISOU 1027  C   ASP A 139     2547   4147   5353     57  -1136    804  A    C  
ATOM   1028  O   ASP A 139       7.241 151.717 248.367  1.00 33.40      A    O  
ANISOU 1028  O   ASP A 139     2750   4436   5502     55  -1167    781  A    O  
ATOM   1029  CB  ASP A 139       8.441 154.757 248.248  1.00 38.11      A    C  
ANISOU 1029  CB  ASP A 139     3391   4866   6223     91  -1221    979  A    C  
ATOM   1030  CG  ASP A 139       8.137 156.243 248.156  1.00 47.29      A    C  
ANISOU 1030  CG  ASP A 139     4535   5933   7500    133  -1266   1051  A    C  
ATOM   1031  OD1 ASP A 139       6.958 156.621 248.327  1.00 49.79      A    O  
ANISOU 1031  OD1 ASP A 139     4790   6211   7916    181  -1284   1023  A    O  
ATOM   1032  OD2 ASP A 139       9.082 157.033 247.935  1.00 48.34      A    O1-
ANISOU 1032  OD2 ASP A 139     4713   6026   7629    116  -1283   1136  A    O1-
ATOM   1033  N   ASN A 140       8.671 152.163 250.051  1.00 32.08      A    N  
ANISOU 1033  N   ASN A 140     2630   4178   5380     21  -1073    772  A    N  
ATOM   1034  CA  ASN A 140       9.071 150.777 250.258  1.00 34.99      A    C  
ANISOU 1034  CA  ASN A 140     3028   4615   5652    -23  -1030    704  A    C  
ATOM   1035  C   ASN A 140       9.139 150.425 251.737  1.00 33.80      A    C  
ANISOU 1035  C   ASN A 140     2867   4421   5555    -40   -951    632  A    C  
ATOM   1036  O   ASN A 140       9.522 151.256 252.563  1.00 30.96      A    O  
ANISOU 1036  O   ASN A 140     2509   3984   5272    -29   -928    644  A    O  
ATOM   1037  CB  ASN A 140      10.430 150.504 249.612  1.00 32.81      A    C  
ANISOU 1037  CB  ASN A 140     2826   4388   5251    -58  -1040    749  A    C  
ATOM   1038  CG  ASN A 140      10.406 150.671 248.108  1.00 33.78      A    C  
ANISOU 1038  CG  ASN A 140     2962   4571   5300    -42  -1111    816  A    C  
ATOM   1039  ND2 ASN A 140       9.906 149.661 247.410  1.00 31.52      A    N  
ANISOU 1039  ND2 ASN A 140     2671   4363   4941    -41  -1137    769  A    N  
ATOM   1040  OD1 ASN A 140      10.829 151.699 247.580  1.00 37.54      A    O  
ANISOU 1040  OD1 ASN A 140     3455   5023   5786    -31  -1146    910  A    O  
ATOM   1041  N   ALA A 141       8.760 149.194 252.068  1.00 33.66      A    N  
ANISOU 1041  N   ALA A 141     2839   4450   5500    -65   -913    556  A    N  
ATOM   1042  CA  ALA A 141       8.864 148.705 253.437  1.00 30.35      A    C  
ANISOU 1042  CA  ALA A 141     2415   4002   5114    -88   -834    490  A    C  
ATOM   1043  C   ALA A 141       9.723 147.447 253.477  1.00 30.46      A    C  
ANISOU 1043  C   ALA A 141     2492   4072   5010   -141   -808    452  A    C  
ATOM   1044  O   ALA A 141       9.637 146.596 252.596  1.00 28.59      A    O  
ANISOU 1044  O   ALA A 141     2270   3904   4691   -155   -839    440  A    O  
ATOM   1045  CB  ALA A 141       7.488 148.419 254.005  1.00 22.54      A    C  
ANISOU 1045  CB  ALA A 141     1345   3005   4213    -70   -799    437  A    C  
ATOM   1046  N   ILE A 142      10.530 147.318 254.521  1.00 28.46      A    N  
ANISOU 1046  N   ILE A 142     2274   3785   4753   -168   -754    427  A    N  
ATOM   1047  CA  ILE A 142      11.336 146.126 254.703  1.00 23.94      A    C  
ANISOU 1047  CA  ILE A 142     1761   3255   4079   -216   -726    385  A    C  
ATOM   1048  C   ILE A 142      10.948 145.488 256.028  1.00 23.17      A    C  
ANISOU 1048  C   ILE A 142     1645   3135   4025   -239   -654    319  A    C  
ATOM   1049  O   ILE A 142      11.191 146.047 257.102  1.00 21.25      A    O  
ANISOU 1049  O   ILE A 142     1397   2830   3846   -236   -614    310  A    O  
ATOM   1050  CB  ILE A 142      12.858 146.423 254.669  1.00 26.58      A    C  
ANISOU 1050  CB  ILE A 142     2168   3581   4351   -236   -732    421  A    C  
ATOM   1051  CG1 ILE A 142      13.252 147.129 253.369  1.00 26.16      A    C  
ANISOU 1051  CG1 ILE A 142     2128   3552   4261   -217   -795    501  A    C  
ATOM   1052  CG2 ILE A 142      13.658 145.137 254.801  1.00 17.89      A    C  
ANISOU 1052  CG2 ILE A 142     1127   2525   3147   -278   -706    373  A    C  
ATOM   1053  CD1 ILE A 142      14.760 147.454 253.268  1.00 18.61      A    C  
ANISOU 1053  CD1 ILE A 142     1232   2590   3249   -240   -796    549  A    C  
ATOM   1054  N   ILE A 143      10.299 144.333 255.934  1.00 19.16      A    N  
ANISOU 1054  N   ILE A 143     1121   2672   3488   -260   -641    274  A    N  
ATOM   1055  CA  ILE A 143       9.860 143.591 257.101  1.00 19.06      A    C  
ANISOU 1055  CA  ILE A 143     1088   2645   3510   -288   -570    221  A    C  
ATOM   1056  C   ILE A 143      10.987 142.716 257.633  1.00 23.13      A    C  
ANISOU 1056  C   ILE A 143     1682   3166   3940   -336   -543    192  A    C  
ATOM   1057  O   ILE A 143      11.478 141.819 256.940  1.00 23.51      A    O  
ANISOU 1057  O   ILE A 143     1777   3261   3895   -356   -572    179  A    O  
ATOM   1058  CB  ILE A 143       8.644 142.711 256.765  1.00 25.95      A    C  
ANISOU 1058  CB  ILE A 143     1905   3556   4398   -296   -573    194  A    C  
ATOM   1059  CG1 ILE A 143       7.476 143.586 256.291  1.00 20.67      A    C  
ANISOU 1059  CG1 ILE A 143     1153   2878   3821   -247   -601    220  A    C  
ATOM   1060  CG2 ILE A 143       8.223 141.895 257.973  1.00 21.29      A    C  
ANISOU 1060  CG2 ILE A 143     1294   2952   3841   -333   -494    151  A    C  
ATOM   1061  CD1 ILE A 143       6.300 142.802 255.746  1.00 21.37      A    C  
ANISOU 1061  CD1 ILE A 143     1187   3008   3926   -254   -624    201  A    C  
ATOM   1062  N   ALA A 144      11.394 142.978 258.870  1.00 24.39      A    N  
ANISOU 1062  N   ALA A 144     1854   3276   4137   -349   -488    177  A    N  
ATOM   1063  CA  ALA A 144      12.486 142.232 259.478  1.00 22.48      A    C  
ANISOU 1063  CA  ALA A 144     1690   3031   3822   -393   -466    151  A    C  
ATOM   1064  C   ALA A 144      12.190 142.011 260.953  1.00 21.00      A    C  
ANISOU 1064  C   ALA A 144     1485   2801   3694   -417   -388    114  A    C  
ATOM   1065  O   ALA A 144      13.032 142.278 261.811  1.00 21.77      A    O  
ANISOU 1065  O   ALA A 144     1633   2854   3782   -430   -363    102  A    O  
ATOM   1066  CB  ALA A 144      13.791 142.997 259.301  1.00 16.59      A    C  
ANISOU 1066  CB  ALA A 144     1003   2262   3038   -387   -499    183  A    C  
ATOM   1067  N   ALA A 145      11.000 141.489 261.237  1.00 19.33      A    N  
ANISOU 1067  N   ALA A 145     1209   2603   3533   -422   -344     95  A    N  
ATOM   1068  CA  ALA A 145      10.497 141.446 262.607  1.00 18.11      A    C  
ANISOU 1068  CA  ALA A 145     1019   2412   3451   -433   -248     65  A    C  
ATOM   1069  C   ALA A 145      10.845 140.152 263.342  1.00 22.63      A    C  
ANISOU 1069  C   ALA A 145     1650   2990   3957   -493   -203     38  A    C  
ATOM   1070  O   ALA A 145      10.361 139.916 264.451  1.00 18.15      A    O  
ANISOU 1070  O   ALA A 145     1091   2407   3400   -499   -107     14  A    O  
ATOM   1071  CB  ALA A 145       8.990 141.692 262.631  1.00 19.14      A    C  
ANISOU 1071  CB  ALA A 145     1039   2550   3682   -400   -206     65  A    C  
ATOM   1072  N   GLY A 146      11.650 139.300 262.711  1.00 22.05      A    N  
ANISOU 1072  N   GLY A 146     1642   2946   3790   -526   -265     40  A    N  
ATOM   1073  CA  GLY A 146      12.266 138.179 263.409  1.00 17.95      A    C  
ANISOU 1073  CA  GLY A 146     1190   2419   3210   -581   -240     18  A    C  
ATOM   1074  C   GLY A 146      11.404 137.013 263.876  1.00 17.51      A    C  
ANISOU 1074  C   GLY A 146     1108   2375   3172   -623   -190      7  A    C  
ATOM   1075  O   GLY A 146      10.322 136.745 263.343  1.00 17.69      A    O  
ANISOU 1075  O   GLY A 146     1063   2427   3230   -615   -195     14  A    O  
ATOM   1076  N   SER A 147      11.900 136.328 264.905  1.00 16.88      A    N  
ANISOU 1076  N   SER A 147     1084   2266   3063   -669   -142     -7  A    N  
ATOM   1077  CA  SER A 147      11.241 135.147 265.447  1.00 20.01      A    C  
ANISOU 1077  CA  SER A 147     1465   2664   3474   -721    -93     -7  A    C  
ATOM   1078  C   SER A 147      11.213 135.209 266.976  1.00 22.84      A    C  
ANISOU 1078  C   SER A 147     1886   2991   3802   -724     24    -14  A    C  
ATOM   1079  O   SER A 147      11.676 136.184 267.579  1.00 22.71      A    O  
ANISOU 1079  O   SER A 147     1933   2951   3744   -678     59    -30  A    O  
ATOM   1080  CB  SER A 147      11.969 133.875 264.988  1.00 20.42      A    C  
ANISOU 1080  CB  SER A 147     1596   2728   3435   -755   -160    -17  A    C  
ATOM   1081  OG  SER A 147      13.327 133.853 265.425  1.00 22.90      A    O  
ANISOU 1081  OG  SER A 147     2006   3013   3683   -767   -179    -29  A    O  
ATOM   1082  N   ARG A 148      10.690 134.151 267.591  1.00 23.43      A    N  
ANISOU 1082  N   ARG A 148     1952   3064   3889   -777     79     -3  A    N  
ATOM   1083  CA  ARG A 148      10.556 134.074 269.043  1.00 26.94      A    C  
ANISOU 1083  CA  ARG A 148     2460   3488   4288   -782    199     -2  A    C  
ATOM   1084  C   ARG A 148      10.576 132.599 269.449  1.00 28.81      A    C  
ANISOU 1084  C   ARG A 148     2726   3714   4505   -858    209     20  A    C  
ATOM   1085  O   ARG A 148      10.312 131.732 268.622  1.00 27.64      A    O  
ANISOU 1085  O   ARG A 148     2514   3574   4413   -904    139     32  A    O  
ATOM   1086  CB  ARG A 148       9.247 134.747 269.469  1.00 19.77      A    C  
ANISOU 1086  CB  ARG A 148     1455   2597   3458   -746    305      6  A    C  
ATOM   1087  CG  ARG A 148       8.014 133.981 269.018  1.00 30.04      A    C  
ANISOU 1087  CG  ARG A 148     2616   3924   4873   -793    316     37  A    C  
ATOM   1088  CD  ARG A 148       6.720 134.701 269.359  1.00 29.72      A    C  
ANISOU 1088  CD  ARG A 148     2462   3904   4924   -751    419     45  A    C  
ATOM   1089  NE  ARG A 148       5.557 133.893 268.991  1.00 33.15      A    N  
ANISOU 1089  NE  ARG A 148     2777   4365   5455   -795    421     79  A    N  
ATOM   1090  CZ  ARG A 148       5.010 133.883 267.776  1.00 36.38      A    C  
ANISOU 1090  CZ  ARG A 148     3129   4798   5894   -776    311     81  A    C  
ATOM   1091  NH1 ARG A 148       5.523 134.629 266.803  1.00 31.23      A    N1+
ANISOU 1091  NH1 ARG A 148     2493   4148   5227   -729    211     60  A    N1+
ATOM   1092  NH2 ARG A 148       3.956 133.119 267.527  1.00 33.93      A    N  
ANISOU 1092  NH2 ARG A 148     2754   4510   5628   -805    305    105  A    N  
ATOM   1093  N   PRO A 149      10.872 132.308 270.727  1.00 30.47      A    N  
ANISOU 1093  N   PRO A 149     3036   3903   4637   -872    291     26  A    N  
ATOM   1094  CA  PRO A 149      10.949 130.903 271.167  1.00 24.02      A    C  
ANISOU 1094  CA  PRO A 149     2258   3068   3801   -946    297     56  A    C  
ATOM   1095  C   PRO A 149       9.619 130.148 271.150  1.00 26.27      A    C  
ANISOU 1095  C   PRO A 149     2423   3367   4191  -1000    353     99  A    C  
ATOM   1096  O   PRO A 149       8.563 130.735 271.378  1.00 24.77      A    O  
ANISOU 1096  O   PRO A 149     2141   3204   4065   -976    443    110  A    O  
ATOM   1097  CB  PRO A 149      11.466 131.015 272.607  1.00 25.47      A    C  
ANISOU 1097  CB  PRO A 149     2575   3230   3870   -935    383     57  A    C  
ATOM   1098  CG  PRO A 149      12.142 132.361 272.677  1.00 27.56      A    C  
ANISOU 1098  CG  PRO A 149     2899   3493   4082   -858    368     11  A    C  
ATOM   1099  CD  PRO A 149      11.340 133.244 271.768  1.00 26.71      A    C  
ANISOU 1099  CD  PRO A 149     2661   3413   4076   -817    359      2  A    C  
ATOM   1100  N   ILE A 150       9.682 128.846 270.882  1.00 24.92      A    N  
ANISOU 1100  N   ILE A 150     2249   3173   4046  -1073    296    121  A    N  
ATOM   1101  CA  ILE A 150       8.502 127.993 270.939  1.00 23.96      A    C  
ANISOU 1101  CA  ILE A 150     2031   3058   4015  -1130    337    168  A    C  
ATOM   1102  C   ILE A 150       8.076 127.740 272.384  1.00 29.42      A    C  
ANISOU 1102  C   ILE A 150     2751   3742   4684  -1163    492    218  A    C  
ATOM   1103  O   ILE A 150       8.906 127.434 273.241  1.00 26.76      A    O  
ANISOU 1103  O   ILE A 150     2553   3381   4235  -1170    513    225  A    O  
ATOM   1104  CB  ILE A 150       8.747 126.634 270.238  1.00 26.29      A    C  
ANISOU 1104  CB  ILE A 150     2363   3334   4290  -1174    215    162  A    C  
ATOM   1105  CG1 ILE A 150       8.790 126.816 268.715  1.00 30.11      A    C  
ANISOU 1105  CG1 ILE A 150     2816   3848   4776  -1124     91    105  A    C  
ATOM   1106  CG2 ILE A 150       7.664 125.629 270.607  1.00 22.99      A    C  
ANISOU 1106  CG2 ILE A 150     1894   2913   3926  -1233    265    208  A    C  
ATOM   1107  CD1 ILE A 150       9.182 125.563 267.933  1.00 23.84      A    C  
ANISOU 1107  CD1 ILE A 150     2070   3030   3959  -1141    -12     67  A    C  
ATOM   1108  N   GLN A 151       6.784 127.905 272.657  1.00 31.05      A    N  
ANISOU 1108  N   GLN A 151     2846   3983   4971  -1165    593    253  A    N  
ATOM   1109  CA  GLN A 151       6.215 127.516 273.940  1.00 31.78      A    C  
ANISOU 1109  CA  GLN A 151     2948   4080   5048  -1201    748    313  A    C  
ATOM   1110  C   GLN A 151       5.278 126.332 273.716  1.00 36.21      A    C  
ANISOU 1110  C   GLN A 151     3443   4649   5668  -1262    712    367  A    C  
ATOM   1111  O   GLN A 151       4.701 126.196 272.633  1.00 33.96      A    O  
ANISOU 1111  O   GLN A 151     3075   4380   5448  -1255    611    342  A    O  
ATOM   1112  CB  GLN A 151       5.458 128.691 274.561  1.00 30.17      A    C  
ANISOU 1112  CB  GLN A 151     2691   3925   4849  -1132    895    304  A    C  
ATOM   1113  CG  GLN A 151       6.345 129.611 275.393  1.00 37.62      A    C  
ANISOU 1113  CG  GLN A 151     3788   4870   5636  -1054    938    259  A    C  
ATOM   1114  CD  GLN A 151       5.630 130.865 275.869  1.00 39.48      A    C  
ANISOU 1114  CD  GLN A 151     3974   5149   5878   -968   1061    233  A    C  
ATOM   1115  NE2 GLN A 151       6.403 131.878 276.243  1.00 39.94      A    N  
ANISOU 1115  NE2 GLN A 151     4145   5200   5828   -889   1057    173  A    N  
ATOM   1116  OE1 GLN A 151       4.401 130.923 275.898  1.00 42.68      A    O  
ANISOU 1116  OE1 GLN A 151     4237   5590   6389   -972   1155    263  A    O  
ATOM   1117  N   LEU A 152       5.136 125.479 274.732  1.00 39.45      A    N  
ANISOU 1117  N   LEU A 152     3898   5043   6047  -1323    797    434  A    N  
ATOM   1118  CA  LEU A 152       4.212 124.344 274.684  1.00 39.92      A    C  
ANISOU 1118  CA  LEU A 152     3899   5105   6165  -1392    784    483  A    C  
ATOM   1119  C   LEU A 152       3.072 124.550 275.687  1.00 45.12      A    C  
ANISOU 1119  C   LEU A 152     4486   5814   6844  -1393    957    546  A    C  
ATOM   1120  O   LEU A 152       3.308 124.983 276.815  1.00 46.15      A    O  
ANISOU 1120  O   LEU A 152     4680   5959   6897  -1372   1098    575  A    O  
ATOM   1121  CB  LEU A 152       4.936 123.016 274.950  1.00 38.98      A    C  
ANISOU 1121  CB  LEU A 152     3888   4921   6002  -1470    725    512  A    C  
ATOM   1122  CG  LEU A 152       6.031 122.617 273.951  1.00 38.83      A    C  
ANISOU 1122  CG  LEU A 152     3941   4850   5962  -1466    557    439  A    C  
ATOM   1123  CD1 LEU A 152       6.698 121.308 274.350  1.00 38.51      A    C  
ANISOU 1123  CD1 LEU A 152     4009   4731   5891  -1529    523    458  A    C  
ATOM   1124  CD2 LEU A 152       5.487 122.531 272.529  1.00 36.40      A    C  
ANISOU 1124  CD2 LEU A 152     3544   4557   5731  -1441    439    375  A    C  
ATOM   1125  N   PRO A 153       1.828 124.265 275.262  1.00 48.33      A    N  
ANISOU 1125  N   PRO A 153     4766   6249   7349  -1412    952    558  A    N  
ATOM   1126  CA  PRO A 153       0.607 124.505 276.045  1.00 49.97      A    C  
ANISOU 1126  CA  PRO A 153     4879   6513   7593  -1407   1107    610  A    C  
ATOM   1127  C   PRO A 153       0.559 123.795 277.399  1.00 45.98      A    C  
ANISOU 1127  C   PRO A 153     4439   6012   7020  -1465   1238    698  A    C  
ATOM   1128  O   PRO A 153      -0.024 124.338 278.340  1.00 48.22      A    O  
ANISOU 1128  O   PRO A 153     4695   6352   7274  -1430   1402    732  A    O  
ATOM   1129  CB  PRO A 153      -0.506 123.955 275.142  1.00 53.99      A    C  
ANISOU 1129  CB  PRO A 153     5260   7027   8228  -1441   1027    605  A    C  
ATOM   1130  CG  PRO A 153       0.071 123.943 273.776  1.00 54.53      A    C  
ANISOU 1130  CG  PRO A 153     5345   7059   8316  -1423    846    530  A    C  
ATOM   1131  CD  PRO A 153       1.530 123.669 273.947  1.00 50.01      A    C  
ANISOU 1131  CD  PRO A 153     4922   6438   7641  -1435    794    515  A    C  
ATOM   1132  N   PHE A 154       1.158 122.612 277.502  1.00 42.76      A    N  
ANISOU 1132  N   PHE A 154     4121   5543   6581  -1545   1170    731  A    N  
ATOM   1133  CA  PHE A 154       1.050 121.823 278.731  1.00 44.81      A    C  
ANISOU 1133  CA  PHE A 154     4444   5802   6779  -1609   1281    826  A    C  
ATOM   1134  C   PHE A 154       2.125 122.185 279.755  1.00 45.63      A    C  
ANISOU 1134  C   PHE A 154     4702   5901   6736  -1577   1360    850  A    C  
ATOM   1135  O   PHE A 154       2.188 121.603 280.837  1.00 47.26      A    O  
ANISOU 1135  O   PHE A 154     4987   6108   6863  -1618   1451    932  A    O  
ATOM   1136  CB  PHE A 154       1.065 120.316 278.427  1.00 45.06      A    C  
ANISOU 1136  CB  PHE A 154     4501   5761   6859  -1712   1180    852  A    C  
ATOM   1137  CG  PHE A 154       2.357 119.817 277.827  1.00 42.42      A    C  
ANISOU 1137  CG  PHE A 154     4284   5344   6490  -1725   1029    800  A    C  
ATOM   1138  CD1 PHE A 154       3.402 119.395 278.640  1.00 40.29      A    C  
ANISOU 1138  CD1 PHE A 154     4168   5029   6112  -1751   1045    841  A    C  
ATOM   1139  CD2 PHE A 154       2.513 119.742 276.450  1.00 40.77      A    C  
ANISOU 1139  CD2 PHE A 154     4034   5102   6353  -1704    872    711  A    C  
ATOM   1140  CE1 PHE A 154       4.586 118.927 278.093  1.00 37.69      A    C  
ANISOU 1140  CE1 PHE A 154     3943   4616   5762  -1755    913    782  A    C  
ATOM   1141  CE2 PHE A 154       3.693 119.272 275.896  1.00 41.82      A    C  
ANISOU 1141  CE2 PHE A 154     4271   5163   6455  -1703    743    654  A    C  
ATOM   1142  CZ  PHE A 154       4.731 118.864 276.720  1.00 40.85      A    C  
ANISOU 1142  CZ  PHE A 154     4292   4987   6241  -1726    766    686  A    C  
ATOM   1143  N   ILE A 155       2.980 123.135 279.392  1.00 42.73      A    N  
ANISOU 1143  N   ILE A 155     4383   5522   6329  -1502   1324    775  A    N  
ATOM   1144  CA  ILE A 155       4.042 123.601 280.276  1.00 42.60      A    C  
ANISOU 1144  CA  ILE A 155     4528   5489   6168  -1463   1399    767  A    C  
ATOM   1145  C   ILE A 155       3.666 124.921 280.961  1.00 43.52      A    C  
ANISOU 1145  C   ILE A 155     4639   5674   6221  -1370   1569    731  A    C  
ATOM   1146  O   ILE A 155       3.206 125.859 280.306  1.00 43.84      A    O  
ANISOU 1146  O   ILE A 155     4574   5747   6338  -1309   1563    667  A    O  
ATOM   1147  CB  ILE A 155       5.365 123.774 279.493  1.00 43.71      A    C  
ANISOU 1147  CB  ILE A 155     4756   5564   6289  -1451   1253    686  A    C  
ATOM   1148  CG1 ILE A 155       5.819 122.432 278.915  1.00 44.34      A    C  
ANISOU 1148  CG1 ILE A 155     4858   5573   6416  -1530   1089    717  A    C  
ATOM   1149  CG2 ILE A 155       6.455 124.365 280.376  1.00 44.70      A    C  
ANISOU 1149  CG2 ILE A 155     5071   5685   6229  -1398   1297    646  A    C  
ATOM   1150  CD1 ILE A 155       7.188 122.482 278.240  1.00 41.05      A    C  
ANISOU 1150  CD1 ILE A 155     4539   5094   5962  -1518    946    639  A    C  
ATOM   1151  N   PRO A 156       3.863 125.001 282.284  1.00 42.90      A    N  
ANISOU 1151  N   PRO A 156     4685   5620   5995  -1353   1714    767  A    N  
ATOM   1152  CA  PRO A 156       3.574 126.258 282.983  1.00 43.28      A    C  
ANISOU 1152  CA  PRO A 156     4750   5732   5961  -1255   1874    718  A    C  
ATOM   1153  C   PRO A 156       4.665 127.293 282.735  1.00 42.83      A    C  
ANISOU 1153  C   PRO A 156     4810   5652   5812  -1170   1788    601  A    C  
ATOM   1154  O   PRO A 156       5.492 127.521 283.620  1.00 43.86      A    O  
ANISOU 1154  O   PRO A 156     5122   5779   5765  -1128   1803    578  A    O  
ATOM   1155  CB  PRO A 156       3.569 125.843 284.457  1.00 45.26      A    C  
ANISOU 1155  CB  PRO A 156     5128   6016   6051  -1261   2012    792  A    C  
ATOM   1156  CG  PRO A 156       4.452 124.643 284.513  1.00 46.22      A    C  
ANISOU 1156  CG  PRO A 156     5366   6064   6131  -1350   1903    849  A    C  
ATOM   1157  CD  PRO A 156       4.249 123.921 283.210  1.00 46.19      A    C  
ANISOU 1157  CD  PRO A 156     5227   6012   6313  -1418   1736    858  A    C  
ATOM   1158  N   HIS A 157       4.652 127.928 281.562  1.00 43.89      A    N  
ANISOU 1158  N   HIS A 157     4844   5775   6058  -1135   1677    529  A    N  
ATOM   1159  CA  HIS A 157       5.724 128.839 281.169  1.00 42.92      A    C  
ANISOU 1159  CA  HIS A 157     4821   5625   5862  -1058   1554    427  A    C  
ATOM   1160  C   HIS A 157       5.691 130.122 281.987  1.00 46.95      A    C  
ANISOU 1160  C   HIS A 157     5399   6175   6264   -945   1661    363  A    C  
ATOM   1161  O   HIS A 157       6.541 130.999 281.816  1.00 48.89      A    O  
ANISOU 1161  O   HIS A 157     5732   6397   6446   -875   1574    278  A    O  
ATOM   1162  CB  HIS A 157       5.582 129.221 279.690  1.00 43.81      A    C  
ANISOU 1162  CB  HIS A 157     4798   5723   6126  -1049   1423    380  A    C  
ATOM   1163  CG  HIS A 157       6.084 128.189 278.728  1.00 44.03      A    C  
ANISOU 1163  CG  HIS A 157     4809   5697   6222  -1132   1261    400  A    C  
ATOM   1164  CD2 HIS A 157       5.427 127.248 278.004  1.00 43.47      A    C  
ANISOU 1164  CD2 HIS A 157     4608   5612   6296  -1216   1219    452  A    C  
ATOM   1165  ND1 HIS A 157       7.418 128.059 278.402  1.00 39.66      A    N  
ANISOU 1165  ND1 HIS A 157     4383   5095   5590  -1129   1116    358  A    N  
ATOM   1166  CE1 HIS A 157       7.561 127.084 277.521  1.00 40.39      A    C  
ANISOU 1166  CE1 HIS A 157     4428   5151   5769  -1201    997    380  A    C  
ATOM   1167  NE2 HIS A 157       6.370 126.573 277.266  1.00 43.16      A    N  
ANISOU 1167  NE2 HIS A 157     4627   5518   6254  -1256   1051    435  A    N  
ATOM   1168  N   GLU A 158       4.733 130.213 282.901  1.00 45.95      A    N  
ANISOU 1168  N   GLU A 158     5236   6109   6116   -927   1851    403  A    N  
ATOM   1169  CA  GLU A 158       4.608 131.373 283.768  1.00 52.07      A    C  
ANISOU 1169  CA  GLU A 158     6077   6925   6782   -815   1969    338  A    C  
ATOM   1170  C   GLU A 158       5.350 131.195 285.088  1.00 50.76      A    C  
ANISOU 1170  C   GLU A 158     6125   6762   6400   -798   2024    344  A    C  
ATOM   1171  O   GLU A 158       5.538 132.157 285.829  1.00 53.15      A    O  
ANISOU 1171  O   GLU A 158     6527   7085   6582   -699   2086    272  A    O  
ATOM   1172  CB  GLU A 158       3.131 131.756 283.975  1.00 63.09      A    C  
ANISOU 1172  CB  GLU A 158     7304   8393   8274   -781   2149    360  A    C  
ATOM   1173  CG  GLU A 158       2.267 130.716 284.690  1.00 73.60      A    C  
ANISOU 1173  CG  GLU A 158     8578   9770   9614   -859   2309    479  A    C  
ATOM   1174  CD  GLU A 158       1.882 129.547 283.785  1.00 79.80      A    C  
ANISOU 1174  CD  GLU A 158     9229  10526  10564   -979   2208    563  A    C  
ATOM   1175  OE1 GLU A 158       2.201 129.595 282.577  1.00 81.92      A    O  
ANISOU 1175  OE1 GLU A 158     9432  10745  10948  -1002   2058    526  A    O  
ATOM   1176  OE2 GLU A 158       1.246 128.587 284.273  1.00 82.35      A    O1-
ANISOU 1176  OE2 GLU A 158     9518  10880  10892  -1040   2251    661  A    O1-
ATOM   1177  N   ASP A 159       5.790 129.971 285.366  1.00 45.32      A    N  
ANISOU 1177  N   ASP A 159     5512   6046   5662   -892   1990    426  A    N  
ATOM   1178  CA  ASP A 159       6.629 129.716 286.531  1.00 41.02      A    C  
ANISOU 1178  CA  ASP A 159     5182   5494   4910   -882   2008    436  A    C  
ATOM   1179  C   ASP A 159       8.031 130.205 286.194  1.00 40.84      A    C  
ANISOU 1179  C   ASP A 159     5292   5406   4821   -843   1822    345  A    C  
ATOM   1180  O   ASP A 159       8.532 129.957 285.096  1.00 42.60      A    O  
ANISOU 1180  O   ASP A 159     5461   5577   5147   -883   1664    331  A    O  
ATOM   1181  CB  ASP A 159       6.647 128.226 286.874  1.00 38.97      A    C  
ANISOU 1181  CB  ASP A 159     4954   5217   4636   -997   2019    560  A    C  
ATOM   1182  CG  ASP A 159       7.262 127.944 288.235  1.00 43.03      A    C  
ANISOU 1182  CG  ASP A 159     5681   5738   4930   -985   2075    590  A    C  
ATOM   1183  OD1 ASP A 159       6.508 127.631 289.184  1.00 47.84      A    O  
ANISOU 1183  OD1 ASP A 159     6298   6409   5472   -996   2256    669  A    O  
ATOM   1184  OD2 ASP A 159       8.502 128.039 288.354  1.00 39.96      A    O1-
ANISOU 1184  OD2 ASP A 159     5451   5298   4436   -964   1938    539  A    O1-
ATOM   1185  N   PRO A 160       8.669 130.915 287.134  1.00 38.69      A    N  
ANISOU 1185  N   PRO A 160     5190   5138   4374   -762   1840    282  A    N  
ATOM   1186  CA  PRO A 160       9.985 131.501 286.856  1.00 39.14      A    C  
ANISOU 1186  CA  PRO A 160     5363   5132   4377   -721   1667    192  A    C  
ATOM   1187  C   PRO A 160      11.074 130.453 286.655  1.00 40.59      A    C  
ANISOU 1187  C   PRO A 160     5636   5253   4533   -800   1517    235  A    C  
ATOM   1188  O   PRO A 160      12.144 130.771 286.129  1.00 39.97      A    O  
ANISOU 1188  O   PRO A 160     5610   5121   4457   -785   1357    174  A    O  
ATOM   1189  CB  PRO A 160      10.284 132.300 288.130  1.00 40.43      A    C  
ANISOU 1189  CB  PRO A 160     5696   5316   4348   -627   1740    130  A    C  
ATOM   1190  CG  PRO A 160       8.956 132.490 288.798  1.00 39.59      A    C  
ANISOU 1190  CG  PRO A 160     5520   5293   4229   -592   1960    159  A    C  
ATOM   1191  CD  PRO A 160       8.177 131.266 288.476  1.00 35.27      A    C  
ANISOU 1191  CD  PRO A 160     4845   4768   3790   -701   2022    284  A    C  
ATOM   1192  N   ARG A 161      10.801 129.217 287.056  1.00 39.14      A    N  
ANISOU 1192  N   ARG A 161     5463   5075   4332   -884   1569    341  A    N  
ATOM   1193  CA  ARG A 161      11.782 128.154 286.905  1.00 34.22      A    C  
ANISOU 1193  CA  ARG A 161     4923   4388   3689   -957   1429    385  A    C  
ATOM   1194  C   ARG A 161      11.707 127.477 285.535  1.00 33.72      A    C  
ANISOU 1194  C   ARG A 161     4713   4287   3812  -1031   1319    409  A    C  
ATOM   1195  O   ARG A 161      12.531 126.619 285.214  1.00 32.23      A    O  
ANISOU 1195  O   ARG A 161     4574   4041   3632  -1086   1189    432  A    O  
ATOM   1196  CB  ARG A 161      11.628 127.130 288.032  1.00 33.35      A    C  
ANISOU 1196  CB  ARG A 161     4917   4290   3464  -1011   1522    490  A    C  
ATOM   1197  CG  ARG A 161      11.924 127.698 289.420  1.00 32.56      A    C  
ANISOU 1197  CG  ARG A 161     5000   4222   3148   -936   1604    463  A    C  
ATOM   1198  CD  ARG A 161      11.388 126.777 290.502  1.00 37.57      A    C  
ANISOU 1198  CD  ARG A 161     5700   4893   3681   -986   1745    584  A    C  
ATOM   1199  NE  ARG A 161       9.933 126.671 290.437  1.00 38.38      A    N  
ANISOU 1199  NE  ARG A 161     5637   5063   3883  -1012   1925    649  A    N  
ATOM   1200  CZ  ARG A 161       9.200 125.889 291.222  1.00 41.52      A    C  
ANISOU 1200  CZ  ARG A 161     6039   5503   4235  -1065   2077    769  A    C  
ATOM   1201  NH1 ARG A 161       9.781 125.126 292.137  1.00 39.05      A    N1+
ANISOU 1201  NH1 ARG A 161     5897   5171   3770  -1099   2069    842  A    N1+
ATOM   1202  NH2 ARG A 161       7.882 125.862 291.080  1.00 43.45      A    N  
ANISOU 1202  NH2 ARG A 161     6112   5808   4590  -1087   2237    823  A    N  
ATOM   1203  N   ILE A 162      10.726 127.869 284.727  1.00 28.80      A    N  
ANISOU 1203  N   ILE A 162     3910   3697   3335  -1027   1366    398  A    N  
ATOM   1204  CA  ILE A 162      10.659 127.418 283.341  1.00 33.04      A    C  
ANISOU 1204  CA  ILE A 162     4308   4202   4042  -1080   1249    400  A    C  
ATOM   1205  C   ILE A 162      11.276 128.503 282.469  1.00 31.27      A    C  
ANISOU 1205  C   ILE A 162     4065   3965   3851  -1011   1136    298  A    C  
ATOM   1206  O   ILE A 162      10.736 129.605 282.360  1.00 33.39      A    O  
ANISOU 1206  O   ILE A 162     4270   4270   4149   -943   1197    247  A    O  
ATOM   1207  CB  ILE A 162       9.209 127.160 282.884  1.00 35.74      A    C  
ANISOU 1207  CB  ILE A 162     4456   4584   4538  -1122   1350    454  A    C  
ATOM   1208  CG1 ILE A 162       8.530 126.135 283.798  1.00 38.05      A    C  
ANISOU 1208  CG1 ILE A 162     4758   4893   4805  -1195   1480    568  A    C  
ATOM   1209  CG2 ILE A 162       9.181 126.695 281.429  1.00 30.07      A    C  
ANISOU 1209  CG2 ILE A 162     3608   3832   3986  -1173   1212    448  A    C  
ATOM   1210  CD1 ILE A 162       9.236 124.796 283.850  1.00 36.27      A    C  
ANISOU 1210  CD1 ILE A 162     4618   4602   4562  -1282   1380    633  A    C  
ATOM   1211  N   TRP A 163      12.410 128.184 281.851  1.00 32.28      A    N  
ANISOU 1211  N   TRP A 163     4246   4039   3979  -1029    972    271  A    N  
ATOM   1212  CA  TRP A 163      13.199 129.170 281.121  1.00 30.73      A    C  
ANISOU 1212  CA  TRP A 163     4054   3827   3795   -968    859    184  A    C  
ATOM   1213  C   TRP A 163      13.086 129.024 279.607  1.00 29.45      A    C  
ANISOU 1213  C   TRP A 163     3750   3657   3782   -994    757    173  A    C  
ATOM   1214  O   TRP A 163      12.942 127.912 279.087  1.00 26.46      A    O  
ANISOU 1214  O   TRP A 163     3319   3260   3474  -1066    711    219  A    O  
ATOM   1215  CB  TRP A 163      14.679 129.001 281.469  1.00 33.19      A    C  
ANISOU 1215  CB  TRP A 163     4525   4088   3997   -961    743    158  A    C  
ATOM   1216  CG  TRP A 163      15.046 129.275 282.892  1.00 32.75      A    C  
ANISOU 1216  CG  TRP A 163     4633   4032   3778   -924    805    152  A    C  
ATOM   1217  CD1 TRP A 163      14.229 129.728 283.887  1.00 33.31      A    C  
ANISOU 1217  CD1 TRP A 163     4731   4149   3777   -887    960    160  A    C  
ATOM   1218  CD2 TRP A 163      16.347 129.129 283.472  1.00 30.93      A    C  
ANISOU 1218  CD2 TRP A 163     4565   3757   3431   -914    708    132  A    C  
ATOM   1219  CE2 TRP A 163      16.243 129.499 284.827  1.00 31.40      A    C  
ANISOU 1219  CE2 TRP A 163     4752   3835   3343   -872    804    128  A    C  
ATOM   1220  CE3 TRP A 163      17.587 128.713 282.977  1.00 27.81      A    C  
ANISOU 1220  CE3 TRP A 163     4216   3308   3041   -933    548    115  A    C  
ATOM   1221  NE1 TRP A 163      14.943 129.863 285.057  1.00 31.10      A    N  
ANISOU 1221  NE1 TRP A 163     4631   3856   3332   -854    963    144  A    N  
ATOM   1222  CZ2 TRP A 163      17.338 129.471 285.690  1.00 35.12      A    C  
ANISOU 1222  CZ2 TRP A 163     5400   4270   3675   -851    735    108  A    C  
ATOM   1223  CZ3 TRP A 163      18.668 128.685 283.833  1.00 26.41      A    C  
ANISOU 1223  CZ3 TRP A 163     4202   3094   2737   -914    483     99  A    C  
ATOM   1224  CH2 TRP A 163      18.538 129.061 285.174  1.00 32.52      A    C  
ANISOU 1224  CH2 TRP A 163     5105   3884   3367   -875    571     96  A    C  
ATOM   1225  N   ASP A 164      13.170 130.149 278.900  1.00 22.02      A    N  
ANISOU 1225  N   ASP A 164     2755   2727   2886   -933    717    111  A    N  
ATOM   1226  CA  ASP A 164      13.576 130.114 277.500  1.00 23.58      A    C  
ANISOU 1226  CA  ASP A 164     2873   2911   3176   -945    583     88  A    C  
ATOM   1227  C   ASP A 164      15.011 130.625 277.425  1.00 20.99      A    C  
ANISOU 1227  C   ASP A 164     2653   2548   2774   -907    472     36  A    C  
ATOM   1228  O   ASP A 164      15.632 130.864 278.463  1.00 21.50      A    O  
ANISOU 1228  O   ASP A 164     2851   2594   2725   -881    490     21  A    O  
ATOM   1229  CB  ASP A 164      12.625 130.896 276.582  1.00 32.25      A    C  
ANISOU 1229  CB  ASP A 164     3815   4044   4394   -914    603     71  A    C  
ATOM   1230  CG  ASP A 164      12.528 132.374 276.940  1.00 35.60      A    C  
ANISOU 1230  CG  ASP A 164     4255   4482   4790   -827    655     19  A    C  
ATOM   1231  OD1 ASP A 164      13.406 132.894 277.661  1.00 36.36      A    O  
ANISOU 1231  OD1 ASP A 164     4483   4554   4780   -787    641    -17  A    O  
ATOM   1232  OD2 ASP A 164      11.565 133.024 276.478  1.00 36.94      A    O1-
ANISOU 1232  OD2 ASP A 164     4303   4682   5052   -796    701     13  A    O1-
ATOM   1233  N   SER A 165      15.534 130.786 276.215  1.00 21.48      A    N  
ANISOU 1233  N   SER A 165     2210   2546   3404   -273    634    -91  A    N  
ATOM   1234  CA  SER A 165      16.924 131.193 276.039  1.00 22.86      A    C  
ANISOU 1234  CA  SER A 165     2554   2689   3443   -249    546   -113  A    C  
ATOM   1235  C   SER A 165      17.254 132.544 276.690  1.00 24.41      A    C  
ANISOU 1235  C   SER A 165     2832   2880   3565   -155    579   -167  A    C  
ATOM   1236  O   SER A 165      18.351 132.733 277.218  1.00 18.61      A    O  
ANISOU 1236  O   SER A 165     2241   2142   2687   -158    572   -177  A    O  
ATOM   1237  CB  SER A 165      17.290 131.213 274.552  1.00 21.14      A    C  
ANISOU 1237  CB  SER A 165     2324   2455   3254   -272    371   -120  A    C  
ATOM   1238  OG  SER A 165      16.343 131.960 273.813  1.00 23.19      A    O  
ANISOU 1238  OG  SER A 165     2456   2720   3634   -233    309   -128  A    O  
ATOM   1239  N   THR A 166      16.314 133.483 276.640  1.00 25.69      A    N  
ANISOU 1239  N   THR A 166     2899   3031   3831    -69    602   -207  A    N  
ATOM   1240  CA  THR A 166      16.521 134.792 277.262  1.00 22.78      A    C  
ANISOU 1240  CA  THR A 166     2621   2618   3417     32    628   -284  A    C  
ATOM   1241  C   THR A 166      16.708 134.671 278.778  1.00 26.88      A    C  
ANISOU 1241  C   THR A 166     3228   3192   3795     47    792   -328  A    C  
ATOM   1242  O   THR A 166      17.663 135.227 279.350  1.00 23.98      A    O  
ANISOU 1242  O   THR A 166     3023   2799   3291     53    772   -377  A    O  
ATOM   1243  CB  THR A 166      15.361 135.761 276.918  1.00 26.58      A    C  
ANISOU 1243  CB  THR A 166     2972   3062   4066    155    622   -325  A    C  
ATOM   1244  CG2 THR A 166      15.544 137.114 277.607  1.00 21.81      A    C  
ANISOU 1244  CG2 THR A 166     2484   2369   3433    277    647   -430  A    C  
ATOM   1245  OG1 THR A 166      15.333 135.963 275.499  1.00 25.86      A    O  
ANISOU 1245  OG1 THR A 166     2828   2928   4069    134    443   -266  A    O  
ATOM   1246  N   ASP A 167      15.817 133.912 279.414  1.00 31.72      A    N  
ANISOU 1246  N   ASP A 167     3728   3895   4428     34    945   -300  A    N  
ATOM   1247  CA  ASP A 167      15.912 133.637 280.846  1.00 34.33      A    C  
ANISOU 1247  CA  ASP A 167     4129   4316   4597     31   1113   -312  A    C  
ATOM   1248  C   ASP A 167      17.269 133.027 281.192  1.00 33.08      A    C  
ANISOU 1248  C   ASP A 167     4146   4156   4267    -55   1054   -258  A    C  
ATOM   1249  O   ASP A 167      17.909 133.419 282.170  1.00 32.88      A    O  
ANISOU 1249  O   ASP A 167     4258   4169   4067    -35   1095   -307  A    O  
ATOM   1250  CB  ASP A 167      14.796 132.686 281.285  1.00 38.10      A    C  
ANISOU 1250  CB  ASP A 167     4443   4906   5130    -19   1273   -236  A    C  
ATOM   1251  CG  ASP A 167      13.412 133.252 281.034  1.00 40.83      A    C  
ANISOU 1251  CG  ASP A 167     4572   5295   5646     76   1345   -287  A    C  
ATOM   1252  OD1 ASP A 167      13.190 134.444 281.332  1.00 44.94      A    O  
ANISOU 1252  OD1 ASP A 167     5105   5802   6167    228   1381   -413  A    O  
ATOM   1253  OD2 ASP A 167      12.549 132.504 280.524  1.00 38.13      A    O1-
ANISOU 1253  OD2 ASP A 167     4044   4994   5448      1   1354   -205  A    O1-
ATOM   1254  N   ALA A 168      17.696 132.061 280.383  1.00 26.96      A    N  
ANISOU 1254  N   ALA A 168     3359   3343   3540   -143    950   -166  A    N  
ATOM   1255  CA  ALA A 168      18.970 131.394 280.594  1.00 23.26      A    C  
ANISOU 1255  CA  ALA A 168     3026   2874   2938   -199    883   -108  A    C  
ATOM   1256  C   ALA A 168      20.111 132.398 280.504  1.00 25.57      A    C  
ANISOU 1256  C   ALA A 168     3440   3146   3130   -169    772   -177  A    C  
ATOM   1257  O   ALA A 168      21.049 132.368 281.306  1.00 21.13      A    O  
ANISOU 1257  O   ALA A 168     2997   2630   2401   -183    766   -171  A    O  
ATOM   1258  CB  ALA A 168      19.162 130.300 279.566  1.00 23.30      A    C  
ANISOU 1258  CB  ALA A 168     2988   2824   3041   -265    783    -37  A    C  
ATOM   1259  N   LEU A 169      20.026 133.299 279.531  1.00 22.30      A    N  
ANISOU 1259  N   LEU A 169     2990   2666   2815   -140    674   -229  A    N  
ATOM   1260  CA  LEU A 169      21.100 134.266 279.338  1.00 25.07      A    C  
ANISOU 1260  CA  LEU A 169     3449   2986   3092   -146    556   -272  A    C  
ATOM   1261  C   LEU A 169      21.066 135.365 280.401  1.00 28.04      A    C  
ANISOU 1261  C   LEU A 169     3924   3344   3385    -95    612   -380  A    C  
ATOM   1262  O   LEU A 169      22.028 136.117 280.555  1.00 31.84      A    O  
ANISOU 1262  O   LEU A 169     4519   3800   3779   -126    521   -421  A    O  
ATOM   1263  CB  LEU A 169      21.057 134.861 277.928  1.00 16.20      A    C  
ANISOU 1263  CB  LEU A 169     2269   1796   2090   -151    424   -262  A    C  
ATOM   1264  CG  LEU A 169      21.357 133.862 276.807  1.00 23.61      A    C  
ANISOU 1264  CG  LEU A 169     3138   2771   3061   -206    345   -189  A    C  
ATOM   1265  CD1 LEU A 169      21.078 134.485 275.443  1.00 26.74      A    C  
ANISOU 1265  CD1 LEU A 169     3470   3132   3558   -209    228   -173  A    C  
ATOM   1266  CD2 LEU A 169      22.789 133.357 276.885  1.00 22.55      A    C  
ANISOU 1266  CD2 LEU A 169     3078   2702   2788   -254    290   -157  A    C  
ATOM   1267  N   GLU A 170      19.968 135.462 281.141  1.00 28.01      A    N  
ANISOU 1267  N   GLU A 170     3875   3363   3405    -21    763   -435  A    N  
ATOM   1268  CA  GLU A 170      19.932 136.424 282.247  1.00 36.17      A    C  
ANISOU 1268  CA  GLU A 170     5017   4394   4332     45    834   -570  A    C  
ATOM   1269  C   GLU A 170      20.798 135.998 283.444  1.00 35.77      A    C  
ANISOU 1269  C   GLU A 170     5095   4456   4040    -10    872   -568  A    C  
ATOM   1270  O   GLU A 170      21.152 136.831 284.287  1.00 27.85      A    O  
ANISOU 1270  O   GLU A 170     4222   3453   2906     13    877   -692  A    O  
ATOM   1271  CB  GLU A 170      18.495 136.720 282.679  1.00 41.00      A    C  
ANISOU 1271  CB  GLU A 170     5523   5028   5027    166    999   -648  A    C  
ATOM   1272  CG  GLU A 170      17.775 137.670 281.730  1.00 49.64      A    C  
ANISOU 1272  CG  GLU A 170     6534   5987   6339    263    929   -698  A    C  
ATOM   1273  CD  GLU A 170      16.327 137.889 282.116  1.00 60.24      A    C  
ANISOU 1273  CD  GLU A 170     7728   7378   7782    403   1095   -771  A    C  
ATOM   1274  OE1 GLU A 170      15.910 137.373 283.177  1.00 61.62      A    O  
ANISOU 1274  OE1 GLU A 170     7872   7704   7835    414   1281   -792  A    O  
ATOM   1275  OE2 GLU A 170      15.603 138.567 281.353  1.00 66.67      A    O1-
ANISOU 1275  OE2 GLU A 170     8443   8096   8792    505   1040   -794  A    O1-
ATOM   1276  N   LEU A 171      21.140 134.710 283.505  1.00 34.37      A    N  
ANISOU 1276  N   LEU A 171     4890   4364   3807    -80    884   -429  A    N  
ATOM   1277  CA  LEU A 171      22.029 134.188 284.544  1.00 36.05      A    C  
ANISOU 1277  CA  LEU A 171     5214   4687   3795   -130    890   -385  A    C  
ATOM   1278  C   LEU A 171      21.498 134.524 285.939  1.00 38.67      A    C  
ANISOU 1278  C   LEU A 171     5613   5125   3957    -84   1048   -474  A    C  
ATOM   1279  O   LEU A 171      22.196 135.136 286.752  1.00 34.80      A    O  
ANISOU 1279  O   LEU A 171     5261   4680   3280    -91   1012   -566  A    O  
ATOM   1280  CB  LEU A 171      23.429 134.791 284.374  1.00 39.76      A    C  
ANISOU 1280  CB  LEU A 171     5788   5135   4183   -182    713   -418  A    C  
ATOM   1281  CG  LEU A 171      24.575 133.894 283.904  1.00 41.30      A    C  
ANISOU 1281  CG  LEU A 171     5970   5373   4351   -244    591   -287  A    C  
ATOM   1282  CD1 LEU A 171      25.895 134.651 284.004  1.00 39.15      A    C  
ANISOU 1282  CD1 LEU A 171     5780   5126   3967   -304    440   -333  A    C  
ATOM   1283  CD2 LEU A 171      24.631 132.592 284.679  1.00 40.40      A    C  
ANISOU 1283  CD2 LEU A 171     5865   5355   4130   -249    661   -160  A    C  
ATOM   1284  N   LYS A 172      20.259 134.126 286.207  1.00 41.31      A    N  
ANISOU 1284  N   LYS A 172     5839   5514   4343    -45   1225   -451  A    N  
ATOM   1285  CA  LYS A 172      19.599 134.454 287.466  1.00 40.14      A    C  
ANISOU 1285  CA  LYS A 172     5722   5501   4028     13   1411   -544  A    C  
ATOM   1286  C   LYS A 172      20.215 133.679 288.626  1.00 38.17      A    C  
ANISOU 1286  C   LYS A 172     5581   5415   3507    -59   1453   -442  A    C  
ATOM   1287  O   LYS A 172      20.294 134.181 289.749  1.00 38.62      A    O  
ANISOU 1287  O   LYS A 172     5747   5595   3331    -29   1531   -551  A    O  
ATOM   1288  CB  LYS A 172      18.105 134.140 287.368  1.00 44.08      A    C  
ANISOU 1288  CB  LYS A 172     6031   6052   4666     59   1596   -517  A    C  
ATOM   1289  CG  LYS A 172      17.392 134.888 286.248  1.00 51.13      A    C  
ANISOU 1289  CG  LYS A 172     6796   6803   5828    147   1547   -602  A    C  
ATOM   1290  CD  LYS A 172      15.887 134.698 286.329  1.00 58.25      A    C  
ANISOU 1290  CD  LYS A 172     7487   7799   6846    206   1738   -597  A    C  
ATOM   1291  CE  LYS A 172      15.507 133.246 286.092  1.00 59.21      A    C  
ANISOU 1291  CE  LYS A 172     7483   7981   7032     70   1781   -380  A    C  
ATOM   1292  NZ  LYS A 172      14.036 133.021 286.225  1.00 63.88      A    N1+
ANISOU 1292  NZ  LYS A 172     7841   8696   7733     95   1971   -357  A    N1+
ATOM   1293  N   GLU A 173      20.653 132.456 288.337  1.00 33.79      A    N  
ANISOU 1293  N   GLU A 173     5005   4855   2980   -146   1391   -235  A    N  
ATOM   1294  CA  GLU A 173      21.243 131.572 289.335  1.00 34.67      A    C  
ANISOU 1294  CA  GLU A 173     5213   5099   2863   -210   1405    -86  A    C  
ATOM   1295  C   GLU A 173      21.895 130.394 288.629  1.00 33.10      A    C  
ANISOU 1295  C   GLU A 173     4992   4805   2781   -270   1272    107  A    C  
ATOM   1296  O   GLU A 173      21.771 130.238 287.417  1.00 36.37      A    O  
ANISOU 1296  O   GLU A 173     5311   5076   3431   -268   1197    109  A    O  
ATOM   1297  CB  GLU A 173      20.180 131.017 290.283  1.00 36.32      A    C  
ANISOU 1297  CB  GLU A 173     5352   5464   2983   -222   1607      4  A    C  
ATOM   1298  CG  GLU A 173      19.204 130.065 289.596  1.00 44.07      A    C  
ANISOU 1298  CG  GLU A 173     6182   6380   4181   -283   1709    151  A    C  
ATOM   1299  CD  GLU A 173      18.117 129.562 290.530  1.00 58.57      A    C  
ANISOU 1299  CD  GLU A 173     7907   8395   5954   -310   1877    255  A    C  
ATOM   1300  OE1 GLU A 173      18.432 129.250 291.700  1.00 63.38      A    O  
ANISOU 1300  OE1 GLU A 173     8585   9164   6331   -326   1883    344  A    O  
ATOM   1301  OE2 GLU A 173      16.950 129.468 290.094  1.00 62.34      A    O1-
ANISOU 1301  OE2 GLU A 173     8210   8870   6606   -321   1996    258  A    O1-
ATOM   1302  N   VAL A 174      22.615 129.582 289.391  1.00 31.19      A    N  
ANISOU 1302  N   VAL A 174     4843   4645   2363   -312   1233    261  A    N  
ATOM   1303  CA  VAL A 174      23.145 128.330 288.881  1.00 31.06      A    C  
ANISOU 1303  CA  VAL A 174     4815   4530   2455   -344   1126    451  A    C  
ATOM   1304  C   VAL A 174      22.330 127.207 289.504  1.00 32.40      A    C  
ANISOU 1304  C   VAL A 174     4970   4733   2607   -411   1267    654  A    C  
ATOM   1305  O   VAL A 174      22.565 126.828 290.648  1.00 35.30      A    O  
ANISOU 1305  O   VAL A 174     5399   5236   2777   -426   1277    771  A    O  
ATOM   1306  CB  VAL A 174      24.646 128.184 289.209  1.00 32.27      A    C  
ANISOU 1306  CB  VAL A 174     5074   4731   2455   -328    948    502  A    C  
ATOM   1307  CG1 VAL A 174      25.203 126.864 288.686  1.00 32.73      A    C  
ANISOU 1307  CG1 VAL A 174     5120   4676   2642   -321    839    685  A    C  
ATOM   1308  CG2 VAL A 174      25.426 129.369 288.638  1.00 26.33      A    C  
ANISOU 1308  CG2 VAL A 174     4323   3964   1716   -298    818    312  A    C  
ATOM   1309  N   PRO A 175      21.341 126.689 288.758  1.00 32.70      A    N  
ANISOU 1309  N   PRO A 175     4884   4657   2883   -451   1335    695  A    N  
ATOM   1310  CA  PRO A 175      20.506 125.610 289.296  1.00 35.16      A    C  
ANISOU 1310  CA  PRO A 175     5168   4986   3205   -552   1466    905  A    C  
ATOM   1311  C   PRO A 175      21.340 124.358 289.532  1.00 35.96      A    C  
ANISOU 1311  C   PRO A 175     5382   4999   3283   -585   1346   1130  A    C  
ATOM   1312  O   PRO A 175      22.191 124.023 288.708  1.00 33.46      A    O  
ANISOU 1312  O   PRO A 175     5089   4530   3095   -530   1169   1115  A    O  
ATOM   1313  CB  PRO A 175      19.462 125.380 288.193  1.00 31.75      A    C  
ANISOU 1313  CB  PRO A 175     4570   4420   3073   -595   1501    872  A    C  
ATOM   1314  CG  PRO A 175      20.044 125.985 286.967  1.00 34.77      A    C  
ANISOU 1314  CG  PRO A 175     4930   4681   3601   -511   1338    700  A    C  
ATOM   1315  CD  PRO A 175      20.909 127.118 287.418  1.00 29.48      A    C  
ANISOU 1315  CD  PRO A 175     4353   4116   2732   -424   1290    559  A    C  
ATOM   1316  N   GLU A 176      21.096 123.682 290.648  1.00 39.04      A    N  
ANISOU 1316  N   GLU A 176     5783   5502   3547   -646   1386   1316  A    N  
ATOM   1317  CA  GLU A 176      21.845 122.485 290.987  1.00 42.13      A    C  
ANISOU 1317  CA  GLU A 176     6279   5805   3923   -669   1259   1550  A    C  
ATOM   1318  C   GLU A 176      21.585 121.427 289.926  1.00 40.72      A    C  
ANISOU 1318  C   GLU A 176     6096   5337   4041   -722   1211   1643  A    C  
ATOM   1319  O   GLU A 176      22.506 120.753 289.460  1.00 33.27      A    O  
ANISOU 1319  O   GLU A 176     5250   4211   3179   -656   1062   1713  A    O  
ATOM   1320  CB  GLU A 176      21.412 121.984 292.362  1.00 44.92      A    C  
ANISOU 1320  CB  GLU A 176     6624   6334   4110   -742   1326   1734  A    C  
ATOM   1321  CG  GLU A 176      22.182 120.792 292.888  1.00 52.39      A    C  
ANISOU 1321  CG  GLU A 176     7856   7038   5010   -733   1261   1893  A    C  
ATOM   1322  CD  GLU A 176      21.675 120.370 294.253  1.00 65.00      A    C  
ANISOU 1322  CD  GLU A 176     9527   8739   6433   -778   1400   2046  A    C  
ATOM   1323  OE1 GLU A 176      20.684 120.973 294.721  1.00 68.44      A    O  
ANISOU 1323  OE1 GLU A 176     9880   9332   6793   -814   1595   1964  A    O  
ATOM   1324  OE2 GLU A 176      22.258 119.443 294.854  1.00 67.42      A    O1-
ANISOU 1324  OE2 GLU A 176     9973   8974   6670   -778   1311   2250  A    O1-
ATOM   1325  N   ARG A 177      20.327 121.328 289.510  1.00 39.12      A    N  
ANISOU 1325  N   ARG A 177     5761   5094   4007   -824   1330   1623  A    N  
ATOM   1326  CA  ARG A 177      19.946 120.385 288.474  1.00 39.36      A    C  
ANISOU 1326  CA  ARG A 177     5764   4854   4336   -893   1276   1678  A    C  
ATOM   1327  C   ARG A 177      19.102 121.065 287.405  1.00 41.10      A    C  
ANISOU 1327  C   ARG A 177     5820   5053   4743   -901   1335   1474  A    C  
ATOM   1328  O   ARG A 177      18.016 121.580 287.686  1.00 40.63      A    O  
ANISOU 1328  O   ARG A 177     5622   5148   4667   -965   1492   1435  A    O  
ATOM   1329  CB  ARG A 177      19.177 119.215 289.083  1.00 43.02      A    C  
ANISOU 1329  CB  ARG A 177     6228   5270   4847  -1073   1296   1897  A    C  
ATOM   1330  CG  ARG A 177      19.131 117.999 288.194  1.00 51.62      A    C  
ANISOU 1330  CG  ARG A 177     7365   6027   6221  -1135   1173   1969  A    C  
ATOM   1331  CD  ARG A 177      18.454 116.831 288.880  1.00 62.89      A    C  
ANISOU 1331  CD  ARG A 177     8881   7347   7667  -1306   1222   2150  A    C  
ATOM   1332  NE  ARG A 177      18.441 115.653 288.019  1.00 68.80      A    N  
ANISOU 1332  NE  ARG A 177     9690   7752   8698  -1346   1093   2187  A    N  
ATOM   1333  CZ  ARG A 177      17.514 114.701 288.063  1.00 73.84      A    C  
ANISOU 1333  CZ  ARG A 177    10327   8247   9482  -1510   1141   2277  A    C  
ATOM   1334  NH1 ARG A 177      16.515 114.777 288.936  1.00 74.35      A    N1+
ANISOU 1334  NH1 ARG A 177    10317   8492   9442  -1648   1331   2361  A    N1+
ATOM   1335  NH2 ARG A 177      17.589 113.668 287.234  1.00 75.16      A    N  
ANISOU 1335  NH2 ARG A 177    10562   8094   9902  -1530   1002   2272  A    N  
ATOM   1336  N   LEU A 178      19.613 121.044 286.174  1.00 36.38      A    N  
ANISOU 1336  N   LEU A 178     5212   4290   4319   -823   1172   1328  A    N  
ATOM   1337  CA  LEU A 178      18.964 121.688 285.037  1.00 30.28      A    C  
ANISOU 1337  CA  LEU A 178     4288   3501   3717   -815   1166   1129  A    C  
ATOM   1338  C   LEU A 178      18.597 120.704 283.925  1.00 34.23      A    C  
ANISOU 1338  C   LEU A 178     4752   3767   4489   -890   1060   1130  A    C  
ATOM   1339  O   LEU A 178      19.430 119.895 283.486  1.00 32.49      A    O  
ANISOU 1339  O   LEU A 178     4642   3364   4337   -843    912   1150  A    O  
ATOM   1340  CB  LEU A 178      19.866 122.789 284.470  1.00 30.80      A    C  
ANISOU 1340  CB  LEU A 178     4366   3625   3710   -661   1068    924  A    C  
ATOM   1341  CG  LEU A 178      19.454 123.394 283.126  1.00 29.71      A    C  
ANISOU 1341  CG  LEU A 178     4102   3445   3742   -636   1009    738  A    C  
ATOM   1342  CD1 LEU A 178      18.151 124.167 283.245  1.00 30.20      A    C  
ANISOU 1342  CD1 LEU A 178     4008   3626   3841   -678   1155    683  A    C  
ATOM   1343  CD2 LEU A 178      20.558 124.279 282.550  1.00 31.24      A    C  
ANISOU 1343  CD2 LEU A 178     4335   3673   3861   -509    890    589  A    C  
ATOM   1344  N   LEU A 179      17.345 120.783 283.476  1.00 34.31      A    N  
ANISOU 1344  N   LEU A 179     4598   3789   4650  -1001   1132   1096  A    N  
ATOM   1345  CA  LEU A 179      16.893 120.046 282.298  1.00 34.68      A    C  
ANISOU 1345  CA  LEU A 179     4588   3639   4948  -1083   1018   1046  A    C  
ATOM   1346  C   LEU A 179      16.836 120.952 281.068  1.00 33.44      A    C  
ANISOU 1346  C   LEU A 179     4325   3524   4857   -994    936    816  A    C  
ATOM   1347  O   LEU A 179      16.229 122.025 281.099  1.00 32.11      A    O  
ANISOU 1347  O   LEU A 179     4024   3526   4652   -964   1025    737  A    O  
ATOM   1348  CB  LEU A 179      15.519 119.429 282.530  1.00 32.84      A    C  
ANISOU 1348  CB  LEU A 179     4226   3394   4858  -1296   1121   1178  A    C  
ATOM   1349  CG  LEU A 179      14.934 118.706 281.311  1.00 36.30      A    C  
ANISOU 1349  CG  LEU A 179     4595   3638   5560  -1411    990   1109  A    C  
ATOM   1350  CD1 LEU A 179      15.777 117.492 280.931  1.00 36.31      A    C  
ANISOU 1350  CD1 LEU A 179     4796   3345   5655  -1407    821   1139  A    C  
ATOM   1351  CD2 LEU A 179      13.487 118.290 281.558  1.00 35.20      A    C  
ANISOU 1351  CD2 LEU A 179     4298   3584   5491  -1610   1048   1189  A    C  
ATOM   1352  N   VAL A 180      17.493 120.518 279.998  1.00 30.54      A    N  
ANISOU 1352  N   VAL A 180     4024   3003   4577   -940    766    712  A    N  
ATOM   1353  CA  VAL A 180      17.404 121.180 278.698  1.00 27.52      A    C  
ANISOU 1353  CA  VAL A 180     3548   2651   4259   -884    670    519  A    C  
ATOM   1354  C   VAL A 180      16.503 120.358 277.783  1.00 29.33      A    C  
ANISOU 1354  C   VAL A 180     3698   2743   4704  -1024    590    486  A    C  
ATOM   1355  O   VAL A 180      16.813 119.206 277.460  1.00 32.52      A    O  
ANISOU 1355  O   VAL A 180     4211   2940   5205  -1066    490    497  A    O  
ATOM   1356  CB  VAL A 180      18.791 121.339 278.043  1.00 28.83      A    C  
ANISOU 1356  CB  VAL A 180     3825   2792   4338   -728    540    405  A    C  
ATOM   1357  CG1 VAL A 180      18.662 121.973 276.671  1.00 27.82      A    C  
ANISOU 1357  CG1 VAL A 180     3604   2710   4255   -694    444    233  A    C  
ATOM   1358  CG2 VAL A 180      19.720 122.178 278.932  1.00 26.91      A    C  
ANISOU 1358  CG2 VAL A 180     3650   2690   3886   -614    596    434  A    C  
ATOM   1359  N   MET A 181      15.372 120.934 277.390  1.00 26.81      A    N  
ANISOU 1359  N   MET A 181     3189   2531   4467  -1094    624    442  A    N  
ATOM   1360  CA  MET A 181      14.480 120.266 276.449  1.00 29.16      A    C  
ANISOU 1360  CA  MET A 181     3386   2731   4961  -1240    526    394  A    C  
ATOM   1361  C   MET A 181      14.850 120.686 275.040  1.00 30.69      A    C  
ANISOU 1361  C   MET A 181     3573   2936   5153  -1149    365    202  A    C  
ATOM   1362  O   MET A 181      14.676 121.853 274.665  1.00 26.19      A    O  
ANISOU 1362  O   MET A 181     2896   2529   4524  -1065    370    135  A    O  
ATOM   1363  CB  MET A 181      13.013 120.609 276.714  1.00 30.44      A    C  
ANISOU 1363  CB  MET A 181     3312   3030   5223  -1368    632    458  A    C  
ATOM   1364  CG  MET A 181      12.466 120.068 278.014  1.00 31.43      A    C  
ANISOU 1364  CG  MET A 181     3414   3174   5353  -1501    800    661  A    C  
ATOM   1365  SD  MET A 181      10.744 120.537 278.269  1.00 42.47      A    S  
ANISOU 1365  SD  MET A 181     4516   4823   6796  -1599    909    700  A    S  
ATOM   1366  CE  MET A 181      10.004 119.972 276.739  1.00 33.25      A    C  
ANISOU 1366  CE  MET A 181     3253   3570   5809  -1719    686    578  A    C  
ATOM   1367  N   GLY A 182      15.387 119.741 274.275  1.00 28.16      A    N  
ANISOU 1367  N   GLY A 182     3375   2440   4885  -1158    224    116  A    N  
ATOM   1368  CA  GLY A 182      15.824 120.014 272.922  1.00 26.28      A    C  
ANISOU 1368  CA  GLY A 182     3146   2231   4609  -1074     77    -70  A    C  
ATOM   1369  C   GLY A 182      17.325 119.881 272.794  1.00 28.82      A    C  
ANISOU 1369  C   GLY A 182     3641   2514   4797   -904     37   -135  A    C  
ATOM   1370  O   GLY A 182      18.087 120.594 273.457  1.00 31.69      A    O  
ANISOU 1370  O   GLY A 182     4041   2983   5018   -787    116    -79  A    O  
ATOM   1371  N   GLY A 183      17.746 118.982 271.911  1.00 33.27      A    N  
ANISOU 1371  N   GLY A 183     4299   2938   5403   -888    -92   -269  A    N  
ATOM   1372  CA  GLY A 183      19.154 118.735 271.673  1.00 31.10      A    C  
ANISOU 1372  CA  GLY A 183     4161   2637   5017   -712   -133   -351  A    C  
ATOM   1373  C   GLY A 183      19.641 119.508 270.464  1.00 28.03      A    C  
ANISOU 1373  C   GLY A 183     3724   2434   4491   -616   -204   -510  A    C  
ATOM   1374  O   GLY A 183      20.527 119.052 269.735  1.00 27.88      A    O  
ANISOU 1374  O   GLY A 183     3786   2396   4410   -504   -276   -651  A    O  
ATOM   1375  N   GLY A 184      19.021 120.659 270.222  1.00 27.49      A    N  
ANISOU 1375  N   GLY A 184     3518   2548   4378   -658   -184   -485  A    N  
ATOM   1376  CA  GLY A 184      19.495 121.584 269.207  1.00 29.37      A    C  
ANISOU 1376  CA  GLY A 184     3710   2982   4467   -580   -240   -577  A    C  
ATOM   1377  C   GLY A 184      20.659 122.435 269.695  1.00 25.92      A    C  
ANISOU 1377  C   GLY A 184     3305   2674   3870   -453   -171   -518  A    C  
ATOM   1378  O   GLY A 184      21.154 122.263 270.814  1.00 28.91      A    O  
ANISOU 1378  O   GLY A 184     3747   2995   4242   -410    -89   -422  A    O  
ATOM   1379  N   ILE A 185      21.073 123.389 268.871  1.00 21.78      A    N  
ANISOU 1379  N   ILE A 185     2732   2332   3212   -409   -211   -559  A    N  
ATOM   1380  CA  ILE A 185      22.266 124.175 269.163  1.00 19.06      A    C  
ANISOU 1380  CA  ILE A 185     2411   2117   2715   -315   -168   -514  A    C  
ATOM   1381  C   ILE A 185      22.121 125.061 270.414  1.00 18.14      A    C  
ANISOU 1381  C   ILE A 185     2283   2007   2602   -327    -72   -376  A    C  
ATOM   1382  O   ILE A 185      22.999 125.066 271.277  1.00 20.33      A    O  
ANISOU 1382  O   ILE A 185     2621   2290   2814   -268    -19   -323  A    O  
ATOM   1383  CB  ILE A 185      22.709 124.993 267.922  1.00 24.50      A    C  
ANISOU 1383  CB  ILE A 185     3048   3003   3257   -297   -238   -569  A    C  
ATOM   1384  CG1 ILE A 185      23.172 124.036 266.815  1.00 23.21      A    C  
ANISOU 1384  CG1 ILE A 185     2917   2868   3035   -249   -309   -733  A    C  
ATOM   1385  CG2 ILE A 185      23.796 126.007 268.288  1.00 19.42      A    C  
ANISOU 1385  CG2 ILE A 185     2405   2497   2477   -249   -196   -489  A    C  
ATOM   1386  CD1 ILE A 185      23.547 124.713 265.510  1.00 24.03      A    C  
ANISOU 1386  CD1 ILE A 185     2968   3198   2963   -246   -372   -785  A    C  
ATOM   1387  N   ILE A 186      21.011 125.790 270.512  1.00 18.31      A    N  
ANISOU 1387  N   ILE A 186     2225   2036   2697   -394    -56   -329  A    N  
ATOM   1388  CA  ILE A 186      20.780 126.709 271.625  1.00 19.69      A    C  
ANISOU 1388  CA  ILE A 186     2389   2222   2869   -390     39   -235  A    C  
ATOM   1389  C   ILE A 186      20.795 125.972 272.973  1.00 19.92      A    C  
ANISOU 1389  C   ILE A 186     2483   2159   2928   -394    142   -167  A    C  
ATOM   1390  O   ILE A 186      21.495 126.368 273.926  1.00 20.65      A    O  
ANISOU 1390  O   ILE A 186     2638   2284   2923   -350    201   -116  A    O  
ATOM   1391  CB  ILE A 186      19.436 127.453 271.430  1.00 24.22      A    C  
ANISOU 1391  CB  ILE A 186     2845   2810   3547   -434     39   -215  A    C  
ATOM   1392  CG1 ILE A 186      19.569 128.499 270.321  1.00 23.63      A    C  
ANISOU 1392  CG1 ILE A 186     2729   2835   3413   -416    -63   -232  A    C  
ATOM   1393  CG2 ILE A 186      18.967 128.098 272.730  1.00 17.38      A    C  
ANISOU 1393  CG2 ILE A 186     1966   1931   2705   -418    165   -148  A    C  
ATOM   1394  CD1 ILE A 186      18.247 129.133 269.932  1.00 26.99      A    C  
ANISOU 1394  CD1 ILE A 186     3026   3273   3957   -438    -99   -211  A    C  
ATOM   1395  N   GLY A 187      20.047 124.874 273.027  1.00 20.86      A    N  
ANISOU 1395  N   GLY A 187     2591   2164   3173   -461    149   -161  A    N  
ATOM   1396  CA  GLY A 187      20.015 124.026 274.205  1.00 23.17      A    C  
ANISOU 1396  CA  GLY A 187     2951   2356   3498   -487    234    -68  A    C  
ATOM   1397  C   GLY A 187      21.378 123.507 274.633  1.00 24.47      A    C  
ANISOU 1397  C   GLY A 187     3243   2494   3561   -396    219    -48  A    C  
ATOM   1398  O   GLY A 187      21.743 123.584 275.807  1.00 22.24      A    O  
ANISOU 1398  O   GLY A 187     3019   2228   3204   -374    293     50  A    O  
ATOM   1399  N   LEU A 188      22.135 122.967 273.685  1.00 22.11      A    N  
ANISOU 1399  N   LEU A 188     2979   2171   3249   -333    120   -145  A    N  
ATOM   1400  CA  LEU A 188      23.465 122.452 273.996  1.00 24.61      A    C  
ANISOU 1400  CA  LEU A 188     3387   2480   3485   -217     97   -136  A    C  
ATOM   1401  C   LEU A 188      24.425 123.548 274.453  1.00 24.75      A    C  
ANISOU 1401  C   LEU A 188     3396   2674   3337   -155    120   -102  A    C  
ATOM   1402  O   LEU A 188      25.249 123.323 275.346  1.00 16.64      A    O  
ANISOU 1402  O   LEU A 188     2429   1657   2237    -93    135    -27  A    O  
ATOM   1403  CB  LEU A 188      24.048 121.697 272.799  1.00 22.87      A    C  
ANISOU 1403  CB  LEU A 188     3186   2223   3281   -140     -2   -279  A    C  
ATOM   1404  CG  LEU A 188      23.303 120.413 272.429  1.00 26.52      A    C  
ANISOU 1404  CG  LEU A 188     3698   2464   3913   -196    -50   -332  A    C  
ATOM   1405  CD1 LEU A 188      23.865 119.814 271.151  1.00 23.85      A    C  
ANISOU 1405  CD1 LEU A 188     3382   2113   3564   -104   -147   -521  A    C  
ATOM   1406  CD2 LEU A 188      23.396 119.414 273.570  1.00 27.87      A    C  
ANISOU 1406  CD2 LEU A 188     3978   2444   4168   -190    -21   -201  A    C  
ATOM   1407  N   GLU A 189      24.339 124.721 273.830  1.00 16.69      A    N  
ANISOU 1407  N   GLU A 189     2301   1784   2257   -180    106   -149  A    N  
ATOM   1408  CA  GLU A 189      25.190 125.843 274.222  1.00 15.16      A    C  
ANISOU 1408  CA  GLU A 189     2103   1735   1924   -155    113   -119  A    C  
ATOM   1409  C   GLU A 189      24.894 126.279 275.659  1.00 17.50      A    C  
ANISOU 1409  C   GLU A 189     2443   2018   2186   -185    198    -28  A    C  
ATOM   1410  O   GLU A 189      25.812 126.459 276.485  1.00 24.13      A    O  
ANISOU 1410  O   GLU A 189     3333   2924   2913   -150    201     19  A    O  
ATOM   1411  CB  GLU A 189      25.054 127.011 273.228  1.00 16.64      A    C  
ANISOU 1411  CB  GLU A 189     2219   2027   2078   -194     70   -166  A    C  
ATOM   1412  CG  GLU A 189      25.669 126.720 271.834  1.00 19.01      A    C  
ANISOU 1412  CG  GLU A 189     2476   2414   2331   -159     -9   -251  A    C  
ATOM   1413  CD  GLU A 189      25.580 127.908 270.872  1.00 26.94      A    C  
ANISOU 1413  CD  GLU A 189     3419   3538   3280   -213    -58   -256  A    C  
ATOM   1414  OE1 GLU A 189      25.016 128.961 271.254  1.00 34.11      A    O  
ANISOU 1414  OE1 GLU A 189     4321   4425   4212   -264    -43   -201  A    O  
ATOM   1415  OE2 GLU A 189      26.083 127.797 269.732  1.00 22.78      A    O1-
ANISOU 1415  OE2 GLU A 189     2852   3126   2677   -197   -112   -313  A    O1-
ATOM   1416  N   MET A 190      23.607 126.436 275.963  1.00 16.26      A    N  
ANISOU 1416  N   MET A 190     2259   1799   2118   -249    267     -9  A    N  
ATOM   1417  CA  MET A 190      23.218 126.815 277.320  1.00 19.59      A    C  
ANISOU 1417  CA  MET A 190     2718   2234   2491   -270    371     59  A    C  
ATOM   1418  C   MET A 190      23.633 125.749 278.337  1.00 22.84      A    C  
ANISOU 1418  C   MET A 190     3216   2601   2859   -257    404    160  A    C  
ATOM   1419  O   MET A 190      24.094 126.062 279.449  1.00 26.02      A    O  
ANISOU 1419  O   MET A 190     3684   3075   3129   -243    444    216  A    O  
ATOM   1420  CB  MET A 190      21.714 127.051 277.375  1.00 23.01      A    C  
ANISOU 1420  CB  MET A 190     3070   2633   3039   -328    452     58  A    C  
ATOM   1421  CG  MET A 190      21.276 128.239 276.544  1.00 20.19      A    C  
ANISOU 1421  CG  MET A 190     2634   2316   2722   -321    413    -17  A    C  
ATOM   1422  SD  MET A 190      22.104 129.764 277.040  1.00 31.70      A    S  
ANISOU 1422  SD  MET A 190     4157   3851   4037   -279    402    -50  A    S  
ATOM   1423  CE  MET A 190      23.363 129.927 275.777  1.00 25.96      A    C  
ANISOU 1423  CE  MET A 190     3434   3176   3255   -273    255    -76  A    C  
ATOM   1424  N   GLY A 191      23.484 124.489 277.937  1.00 20.97      A    N  
ANISOU 1424  N   GLY A 191     2993   2242   2734   -262    371    184  A    N  
ATOM   1425  CA  GLY A 191      23.915 123.374 278.758  1.00 23.88      A    C  
ANISOU 1425  CA  GLY A 191     3457   2528   3089   -240    374    299  A    C  
ATOM   1426  C   GLY A 191      25.401 123.457 279.050  1.00 20.83      A    C  
ANISOU 1426  C   GLY A 191     3122   2228   2565   -132    304    311  A    C  
ATOM   1427  O   GLY A 191      25.840 123.183 280.163  1.00 21.42      A    O  
ANISOU 1427  O   GLY A 191     3270   2325   2542   -111    321    427  A    O  
ATOM   1428  N   THR A 192      26.173 123.838 278.040  1.00 18.25      A    N  
ANISOU 1428  N   THR A 192     2742   1972   2218    -69    224    202  A    N  
ATOM   1429  CA  THR A 192      27.618 123.991 278.174  1.00 25.89      A    C  
ANISOU 1429  CA  THR A 192     3712   3062   3063     27    154    205  A    C  
ATOM   1430  C   THR A 192      27.940 125.080 279.197  1.00 23.74      A    C  
ANISOU 1430  C   THR A 192     3457   2931   2631    -14    181    249  A    C  
ATOM   1431  O   THR A 192      28.749 124.884 280.141  1.00 20.72      A    O  
ANISOU 1431  O   THR A 192     3122   2613   2137     29    152    334  A    O  
ATOM   1432  CB  THR A 192      28.253 124.314 276.801  1.00 22.08      A    C  
ANISOU 1432  CB  THR A 192     3141   2668   2579     74     86     79  A    C  
ATOM   1433  CG2 THR A 192      29.772 124.431 276.908  1.00 16.45      A    C  
ANISOU 1433  CG2 THR A 192     2391   2113   1747    168     21     88  A    C  
ATOM   1434  OG1 THR A 192      27.912 123.279 275.865  1.00 22.77      A    O  
ANISOU 1434  OG1 THR A 192     3229   2624   2797    115     58      6  A    O  
ATOM   1435  N   VAL A 193      27.283 126.226 279.017  1.00 23.55      A    N  
ANISOU 1435  N   VAL A 193     3401   2948   2600    -93    225    187  A    N  
ATOM   1436  CA  VAL A 193      27.479 127.343 279.936  1.00 24.28      A    C  
ANISOU 1436  CA  VAL A 193     3528   3144   2555   -135    247    189  A    C  
ATOM   1437  C   VAL A 193      27.194 126.944 281.383  1.00 23.40      A    C  
ANISOU 1437  C   VAL A 193     3505   3031   2354   -146    319    288  A    C  
ATOM   1438  O   VAL A 193      28.036 127.133 282.267  1.00 21.69      A    O  
ANISOU 1438  O   VAL A 193     3341   2919   1982   -133    281    331  A    O  
ATOM   1439  CB  VAL A 193      26.590 128.550 279.584  1.00 20.10      A    C  
ANISOU 1439  CB  VAL A 193     2967   2602   2067   -197    291    105  A    C  
ATOM   1440  CG1 VAL A 193      26.662 129.596 280.700  1.00 19.08      A    C  
ANISOU 1440  CG1 VAL A 193     2906   2540   1804   -229    325     85  A    C  
ATOM   1441  CG2 VAL A 193      27.009 129.149 278.260  1.00 16.69      A    C  
ANISOU 1441  CG2 VAL A 193     2462   2204   1674   -205    207     38  A    C  
ATOM   1442  N   TYR A 194      26.006 126.406 281.632  1.00 25.87      A    N  
ANISOU 1442  N   TYR A 194     3826   3248   2753   -182    420    333  A    N  
ATOM   1443  CA  TYR A 194      25.630 126.100 283.011  1.00 27.22      A    C  
ANISOU 1443  CA  TYR A 194     4075   3450   2816   -211    511    441  A    C  
ATOM   1444  C   TYR A 194      26.403 124.934 283.611  1.00 27.28      A    C  
ANISOU 1444  C   TYR A 194     4158   3438   2770   -167    453    592  A    C  
ATOM   1445  O   TYR A 194      26.642 124.892 284.820  1.00 24.03      A    O  
ANISOU 1445  O   TYR A 194     3825   3116   2189   -176    478    690  A    O  
ATOM   1446  CB  TYR A 194      24.123 125.910 283.141  1.00 26.47      A    C  
ANISOU 1446  CB  TYR A 194     3941   3294   2821   -281    650    463  A    C  
ATOM   1447  CG  TYR A 194      23.407 127.228 283.216  1.00 27.17      A    C  
ANISOU 1447  CG  TYR A 194     3983   3453   2886   -296    731    341  A    C  
ATOM   1448  CD1 TYR A 194      23.223 127.866 284.437  1.00 24.54      A    C  
ANISOU 1448  CD1 TYR A 194     3708   3238   2379   -302    829    332  A    C  
ATOM   1449  CD2 TYR A 194      22.956 127.862 282.063  1.00 24.36      A    C  
ANISOU 1449  CD2 TYR A 194     3533   3047   2673   -291    699    229  A    C  
ATOM   1450  CE1 TYR A 194      22.584 129.084 284.512  1.00 26.16      A    C  
ANISOU 1450  CE1 TYR A 194     3881   3484   2575   -287    900    197  A    C  
ATOM   1451  CE2 TYR A 194      22.316 129.083 282.128  1.00 20.92      A    C  
ANISOU 1451  CE2 TYR A 194     3061   2648   2237   -280    758    124  A    C  
ATOM   1452  CZ  TYR A 194      22.134 129.686 283.355  1.00 25.50      A    C  
ANISOU 1452  CZ  TYR A 194     3702   3320   2664   -269    860     99  A    C  
ATOM   1453  OH  TYR A 194      21.496 130.897 283.436  1.00 24.72      A    O  
ANISOU 1453  OH  TYR A 194     3578   3235   2579   -231    917    -28  A    O  
ATOM   1454  N   HIS A 195      26.795 123.983 282.773  1.00 25.92      A    N  
ANISOU 1454  N   HIS A 195     3966   3146   2735   -108    370    607  A    N  
ATOM   1455  CA  HIS A 195      27.636 122.904 283.261  1.00 25.96      A    C  
ANISOU 1455  CA  HIS A 195     4042   3109   2714    -28    291    744  A    C  
ATOM   1456  C   HIS A 195      28.958 123.467 283.738  1.00 27.29      A    C  
ANISOU 1456  C   HIS A 195     4210   3457   2702     38    198    743  A    C  
ATOM   1457  O   HIS A 195      29.455 123.074 284.794  1.00 27.45      A    O  
ANISOU 1457  O   HIS A 195     4303   3534   2593     65    164    883  A    O  
ATOM   1458  CB  HIS A 195      27.889 121.830 282.206  1.00 25.72      A    C  
ANISOU 1458  CB  HIS A 195     3994   2905   2873     54    210    718  A    C  
ATOM   1459  CG  HIS A 195      28.755 120.717 282.699  1.00 26.87      A    C  
ANISOU 1459  CG  HIS A 195     4215   2977   3017    169    118    857  A    C  
ATOM   1460  CD2 HIS A 195      28.454 119.585 283.382  1.00 27.30      A    C  
ANISOU 1460  CD2 HIS A 195     4377   2867   3128    162    117   1038  A    C  
ATOM   1461  ND1 HIS A 195      30.124 120.710 282.532  1.00 30.55      A    N  
ANISOU 1461  ND1 HIS A 195     4641   3545   3423    313      4    832  A    N  
ATOM   1462  CE1 HIS A 195      30.625 119.618 283.077  1.00 32.74      A    C  
ANISOU 1462  CE1 HIS A 195     4995   3717   3727    416    -70    983  A    C  
ATOM   1463  NE2 HIS A 195      29.635 118.919 283.600  1.00 35.29      A    N  
ANISOU 1463  NE2 HIS A 195     5422   3864   4121    323     -7   1117  A    N  
ATOM   1464  N   ALA A 196      29.540 124.379 282.961  1.00 27.70      A    N  
ANISOU 1464  N   ALA A 196     4175   3609   2740     51    146    601  A    N  
ATOM   1465  CA  ALA A 196      30.793 124.977 283.420  1.00 29.69      A    C  
ANISOU 1465  CA  ALA A 196     4406   4047   2826     81     50    601  A    C  
ATOM   1466  C   ALA A 196      30.640 125.691 284.770  1.00 29.64      A    C  
ANISOU 1466  C   ALA A 196     4485   4159   2617      0     87    639  A    C  
ATOM   1467  O   ALA A 196      31.595 125.773 285.546  1.00 29.51      A    O  
ANISOU 1467  O   ALA A 196     4489   4283   2440     22     -3    699  A    O  
ATOM   1468  CB  ALA A 196      31.333 125.926 282.391  1.00 27.75      A    C  
ANISOU 1468  CB  ALA A 196     4053   3893   2598     64      1    462  A    C  
ATOM   1469  N   LEU A 197      29.449 126.220 285.039  1.00 32.29      A    N  
ANISOU 1469  N   LEU A 197     4498   5360   2410   -638    -27    144  A    N  
ATOM   1470  CA  LEU A 197      29.185 126.915 286.302  1.00 30.49      A    C  
ANISOU 1470  CA  LEU A 197     4316   5249   2020   -725     43     77  A    C  
ATOM   1471  C   LEU A 197      28.831 126.009 287.483  1.00 33.01      A    C  
ANISOU 1471  C   LEU A 197     4684   5640   2219   -661    101    217  A    C  
ATOM   1472  O   LEU A 197      28.682 126.487 288.607  1.00 33.08      A    O  
ANISOU 1472  O   LEU A 197     4731   5774   2062   -722    156    172  A    O  
ATOM   1473  CB  LEU A 197      28.112 127.989 286.105  1.00 28.76      A    C  
ANISOU 1473  CB  LEU A 197     4139   4868   1921   -818    149    -63  A    C  
ATOM   1474  CG  LEU A 197      28.581 129.083 285.144  1.00 31.17      A    C  
ANISOU 1474  CG  LEU A 197     4415   5130   2297   -892    105   -206  A    C  
ATOM   1475  CD1 LEU A 197      27.532 130.179 284.966  1.00 31.67      A    C  
ANISOU 1475  CD1 LEU A 197     4533   5029   2473   -956    223   -330  A    C  
ATOM   1476  CD2 LEU A 197      29.897 129.666 285.646  1.00 29.04      A    C  
ANISOU 1476  CD2 LEU A 197     4119   5096   1819   -978     27   -284  A    C  
ATOM   1477  N   GLY A 198      28.687 124.710 287.240  1.00 32.52      A    N  
ANISOU 1477  N   GLY A 198     4631   5490   2234   -541    100    385  A    N  
ATOM   1478  CA  GLY A 198      28.440 123.785 288.334  1.00 32.02      A    C  
ANISOU 1478  CA  GLY A 198     4624   5488   2053   -469    161    542  A    C  
ATOM   1479  C   GLY A 198      27.113 123.055 288.264  1.00 34.07      A    C  
ANISOU 1479  C   GLY A 198     4942   5519   2485   -451    284    626  A    C  
ATOM   1480  O   GLY A 198      26.847 122.180 289.086  1.00 32.20      A    O  
ANISOU 1480  O   GLY A 198     4762   5297   2175   -391    352    775  A    O  
ATOM   1481  N   SER A 199      26.261 123.424 287.311  1.00 29.08      A    N  
ANISOU 1481  N   SER A 199     4292   4686   2073   -508    319    533  A    N  
ATOM   1482  CA  SER A 199      24.979 122.740 287.156  1.00 33.09      A    C  
ANISOU 1482  CA  SER A 199     4829   4993   2751   -511    429    599  A    C  
ATOM   1483  C   SER A 199      25.161 121.313 286.657  1.00 33.47      A    C  
ANISOU 1483  C   SER A 199     4905   4921   2890   -418    410    751  A    C  
ATOM   1484  O   SER A 199      26.050 121.028 285.848  1.00 33.03      A    O  
ANISOU 1484  O   SER A 199     4826   4863   2862   -354    305    759  A    O  
ATOM   1485  CB  SER A 199      24.044 123.499 286.209  1.00 33.03      A    C  
ANISOU 1485  CB  SER A 199     4773   4832   2943   -586    459    464  A    C  
ATOM   1486  OG  SER A 199      23.646 124.743 286.757  1.00 35.73      A    O  
ANISOU 1486  OG  SER A 199     5115   5241   3220   -660    520    338  A    O  
ATOM   1487  N   GLN A 200      24.312 120.422 287.150  1.00 31.06      A    N  
ANISOU 1487  N   GLN A 200     4659   4510   2632   -414    524    870  A    N  
ATOM   1488  CA  GLN A 200      24.206 119.081 286.604  1.00 34.15      A    C  
ANISOU 1488  CA  GLN A 200     5100   4724   3153   -355    543    994  A    C  
ATOM   1489  C   GLN A 200      23.205 119.137 285.449  1.00 30.54      A    C  
ANISOU 1489  C   GLN A 200     4595   4068   2941   -442    563    895  A    C  
ATOM   1490  O   GLN A 200      22.107 119.679 285.603  1.00 30.53      A    O  
ANISOU 1490  O   GLN A 200     4555   4036   3008   -537    644    825  A    O  
ATOM   1491  CB  GLN A 200      23.767 118.121 287.705  1.00 42.63      A    C  
ANISOU 1491  CB  GLN A 200     6268   5774   4156   -327    670   1169  A    C  
ATOM   1492  CG  GLN A 200      23.808 116.655 287.343  1.00 53.34      A    C  
ANISOU 1492  CG  GLN A 200     7711   6942   5613   -255    709   1321  A    C  
ATOM   1493  CD  GLN A 200      23.259 115.799 288.462  1.00 65.60      A    C  
ANISOU 1493  CD  GLN A 200     9366   8455   7104   -243    859   1497  A    C  
ATOM   1494  NE2 GLN A 200      22.605 114.700 288.103  1.00 69.34      A    N  
ANISOU 1494  NE2 GLN A 200     9914   8688   7743   -270    956   1580  A    N  
ATOM   1495  OE1 GLN A 200      23.402 116.134 289.640  1.00 67.72      A    O  
ANISOU 1495  OE1 GLN A 200     9649   8909   7172   -219    894   1553  A    O  
ATOM   1496  N   ILE A 201      23.595 118.609 284.291  1.00 29.29      A    N  
ANISOU 1496  N   ILE A 201     4430   3794   2904   -402    487    884  A    N  
ATOM   1497  CA  ILE A 201      22.826 118.807 283.061  1.00 30.76      A    C  
ANISOU 1497  CA  ILE A 201     4552   3839   3295   -479    472    768  A    C  
ATOM   1498  C   ILE A 201      22.166 117.524 282.537  1.00 32.05      A    C  
ANISOU 1498  C   ILE A 201     4765   3789   3622   -507    533    830  A    C  
ATOM   1499  O   ILE A 201      22.841 116.524 282.285  1.00 33.23      A    O  
ANISOU 1499  O   ILE A 201     4996   3857   3774   -424    512    918  A    O  
ATOM   1500  CB  ILE A 201      23.717 119.393 281.931  1.00 29.55      A    C  
ANISOU 1500  CB  ILE A 201     4341   3726   3163   -437    332    664  A    C  
ATOM   1501  CG1 ILE A 201      24.454 120.651 282.399  1.00 28.21      A    C  
ANISOU 1501  CG1 ILE A 201     4129   3755   2835   -433    274    592  A    C  
ATOM   1502  CG2 ILE A 201      22.893 119.680 280.674  1.00 24.84      A    C  
ANISOU 1502  CG2 ILE A 201     3672   3011   2756   -508    313    546  A    C  
ATOM   1503  CD1 ILE A 201      23.545 121.809 282.751  1.00 26.12      A    C  
ANISOU 1503  CD1 ILE A 201     3820   3524   2581   -527    339    487  A    C  
ATOM   1504  N   ASP A 202      20.844 117.559 282.383  1.00 28.26      A    N  
ANISOU 1504  N   ASP A 202     4238   3223   3275   -625    615    782  A    N  
ATOM   1505  CA  ASP A 202      20.128 116.510 281.655  1.00 28.84      A    C  
ANISOU 1505  CA  ASP A 202     4333   3101   3524   -696    659    791  A    C  
ATOM   1506  C   ASP A 202      19.635 117.120 280.340  1.00 31.43      A    C  
ANISOU 1506  C   ASP A 202     4541   3411   3989   -757    581    632  A    C  
ATOM   1507  O   ASP A 202      19.211 118.271 280.318  1.00 33.76      A    O  
ANISOU 1507  O   ASP A 202     4735   3815   4277   -784    567    544  A    O  
ATOM   1508  CB  ASP A 202      18.938 115.992 282.471  1.00 33.06      A    C  
ANISOU 1508  CB  ASP A 202     4885   3571   4106   -802    817    863  A    C  
ATOM   1509  CG  ASP A 202      19.349 115.021 283.579  1.00 40.81      A    C  
ANISOU 1509  CG  ASP A 202     6013   4513   4981   -741    911   1047  A    C  
ATOM   1510  OD1 ASP A 202      20.562 114.793 283.774  1.00 41.41      A    O  
ANISOU 1510  OD1 ASP A 202     6165   4634   4935   -602    848   1123  A    O  
ATOM   1511  OD2 ASP A 202      18.446 114.493 284.268  1.00 41.79      A    O1-
ANISOU 1511  OD2 ASP A 202     6168   4572   5138   -827   1053   1126  A    O1-
ATOM   1512  N   VAL A 203      19.716 116.376 279.240  1.00 28.32      A    N  
ANISOU 1512  N   VAL A 203     4166   2886   3711   -769    533    596  A    N  
ATOM   1513  CA  VAL A 203      19.172 116.857 277.964  1.00 26.47      A    C  
ANISOU 1513  CA  VAL A 203     3814   2646   3597   -829    460    453  A    C  
ATOM   1514  C   VAL A 203      18.166 115.847 277.424  1.00 32.40      A    C  
ANISOU 1514  C   VAL A 203     4562   3246   4503   -960    518    429  A    C  
ATOM   1515  O   VAL A 203      18.497 114.674 277.247  1.00 35.10      A    O  
ANISOU 1515  O   VAL A 203     5023   3432   4881   -959    543    478  A    O  
ATOM   1516  CB  VAL A 203      20.281 117.087 276.912  1.00 25.21      A    C  
ANISOU 1516  CB  VAL A 203     3656   2505   3416   -729    322    392  A    C  
ATOM   1517  CG1 VAL A 203      19.684 117.567 275.583  1.00 24.37      A    C  
ANISOU 1517  CG1 VAL A 203     3433   2406   3421   -784    250    255  A    C  
ATOM   1518  CG2 VAL A 203      21.312 118.079 277.429  1.00 24.27      A    C  
ANISOU 1518  CG2 VAL A 203     3533   2545   3144   -626    266    407  A    C  
ATOM   1519  N   VAL A 204      16.939 116.294 277.166  1.00 27.76      A    N  
ANISOU 1519  N   VAL A 204     3839   2704   4004  -1075    546    352  A    N  
ATOM   1520  CA  VAL A 204      15.933 115.399 276.589  1.00 30.62      A    C  
ANISOU 1520  CA  VAL A 204     4169   2955   4511  -1229    591    307  A    C  
ATOM   1521  C   VAL A 204      15.648 115.778 275.130  1.00 35.43      A    C  
ANISOU 1521  C   VAL A 204     4655   3608   5200  -1258    474    161  A    C  
ATOM   1522  O   VAL A 204      15.391 116.944 274.819  1.00 39.68      A    O  
ANISOU 1522  O   VAL A 204     5061   4296   5720  -1217    418    101  A    O  
ATOM   1523  CB  VAL A 204      14.633 115.355 277.449  1.00 34.14      A    C  
ANISOU 1523  CB  VAL A 204     4541   3431   5001  -1360    730    346  A    C  
ATOM   1524  CG1 VAL A 204      13.973 116.725 277.520  1.00 30.48      A    C  
ANISOU 1524  CG1 VAL A 204     3905   3158   4517  -1342    716    288  A    C  
ATOM   1525  CG2 VAL A 204      13.657 114.299 276.927  1.00 34.68      A    C  
ANISOU 1525  CG2 VAL A 204     4583   3380   5215  -1549    787    303  A    C  
ATOM   1526  N   GLU A 205      15.750 114.800 274.233  1.00 29.92      A    N  
ANISOU 1526  N   GLU A 205     4013   2776   4577  -1315    442    108  A    N  
ATOM   1527  CA  GLU A 205      15.583 115.051 272.801  1.00 29.55      A    C  
ANISOU 1527  CA  GLU A 205     3865   2777   4584  -1336    324    -31  A    C  
ATOM   1528  C   GLU A 205      14.807 113.928 272.118  1.00 37.11      A    C  
ANISOU 1528  C   GLU A 205     4823   3616   5661  -1516    351   -112  A    C  
ATOM   1529  O   GLU A 205      15.112 112.749 272.305  1.00 34.19      A    O  
ANISOU 1529  O   GLU A 205     4617   3050   5323  -1559    419    -74  A    O  
ATOM   1530  CB  GLU A 205      16.941 115.246 272.119  1.00 31.20      A    C  
ANISOU 1530  CB  GLU A 205     4152   2979   4722  -1177    211    -48  A    C  
ATOM   1531  CG  GLU A 205      16.893 115.207 270.597  1.00 32.98      A    C  
ANISOU 1531  CG  GLU A 205     4316   3220   4996  -1198    100   -183  A    C  
ATOM   1532  CD  GLU A 205      16.070 116.342 270.014  1.00 38.48      A    C  
ANISOU 1532  CD  GLU A 205     4811   4105   5707  -1217     37   -261  A    C  
ATOM   1533  OE1 GLU A 205      16.286 117.505 270.422  1.00 41.28      A    O  
ANISOU 1533  OE1 GLU A 205     5110   4579   5995  -1115     24   -222  A    O  
ATOM   1534  OE2 GLU A 205      15.212 116.072 269.145  1.00 36.68      A    O1-
ANISOU 1534  OE2 GLU A 205     4480   3907   5550  -1331      3   -362  A    O1-
ATOM   1535  N   MET A 206      13.808 114.302 271.326  1.00 39.99      A    N  
ANISOU 1535  N   MET A 206     5005   4101   6087  -1619    301   -224  A    N  
ATOM   1536  CA  MET A 206      12.936 113.339 270.663  1.00 45.86      A    C  
ANISOU 1536  CA  MET A 206     5713   4775   6937  -1824    319   -325  A    C  
ATOM   1537  C   MET A 206      13.643 112.623 269.513  1.00 41.79      A    C  
ANISOU 1537  C   MET A 206     5308   4138   6431  -1815    237   -423  A    C  
ATOM   1538  O   MET A 206      13.353 111.465 269.217  1.00 35.82      A    O  
ANISOU 1538  O   MET A 206     4639   3220   5751  -1970    288   -483  A    O  
ATOM   1539  CB  MET A 206      11.698 114.061 270.126  1.00 54.20      A    C  
ANISOU 1539  CB  MET A 206     6510   6051   8031  -1916    273   -414  A    C  
ATOM   1540  CG  MET A 206      10.862 113.249 269.149  1.00 62.59      A    C  
ANISOU 1540  CG  MET A 206     7495   7109   9178  -2121    242   -554  A    C  
ATOM   1541  SD  MET A 206       9.645 112.231 269.989  1.00136.44      A    S  
ANISOU 1541  SD  MET A 206    16838  16403  18602  -2310    378   -497  A    S  
ATOM   1542  CE  MET A 206       8.503 113.510 270.499  1.00 75.33      A    C  
ANISOU 1542  CE  MET A 206     8818   8948  10857  -2307    403   -463  A    C  
ATOM   1543  N   PHE A 207      14.605 113.292 268.890  1.00 39.78      A    N  
ANISOU 1543  N   PHE A 207     5064   3951   6098  -1636    121   -439  A    N  
ATOM   1544  CA  PHE A 207      15.274 112.701 267.741  1.00 34.39      A    C  
ANISOU 1544  CA  PHE A 207     4474   3179   5414  -1612     43   -537  A    C  
ATOM   1545  C   PHE A 207      16.345 111.727 268.230  1.00 32.44      A    C  
ANISOU 1545  C   PHE A 207     4474   2701   5151  -1530    116   -452  A    C  
ATOM   1546  O   PHE A 207      16.625 111.654 269.430  1.00 36.03      A    O  
ANISOU 1546  O   PHE A 207     5010   3099   5579  -1475    208   -310  A    O  
ATOM   1547  CB  PHE A 207      15.877 113.817 266.886  1.00 31.90      A    C  
ANISOU 1547  CB  PHE A 207     4067   3036   5018  -1449    -97   -576  A    C  
ATOM   1548  CG  PHE A 207      16.112 113.436 265.453  1.00 34.44      A    C  
ANISOU 1548  CG  PHE A 207     4398   3349   5337  -1462   -196   -715  A    C  
ATOM   1549  CD1 PHE A 207      15.048 113.121 264.614  1.00 34.36      A    C  
ANISOU 1549  CD1 PHE A 207     4270   3404   5382  -1638   -233   -855  A    C  
ATOM   1550  CD2 PHE A 207      17.399 113.425 264.934  1.00 33.19      A    C  
ANISOU 1550  CD2 PHE A 207     4355   3144   5110  -1297   -254   -711  A    C  
ATOM   1551  CE1 PHE A 207      15.268 112.781 263.285  1.00 34.92      A    C  
ANISOU 1551  CE1 PHE A 207     4353   3484   5433  -1652   -326   -994  A    C  
ATOM   1552  CE2 PHE A 207      17.627 113.093 263.608  1.00 33.69      A    C  
ANISOU 1552  CE2 PHE A 207     4432   3209   5161  -1300   -338   -841  A    C  
ATOM   1553  CZ  PHE A 207      16.561 112.771 262.782  1.00 34.38      A    C  
ANISOU 1553  CZ  PHE A 207     4414   3353   5295  -1478   -375   -986  A    C  
ATOM   1554  N   ASP A 208      16.927 110.962 267.311  1.00 31.49      A    N  
ANISOU 1554  N   ASP A 208     4472   2453   5039  -1514     81   -535  A    N  
ATOM   1555  CA  ASP A 208      17.867 109.913 267.700  1.00 38.81      A    C  
ANISOU 1555  CA  ASP A 208     5641   3144   5961  -1429    166   -455  A    C  
ATOM   1556  C   ASP A 208      19.286 110.443 267.735  1.00 36.10      A    C  
ANISOU 1556  C   ASP A 208     5348   2860   5506  -1175    100   -370  A    C  
ATOM   1557  O   ASP A 208      20.240 109.679 267.894  1.00 31.12      A    O  
ANISOU 1557  O   ASP A 208     4899   2074   4851  -1054    148   -302  A    O  
ATOM   1558  CB  ASP A 208      17.790 108.711 266.750  1.00 36.30      A    C  
ANISOU 1558  CB  ASP A 208     5453   2626   5712  -1539    189   -589  A    C  
ATOM   1559  CG  ASP A 208      18.347 109.015 265.363  1.00 42.20      A    C  
ANISOU 1559  CG  ASP A 208     6164   3461   6409  -1454     52   -722  A    C  
ATOM   1560  OD1 ASP A 208      18.316 110.190 264.930  1.00 41.40      A    O  
ANISOU 1560  OD1 ASP A 208     5881   3600   6249  -1390    -68   -748  A    O  
ATOM   1561  OD2 ASP A 208      18.845 108.071 264.712  1.00 50.46      A    O1-
ANISOU 1561  OD2 ASP A 208     7376   4327   7471  -1441     75   -794  A    O1-
ATOM   1562  N   GLN A 209      19.410 111.757 267.579  1.00 30.61      A    N  
ANISOU 1562  N   GLN A 209     4492   2395   4745  -1094     -2   -374  A    N  
ATOM   1563  CA  GLN A 209      20.705 112.405 267.481  1.00 28.94      A    C  
ANISOU 1563  CA  GLN A 209     4294   2275   4427   -884    -76   -317  A    C  
ATOM   1564  C   GLN A 209      20.553 113.864 267.892  1.00 27.65      A    C  
ANISOU 1564  C   GLN A 209     3969   2330   4206   -845   -127   -282  A    C  
ATOM   1565  O   GLN A 209      19.532 114.477 267.587  1.00 29.94      A    O  
ANISOU 1565  O   GLN A 209     4112   2727   4536   -947   -154   -352  A    O  
ATOM   1566  CB  GLN A 209      21.121 112.349 266.013  1.00 30.44      A    C  
ANISOU 1566  CB  GLN A 209     4477   2483   4606   -843   -175   -446  A    C  
ATOM   1567  CG  GLN A 209      22.525 112.780 265.698  1.00 31.62      A    C  
ANISOU 1567  CG  GLN A 209     4656   2704   4656   -637   -242   -404  A    C  
ATOM   1568  CD  GLN A 209      22.665 113.200 264.243  1.00 33.42      A    C  
ANISOU 1568  CD  GLN A 209     4807   3031   4861   -614   -353   -534  A    C  
ATOM   1569  NE2 GLN A 209      22.933 114.484 264.022  1.00 25.77      A    N  
ANISOU 1569  NE2 GLN A 209     3707   2256   3827   -541   -434   -522  A    N  
ATOM   1570  OE1 GLN A 209      22.537 112.380 263.329  1.00 31.61      A    O  
ANISOU 1570  OE1 GLN A 209     4644   2699   4666   -663   -360   -645  A    O  
ATOM   1571  N   VAL A 210      21.549 114.426 268.580  1.00 24.40      A    N  
ANISOU 1571  N   VAL A 210     3583   1990   3697   -699   -136   -177  A    N  
ATOM   1572  CA  VAL A 210      21.593 115.876 268.783  1.00 22.88      A    C  
ANISOU 1572  CA  VAL A 210     3260   1990   3443   -655   -189   -168  A    C  
ATOM   1573  C   VAL A 210      22.040 116.551 267.488  1.00 24.57      A    C  
ANISOU 1573  C   VAL A 210     3402   2303   3631   -589   -303   -257  A    C  
ATOM   1574  O   VAL A 210      22.614 115.884 266.623  1.00 26.77      A    O  
ANISOU 1574  O   VAL A 210     3747   2515   3910   -543   -340   -304  A    O  
ATOM   1575  CB  VAL A 210      22.523 116.293 269.938  1.00 29.64      A    C  
ANISOU 1575  CB  VAL A 210     4163   2907   4192   -546   -164    -45  A    C  
ATOM   1576  CG1 VAL A 210      22.079 115.644 271.239  1.00 24.96      A    C  
ANISOU 1576  CG1 VAL A 210     3646   2231   3608   -599    -47     56  A    C  
ATOM   1577  CG2 VAL A 210      23.972 115.960 269.611  1.00 22.09      A    C  
ANISOU 1577  CG2 VAL A 210     3289   1944   3159   -395   -212     -9  A    C  
ATOM   1578  N   ILE A 211      21.774 117.856 267.364  1.00 25.53      A    N  
ANISOU 1578  N   ILE A 211     3398   2575   3726   -579   -344   -277  A    N  
ATOM   1579  CA  ILE A 211      22.048 118.620 266.138  1.00 24.46      A    C  
ANISOU 1579  CA  ILE A 211     3185   2542   3566   -522   -440   -350  A    C  
ATOM   1580  C   ILE A 211      21.684 117.774 264.913  1.00 26.56      A    C  
ANISOU 1580  C   ILE A 211     3455   2751   3885   -572   -485   -454  A    C  
ATOM   1581  O   ILE A 211      22.568 117.352 264.151  1.00 23.17      A    O  
ANISOU 1581  O   ILE A 211     3092   2290   3421   -495   -530   -483  A    O  
ATOM   1582  CB  ILE A 211      23.517 119.084 266.053  1.00 25.28      A    C  
ANISOU 1582  CB  ILE A 211     3332   2701   3573   -386   -484   -307  A    C  
ATOM   1583  CG1 ILE A 211      24.017 119.549 267.419  1.00 25.41      A    C  
ANISOU 1583  CG1 ILE A 211     3377   2754   3524   -357   -432   -209  A    C  
ATOM   1584  CG2 ILE A 211      23.670 120.201 265.014  1.00 23.50      A    C  
ANISOU 1584  CG2 ILE A 211     3014   2597   3317   -338   -558   -358  A    C  
ATOM   1585  CD1 ILE A 211      25.484 119.964 267.426  1.00 19.27      A    C  
ANISOU 1585  CD1 ILE A 211     2624   2055   2643   -244   -475   -168  A    C  
ATOM   1586  N   PRO A 212      20.382 117.477 264.756  1.00 27.73      A    N  
ANISOU 1586  N   PRO A 212     3532   2893   4112   -708   -467   -516  A    N  
ATOM   1587  CA  PRO A 212      19.894 116.480 263.793  1.00 30.12      A    C  
ANISOU 1587  CA  PRO A 212     3849   3128   4468   -803   -493   -629  A    C  
ATOM   1588  C   PRO A 212      20.304 116.706 262.340  1.00 33.88      A    C  
ANISOU 1588  C   PRO A 212     4292   3683   4896   -738   -598   -721  A    C  
ATOM   1589  O   PRO A 212      20.444 115.730 261.603  1.00 32.83      A    O  
ANISOU 1589  O   PRO A 212     4238   3460   4777   -774   -613   -808  A    O  
ATOM   1590  CB  PRO A 212      18.362 116.554 263.934  1.00 29.44      A    C  
ANISOU 1590  CB  PRO A 212     3628   3102   4455   -961   -468   -672  A    C  
ATOM   1591  CG  PRO A 212      18.076 117.773 264.708  1.00 33.60      A    C  
ANISOU 1591  CG  PRO A 212     4058   3750   4961   -910   -444   -589  A    C  
ATOM   1592  CD  PRO A 212      19.284 118.093 265.523  1.00 28.78      A    C  
ANISOU 1592  CD  PRO A 212     3557   3096   4282   -784   -415   -485  A    C  
ATOM   1593  N   ALA A 213      20.493 117.952 261.923  1.00 33.93      A    N  
ANISOU 1593  N   ALA A 213     4197   3848   4846   -645   -659   -703  A    N  
ATOM   1594  CA  ALA A 213      20.875 118.198 260.533  1.00 30.74      A    C  
ANISOU 1594  CA  ALA A 213     3762   3531   4386   -577   -752   -777  A    C  
ATOM   1595  C   ALA A 213      22.323 117.808 260.235  1.00 29.90      A    C  
ANISOU 1595  C   ALA A 213     3785   3355   4219   -456   -763   -761  A    C  
ATOM   1596  O   ALA A 213      22.672 117.554 259.084  1.00 32.01      A    O  
ANISOU 1596  O   ALA A 213     4067   3648   4446   -417   -822   -839  A    O  
ATOM   1597  CB  ALA A 213      20.634 119.656 260.161  1.00 26.78      A    C  
ANISOU 1597  CB  ALA A 213     3125   3207   3842   -505   -798   -747  A    C  
ATOM   1598  N   ALA A 214      23.147 117.688 261.271  1.00 26.86      A    N  
ANISOU 1598  N   ALA A 214     3491   2895   3821   -396   -704   -660  A    N  
ATOM   1599  CA  ALA A 214      24.564 117.406 261.058  1.00 24.16      A    C  
ANISOU 1599  CA  ALA A 214     3244   2522   3412   -263   -713   -627  A    C  
ATOM   1600  C   ALA A 214      24.801 115.917 260.868  1.00 22.36      A    C  
ANISOU 1600  C   ALA A 214     3158   2122   3214   -271   -676   -671  A    C  
ATOM   1601  O   ALA A 214      24.021 115.086 261.349  1.00 24.60      A    O  
ANISOU 1601  O   ALA A 214     3496   2278   3575   -385   -616   -691  A    O  
ATOM   1602  CB  ALA A 214      25.392 117.935 262.210  1.00 23.48      A    C  
ANISOU 1602  CB  ALA A 214     3178   2463   3281   -189   -675   -502  A    C  
ATOM   1603  N   ASP A 215      25.876 115.594 260.151  1.00 27.06      A    N  
ANISOU 1603  N   ASP A 215     3821   2711   3751   -148   -699   -688  A    N  
ATOM   1604  CA  ASP A 215      26.233 114.213 259.813  1.00 29.90      A    C  
ANISOU 1604  CA  ASP A 215     4333   2897   4129   -123   -655   -737  A    C  
ATOM   1605  C   ASP A 215      26.516 113.328 261.030  1.00 33.70      A    C  
ANISOU 1605  C   ASP A 215     4947   3213   4646    -99   -553   -633  A    C  
ATOM   1606  O   ASP A 215      26.924 113.819 262.088  1.00 31.47      A    O  
ANISOU 1606  O   ASP A 215     4637   2987   4332    -45   -532   -505  A    O  
ATOM   1607  CB  ASP A 215      27.440 114.200 258.870  1.00 28.00      A    C  
ANISOU 1607  CB  ASP A 215     4125   2711   3804     37   -693   -756  A    C  
ATOM   1608  CG  ASP A 215      27.047 114.366 257.404  1.00 32.62      A    C  
ANISOU 1608  CG  ASP A 215     4657   3374   4362      0   -768   -900  A    C  
ATOM   1609  OD1 ASP A 215      25.909 113.993 257.030  1.00 32.34      A    O  
ANISOU 1609  OD1 ASP A 215     4609   3298   4382   -150   -779  -1011  A    O  
ATOM   1610  OD2 ASP A 215      27.885 114.881 256.629  1.00 26.57      A    O1-
ANISOU 1610  OD2 ASP A 215     3855   2729   3513    119   -815   -900  A    O1-
ATOM   1611  N   LYS A 216      26.313 112.024 260.857  1.00 29.98      A    N  
ANISOU 1611  N   LYS A 216     4624   2536   4231   -139   -486   -690  A    N  
ATOM   1612  CA ALYS A 216      26.528 111.039 261.916  0.39 33.85      A    C  
ANISOU 1612  CA ALYS A 216     5266   2837   4758   -109   -372   -586  A    C  
ATOM   1613  CA BLYS A 216      26.519 111.066 261.938  0.61 32.84      A    C  
ANISOU 1613  CA BLYS A 216     5134   2712   4630   -110   -373   -584  A    C  
ATOM   1614  C   LYS A 216      27.952 111.048 262.460  1.00 31.95      A    C  
ANISOU 1614  C   LYS A 216     5072   2635   4431    113   -354   -440  A    C  
ATOM   1615  O   LYS A 216      28.162 111.068 263.665  1.00 29.78      A    O  
ANISOU 1615  O   LYS A 216     4814   2360   4141    153   -305   -300  A    O  
ATOM   1616  CB ALYS A 216      26.209 109.631 261.407  0.39 39.48      A    C  
ANISOU 1616  CB ALYS A 216     6157   3302   5543   -174   -295   -688  A    C  
ATOM   1617  CB BLYS A 216      26.121 109.657 261.499  0.61 39.79      A    C  
ANISOU 1617  CB BLYS A 216     6190   3342   5588   -187   -292   -683  A    C  
ATOM   1618  CG ALYS A 216      24.787 109.442 260.906  0.39 45.31      A    C  
ANISOU 1618  CG ALYS A 216     6850   4000   6364   -419   -306   -844  A    C  
ATOM   1619  CG BLYS A 216      24.678 109.535 261.045  0.61 47.66      A    C  
ANISOU 1619  CG BLYS A 216     7131   4310   6666   -434   -306   -832  A    C  
ATOM   1620  CD ALYS A 216      23.769 109.725 261.999  0.39 47.92      A    C  
ANISOU 1620  CD ALYS A 216     7105   4343   6759   -569   -266   -776  A    C  
ATOM   1621  CD BLYS A 216      23.704 109.630 262.213  0.61 49.06      A    C  
ANISOU 1621  CD BLYS A 216     7264   4463   6915   -580   -246   -757  A    C  
ATOM   1622  CE ALYS A 216      22.350 109.481 261.503  0.39 47.37      A    C  
ANISOU 1622  CE ALYS A 216     6971   4256   6770   -819   -274   -929  A    C  
ATOM   1623  CE BLYS A 216      22.261 109.582 261.720  0.61 47.31      A    C  
ANISOU 1623  CE BLYS A 216     6947   4260   6767   -827   -268   -906  A    C  
ATOM   1624  NZ ALYS A 216      21.345 109.856 262.533  0.39 44.56      A    N1+
ANISOU 1624  NZ ALYS A 216     6514   3946   6471   -955   -235   -860  A    N1+
ATOM   1625  NZ BLYS A 216      22.181 109.071 260.318  0.61 44.50      A    N1+
ANISOU 1625  NZ BLYS A 216     6630   3872   6407   -881   -317  -1095  A    N1+
ATOM   1626  N   ASP A 217      28.933 111.004 261.562  1.00 33.22      A    N  
ANISOU 1626  N   ASP A 217     5249   2846   4528    259   -391   -473  A    N  
ATOM   1627  CA  ASP A 217      30.338 110.888 261.980  1.00 26.03      A    C  
ANISOU 1627  CA  ASP A 217     4372   1986   3530    481   -371   -339  A    C  
ATOM   1628  C   ASP A 217      30.860 112.111 262.770  1.00 24.42      A    C  
ANISOU 1628  C   ASP A 217     4014   2018   3246    523   -428   -224  A    C  
ATOM   1629  O   ASP A 217      31.611 111.959 263.731  1.00 30.25      A    O  
ANISOU 1629  O   ASP A 217     4774   2791   3927    640   -393    -82  A    O  
ATOM   1630  CB  ASP A 217      31.243 110.470 260.802  1.00 30.02      A    C  
ANISOU 1630  CB  ASP A 217     4933   2487   3988    630   -383   -405  A    C  
ATOM   1631  CG  ASP A 217      31.106 111.385 259.581  1.00 35.10      A    C  
ANISOU 1631  CG  ASP A 217     5444   3297   4596    578   -488   -531  A    C  
ATOM   1632  OD1 ASP A 217      30.213 112.264 259.561  1.00 32.90      A    O  
ANISOU 1632  OD1 ASP A 217     5044   3115   4343    425   -549   -576  A    O  
ATOM   1633  OD2 ASP A 217      31.865 111.179 258.608  1.00 35.40      A    O1-
ANISOU 1633  OD2 ASP A 217     5507   3363   4578    699   -501   -583  A    O1-
ATOM   1634  N   ILE A 218      30.453 113.311 262.368  1.00 23.80      A    N  
ANISOU 1634  N   ILE A 218     3786   2101   3156    427   -512   -287  A    N  
ATOM   1635  CA  ILE A 218      30.770 114.544 263.099  1.00 25.11      A    C  
ANISOU 1635  CA  ILE A 218     3820   2463   3258    424   -555   -206  A    C  
ATOM   1636  C   ILE A 218      30.194 114.551 264.537  1.00 23.92      A    C  
ANISOU 1636  C   ILE A 218     3682   2276   3129    347   -501   -116  A    C  
ATOM   1637  O   ILE A 218      30.893 114.756 265.586  1.00 27.61      A    O  
ANISOU 1637  O   ILE A 218     4136   2834   3521    420   -486      5  A    O  
ATOM   1638  CB  ILE A 218      30.165 115.743 262.324  1.00 23.83      A    C  
ANISOU 1638  CB  ILE A 218     3525   2424   3104    320   -630   -302  A    C  
ATOM   1639  CG1 ILE A 218      30.703 115.790 260.886  1.00 23.11      A    C  
ANISOU 1639  CG1 ILE A 218     3418   2386   2977    394   -682   -385  A    C  
ATOM   1640  CG2 ILE A 218      30.397 117.048 263.057  1.00 20.22      A    C  
ANISOU 1640  CG2 ILE A 218     2955   2135   2593    297   -657   -236  A    C  
ATOM   1641  CD1 ILE A 218      32.176 116.156 260.787  1.00 26.23      A    C  
ANISOU 1641  CD1 ILE A 218     3772   2925   3270    547   -702   -314  A    C  
ATOM   1642  N   VAL A 219      28.884 114.321 264.558  1.00 26.61      A    N  
ANISOU 1642  N   VAL A 219     4041   2501   3567    193   -471   -181  A    N  
ATOM   1643  CA  VAL A 219      28.087 114.348 265.771  1.00 27.93      A    C  
ANISOU 1643  CA  VAL A 219     4214   2630   3769     92   -413   -118  A    C  
ATOM   1644  C   VAL A 219      28.486 113.212 266.696  1.00 29.73      A    C  
ANISOU 1644  C   VAL A 219     4585   2722   3988    172   -320      2  A    C  
ATOM   1645  O   VAL A 219      28.237 113.276 267.873  1.00 33.43      A    O  
ANISOU 1645  O   VAL A 219     5061   3199   4441    143   -270     97  A    O  
ATOM   1646  CB  VAL A 219      26.566 114.312 265.438  1.00 31.02      A    C  
ANISOU 1646  CB  VAL A 219     4573   2945   4269    -95   -401   -223  A    C  
ATOM   1647  CG1 VAL A 219      25.715 114.204 266.689  1.00 29.59      A    C  
ANISOU 1647  CG1 VAL A 219     4403   2711   4128   -198   -322   -154  A    C  
ATOM   1648  CG2 VAL A 219      26.178 115.559 264.679  1.00 31.22      A    C  
ANISOU 1648  CG2 VAL A 219     4447   3131   4286   -144   -488   -307  A    C  
ATOM   1649  N   LYS A 220      29.082 112.158 266.155  1.00 25.69      A    N  
ANISOU 1649  N   LYS A 220     4197   2080   3485    282   -287      1  A    N  
ATOM   1650  CA  LYS A 220      29.556 111.047 266.975  1.00 26.35      A    C  
ANISOU 1650  CA  LYS A 220     4433   2025   3555    396   -188    134  A    C  
ATOM   1651  C   LYS A 220      30.736 111.495 267.841  1.00 35.19      A    C  
ANISOU 1651  C   LYS A 220     5497   3335   4539    561   -212    284  A    C  
ATOM   1652  O   LYS A 220      30.789 111.199 269.034  1.00 26.77      A    O  
ANISOU 1652  O   LYS A 220     4478   2259   3434    597   -151    419  A    O  
ATOM   1653  CB  LYS A 220      29.916 109.827 266.111  1.00 27.88      A    C  
ANISOU 1653  CB  LYS A 220     4786   2017   3791    487   -134     88  A    C  
ATOM   1654  CG  LYS A 220      30.288 108.584 266.917  1.00 31.86      A    C  
ANISOU 1654  CG  LYS A 220     5477   2330   4297    612     -6    232  A    C  
ATOM   1655  CD  LYS A 220      30.678 107.419 266.014  1.00 38.23      A    C  
ANISOU 1655  CD  LYS A 220     6459   2920   5146    715     60    176  A    C  
ATOM   1656  CE  LYS A 220      31.014 106.166 266.827  1.00 43.84      A    C  
ANISOU 1656  CE  LYS A 220     7379   3413   5866    855    209    334  A    C  
ATOM   1657  NZ  LYS A 220      31.467 105.039 265.960  1.00 47.99      A    N1+
ANISOU 1657  NZ  LYS A 220     8095   3710   6430    979    291    281  A    N1+
ATOM   1658  N   VAL A 221      31.689 112.194 267.228  1.00 33.90      A    N  
ANISOU 1658  N   VAL A 221     5227   3356   4295    656   -300    259  A    N  
ATOM   1659  CA  VAL A 221      32.808 112.764 267.969  1.00 31.88      A    C  
ANISOU 1659  CA  VAL A 221     4882   3327   3903    780   -339    377  A    C  
ATOM   1660  C   VAL A 221      32.250 113.709 269.020  1.00 28.74      A    C  
ANISOU 1660  C   VAL A 221     4397   3048   3475    647   -354    403  A    C  
ATOM   1661  O   VAL A 221      32.577 113.612 270.245  1.00 27.65      A    O  
ANISOU 1661  O   VAL A 221     4269   2983   3252    701   -323    534  A    O  
ATOM   1662  CB  VAL A 221      33.777 113.509 267.029  1.00 32.67      A    C  
ANISOU 1662  CB  VAL A 221     4862   3614   3936    853   -430    321  A    C  
ATOM   1663  CG1 VAL A 221      34.888 114.190 267.823  1.00 32.87      A    C  
ANISOU 1663  CG1 VAL A 221     4771   3901   3816    940   -475    427  A    C  
ATOM   1664  CG2 VAL A 221      34.359 112.542 266.007  1.00 24.86      A    C  
ANISOU 1664  CG2 VAL A 221     3966   2515   2966   1001   -404    295  A    C  
ATOM   1665  N   PHE A 222      31.367 114.599 268.560  1.00 27.95      A    N  
ANISOU 1665  N   PHE A 222     4217   2965   3438    482   -394    282  A    N  
ATOM   1666  CA  PHE A 222      30.810 115.541 269.535  1.00 26.13      A    C  
ANISOU 1666  CA  PHE A 222     3912   2836   3180    364   -395    297  A    C  
ATOM   1667  C   PHE A 222      30.112 114.851 270.726  1.00 25.37      A    C  
ANISOU 1667  C   PHE A 222     3907   2627   3103    323   -300    389  A    C  
ATOM   1668  O   PHE A 222      30.336 115.204 271.877  1.00 30.31      A    O  
ANISOU 1668  O   PHE A 222     4511   3370   3637    332   -286    477  A    O  
ATOM   1669  CB  PHE A 222      29.868 116.557 268.886  1.00 27.38      A    C  
ANISOU 1669  CB  PHE A 222     3979   3014   3409    213   -434    167  A    C  
ATOM   1670  CG  PHE A 222      29.142 117.408 269.886  1.00 27.07      A    C  
ANISOU 1670  CG  PHE A 222     3888   3039   3358     99   -409    178  A    C  
ATOM   1671  CD1 PHE A 222      27.786 117.230 270.119  1.00 26.42      A    C  
ANISOU 1671  CD1 PHE A 222     3823   2843   3374    -25   -352    146  A    C  
ATOM   1672  CD2 PHE A 222      29.825 118.367 270.617  1.00 30.06      A    C  
ANISOU 1672  CD2 PHE A 222     4200   3601   3623    112   -436    214  A    C  
ATOM   1673  CE1 PHE A 222      27.123 118.005 271.055  1.00 34.13      A    C  
ANISOU 1673  CE1 PHE A 222     4753   3882   4334   -114   -317    158  A    C  
ATOM   1674  CE2 PHE A 222      29.170 119.145 271.556  1.00 29.94      A    C  
ANISOU 1674  CE2 PHE A 222     4151   3635   3588     11   -402    213  A    C  
ATOM   1675  CZ  PHE A 222      27.817 118.964 271.775  1.00 34.07      A    C  
ANISOU 1675  CZ  PHE A 222     4695   4039   4209    -91   -339    189  A    C  
ATOM   1676  N   THR A 223      29.300 113.848 270.434  1.00 31.94      A    N  
ANISOU 1676  N   THR A 223     4847   3237   4050    273   -231    366  A    N  
ATOM   1677  CA  THR A 223      28.498 113.127 271.417  1.00 31.58      A    C  
ANISOU 1677  CA  THR A 223     4898   3053   4047    209   -124    445  A    C  
ATOM   1678  C   THR A 223      29.390 112.375 272.382  1.00 32.48      A    C  
ANISOU 1678  C   THR A 223     5109   3170   4061    375    -69    621  A    C  
ATOM   1679  O   THR A 223      29.125 112.341 273.582  1.00 35.57      A    O  
ANISOU 1679  O   THR A 223     5524   3589   4403    357    -10    725  A    O  
ATOM   1680  CB  THR A 223      27.519 112.132 270.730  1.00 33.10      A    C  
ANISOU 1680  CB  THR A 223     5192   2995   4390    105    -58    367  A    C  
ATOM   1681  CG2 THR A 223      26.767 111.307 271.754  1.00 34.76      A    C  
ANISOU 1681  CG2 THR A 223     5513   3048   4645     36     71    462  A    C  
ATOM   1682  OG1 THR A 223      26.565 112.861 269.945  1.00 36.55      A    O  
ANISOU 1682  OG1 THR A 223     5516   3465   4905    -53   -111    215  A    O  
ATOM   1683  N   LYS A 224      30.443 111.763 271.848  1.00 29.26      A    N  
ANISOU 1683  N   LYS A 224     4755   2745   3617    550    -83    659  A    N  
ATOM   1684  CA  LYS A 224      31.419 111.073 272.675  1.00 36.38      A    C  
ANISOU 1684  CA  LYS A 224     5732   3683   4409    749    -39    839  A    C  
ATOM   1685  C   LYS A 224      31.989 112.058 273.665  1.00 40.63      A    C  
ANISOU 1685  C   LYS A 224     6139   4509   4790    772   -102    909  A    C  
ATOM   1686  O   LYS A 224      32.129 111.749 274.853  1.00 41.72      A    O  
ANISOU 1686  O   LYS A 224     6320   4694   4837    835    -49   1056  A    O  
ATOM   1687  CB  LYS A 224      32.539 110.493 271.810  1.00 41.81      A    C  
ANISOU 1687  CB  LYS A 224     6457   4357   5071    947    -59    852  A    C  
ATOM   1688  CG  LYS A 224      33.612 109.724 272.576  1.00 55.35      A    C  
ANISOU 1688  CG  LYS A 224     8241   6122   6667   1193    -12   1052  A    C  
ATOM   1689  CD  LYS A 224      33.032 108.750 273.589  1.00 70.00      A    C  
ANISOU 1689  CD  LYS A 224    10263   7785   8547   1206    124   1193  A    C  
ATOM   1690  CE  LYS A 224      34.096 107.792 274.134  1.00 75.94      A    C  
ANISOU 1690  CE  LYS A 224    11116   8543   9196   1491    189   1402  A    C  
ATOM   1691  NZ  LYS A 224      35.094 108.435 275.045  1.00 77.81      A    N1+
ANISOU 1691  NZ  LYS A 224    11204   9132   9230   1620    108   1529  A    N1+
ATOM   1692  N   ARG A 225      32.281 113.266 273.196  1.00 42.30      A    N  
ANISOU 1692  N   ARG A 225     6196   4911   4964    710   -208    802  A    N  
ATOM   1693  CA  ARG A 225      32.782 114.252 274.147  1.00 43.60      A    C  
ANISOU 1693  CA  ARG A 225     6244   5342   4980    699   -262    843  A    C  
ATOM   1694  C   ARG A 225      31.738 114.704 275.184  1.00 41.98      A    C  
ANISOU 1694  C   ARG A 225     6042   5132   4776    545   -213    845  A    C  
ATOM   1695  O   ARG A 225      32.044 114.845 276.365  1.00 40.97      A    O  
ANISOU 1695  O   ARG A 225     5903   5149   4515    577   -201    946  A    O  
ATOM   1696  CB  ARG A 225      33.389 115.448 273.411  1.00 49.17      A    C  
ANISOU 1696  CB  ARG A 225     6799   6236   5647    659   -371    729  A    C  
ATOM   1697  CG  ARG A 225      34.033 116.469 274.336  1.00 62.42      A    C  
ANISOU 1697  CG  ARG A 225     8361   8193   7164    632   -426    752  A    C  
ATOM   1698  CD  ARG A 225      34.980 115.807 275.352  1.00 73.86      A    C  
ANISOU 1698  CD  ARG A 225     9822   9787   8454    801   -417    925  A    C  
ATOM   1699  NE  ARG A 225      36.360 115.707 274.882  1.00 79.85      A    N  
ANISOU 1699  NE  ARG A 225    10499  10721   9121    958   -484    965  A    N  
ATOM   1700  CZ  ARG A 225      37.128 114.629 275.016  1.00 86.42      A    C  
ANISOU 1700  CZ  ARG A 225    11380  11562   9895   1178   -458   1111  A    C  
ATOM   1701  NH1 ARG A 225      36.658 113.527 275.587  1.00 88.22      A    N1+
ANISOU 1701  NH1 ARG A 225    11760  11608  10152   1264   -360   1233  A    N1+
ATOM   1702  NH2 ARG A 225      38.374 114.652 274.566  1.00 88.21      A    N  
ANISOU 1702  NH2 ARG A 225    11505  11979  10034   1318   -520   1140  A    N  
ATOM   1703  N   ILE A 226      30.507 114.916 274.737  1.00 43.15      A    N  
ANISOU 1703  N   ILE A 226     6200   5130   5066    384   -182    735  A    N  
ATOM   1704  CA  ILE A 226      29.472 115.541 275.558  1.00 43.73      A    C  
ANISOU 1704  CA  ILE A 226     6248   5219   5148    233   -138    712  A    C  
ATOM   1705  C   ILE A 226      28.745 114.602 276.533  1.00 43.47      A    C  
ANISOU 1705  C   ILE A 226     6333   5049   5136    217    -17    827  A    C  
ATOM   1706  O   ILE A 226      28.121 115.057 277.492  1.00 42.17      A    O  
ANISOU 1706  O   ILE A 226     6150   4942   4931    130     29    846  A    O  
ATOM   1707  CB  ILE A 226      28.438 116.271 274.647  1.00 43.85      A    C  
ANISOU 1707  CB  ILE A 226     6196   5167   5299     78   -159    550  A    C  
ATOM   1708  CG1 ILE A 226      27.923 117.547 275.301  1.00 48.78      A    C  
ANISOU 1708  CG1 ILE A 226     6733   5921   5879    -34   -160    497  A    C  
ATOM   1709  CG2 ILE A 226      27.262 115.380 274.304  1.00 43.11      A    C  
ANISOU 1709  CG2 ILE A 226     6178   4843   5358     -8    -80    527  A    C  
ATOM   1710  CD1 ILE A 226      28.988 118.541 275.616  1.00 53.59      A    C  
ANISOU 1710  CD1 ILE A 226     7266   6753   6343      5   -233    489  A    C  
ATOM   1711  N  ASER A 227      28.825 113.298 276.281  0.52 43.14      A    N  
ANISOU 1711  N  ASER A 227     6420   4815   5155    301     47    903  A    N  
ATOM   1712  N  BSER A 227      28.832 113.298 276.280  0.48 43.13      A    N  
ANISOU 1712  N  BSER A 227     6418   4815   5153    302     46    904  A    N  
ATOM   1713  CA ASER A 227      28.166 112.308 277.129  0.52 43.83      A    C  
ANISOU 1713  CA ASER A 227     6641   4740   5273    286    180   1024  A    C  
ATOM   1714  CA BSER A 227      28.170 112.308 277.123  0.48 43.78      A    C  
ANISOU 1714  CA BSER A 227     6634   4733   5267    286    179   1024  A    C  
ATOM   1715  C  ASER A 227      28.874 112.139 278.470  0.52 44.84      A    C  
ANISOU 1715  C  ASER A 227     6802   5014   5222    418    209   1206  A    C  
ATOM   1716  C  BSER A 227      28.866 112.154 278.469  0.48 44.89      A    C  
ANISOU 1716  C  BSER A 227     6806   5022   5228    416    208   1204  A    C  
ATOM   1717  O  ASER A 227      28.351 111.502 279.383  0.52 44.61      A    O  
ANISOU 1717  O  ASER A 227     6872   4894   5184    407    323   1326  A    O  
ATOM   1718  O  BSER A 227      28.323 111.545 279.387  0.48 44.74      A    O  
ANISOU 1718  O  BSER A 227     6883   4914   5200    401    321   1321  A    O  
ATOM   1719  CB ASER A 227      28.027 110.963 276.409  0.52 42.56      A    C  
ANISOU 1719  CB ASER A 227     6630   4300   5240    325    255   1041  A    C  
ATOM   1720  CB BSER A 227      28.092 110.952 276.414  0.48 42.64      A    C  
ANISOU 1720  CB BSER A 227     6641   4315   5244    335    253   1046  A    C  
ATOM   1721  OG ASER A 227      29.294 110.406 276.105  0.52 40.90      A    O  
ANISOU 1721  OG ASER A 227     6474   4108   4959    540    226   1120  A    O  
ATOM   1722  OG BSER A 227      26.990 110.896 275.527  0.48 40.31      A    O  
ANISOU 1722  OG BSER A 227     6340   3858   5119    155    269    894  A    O  
ATOM   1723  N   LYS A 228      30.071 112.704 278.581  1.00 49.88      A    N  
ANISOU 1723  N   LYS A 228     7350   5892   5709    540    108   1229  A    N  
ATOM   1724  CA  LYS A 228      30.819 112.635 279.826  1.00 59.80      A    C  
ANISOU 1724  CA  LYS A 228     8608   7346   6767    668    113   1391  A    C  
ATOM   1725  C   LYS A 228      30.298 113.688 280.788  1.00 58.37      A    C  
ANISOU 1725  C   LYS A 228     8346   7335   6496    528    107   1349  A    C  
ATOM   1726  O   LYS A 228      30.356 113.512 282.006  1.00 62.82      A    O  
ANISOU 1726  O   LYS A 228     8945   8002   6922    573    156   1480  A    O  
ATOM   1727  CB  LYS A 228      32.314 112.845 279.565  1.00 66.47      A    C  
ANISOU 1727  CB  LYS A 228     9365   8416   7477    839      2   1423  A    C  
ATOM   1728  CG  LYS A 228      32.907 111.774 278.666  1.00 69.68      A    C  
ANISOU 1728  CG  LYS A 228     9858   8663   7955   1010     20   1475  A    C  
ATOM   1729  CD  LYS A 228      34.350 112.045 278.259  1.00 74.90      A    C  
ANISOU 1729  CD  LYS A 228    10404   9558   8495   1172    -90   1490  A    C  
ATOM   1730  CE  LYS A 228      34.879 110.846 277.468  1.00 84.78      A    C  
ANISOU 1730  CE  LYS A 228    11769  10629   9816   1370    -42   1561  A    C  
ATOM   1731  NZ  LYS A 228      36.263 111.005 276.930  1.00 89.55      A    N1+
ANISOU 1731  NZ  LYS A 228    12258  11447  10320   1544   -135   1577  A    N1+
ATOM   1732  N   LYS A 229      29.795 114.787 280.237  1.00 49.60      A    N  
ANISOU 1732  N   LYS A 229     7134   6257   5456    369     52   1169  A    N  
ATOM   1733  CA  LYS A 229      29.280 115.867 281.072  1.00 46.21      A    C  
ANISOU 1733  CA  LYS A 229     6636   5971   4949    239     57   1108  A    C  
ATOM   1734  C   LYS A 229      27.749 116.014 281.125  1.00 37.47      A    C  
ANISOU 1734  C   LYS A 229     5551   4700   3984     72    151   1040  A    C  
ATOM   1735  O   LYS A 229      27.210 116.453 282.140  1.00 38.69      A    O  
ANISOU 1735  O   LYS A 229     5702   4934   4066      2    209   1055  A    O  
ATOM   1736  CB  LYS A 229      30.031 117.195 280.855  1.00 46.00      A    C  
ANISOU 1736  CB  LYS A 229     6476   6175   4828    203    -61    986  A    C  
ATOM   1737  CG  LYS A 229      29.979 117.836 279.485  1.00 48.76      A    C  
ANISOU 1737  CG  LYS A 229     6755   6464   5309    139   -129    829  A    C  
ATOM   1738  CD  LYS A 229      30.717 119.183 279.559  1.00 54.61      A    C  
ANISOU 1738  CD  LYS A 229     7381   7435   5931     88   -217    729  A    C  
ATOM   1739  CE  LYS A 229      30.857 119.866 278.208  1.00 60.49      A    C  
ANISOU 1739  CE  LYS A 229     8057   8144   6782     44   -285    594  A    C  
ATOM   1740  NZ  LYS A 229      31.700 121.098 278.292  1.00 63.85      A    N1+
ANISOU 1740  NZ  LYS A 229     8387   8784   7090     -9   -358    510  A    N1+
ATOM   1741  N   PHE A 230      27.050 115.649 280.051  1.00 30.92      A    N  
ANISOU 1741  N   PHE A 230     4736   3664   3346      9    168    963  A    N  
ATOM   1742  CA  PHE A 230      25.588 115.739 280.060  1.00 33.08      A    C  
ANISOU 1742  CA  PHE A 230     5006   3809   3754   -149    254    901  A    C  
ATOM   1743  C   PHE A 230      24.985 114.337 280.148  1.00 38.27      A    C  
ANISOU 1743  C   PHE A 230     5791   4238   4514   -157    369   1002  A    C  
ATOM   1744  O   PHE A 230      25.577 113.369 279.667  1.00 41.63      A    O  
ANISOU 1744  O   PHE A 230     6304   4544   4968    -56    368   1062  A    O  
ATOM   1745  CB  PHE A 230      25.036 116.421 278.794  1.00 30.83      A    C  
ANISOU 1745  CB  PHE A 230     4626   3476   3611   -245    193    728  A    C  
ATOM   1746  CG  PHE A 230      25.583 117.806 278.528  1.00 30.37      A    C  
ANISOU 1746  CG  PHE A 230     4460   3600   3480   -246     94    623  A    C  
ATOM   1747  CD1 PHE A 230      26.320 118.491 279.482  1.00 28.04      A    C  
ANISOU 1747  CD1 PHE A 230     4145   3500   3009   -210     71    655  A    C  
ATOM   1748  CD2 PHE A 230      25.324 118.434 277.313  1.00 32.39      A    C  
ANISOU 1748  CD2 PHE A 230     4637   3829   3841   -294     30    490  A    C  
ATOM   1749  CE1 PHE A 230      26.817 119.767 279.218  1.00 27.91      A    C  
ANISOU 1749  CE1 PHE A 230     4043   3629   2934   -235     -7    547  A    C  
ATOM   1750  CE2 PHE A 230      25.815 119.708 277.047  1.00 29.52      A    C  
ANISOU 1750  CE2 PHE A 230     4191   3606   3418   -299    -43    401  A    C  
ATOM   1751  CZ  PHE A 230      26.559 120.373 278.003  1.00 27.77      A    C  
ANISOU 1751  CZ  PHE A 230     3961   3557   3034   -279    -56    426  A    C  
ATOM   1752  N   ASN A 231      23.805 114.235 280.757  1.00 38.56      A    N  
ANISOU 1752  N   ASN A 231     5839   4207   4605   -281    481   1018  A    N  
ATOM   1753  CA  ASN A 231      22.998 113.015 280.690  1.00 40.13      A    C  
ANISOU 1753  CA  ASN A 231     6143   4167   4936   -349    602   1077  A    C  
ATOM   1754  C   ASN A 231      22.044 113.083 279.502  1.00 37.48      A    C  
ANISOU 1754  C   ASN A 231     5737   3713   4791   -499    585    917  A    C  
ATOM   1755  O   ASN A 231      20.969 113.683 279.597  1.00 38.18      A    O  
ANISOU 1755  O   ASN A 231     5727   3841   4938   -635    617    842  A    O  
ATOM   1756  CB  ASN A 231      22.227 112.797 282.001  1.00 43.55      A    C  
ANISOU 1756  CB  ASN A 231     6622   4602   5324   -412    743   1191  A    C  
ATOM   1757  CG  ASN A 231      21.301 111.580 281.956  1.00 47.02      A    C  
ANISOU 1757  CG  ASN A 231     7166   4788   5911   -519    886   1248  A    C  
ATOM   1758  ND2 ASN A 231      20.264 111.598 282.784  1.00 43.32      A    N  
ANISOU 1758  ND2 ASN A 231     6685   4319   5456   -639   1008   1289  A    N  
ATOM   1759  OD1 ASN A 231      21.528 110.634 281.204  1.00 53.53      A    O  
ANISOU 1759  OD1 ASN A 231     8087   5420   6834   -498    896   1251  A    O  
ATOM   1760  N   LEU A 232      22.435 112.469 278.388  1.00 33.19      A    N  
ANISOU 1760  N   LEU A 232     5239   3040   4333   -466    536    865  A    N  
ATOM   1761  CA  LEU A 232      21.665 112.582 277.153  1.00 36.20      A    C  
ANISOU 1761  CA  LEU A 232     5541   3347   4867   -595    494    700  A    C  
ATOM   1762  C   LEU A 232      20.556 111.550 277.087  1.00 35.76      A    C  
ANISOU 1762  C   LEU A 232     5551   3082   4955   -754    616    698  A    C  
ATOM   1763  O   LEU A 232      20.802 110.349 277.204  1.00 34.16      A    O  
ANISOU 1763  O   LEU A 232     5512   2686   4782   -725    700    785  A    O  
ATOM   1764  CB  LEU A 232      22.556 112.406 275.921  1.00 39.04      A    C  
ANISOU 1764  CB  LEU A 232     5917   3671   5244   -500    387    626  A    C  
ATOM   1765  CG  LEU A 232      23.655 113.416 275.630  1.00 40.33      A    C  
ANISOU 1765  CG  LEU A 232     5998   4032   5294   -370    255    594  A    C  
ATOM   1766  CD1 LEU A 232      24.466 112.967 274.420  1.00 39.62      A    C  
ANISOU 1766  CD1 LEU A 232     5947   3874   5233   -277    180    538  A    C  
ATOM   1767  CD2 LEU A 232      23.042 114.780 275.388  1.00 40.69      A    C  
ANISOU 1767  CD2 LEU A 232     5881   4231   5350   -461    195    477  A    C  
ATOM   1768  N   MET A 233      19.330 112.031 276.918  1.00 33.76      A    N  
ANISOU 1768  N   MET A 233     5167   2871   4788   -923    633    601  A    N  
ATOM   1769  CA  MET A 233      18.185 111.146 276.778  1.00 35.87      A    C  
ANISOU 1769  CA  MET A 233     5460   2973   5197  -1112    741    574  A    C  
ATOM   1770  C   MET A 233      17.568 111.325 275.394  1.00 33.83      A    C  
ANISOU 1770  C   MET A 233     5082   2717   5054  -1230    654    388  A    C  
ATOM   1771  O   MET A 233      16.711 112.183 275.182  1.00 33.06      A    O  
ANISOU 1771  O   MET A 233     4806   2767   4987  -1318    619    301  A    O  
ATOM   1772  CB  MET A 233      17.174 111.391 277.897  1.00 36.02      A    C  
ANISOU 1772  CB  MET A 233     5420   3055   5212  -1219    859    642  A    C  
ATOM   1773  CG  MET A 233      17.686 110.941 279.263  1.00 40.16      A    C  
ANISOU 1773  CG  MET A 233     6088   3548   5622  -1121    967    838  A    C  
ATOM   1774  SD  MET A 233      16.584 111.357 280.624  1.00 51.22      A    S  
ANISOU 1774  SD  MET A 233     7417   5057   6987  -1226   1107    918  A    S  
ATOM   1775  CE  MET A 233      17.023 113.073 280.882  1.00 33.32      A    C  
ANISOU 1775  CE  MET A 233     5004   3080   4577  -1107    985    858  A    C  
ATOM   1776  N   LEU A 234      18.045 110.521 274.451  1.00 34.07      A    N  
ANISOU 1776  N   LEU A 234     5213   2596   5137  -1215    621    329  A    N  
ATOM   1777  CA  LEU A 234      17.575 110.576 273.073  1.00 34.34      A    C  
ANISOU 1777  CA  LEU A 234     5153   2636   5261  -1319    532    148  A    C  
ATOM   1778  C   LEU A 234      16.334 109.715 272.851  1.00 36.24      A    C  
ANISOU 1778  C   LEU A 234     5388   2743   5638  -1564    625     76  A    C  
ATOM   1779  O   LEU A 234      16.043 108.815 273.643  1.00 42.69      A    O  
ANISOU 1779  O   LEU A 234     6333   3394   6495  -1642    772    172  A    O  
ATOM   1780  CB  LEU A 234      18.695 110.193 272.098  1.00 34.60      A    C  
ANISOU 1780  CB  LEU A 234     5288   2588   5269  -1186    448    100  A    C  
ATOM   1781  CG  LEU A 234      19.897 111.150 272.125  1.00 38.59      A    C  
ANISOU 1781  CG  LEU A 234     5757   3262   5643   -969    338    145  A    C  
ATOM   1782  CD1 LEU A 234      21.063 110.630 271.294  1.00 36.06      A    C  
ANISOU 1782  CD1 LEU A 234     5549   2856   5294   -825    281    124  A    C  
ATOM   1783  CD2 LEU A 234      19.472 112.522 271.634  1.00 28.37      A    C  
ANISOU 1783  CD2 LEU A 234     4255   2192   4333   -993    229     47  A    C  
ATOM   1784  N   GLU A 235      15.605 110.024 271.780  1.00 35.83      A    N  
ANISOU 1784  N   GLU A 235     5182   2781   5650  -1689    540    -91  A    N  
ATOM   1785  CA  GLU A 235      14.359 109.349 271.428  1.00 37.94      A    C  
ANISOU 1785  CA  GLU A 235     5395   2982   6041  -1949    602   -193  A    C  
ATOM   1786  C   GLU A 235      13.417 109.292 272.623  1.00 41.99      A    C  
ANISOU 1786  C   GLU A 235     5852   3526   6577  -2053    731    -88  A    C  
ATOM   1787  O   GLU A 235      12.761 108.279 272.868  1.00 43.75      A    O  
ANISOU 1787  O   GLU A 235     6123   3644   6857  -2169    811    -71  A    O  
ATOM   1788  CB  GLU A 235      14.670 107.939 270.924  1.00 38.42      A    C  
ANISOU 1788  CB  GLU A 235     5644   2811   6145  -1970    632   -226  A    C  
ATOM   1789  CG  GLU A 235      15.510 107.940 269.655  1.00 42.19      A    C  
ANISOU 1789  CG  GLU A 235     6169   3262   6599  -1878    513   -347  A    C  
ATOM   1790  CD  GLU A 235      15.818 106.550 269.140  1.00 51.14      A    C  
ANISOU 1790  CD  GLU A 235     7490   4170   7770  -1884    550   -387  A    C  
ATOM   1791  OE1 GLU A 235      16.774 105.934 269.654  1.00 58.65      A    O  
ANISOU 1791  OE1 GLU A 235     8653   4936   8696  -1743    633   -269  A    O  
ATOM   1792  OE2 GLU A 235      15.127 106.087 268.209  1.00 51.28      A    O1-
ANISOU 1792  OE2 GLU A 235     7445   4206   7834  -2017    497   -534  A    O1-
ATOM   1793  N   THR A 236      13.364 110.396 273.362  1.00 38.28      A    N  
ANISOU 1793  N   THR A 236     5272   3235   6038  -1968    728    -13  A    N  
ATOM   1794  CA  THR A 236      12.566 110.503 274.578  1.00 43.23      A    C  
ANISOU 1794  CA  THR A 236     5849   3908   6670  -2047    862     92  A    C  
ATOM   1795  C   THR A 236      11.781 111.812 274.515  1.00 42.05      A    C  
ANISOU 1795  C   THR A 236     5445   4032   6502  -2047    801     38  A    C  
ATOM   1796  O   THR A 236      12.288 112.790 273.966  1.00 35.76      A    O  
ANISOU 1796  O   THR A 236     4573   3371   5642  -1900    670    -10  A    O  
ATOM   1797  CB  THR A 236      13.490 110.515 275.814  1.00 43.58      A    C  
ANISOU 1797  CB  THR A 236     6055   3904   6601  -1870    932    277  A    C  
ATOM   1798  CG2 THR A 236      12.691 110.697 277.095  1.00 42.24      A    C  
ANISOU 1798  CG2 THR A 236     5834   3800   6414  -1938   1072    387  A    C  
ATOM   1799  OG1 THR A 236      14.224 109.283 275.879  1.00 46.11      A    O  
ANISOU 1799  OG1 THR A 236     6615   3970   6935  -1840    999    347  A    O  
ATOM   1800  N   LYS A 237      10.556 111.847 275.044  1.00 41.28      A    N  
ANISOU 1800  N   LYS A 237     5213   4013   6460  -2203    902     50  A    N  
ATOM   1801  CA  LYS A 237       9.798 113.102 275.023  1.00 47.32      A    C  
ANISOU 1801  CA  LYS A 237     5737   5038   7205  -2173    860     11  A    C  
ATOM   1802  C   LYS A 237       9.176 113.428 276.377  1.00 48.49      A    C  
ANISOU 1802  C   LYS A 237     5841   5260   7322  -2187   1006    128  A    C  
ATOM   1803  O   LYS A 237       8.871 112.531 277.165  1.00 48.85      A    O  
ANISOU 1803  O   LYS A 237     5982   5185   7394  -2291   1141    216  A    O  
ATOM   1804  CB  LYS A 237       8.681 113.103 273.973  1.00 50.42      A    C  
ANISOU 1804  CB  LYS A 237     5913   5563   7680  -2316    788   -127  A    C  
ATOM   1805  CG  LYS A 237       7.442 112.295 274.328  1.00 55.02      A    C  
ANISOU 1805  CG  LYS A 237     6424   6154   8325  -2482    870   -107  A    C  
ATOM   1806  CD  LYS A 237       6.534 112.139 273.116  1.00 62.48      A    C  
ANISOU 1806  CD  LYS A 237     7187   7228   9324  -2588    757   -244  A    C  
ATOM   1807  CE  LYS A 237       5.123 111.760 273.526  1.00 69.76      A    C  
ANISOU 1807  CE  LYS A 237     7958   8246  10302  -2744    837   -224  A    C  
ATOM   1808  NZ  LYS A 237       4.453 112.938 274.160  1.00 69.54      A    N1+
ANISOU 1808  NZ  LYS A 237     7730   8446  10247  -2680    888   -170  A    N1+
ATOM   1809  N   VAL A 238       8.966 114.719 276.622  1.00 42.47      A    N  
ANISOU 1809  N   VAL A 238     4941   4699   6495  -2064    977    130  A    N  
ATOM   1810  CA  VAL A 238       8.290 115.179 277.829  1.00 43.78      A    C  
ANISOU 1810  CA  VAL A 238     5042   4967   6624  -2065   1114    220  A    C  
ATOM   1811  C   VAL A 238       6.778 115.149 277.608  1.00 45.84      A    C  
ANISOU 1811  C   VAL A 238     5066   5364   6987  -2241   1174    165  A    C  
ATOM   1812  O   VAL A 238       6.279 115.676 276.610  1.00 47.63      A    O  
ANISOU 1812  O   VAL A 238     5106   5736   7255  -2245   1071     58  A    O  
ATOM   1813  CB  VAL A 238       8.722 116.613 278.202  1.00 40.68      A    C  
ANISOU 1813  CB  VAL A 238     4619   4721   6117  -1855   1072    234  A    C  
ATOM   1814  CG1 VAL A 238       7.885 117.144 279.347  1.00 39.18      A    C  
ANISOU 1814  CG1 VAL A 238     4344   4652   5892  -1859   1219    302  A    C  
ATOM   1815  CG2 VAL A 238      10.199 116.654 278.554  1.00 37.73      A    C  
ANISOU 1815  CG2 VAL A 238     4459   4247   5630  -1701   1021    292  A    C  
ATOM   1816  N   THR A 239       6.063 114.512 278.534  1.00 44.51      A    N  
ANISOU 1816  N   THR A 239     4906   5168   6838  -2351   1318    252  A    N  
ATOM   1817  CA  THR A 239       4.610 114.385 278.463  1.00 46.90      A    C  
ANISOU 1817  CA  THR A 239     4993   5619   7207  -2471   1348    229  A    C  
ATOM   1818  C   THR A 239       3.894 115.255 279.492  1.00 52.49      A    C  
ANISOU 1818  C   THR A 239     5573   6502   7867  -2418   1476    300  A    C  
ATOM   1819  O   THR A 239       2.709 115.567 279.334  1.00 56.34      A    O  
ANISOU 1819  O   THR A 239     5832   7176   8398  -2465   1488    273  A    O  
ATOM   1820  CB  THR A 239       4.169 112.930 278.688  1.00 46.75      A    C  
ANISOU 1820  CB  THR A 239     5064   5450   7250  -2637   1407    271  A    C  
ATOM   1821  CG2 THR A 239       4.719 112.033 277.594  1.00 47.38      A    C  
ANISOU 1821  CG2 THR A 239     5257   5362   7382  -2695   1291    182  A    C  
ATOM   1822  OG1 THR A 239       4.656 112.480 279.958  1.00 47.64      A    O  
ANISOU 1822  OG1 THR A 239     5376   5424   7302  -2606   1544    417  A    O  
ATOM   1823  N   ALA A 240       4.598 115.605 280.566  1.00 52.03      A    N  
ANISOU 1823  N   ALA A 240     5668   6391   7712  -2314   1575    396  A    N  
ATOM   1824  CA  ALA A 240       4.027 116.463 281.600  1.00 51.41      A    C  
ANISOU 1824  CA  ALA A 240     5499   6468   7566  -2243   1706    458  A    C  
ATOM   1825  C   ALA A 240       5.090 117.252 282.362  1.00 49.35      A    C  
ANISOU 1825  C   ALA A 240     5404   6186   7160  -2049   1718    510  A    C  
ATOM   1826  O   ALA A 240       6.202 116.773 282.583  1.00 48.35      A    O  
ANISOU 1826  O   ALA A 240     5497   5904   6970  -2000   1680    559  A    O  
ATOM   1827  CB  ALA A 240       3.186 115.638 282.565  1.00 47.07      A    C  
ANISOU 1827  CB  ALA A 240     4953   5909   7025  -2353   1840    564  A    C  
ATOM   1828  N   VAL A 241       4.731 118.474 282.747  1.00 48.80      A    N  
ANISOU 1828  N   VAL A 241     5231   6285   7026  -1916   1752    495  A    N  
ATOM   1829  CA  VAL A 241       5.586 119.353 283.538  1.00 44.35      A    C  
ANISOU 1829  CA  VAL A 241     4812   5733   6308  -1731   1758    525  A    C  
ATOM   1830  C   VAL A 241       4.706 120.005 284.601  1.00 46.91      A    C  
ANISOU 1830  C   VAL A 241     5047   6202   6574  -1697   1930    567  A    C  
ATOM   1831  O   VAL A 241       3.732 120.679 284.272  1.00 46.82      A    O  
ANISOU 1831  O   VAL A 241     4830   6341   6621  -1676   1959    517  A    O  
ATOM   1832  CB  VAL A 241       6.239 120.449 282.661  1.00 39.83      A    C  
ANISOU 1832  CB  VAL A 241     4226   5199   5710  -1569   1599    424  A    C  
ATOM   1833  CG1 VAL A 241       7.094 121.392 283.501  1.00 38.29      A    C  
ANISOU 1833  CG1 VAL A 241     4176   5017   5353  -1407   1614    436  A    C  
ATOM   1834  CG2 VAL A 241       7.076 119.832 281.552  1.00 35.64      A    C  
ANISOU 1834  CG2 VAL A 241     3768   4541   5231  -1595   1433    377  A    C  
ATOM   1835  N   GLU A 242       5.045 119.802 285.870  1.00 50.51      A    N  
ANISOU 1835  N   GLU A 242     5657   6626   6907  -1680   2046    664  A    N  
ATOM   1836  CA  GLU A 242       4.230 120.292 286.978  1.00 56.74      A    C  
ANISOU 1836  CA  GLU A 242     6384   7547   7628  -1657   2228    712  A    C  
ATOM   1837  C   GLU A 242       5.077 121.105 287.937  1.00 58.27      A    C  
ANISOU 1837  C   GLU A 242     6748   7762   7629  -1500   2250    722  A    C  
ATOM   1838  O   GLU A 242       6.115 120.639 288.409  1.00 58.30      A    O  
ANISOU 1838  O   GLU A 242     6949   7673   7529  -1482   2214    780  A    O  
ATOM   1839  CB  GLU A 242       3.581 119.135 287.742  1.00 60.91      A    C  
ANISOU 1839  CB  GLU A 242     6919   8042   8181  -1820   2382    832  A    C  
ATOM   1840  CG  GLU A 242       2.753 119.586 288.947  1.00 66.88      A    C  
ANISOU 1840  CG  GLU A 242     7620   8947   8844  -1771   2541    890  A    C  
ATOM   1841  CD  GLU A 242       2.042 118.438 289.658  1.00 72.80      A    C  
ANISOU 1841  CD  GLU A 242     8368   9681   9612  -1901   2630   1012  A    C  
ATOM   1842  OE1 GLU A 242       2.172 117.279 289.210  1.00 72.64      A    O  
ANISOU 1842  OE1 GLU A 242     8398   9518   9683  -2031   2573   1049  A    O  
ATOM   1843  OE2 GLU A 242       1.360 118.698 290.676  1.00 72.34      A    O1-
ANISOU 1843  OE2 GLU A 242     8266   9745   9473  -1872   2763   1069  A    O1-
ATOM   1844  N   ALA A 243       4.629 122.322 288.224  1.00 57.61      A    N  
ANISOU 1844  N   ALA A 243     6588   7808   7495  -1383   2313    662  A    N  
ATOM   1845  CA  ALA A 243       5.333 123.193 289.155  1.00 56.01      A    C  
ANISOU 1845  CA  ALA A 243     6541   7637   7105  -1251   2349    644  A    C  
ATOM   1846  C   ALA A 243       4.962 122.865 290.597  1.00 57.82      A    C  
ANISOU 1846  C   ALA A 243     6833   7925   7210  -1284   2539    745  A    C  
ATOM   1847  O   ALA A 243       3.794 122.946 290.980  1.00 58.55      A    O  
ANISOU 1847  O   ALA A 243     6785   8118   7342  -1315   2696    771  A    O  
ATOM   1848  CB  ALA A 243       5.012 124.644 288.849  1.00 54.84      A    C  
ANISOU 1848  CB  ALA A 243     6310   7573   6954  -1109   2354    530  A    C  
ATOM   1849  N   LYS A 244       5.958 122.482 291.392  1.00 58.38      A    N  
ANISOU 1849  N   LYS A 244     7107   7951   7124  -1271   2527    809  A    N  
ATOM   1850  CA  LYS A 244       5.748 122.266 292.818  1.00 58.45      A    C  
ANISOU 1850  CA  LYS A 244     7200   8033   6976  -1279   2700    907  A    C  
ATOM   1851  C   LYS A 244       6.758 123.101 293.596  1.00 58.72      A    C  
ANISOU 1851  C   LYS A 244     7406   8123   6784  -1159   2671    855  A    C  
ATOM   1852  O   LYS A 244       7.749 123.572 293.027  1.00 58.49      A    O  
ANISOU 1852  O   LYS A 244     7444   8049   6729  -1098   2508    769  A    O  
ATOM   1853  CB  LYS A 244       5.943 120.787 293.151  1.00 60.97      A    C  
ANISOU 1853  CB  LYS A 244     7605   8258   7302  -1387   2718   1065  A    C  
ATOM   1854  CG  LYS A 244       5.003 119.850 292.408  1.00 67.02      A    C  
ANISOU 1854  CG  LYS A 244     8221   8957   8287  -1527   2714   1102  A    C  
ATOM   1855  CD  LYS A 244       5.246 118.398 292.800  1.00 74.32      A    C  
ANISOU 1855  CD  LYS A 244     9264   9764   9213  -1615   2721   1252  A    C  
ATOM   1856  CE  LYS A 244       4.372 117.436 292.001  1.00 76.27      A    C  
ANISOU 1856  CE  LYS A 244     9380   9927   9674  -1775   2706   1266  A    C  
ATOM   1857  NZ  LYS A 244       4.682 116.011 292.326  1.00 74.43      A    N1+
ANISOU 1857  NZ  LYS A 244     9291   9542   9448  -1855   2717   1404  A    N1+
ATOM   1858  N   GLU A 245       6.563 123.211 294.907  1.00 60.11      A    N  
ANISOU 1858  N   GLU A 245     7652   8400   6785  -1136   2819    909  A    N  
ATOM   1859  CA  GLU A 245       7.336 124.161 295.699  1.00 59.96      A    C  
ANISOU 1859  CA  GLU A 245     7775   8467   6539  -1037   2817    828  A    C  
ATOM   1860  C   GLU A 245       8.819 123.799 295.720  1.00 54.52      A    C  
ANISOU 1860  C   GLU A 245     7247   7741   5727  -1021   2653    852  A    C  
ATOM   1861  O   GLU A 245       9.682 124.679 295.679  1.00 51.26      A    O  
ANISOU 1861  O   GLU A 245     6911   7360   5207   -956   2553    732  A    O  
ATOM   1862  CB  GLU A 245       6.816 124.249 297.134  1.00 66.79      A    C  
ANISOU 1862  CB  GLU A 245     8668   9467   7244   -999   2944    880  A    C  
ATOM   1863  CG  GLU A 245       5.389 124.775 297.278  1.00 78.93      A    C  
ANISOU 1863  CG  GLU A 245    10041  11078   8870   -976   3080    844  A    C  
ATOM   1864  CD  GLU A 245       5.022 125.019 298.733  1.00 89.39      A    C  
ANISOU 1864  CD  GLU A 245    11415  12546  10003   -927   3201    872  A    C  
ATOM   1865  OE1 GLU A 245       5.941 124.998 299.583  1.00 93.14      A    O  
ANISOU 1865  OE1 GLU A 245    12051  13072  10266   -898   3168    888  A    O  
ATOM   1866  OE2 GLU A 245       3.819 125.187 299.036  1.00 91.77      A    O1-
ANISOU 1866  OE2 GLU A 245    11585  12926  10359   -918   3325    883  A    O1-
ATOM   1867  N   ASP A 246       9.111 122.502 295.729  1.00 53.66      A    N  
ANISOU 1867  N   ASP A 246     7184   7561   5643  -1078   2626   1006  A    N  
ATOM   1868  CA  ASP A 246      10.491 122.059 295.846  1.00 56.68      A    C  
ANISOU 1868  CA  ASP A 246     7710   7930   5894  -1040   2485   1058  A    C  
ATOM   1869  C   ASP A 246      11.102 121.861 294.473  1.00 51.79      A    C  
ANISOU 1869  C   ASP A 246     7058   7180   5440  -1044   2295   1006  A    C  
ATOM   1870  O   ASP A 246      12.242 121.407 294.366  1.00 51.66      A    O  
ANISOU 1870  O   ASP A 246     7138   7140   5350  -1007   2168   1053  A    O  
ATOM   1871  CB  ASP A 246      10.576 120.734 296.618  1.00 63.28      A    C  
ANISOU 1871  CB  ASP A 246     8641   8747   6654  -1070   2568   1271  A    C  
ATOM   1872  CG  ASP A 246       9.900 119.581 295.884  1.00 69.08      A    C  
ANISOU 1872  CG  ASP A 246     9305   9314   7629  -1170   2595   1370  A    C  
ATOM   1873  OD1 ASP A 246      10.370 118.430 296.016  1.00 72.65      A    O  
ANISOU 1873  OD1 ASP A 246     9851   9679   8075  -1175   2569   1518  A    O  
ATOM   1874  OD2 ASP A 246       8.909 119.822 295.164  1.00 72.89      A    O1-
ANISOU 1874  OD2 ASP A 246     9634   9755   8305  -1239   2632   1293  A    O1-
ATOM   1875  N   GLY A 247      10.366 122.209 293.420  1.00 50.25      A    N  
ANISOU 1875  N   GLY A 247     6720   6916   5456  -1077   2275    913  A    N  
ATOM   1876  CA  GLY A 247      10.936 122.093 292.090  1.00 45.15      A    C  
ANISOU 1876  CA  GLY A 247     6042   6161   4953  -1076   2096    854  A    C  
ATOM   1877  C   GLY A 247       9.958 121.802 290.971  1.00 42.21      A    C  
ANISOU 1877  C   GLY A 247     5509   5700   4828  -1151   2094    826  A    C  
ATOM   1878  O   GLY A 247       8.750 121.727 291.175  1.00 42.57      A    O  
ANISOU 1878  O   GLY A 247     5443   5778   4953  -1210   2233    849  A    O  
ATOM   1879  N   ILE A 248      10.503 121.616 289.776  1.00 45.50      A    N  
ANISOU 1879  N   ILE A 248     5908   6022   5358  -1150   1933    777  A    N  
ATOM   1880  CA  ILE A 248       9.704 121.333 288.600  1.00 41.31      A    C  
ANISOU 1880  CA  ILE A 248     5227   5423   5046  -1223   1901    736  A    C  
ATOM   1881  C   ILE A 248       9.775 119.843 288.297  1.00 42.51      A    C  
ANISOU 1881  C   ILE A 248     5422   5438   5291  -1324   1890    840  A    C  
ATOM   1882  O   ILE A 248      10.853 119.305 288.023  1.00 41.55      A    O  
ANISOU 1882  O   ILE A 248     5421   5230   5136  -1290   1781    872  A    O  
ATOM   1883  CB  ILE A 248      10.248 122.099 287.385  1.00 38.02      A    C  
ANISOU 1883  CB  ILE A 248     4767   4987   4693  -1157   1732    607  A    C  
ATOM   1884  CG1 ILE A 248      10.400 123.587 287.713  1.00 36.87      A    C  
ANISOU 1884  CG1 ILE A 248     4628   4940   4442  -1051   1745    505  A    C  
ATOM   1885  CG2 ILE A 248       9.381 121.852 286.157  1.00 39.56      A    C  
ANISOU 1885  CG2 ILE A 248     4793   5144   5093  -1226   1693    560  A    C  
ATOM   1886  CD1 ILE A 248       9.090 124.289 288.002  1.00 39.67      A    C  
ANISOU 1886  CD1 ILE A 248     4851   5382   4839  -1041   1892    472  A    C  
ATOM   1887  N   TYR A 249       8.620 119.184 288.315  1.00 41.10      A    N  
ANISOU 1887  N   TYR A 249     5145   5239   5234  -1451   2009    888  A    N  
ATOM   1888  CA  TYR A 249       8.565 117.745 288.084  1.00 46.13      A    C  
ANISOU 1888  CA  TYR A 249     5837   5722   5969  -1573   2033    981  A    C  
ATOM   1889  C   TYR A 249       8.193 117.430 286.648  1.00 48.17      A    C  
ANISOU 1889  C   TYR A 249     5975   5906   6422  -1663   1930    886  A    C  
ATOM   1890  O   TYR A 249       7.142 117.846 286.157  1.00 50.89      A    O  
ANISOU 1890  O   TYR A 249     6125   6338   6874  -1726   1953    809  A    O  
ATOM   1891  CB  TYR A 249       7.603 117.084 289.067  1.00 47.43      A    C  
ANISOU 1891  CB  TYR A 249     5989   5897   6135  -1686   2241   1102  A    C  
ATOM   1892  CG  TYR A 249       8.194 116.948 290.446  1.00 48.84      A    C  
ANISOU 1892  CG  TYR A 249     6342   6107   6110  -1606   2333   1234  A    C  
ATOM   1893  CD1 TYR A 249       8.301 118.045 291.290  1.00 47.88      A    C  
ANISOU 1893  CD1 TYR A 249     6224   6151   5818  -1494   2368   1202  A    C  
ATOM   1894  CD2 TYR A 249       8.624 115.713 290.914  1.00 49.47      A    C  
ANISOU 1894  CD2 TYR A 249     6583   6056   6159  -1635   2381   1389  A    C  
ATOM   1895  CE1 TYR A 249       8.842 117.921 292.550  1.00 51.43      A    C  
ANISOU 1895  CE1 TYR A 249     6824   6656   6060  -1425   2445   1315  A    C  
ATOM   1896  CE2 TYR A 249       9.161 115.578 292.172  1.00 53.77      A    C  
ANISOU 1896  CE2 TYR A 249     7270   6660   6501  -1539   2440   1516  A    C  
ATOM   1897  CZ  TYR A 249       9.267 116.685 292.987  1.00 55.35      A    C  
ANISOU 1897  CZ  TYR A 249     7465   7045   6522  -1446   2480   1480  A    C  
ATOM   1898  OH  TYR A 249       9.804 116.554 294.244  1.00 58.37      A    O  
ANISOU 1898  OH  TYR A 249     7979   7514   6686  -1354   2523   1596  A    O  
ATOM   1899  N  AVAL A 250       9.050 116.666 285.983  0.24 45.44      A    N  
ANISOU 1899  N  AVAL A 250     5741   5410   6113  -1666   1822    894  A    N  
ATOM   1900  N  BVAL A 250       9.068 116.681 285.978  0.76 45.31      A    N  
ANISOU 1900  N  BVAL A 250     5726   5394   6095  -1663   1819    893  A    N  
ATOM   1901  CA AVAL A 250       8.858 116.385 284.571  0.24 44.28      A    C  
ANISOU 1901  CA AVAL A 250     5502   5195   6127  -1741   1708    788  A    C  
ATOM   1902  CA BVAL A 250       8.939 116.405 284.551  0.76 43.33      A    C  
ANISOU 1902  CA BVAL A 250     5390   5073   6001  -1732   1699    787  A    C  
ATOM   1903  C  AVAL A 250       8.757 114.893 284.310  0.24 47.45      A    C  
ANISOU 1903  C  AVAL A 250     5991   5402   6635  -1890   1755    848  A    C  
ATOM   1904  C  BVAL A 250       8.793 114.908 284.273  0.76 47.48      A    C  
ANISOU 1904  C  BVAL A 250     5995   5405   6638  -1885   1748    844  A    C  
ATOM   1905  O  AVAL A 250       9.539 114.087 284.817  0.24 49.02      A    O  
ANISOU 1905  O  AVAL A 250     6387   5466   6772  -1855   1788    961  A    O  
ATOM   1906  O  BVAL A 250       9.616 114.106 284.717  0.76 49.41      A    O  
ANISOU 1906  O  BVAL A 250     6438   5511   6823  -1847   1772    952  A    O  
ATOM   1907  CB AVAL A 250       9.941 117.036 283.677  0.24 39.04      A    C  
ANISOU 1907  CB AVAL A 250     4870   4535   5430  -1603   1515    694  A    C  
ATOM   1908  CB BVAL A 250      10.170 116.933 283.784  0.76 39.83      A    C  
ANISOU 1908  CB BVAL A 250     5010   4616   5508  -1588   1512    712  A    C  
ATOM   1909  CG1AVAL A 250      10.025 118.529 283.944  0.24 37.59      A    C  
ANISOU 1909  CG1AVAL A 250     4619   4517   5147  -1472   1488    631  A    C  
ATOM   1910  CG1BVAL A 250      10.052 116.625 282.299  0.76 37.38      A    C  
ANISOU 1910  CG1BVAL A 250     4618   4240   5344  -1653   1390    603  A    C  
ATOM   1911  CG2AVAL A 250      11.284 116.389 283.899  0.24 38.97      A    C  
ANISOU 1911  CG2AVAL A 250     5070   4406   5330  -1520   1462    774  A    C  
ATOM   1912  CG2BVAL A 250      10.338 118.431 284.007  0.76 34.92      A    C  
ANISOU 1912  CG2BVAL A 250     4327   4157   4785  -1454   1473    645  A    C  
ATOM   1913  N   THR A 251       7.747 114.532 283.539  1.00 49.09      A    N  
ANISOU 1913  N   THR A 251     6049   5603   7001  -2058   1767    771  A    N  
ATOM   1914  CA  THR A 251       7.547 113.146 283.169  1.00 50.42      A    C  
ANISOU 1914  CA  THR A 251     6289   5592   7276  -2200   1781    791  A    C  
ATOM   1915  C   THR A 251       7.959 112.953 281.726  1.00 51.74      A    C  
ANISOU 1915  C   THR A 251     6445   5679   7534  -2224   1627    661  A    C  
ATOM   1916  O   THR A 251       7.594 113.738 280.845  1.00 48.08      A    O  
ANISOU 1916  O   THR A 251     5803   5347   7120  -2233   1535    533  A    O  
ATOM   1917  CB  THR A 251       6.084 112.707 283.347  1.00 51.22      A    C  
ANISOU 1917  CB  THR A 251     6231   5765   7465  -2356   1855    790  A    C  
ATOM   1918  CG2 THR A 251       5.892 111.270 282.849  1.00 49.83      A    C  
ANISOU 1918  CG2 THR A 251     6135   5401   7395  -2496   1840    786  A    C  
ATOM   1919  OG1 THR A 251       5.734 112.783 284.735  1.00 54.10      A    O  
ANISOU 1919  OG1 THR A 251     6623   6194   7738  -2330   2005    921  A    O  
ATOM   1920  N   MET A 252       8.750 111.912 281.500  1.00 53.91      A    N  
ANISOU 1920  N   MET A 252     6918   5744   7821  -2217   1603    699  A    N  
ATOM   1921  CA  MET A 252       9.231 111.607 280.172  1.00 50.96      A    C  
ANISOU 1921  CA  MET A 252     6566   5277   7521  -2230   1465    579  A    C  
ATOM   1922  C   MET A 252       8.771 110.215 279.794  1.00 56.96      A    C  
ANISOU 1922  C   MET A 252     7388   5875   8381  -2367   1481    564  A    C  
ATOM   1923  O   MET A 252       8.542 109.363 280.651  1.00 57.26      A    O  
ANISOU 1923  O   MET A 252     7532   5810   8415  -2410   1601    681  A    O  
ATOM   1924  CB  MET A 252      10.753 111.727 280.102  1.00 48.13      A    C  
ANISOU 1924  CB  MET A 252     6389   4832   7065  -2041   1388    620  A    C  
ATOM   1925  CG  MET A 252      11.257 113.125 280.427  1.00 46.23      A    C  
ANISOU 1925  CG  MET A 252     6078   4797   6691  -1849   1301    616  A    C  
ATOM   1926  SD  MET A 252      13.049 113.222 280.619  1.00 57.28      A    S  
ANISOU 1926  SD  MET A 252     7671   6153   7939  -1610   1202    688  A    S  
ATOM   1927  CE  MET A 252      13.202 113.170 282.403  1.00 57.65      A    C  
ANISOU 1927  CE  MET A 252     7829   6239   7836  -1545   1353    876  A    C  
ATOM   1928  N   GLU A 253       8.635 109.992 278.498  1.00 60.43      A    N  
ANISOU 1928  N   GLU A 253     7761   6295   8902  -2435   1361    416  A    N  
ATOM   1929  CA  GLU A 253       8.313 108.681 277.988  1.00 64.79      A    C  
ANISOU 1929  CA  GLU A 253     8390   6683   9544  -2564   1366    374  A    C  
ATOM   1930  C   GLU A 253       9.244 108.451 276.815  1.00 62.35      A    C  
ANISOU 1930  C   GLU A 253     8178   6264   9247  -2501   1239    271  A    C  
ATOM   1931  O   GLU A 253       9.566 109.387 276.084  1.00 62.19      A    O  
ANISOU 1931  O   GLU A 253     8057   6370   9204  -2430   1120    179  A    O  
ATOM   1932  CB  GLU A 253       6.839 108.694 277.580  1.00 70.49      A    C  
ANISOU 1932  CB  GLU A 253     8877   7557  10349  -2747   1353    279  A    C  
ATOM   1933  CG  GLU A 253       6.418 107.774 276.471  1.00 78.99      A    C  
ANISOU 1933  CG  GLU A 253     9944   8553  11516  -2893   1285    147  A    C  
ATOM   1934  CD  GLU A 253       4.970 108.013 276.084  1.00 85.75      A    C  
ANISOU 1934  CD  GLU A 253    10532   9618  12432  -3052   1259     60  A    C  
ATOM   1935  OE1 GLU A 253       4.161 108.342 276.981  1.00 86.33      A    O  
ANISOU 1935  OE1 GLU A 253    10485   9814  12501  -3093   1357    143  A    O  
ATOM   1936  OE2 GLU A 253       4.646 107.884 274.885  1.00 88.34      A    O1-
ANISOU 1936  OE2 GLU A 253    10762  10000  12801  -3128   1142    -87  A    O1-
ATOM   1937  N   GLY A 254       9.677 107.211 276.630  1.00 62.35      A    N  
ANISOU 1937  N   GLY A 254     8376   6032   9281  -2518   1271    286  A    N  
ATOM   1938  CA  GLY A 254      10.600 106.898 275.557  1.00 59.09      A    C  
ANISOU 1938  CA  GLY A 254     8075   5503   8875  -2444   1168    194  A    C  
ATOM   1939  C   GLY A 254      11.764 106.041 276.022  1.00 58.49      A    C  
ANISOU 1939  C   GLY A 254     8277   5186   8759  -2305   1241    319  A    C  
ATOM   1940  O   GLY A 254      11.799 105.572 277.164  1.00 56.61      A    O  
ANISOU 1940  O   GLY A 254     8153   4866   8492  -2277   1372    480  A    O  
ATOM   1941  N   LYS A 255      12.725 105.852 275.125  1.00 60.61      A    N  
ANISOU 1941  N   LYS A 255     8651   5359   9019  -2203   1155    251  A    N  
ATOM   1942  CA  LYS A 255      13.798 104.876 275.297  1.00 65.35      A    C  
ANISOU 1942  CA  LYS A 255     9511   5724   9595  -2063   1214    346  A    C  
ATOM   1943  C   LYS A 255      14.699 105.084 276.512  1.00 66.30      A    C  
ANISOU 1943  C   LYS A 255     9760   5824   9605  -1869   1293    558  A    C  
ATOM   1944  O   LYS A 255      15.193 104.119 277.100  1.00 64.88      A    O  
ANISOU 1944  O   LYS A 255     9775   5471   9404  -1780   1392    691  A    O  
ATOM   1945  CB  LYS A 255      14.658 104.834 274.031  1.00 66.49      A    C  
ANISOU 1945  CB  LYS A 255     9710   5812   9739  -1973   1095    221  A    C  
ATOM   1946  CG  LYS A 255      13.909 104.343 272.803  1.00 70.98      A    C  
ANISOU 1946  CG  LYS A 255    10202   6369  10397  -2146   1026     21  A    C  
ATOM   1947  CD  LYS A 255      14.841 104.157 271.613  1.00 72.44      A    C  
ANISOU 1947  CD  LYS A 255    10475   6480  10569  -2040    928    -90  A    C  
ATOM   1948  CE  LYS A 255      14.153 103.381 270.494  1.00 75.51      A    C  
ANISOU 1948  CE  LYS A 255    10840   6818  11033  -2209    888   -272  A    C  
ATOM   1949  NZ  LYS A 255      13.100 104.186 269.810  1.00 76.45      A    N1+
ANISOU 1949  NZ  LYS A 255    10695   7184  11170  -2362    771   -415  A    N1+
ATOM   1950  N   LYS A 256      14.910 106.337 276.897  1.00 67.19      A    N  
ANISOU 1950  N   LYS A 256     9765   6126   9640  -1798   1250    592  A    N  
ATOM   1951  CA  LYS A 256      15.873 106.618 277.946  1.00 69.61      A    C  
ANISOU 1951  CA  LYS A 256    10190   6445   9815  -1602   1302    783  A    C  
ATOM   1952  C   LYS A 256      15.154 107.306 279.094  1.00 69.27      A    C  
ANISOU 1952  C   LYS A 256    10036   6565   9719  -1658   1379    870  A    C  
ATOM   1953  O   LYS A 256      15.787 107.872 279.986  1.00 68.80      A    O  
ANISOU 1953  O   LYS A 256    10007   6614   9521  -1504   1389   1000  A    O  
ATOM   1954  CB  LYS A 256      16.961 107.549 277.405  1.00 69.93      A    C  
ANISOU 1954  CB  LYS A 256    10189   6620   9761  -1415   1147    741  A    C  
ATOM   1955  CG  LYS A 256      17.942 106.888 276.436  1.00 72.02      A    C  
ANISOU 1955  CG  LYS A 256    10593   6727  10043  -1301   1088    694  A    C  
ATOM   1956  CD  LYS A 256      18.609 105.640 276.990  1.00 78.43      A    C  
ANISOU 1956  CD  LYS A 256    11658   7303  10837  -1185   1217    861  A    C  
ATOM   1957  CE  LYS A 256      19.594 105.952 278.097  1.00 80.57      A    C  
ANISOU 1957  CE  LYS A 256    11987   7687  10937   -948   1226   1065  A    C  
ATOM   1958  NZ  LYS A 256      20.387 104.737 278.430  1.00 82.74      A    N1+
ANISOU 1958  NZ  LYS A 256    12486   7768  11184   -781   1317   1217  A    N1+
ATOM   1959  N   ALA A 257      13.827 107.246 279.072  1.00 70.26      A    N  
ANISOU 1959  N   ALA A 257    10014   6745   9934  -1858   1413    793  A    N  
ATOM   1960  CA  ALA A 257      13.022 107.864 280.116  1.00 68.36      A    C  
ANISOU 1960  CA  ALA A 257     9655   6665   9652  -1916   1495    863  A    C  
ATOM   1961  C   ALA A 257      13.143 107.088 281.420  1.00 70.71      A    C  
ANISOU 1961  C   ALA A 257    10109   6876   9881  -1859   1638   1064  A    C  
ATOM   1962  O   ALA A 257      13.158 105.857 281.418  1.00 73.02      A    O  
ANISOU 1962  O   ALA A 257    10542   6976  10226  -1882   1697   1108  A    O  
ATOM   1963  CB  ALA A 257      11.569 107.941 279.682  1.00 67.17      A    C  
ANISOU 1963  CB  ALA A 257     9298   6609   9616  -2131   1489    733  A    C  
ATOM   1964  N   PRO A 258      13.226 107.811 282.543  1.00 67.34      A    N  
ANISOU 1964  N   PRO A 258     9661   6597   9327  -1779   1696   1183  A    N  
ATOM   1965  CA  PRO A 258      13.186 107.200 283.875  1.00 62.72      A    C  
ANISOU 1965  CA  PRO A 258     9191   5982   8659  -1732   1830   1373  A    C  
ATOM   1966  C   PRO A 258      11.771 106.756 284.212  1.00 64.04      A    C  
ANISOU 1966  C   PRO A 258     9260   6151   8921  -1934   1929   1358  A    C  
ATOM   1967  O   PRO A 258      10.821 107.230 283.590  1.00 60.24      A    O  
ANISOU 1967  O   PRO A 258     8586   5765   8536  -2086   1889   1212  A    O  
ATOM   1968  CB  PRO A 258      13.614 108.347 284.800  1.00 61.00      A    C  
ANISOU 1968  CB  PRO A 258     8937   5975   8265  -1603   1837   1458  A    C  
ATOM   1969  CG  PRO A 258      14.288 109.350 283.892  1.00 61.27      A    C  
ANISOU 1969  CG  PRO A 258     8897   6102   8281  -1528   1685   1331  A    C  
ATOM   1970  CD  PRO A 258      13.536 109.248 282.609  1.00 62.68      A    C  
ANISOU 1970  CD  PRO A 258     8960   6211   8644  -1705   1633   1147  A    C  
ATOM   1971  N   ALA A 259      11.630 105.863 285.186  1.00 67.78      A    N  
ANISOU 1971  N   ALA A 259     9857   6534   9362  -1929   2055   1513  A    N  
ATOM   1972  CA  ALA A 259      10.315 105.356 285.550  1.00 69.95      A    C  
ANISOU 1972  CA  ALA A 259    10052   6800   9723  -2125   2160   1514  A    C  
ATOM   1973  C   ALA A 259       9.499 106.461 286.204  1.00 70.91      A    C  
ANISOU 1973  C   ALA A 259     9980   7173   9790  -2172   2194   1508  A    C  
ATOM   1974  O   ALA A 259       8.320 106.646 285.895  1.00 72.31      A    O  
ANISOU 1974  O   ALA A 259     9974   7435  10068  -2346   2204   1409  A    O  
ATOM   1975  CB  ALA A 259      10.443 104.163 286.483  1.00 70.90      A    C  
ANISOU 1975  CB  ALA A 259    10367   6761   9811  -2094   2295   1694  A    C  
ATOM   1976  N   GLU A 260      10.139 107.203 287.102  1.00 68.28      A    N  
ANISOU 1976  N   GLU A 260     9683   6972   9287  -2007   2209   1612  A    N  
ATOM   1977  CA  GLU A 260       9.452 108.224 287.881  1.00 67.30      A    C  
ANISOU 1977  CA  GLU A 260     9405   7080   9084  -2024   2262   1620  A    C  
ATOM   1978  C   GLU A 260       9.692 109.617 287.321  1.00 62.01      A    C  
ANISOU 1978  C   GLU A 260     8600   6577   8384  -1967   2158   1490  A    C  
ATOM   1979  O   GLU A 260      10.710 109.863 286.673  1.00 58.53      A    O  
ANISOU 1979  O   GLU A 260     8227   6091   7919  -1863   2053   1448  A    O  
ATOM   1980  CB  GLU A 260       9.915 108.171 289.341  1.00 72.79      A    C  
ANISOU 1980  CB  GLU A 260    10227   7838   9590  -1887   2357   1811  A    C  
ATOM   1981  CG  GLU A 260       9.565 106.889 290.076  1.00 78.53      A    C  
ANISOU 1981  CG  GLU A 260    11078   8426  10333  -1941   2482   1957  A    C  
ATOM   1982  CD  GLU A 260       8.067 106.643 290.130  1.00 84.22      A    C  
ANISOU 1982  CD  GLU A 260    11650   9171  11179  -2160   2572   1914  A    C  
ATOM   1983  OE1 GLU A 260       7.298 107.629 290.187  1.00 83.34      A    O  
ANISOU 1983  OE1 GLU A 260    11342   9259  11066  -2216   2575   1832  A    O  
ATOM   1984  OE2 GLU A 260       7.658 105.463 290.127  1.00 89.87      A    O1-
ANISOU 1984  OE2 GLU A 260    12445   9712  11991  -2271   2646   1963  A    O1-
ATOM   1985  N   PRO A 261       8.749 110.537 287.576  1.00 60.06      A    N  
ANISOU 1985  N   PRO A 261     8161   6524   8135  -2028   2194   1428  A    N  
ATOM   1986  CA  PRO A 261       8.936 111.951 287.235  1.00 55.45      A    C  
ANISOU 1986  CA  PRO A 261     7455   6110   7503  -1958   2123   1318  A    C  
ATOM   1987  C   PRO A 261      10.183 112.496 287.920  1.00 54.98      A    C  
ANISOU 1987  C   PRO A 261     7541   6102   7246  -1770   2111   1401  A    C  
ATOM   1988  O   PRO A 261      10.446 112.148 289.070  1.00 59.60      A    O  
ANISOU 1988  O   PRO A 261     8244   6705   7696  -1698   2194   1549  A    O  
ATOM   1989  CB  PRO A 261       7.681 112.618 287.798  1.00 55.90      A    C  
ANISOU 1989  CB  PRO A 261     7322   6355   7561  -2026   2215   1294  A    C  
ATOM   1990  CG  PRO A 261       6.650 111.537 287.821  1.00 59.26      A    C  
ANISOU 1990  CG  PRO A 261     7703   6703   8109  -2193   2283   1327  A    C  
ATOM   1991  CD  PRO A 261       7.382 110.246 288.045  1.00 60.28      A    C  
ANISOU 1991  CD  PRO A 261     8062   6612   8228  -2178   2303   1446  A    C  
ATOM   1992  N   GLN A 262      10.940 113.338 287.228  1.00 47.23      A    N  
ANISOU 1992  N   GLN A 262     6140   5441   6362  -1246   1572   1604  A    N  
ATOM   1993  CA  GLN A 262      12.192 113.842 287.774  1.00 49.07      A    C  
ANISOU 1993  CA  GLN A 262     6416   5744   6483  -1095   1584   1606  A    C  
ATOM   1994  C   GLN A 262      12.050 115.275 288.259  1.00 43.84      A    C  
ANISOU 1994  C   GLN A 262     5643   5297   5718  -1037   1618   1523  A    C  
ATOM   1995  O   GLN A 262      11.356 116.079 287.640  1.00 42.31      A    O  
ANISOU 1995  O   GLN A 262     5359   5149   5570  -1070   1603   1418  A    O  
ATOM   1996  CB  GLN A 262      13.294 113.769 286.718  1.00 53.15      A    C  
ANISOU 1996  CB  GLN A 262     7027   6110   7058  -1006   1516   1540  A    C  
ATOM   1997  CG  GLN A 262      13.624 112.364 286.266  1.00 58.31      A    C  
ANISOU 1997  CG  GLN A 262     7801   6548   7806  -1036   1477   1607  A    C  
ATOM   1998  CD  GLN A 262      14.183 111.530 287.394  1.00 64.69      A    C  
ANISOU 1998  CD  GLN A 262     8679   7356   8543  -1000   1512   1757  A    C  
ATOM   1999  NE2 GLN A 262      13.585 110.368 287.626  1.00 63.73      A    N  
ANISOU 1999  NE2 GLN A 262     8598   7133   8484  -1107   1520   1861  A    N  
ATOM   2000  OE1 GLN A 262      15.144 111.928 288.055  1.00 67.93      A    O  
ANISOU 2000  OE1 GLN A 262     9107   7859   8843   -879   1529   1781  A    O  
ATOM   2001  N   ARG A 263      12.712 115.587 289.370  1.00 42.87      A    N  
ANISOU 2001  N   ARG A 263     5527   5305   5455   -947   1657   1566  A    N  
ATOM   2002  CA  ARG A 263      12.680 116.937 289.922  1.00 45.69      A    C  
ANISOU 2002  CA  ARG A 263     5789   5865   5705   -881   1685   1476  A    C  
ATOM   2003  C   ARG A 263      13.881 117.758 289.440  1.00 45.62      A    C  
ANISOU 2003  C   ARG A 263     5812   5853   5669   -749   1636   1384  A    C  
ATOM   2004  O   ARG A 263      15.030 117.329 289.551  1.00 47.61      A    O  
ANISOU 2004  O   ARG A 263     6159   6045   5887   -665   1614   1434  A    O  
ATOM   2005  CB  ARG A 263      12.641 116.889 291.456  1.00 49.46      A    C  
ANISOU 2005  CB  ARG A 263     6251   6504   6038   -863   1755   1555  A    C  
ATOM   2006  CG  ARG A 263      12.347 118.233 292.119  1.00 51.88      A    C  
ANISOU 2006  CG  ARG A 263     6451   7023   6238   -815   1791   1448  A    C  
ATOM   2007  CD  ARG A 263      12.796 118.252 293.572  1.00 55.41      A    C  
ANISOU 2007  CD  ARG A 263     6915   7612   6527   -751   1841   1506  A    C  
ATOM   2008  NE  ARG A 263      14.208 117.908 293.670  1.00 59.35      A    N  
ANISOU 2008  NE  ARG A 263     7515   8055   6980   -647   1794   1558  A    N  
ATOM   2009  CZ  ARG A 263      15.205 118.767 293.475  1.00 63.93      A    C  
ANISOU 2009  CZ  ARG A 263     8102   8675   7515   -533   1746   1466  A    C  
ATOM   2010  NH1 ARG A 263      14.951 120.032 293.157  1.00 61.84      A    N1+
ANISOU 2010  NH1 ARG A 263     7754   8494   7248   -510   1735   1316  A    N1+
ATOM   2011  NH2 ARG A 263      16.462 118.355 293.582  1.00 67.00      A    N  
ANISOU 2011  NH2 ARG A 263     8578   9014   7864   -443   1706   1522  A    N  
ATOM   2012  N   TYR A 264      13.599 118.938 288.898  1.00 41.49      A    N  
ANISOU 2012  N   TYR A 264     5206   5395   5163   -730   1619   1252  A    N  
ATOM   2013  CA  TYR A 264      14.634 119.860 288.442  1.00 36.75      A    C  
ANISOU 2013  CA  TYR A 264     4621   4805   4536   -616   1576   1154  A    C  
ATOM   2014  C   TYR A 264      14.467 121.219 289.107  1.00 36.73      A    C  
ANISOU 2014  C   TYR A 264     4517   5001   4436   -564   1595   1055  A    C  
ATOM   2015  O   TYR A 264      13.362 121.583 289.511  1.00 34.45      A    O  
ANISOU 2015  O   TYR A 264     4132   4818   4140   -625   1634   1028  A    O  
ATOM   2016  CB  TYR A 264      14.591 119.996 286.921  1.00 34.29      A    C  
ANISOU 2016  CB  TYR A 264     4324   4345   4359   -639   1522   1071  A    C  
ATOM   2017  CG  TYR A 264      14.957 118.729 286.195  1.00 35.87      A    C  
ANISOU 2017  CG  TYR A 264     4639   4340   4650   -670   1492   1137  A    C  
ATOM   2018  CD1 TYR A 264      16.282 118.433 285.910  1.00 32.72      A    C  
ANISOU 2018  CD1 TYR A 264     4344   3854   4235   -575   1461   1150  A    C  
ATOM   2019  CD2 TYR A 264      13.988 117.801 285.847  1.00 37.18      A    C  
ANISOU 2019  CD2 TYR A 264     4807   4404   4915   -792   1490   1184  A    C  
ATOM   2020  CE1 TYR A 264      16.628 117.270 285.253  1.00 32.58      A    C  
ANISOU 2020  CE1 TYR A 264     4431   3647   4299   -593   1431   1197  A    C  
ATOM   2021  CE2 TYR A 264      14.326 116.635 285.202  1.00 41.26      A    C  
ANISOU 2021  CE2 TYR A 264     5431   4730   5516   -818   1455   1229  A    C  
ATOM   2022  CZ  TYR A 264      15.643 116.370 284.905  1.00 42.12      A    C  
ANISOU 2022  CZ  TYR A 264     5645   4750   5610   -715   1427   1233  A    C  
ATOM   2023  OH  TYR A 264      15.967 115.195 284.259  1.00 42.27      A    O  
ANISOU 2023  OH  TYR A 264     5771   4577   5715   -733   1390   1266  A    O  
ATOM   2024  N   ASP A 265      15.568 121.951 289.250  1.00 35.84      A    N  
ANISOU 2024  N   ASP A 265     4426   4940   4250   -452   1566    997  A    N  
ATOM   2025  CA  ASP A 265      15.512 123.286 289.829  1.00 38.48      A    C  
ANISOU 2025  CA  ASP A 265     4674   5446   4501   -397   1571    881  A    C  
ATOM   2026  C   ASP A 265      15.146 124.306 288.751  1.00 39.57      A    C  
ANISOU 2026  C   ASP A 265     4745   5557   4733   -399   1533    751  A    C  
ATOM   2027  O   ASP A 265      14.656 125.402 289.048  1.00 39.64      A    O  
ANISOU 2027  O   ASP A 265     4659   5689   4715   -381   1538    646  A    O  
ATOM   2028  CB  ASP A 265      16.845 123.634 290.492  1.00 42.07      A    C  
ANISOU 2028  CB  ASP A 265     5177   5969   4838   -284   1546    870  A    C  
ATOM   2029  CG  ASP A 265      17.237 122.635 291.566  1.00 49.23      A    C  
ANISOU 2029  CG  ASP A 265     6149   6905   5653   -273   1577   1004  A    C  
ATOM   2030  OD1 ASP A 265      16.640 122.670 292.664  1.00 57.00      A    O  
ANISOU 2030  OD1 ASP A 265     7090   8012   6554   -297   1630   1024  A    O  
ATOM   2031  OD2 ASP A 265      18.150 121.818 291.311  1.00 49.02      A    O1-
ANISOU 2031  OD2 ASP A 265     6215   6773   5637   -235   1549   1090  A    O1-
ATOM   2032  N   ALA A 266      15.387 123.930 287.498  1.00 38.59      A    N  
ANISOU 2032  N   ALA A 266     4675   5267   4722   -418   1494    753  A    N  
ATOM   2033  CA  ALA A 266      14.994 124.743 286.351  1.00 37.57      A    C  
ANISOU 2033  CA  ALA A 266     4492   5086   4696   -432   1454    642  A    C  
ATOM   2034  C   ALA A 266      14.897 123.879 285.099  1.00 33.61      A    C  
ANISOU 2034  C   ALA A 266     4056   4392   4320   -498   1426    672  A    C  
ATOM   2035  O   ALA A 266      15.623 122.895 284.956  1.00 32.71      A    O  
ANISOU 2035  O   ALA A 266     4050   4170   4209   -489   1421    750  A    O  
ATOM   2036  CB  ALA A 266      15.989 125.878 286.127  1.00 37.31      A    C  
ANISOU 2036  CB  ALA A 266     4458   5089   4628   -330   1410    540  A    C  
ATOM   2037  N   VAL A 267      14.014 124.268 284.184  1.00 31.40      A    N  
ANISOU 2037  N   VAL A 267     3713   4072   4144   -559   1399    599  A    N  
ATOM   2038  CA  VAL A 267      13.868 123.586 282.904  1.00 30.67      A    C  
ANISOU 2038  CA  VAL A 267     3675   3809   4170   -626   1358    596  A    C  
ATOM   2039  C   VAL A 267      13.968 124.616 281.787  1.00 30.56      A    C  
ANISOU 2039  C   VAL A 267     3625   3770   4217   -603   1301    473  A    C  
ATOM   2040  O   VAL A 267      13.206 125.585 281.766  1.00 28.77      A    O  
ANISOU 2040  O   VAL A 267     3289   3632   4010   -608   1291    399  A    O  
ATOM   2041  CB  VAL A 267      12.514 122.837 282.798  1.00 33.18      A    C  
ANISOU 2041  CB  VAL A 267     3947   4097   4562   -748   1365    638  A    C  
ATOM   2042  CG1 VAL A 267      12.318 122.257 281.399  1.00 27.91      A    C  
ANISOU 2042  CG1 VAL A 267     3328   3265   4013   -816   1303    605  A    C  
ATOM   2043  CG2 VAL A 267      12.407 121.744 283.858  1.00 31.61      A    C  
ANISOU 2043  CG2 VAL A 267     3787   3911   4310   -783   1419    771  A    C  
ATOM   2044  N   LEU A 268      14.921 124.416 280.878  1.00 23.04      A    N  
ANISOU 2044  N   LEU A 268     2762   2703   3291   -573   1264    455  A    N  
ATOM   2045  CA  LEU A 268      15.064 125.281 279.717  1.00 24.43      A    C  
ANISOU 2045  CA  LEU A 268     2913   2850   3521   -556   1193    348  A    C  
ATOM   2046  C   LEU A 268      14.314 124.651 278.553  1.00 31.70      A    C  
ANISOU 2046  C   LEU A 268     3843   3651   4549   -655   1152    330  A    C  
ATOM   2047  O   LEU A 268      14.642 123.544 278.119  1.00 31.68      A    O  
ANISOU 2047  O   LEU A 268     3942   3523   4573   -685   1144    373  A    O  
ATOM   2048  CB  LEU A 268      16.545 125.461 279.347  1.00 24.07      A    C  
ANISOU 2048  CB  LEU A 268     2954   2770   3422   -455   1141    327  A    C  
ATOM   2049  CG  LEU A 268      16.837 126.119 277.985  1.00 22.80      A    C  
ANISOU 2049  CG  LEU A 268     2792   2562   3308   -436   1049    233  A    C  
ATOM   2050  CD1 LEU A 268      16.323 127.544 277.922  1.00 20.10      A    C  
ANISOU 2050  CD1 LEU A 268     2335   2316   2986   -420   1021    149  A    C  
ATOM   2051  CD2 LEU A 268      18.316 126.075 277.627  1.00 18.57      A    C  
ANISOU 2051  CD2 LEU A 268     2345   1990   2721   -345   1010    232  A    C  
ATOM   2052  N   VAL A 269      13.303 125.356 278.051  1.00 26.58      A    N  
ANISOU 2052  N   VAL A 269     3091   3046   3962   -700   1119    261  A    N  
ATOM   2053  CA  VAL A 269      12.546 124.874 276.906  1.00 26.13      A    C  
ANISOU 2053  CA  VAL A 269     3032   2903   3995   -786   1055    230  A    C  
ATOM   2054  C   VAL A 269      13.179 125.444 275.638  1.00 27.48      A    C  
ANISOU 2054  C   VAL A 269     3231   3024   4187   -747    976    149  A    C  
ATOM   2055  O   VAL A 269      12.985 126.612 275.302  1.00 27.49      A    O  
ANISOU 2055  O   VAL A 269     3151   3096   4197   -711    934     83  A    O  
ATOM   2056  CB  VAL A 269      11.054 125.267 276.996  1.00 24.76      A    C  
ANISOU 2056  CB  VAL A 269     2728   2813   3866   -848   1042    207  A    C  
ATOM   2057  CG1 VAL A 269      10.300 124.742 275.802  1.00 26.81      A    C  
ANISOU 2057  CG1 VAL A 269     2985   2994   4206   -934    967    175  A    C  
ATOM   2058  CG2 VAL A 269      10.431 124.730 278.277  1.00 27.80      A    C  
ANISOU 2058  CG2 VAL A 269     3080   3267   4215   -882   1116    292  A    C  
ATOM   2059  N   ALA A 270      13.961 124.622 274.948  1.00 27.27      A    N  
ANISOU 2059  N   ALA A 270     3323   2883   4156   -738    944    156  A    N  
ATOM   2060  CA  ALA A 270      14.663 125.082 273.757  1.00 24.58      A    C  
ANISOU 2060  CA  ALA A 270     3018   2512   3807   -685    860     87  A    C  
ATOM   2061  C   ALA A 270      14.315 124.201 272.569  1.00 22.56      A    C  
ANISOU 2061  C   ALA A 270     2816   2143   3611   -760    809     56  A    C  
ATOM   2062  O   ALA A 270      15.200 123.647 271.912  1.00 23.66      A    O  
ANISOU 2062  O   ALA A 270     3061   2202   3727   -722    779     42  A    O  
ATOM   2063  CB  ALA A 270      16.157 125.098 273.997  1.00 20.77      A    C  
ANISOU 2063  CB  ALA A 270     2624   2024   3244   -575    865    107  A    C  
ATOM   2064  N   ILE A 271      13.016 124.113 272.286  1.00 26.54      A    N  
ANISOU 2064  N   ILE A 271     3242   2654   4188   -862    793     36  A    N  
ATOM   2065  CA  ILE A 271      12.470 123.250 271.234  1.00 31.01      A    C  
ANISOU 2065  CA  ILE A 271     3845   3139   4799   -936    723      0  A    C  
ATOM   2066  C   ILE A 271      12.722 123.827 269.843  1.00 31.86      A    C  
ANISOU 2066  C   ILE A 271     3954   3242   4908   -917    640    -85  A    C  
ATOM   2067  O   ILE A 271      12.896 123.088 268.870  1.00 35.41      A    O  
ANISOU 2067  O   ILE A 271     4482   3608   5364   -940    587   -126  A    O  
ATOM   2068  CB  ILE A 271      10.947 123.046 271.445  1.00 44.48      A    C  
ANISOU 2068  CB  ILE A 271     5452   4891   6556  -1031    711     14  A    C  
ATOM   2069  CG1 ILE A 271      10.704 122.230 272.708  1.00 45.99      A    C  
ANISOU 2069  CG1 ILE A 271     5657   5072   6743  -1064    789    107  A    C  
ATOM   2070  CG2 ILE A 271      10.316 122.304 270.282  1.00 46.73      A    C  
ANISOU 2070  CG2 ILE A 271     5759   5108   6888  -1112    627    -34  A    C  
ATOM   2071  CD1 ILE A 271      11.537 120.966 272.757  1.00 47.97      A    C  
ANISOU 2071  CD1 ILE A 271     6051   5190   6985  -1058    806    149  A    C  
ATOM   2072  N   GLY A 272      12.754 125.150 269.754  1.00 28.40      A    N  
ANISOU 2072  N   GLY A 272     3432   2903   4457   -864    620   -111  A    N  
ATOM   2073  CA  GLY A 272      12.962 125.815 268.482  1.00 26.57      A    C  
ANISOU 2073  CA  GLY A 272     3190   2693   4211   -832    531   -174  A    C  
ATOM   2074  C   GLY A 272      12.365 127.204 268.517  1.00 28.02      A    C  
ANISOU 2074  C   GLY A 272     3243   2988   4416   -810    505   -189  A    C  
ATOM   2075  O   GLY A 272      11.986 127.693 269.585  1.00 28.21      A    O  
ANISOU 2075  O   GLY A 272     3193   3072   4453   -799    561   -161  A    O  
ATOM   2076  N   ARG A 273      12.272 127.833 267.348  1.00 24.22      A    N  
ANISOU 2076  N   ARG A 273     2733   2534   3936   -798    420   -234  A    N  
ATOM   2077  CA  ARG A 273      11.777 129.203 267.234  1.00 27.08      A    C  
ANISOU 2077  CA  ARG A 273     2977   2988   4325   -764    383   -245  A    C  
ATOM   2078  C   ARG A 273      10.772 129.323 266.085  1.00 27.91      A    C  
ANISOU 2078  C   ARG A 273     3015   3116   4475   -827    297   -284  A    C  
ATOM   2079  O   ARG A 273      10.872 128.603 265.091  1.00 29.75      A    O  
ANISOU 2079  O   ARG A 273     3313   3303   4688   -866    246   -314  A    O  
ATOM   2080  CB  ARG A 273      12.949 130.178 267.045  1.00 26.08      A    C  
ANISOU 2080  CB  ARG A 273     2878   2887   4143   -656    363   -240  A    C  
ATOM   2081  CG  ARG A 273      13.902 130.239 268.244  1.00 21.16      A    C  
ANISOU 2081  CG  ARG A 273     2300   2263   3476   -590    440   -206  A    C  
ATOM   2082  CD  ARG A 273      15.123 131.124 267.980  1.00 23.34      A    C  
ANISOU 2082  CD  ARG A 273     2605   2561   3704   -495    414   -203  A    C  
ATOM   2083  NE  ARG A 273      14.770 132.528 267.764  1.00 21.14      A    N  
ANISOU 2083  NE  ARG A 273     2227   2340   3465   -463    369   -216  A    N  
ATOM   2084  CZ  ARG A 273      14.461 133.387 268.732  1.00 20.55      A    C  
ANISOU 2084  CZ  ARG A 273     2075   2310   3424   -434    400   -219  A    C  
ATOM   2085  NH1 ARG A 273      14.460 132.995 270.002  1.00 16.29      A    N1+
ANISOU 2085  NH1 ARG A 273     1541   1781   2867   -433    479   -209  A    N1+
ATOM   2086  NH2 ARG A 273      14.163 134.649 268.431  1.00 15.49      A    N  
ANISOU 2086  NH2 ARG A 273     1352   1703   2831   -400    353   -234  A    N  
ATOM   2087  N   VAL A 274       9.789 130.207 266.248  1.00 29.35      A    N  
ANISOU 2087  N   VAL A 274     3069   3374   4708   -829    278   -284  A    N  
ATOM   2088  CA  VAL A 274       8.764 130.448 265.233  1.00 25.47      A    C  
ANISOU 2088  CA  VAL A 274     2506   2928   4243   -868    188   -306  A    C  
ATOM   2089  C   VAL A 274       8.755 131.922 264.802  1.00 26.28      A    C  
ANISOU 2089  C   VAL A 274     2527   3096   4363   -792    133   -305  A    C  
ATOM   2090  O   VAL A 274       9.028 132.810 265.616  1.00 22.46      A    O  
ANISOU 2090  O   VAL A 274     2008   2637   3889   -721    175   -288  A    O  
ATOM   2091  CB  VAL A 274       7.367 130.043 265.747  1.00 25.66      A    C  
ANISOU 2091  CB  VAL A 274     2456   2993   4302   -933    201   -291  A    C  
ATOM   2092  CG1 VAL A 274       7.278 128.531 265.916  1.00 29.91      A    C  
ANISOU 2092  CG1 VAL A 274     3074   3455   4834  -1020    231   -286  A    C  
ATOM   2093  CG2 VAL A 274       7.064 130.744 267.057  1.00 23.87      A    C  
ANISOU 2093  CG2 VAL A 274     2157   2821   4090   -882    273   -262  A    C  
ATOM   2094  N   PRO A 275       8.460 132.183 263.514  1.00 22.23      A    N  
ANISOU 2094  N   PRO A 275     1986   2609   3852   -807     37   -323  A    N  
ATOM   2095  CA  PRO A 275       8.476 133.542 262.946  1.00 22.36      A    C  
ANISOU 2095  CA  PRO A 275     1932   2677   3886   -736    -26   -307  A    C  
ATOM   2096  C   PRO A 275       7.327 134.440 263.431  1.00 26.48      A    C  
ANISOU 2096  C   PRO A 275     2339   3268   4455   -704    -30   -289  A    C  
ATOM   2097  O   PRO A 275       6.246 133.942 263.754  1.00 18.72      A    O  
ANISOU 2097  O   PRO A 275     1310   2314   3489   -759    -17   -293  A    O  
ATOM   2098  CB  PRO A 275       8.341 133.291 261.442  1.00 17.88      A    C  
ANISOU 2098  CB  PRO A 275     1377   2128   3288   -774   -127   -326  A    C  
ATOM   2099  CG  PRO A 275       7.586 131.998 261.361  1.00 18.80      A    C  
ANISOU 2099  CG  PRO A 275     1511   2225   3408   -880   -126   -363  A    C  
ATOM   2100  CD  PRO A 275       8.101 131.169 262.503  1.00 19.59      A    C  
ANISOU 2100  CD  PRO A 275     1690   2253   3501   -894    -22   -359  A    C  
ATOM   2101  N   ASN A 276       7.552 135.753 263.425  1.00 22.77      A    N  
ANISOU 2101  N   ASN A 276     1825   2819   4008   -616    -52   -268  A    N  
ATOM   2102  CA  ASN A 276       6.569 136.718 263.919  1.00 21.66      A    C  
ANISOU 2102  CA  ASN A 276     1585   2731   3915   -567    -51   -259  A    C  
ATOM   2103  C   ASN A 276       5.679 137.295 262.812  1.00 25.82      A    C  
ANISOU 2103  C   ASN A 276     2033   3312   4465   -565   -149   -244  A    C  
ATOM   2104  O   ASN A 276       5.143 138.398 262.952  1.00 28.24      A    O  
ANISOU 2104  O   ASN A 276     2267   3648   4815   -497   -166   -229  A    O  
ATOM   2105  CB  ASN A 276       7.284 137.875 264.631  1.00 20.74      A    C  
ANISOU 2105  CB  ASN A 276     1470   2592   3818   -468    -19   -251  A    C  
ATOM   2106  CG  ASN A 276       7.936 137.450 265.930  1.00 22.32      A    C  
ANISOU 2106  CG  ASN A 276     1722   2763   3996   -462     81   -268  A    C  
ATOM   2107  ND2 ASN A 276       9.094 138.034 266.234  1.00 16.47      A    N  
ANISOU 2107  ND2 ASN A 276     1027   1985   3246   -402     99   -266  A    N  
ATOM   2108  OD1 ASN A 276       7.408 136.605 266.650  1.00 25.43      A    O  
ANISOU 2108  OD1 ASN A 276     2112   3171   4379   -513    139   -278  A    O  
ATOM   2109  N   GLY A 277       5.511 136.553 261.720  1.00 20.91      A    N  
ANISOU 2109  N   GLY A 277     1427   2704   3814   -635   -214   -252  A    N  
ATOM   2110  CA  GLY A 277       4.808 137.083 260.563  1.00 23.52      A    C  
ANISOU 2110  CA  GLY A 277     1688   3097   4153   -631   -316   -234  A    C  
ATOM   2111  C   GLY A 277       3.330 137.356 260.772  1.00 28.10      A    C  
ANISOU 2111  C   GLY A 277     2157   3746   4773   -638   -326   -232  A    C  
ATOM   2112  O   GLY A 277       2.733 138.151 260.042  1.00 30.61      A    O  
ANISOU 2112  O   GLY A 277     2402   4118   5110   -601   -400   -208  A    O  
ATOM   2113  N   LYS A 278       2.735 136.721 261.777  1.00 27.14      A    N  
ANISOU 2113  N   LYS A 278     2018   3629   4665   -683   -253   -252  A    N  
ATOM   2114  CA  LYS A 278       1.300 136.848 261.992  1.00 26.26      A    C  
ANISOU 2114  CA  LYS A 278     1794   3593   4591   -702   -259   -249  A    C  
ATOM   2115  C   LYS A 278       0.953 138.032 262.883  1.00 29.68      A    C  
ANISOU 2115  C   LYS A 278     2159   4044   5074   -603   -216   -239  A    C  
ATOM   2116  O   LYS A 278      -0.224 138.277 263.152  1.00 37.11      A    O  
ANISOU 2116  O   LYS A 278     2997   5052   6050   -602   -214   -237  A    O  
ATOM   2117  CB  LYS A 278       0.730 135.580 262.636  1.00 26.67      A    C  
ANISOU 2117  CB  LYS A 278     1848   3648   4637   -806   -203   -265  A    C  
ATOM   2118  CG  LYS A 278       0.793 134.332 261.776  1.00 28.55      A    C  
ANISOU 2118  CG  LYS A 278     2145   3864   4837   -917   -250   -286  A    C  
ATOM   2119  CD  LYS A 278       0.091 133.177 262.476  1.00 31.23      A    C  
ANISOU 2119  CD  LYS A 278     2477   4201   5189  -1018   -197   -289  A    C  
ATOM   2120  CE  LYS A 278       0.207 131.885 261.676  1.00 33.96      A    C  
ANISOU 2120  CE  LYS A 278     2898   4500   5504  -1130   -244   -317  A    C  
ATOM   2121  NZ  LYS A 278      -0.491 130.756 262.356  1.00 36.59      A    N1+
ANISOU 2121  NZ  LYS A 278     3225   4816   5860  -1233   -197   -308  A    N1+
ATOM   2122  N   ASN A 279       1.963 138.775 263.326  1.00 24.92      A    N  
ANISOU 2122  N   ASN A 279     1610   3382   4476   -520   -184   -236  A    N  
ATOM   2123  CA  ASN A 279       1.747 139.808 264.337  1.00 28.52      A    C  
ANISOU 2123  CA  ASN A 279     2021   3839   4978   -429   -134   -243  A    C  
ATOM   2124  C   ASN A 279       1.902 141.234 263.816  1.00 26.86      A    C  
ANISOU 2124  C   ASN A 279     1785   3610   4809   -329   -193   -221  A    C  
ATOM   2125  O   ASN A 279       2.065 142.165 264.601  1.00 25.33      A    O  
ANISOU 2125  O   ASN A 279     1584   3387   4653   -248   -156   -234  A    O  
ATOM   2126  CB  ASN A 279       2.698 139.603 265.522  1.00 33.63      A    C  
ANISOU 2126  CB  ASN A 279     2743   4432   5604   -412    -41   -264  A    C  
ATOM   2127  CG  ASN A 279       2.521 138.253 266.190  1.00 39.33      A    C  
ANISOU 2127  CG  ASN A 279     3487   5166   6290   -503     28   -275  A    C  
ATOM   2128  ND2 ASN A 279       3.618 137.691 266.687  1.00 41.74      A    N  
ANISOU 2128  ND2 ASN A 279     3889   5415   6556   -515     82   -281  A    N  
ATOM   2129  OD1 ASN A 279       1.410 137.729 266.272  1.00 35.78      A    O  
ANISOU 2129  OD1 ASN A 279     2968   4775   5851   -562     33   -271  A    O  
ATOM   2130  N   LEU A 280       1.837 141.406 262.500  1.00 26.39      A    N  
ANISOU 2130  N   LEU A 280     1716   3568   4744   -336   -288   -187  A    N  
ATOM   2131  CA  LEU A 280       2.165 142.689 261.890  1.00 27.18      A    C  
ANISOU 2131  CA  LEU A 280     1810   3637   4879   -247   -349   -148  A    C  
ATOM   2132  C   LEU A 280       0.980 143.352 261.184  1.00 30.24      A    C  
ANISOU 2132  C   LEU A 280     2093   4090   5306   -216   -422   -121  A    C  
ATOM   2133  O   LEU A 280       1.126 144.453 260.641  1.00 31.04      A    O  
ANISOU 2133  O   LEU A 280     2184   4165   5445   -140   -476    -78  A    O  
ATOM   2134  CB  LEU A 280       3.302 142.505 260.882  1.00 27.91      A    C  
ANISOU 2134  CB  LEU A 280     1985   3695   4925   -265   -402   -114  A    C  
ATOM   2135  CG  LEU A 280       4.476 141.644 261.353  1.00 28.51      A    C  
ANISOU 2135  CG  LEU A 280     2162   3719   4952   -308   -341   -138  A    C  
ATOM   2136  CD1 LEU A 280       5.506 141.449 260.245  1.00 25.35      A    C  
ANISOU 2136  CD1 LEU A 280     1827   3301   4503   -325   -401   -102  A    C  
ATOM   2137  CD2 LEU A 280       5.118 142.233 262.603  1.00 30.67      A    C  
ANISOU 2137  CD2 LEU A 280     2469   3931   5254   -246   -262   -159  A    C  
ATOM   2138  N   ASP A 281      -0.184 142.697 261.207  1.00 29.40      A    N  
ANISOU 2138  N   ASP A 281     1908   4067   5195   -274   -422   -140  A    N  
ATOM   2139  CA  ASP A 281      -1.310 143.072 260.343  1.00 32.94      A    C  
ANISOU 2139  CA  ASP A 281     2253   4598   5663   -264   -503   -114  A    C  
ATOM   2140  C   ASP A 281      -0.837 143.211 258.895  1.00 35.08      A    C  
ANISOU 2140  C   ASP A 281     2556   4876   5897   -266   -605    -67  A    C  
ATOM   2141  O   ASP A 281      -1.244 144.132 258.186  1.00 34.16      A    O  
ANISOU 2141  O   ASP A 281     2386   4784   5808   -201   -676    -22  A    O  
ATOM   2142  CB  ASP A 281      -1.953 144.389 260.801  1.00 35.91      A    C  
ANISOU 2142  CB  ASP A 281     2553   4973   6119   -154   -498   -104  A    C  
ATOM   2143  CG  ASP A 281      -2.760 144.240 262.076  1.00 42.94      A    C  
ANISOU 2143  CG  ASP A 281     3377   5898   7039   -153   -411   -148  A    C  
ATOM   2144  OD1 ASP A 281      -3.142 143.100 262.416  1.00 47.15      A    O  
ANISOU 2144  OD1 ASP A 281     3897   6482   7536   -247   -372   -172  A    O  
ATOM   2145  OD2 ASP A 281      -3.009 145.268 262.741  1.00 46.68      A    O1-
ANISOU 2145  OD2 ASP A 281     3814   6349   7574    -59   -383   -159  A    O1-
ATOM   2146  N   ALA A 282       0.013 142.286 258.459  1.00 33.31      A    N  
ANISOU 2146  N   ALA A 282     2417   4632   5606   -338   -612    -77  A    N  
ATOM   2147  CA  ALA A 282       0.599 142.355 257.123  1.00 30.81      A    C  
ANISOU 2147  CA  ALA A 282     2138   4328   5240   -340   -704    -34  A    C  
ATOM   2148  C   ALA A 282      -0.456 142.245 256.023  1.00 29.42      A    C  
ANISOU 2148  C   ALA A 282     1876   4261   5040   -368   -802    -23  A    C  
ATOM   2149  O   ALA A 282      -0.289 142.801 254.928  1.00 26.56      A    O  
ANISOU 2149  O   ALA A 282     1510   3928   4653   -329   -890     32  A    O  
ATOM   2150  CB  ALA A 282       1.659 141.280 256.961  1.00 26.63      A    C  
ANISOU 2150  CB  ALA A 282     1713   3763   4643   -415   -687    -61  A    C  
ATOM   2151  N   GLY A 283      -1.542 141.536 256.325  1.00 27.56      A    N  
ANISOU 2151  N   GLY A 283     1570   4092   4810   -436   -786    -68  A    N  
ATOM   2152  CA  GLY A 283      -2.657 141.395 255.404  1.00 30.56      A    C  
ANISOU 2152  CA  GLY A 283     1853   4587   5170   -468   -874    -68  A    C  
ATOM   2153  C   GLY A 283      -3.270 142.725 254.997  1.00 34.01      A    C  
ANISOU 2153  C   GLY A 283     2204   5062   5654   -359   -931    -11  A    C  
ATOM   2154  O   GLY A 283      -3.806 142.862 253.895  1.00 38.49      A    O  
ANISOU 2154  O   GLY A 283     2716   5716   6191   -356  -1029     11  A    O  
ATOM   2155  N   LYS A 284      -3.203 143.712 255.887  1.00 33.19      A    N  
ANISOU 2155  N   LYS A 284     2092   4892   5627   -265   -872     10  A    N  
ATOM   2156  CA  LYS A 284      -3.754 145.030 255.578  1.00 39.43      A    C  
ANISOU 2156  CA  LYS A 284     2810   5696   6475   -155   -921     65  A    C  
ATOM   2157  C   LYS A 284      -2.935 145.736 254.503  1.00 36.63      A    C  
ANISOU 2157  C   LYS A 284     2514   5308   6095   -100  -1000    141  A    C  
ATOM   2158  O   LYS A 284      -3.410 146.676 253.865  1.00 35.02      A    O  
ANISOU 2158  O   LYS A 284     2255   5132   5920    -23  -1068    201  A    O  
ATOM   2159  CB  LYS A 284      -3.871 145.901 256.837  1.00 39.05      A    C  
ANISOU 2159  CB  LYS A 284     2745   5577   6518    -71   -838     56  A    C  
ATOM   2160  CG  LYS A 284      -4.860 145.359 257.865  1.00 40.27      A    C  
ANISOU 2160  CG  LYS A 284     2818   5787   6696   -110   -766     -4  A    C  
ATOM   2161  CD  LYS A 284      -5.056 146.307 259.041  1.00 45.82      A    C  
ANISOU 2161  CD  LYS A 284     3494   6435   7482    -14   -693    -18  A    C  
ATOM   2162  CE  LYS A 284      -5.989 145.682 260.069  1.00 48.48      A    C  
ANISOU 2162  CE  LYS A 284     3751   6841   7828    -59   -616    -69  A    C  
ATOM   2163  NZ  LYS A 284      -7.310 145.368 259.465  1.00 50.50      A    N1+
ANISOU 2163  NZ  LYS A 284     3877   7231   8078    -96   -673    -61  A    N1+
ATOM   2164  N   ALA A 285      -1.714 145.259 254.283  1.00 36.77      A    N  
ANISOU 2164  N   ALA A 285     2642   5272   6056   -140   -990    146  A    N  
ATOM   2165  CA  ALA A 285      -0.874 145.805 253.231  1.00 34.91      A    C  
ANISOU 2165  CA  ALA A 285     2465   5019   5781   -101  -1061    227  A    C  
ATOM   2166  C   ALA A 285      -0.939 144.879 252.031  1.00 34.32      A    C  
ANISOU 2166  C   ALA A 285     2394   5048   5600   -177  -1145    218  A    C  
ATOM   2167  O   ALA A 285      -0.272 145.103 251.021  1.00 34.30      A    O  
ANISOU 2167  O   ALA A 285     2440   5060   5534   -161  -1211    283  A    O  
ATOM   2168  CB  ALA A 285       0.549 145.947 253.715  1.00 34.00      A    C  
ANISOU 2168  CB  ALA A 285     2462   4789   5667    -89  -1002    242  A    C  
ATOM   2169  N   GLY A 286      -1.735 143.821 252.165  1.00 35.73      A    N  
ANISOU 2169  N   GLY A 286     2524   5298   5755   -265  -1140    137  A    N  
ATOM   2170  CA  GLY A 286      -1.913 142.854 251.097  1.00 33.37      A    C  
ANISOU 2170  CA  GLY A 286     2225   5096   5359   -348  -1221    102  A    C  
ATOM   2171  C   GLY A 286      -0.852 141.769 251.106  1.00 32.09      A    C  
ANISOU 2171  C   GLY A 286     2173   4891   5129   -431  -1192     55  A    C  
ATOM   2172  O   GLY A 286      -0.815 140.923 250.214  1.00 35.01      A    O  
ANISOU 2172  O   GLY A 286     2565   5326   5411   -501  -1259     16  A    O  
ATOM   2173  N   VAL A 287       0.006 141.777 252.121  1.00 31.70      A    N  
ANISOU 2173  N   VAL A 287     2195   4731   5118   -422  -1095     51  A    N  
ATOM   2174  CA  VAL A 287       1.111 140.825 252.179  1.00 31.62      A    C  
ANISOU 2174  CA  VAL A 287     2293   4670   5050   -487  -1064     13  A    C  
ATOM   2175  C   VAL A 287       0.628 139.457 252.660  1.00 33.35      A    C  
ANISOU 2175  C   VAL A 287     2516   4896   5261   -604  -1023    -86  A    C  
ATOM   2176  O   VAL A 287      -0.146 139.358 253.621  1.00 29.29      A    O  
ANISOU 2176  O   VAL A 287     1948   4372   4810   -620   -956   -114  A    O  
ATOM   2177  CB  VAL A 287       2.268 141.345 253.056  1.00 35.23      A    C  
ANISOU 2177  CB  VAL A 287     2825   5011   5549   -431   -980     46  A    C  
ATOM   2178  CG1 VAL A 287       3.311 140.258 253.285  1.00 34.74      A    C  
ANISOU 2178  CG1 VAL A 287     2865   4896   5438   -501   -937     -5  A    C  
ATOM   2179  CG2 VAL A 287       2.911 142.564 252.408  1.00 31.39      A    C  
ANISOU 2179  CG2 VAL A 287     2354   4512   5060   -337  -1028    150  A    C  
ATOM   2180  N   GLU A 288       1.042 138.413 251.944  1.00 31.48      A    N  
ANISOU 2180  N   GLU A 288     2342   4678   4942   -685  -1067   -136  A    N  
ATOM   2181  CA  GLU A 288       0.674 137.043 252.287  1.00 31.13      A    C  
ANISOU 2181  CA  GLU A 288     2320   4621   4886   -806  -1034   -229  A    C  
ATOM   2182  C   GLU A 288       1.576 136.473 253.373  1.00 27.91      A    C  
ANISOU 2182  C   GLU A 288     2009   4092   4504   -828   -924   -253  A    C  
ATOM   2183  O   GLU A 288       2.809 136.531 253.277  1.00 29.32      A    O  
ANISOU 2183  O   GLU A 288     2275   4213   4653   -796   -915   -238  A    O  
ATOM   2184  CB  GLU A 288       0.731 136.150 251.045  1.00 37.75      A    C  
ANISOU 2184  CB  GLU A 288     3197   5522   5626   -882  -1132   -289  A    C  
ATOM   2185  CG  GLU A 288      -0.322 136.471 249.990  1.00 48.96      A    C  
ANISOU 2185  CG  GLU A 288     4516   7072   7014   -875  -1241   -289  A    C  
ATOM   2186  CD  GLU A 288      -0.167 135.632 248.729  1.00 57.71      A    C  
ANISOU 2186  CD  GLU A 288     5673   8239   8014   -934  -1344   -361  A    C  
ATOM   2187  OE1 GLU A 288       0.859 134.928 248.600  1.00 62.32      A    O  
ANISOU 2187  OE1 GLU A 288     6377   8765   8538   -970  -1335   -398  A    O  
ATOM   2188  OE2 GLU A 288      -1.074 135.674 247.870  1.00 58.34      A    O1-
ANISOU 2188  OE2 GLU A 288     5676   8418   8072   -938  -1438   -387  A    O1-
ATOM   2189  N   VAL A 289       0.956 135.911 254.402  1.00 26.55      A    N  
ANISOU 2189  N   VAL A 289     1818   3888   4382   -882   -843   -284  A    N  
ATOM   2190  CA  VAL A 289       1.688 135.255 255.472  1.00 31.28      A    C  
ANISOU 2190  CA  VAL A 289     2507   4379   5000   -906   -737   -308  A    C  
ATOM   2191  C   VAL A 289       1.250 133.803 255.497  1.00 33.56      A    C  
ANISOU 2191  C   VAL A 289     2833   4647   5270  -1034   -729   -372  A    C  
ATOM   2192  O   VAL A 289       0.053 133.522 255.495  1.00 34.19      A    O  
ANISOU 2192  O   VAL A 289     2835   4786   5370  -1095   -748   -379  A    O  
ATOM   2193  CB  VAL A 289       1.354 135.878 256.838  1.00 32.73      A    C  
ANISOU 2193  CB  VAL A 289     2643   4536   5256   -850   -638   -275  A    C  
ATOM   2194  CG1 VAL A 289       2.192 135.234 257.938  1.00 27.55      A    C  
ANISOU 2194  CG1 VAL A 289     2083   3779   4607   -865   -530   -294  A    C  
ATOM   2195  CG2 VAL A 289       1.576 137.386 256.806  1.00 31.22      A    C  
ANISOU 2195  CG2 VAL A 289     2407   4357   5096   -725   -653   -215  A    C  
ATOM   2196  N   ASP A 290       2.198 132.873 255.488  1.00 33.73      A    N  
ANISOU 2196  N   ASP A 290     2976   4583   5256  -1076   -704   -416  A    N  
ATOM   2197  CA  ASP A 290       1.805 131.469 255.491  1.00 31.25      A    C  
ANISOU 2197  CA  ASP A 290     2714   4226   4933  -1195   -699   -474  A    C  
ATOM   2198  C   ASP A 290       1.314 130.992 256.856  1.00 31.19      A    C  
ANISOU 2198  C   ASP A 290     2696   4165   4987  -1231   -594   -453  A    C  
ATOM   2199  O   ASP A 290       1.359 131.737 257.840  1.00 32.63      A    O  
ANISOU 2199  O   ASP A 290     2839   4348   5210  -1160   -519   -406  A    O  
ATOM   2200  CB  ASP A 290       2.865 130.548 254.861  1.00 34.01      A    C  
ANISOU 2200  CB  ASP A 290     3200   4503   5219  -1227   -721   -543  A    C  
ATOM   2201  CG  ASP A 290       4.032 130.229 255.789  1.00 32.21      A    C  
ANISOU 2201  CG  ASP A 290     3077   4160   5001  -1192   -612   -545  A    C  
ATOM   2202  OD1 ASP A 290       3.999 130.538 256.999  1.00 33.21      A    O  
ANISOU 2202  OD1 ASP A 290     3182   4257   5181  -1159   -517   -494  A    O  
ATOM   2203  OD2 ASP A 290       4.997 129.620 255.285  1.00 34.25      A    O1-
ANISOU 2203  OD2 ASP A 290     3445   4365   5203  -1198   -621   -604  A    O1-
ATOM   2204  N   ASP A 291       0.887 129.737 256.906  1.00 31.93      A    N  
ANISOU 2204  N   ASP A 291     2833   4212   5088  -1339   -593   -488  A    N  
ATOM   2205  CA  ASP A 291       0.221 129.171 258.073  1.00 32.01      A    C  
ANISOU 2205  CA  ASP A 291     2818   4188   5155  -1392   -512   -459  A    C  
ATOM   2206  C   ASP A 291       1.140 129.050 259.278  1.00 27.85      A    C  
ANISOU 2206  C   ASP A 291     2368   3573   4639  -1344   -393   -436  A    C  
ATOM   2207  O   ASP A 291       0.680 129.005 260.418  1.00 30.73      A    O  
ANISOU 2207  O   ASP A 291     2691   3939   5046  -1349   -313   -395  A    O  
ATOM   2208  CB  ASP A 291      -0.326 127.793 257.696  1.00 45.55      A    C  
ANISOU 2208  CB  ASP A 291     4575   5855   6878  -1521   -553   -499  A    C  
ATOM   2209  CG  ASP A 291      -1.669 127.878 257.015  1.00 61.36      A    C  
ANISOU 2209  CG  ASP A 291     6458   7958   8896  -1586   -647   -499  A    C  
ATOM   2210  OD1 ASP A 291      -2.265 128.978 257.040  1.00 66.91      A    O  
ANISOU 2210  OD1 ASP A 291     7040   8772   9610  -1529   -659   -459  A    O  
ATOM   2211  OD2 ASP A 291      -2.100 126.873 256.406  1.00 69.01      A    O1-
ANISOU 2211  OD2 ASP A 291     7457   8895   9869  -1687   -713   -542  A    O1-
ATOM   2212  N   ARG A 292       2.440 129.020 259.016  1.00 24.71      A    N  
ANISOU 2212  N   ARG A 292     2078   3112   4200  -1295   -382   -461  A    N  
ATOM   2213  CA  ARG A 292       3.442 128.870 260.059  1.00 28.89      A    C  
ANISOU 2213  CA  ARG A 292     2689   3559   4730  -1247   -276   -441  A    C  
ATOM   2214  C   ARG A 292       4.002 130.214 260.500  1.00 29.71      A    C  
ANISOU 2214  C   ARG A 292     2751   3700   4836  -1130   -242   -404  A    C  
ATOM   2215  O   ARG A 292       4.873 130.281 261.366  1.00 35.01      A    O  
ANISOU 2215  O   ARG A 292     3479   4319   5504  -1079   -160   -386  A    O  
ATOM   2216  CB  ARG A 292       4.550 127.954 259.539  1.00 26.18      A    C  
ANISOU 2216  CB  ARG A 292     2490   3117   4340  -1265   -281   -494  A    C  
ATOM   2217  CG  ARG A 292       4.053 126.512 259.357  1.00 35.96      A    C  
ANISOU 2217  CG  ARG A 292     3787   4286   5589  -1375   -298   -530  A    C  
ATOM   2218  CD  ARG A 292       5.034 125.643 258.591  1.00 39.16      A    C  
ANISOU 2218  CD  ARG A 292     4333   4601   5943  -1386   -322   -602  A    C  
ATOM   2219  NE  ARG A 292       6.292 125.432 259.294  1.00 37.33      A    N  
ANISOU 2219  NE  ARG A 292     4206   4283   5693  -1325   -230   -589  A    N  
ATOM   2220  CZ  ARG A 292       7.483 125.541 258.715  1.00 35.13      A    C  
ANISOU 2220  CZ  ARG A 292     4013   3978   5356  -1268   -235   -634  A    C  
ATOM   2221  NH1 ARG A 292       7.564 125.848 257.427  1.00 28.34      A    N1+
ANISOU 2221  NH1 ARG A 292     3145   3178   4443  -1265   -329   -697  A    N1+
ATOM   2222  NH2 ARG A 292       8.590 125.338 259.417  1.00 41.32      A    N  
ANISOU 2222  NH2 ARG A 292     4886   4687   6125  -1213   -148   -615  A    N  
ATOM   2223  N   GLY A 293       3.505 131.288 259.902  1.00 28.28      A    N  
ANISOU 2223  N   GLY A 293     2474   3608   4663  -1085   -309   -390  A    N  
ATOM   2224  CA  GLY A 293       3.878 132.617 260.345  1.00 25.44      A    C  
ANISOU 2224  CA  GLY A 293     2069   3277   4322   -973   -284   -351  A    C  
ATOM   2225  C   GLY A 293       5.043 133.159 259.550  1.00 28.00      A    C  
ANISOU 2225  C   GLY A 293     2445   3583   4611   -912   -329   -353  A    C  
ATOM   2226  O   GLY A 293       5.606 134.199 259.894  1.00 24.95      A    O  
ANISOU 2226  O   GLY A 293     2044   3197   4240   -821   -308   -317  A    O  
ATOM   2227  N   PHE A 294       5.438 132.447 258.500  1.00 26.44      A    N  
ANISOU 2227  N   PHE A 294     2311   3369   4367   -963   -391   -396  A    N  
ATOM   2228  CA  PHE A 294       6.499 132.956 257.641  1.00 27.60      A    C  
ANISOU 2228  CA  PHE A 294     2508   3520   4458   -900   -441   -388  A    C  
ATOM   2229  C   PHE A 294       5.948 133.920 256.605  1.00 30.14      A    C  
ANISOU 2229  C   PHE A 294     2736   3938   4777   -868   -551   -357  A    C  
ATOM   2230  O   PHE A 294       4.820 133.764 256.127  1.00 30.39      A    O  
ANISOU 2230  O   PHE A 294     2691   4034   4823   -922   -613   -373  A    O  
ATOM   2231  CB  PHE A 294       7.242 131.816 256.945  1.00 27.94      A    C  
ANISOU 2231  CB  PHE A 294     2692   3521   4405   -937   -451   -441  A    C  
ATOM   2232  CG  PHE A 294       8.103 131.009 257.865  1.00 25.45      A    C  
ANISOU 2232  CG  PHE A 294     2488   3104   4077   -936   -346   -453  A    C  
ATOM   2233  CD1 PHE A 294       7.717 129.734 258.255  1.00 20.75      A    C  
ANISOU 2233  CD1 PHE A 294     1932   2440   3512  -1031   -311   -503  A    C  
ATOM   2234  CD2 PHE A 294       9.297 131.525 258.347  1.00 20.16      A    C  
ANISOU 2234  CD2 PHE A 294     1881   2407   3371   -843   -285   -408  A    C  
ATOM   2235  CE1 PHE A 294       8.505 128.985 259.104  1.00 20.84      A    C  
ANISOU 2235  CE1 PHE A 294     2047   2357   3515  -1024   -217   -502  A    C  
ATOM   2236  CE2 PHE A 294      10.096 130.780 259.205  1.00 21.31      A    C  
ANISOU 2236  CE2 PHE A 294     2125   2469   3504   -836   -193   -414  A    C  
ATOM   2237  CZ  PHE A 294       9.695 129.510 259.585  1.00 26.70      A    C  
ANISOU 2237  CZ  PHE A 294     2848   3082   4212   -922   -158   -457  A    C  
ATOM   2238  N   ILE A 295       6.759 134.909 256.251  1.00 26.49      A    N  
ANISOU 2238  N   ILE A 295     2297   3492   4276   -773   -566   -297  A    N  
ATOM   2239  CA  ILE A 295       6.447 135.778 255.129  1.00 26.22      A    C  
ANISOU 2239  CA  ILE A 295     2199   3545   4218   -735   -673   -251  A    C  
ATOM   2240  C   ILE A 295       7.416 135.425 254.011  1.00 30.10      A    C  
ANISOU 2240  C   ILE A 295     2805   4059   4573   -722   -711   -253  A    C  
ATOM   2241  O   ILE A 295       8.585 135.805 254.051  1.00 29.24      A    O  
ANISOU 2241  O   ILE A 295     2773   3922   4415   -656   -670   -211  A    O  
ATOM   2242  CB  ILE A 295       6.576 137.259 255.508  1.00 25.68      A    C  
ANISOU 2242  CB  ILE A 295     2061   3477   4217   -637   -667   -169  A    C  
ATOM   2243  CG1 ILE A 295       5.585 137.594 256.626  1.00 29.98      A    C  
ANISOU 2243  CG1 ILE A 295     2515   4013   4863   -631   -611   -177  A    C  
ATOM   2244  CG2 ILE A 295       6.321 138.135 254.294  1.00 26.28      A    C  
ANISOU 2244  CG2 ILE A 295     2080   3637   4267   -594   -780   -103  A    C  
ATOM   2245  CD1 ILE A 295       5.616 139.040 257.083  1.00 30.80      A    C  
ANISOU 2245  CD1 ILE A 295     2573   4107   5024   -525   -593   -115  A    C  
ATOM   2246  N   ARG A 296       6.932 134.653 253.043  1.00 30.23      A    N  
ANISOU 2246  N   ARG A 296     2832   4130   4526   -789   -787   -309  A    N  
ATOM   2247  CA  ARG A 296       7.777 134.107 251.988  1.00 31.49      A    C  
ANISOU 2247  CA  ARG A 296     3104   4318   4544   -784   -818   -336  A    C  
ATOM   2248  C   ARG A 296       8.118 135.161 250.936  1.00 31.02      A    C  
ANISOU 2248  C   ARG A 296     3022   4354   4410   -710   -891   -250  A    C  
ATOM   2249  O   ARG A 296       7.287 136.010 250.603  1.00 32.86      A    O  
ANISOU 2249  O   ARG A 296     3140   4656   4689   -695   -966   -194  A    O  
ATOM   2250  CB  ARG A 296       7.073 132.915 251.339  1.00 29.61      A    C  
ANISOU 2250  CB  ARG A 296     2881   4105   4266   -885   -878   -440  A    C  
ATOM   2251  CG  ARG A 296       6.698 131.824 252.338  1.00 32.91      A    C  
ANISOU 2251  CG  ARG A 296     3321   4419   4764   -970   -808   -515  A    C  
ATOM   2252  CD  ARG A 296       7.933 131.278 253.041  1.00 36.65      A    C  
ANISOU 2252  CD  ARG A 296     3929   4785   5212   -936   -697   -525  A    C  
ATOM   2253  NE  ARG A 296       7.613 130.140 253.898  1.00 40.63      A    N  
ANISOU 2253  NE  ARG A 296     4466   5188   5783  -1020   -634   -587  A    N  
ATOM   2254  CZ  ARG A 296       8.519 129.391 254.516  1.00 36.84      A    C  
ANISOU 2254  CZ  ARG A 296     4103   4605   5287  -1008   -545   -607  A    C  
ATOM   2255  NH1 ARG A 296       9.814 129.633 254.350  1.00 28.21      A    N1+
ANISOU 2255  NH1 ARG A 296     3102   3506   4112   -917   -509   -579  A    N1+
ATOM   2256  NH2 ARG A 296       8.133 128.378 255.284  1.00 39.62      A    N  
ANISOU 2256  NH2 ARG A 296     4479   4865   5708  -1088   -493   -650  A    N  
ATOM   2257  N   VAL A 297       9.337 135.091 250.407  1.00 23.52      A    N  
ANISOU 2257  N   VAL A 297     2178   3413   3346   -663   -869   -234  A    N  
ATOM   2258  CA  VAL A 297       9.831 136.091 249.467  1.00 24.60      A    C  
ANISOU 2258  CA  VAL A 297     2303   3638   3407   -592   -922   -135  A    C  
ATOM   2259  C   VAL A 297      10.571 135.415 248.322  1.00 32.44      A    C  
ANISOU 2259  C   VAL A 297     3396   4702   4229   -591   -948   -174  A    C  
ATOM   2260  O   VAL A 297      10.911 134.232 248.411  1.00 35.49      A    O  
ANISOU 2260  O   VAL A 297     3874   5041   4567   -629   -907   -278  A    O  
ATOM   2261  CB  VAL A 297      10.795 137.072 250.146  1.00 27.05      A    C  
ANISOU 2261  CB  VAL A 297     2624   3890   3765   -513   -850    -40  A    C  
ATOM   2262  CG1 VAL A 297      10.065 137.906 251.187  1.00 25.33      A    C  
ANISOU 2262  CG1 VAL A 297     2301   3614   3709   -500   -833     -2  A    C  
ATOM   2263  CG2 VAL A 297      11.949 136.312 250.781  1.00 27.26      A    C  
ANISOU 2263  CG2 VAL A 297     2767   3834   3755   -506   -745    -89  A    C  
ATOM   2264  N   ASP A 298      10.820 136.166 247.251  1.00 31.19      A    N  
ANISOU 2264  N   ASP A 298     3219   4655   3977   -543  -1013    -89  A    N  
ATOM   2265  CA  ASP A 298      11.593 135.652 246.126  1.00 30.49      A    C  
ANISOU 2265  CA  ASP A 298     3220   4656   3710   -528  -1031   -117  A    C  
ATOM   2266  C   ASP A 298      13.079 135.950 246.305  1.00 29.40      A    C  
ANISOU 2266  C   ASP A 298     3159   4490   3524   -458   -941    -56  A    C  
ATOM   2267  O   ASP A 298      13.511 136.339 247.397  1.00 26.33      A    O  
ANISOU 2267  O   ASP A 298     2767   3996   3242   -435   -862    -18  A    O  
ATOM   2268  CB  ASP A 298      11.072 136.206 244.789  1.00 33.49      A    C  
ANISOU 2268  CB  ASP A 298     3539   5196   3990   -517  -1151    -57  A    C  
ATOM   2269  CG  ASP A 298      11.201 137.730 244.671  1.00 36.13      A    C  
ANISOU 2269  CG  ASP A 298     3796   5564   4368   -449  -1173    118  A    C  
ATOM   2270  OD1 ASP A 298      11.951 138.368 245.446  1.00 33.61      A    O  
ANISOU 2270  OD1 ASP A 298     3488   5156   4127   -404  -1093    191  A    O  
ATOM   2271  OD2 ASP A 298      10.543 138.298 243.773  1.00 40.15      A    O1-
ANISOU 2271  OD2 ASP A 298     4232   6189   4833   -440  -1276    186  A    O1-
ATOM   2272  N   LYS A 299      13.848 135.798 245.229  1.00 29.49      A    N  
ANISOU 2272  N   LYS A 299     3230   4605   3370   -425   -954    -46  A    N  
ATOM   2273  CA  LYS A 299      15.300 135.967 245.292  1.00 35.09      A    C  
ANISOU 2273  CA  LYS A 299     4009   5307   4018   -363   -868      6  A    C  
ATOM   2274  C   LYS A 299      15.739 137.431 245.373  1.00 34.27      A    C  
ANISOU 2274  C   LYS A 299     3841   5216   3964   -310   -862    177  A    C  
ATOM   2275  O   LYS A 299      16.925 137.727 245.544  1.00 34.81      A    O  
ANISOU 2275  O   LYS A 299     3947   5271   4007   -265   -790    236  A    O  
ATOM   2276  CB  LYS A 299      15.979 135.227 244.135  1.00 37.76      A    C  
ANISOU 2276  CB  LYS A 299     4431   5759   4158   -344   -875    -53  A    C  
ATOM   2277  CG  LYS A 299      15.933 133.709 244.320  1.00 42.40      A    C  
ANISOU 2277  CG  LYS A 299     5110   6282   4719   -383   -847   -231  A    C  
ATOM   2278  CD  LYS A 299      16.362 132.951 243.080  1.00 49.84      A    C  
ANISOU 2278  CD  LYS A 299     6128   7344   5465   -366   -873   -315  A    C  
ATOM   2279  CE  LYS A 299      16.042 131.469 243.228  1.00 58.05      A    C  
ANISOU 2279  CE  LYS A 299     7249   8302   6504   -418   -868   -502  A    C  
ATOM   2280  NZ  LYS A 299      17.287 130.652 243.188  1.00 61.34      A    N1+
ANISOU 2280  NZ  LYS A 299     7781   8693   6833   -361   -780   -574  A    N1+
ATOM   2281  N   GLN A 300      14.776 138.342 245.273  1.00 32.03      A    N  
ANISOU 2281  N   GLN A 300     3457   4953   3762   -317   -938    257  A    N  
ATOM   2282  CA  GLN A 300      15.058 139.756 245.496  1.00 32.82      A    C  
ANISOU 2282  CA  GLN A 300     3493   5030   3947   -271   -936    414  A    C  
ATOM   2283  C   GLN A 300      14.431 140.211 246.806  1.00 32.18      A    C  
ANISOU 2283  C   GLN A 300     3349   4812   4064   -280   -912    407  A    C  
ATOM   2284  O   GLN A 300      14.335 141.412 247.078  1.00 30.77      A    O  
ANISOU 2284  O   GLN A 300     3103   4597   3991   -247   -927    518  A    O  
ATOM   2285  CB  GLN A 300      14.555 140.607 244.335  1.00 33.04      A    C  
ANISOU 2285  CB  GLN A 300     3452   5185   3917   -252  -1040    533  A    C  
ATOM   2286  CG  GLN A 300      15.352 140.401 243.065  1.00 34.83      A    C  
ANISOU 2286  CG  GLN A 300     3734   5560   3940   -229  -1052    571  A    C  
ATOM   2287  CD  GLN A 300      15.052 141.450 242.027  1.00 36.96      A    C  
ANISOU 2287  CD  GLN A 300     3935   5950   4159   -201  -1141    731  A    C  
ATOM   2288  NE2 GLN A 300      16.100 142.089 241.519  1.00 32.76      A    N  
ANISOU 2288  NE2 GLN A 300     3421   5475   3553   -161  -1109    862  A    N  
ATOM   2289  OE1 GLN A 300      13.892 141.698 241.690  1.00 40.46      A    O  
ANISOU 2289  OE1 GLN A 300     4305   6437   4632   -214  -1239    745  A    O  
ATOM   2290  N   LEU A 301      14.012 139.228 247.604  1.00 28.51      A    N  
ANISOU 2290  N   LEU A 301     2911   4274   3648   -325   -874    275  A    N  
ATOM   2291  CA  LEU A 301      13.435 139.445 248.931  1.00 27.73      A    C  
ANISOU 2291  CA  LEU A 301     2761   4057   3718   -338   -836    248  A    C  
ATOM   2292  C   LEU A 301      12.090 140.178 248.899  1.00 25.90      A    C  
ANISOU 2292  C   LEU A 301     2409   3843   3591   -343   -918    286  A    C  
ATOM   2293  O   LEU A 301      11.659 140.730 249.909  1.00 23.51      A    O  
ANISOU 2293  O   LEU A 301     2045   3456   3432   -332   -892    294  A    O  
ATOM   2294  CB  LEU A 301      14.427 140.165 249.866  1.00 27.84      A    C  
ANISOU 2294  CB  LEU A 301     2791   3979   3809   -292   -753    307  A    C  
ATOM   2295  CG  LEU A 301      15.738 139.456 250.246  1.00 27.45      A    C  
ANISOU 2295  CG  LEU A 301     2845   3893   3690   -282   -659    264  A    C  
ATOM   2296  CD1 LEU A 301      15.509 137.987 250.595  1.00 21.36      A    C  
ANISOU 2296  CD1 LEU A 301     2139   3090   2885   -329   -623    126  A    C  
ATOM   2297  CD2 LEU A 301      16.809 139.596 249.170  1.00 30.95      A    C  
ANISOU 2297  CD2 LEU A 301     3337   4428   3993   -248   -662    332  A    C  
ATOM   2298  N   ARG A 302      11.422 140.158 247.749  1.00 28.16      A    N  
ANISOU 2298  N   ARG A 302     2657   4244   3798   -357  -1018    304  A    N  
ATOM   2299  CA  ARG A 302      10.097 140.760 247.621  1.00 31.75      A    C  
ANISOU 2299  CA  ARG A 302     2990   4732   4342   -360  -1106    338  A    C  
ATOM   2300  C   ARG A 302       9.000 139.826 248.115  1.00 32.53      A    C  
ANISOU 2300  C   ARG A 302     3052   4813   4495   -431  -1114    212  A    C  
ATOM   2301  O   ARG A 302       9.025 138.632 247.828  1.00 29.53      A    O  
ANISOU 2301  O   ARG A 302     2737   4457   4026   -490  -1111    106  A    O  
ATOM   2302  CB  ARG A 302       9.789 141.107 246.163  1.00 30.45      A    C  
ANISOU 2302  CB  ARG A 302     2792   4714   4064   -346  -1219    415  A    C  
ATOM   2303  CG  ARG A 302      10.700 142.135 245.505  1.00 34.84      A    C  
ANISOU 2303  CG  ARG A 302     3364   5309   4565   -280  -1228    569  A    C  
ATOM   2304  CD  ARG A 302      10.209 142.429 244.081  1.00 36.96      A    C  
ANISOU 2304  CD  ARG A 302     3588   5738   4717   -269  -1348    647  A    C  
ATOM   2305  NE  ARG A 302      11.223 143.090 243.265  1.00 39.55      A    N  
ANISOU 2305  NE  ARG A 302     3955   6132   4941   -222  -1347    784  A    N  
ATOM   2306  CZ  ARG A 302      11.362 144.409 243.168  1.00 42.49      A    C  
ANISOU 2306  CZ  ARG A 302     4280   6476   5390   -165  -1363    944  A    C  
ATOM   2307  NH1 ARG A 302      10.546 145.215 243.837  1.00 42.93      A    N1+
ANISOU 2307  NH1 ARG A 302     4268   6423   5622   -137  -1362    962  A    N1+
ATOM   2308  NH2 ARG A 302      12.312 144.921 242.398  1.00 40.19      A    N  
ANISOU 2308  NH2 ARG A 302     4036   6239   4998   -132  -1344   1061  A    N  
ATOM   2309  N   THR A 303       8.030 140.372 248.843  1.00 32.44      A    N  
ANISOU 2309  N   THR A 303     2933   4761   4633   -427  -1125    223  A    N  
ATOM   2310  CA  THR A 303       6.817 139.619 249.144  1.00 34.38      A    C  
ANISOU 2310  CA  THR A 303     3113   5018   4931   -498  -1150    125  A    C  
ATOM   2311  C   THR A 303       5.962 139.577 247.882  1.00 32.76      A    C  
ANISOU 2311  C   THR A 303     2843   4952   4652   -521  -1282    137  A    C  
ATOM   2312  O   THR A 303       6.399 140.001 246.810  1.00 32.64      A    O  
ANISOU 2312  O   THR A 303     2851   5022   4528   -483  -1342    213  A    O  
ATOM   2313  CB  THR A 303       5.979 140.283 250.254  1.00 30.88      A    C  
ANISOU 2313  CB  THR A 303     2556   4510   4665   -478  -1123    137  A    C  
ATOM   2314  CG2 THR A 303       6.817 140.508 251.500  1.00 22.43      A    C  
ANISOU 2314  CG2 THR A 303     1541   3317   3665   -444  -1002    133  A    C  
ATOM   2315  OG1 THR A 303       5.460 141.534 249.783  1.00 28.70      A    O  
ANISOU 2315  OG1 THR A 303     2205   4275   4424   -399  -1177    234  A    O  
ATOM   2316  N   ASN A 304       4.733 139.088 248.016  1.00 30.69      A    N  
ANISOU 2316  N   ASN A 304     2495   4720   4447   -584  -1324     65  A    N  
ATOM   2317  CA  ASN A 304       3.782 139.077 246.910  1.00 33.93      A    C  
ANISOU 2317  CA  ASN A 304     2848   5254   4789   -591  -1426     56  A    C  
ATOM   2318  C   ASN A 304       3.378 140.488 246.493  1.00 39.43      A    C  
ANISOU 2318  C   ASN A 304     3473   5989   5519   -486  -1464    178  A    C  
ATOM   2319  O   ASN A 304       2.893 140.706 245.380  1.00 38.18      A    O  
ANISOU 2319  O   ASN A 304     3285   5940   5282   -467  -1557    207  A    O  
ATOM   2320  CB  ASN A 304       2.555 138.246 247.277  1.00 33.69      A    C  
ANISOU 2320  CB  ASN A 304     2755   5228   4818   -670  -1425    -61  A    C  
ATOM   2321  CG  ASN A 304       1.827 138.799 248.479  1.00 31.51      A    C  
ANISOU 2321  CG  ASN A 304     2395   4884   4691   -640  -1344    -52  A    C  
ATOM   2322  ND2 ASN A 304       0.599 139.257 248.272  1.00 31.10      A    N  
ANISOU 2322  ND2 ASN A 304     2234   4902   4681   -618  -1386    -45  A    N  
ATOM   2323  OD1 ASN A 304       2.362 138.803 249.589  1.00 31.63      A    O  
ANISOU 2323  OD1 ASN A 304     2447   4794   4777   -635  -1244    -54  A    O  
ATOM   2324  N   VAL A 305       3.560 141.435 247.411  1.00 40.76      A    N  
ANISOU 2324  N   VAL A 305     3620   6059   5806   -418  -1391    241  A    N  
ATOM   2325  CA  VAL A 305       3.421 142.854 247.109  1.00 36.83      A    C  
ANISOU 2325  CA  VAL A 305     3081   5562   5350   -315  -1414    364  A    C  
ATOM   2326  C   VAL A 305       4.813 143.408 246.804  1.00 36.40      A    C  
ANISOU 2326  C   VAL A 305     3112   5476   5243   -271  -1398    467  A    C  
ATOM   2327  O   VAL A 305       5.644 143.544 247.701  1.00 38.17      A    O  
ANISOU 2327  O   VAL A 305     3380   5595   5528   -261  -1316    472  A    O  
ATOM   2328  CB  VAL A 305       2.806 143.623 248.293  1.00 35.09      A    C  
ANISOU 2328  CB  VAL A 305     2796   5248   5287   -265  -1343    364  A    C  
ATOM   2329  CG1 VAL A 305       2.609 145.074 247.926  1.00 36.67      A    C  
ANISOU 2329  CG1 VAL A 305     2960   5438   5535   -163  -1376    483  A    C  
ATOM   2330  CG2 VAL A 305       1.482 142.994 248.718  1.00 31.48      A    C  
ANISOU 2330  CG2 VAL A 305     2254   4831   4877   -317  -1341    262  A    C  
ATOM   2331  N   PRO A 306       5.066 143.738 245.528  1.00 38.63      A    N  
ANISOU 2331  N   PRO A 306     3415   5856   5408   -243  -1474    553  A    N  
ATOM   2332  CA  PRO A 306       6.408 143.996 244.981  1.00 38.64      A    C  
ANISOU 2332  CA  PRO A 306     3502   5870   5311   -220  -1464    646  A    C  
ATOM   2333  C   PRO A 306       7.211 145.093 245.683  1.00 37.01      A    C  
ANISOU 2333  C   PRO A 306     3316   5537   5210   -157  -1391    742  A    C  
ATOM   2334  O   PRO A 306       8.440 144.987 245.730  1.00 31.76      A    O  
ANISOU 2334  O   PRO A 306     2723   4852   4494   -162  -1348    776  A    O  
ATOM   2335  CB  PRO A 306       6.123 144.399 243.527  1.00 41.59      A    C  
ANISOU 2335  CB  PRO A 306     3866   6373   5562   -188  -1556    728  A    C  
ATOM   2336  CG  PRO A 306       4.786 143.788 243.224  1.00 44.54      A    C  
ANISOU 2336  CG  PRO A 306     4169   6826   5928   -226  -1626    631  A    C  
ATOM   2337  CD  PRO A 306       4.018 143.903 244.506  1.00 42.26      A    C  
ANISOU 2337  CD  PRO A 306     3812   6431   5815   -229  -1572    568  A    C  
ATOM   2338  N   HIS A 307       6.551 146.113 246.224  1.00 36.29      A    N  
ANISOU 2338  N   HIS A 307     3165   5364   5259   -101  -1376    777  A    N  
ATOM   2339  CA  HIS A 307       7.281 147.188 246.898  1.00 32.27      A    C  
ANISOU 2339  CA  HIS A 307     2681   4725   4857    -47  -1310    854  A    C  
ATOM   2340  C   HIS A 307       7.492 146.902 248.386  1.00 32.81      A    C  
ANISOU 2340  C   HIS A 307     2757   4674   5035    -63  -1218    757  A    C  
ATOM   2341  O   HIS A 307       8.118 147.691 249.100  1.00 30.50      A    O  
ANISOU 2341  O   HIS A 307     2489   4266   4833    -26  -1159    793  A    O  
ATOM   2342  CB  HIS A 307       6.598 148.546 246.698  1.00 35.88      A    C  
ANISOU 2342  CB  HIS A 307     3085   5143   5405     28  -1341    945  A    C  
ATOM   2343  CG  HIS A 307       5.268 148.665 247.369  1.00 39.22      A    C  
ANISOU 2343  CG  HIS A 307     3423   5543   5937     46  -1342    869  A    C  
ATOM   2344  CD2 HIS A 307       4.895 149.306 248.504  1.00 38.28      A    C  
ANISOU 2344  CD2 HIS A 307     3272   5310   5965     85  -1285    835  A    C  
ATOM   2345  ND1 HIS A 307       4.124 148.068 246.876  1.00 43.34      A    N  
ANISOU 2345  ND1 HIS A 307     3878   6177   6413     23  -1407    813  A    N  
ATOM   2346  CE1 HIS A 307       3.106 148.354 247.667  1.00 40.54      A    C  
ANISOU 2346  CE1 HIS A 307     3449   5783   6173     48  -1385    757  A    C  
ATOM   2347  NE2 HIS A 307       3.547 149.095 248.667  1.00 38.19      A    N  
ANISOU 2347  NE2 HIS A 307     3173   5349   5988     88  -1311    768  A    N  
ATOM   2348  N   ILE A 308       6.980 145.765 248.847  1.00 28.08      A    N  
ANISOU 2348  N   ILE A 308     2140   4102   4425   -124  -1204    633  A    N  
ATOM   2349  CA  ILE A 308       7.209 145.345 250.223  1.00 26.61      A    C  
ANISOU 2349  CA  ILE A 308     1969   3818   4322   -147  -1110    540  A    C  
ATOM   2350  C   ILE A 308       8.117 144.116 250.292  1.00 28.56      A    C  
ANISOU 2350  C   ILE A 308     2286   4082   4485   -217  -1085    481  A    C  
ATOM   2351  O   ILE A 308       7.822 143.077 249.703  1.00 33.50      A    O  
ANISOU 2351  O   ILE A 308     2918   4794   5018   -282  -1131    424  A    O  
ATOM   2352  CB  ILE A 308       5.881 145.094 250.975  1.00 27.02      A    C  
ANISOU 2352  CB  ILE A 308     1947   3864   4454   -160  -1088    445  A    C  
ATOM   2353  CG1 ILE A 308       5.066 146.393 251.047  1.00 26.32      A    C  
ANISOU 2353  CG1 ILE A 308     1793   3749   4461    -79  -1106    502  A    C  
ATOM   2354  CG2 ILE A 308       6.153 144.548 252.378  1.00 25.71      A    C  
ANISOU 2354  CG2 ILE A 308     1807   3612   4349   -189   -984    351  A    C  
ATOM   2355  CD1 ILE A 308       3.746 146.271 251.799  1.00 26.85      A    C  
ANISOU 2355  CD1 ILE A 308     1777   3824   4603    -81  -1082    420  A    C  
ATOM   2356  N   PHE A 309       9.226 144.258 251.016  1.00 28.98      A    N  
ANISOU 2356  N   PHE A 309     2396   4048   4567   -204  -1009    489  A    N  
ATOM   2357  CA  PHE A 309      10.258 143.233 251.120  1.00 23.28      A    C  
ANISOU 2357  CA  PHE A 309     1795   3319   3731   -244   -936    424  A    C  
ATOM   2358  C   PHE A 309      10.222 142.585 252.502  1.00 27.57      A    C  
ANISOU 2358  C   PHE A 309     2359   3776   4342   -272   -839    315  A    C  
ATOM   2359  O   PHE A 309       9.608 143.122 253.427  1.00 26.53      A    O  
ANISOU 2359  O   PHE A 309     2152   3585   4341   -250   -819    300  A    O  
ATOM   2360  CB  PHE A 309      11.639 143.850 250.889  1.00 25.70      A    C  
ANISOU 2360  CB  PHE A 309     2169   3600   3995   -202   -904    514  A    C  
ATOM   2361  CG  PHE A 309      11.850 144.390 249.498  1.00 27.75      A    C  
ANISOU 2361  CG  PHE A 309     2423   3956   4164   -179   -985    634  A    C  
ATOM   2362  CD1 PHE A 309      12.708 143.751 248.617  1.00 29.24      A    C  
ANISOU 2362  CD1 PHE A 309     2697   4228   4184   -196   -978    640  A    C  
ATOM   2363  CD2 PHE A 309      11.207 145.548 249.080  1.00 28.79      A    C  
ANISOU 2363  CD2 PHE A 309     2464   4098   4377   -135  -1066    745  A    C  
ATOM   2364  CE1 PHE A 309      12.912 144.246 247.341  1.00 31.18      A    C  
ANISOU 2364  CE1 PHE A 309     2937   4579   4332   -174  -1048    756  A    C  
ATOM   2365  CE2 PHE A 309      11.397 146.045 247.803  1.00 30.31      A    C  
ANISOU 2365  CE2 PHE A 309     2654   4385   4477   -113  -1137    868  A    C  
ATOM   2366  CZ  PHE A 309      12.257 145.397 246.934  1.00 31.61      A    C  
ANISOU 2366  CZ  PHE A 309     2900   4646   4464   -135  -1130    878  A    C  
ATOM   2367  N   ALA A 310      10.880 141.437 252.646  1.00 21.73      A    N  
ANISOU 2367  N   ALA A 310     1718   3029   3509   -315   -779    239  A    N  
ATOM   2368  CA  ALA A 310      10.987 140.780 253.945  1.00 18.46      A    C  
ANISOU 2368  CA  ALA A 310     1335   2535   3144   -339   -683    152  A    C  
ATOM   2369  C   ALA A 310      12.305 140.028 254.016  1.00 20.56      A    C  
ANISOU 2369  C   ALA A 310     1726   2777   3308   -344   -614    126  A    C  
ATOM   2370  O   ALA A 310      12.746 139.450 253.019  1.00 24.78      A    O  
ANISOU 2370  O   ALA A 310     2323   3371   3720   -358   -641    124  A    O  
ATOM   2371  CB  ALA A 310       9.799 139.833 254.172  1.00 18.97      A    C  
ANISOU 2371  CB  ALA A 310     1359   2619   3232   -409   -693     62  A    C  
ATOM   2372  N   ILE A 311      12.938 140.034 255.187  1.00 19.15      A    N  
ANISOU 2372  N   ILE A 311     1580   2519   3175   -327   -526    104  A    N  
ATOM   2373  CA  ILE A 311      14.282 139.481 255.336  1.00 16.89      A    C  
ANISOU 2373  CA  ILE A 311     1403   2210   2806   -316   -460     93  A    C  
ATOM   2374  C   ILE A 311      14.485 138.832 256.708  1.00 17.59      A    C  
ANISOU 2374  C   ILE A 311     1527   2225   2932   -329   -367     25  A    C  
ATOM   2375  O   ILE A 311      13.740 139.105 257.648  1.00 17.64      A    O  
ANISOU 2375  O   ILE A 311     1469   2197   3038   -334   -345      1  A    O  
ATOM   2376  CB  ILE A 311      15.336 140.590 255.181  1.00 16.25      A    C  
ANISOU 2376  CB  ILE A 311     1326   2122   2728   -258   -457    185  A    C  
ATOM   2377  CG1 ILE A 311      15.019 141.743 256.141  1.00 15.49      A    C  
ANISOU 2377  CG1 ILE A 311     1151   1960   2773   -225   -448    210  A    C  
ATOM   2378  CG2 ILE A 311      15.374 141.103 253.755  1.00 16.47      A    C  
ANISOU 2378  CG2 ILE A 311     1337   2232   2689   -245   -538    269  A    C  
ATOM   2379  CD1 ILE A 311      16.094 142.830 256.168  1.00 24.11      A    C  
ANISOU 2379  CD1 ILE A 311     2249   3021   3890   -178   -440    292  A    C  
ATOM   2380  N   GLY A 312      15.494 137.975 256.823  1.00 14.82      A    N  
ANISOU 2380  N   GLY A 312     1275   1857   2499   -328   -310     -3  A    N  
ATOM   2381  CA  GLY A 312      15.838 137.379 258.104  1.00 16.91      A    C  
ANISOU 2381  CA  GLY A 312     1581   2057   2788   -331   -223    -50  A    C  
ATOM   2382  C   GLY A 312      14.992 136.186 258.516  1.00 21.98      A    C  
ANISOU 2382  C   GLY A 312     2237   2674   3441   -394   -200   -124  A    C  
ATOM   2383  O   GLY A 312      14.381 135.512 257.669  1.00 21.57      A    O  
ANISOU 2383  O   GLY A 312     2193   2650   3351   -442   -248   -158  A    O  
ATOM   2384  N   ASP A 313      14.943 135.946 259.829  1.00 23.48      A    N  
ANISOU 2384  N   ASP A 313     2426   2813   3681   -398   -127   -148  A    N  
ATOM   2385  CA  ASP A 313      14.231 134.803 260.406  1.00 22.61      A    C  
ANISOU 2385  CA  ASP A 313     2332   2670   3590   -461    -89   -204  A    C  
ATOM   2386  C   ASP A 313      12.795 134.687 259.912  1.00 23.87      A    C  
ANISOU 2386  C   ASP A 313     2411   2861   3797   -525   -149   -228  A    C  
ATOM   2387  O   ASP A 313      12.295 133.588 259.671  1.00 27.39      A    O  
ANISOU 2387  O   ASP A 313     2887   3292   4229   -594   -154   -275  A    O  
ATOM   2388  CB  ASP A 313      14.189 134.922 261.936  1.00 20.12      A    C  
ANISOU 2388  CB  ASP A 313     1993   2320   3333   -450     -9   -207  A    C  
ATOM   2389  CG  ASP A 313      15.504 134.558 262.599  1.00 26.38      A    C  
ANISOU 2389  CG  ASP A 313     2877   3078   4071   -406     60   -198  A    C  
ATOM   2390  OD1 ASP A 313      16.521 134.414 261.887  1.00 26.28      A    O  
ANISOU 2390  OD1 ASP A 313     2932   3068   3984   -374     46   -184  A    O  
ATOM   2391  OD2 ASP A 313      15.510 134.418 263.846  1.00 25.90      A    O1-
ANISOU 2391  OD2 ASP A 313     2811   2994   4034   -402    127   -204  A    O1-
ATOM   2392  N   ILE A 314      12.151 135.834 259.727  1.00 19.23      A    N  
ANISOU 2392  N   ILE A 314     1720   2315   3271   -502   -199   -196  A    N  
ATOM   2393  CA  ILE A 314      10.729 135.877 259.431  1.00 22.19      A    C  
ANISOU 2393  CA  ILE A 314     1994   2730   3707   -553   -254   -213  A    C  
ATOM   2394  C   ILE A 314      10.444 135.342 258.031  1.00 21.52      A    C  
ANISOU 2394  C   ILE A 314     1930   2691   3556   -597   -339   -230  A    C  
ATOM   2395  O   ILE A 314       9.303 135.037 257.688  1.00 24.26      A    O  
ANISOU 2395  O   ILE A 314     2209   3073   3937   -658   -389   -259  A    O  
ATOM   2396  CB  ILE A 314      10.196 137.318 259.573  1.00 22.32      A    C  
ANISOU 2396  CB  ILE A 314     1894   2775   3809   -498   -288   -170  A    C  
ATOM   2397  CG1 ILE A 314       8.706 137.323 259.921  1.00 22.46      A    C  
ANISOU 2397  CG1 ILE A 314     1792   2825   3917   -541   -302   -196  A    C  
ATOM   2398  CG2 ILE A 314      10.465 138.123 258.311  1.00 23.54      A    C  
ANISOU 2398  CG2 ILE A 314     2040   2974   3930   -458   -377   -113  A    C  
ATOM   2399  CD1 ILE A 314       8.227 138.676 260.474  1.00 22.83      A    C  
ANISOU 2399  CD1 ILE A 314     1749   2883   4043   -465   -300   -165  A    C  
ATOM   2400  N   VAL A 315      11.501 135.188 257.243  1.00 19.87      A    N  
ANISOU 2400  N   VAL A 315     1813   2489   3248   -566   -353   -218  A    N  
ATOM   2401  CA  VAL A 315      11.362 134.794 255.848  1.00 17.68      A    C  
ANISOU 2401  CA  VAL A 315     1560   2271   2887   -593   -436   -236  A    C  
ATOM   2402  C   VAL A 315      11.516 133.280 255.640  1.00 27.08      A    C  
ANISOU 2402  C   VAL A 315     2850   3424   4016   -654   -417   -318  A    C  
ATOM   2403  O   VAL A 315      11.023 132.705 254.661  1.00 21.40      A    O  
ANISOU 2403  O   VAL A 315     2138   2746   3247   -704   -486   -366  A    O  
ATOM   2404  CB  VAL A 315      12.383 135.622 255.022  1.00 26.17      A    C  
ANISOU 2404  CB  VAL A 315     2666   3393   3886   -519   -465   -167  A    C  
ATOM   2405  CG1 VAL A 315      13.242 134.766 254.118  1.00 22.34      A    C  
ANISOU 2405  CG1 VAL A 315     2291   2929   3268   -519   -469   -201  A    C  
ATOM   2406  CG2 VAL A 315      11.674 136.752 254.293  1.00 21.58      A    C  
ANISOU 2406  CG2 VAL A 315     1981   2885   3334   -498   -555   -102  A    C  
ATOM   2407  N   GLY A 316      12.173 132.620 256.582  1.00 25.18      A    N  
ANISOU 2407  N   GLY A 316     2684   3101   3780   -650   -326   -338  A    N  
ATOM   2408  CA  GLY A 316      12.332 131.187 256.483  1.00 17.88      A    C  
ANISOU 2408  CA  GLY A 316     1858   2119   2816   -702   -303   -411  A    C  
ATOM   2409  C   GLY A 316      13.624 130.738 257.116  1.00 22.47      A    C  
ANISOU 2409  C   GLY A 316     2546   2634   3359   -649   -215   -405  A    C  
ATOM   2410  O   GLY A 316      14.418 131.562 257.570  1.00 24.04      A    O  
ANISOU 2410  O   GLY A 316     2738   2842   3554   -576   -178   -345  A    O  
ATOM   2411  N   GLN A 317      13.834 129.429 257.143  1.00 21.74      A    N  
ANISOU 2411  N   GLN A 317     2549   2469   3242   -685   -187   -466  A    N  
ATOM   2412  CA  GLN A 317      15.074 128.839 257.635  1.00 26.53      A    C  
ANISOU 2412  CA  GLN A 317     3263   3010   3805   -629   -110   -464  A    C  
ATOM   2413  C   GLN A 317      16.195 128.906 256.595  1.00 23.49      A    C  
ANISOU 2413  C   GLN A 317     2947   2673   3305   -557   -130   -470  A    C  
ATOM   2414  O   GLN A 317      15.922 128.942 255.393  1.00 25.25      A    O  
ANISOU 2414  O   GLN A 317     3165   2961   3469   -571   -204   -503  A    O  
ATOM   2415  CB  GLN A 317      14.818 127.401 258.119  1.00 36.30      A    C  
ANISOU 2415  CB  GLN A 317     4575   4139   5077   -692    -70   -520  A    C  
ATOM   2416  CG  GLN A 317      13.919 127.355 259.344  1.00 45.93      A    C  
ANISOU 2416  CG  GLN A 317     5729   5319   6404   -753    -25   -493  A    C  
ATOM   2417  CD  GLN A 317      13.857 125.986 259.986  1.00 62.22      A    C  
ANISOU 2417  CD  GLN A 317     7873   7266   8504   -807     30   -520  A    C  
ATOM   2418  NE2 GLN A 317      13.512 125.950 261.272  1.00 66.85      A    N  
ANISOU 2418  NE2 GLN A 317     8422   7820   9158   -831     99   -471  A    N  
ATOM   2419  OE1 GLN A 317      14.138 124.972 259.346  1.00 68.65      A    O  
ANISOU 2419  OE1 GLN A 317     8782   8017   9285   -824     14   -582  A    O  
ATOM   2420  N   PRO A 318      17.463 128.888 257.047  1.00 24.56      A    N  
ANISOU 2420  N   PRO A 318     3144   2786   3401   -479    -64   -439  A    N  
ATOM   2421  CA  PRO A 318      17.899 128.825 258.450  1.00 27.22      A    C  
ANISOU 2421  CA  PRO A 318     3492   3060   3791   -454     20   -400  A    C  
ATOM   2422  C   PRO A 318      17.822 130.176 259.150  1.00 29.96      A    C  
ANISOU 2422  C   PRO A 318     3742   3454   4190   -429     28   -328  A    C  
ATOM   2423  O   PRO A 318      18.115 131.217 258.556  1.00 27.86      A    O  
ANISOU 2423  O   PRO A 318     3429   3259   3897   -390    -11   -287  A    O  
ATOM   2424  CB  PRO A 318      19.356 128.376 258.338  1.00 23.17      A    C  
ANISOU 2424  CB  PRO A 318     3074   2533   3196   -372     66   -398  A    C  
ATOM   2425  CG  PRO A 318      19.799 128.924 257.010  1.00 25.01      A    C  
ANISOU 2425  CG  PRO A 318     3300   2862   3340   -334     11   -397  A    C  
ATOM   2426  CD  PRO A 318      18.601 128.832 256.111  1.00 22.95      A    C  
ANISOU 2426  CD  PRO A 318     3004   2631   3084   -408    -69   -446  A    C  
ATOM   2427  N   MET A 319      17.432 130.149 260.419  1.00 26.44      A    N  
ANISOU 2427  N   MET A 319     3266   2964   3817   -449     80   -311  A    N  
ATOM   2428  CA  MET A 319      17.314 131.369 261.204  1.00 25.13      A    C  
ANISOU 2428  CA  MET A 319     3011   2833   3704   -423     93   -262  A    C  
ATOM   2429  C   MET A 319      18.682 131.715 261.783  1.00 22.10      A    C  
ANISOU 2429  C   MET A 319     2664   2450   3281   -343    143   -223  A    C  
ATOM   2430  O   MET A 319      18.987 131.387 262.931  1.00 24.23      A    O  
ANISOU 2430  O   MET A 319     2957   2686   3566   -329    208   -214  A    O  
ATOM   2431  CB  MET A 319      16.263 131.183 262.312  1.00 25.20      A    C  
ANISOU 2431  CB  MET A 319     2966   2812   3797   -477    129   -268  A    C  
ATOM   2432  CG  MET A 319      14.809 131.034 261.801  1.00 29.02      A    C  
ANISOU 2432  CG  MET A 319     3382   3311   4335   -561     75   -300  A    C  
ATOM   2433  SD  MET A 319      13.552 130.948 263.114  1.00 32.66      A    S  
ANISOU 2433  SD  MET A 319     3754   3759   4895   -623    126   -298  A    S  
ATOM   2434  CE  MET A 319      12.048 130.747 262.155  1.00 29.54      A    C  
ANISOU 2434  CE  MET A 319     3281   3395   4549   -717     43   -337  A    C  
ATOM   2435  N   LEU A 320      19.511 132.368 260.973  1.00 16.83      A    N  
ANISOU 2435  N   LEU A 320     2000   1833   2562   -293    112   -196  A    N  
ATOM   2436  CA  LEU A 320      20.873 132.720 261.378  1.00 20.47      A    C  
ANISOU 2436  CA  LEU A 320     2487   2306   2984   -222    152   -158  A    C  
ATOM   2437  C   LEU A 320      21.154 134.179 261.046  1.00 20.89      A    C  
ANISOU 2437  C   LEU A 320     2467   2415   3055   -193    113   -106  A    C  
ATOM   2438  O   LEU A 320      20.559 134.736 260.126  1.00 22.46      A    O  
ANISOU 2438  O   LEU A 320     2620   2650   3263   -214     50    -94  A    O  
ATOM   2439  CB  LEU A 320      21.899 131.818 260.688  1.00 22.91      A    C  
ANISOU 2439  CB  LEU A 320     2891   2615   3199   -183    168   -173  A    C  
ATOM   2440  CG  LEU A 320      21.765 130.313 260.947  1.00 24.56      A    C  
ANISOU 2440  CG  LEU A 320     3187   2749   3395   -202    205   -224  A    C  
ATOM   2441  CD1 LEU A 320      22.600 129.501 259.948  1.00 27.03      A    C  
ANISOU 2441  CD1 LEU A 320     3586   3066   3617   -161    204   -255  A    C  
ATOM   2442  CD2 LEU A 320      22.150 129.977 262.381  1.00 17.34      A    C  
ANISOU 2442  CD2 LEU A 320     2293   1788   2508   -180    275   -203  A    C  
ATOM   2443  N   ALA A 321      22.046 134.800 261.809  1.00 20.53      A    N  
ANISOU 2443  N   ALA A 321     2408   2374   3019   -148    146    -74  A    N  
ATOM   2444  CA  ALA A 321      22.295 136.228 261.666  1.00 18.33      A    C  
ANISOU 2444  CA  ALA A 321     2058   2126   2780   -129    111    -25  A    C  
ATOM   2445  C   ALA A 321      22.883 136.606 260.303  1.00 17.74      A    C  
ANISOU 2445  C   ALA A 321     1987   2106   2646   -113     67     21  A    C  
ATOM   2446  O   ALA A 321      22.423 137.554 259.655  1.00 15.82      A    O  
ANISOU 2446  O   ALA A 321     1684   1887   2439   -124     11     61  A    O  
ATOM   2447  CB  ALA A 321      23.202 136.711 262.791  1.00 19.90      A    C  
ANISOU 2447  CB  ALA A 321     2247   2318   2997    -91    153    -11  A    C  
ATOM   2448  N   HIS A 322      23.876 135.846 259.854  1.00 15.15      A    N  
ANISOU 2448  N   HIS A 322     1727   1802   2226    -82     95     20  A    N  
ATOM   2449  CA  HIS A 322      24.572 136.179 258.616  1.00 18.24      A    C  
ANISOU 2449  CA  HIS A 322     2121   2264   2546    -60     67     68  A    C  
ATOM   2450  C   HIS A 322      23.651 136.135 257.394  1.00 19.54      A    C  
ANISOU 2450  C   HIS A 322     2276   2465   2684    -93      5     63  A    C  
ATOM   2451  O   HIS A 322      23.784 136.962 256.459  1.00 21.39      A    O  
ANISOU 2451  O   HIS A 322     2471   2761   2896    -88    -40    127  A    O  
ATOM   2452  CB  HIS A 322      25.808 135.288 258.425  1.00 15.98      A    C  
ANISOU 2452  CB  HIS A 322     1906   2003   2162    -10    118     57  A    C  
ATOM   2453  CG  HIS A 322      25.621 133.873 258.873  1.00 21.07      A    C  
ANISOU 2453  CG  HIS A 322     2630   2592   2785     -9    158    -17  A    C  
ATOM   2454  CD2 HIS A 322      25.432 132.730 258.165  1.00 17.27      A    C  
ANISOU 2454  CD2 HIS A 322     2219   2102   2238    -10    158    -74  A    C  
ATOM   2455  ND1 HIS A 322      25.657 133.493 260.202  1.00 16.43      A    N  
ANISOU 2455  ND1 HIS A 322     2057   1943   2243     -4    205    -36  A    N  
ATOM   2456  CE1 HIS A 322      25.487 132.189 260.290  1.00 17.41      A    C  
ANISOU 2456  CE1 HIS A 322     2258   2018   2339     -5    233    -90  A    C  
ATOM   2457  NE2 HIS A 322      25.350 131.700 259.070  1.00 17.84      A    N  
ANISOU 2457  NE2 HIS A 322     2350   2097   2333     -9    204   -120  A    N  
ATOM   2458  N   LYS A 323      22.710 135.185 257.414  1.00 20.41      A    N  
ANISOU 2458  N   LYS A 323     2418   2540   2796   -130     -2     -8  A    N  
ATOM   2459  CA  LYS A 323      21.704 135.096 256.360  1.00 21.21      A    C  
ANISOU 2459  CA  LYS A 323     2504   2678   2878   -170    -69    -26  A    C  
ATOM   2460  C   LYS A 323      20.927 136.399 256.282  1.00 18.47      A    C  
ANISOU 2460  C   LYS A 323     2058   2346   2612   -187   -126     32  A    C  
ATOM   2461  O   LYS A 323      20.750 136.966 255.201  1.00 20.61      A    O  
ANISOU 2461  O   LYS A 323     2298   2684   2849   -188   -186     80  A    O  
ATOM   2462  CB  LYS A 323      20.712 133.958 256.610  1.00 17.38      A    C  
ANISOU 2462  CB  LYS A 323     2053   2139   2412   -222    -68   -112  A    C  
ATOM   2463  CG  LYS A 323      19.776 133.734 255.419  1.00 19.37      A    C  
ANISOU 2463  CG  LYS A 323     2293   2439   2627   -265   -144   -143  A    C  
ATOM   2464  CD  LYS A 323      18.510 132.963 255.793  1.00 25.38      A    C  
ANISOU 2464  CD  LYS A 323     3048   3146   3450   -336   -158   -213  A    C  
ATOM   2465  CE  LYS A 323      17.543 133.902 256.494  1.00 26.97      A    C  
ANISOU 2465  CE  LYS A 323     3144   3336   3766   -361   -176   -178  A    C  
ATOM   2466  NZ  LYS A 323      16.156 133.404 256.535  1.00 25.17      A    N1+
ANISOU 2466  NZ  LYS A 323     2877   3092   3593   -436   -210   -230  A    N1+
ATOM   2467  N   GLY A 324      20.449 136.849 257.440  1.00 19.53      A    N  
ANISOU 2467  N   GLY A 324     2145   2422   2853   -198   -107     28  A    N  
ATOM   2468  CA  GLY A 324      19.691 138.084 257.547  1.00 21.29      A    C  
ANISOU 2468  CA  GLY A 324     2274   2643   3173   -204   -154     72  A    C  
ATOM   2469  C   GLY A 324      20.470 139.305 257.095  1.00 21.94      A    C  
ANISOU 2469  C   GLY A 324     2322   2753   3261   -168   -178    164  A    C  
ATOM   2470  O   GLY A 324      19.930 140.173 256.410  1.00 27.49      A    O  
ANISOU 2470  O   GLY A 324     2965   3481   3997   -170   -242    220  A    O  
ATOM   2471  N   VAL A 325      21.736 139.387 257.496  1.00 16.95      A    N  
ANISOU 2471  N   VAL A 325     1723   2114   2602   -136   -128    185  A    N  
ATOM   2472  CA  VAL A 325      22.583 140.498 257.080  1.00 18.72      A    C  
ANISOU 2472  CA  VAL A 325     1915   2364   2835   -112   -146    277  A    C  
ATOM   2473  C   VAL A 325      22.671 140.544 255.555  1.00 19.55      A    C  
ANISOU 2473  C   VAL A 325     2025   2554   2848   -112   -194    338  A    C  
ATOM   2474  O   VAL A 325      22.371 141.589 254.919  1.00 17.32      A    O  
ANISOU 2474  O   VAL A 325     1685   2291   2604   -114   -251    421  A    O  
ATOM   2475  CB  VAL A 325      24.004 140.367 257.674  1.00 19.71      A    C  
ANISOU 2475  CB  VAL A 325     2076   2486   2928    -83    -83    283  A    C  
ATOM   2476  CG1 VAL A 325      24.947 141.384 257.038  1.00 17.31      A    C  
ANISOU 2476  CG1 VAL A 325     1738   2221   2618    -70   -101    386  A    C  
ATOM   2477  CG2 VAL A 325      23.968 140.553 259.174  1.00 18.25      A    C  
ANISOU 2477  CG2 VAL A 325     1874   2230   2829    -79    -45    236  A    C  
ATOM   2478  N   HIS A 326      23.021 139.405 254.950  1.00 19.49      A    N  
ANISOU 2478  N   HIS A 326     2087   2599   2720   -108   -172    295  A    N  
ATOM   2479  CA  HIS A 326      23.149 139.412 253.485  1.00 20.59      A    C  
ANISOU 2479  CA  HIS A 326     2234   2839   2752   -103   -214    344  A    C  
ATOM   2480  C   HIS A 326      21.824 139.705 252.752  1.00 22.47      A    C  
ANISOU 2480  C   HIS A 326     2427   3105   3007   -133   -297    355  A    C  
ATOM   2481  O   HIS A 326      21.788 140.475 251.765  1.00 25.50      A    O  
ANISOU 2481  O   HIS A 326     2771   3556   3360   -128   -351    448  A    O  
ATOM   2482  CB  HIS A 326      23.800 138.118 252.991  1.00 14.43      A    C  
ANISOU 2482  CB  HIS A 326     1539   2108   1835    -84   -173    280  A    C  
ATOM   2483  CG  HIS A 326      25.265 138.038 253.284  1.00 19.88      A    C  
ANISOU 2483  CG  HIS A 326     2257   2813   2483    -41   -105    305  A    C  
ATOM   2484  CD2 HIS A 326      25.938 137.977 254.463  1.00 18.10      A    C  
ANISOU 2484  CD2 HIS A 326     2040   2525   2313    -24    -47    289  A    C  
ATOM   2485  ND1 HIS A 326      26.229 138.055 252.296  1.00 17.10      A    N  
ANISOU 2485  ND1 HIS A 326     1918   2564   2015     -9    -92    357  A    N  
ATOM   2486  CE1 HIS A 326      27.426 137.985 252.850  1.00 22.36      A    C  
ANISOU 2486  CE1 HIS A 326     2595   3227   2674     26    -28    371  A    C  
ATOM   2487  NE2 HIS A 326      27.279 137.933 254.161  1.00 22.25      A    N  
ANISOU 2487  NE2 HIS A 326     2579   3112   2761     17     -4    329  A    N  
ATOM   2488  N   GLU A 327      20.731 139.139 253.265  1.00 21.16      A    N  
ANISOU 2488  N   GLU A 327     2257   2888   2894   -165   -309    271  A    N  
ATOM   2489  CA  GLU A 327      19.410 139.409 252.698  1.00 22.00      A    C  
ANISOU 2489  CA  GLU A 327     2307   3021   3031   -195   -390    275  A    C  
ATOM   2490  C   GLU A 327      19.061 140.897 252.774  1.00 22.73      A    C  
ANISOU 2490  C   GLU A 327     2309   3094   3232   -180   -435    375  A    C  
ATOM   2491  O   GLU A 327      18.522 141.463 251.825  1.00 22.54      A    O  
ANISOU 2491  O   GLU A 327     2240   3132   3194   -180   -509    442  A    O  
ATOM   2492  CB  GLU A 327      18.329 138.573 253.394  1.00 17.45      A    C  
ANISOU 2492  CB  GLU A 327     1731   2390   2511   -237   -385    170  A    C  
ATOM   2493  CG  GLU A 327      18.344 137.097 253.013  1.00 24.92      A    C  
ANISOU 2493  CG  GLU A 327     2759   3353   3356   -263   -369     73  A    C  
ATOM   2494  CD  GLU A 327      17.361 136.273 253.828  1.00 33.86      A    C  
ANISOU 2494  CD  GLU A 327     3891   4417   4559   -315   -354    -18  A    C  
ATOM   2495  OE1 GLU A 327      16.915 136.761 254.891  1.00 35.37      A    O  
ANISOU 2495  OE1 GLU A 327     4027   4548   4864   -320   -331    -10  A    O  
ATOM   2496  OE2 GLU A 327      17.044 135.135 253.415  1.00 36.82      A    O1-
ANISOU 2496  OE2 GLU A 327     4318   4796   4875   -352   -364   -100  A    O1-
ATOM   2497  N   GLY A 328      19.363 141.518 253.910  1.00 18.46      A    N  
ANISOU 2497  N   GLY A 328     1745   2468   2801   -165   -393    383  A    N  
ATOM   2498  CA  GLY A 328      19.122 142.943 254.100  1.00 23.74      A    C  
ANISOU 2498  CA  GLY A 328     2336   3095   3590   -147   -431    465  A    C  
ATOM   2499  C   GLY A 328      19.894 143.792 253.112  1.00 24.71      A    C  
ANISOU 2499  C   GLY A 328     2448   3268   3672   -128   -462    593  A    C  
ATOM   2500  O   GLY A 328      19.356 144.764 252.520  1.00 18.52      A    O  
ANISOU 2500  O   GLY A 328     1603   2493   2941   -119   -531    684  A    O  
ATOM   2501  N   HIS A 329      21.170 143.440 252.939  1.00 22.57      A    N  
ANISOU 2501  N   HIS A 329     2233   3032   3309   -120   -410    610  A    N  
ATOM   2502  CA  HIS A 329      21.975 144.145 251.943  1.00 24.72      A    C  
ANISOU 2502  CA  HIS A 329     2496   3372   3526   -108   -430    738  A    C  
ATOM   2503  C   HIS A 329      21.345 144.038 250.556  1.00 28.37      A    C  
ANISOU 2503  C   HIS A 329     2948   3942   3889   -112   -500    787  A    C  
ATOM   2504  O   HIS A 329      21.188 145.056 249.846  1.00 26.65      A    O  
ANISOU 2504  O   HIS A 329     2679   3750   3696   -105   -557    913  A    O  
ATOM   2505  CB  HIS A 329      23.410 143.620 251.919  1.00 26.08      A    C  
ANISOU 2505  CB  HIS A 329     2724   3588   3599    -96   -358    737  A    C  
ATOM   2506  CG  HIS A 329      24.216 144.018 253.112  1.00 26.33      A    C  
ANISOU 2506  CG  HIS A 329     2750   3533   3723    -91   -304    727  A    C  
ATOM   2507  CD2 HIS A 329      23.894 144.773 254.191  1.00 29.26      A    C  
ANISOU 2507  CD2 HIS A 329     3079   3795   4245    -95   -308    710  A    C  
ATOM   2508  ND1 HIS A 329      25.526 143.633 253.293  1.00 29.41      A    N  
ANISOU 2508  ND1 HIS A 329     3175   3953   4047    -78   -239    726  A    N  
ATOM   2509  CE1 HIS A 329      25.976 144.128 254.428  1.00 28.79      A    C  
ANISOU 2509  CE1 HIS A 329     3077   3791   4072    -79   -210    711  A    C  
ATOM   2510  NE2 HIS A 329      25.008 144.822 254.997  1.00 31.85      A    N  
ANISOU 2510  NE2 HIS A 329     3421   4092   4590    -89   -250    697  A    N  
ATOM   2511  N   VAL A 330      20.959 142.821 250.171  1.00 24.68      A    N  
ANISOU 2511  N   VAL A 330     2529   3535   3312   -123   -499    690  A    N  
ATOM   2512  CA  VAL A 330      20.370 142.663 248.841  1.00 23.81      A    C  
ANISOU 2512  CA  VAL A 330     2412   3541   3093   -129   -571    722  A    C  
ATOM   2513  C   VAL A 330      19.060 143.447 248.686  1.00 24.93      A    C  
ANISOU 2513  C   VAL A 330     2472   3666   3334   -136   -659    768  A    C  
ATOM   2514  O   VAL A 330      18.847 144.113 247.679  1.00 24.62      A    O  
ANISOU 2514  O   VAL A 330     2395   3705   3256   -125   -726    879  A    O  
ATOM   2515  CB  VAL A 330      20.131 141.190 248.478  1.00 23.46      A    C  
ANISOU 2515  CB  VAL A 330     2436   3554   2925   -145   -562    590  A    C  
ATOM   2516  CG1 VAL A 330      19.444 141.097 247.110  1.00 24.97      A    C  
ANISOU 2516  CG1 VAL A 330     2612   3874   3002   -153   -648    615  A    C  
ATOM   2517  CG2 VAL A 330      21.448 140.449 248.436  1.00 19.82      A    C  
ANISOU 2517  CG2 VAL A 330     2052   3123   2354   -123   -482    556  A    C  
ATOM   2518  N   ALA A 331      18.184 143.373 249.682  1.00 23.08      A    N  
ANISOU 2518  N   ALA A 331     2207   3337   3225   -149   -659    689  A    N  
ATOM   2519  CA  ALA A 331      16.909 144.083 249.607  1.00 24.15      A    C  
ANISOU 2519  CA  ALA A 331     2256   3458   3463   -148   -738    723  A    C  
ATOM   2520  C   ALA A 331      17.144 145.583 249.431  1.00 24.57      A    C  
ANISOU 2520  C   ALA A 331     2252   3477   3608   -114   -772    874  A    C  
ATOM   2521  O   ALA A 331      16.536 146.229 248.553  1.00 26.41      A    O  
ANISOU 2521  O   ALA A 331     2431   3765   3839   -100   -855    972  A    O  
ATOM   2522  CB  ALA A 331      16.082 143.818 250.847  1.00 18.38      A    C  
ANISOU 2522  CB  ALA A 331     1497   2631   2857   -162   -713    616  A    C  
ATOM   2523  N   ALA A 332      18.057 146.123 250.239  1.00 21.72      A    N  
ANISOU 2523  N   ALA A 332     1903   3024   3325   -102   -711    896  A    N  
ATOM   2524  CA  ALA A 332      18.387 147.538 250.112  1.00 22.59      A    C  
ANISOU 2524  CA  ALA A 332     1966   3082   3535    -77   -740   1037  A    C  
ATOM   2525  C   ALA A 332      18.880 147.855 248.704  1.00 27.20      A    C  
ANISOU 2525  C   ALA A 332     2555   3781   4000    -74   -780   1180  A    C  
ATOM   2526  O   ALA A 332      18.411 148.816 248.082  1.00 25.23      A    O  
ANISOU 2526  O   ALA A 332     2249   3537   3801    -55   -853   1306  A    O  
ATOM   2527  CB  ALA A 332      19.435 147.934 251.138  1.00 18.42      A    C  
ANISOU 2527  CB  ALA A 332     1458   2451   3088    -76   -667   1026  A    C  
ATOM   2528  N   GLU A 333      19.784 147.021 248.186  1.00 27.99      A    N  
ANISOU 2528  N   GLU A 333     2720   3979   3937    -86   -733   1163  A    N  
ATOM   2529  CA  GLU A 333      20.347 147.250 246.851  1.00 25.74      A    C  
ANISOU 2529  CA  GLU A 333     2441   3824   3514    -81   -759   1295  A    C  
ATOM   2530  C   GLU A 333      19.301 147.201 245.731  1.00 25.19      A    C  
ANISOU 2530  C   GLU A 333     2341   3867   3363    -75   -853   1336  A    C  
ATOM   2531  O   GLU A 333      19.384 147.960 244.765  1.00 28.36      A    O  
ANISOU 2531  O   GLU A 333     2711   4341   3723    -62   -904   1493  A    O  
ATOM   2532  CB  GLU A 333      21.483 146.261 246.563  1.00 28.83      A    C  
ANISOU 2532  CB  GLU A 333     2907   4307   3740    -86   -683   1244  A    C  
ATOM   2533  CG  GLU A 333      22.761 146.543 247.349  1.00 30.97      A    C  
ANISOU 2533  CG  GLU A 333     3194   4505   4068    -88   -600   1261  A    C  
ATOM   2534  CD  GLU A 333      23.567 145.284 247.618  1.00 33.81      A    C  
ANISOU 2534  CD  GLU A 333     3628   4907   4314    -85   -518   1139  A    C  
ATOM   2535  OE1 GLU A 333      23.331 144.276 246.916  1.00 33.34      A    O  
ANISOU 2535  OE1 GLU A 333     3611   4949   4107    -80   -524   1068  A    O  
ATOM   2536  OE2 GLU A 333      24.419 145.295 248.539  1.00 32.64      A    O1-
ANISOU 2536  OE2 GLU A 333     3492   4686   4225    -85   -451   1110  A    O1-
ATOM   2537  N   VAL A 334      18.338 146.290 245.853  1.00 27.10      A    N  
ANISOU 2537  N   VAL A 334     2590   4129   3579    -88   -878   1200  A    N  
ATOM   2538  CA  VAL A 334      17.259 146.159 244.874  1.00 30.93      A    C  
ANISOU 2538  CA  VAL A 334     3039   4724   3990    -89   -975   1216  A    C  
ATOM   2539  C   VAL A 334      16.368 147.393 244.932  1.00 33.56      A    C  
ANISOU 2539  C   VAL A 334     3281   4993   4477    -64  -1051   1325  A    C  
ATOM   2540  O   VAL A 334      15.990 147.944 243.892  1.00 35.91      A    O  
ANISOU 2540  O   VAL A 334     3567   5359   4718    -49  -1095   1411  A    O  
ATOM   2541  CB  VAL A 334      16.410 144.883 245.102  1.00 29.75      A    C  
ANISOU 2541  CB  VAL A 334     2912   4594   3799   -120   -983   1035  A    C  
ATOM   2542  CG1 VAL A 334      15.155 144.908 244.247  1.00 25.44      A    C  
ANISOU 2542  CG1 VAL A 334     2306   4146   3215   -124  -1096   1051  A    C  
ATOM   2543  CG2 VAL A 334      17.224 143.637 244.804  1.00 30.07      A    C  
ANISOU 2543  CG2 VAL A 334     3048   4706   3673   -136   -922    932  A    C  
ATOM   2544  N   ILE A 335      16.032 147.829 246.146  1.00 31.33      A    N  
ANISOU 2544  N   ILE A 335     2965   4556   4382    -57  -1026   1278  A    N  
ATOM   2545  CA  ILE A 335      15.233 149.050 246.292  1.00 29.72      A    C  
ANISOU 2545  CA  ILE A 335     2714   4253   4325    -27  -1050   1330  A    C  
ATOM   2546  C   ILE A 335      15.956 150.245 245.659  1.00 30.91      A    C  
ANISOU 2546  C   ILE A 335     2878   4383   4484    -13  -1037   1487  A    C  
ATOM   2547  O   ILE A 335      15.328 151.119 245.062  1.00 34.10      A    O  
ANISOU 2547  O   ILE A 335     3250   4782   4924      9  -1082   1568  A    O  
ATOM   2548  CB  ILE A 335      14.873 149.337 247.769  1.00 29.23      A    C  
ANISOU 2548  CB  ILE A 335     2625   4032   4451    -18  -1010   1239  A    C  
ATOM   2549  CG1 ILE A 335      13.866 148.301 248.264  1.00 30.50      A    C  
ANISOU 2549  CG1 ILE A 335     2755   4219   4615    -37  -1027   1096  A    C  
ATOM   2550  CG2 ILE A 335      14.283 150.735 247.930  1.00 26.80      A    C  
ANISOU 2550  CG2 ILE A 335     2279   3615   4290     19  -1025   1301  A    C  
ATOM   2551  CD1 ILE A 335      13.515 148.429 249.733  1.00 31.95      A    C  
ANISOU 2551  CD1 ILE A 335     2915   4268   4956    -29   -972    993  A    C  
ATOM   2552  N   ALA A 336      17.284 150.253 245.754  1.00 32.06      A    N  
ANISOU 2552  N   ALA A 336     3325   4338   4520    947     34   1631  A    N  
ATOM   2553  CA  ALA A 336      18.073 151.335 245.175  1.00 32.15      A    C  
ANISOU 2553  CA  ALA A 336     3393   4274   4546   1038    199   1732  A    C  
ATOM   2554  C   ALA A 336      18.118 151.238 243.653  1.00 37.22      A    C  
ANISOU 2554  C   ALA A 336     4160   4993   4988   1151    140   1840  A    C  
ATOM   2555  O   ALA A 336      18.577 152.165 242.980  1.00 42.81      A    O  
ANISOU 2555  O   ALA A 336     4919   5652   5696   1257    277   1967  A    O  
ATOM   2556  CB  ALA A 336      19.473 151.318 245.738  1.00 31.77      A    C  
ANISOU 2556  CB  ALA A 336     3385   4125   4562    973    338   1643  A    C  
ATOM   2557  N   GLY A 337      17.636 150.120 243.115  1.00 35.89      A    N  
ANISOU 2557  N   GLY A 337     4054   4935   4647   1134    -63   1791  A    N  
ATOM   2558  CA  GLY A 337      17.519 149.961 241.677  1.00 38.65      A    C  
ANISOU 2558  CA  GLY A 337     4556   5361   4769   1254   -160   1878  A    C  
ATOM   2559  C   GLY A 337      18.567 149.067 241.043  1.00 38.36      A    C  
ANISOU 2559  C   GLY A 337     4710   5335   4530   1265   -143   1809  A    C  
ATOM   2560  O   GLY A 337      18.642 148.982 239.822  1.00 41.63      A    O  
ANISOU 2560  O   GLY A 337     5298   5796   4724   1389   -186   1882  A    O  
ATOM   2561  N   LYS A 338      19.364 148.390 241.863  1.00 39.28      A    N  
ANISOU 2561  N   LYS A 338     4807   5407   4712   1149    -78   1674  A    N  
ATOM   2562  CA  LYS A 338      20.373 147.468 241.347  1.00 39.91      A    C  
ANISOU 2562  CA  LYS A 338     5054   5487   4623   1157    -46   1609  A    C  
ATOM   2563  C   LYS A 338      19.767 146.097 241.075  1.00 44.23      A    C  
ANISOU 2563  C   LYS A 338     5682   6122   5002   1106   -294   1490  A    C  
ATOM   2564  O   LYS A 338      18.903 145.642 241.820  1.00 42.76      A    O  
ANISOU 2564  O   LYS A 338     5365   5966   4917    996   -446   1412  A    O  
ATOM   2565  CB  LYS A 338      21.534 147.347 242.337  1.00 36.17      A    C  
ANISOU 2565  CB  LYS A 338     4513   4918   4312   1059    123   1528  A    C  
ATOM   2566  CG  LYS A 338      22.265 148.656 242.568  1.00 41.51      A    C  
ANISOU 2566  CG  LYS A 338     5115   5479   5176   1099    352   1634  A    C  
ATOM   2567  CD  LYS A 338      23.335 148.531 243.640  1.00 47.31      A    C  
ANISOU 2567  CD  LYS A 338     5767   6114   6096    986    463   1542  A    C  
ATOM   2568  CE  LYS A 338      23.953 149.893 243.938  1.00 51.96      A    C  
ANISOU 2568  CE  LYS A 338     6264   6566   6911   1009    653   1638  A    C  
ATOM   2569  NZ  LYS A 338      25.040 150.267 242.983  1.00 55.03      A    N1+
ANISOU 2569  NZ  LYS A 338     6729   6886   7292   1117    846   1774  A    N1+
ATOM   2570  N   LYS A 339      20.218 145.429 240.019  1.00 49.41      A    N  
ANISOU 2570  N   LYS A 339     6559   6805   5410   1189   -326   1479  A    N  
ATOM   2571  CA  LYS A 339      19.669 144.112 239.712  1.00 51.39      A    C  
ANISOU 2571  CA  LYS A 339     6909   7118   5499   1139   -577   1353  A    C  
ATOM   2572  C   LYS A 339      20.427 143.009 240.445  1.00 46.01      A    C  
ANISOU 2572  C   LYS A 339     6224   6399   4859   1018   -533   1202  A    C  
ATOM   2573  O   LYS A 339      21.220 142.274 239.850  1.00 48.11      A    O  
ANISOU 2573  O   LYS A 339     6682   6650   4950   1066   -487   1156  A    O  
ATOM   2574  CB  LYS A 339      19.577 143.872 238.196  1.00 61.19      A    C  
ANISOU 2574  CB  LYS A 339     8423   8405   6420   1297   -685   1396  A    C  
ATOM   2575  CG  LYS A 339      18.850 142.578 237.780  1.00 72.44      A    C  
ANISOU 2575  CG  LYS A 339     9965   9881   7678   1248  -1001   1259  A    C  
ATOM   2576  CD  LYS A 339      18.565 142.541 236.265  1.00 80.38      A    C  
ANISOU 2576  CD  LYS A 339    11257  10931   8351   1423  -1152   1308  A    C  
ATOM   2577  CE  LYS A 339      19.635 141.761 235.489  1.00 83.78      A    C  
ANISOU 2577  CE  LYS A 339    11976  11316   8540   1493  -1032   1231  A    C  
ATOM   2578  NZ  LYS A 339      19.553 140.286 235.725  1.00 85.42      A    N1+
ANISOU 2578  NZ  LYS A 339    12251  11514   8693   1378  -1215   1038  A    N1+
ATOM   2579  N   HIS A 340      20.185 142.917 241.750  1.00 39.94      A    N  
ANISOU 2579  N   HIS A 340     5246   5610   4320    875   -533   1136  A    N  
ATOM   2580  CA  HIS A 340      20.881 141.954 242.586  1.00 37.47      A    C  
ANISOU 2580  CA  HIS A 340     4907   5260   4070    761   -487   1007  A    C  
ATOM   2581  C   HIS A 340      19.905 140.896 243.079  1.00 35.95      A    C  
ANISOU 2581  C   HIS A 340     4642   5106   3912    642   -712    895  A    C  
ATOM   2582  O   HIS A 340      18.695 141.131 243.158  1.00 32.24      A    O  
ANISOU 2582  O   HIS A 340     4061   4676   3514    622   -866    929  A    O  
ATOM   2583  CB  HIS A 340      21.538 142.656 243.781  1.00 35.90      A    C  
ANISOU 2583  CB  HIS A 340     4548   4991   4102    700   -293   1018  A    C  
ATOM   2584  CG  HIS A 340      22.698 143.518 243.402  1.00 36.39      A    C  
ANISOU 2584  CG  HIS A 340     4660   4984   4183    790    -65   1116  A    C  
ATOM   2585  CD2 HIS A 340      23.263 143.763 242.196  1.00 37.23      A    C  
ANISOU 2585  CD2 HIS A 340     4929   5083   4133    929     32   1213  A    C  
ATOM   2586  ND1 HIS A 340      23.396 144.284 244.314  1.00 40.81      A    N  
ANISOU 2586  ND1 HIS A 340     5092   5457   4956    746     95   1134  A    N  
ATOM   2587  CE1 HIS A 340      24.352 144.943 243.688  1.00 41.94      A    C  
ANISOU 2587  CE1 HIS A 340     5292   5537   5107    840    277   1241  A    C  
ATOM   2588  NE2 HIS A 340      24.294 144.648 242.404  1.00 39.91      A    N  
ANISOU 2588  NE2 HIS A 340     5212   5329   4625    959    262   1300  A    N  
ATOM   2589  N   TYR A 341      20.445 139.730 243.408  1.00 35.44      A    N  
ANISOU 2589  N   TYR A 341     4627   5020   3818    567   -721    776  A    N  
ATOM   2590  CA  TYR A 341      19.640 138.605 243.836  1.00 35.25      A    C  
ANISOU 2590  CA  TYR A 341     4543   5013   3836    454   -917    671  A    C  
ATOM   2591  C   TYR A 341      20.332 137.968 245.025  1.00 32.16      A    C  
ANISOU 2591  C   TYR A 341     4073   4577   3569    351   -803    586  A    C  
ATOM   2592  O   TYR A 341      21.556 138.012 245.131  1.00 32.52      A    O  
ANISOU 2592  O   TYR A 341     4181   4582   3594    376   -627    581  A    O  
ATOM   2593  CB  TYR A 341      19.501 137.597 242.694  1.00 36.03      A    C  
ANISOU 2593  CB  TYR A 341     4854   5128   3710    488  -1100    600  A    C  
ATOM   2594  CG  TYR A 341      18.827 138.178 241.477  1.00 38.01      A    C  
ANISOU 2594  CG  TYR A 341     5214   5424   3803    603  -1243    679  A    C  
ATOM   2595  CD1 TYR A 341      19.571 138.770 240.463  1.00 40.72      A    C  
ANISOU 2595  CD1 TYR A 341     5758   5768   3946    760  -1116    756  A    C  
ATOM   2596  CD2 TYR A 341      17.444 138.152 241.348  1.00 38.20      A    C  
ANISOU 2596  CD2 TYR A 341     5135   5487   3893    564  -1501    694  A    C  
ATOM   2597  CE1 TYR A 341      18.956 139.318 239.350  1.00 37.42      A    C  
ANISOU 2597  CE1 TYR A 341     5460   5395   3363    883  -1248    838  A    C  
ATOM   2598  CE2 TYR A 341      16.821 138.696 240.238  1.00 39.88      A    C  
ANISOU 2598  CE2 TYR A 341     5448   5743   3961    674  -1657    773  A    C  
ATOM   2599  CZ  TYR A 341      17.583 139.275 239.242  1.00 41.34      A    C  
ANISOU 2599  CZ  TYR A 341     5858   5936   3914    838  -1532    841  A    C  
ATOM   2600  OH  TYR A 341      16.973 139.818 238.132  1.00 46.74      A    O  
ANISOU 2600  OH  TYR A 341     6663   6666   4430    965  -1687    928  A    O  
ATOM   2601  N   PHE A 342      19.545 137.378 245.917  1.00 28.84      A    N  
ANISOU 2601  N   PHE A 342     3509   4158   3289    243   -901    535  A    N  
ATOM   2602  CA  PHE A 342      20.091 136.587 247.005  1.00 23.47      A    C  
ANISOU 2602  CA  PHE A 342     2776   3441   2701    152   -824    452  A    C  
ATOM   2603  C   PHE A 342      19.957 135.119 246.643  1.00 27.20      A    C  
ANISOU 2603  C   PHE A 342     3337   3905   3093     97   -970    349  A    C  
ATOM   2604  O   PHE A 342      18.858 134.559 246.662  1.00 28.40      A    O  
ANISOU 2604  O   PHE A 342     3415   4065   3309     35  -1151    328  A    O  
ATOM   2605  CB  PHE A 342      19.374 136.891 248.319  1.00 22.52      A    C  
ANISOU 2605  CB  PHE A 342     2455   3314   2786     87   -796    474  A    C  
ATOM   2606  CG  PHE A 342      19.899 136.105 249.484  1.00 24.35      A    C  
ANISOU 2606  CG  PHE A 342     2647   3510   3095     10   -719    399  A    C  
ATOM   2607  CD1 PHE A 342      21.114 136.430 250.067  1.00 20.40      A    C  
ANISOU 2607  CD1 PHE A 342     2175   2973   2603     20   -557    383  A    C  
ATOM   2608  CD2 PHE A 342      19.172 135.038 249.999  1.00 23.25      A    C  
ANISOU 2608  CD2 PHE A 342     2434   3365   3035    -72   -816    354  A    C  
ATOM   2609  CE1 PHE A 342      21.603 135.703 251.138  1.00 24.32      A    C  
ANISOU 2609  CE1 PHE A 342     2643   3439   3158    -41   -504    320  A    C  
ATOM   2610  CE2 PHE A 342      19.651 134.308 251.072  1.00 25.38      A    C  
ANISOU 2610  CE2 PHE A 342     2677   3602   3365   -129   -737    299  A    C  
ATOM   2611  CZ  PHE A 342      20.870 134.637 251.642  1.00 25.61      A    C  
ANISOU 2611  CZ  PHE A 342     2751   3606   3374   -110   -586    279  A    C  
ATOM   2612  N   ASP A 343      21.078 134.516 246.267  1.00 31.85      A    N  
ANISOU 2612  N   ASP A 343     4081   4463   3556    123   -888    294  A    N  
ATOM   2613  CA  ASP A 343      21.095 133.127 245.830  1.00 35.72      A    C  
ANISOU 2613  CA  ASP A 343     4696   4927   3949     87  -1006    188  A    C  
ATOM   2614  C   ASP A 343      22.434 132.493 246.172  1.00 29.26      A    C  
ANISOU 2614  C   ASP A 343     3951   4061   3107     86   -836    141  A    C  
ATOM   2615  O   ASP A 343      23.189 132.107 245.280  1.00 29.58      A    O  
ANISOU 2615  O   ASP A 343     4185   4075   2978    161   -789    118  A    O  
ATOM   2616  CB  ASP A 343      20.841 133.052 244.320  1.00 41.02      A    C  
ANISOU 2616  CB  ASP A 343     5578   5612   4397    177  -1147    179  A    C  
ATOM   2617  CG  ASP A 343      20.398 131.671 243.864  1.00 48.78      A    C  
ANISOU 2617  CG  ASP A 343     6675   6558   5303    123  -1354     56  A    C  
ATOM   2618  OD1 ASP A 343      19.787 130.941 244.674  1.00 51.23      A    O  
ANISOU 2618  OD1 ASP A 343     6835   6844   5784      0  -1445      7  A    O  
ATOM   2619  OD2 ASP A 343      20.647 131.324 242.688  1.00 54.66      A    O1-
ANISOU 2619  OD2 ASP A 343     7668   7287   5814    210  -1424     11  A    O1-
ATOM   2620  N   PRO A 344      22.745 132.394 247.471  1.00 24.91      A    N  
ANISOU 2620  N   PRO A 344     3250   3493   2720     12   -738    135  A    N  
ATOM   2621  CA  PRO A 344      24.047 131.848 247.860  1.00 26.04      A    C  
ANISOU 2621  CA  PRO A 344     3439   3590   2865     13   -587    106  A    C  
ATOM   2622  C   PRO A 344      24.080 130.348 247.604  1.00 29.44      A    C  
ANISOU 2622  C   PRO A 344     3974   3982   3228    -26   -664      7  A    C  
ATOM   2623  O   PRO A 344      23.050 129.684 247.729  1.00 23.31      A    O  
ANISOU 2623  O   PRO A 344     3156   3206   2495    -99   -828    -44  A    O  
ATOM   2624  CB  PRO A 344      24.089 132.104 249.364  1.00 21.42      A    C  
ANISOU 2624  CB  PRO A 344     2674   3003   2464    -58   -521    118  A    C  
ATOM   2625  CG  PRO A 344      22.663 132.020 249.782  1.00 22.77      A    C  
ANISOU 2625  CG  PRO A 344     2731   3201   2719   -119   -658    115  A    C  
ATOM   2626  CD  PRO A 344      21.870 132.610 248.638  1.00 25.67      A    C  
ANISOU 2626  CD  PRO A 344     3147   3605   3001    -67   -773    153  A    C  
ATOM   2627  N   LYS A 345      25.235 129.823 247.218  1.00 31.15      A    N  
ANISOU 2627  N   LYS A 345     4322   4154   3359     26   -544    -11  A    N  
ATOM   2628  CA  LYS A 345      25.379 128.379 247.096  1.00 29.44      A    C  
ANISOU 2628  CA  LYS A 345     4207   3883   3095     -7   -590   -106  A    C  
ATOM   2629  C   LYS A 345      25.311 127.724 248.468  1.00 26.36      A    C  
ANISOU 2629  C   LYS A 345     3656   3478   2883   -115   -582   -133  A    C  
ATOM   2630  O   LYS A 345      24.765 126.628 248.613  1.00 33.27      A    O  
ANISOU 2630  O   LYS A 345     4538   4317   3785   -184   -688   -207  A    O  
ATOM   2631  CB  LYS A 345      26.681 128.013 246.388  1.00 33.99      A    C  
ANISOU 2631  CB  LYS A 345     4961   4406   3548     93   -427   -101  A    C  
ATOM   2632  CG  LYS A 345      26.553 127.983 244.878  1.00 42.24      A    C  
ANISOU 2632  CG  LYS A 345     6256   5439   4354    205   -476   -120  A    C  
ATOM   2633  CD  LYS A 345      27.794 127.412 244.214  1.00 50.57      A    C  
ANISOU 2633  CD  LYS A 345     7506   6422   5285    317   -291   -116  A    C  
ATOM   2634  CE  LYS A 345      27.811 127.803 242.749  1.00 55.33      A    C  
ANISOU 2634  CE  LYS A 345     8366   7023   5635    472   -278    -92  A    C  
ATOM   2635  NZ  LYS A 345      27.666 129.282 242.613  1.00 55.56      A    N1+
ANISOU 2635  NZ  LYS A 345     8302   7117   5692    521   -232     30  A    N1+
ATOM   2636  N   VAL A 346      25.908 128.377 249.464  1.00 22.51      A    N  
ANISOU 2636  N   VAL A 346     3033   3005   2514   -123   -456    -72  A    N  
ATOM   2637  CA  VAL A 346      25.984 127.814 250.811  1.00 24.08      A    C  
ANISOU 2637  CA  VAL A 346     3106   3189   2853   -199   -431    -87  A    C  
ATOM   2638  C   VAL A 346      25.694 128.823 251.915  1.00 26.20      A    C  
ANISOU 2638  C   VAL A 346     3218   3495   3240   -221   -405    -33  A    C  
ATOM   2639  O   VAL A 346      25.914 130.027 251.757  1.00 26.74      A    O  
ANISOU 2639  O   VAL A 346     3266   3585   3309   -175   -357     22  A    O  
ATOM   2640  CB  VAL A 346      27.356 127.170 251.085  1.00 22.63      A    C  
ANISOU 2640  CB  VAL A 346     2962   2956   2681   -177   -298    -88  A    C  
ATOM   2641  CG1 VAL A 346      27.623 126.053 250.097  1.00 21.78      A    C  
ANISOU 2641  CG1 VAL A 346     3025   2794   2455   -147   -304   -148  A    C  
ATOM   2642  CG2 VAL A 346      28.461 128.219 251.011  1.00 19.35      A    C  
ANISOU 2642  CG2 VAL A 346     2528   2539   2286   -110   -165    -11  A    C  
ATOM   2643  N   ILE A 347      25.189 128.310 253.031  1.00 21.91      A    N  
ANISOU 2643  N   ILE A 347     2579   2949   2797   -283   -427    -46  A    N  
ATOM   2644  CA  ILE A 347      25.035 129.085 254.253  1.00 19.27      A    C  
ANISOU 2644  CA  ILE A 347     2134   2635   2555   -289   -382     -5  A    C  
ATOM   2645  C   ILE A 347      25.591 128.254 255.405  1.00 18.25      A    C  
ANISOU 2645  C   ILE A 347     1979   2476   2478   -315   -330    -21  A    C  
ATOM   2646  O   ILE A 347      25.083 127.177 255.691  1.00 21.34      A    O  
ANISOU 2646  O   ILE A 347     2356   2849   2903   -357   -360    -43  A    O  
ATOM   2647  CB  ILE A 347      23.558 129.415 254.545  1.00 19.96      A    C  
ANISOU 2647  CB  ILE A 347     2128   2749   2707   -313   -451     22  A    C  
ATOM   2648  CG1 ILE A 347      22.914 130.118 253.345  1.00 22.11      A    C  
ANISOU 2648  CG1 ILE A 347     2422   3050   2927   -287   -532     43  A    C  
ATOM   2649  CG2 ILE A 347      23.439 130.268 255.807  1.00 16.06      A    C  
ANISOU 2649  CG2 ILE A 347     1558   2263   2283   -294   -379     62  A    C  
ATOM   2650  CD1 ILE A 347      21.445 130.437 253.524  1.00 27.34      A    C  
ANISOU 2650  CD1 ILE A 347     2972   3735   3682   -307   -609     88  A    C  
ATOM   2651  N   PRO A 348      26.647 128.754 256.063  1.00 17.17      A    N  
ANISOU 2651  N   PRO A 348     1834   2328   2361   -289   -261     -6  A    N  
ATOM   2652  CA  PRO A 348      27.318 128.029 257.145  1.00 19.35      A    C  
ANISOU 2652  CA  PRO A 348     2099   2579   2675   -300   -226    -14  A    C  
ATOM   2653  C   PRO A 348      26.464 127.940 258.404  1.00 19.49      A    C  
ANISOU 2653  C   PRO A 348     2067   2607   2730   -310   -230     -3  A    C  
ATOM   2654  O   PRO A 348      25.598 128.790 258.629  1.00 18.54      A    O  
ANISOU 2654  O   PRO A 348     1911   2510   2624   -297   -238     19  A    O  
ATOM   2655  CB  PRO A 348      28.559 128.887 257.418  1.00 21.00      A    C  
ANISOU 2655  CB  PRO A 348     2300   2767   2911   -269   -190      6  A    C  
ATOM   2656  CG  PRO A 348      28.169 130.264 256.988  1.00 19.65      A    C  
ANISOU 2656  CG  PRO A 348     2114   2613   2739   -247   -197     28  A    C  
ATOM   2657  CD  PRO A 348      27.285 130.056 255.790  1.00 20.59      A    C  
ANISOU 2657  CD  PRO A 348     2266   2761   2798   -248   -226     26  A    C  
ATOM   2658  N   SER A 349      26.695 126.896 259.195  1.00 14.69      A    N  
ANISOU 2658  N   SER A 349     1462   1979   2141   -319   -207     -5  A    N  
ATOM   2659  CA  SER A 349      26.042 126.739 260.490  1.00 14.54      A    C  
ANISOU 2659  CA  SER A 349     1418   1961   2144   -304   -179     22  A    C  
ATOM   2660  C   SER A 349      27.110 126.341 261.503  1.00 20.24      A    C  
ANISOU 2660  C   SER A 349     2177   2664   2848   -276   -157     22  A    C  
ATOM   2661  O   SER A 349      27.998 125.541 261.179  1.00 17.30      A    O  
ANISOU 2661  O   SER A 349     1821   2270   2484   -290   -155     12  A    O  
ATOM   2662  CB  SER A 349      24.965 125.655 260.431  1.00 20.16      A    C  
ANISOU 2662  CB  SER A 349     2087   2657   2915   -341   -174     40  A    C  
ATOM   2663  OG  SER A 349      23.939 125.982 259.520  1.00 32.52      A    O  
ANISOU 2663  OG  SER A 349     3608   4235   4514   -371   -228     42  A    O  
ATOM   2664  N   ILE A 350      27.050 126.921 262.703  1.00 18.25      A    N  
ANISOU 2664  N   ILE A 350     1950   2416   2566   -228   -146     35  A    N  
ATOM   2665  CA  ILE A 350      27.992 126.589 263.778  1.00 18.64      A    C  
ANISOU 2665  CA  ILE A 350     2050   2448   2583   -191   -156     36  A    C  
ATOM   2666  C   ILE A 350      27.310 126.431 265.144  1.00 21.09      A    C  
ANISOU 2666  C   ILE A 350     2412   2758   2841   -126   -106     69  A    C  
ATOM   2667  O   ILE A 350      26.510 127.272 265.552  1.00 22.36      A    O  
ANISOU 2667  O   ILE A 350     2595   2925   2973    -85    -77     77  A    O  
ATOM   2668  CB  ILE A 350      29.101 127.644 263.937  1.00 19.31      A    C  
ANISOU 2668  CB  ILE A 350     2158   2517   2660   -177   -230      5  A    C  
ATOM   2669  CG1 ILE A 350      29.850 127.870 262.625  1.00 17.03      A    C  
ANISOU 2669  CG1 ILE A 350     1818   2218   2434   -220   -245     -2  A    C  
ATOM   2670  CG2 ILE A 350      30.081 127.244 265.061  1.00 14.42      A    C  
ANISOU 2670  CG2 ILE A 350     1587   1876   2014   -140   -281      6  A    C  
ATOM   2671  CD1 ILE A 350      30.882 128.996 262.711  1.00 16.78      A    C  
ANISOU 2671  CD1 ILE A 350     1776   2152   2449   -214   -309    -15  A    C  
ATOM   2672  N   ALA A 351      27.621 125.333 265.827  1.00 17.85      A    N  
ANISOU 2672  N   ALA A 351     2028   2335   2418   -104    -79     99  A    N  
ATOM   2673  CA  ALA A 351      27.298 125.142 267.229  1.00 16.38      A    C  
ANISOU 2673  CA  ALA A 351     1924   2143   2155    -16    -27    140  A    C  
ATOM   2674  C   ALA A 351      28.566 125.439 268.009  1.00 17.30      A    C  
ANISOU 2674  C   ALA A 351     2129   2251   2192     28   -127    108  A    C  
ATOM   2675  O   ALA A 351      29.580 124.744 267.833  1.00 17.64      A    O  
ANISOU 2675  O   ALA A 351     2146   2286   2273      1   -176    110  A    O  
ATOM   2676  CB  ALA A 351      26.855 123.708 267.481  1.00 15.98      A    C  
ANISOU 2676  CB  ALA A 351     1845   2075   2150    -13     66    208  A    C  
ATOM   2677  N   TYR A 352      28.505 126.465 268.861  1.00 17.74      A    N  
ANISOU 2677  N   TYR A 352     2290   2301   2149     98   -165     79  A    N  
ATOM   2678  CA  TYR A 352      29.669 126.940 269.602  1.00 18.93      A    C  
ANISOU 2678  CA  TYR A 352     2531   2429   2232    133   -308     31  A    C  
ATOM   2679  C   TYR A 352      29.799 126.186 270.919  1.00 22.63      A    C  
ANISOU 2679  C   TYR A 352     3126   2895   2579    234   -299     71  A    C  
ATOM   2680  O   TYR A 352      30.111 126.760 271.969  1.00 23.23      A    O  
ANISOU 2680  O   TYR A 352     3355   2950   2522    318   -387     35  A    O  
ATOM   2681  CB  TYR A 352      29.580 128.451 269.841  1.00 18.34      A    C  
ANISOU 2681  CB  TYR A 352     2531   2328   2107    158   -377    -37  A    C  
ATOM   2682  CG  TYR A 352      29.561 129.273 268.564  1.00 18.80      A    C  
ANISOU 2682  CG  TYR A 352     2471   2385   2285     70   -389    -66  A    C  
ATOM   2683  CD1 TYR A 352      28.374 129.491 267.877  1.00 17.79      A    C  
ANISOU 2683  CD1 TYR A 352     2285   2283   2192     54   -273    -38  A    C  
ATOM   2684  CD2 TYR A 352      30.723 129.841 268.060  1.00 23.28      A    C  
ANISOU 2684  CD2 TYR A 352     2981   2919   2943     11   -514   -105  A    C  
ATOM   2685  CE1 TYR A 352      28.344 130.240 266.720  1.00 18.52      A    C  
ANISOU 2685  CE1 TYR A 352     2287   2377   2374    -10   -286    -55  A    C  
ATOM   2686  CE2 TYR A 352      30.703 130.596 266.899  1.00 21.44      A    C  
ANISOU 2686  CE2 TYR A 352     2653   2681   2814    -51   -502   -114  A    C  
ATOM   2687  CZ  TYR A 352      29.511 130.788 266.236  1.00 23.72      A    C  
ANISOU 2687  CZ  TYR A 352     2908   3005   3102    -57   -390    -91  A    C  
ATOM   2688  OH  TYR A 352      29.481 131.536 265.084  1.00 24.30      A    O  
ANISOU 2688  OH  TYR A 352     2901   3075   3258   -104   -380    -91  A    O  
ATOM   2689  N   THR A 353      29.549 124.884 270.846  1.00 19.91      A    N  
ANISOU 2689  N   THR A 353     2728   2562   2274    230   -196    146  A    N  
ATOM   2690  CA  THR A 353      29.792 123.986 271.959  1.00 21.42      A    C  
ANISOU 2690  CA  THR A 353     3019   2749   2370    324   -175    206  A    C  
ATOM   2691  C   THR A 353      31.295 123.724 272.003  1.00 22.92      A    C  
ANISOU 2691  C   THR A 353     3191   2930   2588    298   -341    184  A    C  
ATOM   2692  O   THR A 353      32.050 124.271 271.196  1.00 22.16      A    O  
ANISOU 2692  O   THR A 353     3001   2823   2595    213   -447    131  A    O  
ATOM   2693  CB  THR A 353      29.061 122.658 271.740  1.00 24.60      A    C  
ANISOU 2693  CB  THR A 353     3343   3150   2853    313     -5    300  A    C  
ATOM   2694  CG2 THR A 353      27.562 122.839 271.934  1.00 24.01      A    C  
ANISOU 2694  CG2 THR A 353     3277   3071   2775    357    162    352  A    C  
ATOM   2695  OG1 THR A 353      29.305 122.197 270.405  1.00 24.52      A    O  
ANISOU 2695  OG1 THR A 353     3175   3136   3004    188    -13    281  A    O  
ATOM   2696  N   GLU A 354      31.729 122.884 272.935  1.00 24.85      A    N  
ANISOU 2696  N   GLU A 354     3515   3173   2755    379   -356    241  A    N  
ATOM   2697  CA  GLU A 354      33.125 122.470 273.007  1.00 27.63      A    C  
ANISOU 2697  CA  GLU A 354     3827   3513   3160    362   -506    248  A    C  
ATOM   2698  C   GLU A 354      33.222 120.947 273.048  1.00 31.63      A    C  
ANISOU 2698  C   GLU A 354     4284   4018   3716    380   -396    348  A    C  
ATOM   2699  O   GLU A 354      32.856 120.329 274.045  1.00 33.36      A    O  
ANISOU 2699  O   GLU A 354     4618   4242   3817    487   -326    417  A    O  
ATOM   2700  CB  GLU A 354      33.833 123.104 274.206  1.00 36.51      A    C  
ANISOU 2700  CB  GLU A 354     5112   4624   4136    452   -706    209  A    C  
ATOM   2701  CG  GLU A 354      35.357 122.934 274.209  1.00 44.79      A    C  
ANISOU 2701  CG  GLU A 354     6083   5649   5286    418   -911    212  A    C  
ATOM   2702  CD  GLU A 354      36.055 123.703 273.093  1.00 48.71      A    C  
ANISOU 2702  CD  GLU A 354     6409   6115   5981    291   -999    159  A    C  
ATOM   2703  OE1 GLU A 354      35.395 124.504 272.401  1.00 50.64      A    O  
ANISOU 2703  OE1 GLU A 354     6625   6362   6253    237   -931    105  A    O  
ATOM   2704  OE2 GLU A 354      37.273 123.502 272.909  1.00 50.92      A    O1-
ANISOU 2704  OE2 GLU A 354     6578   6366   6403    254  -1127    187  A    O1-
ATOM   2705  N   PRO A 355      33.705 120.333 271.957  1.00 29.43      A    N  
ANISOU 2705  N   PRO A 355     3848   3724   3611    284   -364    361  A    N  
ATOM   2706  CA  PRO A 355      34.214 120.973 270.737  1.00 23.21      A    C  
ANISOU 2706  CA  PRO A 355     2936   2925   2959    177   -419    300  A    C  
ATOM   2707  C   PRO A 355      33.110 121.609 269.910  1.00 21.55      A    C  
ANISOU 2707  C   PRO A 355     2700   2729   2762    119   -329    250  A    C  
ATOM   2708  O   PRO A 355      31.935 121.284 270.101  1.00 19.00      A    O  
ANISOU 2708  O   PRO A 355     2412   2416   2393    143   -204    274  A    O  
ATOM   2709  CB  PRO A 355      34.807 119.799 269.958  1.00 22.42      A    C  
ANISOU 2709  CB  PRO A 355     2723   2796   2998    134   -346    354  A    C  
ATOM   2710  CG  PRO A 355      33.984 118.625 270.391  1.00 25.88      A    C  
ANISOU 2710  CG  PRO A 355     3205   3230   3398    178   -199    419  A    C  
ATOM   2711  CD  PRO A 355      33.711 118.864 271.852  1.00 25.88      A    C  
ANISOU 2711  CD  PRO A 355     3349   3254   3229    291   -240    447  A    C  
ATOM   2712  N   GLU A 356      33.490 122.510 269.010  1.00 20.26      A    N  
ANISOU 2712  N   GLU A 356     2465   2559   2675     50   -391    194  A    N  
ATOM   2713  CA  GLU A 356      32.518 123.173 268.153  1.00 21.95      A    C  
ANISOU 2713  CA  GLU A 356     2651   2787   2902      0   -324    151  A    C  
ATOM   2714  C   GLU A 356      32.088 122.200 267.064  1.00 17.91      A    C  
ANISOU 2714  C   GLU A 356     2064   2268   2474    -58   -206    171  A    C  
ATOM   2715  O   GLU A 356      32.854 121.315 266.669  1.00 21.26      A    O  
ANISOU 2715  O   GLU A 356     2444   2665   2970    -74   -188    200  A    O  
ATOM   2716  CB  GLU A 356      33.108 124.464 267.554  1.00 18.15      A    C  
ANISOU 2716  CB  GLU A 356     2127   2294   2476    -44   -422     97  A    C  
ATOM   2717  CG  GLU A 356      33.683 125.424 268.619  1.00 19.02      A    C  
ANISOU 2717  CG  GLU A 356     2315   2386   2527      2   -578     60  A    C  
ATOM   2718  CD  GLU A 356      34.154 126.768 268.063  1.00 24.92      A    C  
ANISOU 2718  CD  GLU A 356     3012   3101   3357    -46   -669     10  A    C  
ATOM   2719  OE1 GLU A 356      34.066 126.986 266.832  1.00 20.83      A    O  
ANISOU 2719  OE1 GLU A 356     2400   2583   2930   -104   -597     14  A    O  
ATOM   2720  OE2 GLU A 356      34.648 127.598 268.864  1.00 22.82      A    O1-
ANISOU 2720  OE2 GLU A 356     2807   2799   3063    -22   -820    -34  A    O1-
ATOM   2721  N   VAL A 357      30.854 122.337 266.600  1.00 19.37      A    N  
ANISOU 2721  N   VAL A 357     2238   2465   2654    -85   -133    158  A    N  
ATOM   2722  CA  VAL A 357      30.405 121.537 265.466  1.00 19.34      A    C  
ANISOU 2722  CA  VAL A 357     2178   2442   2728   -149    -64    155  A    C  
ATOM   2723  C   VAL A 357      29.997 122.503 264.368  1.00 20.70      A    C  
ANISOU 2723  C   VAL A 357     2320   2632   2914   -197    -89    105  A    C  
ATOM   2724  O   VAL A 357      29.064 123.266 264.547  1.00 16.55      A    O  
ANISOU 2724  O   VAL A 357     1798   2131   2359   -190    -87     98  A    O  
ATOM   2725  CB  VAL A 357      29.204 120.644 265.827  1.00 17.72      A    C  
ANISOU 2725  CB  VAL A 357     1969   2221   2543   -145     29    197  A    C  
ATOM   2726  CG1 VAL A 357      28.659 119.950 264.582  1.00 15.27      A    C  
ANISOU 2726  CG1 VAL A 357     1607   1876   2320   -224     56    171  A    C  
ATOM   2727  CG2 VAL A 357      29.601 119.618 266.872  1.00 19.41      A    C  
ANISOU 2727  CG2 VAL A 357     2219   2413   2744    -86     75    263  A    C  
ATOM   2728  N   ALA A 358      30.700 122.480 263.239  1.00 15.00      A    N  
ANISOU 2728  N   ALA A 358     1573   1892   2232   -232    -99     81  A    N  
ATOM   2729  CA  ALA A 358      30.481 123.472 262.196  1.00 15.01      A    C  
ANISOU 2729  CA  ALA A 358     1561   1910   2232   -259   -121     46  A    C  
ATOM   2730  C   ALA A 358      30.354 122.788 260.854  1.00 19.81      A    C  
ANISOU 2730  C   ALA A 358     2179   2493   2856   -294    -87     23  A    C  
ATOM   2731  O   ALA A 358      31.106 121.871 260.556  1.00 20.67      A    O  
ANISOU 2731  O   ALA A 358     2303   2560   2991   -289    -49     32  A    O  
ATOM   2732  CB  ALA A 358      31.649 124.451 262.146  1.00 13.87      A    C  
ANISOU 2732  CB  ALA A 358     1399   1760   2112   -242   -167     48  A    C  
ATOM   2733  N   TRP A 359      29.422 123.239 260.025  1.00 13.96      A    N  
ANISOU 2733  N   TRP A 359     1441   1770   2093   -320   -108     -5  A    N  
ATOM   2734  CA  TRP A 359      29.338 122.671 258.681  1.00 17.45      A    C  
ANISOU 2734  CA  TRP A 359     1929   2181   2518   -342   -103    -41  A    C  
ATOM   2735  C   TRP A 359      28.764 123.644 257.662  1.00 18.23      A    C  
ANISOU 2735  C   TRP A 359     2044   2311   2572   -346   -145    -62  A    C  
ATOM   2736  O   TRP A 359      28.063 124.599 258.015  1.00 24.24      A    O  
ANISOU 2736  O   TRP A 359     2761   3115   3336   -348   -178    -49  A    O  
ATOM   2737  CB  TRP A 359      28.559 121.350 258.674  1.00 17.02      A    C  
ANISOU 2737  CB  TRP A 359     1886   2084   2497   -382   -105    -61  A    C  
ATOM   2738  CG  TRP A 359      27.085 121.503 258.829  1.00 19.88      A    C  
ANISOU 2738  CG  TRP A 359     2196   2462   2894   -422   -156    -60  A    C  
ATOM   2739  CD1 TRP A 359      26.149 121.417 257.843  1.00 20.70      A    C  
ANISOU 2739  CD1 TRP A 359     2309   2552   3004   -465   -231   -100  A    C  
ATOM   2740  CD2 TRP A 359      26.369 121.751 260.047  1.00 18.52      A    C  
ANISOU 2740  CD2 TRP A 359     1955   2313   2767   -412   -132     -7  A    C  
ATOM   2741  CE2 TRP A 359      25.001 121.807 259.719  1.00 20.61      A    C  
ANISOU 2741  CE2 TRP A 359     2163   2574   3094   -454   -179     -3  A    C  
ATOM   2742  CE3 TRP A 359      26.754 121.937 261.376  1.00 21.54      A    C  
ANISOU 2742  CE3 TRP A 359     2331   2715   3139   -362    -79     40  A    C  
ATOM   2743  NE1 TRP A 359      24.892 121.600 258.369  1.00 24.37      A    N  
ANISOU 2743  NE1 TRP A 359     2682   3029   3548   -493   -259    -64  A    N  
ATOM   2744  CZ2 TRP A 359      24.014 122.042 260.677  1.00 21.62      A    C  
ANISOU 2744  CZ2 TRP A 359     2214   2712   3290   -441   -139     64  A    C  
ATOM   2745  CZ3 TRP A 359      25.776 122.171 262.324  1.00 16.92      A    C  
ANISOU 2745  CZ3 TRP A 359     1705   2142   2581   -340    -43     92  A    C  
ATOM   2746  CH2 TRP A 359      24.419 122.217 261.971  1.00 17.18      A    C  
ANISOU 2746  CH2 TRP A 359     1668   2167   2693   -377    -56    111  A    C  
ATOM   2747  N   VAL A 360      29.083 123.404 256.395  1.00 18.54      A    N  
ANISOU 2747  N   VAL A 360     2161   2323   2559   -334   -136    -90  A    N  
ATOM   2748  CA  VAL A 360      28.633 124.275 255.315  1.00 19.91      A    C  
ANISOU 2748  CA  VAL A 360     2374   2524   2666   -320   -175   -102  A    C  
ATOM   2749  C   VAL A 360      28.454 123.476 254.021  1.00 25.78      A    C  
ANISOU 2749  C   VAL A 360     3244   3225   3327   -314   -200   -157  A    C  
ATOM   2750  O   VAL A 360      29.192 122.514 253.763  1.00 19.21      A    O  
ANISOU 2750  O   VAL A 360     2484   2334   2480   -294   -140   -175  A    O  
ATOM   2751  CB  VAL A 360      29.606 125.470 255.116  1.00 16.37      A    C  
ANISOU 2751  CB  VAL A 360     1913   2091   2217   -267   -116    -54  A    C  
ATOM   2752  CG1 VAL A 360      30.943 125.005 254.586  1.00 16.11      A    C  
ANISOU 2752  CG1 VAL A 360     1933   2004   2185   -218    -16    -30  A    C  
ATOM   2753  CG2 VAL A 360      29.000 126.532 254.203  1.00 15.09      A    C  
ANISOU 2753  CG2 VAL A 360     1777   1964   1994   -246   -151    -47  A    C  
ATOM   2754  N   GLY A 361      27.476 123.882 253.212  1.00 27.07      A    N  
ANISOU 2754  N   GLY A 361     3442   3411   3431   -324   -297   -184  A    N  
ATOM   2755  CA  GLY A 361      27.138 123.153 252.003  1.00 22.51      A    C  
ANISOU 2755  CA  GLY A 361     3009   2788   2755   -319   -367   -254  A    C  
ATOM   2756  C   GLY A 361      26.386 121.867 252.290  1.00 22.84      A    C  
ANISOU 2756  C   GLY A 361     3040   2771   2867   -396   -452   -312  A    C  
ATOM   2757  O   GLY A 361      25.693 121.746 253.312  1.00 19.24      A    O  
ANISOU 2757  O   GLY A 361     2444   2328   2539   -456   -478   -285  A    O  
ATOM   2758  N   LEU A 362      26.505 120.902 251.382  1.00 22.56      A    N  
ANISOU 2758  N   LEU A 362     3161   2659   2751   -387   -488   -390  A    N  
ATOM   2759  CA  LEU A 362      25.788 119.643 251.537  1.00 25.15      A    C  
ANISOU 2759  CA  LEU A 362     3487   2906   3164   -467   -583   -454  A    C  
ATOM   2760  C   LEU A 362      26.387 118.780 252.638  1.00 25.22      A    C  
ANISOU 2760  C   LEU A 362     3423   2874   3287   -485   -461   -422  A    C  
ATOM   2761  O   LEU A 362      27.611 118.663 252.748  1.00 19.32      A    O  
ANISOU 2761  O   LEU A 362     2723   2118   2502   -421   -319   -394  A    O  
ATOM   2762  CB  LEU A 362      25.778 118.848 250.233  1.00 29.03      A    C  
ANISOU 2762  CB  LEU A 362     4199   3306   3524   -446   -669   -564  A    C  
ATOM   2763  CG  LEU A 362      24.958 119.418 249.079  1.00 35.15      A    C  
ANISOU 2763  CG  LEU A 362     5076   4101   4177   -435   -849   -616  A    C  
ATOM   2764  CD1 LEU A 362      25.104 118.541 247.838  1.00 35.86      A    C  
ANISOU 2764  CD1 LEU A 362     5437   4087   4102   -395   -929   -738  A    C  
ATOM   2765  CD2 LEU A 362      23.501 119.590 249.472  1.00 38.14      A    C  
ANISOU 2765  CD2 LEU A 362     5279   4499   4713   -541  -1033   -605  A    C  
ATOM   2766  N   THR A 363      25.518 118.187 253.453  1.00 21.70      A    N  
ANISOU 2766  N   THR A 363     2852   2399   2996   -566   -512   -410  A    N  
ATOM   2767  CA  THR A 363      25.927 117.108 254.350  1.00 23.91      A    C  
ANISOU 2767  CA  THR A 363     3091   2615   3379   -582   -415   -386  A    C  
ATOM   2768  C   THR A 363      25.916 115.788 253.571  1.00 28.30      A    C  
ANISOU 2768  C   THR A 363     3784   3040   3930   -609   -465   -484  A    C  
ATOM   2769  O   THR A 363      25.344 115.707 252.483  1.00 28.01      A    O  
ANISOU 2769  O   THR A 363     3856   2960   3827   -631   -610   -574  A    O  
ATOM   2770  CB  THR A 363      24.957 116.976 255.526  1.00 20.99      A    C  
ANISOU 2770  CB  THR A 363     2541   2252   3183   -643   -425   -318  A    C  
ATOM   2771  CG2 THR A 363      24.863 118.295 256.314  1.00 21.91      A    C  
ANISOU 2771  CG2 THR A 363     2550   2484   3290   -608   -379   -233  A    C  
ATOM   2772  OG1 THR A 363      23.660 116.632 255.027  1.00 20.85      A    O  
ANISOU 2772  OG1 THR A 363     2486   2176   3261   -726   -581   -360  A    O  
ATOM   2773  N   GLU A 364      26.532 114.752 254.131  1.00 30.40      A    N  
ANISOU 2773  N   GLU A 364     4369   3014   4167   -986   -612   -385  A    N  
ATOM   2774  CA  GLU A 364      26.512 113.433 253.501  1.00 31.59      A    C  
ANISOU 2774  CA  GLU A 364     4638   3081   4282  -1008   -641   -421  A    C  
ATOM   2775  C   GLU A 364      25.091 112.871 253.382  1.00 29.93      A    C  
ANISOU 2775  C   GLU A 364     4357   2877   4137  -1113   -698   -426  A    C  
ATOM   2776  O   GLU A 364      24.768 112.190 252.409  1.00 32.27      A    O  
ANISOU 2776  O   GLU A 364     4724   3135   4403  -1141   -764   -472  A    O  
ATOM   2777  CB  GLU A 364      27.446 112.448 254.215  1.00 30.73      A    C  
ANISOU 2777  CB  GLU A 364     4629   2885   4160   -976   -566   -409  A    C  
ATOM   2778  CG  GLU A 364      27.719 111.183 253.413  1.00 33.16      A    C  
ANISOU 2778  CG  GLU A 364     5077   3097   4426   -969   -591   -459  A    C  
ATOM   2779  CD  GLU A 364      28.722 110.256 254.080  1.00 39.76      A    C  
ANISOU 2779  CD  GLU A 364     6009   3840   5257   -920   -518   -440  A    C  
ATOM   2780  OE1 GLU A 364      28.804 109.076 253.664  1.00 41.74      A    O  
ANISOU 2780  OE1 GLU A 364     6356   3998   5505   -926   -532   -475  A    O  
ATOM   2781  OE2 GLU A 364      29.456 110.717 254.984  1.00 38.81      A    O1-
ANISOU 2781  OE2 GLU A 364     5871   3740   5138   -872   -451   -393  A    O1-
ATOM   2782  N   LYS A 365      24.259 113.131 254.389  1.00 26.72      A    N  
ANISOU 2782  N   LYS A 365     3814   2519   3820  -1171   -667   -381  A    N  
ATOM   2783  CA  LYS A 365      22.857 112.715 254.346  1.00 34.27      A    C  
ANISOU 2783  CA  LYS A 365     4682   3493   4848  -1270   -713   -379  A    C  
ATOM   2784  C   LYS A 365      22.198 113.269 253.078  1.00 31.47      A    C  
ANISOU 2784  C   LYS A 365     4297   3190   4471  -1278   -816   -413  A    C  
ATOM   2785  O   LYS A 365      21.557 112.539 252.288  1.00 30.69      A    O  
ANISOU 2785  O   LYS A 365     4232   3061   4367  -1336   -890   -449  A    O  
ATOM   2786  CB  LYS A 365      22.111 113.260 255.568  1.00 34.95      A    C  
ANISOU 2786  CB  LYS A 365     4604   3652   5021  -1312   -655   -326  A    C  
ATOM   2787  CG  LYS A 365      22.611 112.770 256.917  1.00 36.58      A    C  
ANISOU 2787  CG  LYS A 365     4825   3828   5247  -1319   -558   -278  A    C  
ATOM   2788  CD  LYS A 365      21.877 113.492 258.048  1.00 38.73      A    C  
ANISOU 2788  CD  LYS A 365     4928   4196   5591  -1355   -499   -234  A    C  
ATOM   2789  CE  LYS A 365      22.356 113.016 259.413  1.00 42.88      A    C  
ANISOU 2789  CE  LYS A 365     5469   4705   6119  -1372   -406   -175  A    C  
ATOM   2790  NZ  LYS A 365      21.579 113.621 260.531  1.00 41.72      A    N1+
ANISOU 2790  NZ  LYS A 365     5157   4663   6033  -1414   -341   -135  A    N1+
ATOM   2791  N   GLU A 366      22.373 114.577 252.898  1.00 25.88      A    N  
ANISOU 2791  N   GLU A 366     3524   2558   3752  -1222   -826   -399  A    N  
ATOM   2792  CA  GLU A 366      21.799 115.278 251.761  1.00 24.98      A    C  
ANISOU 2792  CA  GLU A 366     3372   2501   3619  -1221   -927   -411  A    C  
ATOM   2793  C   GLU A 366      22.392 114.770 250.466  1.00 24.22      A    C  
ANISOU 2793  C   GLU A 366     3437   2356   3410  -1198   -994   -463  A    C  
ATOM   2794  O   GLU A 366      21.670 114.580 249.490  1.00 27.60      A    O  
ANISOU 2794  O   GLU A 366     3870   2801   3815  -1241  -1091   -489  A    O  
ATOM   2795  CB  GLU A 366      22.011 116.797 251.885  1.00 22.36      A    C  
ANISOU 2795  CB  GLU A 366     2945   2245   3307  -1156   -919   -376  A    C  
ATOM   2796  CG  GLU A 366      21.250 117.432 253.039  1.00 35.54      A    C  
ANISOU 2796  CG  GLU A 366     4438   3979   5088  -1174   -860   -339  A    C  
ATOM   2797  CD  GLU A 366      21.739 118.831 253.369  1.00 41.87      A    C  
ANISOU 2797  CD  GLU A 366     5164   4829   5917  -1095   -828   -314  A    C  
ATOM   2798  OE1 GLU A 366      22.800 119.237 252.844  1.00 38.68      A    O  
ANISOU 2798  OE1 GLU A 366     4849   4398   5448  -1030   -841   -318  A    O  
ATOM   2799  OE2 GLU A 366      21.046 119.538 254.130  1.00 46.60      A    O1-
ANISOU 2799  OE2 GLU A 366     5611   5492   6605  -1097   -790   -292  A    O1-
ATOM   2800  N   ALA A 367      23.698 114.514 250.462  1.00 24.80      A    N  
ANISOU 2800  N   ALA A 367     3642   2372   3408  -1129   -940   -481  A    N  
ATOM   2801  CA  ALA A 367      24.343 114.038 249.240  1.00 27.07      A    C  
ANISOU 2801  CA  ALA A 367     4090   2619   3578  -1095   -987   -537  A    C  
ATOM   2802  C   ALA A 367      23.782 112.681 248.822  1.00 31.60      A    C  
ANISOU 2802  C   ALA A 367     4728   3127   4150  -1164  -1028   -590  A    C  
ATOM   2803  O   ALA A 367      23.482 112.466 247.640  1.00 30.82      A    O  
ANISOU 2803  O   ALA A 367     4691   3037   3983  -1183  -1117   -640  A    O  
ATOM   2804  CB  ALA A 367      25.851 113.965 249.414  1.00 27.92      A    C  
ANISOU 2804  CB  ALA A 367     4317   2677   3615  -1002   -905   -547  A    C  
ATOM   2805  N   LYS A 368      23.633 111.770 249.781  1.00 33.52      A    N  
ANISOU 2805  N   LYS A 368     4961   3306   4469  -1205   -968   -580  A    N  
ATOM   2806  CA  LYS A 368      23.050 110.465 249.469  1.00 37.65      A    C  
ANISOU 2806  CA  LYS A 368     5537   3754   5013  -1280  -1008   -627  A    C  
ATOM   2807  C   LYS A 368      21.606 110.594 248.998  1.00 34.94      A    C  
ANISOU 2807  C   LYS A 368     5088   3469   4718  -1375  -1106   -632  A    C  
ATOM   2808  O   LYS A 368      21.226 109.938 248.026  1.00 33.10      A    O  
ANISOU 2808  O   LYS A 368     4921   3208   4447  -1418  -1187   -695  A    O  
ATOM   2809  CB  LYS A 368      23.288 109.389 250.543  1.00 46.30      A    C  
ANISOU 2809  CB  LYS A 368     6661   4752   6178  -1303   -928   -606  A    C  
ATOM   2810  CG  LYS A 368      22.836 109.701 251.949  1.00 54.17      A    C  
ANISOU 2810  CG  LYS A 368     7523   5783   7275  -1340   -861   -526  A    C  
ATOM   2811  CD  LYS A 368      23.648 108.870 252.948  1.00 57.01      A    C  
ANISOU 2811  CD  LYS A 368     7952   6052   7657  -1317   -771   -494  A    C  
ATOM   2812  CE  LYS A 368      23.964 107.486 252.392  1.00 57.46      A    C  
ANISOU 2812  CE  LYS A 368     8152   5982   7699  -1326   -791   -550  A    C  
ATOM   2813  NZ  LYS A 368      24.837 106.676 253.287  1.00 60.07      A    N1+
ANISOU 2813  NZ  LYS A 368     8557   6216   8052  -1290   -710   -513  A    N1+
ATOM   2814  N   GLU A 369      20.790 111.414 249.667  1.00 27.90      A    N  
ANISOU 2814  N   GLU A 369     4031   2659   3910  -1406  -1098   -571  A    N  
ATOM   2815  CA  GLU A 369      19.432 111.586 249.128  1.00 35.28      A    C  
ANISOU 2815  CA  GLU A 369     4860   3656   4889  -1486  -1196   -574  A    C  
ATOM   2816  C   GLU A 369      19.400 112.194 247.713  1.00 40.19      A    C  
ANISOU 2816  C   GLU A 369     5522   4335   5414  -1459  -1306   -606  A    C  
ATOM   2817  O   GLU A 369      18.560 111.803 246.896  1.00 43.96      A    O  
ANISOU 2817  O   GLU A 369     5994   4825   5885  -1526  -1406   -643  A    O  
ATOM   2818  CB  GLU A 369      18.508 112.410 250.039  1.00 37.91      A    C  
ANISOU 2818  CB  GLU A 369     4999   4076   5331  -1515  -1166   -507  A    C  
ATOM   2819  CG  GLU A 369      17.080 112.496 249.461  1.00 43.22      A    C  
ANISOU 2819  CG  GLU A 369     5558   4810   6054  -1596  -1268   -510  A    C  
ATOM   2820  CD  GLU A 369      16.066 113.126 250.386  1.00 52.02      A    C  
ANISOU 2820  CD  GLU A 369     6477   6004   7285  -1630  -1229   -452  A    C  
ATOM   2821  OE1 GLU A 369      16.257 113.039 251.618  1.00 60.67      A    O  
ANISOU 2821  OE1 GLU A 369     7530   7086   8434  -1628  -1119   -418  A    O  
ATOM   2822  OE2 GLU A 369      15.104 113.754 249.873  1.00 49.12      A    O1-
ANISOU 2822  OE2 GLU A 369     5995   5717   6950  -1651  -1309   -438  A    O1-
ATOM   2823  N   LYS A 370      20.335 113.093 247.399  1.00 31.38      A    N  
ANISOU 2823  N   LYS A 370     4453   3252   4220  -1366  -1292   -592  A    N  
ATOM   2824  CA  LYS A 370      20.341 113.724 246.081  1.00 28.91      A    C  
ANISOU 2824  CA  LYS A 370     4179   2999   3806  -1339  -1396   -608  A    C  
ATOM   2825  C   LYS A 370      20.742 112.737 244.995  1.00 33.85      A    C  
ANISOU 2825  C   LYS A 370     4977   3570   4314  -1345  -1445   -696  A    C  
ATOM   2826  O   LYS A 370      20.402 112.917 243.827  1.00 36.85      A    O  
ANISOU 2826  O   LYS A 370     5388   4000   4611  -1357  -1551   -724  A    O  
ATOM   2827  CB  LYS A 370      21.342 114.888 246.060  1.00 27.39      A    C  
ANISOU 2827  CB  LYS A 370     4004   2845   3559  -1240  -1361   -567  A    C  
ATOM   2828  CG  LYS A 370      21.010 115.998 245.059  1.00 30.01      A    C  
ANISOU 2828  CG  LYS A 370     4292   3270   3840  -1220  -1468   -533  A    C  
ATOM   2829  CD  LYS A 370      22.064 117.111 245.099  1.00 30.92      A    C  
ANISOU 2829  CD  LYS A 370     4426   3409   3911  -1127  -1431   -488  A    C  
ATOM   2830  CE  LYS A 370      21.632 118.315 244.274  1.00 35.89      A    C  
ANISOU 2830  CE  LYS A 370     4984   4132   4522  -1109  -1538   -429  A    C  
ATOM   2831  NZ  LYS A 370      22.740 119.311 244.118  1.00 40.44      A    N1+
ANISOU 2831  NZ  LYS A 370     5603   4723   5039  -1025  -1517   -388  A    N1+
ATOM   2832  N   GLY A 371      21.449 111.685 245.386  1.00 38.43      A    N  
ANISOU 2832  N   GLY A 371     5666   4047   4887  -1333  -1368   -740  A    N  
ATOM   2833  CA  GLY A 371      21.828 110.625 244.468  1.00 42.91      A    C  
ANISOU 2833  CA  GLY A 371     6394   4548   5362  -1335  -1399   -835  A    C  
ATOM   2834  C   GLY A 371      22.946 110.935 243.488  1.00 45.17      A    C  
ANISOU 2834  C   GLY A 371     6823   4852   5489  -1240  -1397   -875  A    C  
ATOM   2835  O   GLY A 371      23.100 110.232 242.487  1.00 48.11      A    O  
ANISOU 2835  O   GLY A 371     7317   5200   5764  -1241  -1441   -962  A    O  
ATOM   2836  N   ILE A 372      23.754 111.945 243.796  1.00 44.72      A    N  
ANISOU 2836  N   ILE A 372     6754   4836   5403  -1157  -1339   -817  A    N  
ATOM   2837  CA  ILE A 372      24.902 112.305 242.966  1.00 43.75      A    C  
ANISOU 2837  CA  ILE A 372     6761   4734   5127  -1061  -1319   -844  A    C  
ATOM   2838  C   ILE A 372      26.097 111.468 243.393  1.00 43.77      A    C  
ANISOU 2838  C   ILE A 372     6880   4638   5112   -991  -1201   -885  A    C  
ATOM   2839  O   ILE A 372      26.206 111.091 244.556  1.00 44.23      A    O  
ANISOU 2839  O   ILE A 372     6893   4633   5280   -998  -1126   -853  A    O  
ATOM   2840  CB  ILE A 372      25.260 113.816 243.020  1.00 66.60      A    C  
ANISOU 2840  CB  ILE A 372     9591   7716   7997  -1006  -1317   -762  A    C  
ATOM   2841  CG1 ILE A 372      25.784 114.231 244.400  1.00 60.76      A    C  
ANISOU 2841  CG1 ILE A 372     8779   6945   7363   -971  -1211   -701  A    C  
ATOM   2842  CG2 ILE A 372      24.091 114.671 242.535  1.00 69.62      A    C  
ANISOU 2842  CG2 ILE A 372     9853   8197   8403  -1064  -1441   -713  A    C  
ATOM   2843  CD1 ILE A 372      27.262 114.593 244.392  1.00 53.30      A    C  
ANISOU 2843  CD1 ILE A 372     7935   5987   6330   -862  -1122   -700  A    C  
ATOM   2844  N   SER A 373      26.997 111.172 242.464  1.00 48.21      A    N  
ANISOU 2844  N   SER A 373     7590   5193   5536   -918  -1180   -950  A    N  
ATOM   2845  CA  SER A 373      28.195 110.437 242.829  1.00 44.95      A    C  
ANISOU 2845  CA  SER A 373     7278   4692   5110   -834  -1064   -984  A    C  
ATOM   2846  C   SER A 373      29.096 111.357 243.629  1.00 36.92      A    C  
ANISOU 2846  C   SER A 373     6222   3697   4109   -756   -973   -906  A    C  
ATOM   2847  O   SER A 373      29.616 112.337 243.095  1.00 40.71      A    O  
ANISOU 2847  O   SER A 373     6722   4254   4492   -697   -971   -883  A    O  
ATOM   2848  CB  SER A 373      28.945 109.994 241.574  1.00 45.09      A    C  
ANISOU 2848  CB  SER A 373     7451   4714   4969   -764  -1054  -1076  A    C  
ATOM   2849  OG  SER A 373      28.257 108.966 240.891  1.00 55.01      A    O  
ANISOU 2849  OG  SER A 373     8759   5930   6213   -832  -1126  -1168  A    O  
ATOM   2850  N   TYR A 374      29.256 111.046 244.918  1.00 29.59      A    N  
ANISOU 2850  N   TYR A 374     5237   2705   3302   -759   -901   -863  A    N  
ATOM   2851  CA  TYR A 374      30.045 111.877 245.826  1.00 25.96      A    C  
ANISOU 2851  CA  TYR A 374     4727   2262   2874   -694   -817   -792  A    C  
ATOM   2852  C   TYR A 374      31.080 111.010 246.540  1.00 32.07      A    C  
ANISOU 2852  C   TYR A 374     5563   2945   3676   -623   -707   -798  A    C  
ATOM   2853  O   TYR A 374      30.947 109.783 246.609  1.00 25.46      A    O  
ANISOU 2853  O   TYR A 374     4777   2022   2875   -646   -703   -840  A    O  
ATOM   2854  CB  TYR A 374      29.154 112.518 246.893  1.00 25.57      A    C  
ANISOU 2854  CB  TYR A 374     4515   2247   2955   -769   -837   -716  A    C  
ATOM   2855  CG  TYR A 374      28.667 111.544 247.952  1.00 29.46      A    C  
ANISOU 2855  CG  TYR A 374     4961   2667   3566   -829   -806   -702  A    C  
ATOM   2856  CD1 TYR A 374      29.342 111.413 249.164  1.00 27.66      A    C  
ANISOU 2856  CD1 TYR A 374     4712   2399   3397   -790   -710   -655  A    C  
ATOM   2857  CD2 TYR A 374      27.538 110.759 247.746  1.00 30.16      A    C  
ANISOU 2857  CD2 TYR A 374     5026   2729   3703   -927   -875   -731  A    C  
ATOM   2858  CE1 TYR A 374      28.909 110.530 250.136  1.00 28.52      A    C  
ANISOU 2858  CE1 TYR A 374     4787   2446   3604   -847   -685   -631  A    C  
ATOM   2859  CE2 TYR A 374      27.097 109.870 248.719  1.00 31.95      A    C  
ANISOU 2859  CE2 TYR A 374     5214   2887   4037   -985   -845   -710  A    C  
ATOM   2860  CZ  TYR A 374      27.790 109.766 249.912  1.00 28.95      A    C  
ANISOU 2860  CZ  TYR A 374     4821   2471   3707   -945   -750   -657  A    C  
ATOM   2861  OH  TYR A 374      27.371 108.891 250.887  1.00 34.87      A    O  
ANISOU 2861  OH  TYR A 374     5540   3155   4555  -1005   -721   -625  A    O  
ATOM   2862  N   GLU A 375      32.109 111.655 247.076  1.00 31.93      A    N  
ANISOU 2862  N   GLU A 375     5538   2943   3649   -538   -623   -754  A    N  
ATOM   2863  CA  GLU A 375      33.102 110.979 247.903  1.00 30.60      A    C  
ANISOU 2863  CA  GLU A 375     5404   2701   3520   -465   -521   -739  A    C  
ATOM   2864  C   GLU A 375      33.494 111.869 249.069  1.00 28.94      A    C  
ANISOU 2864  C   GLU A 375     5100   2524   3373   -442   -464   -659  A    C  
ATOM   2865  O   GLU A 375      33.689 113.074 248.885  1.00 25.15      A    O  
ANISOU 2865  O   GLU A 375     4582   2116   2859   -419   -467   -635  A    O  
ATOM   2866  CB  GLU A 375      34.317 110.600 247.058  1.00 34.21      A    C  
ANISOU 2866  CB  GLU A 375     5986   3141   3870   -347   -458   -793  A    C  
ATOM   2867  CG  GLU A 375      35.433 109.874 247.799  1.00 38.12      A    C  
ANISOU 2867  CG  GLU A 375     6514   3564   4407   -256   -355   -777  A    C  
ATOM   2868  CD  GLU A 375      36.562 109.476 246.859  1.00 41.31      A    C  
ANISOU 2868  CD  GLU A 375     7026   3960   4710   -136   -291   -835  A    C  
ATOM   2869  OE1 GLU A 375      37.709 109.308 247.324  1.00 36.21      A    O  
ANISOU 2869  OE1 GLU A 375     6388   3292   4078    -33   -197   -808  A    O  
ATOM   2870  OE2 GLU A 375      36.298 109.346 245.643  1.00 46.79      A    O1-
ANISOU 2870  OE2 GLU A 375     7791   4680   5309   -145   -335   -907  A    O1-
ATOM   2871  N   THR A 376      33.587 111.292 250.267  1.00 23.35      A    N  
ANISOU 2871  N   THR A 376     4355   1761   2754   -453   -418   -618  A    N  
ATOM   2872  CA  THR A 376      34.019 112.059 251.426  1.00 23.88      A    C  
ANISOU 2872  CA  THR A 376     4340   1861   2873   -430   -361   -548  A    C  
ATOM   2873  C   THR A 376      35.506 111.862 251.656  1.00 21.54      A    C  
ANISOU 2873  C   THR A 376     4106   1534   2544   -303   -266   -537  A    C  
ATOM   2874  O   THR A 376      36.078 110.846 251.267  1.00 23.39      A    O  
ANISOU 2874  O   THR A 376     4432   1705   2752   -246   -238   -572  A    O  
ATOM   2875  CB  THR A 376      33.268 111.659 252.715  1.00 26.52      A    C  
ANISOU 2875  CB  THR A 376     4592   2172   3313   -516   -362   -496  A    C  
ATOM   2876  CG2 THR A 376      31.765 111.795 252.526  1.00 25.34      A    C  
ANISOU 2876  CG2 THR A 376     4362   2058   3209   -636   -446   -502  A    C  
ATOM   2877  OG1 THR A 376      33.582 110.302 253.049  1.00 30.08      A    O  
ANISOU 2877  OG1 THR A 376     5116   2525   3788   -502   -332   -497  A    O  
ATOM   2878  N   ALA A 377      36.122 112.836 252.310  1.00 22.92      A    N  
ANISOU 2878  N   ALA A 377     4169   1801   2739   -247   -208   -472  A    N  
ATOM   2879  CA  ALA A 377      37.519 112.733 252.704  1.00 24.88      A    C  
ANISOU 2879  CA  ALA A 377     4428   2049   2976   -129   -118   -441  A    C  
ATOM   2880  C   ALA A 377      37.647 113.347 254.084  1.00 26.18      A    C  
ANISOU 2880  C   ALA A 377     4461   2277   3210   -136    -84   -365  A    C  
ATOM   2881  O   ALA A 377      37.271 114.511 254.297  1.00 21.79      A    O  
ANISOU 2881  O   ALA A 377     3788   1816   2676   -166    -97   -339  A    O  
ATOM   2882  CB  ALA A 377      38.413 113.459 251.712  1.00 19.21      A    C  
ANISOU 2882  CB  ALA A 377     3716   1402   2181    -34    -79   -451  A    C  
ATOM   2883  N   THR A 378      38.171 112.575 255.030  1.00 24.98      A    N  
ANISOU 2883  N   THR A 378     4329   2072   3091   -108    -43   -329  A    N  
ATOM   2884  CA  THR A 378      38.275 113.073 256.401  1.00 26.34      A    C  
ANISOU 2884  CA  THR A 378     4385   2311   3311   -119    -16   -260  A    C  
ATOM   2885  C   THR A 378      39.709 113.076 256.924  1.00 26.04      A    C  
ANISOU 2885  C   THR A 378     4331   2297   3265     -6     51   -216  A    C  
ATOM   2886  O   THR A 378      40.526 112.244 256.540  1.00 28.48      A    O  
ANISOU 2886  O   THR A 378     4732   2533   3554     75     81   -225  A    O  
ATOM   2887  CB  THR A 378      37.367 112.287 257.372  1.00 26.64      A    C  
ANISOU 2887  CB  THR A 378     4425   2296   3399   -215    -39   -230  A    C  
ATOM   2888  CG2 THR A 378      35.939 112.246 256.856  1.00 25.14      A    C  
ANISOU 2888  CG2 THR A 378     4238   2085   3228   -333   -109   -271  A    C  
ATOM   2889  OG1 THR A 378      37.847 110.945 257.490  1.00 36.95      A    O  
ANISOU 2889  OG1 THR A 378     5846   3481   4711   -181    -23   -220  A    O  
ATOM   2890  N   PHE A 379      40.008 114.043 257.784  1.00 25.00      A    N  
ANISOU 2890  N   PHE A 379     4077   2268   3153      2     71   -174  A    N  
ATOM   2891  CA  PHE A 379      41.272 114.080 258.496  1.00 22.49      A    C  
ANISOU 2891  CA  PHE A 379     3722   1986   2836     91    120   -124  A    C  
ATOM   2892  C   PHE A 379      40.985 114.089 259.991  1.00 21.48      A    C  
ANISOU 2892  C   PHE A 379     3525   1902   2735     41    117    -72  A    C  
ATOM   2893  O   PHE A 379      40.366 115.032 260.507  1.00 23.01      A    O  
ANISOU 2893  O   PHE A 379     3621   2178   2943    -20    103    -77  A    O  
ATOM   2894  CB  PHE A 379      42.085 115.315 258.104  1.00 17.40      A    C  
ANISOU 2894  CB  PHE A 379     2993   1436   2183    149    145   -125  A    C  
ATOM   2895  CG  PHE A 379      43.463 115.337 258.695  1.00 23.05      A    C  
ANISOU 2895  CG  PHE A 379     3664   2190   2903    242    189    -77  A    C  
ATOM   2896  CD1 PHE A 379      43.722 116.019 259.871  1.00 22.82      A    C  
ANISOU 2896  CD1 PHE A 379     3526   2246   2897    228    188    -41  A    C  
ATOM   2897  CD2 PHE A 379      44.503 114.671 258.070  1.00 19.44      A    C  
ANISOU 2897  CD2 PHE A 379     3272   1687   2427    346    231    -73  A    C  
ATOM   2898  CE1 PHE A 379      44.997 116.031 260.414  1.00 21.73      A    C  
ANISOU 2898  CE1 PHE A 379     3342   2151   2765    309    216      4  A    C  
ATOM   2899  CE2 PHE A 379      45.782 114.678 258.610  1.00 20.35      A    C  
ANISOU 2899  CE2 PHE A 379     3333   1843   2555    435    269    -23  A    C  
ATOM   2900  CZ  PHE A 379      46.027 115.360 259.784  1.00 19.53      A    C  
ANISOU 2900  CZ  PHE A 379     3116   1827   2476    412    255     18  A    C  
ATOM   2901  N   PRO A 380      41.433 113.036 260.690  1.00 19.62      A    N  
ANISOU 2901  N   PRO A 380     3340   1611   2502     72    131    -21  A    N  
ATOM   2902  CA  PRO A 380      41.244 112.893 262.136  1.00 16.94      A    C  
ANISOU 2902  CA  PRO A 380     2950   1318   2169     31    132     43  A    C  
ATOM   2903  C   PRO A 380      42.258 113.754 262.891  1.00 21.66      A    C  
ANISOU 2903  C   PRO A 380     3445   2032   2753     91    151     73  A    C  
ATOM   2904  O   PRO A 380      43.432 113.787 262.510  1.00 23.63      A    O  
ANISOU 2904  O   PRO A 380     3695   2283   2999    189    172     81  A    O  
ATOM   2905  CB  PRO A 380      41.511 111.401 262.371  1.00 19.47      A    C  
ANISOU 2905  CB  PRO A 380     3379   1520   2501     59    137     95  A    C  
ATOM   2906  CG  PRO A 380      42.503 111.032 261.313  1.00 21.43      A    C  
ANISOU 2906  CG  PRO A 380     3697   1698   2746    171    158     65  A    C  
ATOM   2907  CD  PRO A 380      42.173 111.899 260.108  1.00 19.32      A    C  
ANISOU 2907  CD  PRO A 380     3418   1462   2462    156    151    -19  A    C  
ATOM   2908  N   TRP A 381      41.816 114.457 263.931  1.00 17.46      A    N  
ANISOU 2908  N   TRP A 381     2822   1601   2213     32    144     83  A    N  
ATOM   2909  CA  TRP A 381      42.710 115.364 264.646  1.00 19.57      A    C  
ANISOU 2909  CA  TRP A 381     2989   1981   2466     75    151     94  A    C  
ATOM   2910  C   TRP A 381      43.725 114.617 265.519  1.00 20.37      A    C  
ANISOU 2910  C   TRP A 381     3103   2093   2544    140    157    174  A    C  
ATOM   2911  O   TRP A 381      44.707 115.208 265.981  1.00 16.54      A    O  
ANISOU 2911  O   TRP A 381     2544   1693   2049    192    155    188  A    O  
ATOM   2912  CB  TRP A 381      41.909 116.388 265.467  1.00 19.99      A    C  
ANISOU 2912  CB  TRP A 381     2944   2137   2513     -5    143     61  A    C  
ATOM   2913  CG  TRP A 381      41.233 117.440 264.622  1.00 22.96      A    C  
ANISOU 2913  CG  TRP A 381     3275   2521   2926    -41    134    -14  A    C  
ATOM   2914  CD1 TRP A 381      40.932 117.357 263.289  1.00 24.70      A    C  
ANISOU 2914  CD1 TRP A 381     3549   2665   3169    -37    126    -44  A    C  
ATOM   2915  CD2 TRP A 381      40.774 118.729 265.054  1.00 18.69      A    C  
ANISOU 2915  CD2 TRP A 381     2630   2067   2405    -82    130    -65  A    C  
ATOM   2916  CE2 TRP A 381      40.215 119.376 263.930  1.00 19.41      A    C  
ANISOU 2916  CE2 TRP A 381     2712   2123   2540    -98    117   -112  A    C  
ATOM   2917  CE3 TRP A 381      40.787 119.403 266.282  1.00 15.05      A    C  
ANISOU 2917  CE3 TRP A 381     2085   1707   1925   -104    134    -80  A    C  
ATOM   2918  NE1 TRP A 381      40.322 118.516 262.866  1.00 20.08      A    N  
ANISOU 2918  NE1 TRP A 381     2896   2118   2618    -73    112    -96  A    N  
ATOM   2919  CZ2 TRP A 381      39.668 120.663 263.998  1.00 16.20      A    C  
ANISOU 2919  CZ2 TRP A 381     2212   1768   2176   -131    108   -166  A    C  
ATOM   2920  CZ3 TRP A 381      40.241 120.684 266.347  1.00 17.49      A    C  
ANISOU 2920  CZ3 TRP A 381     2305   2066   2273   -137    130   -150  A    C  
ATOM   2921  CH2 TRP A 381      39.689 121.296 265.212  1.00 17.26      A    C  
ANISOU 2921  CH2 TRP A 381     2266   1989   2304   -148    118   -188  A    C  
ATOM   2922  N   ALA A 382      43.523 113.312 265.699  1.00 22.70      A    N  
ANISOU 2922  N   ALA A 382     3491   2296   2837    139    157    231  A    N  
ATOM   2923  CA  ALA A 382      44.520 112.491 266.378  1.00 23.30      A    C  
ANISOU 2923  CA  ALA A 382     3590   2362   2902    216    158    320  A    C  
ATOM   2924  C   ALA A 382      45.827 112.508 265.593  1.00 22.99      A    C  
ANISOU 2924  C   ALA A 382     3549   2298   2887    338    174    313  A    C  
ATOM   2925  O   ALA A 382      46.897 112.260 266.147  1.00 28.69      A    O  
ANISOU 2925  O   ALA A 382     4242   3054   3606    417    171    378  A    O  
ATOM   2926  CB  ALA A 382      44.023 111.059 266.529  1.00 25.14      A    C  
ANISOU 2926  CB  ALA A 382     3934   2469   3149    194    156    382  A    C  
ATOM   2927  N   ALA A 383      45.737 112.822 264.305  1.00 19.21      A    N  
ANISOU 2927  N   ALA A 383     3097   1773   2430    352    191    240  A    N  
ATOM   2928  CA  ALA A 383      46.913 112.900 263.447  1.00 22.71      A    C  
ANISOU 2928  CA  ALA A 383     3535   2204   2890    464    221    228  A    C  
ATOM   2929  C   ALA A 383      47.418 114.334 263.298  1.00 24.10      A    C  
ANISOU 2929  C   ALA A 383     3591   2499   3068    468    225    196  A    C  
ATOM   2930  O   ALA A 383      48.371 114.587 262.560  1.00 29.83      A    O  
ANISOU 2930  O   ALA A 383     4292   3233   3808    549    256    189  A    O  
ATOM   2931  CB  ALA A 383      46.594 112.312 262.076  1.00 18.28      A    C  
ANISOU 2931  CB  ALA A 383     3086   1524   2338    484    243    171  A    C  
ATOM   2932  N   SER A 384      46.783 115.270 263.997  1.00 23.25      A    N  
ANISOU 2932  N   SER A 384     3406   2477   2949    380    198    175  A    N  
ATOM   2933  CA  SER A 384      47.167 116.679 263.897  1.00 21.69      A    C  
ANISOU 2933  CA  SER A 384     3098   2376   2768    372    196    138  A    C  
ATOM   2934  C   SER A 384      48.140 117.084 264.990  1.00 21.18      A    C  
ANISOU 2934  C   SER A 384     2934   2412   2699    400    177    179  A    C  
ATOM   2935  O   SER A 384      47.807 117.035 266.177  1.00 21.93      A    O  
ANISOU 2935  O   SER A 384     3008   2563   2761    354    148    197  A    O  
ATOM   2936  CB  SER A 384      45.933 117.573 263.981  1.00 21.22      A    C  
ANISOU 2936  CB  SER A 384     3005   2345   2711    268    176     78  A    C  
ATOM   2937  OG  SER A 384      46.320 118.921 264.190  1.00 22.62      A    O  
ANISOU 2937  OG  SER A 384     3071   2610   2914    256    167     49  A    O  
ATOM   2938  N   GLY A 385      49.335 117.501 264.583  1.00 23.54      A    N  
ANISOU 2938  N   GLY A 385     3171   2745   3029    472    192    192  A    N  
ATOM   2939  CA  GLY A 385      50.330 117.997 265.518  1.00 22.93      A    C  
ANISOU 2939  CA  GLY A 385     2985   2770   2956    494    164    224  A    C  
ATOM   2940  C   GLY A 385      49.815 119.125 266.393  1.00 21.34      A    C  
ANISOU 2940  C   GLY A 385     2705   2658   2745    402    124    173  A    C  
ATOM   2941  O   GLY A 385      50.082 119.162 267.594  1.00 25.55      A    O  
ANISOU 2941  O   GLY A 385     3193   3273   3244    388     85    194  A    O  
ATOM   2942  N  AARG A 386      49.099 120.070 265.786  0.50 19.91      A    N  
ANISOU 2942  N  AARG A 386     2507   2464   2593    344    132    105  A    N  
ATOM   2943  N  BARG A 386      49.064 120.046 265.795  0.15 20.22      A    N  
ANISOU 2943  N  BARG A 386     2550   2502   2631    343    132    104  A    N  
ATOM   2944  N  CARG A 386      49.055 120.036 265.790  0.35 19.77      A    N  
ANISOU 2944  N  CARG A 386     2493   2444   2574    343    133    104  A    N  
ATOM   2945  CA AARG A 386      48.548 121.196 266.534  0.50 20.15      A    C  
ANISOU 2945  CA AARG A 386     2466   2563   2628    264    102     41  A    C  
ATOM   2946  CA BARG A 386      48.540 121.187 266.535  0.15 20.04      A    C  
ANISOU 2946  CA BARG A 386     2452   2549   2613    264    102     41  A    C  
ATOM   2947  CA CARG A 386      48.528 121.192 266.505  0.35 20.12      A    C  
ANISOU 2947  CA CARG A 386     2463   2556   2624    264    102     40  A    C  
ATOM   2948  C  AARG A 386      47.493 120.761 267.552  0.50 20.25      A    C  
ANISOU 2948  C  AARG A 386     2517   2598   2578    204     88     30  A    C  
ATOM   2949  C  BARG A 386      47.495 120.756 267.552  0.15 20.21      A    C  
ANISOU 2949  C  BARG A 386     2513   2594   2574    204     88     30  A    C  
ATOM   2950  C  CARG A 386      47.475 120.786 267.530  0.35 20.21      A    C  
ANISOU 2950  C  CARG A 386     2512   2592   2575    202     88     28  A    C  
ATOM   2951  O  AARG A 386      47.499 121.219 268.700  0.50 20.52      A    O  
ANISOU 2951  O  AARG A 386     2496   2722   2578    168     59      7  A    O  
ATOM   2952  O  BARG A 386      47.517 121.197 268.702  0.15 20.50      A    O  
ANISOU 2952  O  BARG A 386     2495   2721   2576    169     59      8  A    O  
ATOM   2953  O  CARG A 386      47.474 121.272 268.665  0.35 20.38      A    O  
ANISOU 2953  O  CARG A 386     2477   2704   2564    166     59      3  A    O  
ATOM   2954  CB AARG A 386      47.961 122.262 265.602  0.50 19.76      A    C  
ANISOU 2954  CB AARG A 386     2392   2479   2637    223    114    -20  A    C  
ATOM   2955  CB BARG A 386      47.932 122.219 265.586  0.15 19.92      A    C  
ANISOU 2955  CB BARG A 386     2416   2497   2655    224    114    -19  A    C  
ATOM   2956  CB CARG A 386      47.932 122.193 265.513  0.35 18.77      A    C  
ANISOU 2956  CB CARG A 386     2274   2346   2510    226    116    -18  A    C  
ATOM   2957  CG AARG A 386      47.494 123.493 266.367  0.50 21.80      A    C  
ANISOU 2957  CG AARG A 386     2568   2796   2917    153     84    -94  A    C  
ATOM   2958  CG BARG A 386      47.511 123.499 266.284  0.15 21.23      A    C  
ANISOU 2958  CG BARG A 386     2497   2719   2848    155     85    -92  A    C  
ATOM   2959  CG CARG A 386      47.309 123.420 266.160  0.35 20.87      A    C  
ANISOU 2959  CG CARG A 386     2467   2662   2802    152     90    -94  A    C  
ATOM   2960  CD AARG A 386      48.692 124.265 266.910  0.50 22.47      A    C  
ANISOU 2960  CD AARG A 386     2552   2953   3034    166     55    -98  A    C  
ATOM   2961  CD BARG A 386      48.726 124.235 266.831  0.15 22.88      A    C  
ANISOU 2961  CD BARG A 386     2606   3001   3087    170     57    -94  A    C  
ATOM   2962  CD CARG A 386      48.313 124.198 267.002  0.35 22.22      A    C  
ANISOU 2962  CD CARG A 386     2537   2917   2991    152     56   -109  A    C  
ATOM   2963  NE AARG A 386      48.317 125.494 267.610  0.50 24.94      A    N  
ANISOU 2963  NE AARG A 386     2790   3310   3376    102     24   -185  A    N  
ATOM   2964  NE BARG A 386      48.350 125.402 267.622  0.15 23.88      A    N  
ANISOU 2964  NE BARG A 386     2660   3177   3237    105     25   -179  A    N  
ATOM   2965  NE CARG A 386      48.039 125.633 266.954  0.35 25.08      A    N  
ANISOU 2965  NE CARG A 386     2822   3283   3423    101     40   -185  A    N  
ATOM   2966  CZ AARG A 386      47.953 126.639 267.032  0.50 24.03      A    C  
ANISOU 2966  CZ AARG A 386     2632   3156   3344     68     25   -238  A    C  
ATOM   2967  CZ BARG A 386      47.950 126.558 267.102  0.15 23.50      A    C  
ANISOU 2967  CZ BARG A 386     2568   3092   3269     69     25   -236  A    C  
ATOM   2968  CZ CARG A 386      48.296 126.488 267.941  0.35 24.82      A    C  
ANISOU 2968  CZ CARG A 386     2712   3318   3402     65      2   -246  A    C  
ATOM   2969  NH1AARG A 386      47.882 126.755 265.710  0.50 20.84      A    N1+
ANISOU 2969  NH1AARG A 386     2251   2678   2991     88     54   -206  A    N1+
ATOM   2970  NH1BARG A 386      47.861 126.705 265.785  0.15 22.59      A    N1+
ANISOU 2970  NH1BARG A 386     2475   2903   3207     87     53   -207  A    N1+
ATOM   2971  NH1CARG A 386      48.830 126.059 269.080  0.35 13.75      A    N1+
ANISOU 2971  NH1CARG A 386     1295   2001   1929     71    -28   -235  A    N1+
ATOM   2972  NH2AARG A 386      47.644 127.681 267.793  0.50 22.97      A    N  
ANISOU 2972  NH2AARG A 386     2435   3055   3239     17     -3   -325  A    N  
ATOM   2973  NH2BARG A 386      47.629 127.568 267.898  0.15 23.68      A    N  
ANISOU 2973  NH2BARG A 386     2529   3151   3316     17     -3   -323  A    N  
ATOM   2974  NH2CARG A 386      48.008 127.776 267.792  0.35 22.84      A    N  
ANISOU 2974  NH2CARG A 386     2401   3046   3233     23     -9   -318  A    N  
ATOM   2975  N   ALA A 387      46.581 119.900 267.122  1.00 13.51      A    N  
ANISOU 2975  N   ALA A 387     1759   1667   1709    187    109     44  A    N  
ATOM   2976  CA  ALA A 387      45.504 119.440 267.983  1.00 13.71      A    C  
ANISOU 2976  CA  ALA A 387     1819   1709   1683    123    106     45  A    C  
ATOM   2977  C   ALA A 387      46.050 118.675 269.176  1.00 15.58      A    C  
ANISOU 2977  C   ALA A 387     2063   2003   1853    144     89    117  A    C  
ATOM   2978  O   ALA A 387      45.561 118.827 270.302  1.00 20.50      A    O  
ANISOU 2978  O   ALA A 387     2661   2709   2418     92     79    109  A    O  
ATOM   2979  CB  ALA A 387      44.543 118.575 267.203  1.00 17.73      A    C  
ANISOU 2979  CB  ALA A 387     2425   2112   2200    100    127     56  A    C  
ATOM   2980  N   ILE A 388      47.069 117.857 268.937  1.00 17.32      A    N  
ANISOU 2980  N   ILE A 388     2315   2186   2079    227     88    190  A    N  
ATOM   2981  CA  ILE A 388      47.688 117.124 270.032  1.00 25.41      A    C  
ANISOU 2981  CA  ILE A 388     3343   3265   3047    259     62    275  A    C  
ATOM   2982  C   ILE A 388      48.436 118.084 270.945  1.00 26.30      A    C  
ANISOU 2982  C   ILE A 388     3347   3515   3131    255     21    252  A    C  
ATOM   2983  O   ILE A 388      48.237 118.062 272.155  1.00 23.27      A    O  
ANISOU 2983  O   ILE A 388     2947   3225   2668    217     -4    268  A    O  
ATOM   2984  CB  ILE A 388      48.617 116.005 269.527  1.00 28.46      A    C  
ANISOU 2984  CB  ILE A 388     3784   3569   3461    360     70    361  A    C  
ATOM   2985  CG1 ILE A 388      47.791 114.932 268.823  1.00 31.23      A    C  
ANISOU 2985  CG1 ILE A 388     4256   3779   3830    352    102    378  A    C  
ATOM   2986  CG2 ILE A 388      49.379 115.373 270.683  1.00 28.53      A    C  
ANISOU 2986  CG2 ILE A 388     3777   3643   3419    403     33    459  A    C  
ATOM   2987  CD1 ILE A 388      48.618 113.947 268.074  1.00 39.53      A    C  
ANISOU 2987  CD1 ILE A 388     5369   4726   4924    458    121    429  A    C  
ATOM   2988  N   ALA A 389      49.255 118.959 270.363  1.00 23.19      A    N  
ANISOU 2988  N   ALA A 389     2879   3136   2798    287     14    210  A    N  
ATOM   2989  CA  ALA A 389      49.997 119.938 271.156  1.00 22.24      A    C  
ANISOU 2989  CA  ALA A 389     2650   3135   2666    274    -34    176  A    C  
ATOM   2990  C   ALA A 389      49.076 120.912 271.896  1.00 19.91      A    C  
ANISOU 2990  C   ALA A 389     2320   2911   2334    182    -45     79  A    C  
ATOM   2991  O   ALA A 389      49.467 121.482 272.917  1.00 22.07      A    O  
ANISOU 2991  O   ALA A 389     2528   3296   2560    158    -90     48  A    O  
ATOM   2992  CB  ALA A 389      50.989 120.707 270.284  1.00 19.54      A    C  
ANISOU 2992  CB  ALA A 389     2229   2780   2414    315    -33    155  A    C  
ATOM   2993  N   SER A 390      47.864 121.120 271.388  1.00 20.84      A    N  
ANISOU 2993  N   SER A 390     2478   2968   2474    131     -5     24  A    N  
ATOM   2994  CA  SER A 390      46.928 122.022 272.068  1.00 27.00      A    C  
ANISOU 2994  CA  SER A 390     3222   3809   3227     54     -6    -72  A    C  
ATOM   2995  C   SER A 390      45.924 121.261 272.922  1.00 26.67      A    C  
ANISOU 2995  C   SER A 390     3237   3804   3093     10     15    -44  A    C  
ATOM   2996  O   SER A 390      44.964 121.852 273.420  1.00 25.51      A    O  
ANISOU 2996  O   SER A 390     3068   3703   2922    -51     32   -121  A    O  
ATOM   2997  CB  SER A 390      46.160 122.891 271.064  1.00 18.95      A    C  
ANISOU 2997  CB  SER A 390     2188   2715   2299     23     22   -151  A    C  
ATOM   2998  OG  SER A 390      47.036 123.750 270.361  1.00 22.59      A    O  
ANISOU 2998  OG  SER A 390     2586   3152   2844     51      6   -176  A    O  
ATOM   2999  N   ASP A 391      46.150 119.960 273.091  1.00 28.88      A    N  
ANISOU 2999  N   ASP A 391     3587   4060   3328     43     16     68  A    N  
ATOM   3000  CA  ASP A 391      45.272 119.127 273.908  1.00 22.45      A    C  
ANISOU 3000  CA  ASP A 391     2828   3274   2427     -2     37    121  A    C  
ATOM   3001  C   ASP A 391      43.815 119.157 273.435  1.00 24.03      A    C  
ANISOU 3001  C   ASP A 391     3057   3413   2660    -67     86     76  A    C  
ATOM   3002  O   ASP A 391      42.893 119.268 274.244  1.00 21.69      A    O  
ANISOU 3002  O   ASP A 391     2749   3189   2302   -130    110     53  A    O  
ATOM   3003  CB  ASP A 391      45.351 119.560 275.372  1.00 26.68      A    C  
ANISOU 3003  CB  ASP A 391     3316   3971   2851    -34     13     99  A    C  
ATOM   3004  CG  ASP A 391      45.065 118.428 276.332  1.00 32.93      A    C  
ANISOU 3004  CG  ASP A 391     4166   4812   3534    -50     20    212  A    C  
ATOM   3005  OD1 ASP A 391      44.959 117.272 275.875  1.00 35.84      A    O  
ANISOU 3005  OD1 ASP A 391     4612   5076   3931    -29     35    315  A    O  
ATOM   3006  OD2 ASP A 391      44.942 118.700 277.543  1.00 38.51      A    O1-
ANISOU 3006  OD2 ASP A 391     4846   5660   4125    -85     10    198  A    O1-
ATOM   3007  N   CYS A 392      43.603 119.043 272.127  1.00 26.68      A    N  
ANISOU 3007  N   CYS A 392     3426   3625   3087    -52    100     65  A    N  
ATOM   3008  CA  CYS A 392      42.243 118.995 271.594  1.00 27.32      A    C  
ANISOU 3008  CA  CYS A 392     3531   3644   3205   -113    133     31  A    C  
ATOM   3009  C   CYS A 392      42.151 118.001 270.443  1.00 28.72      A    C  
ANISOU 3009  C   CYS A 392     3798   3680   3436    -91    139     84  A    C  
ATOM   3010  O   CYS A 392      41.580 118.308 269.395  1.00 25.94      A    O  
ANISOU 3010  O   CYS A 392     3452   3256   3147   -107    145     35  A    O  
ATOM   3011  CB  CYS A 392      41.765 120.390 271.152  1.00 31.78      A    C  
ANISOU 3011  CB  CYS A 392     4020   4222   3833   -138    137    -85  A    C  
ATOM   3012  SG  CYS A 392      42.795 121.227 269.905  1.00 28.75      A    S  
ANISOU 3012  SG  CYS A 392     3605   3777   3542    -74    113   -122  A    S  
ATOM   3013  N   ALA A 393      42.694 116.803 270.666  1.00 30.30      A    N  
ANISOU 3013  N   ALA A 393     4068   3839   3606    -54    134    183  A    N  
ATOM   3014  CA  ALA A 393      42.868 115.810 269.610  1.00 27.68      A    C  
ANISOU 3014  CA  ALA A 393     3828   3367   3324    -13    137    225  A    C  
ATOM   3015  C   ALA A 393      41.584 115.109 269.182  1.00 28.72      A    C  
ANISOU 3015  C   ALA A 393     4026   3406   3479    -86    152    229  A    C  
ATOM   3016  O   ALA A 393      41.558 114.413 268.164  1.00 31.72      A    O  
ANISOU 3016  O   ALA A 393     4485   3663   3904    -66    151    234  A    O  
ATOM   3017  CB  ALA A 393      43.897 114.776 270.037  1.00 24.19      A    C  
ANISOU 3017  CB  ALA A 393     3435   2902   2857     59    125    329  A    C  
ATOM   3018  N   ASP A 394      40.523 115.287 269.953  1.00 29.05      A    N  
ANISOU 3018  N   ASP A 394     4033   3513   3491   -173    167    223  A    N  
ATOM   3019  CA  ASP A 394      39.237 114.711 269.593  1.00 32.19      A    C  
ANISOU 3019  CA  ASP A 394     4472   3837   3921   -255    179    226  A    C  
ATOM   3020  C   ASP A 394      38.513 115.670 268.661  1.00 35.24      A    C  
ANISOU 3020  C   ASP A 394     4810   4214   4364   -285    174    125  A    C  
ATOM   3021  O   ASP A 394      37.787 116.574 269.093  1.00 36.34      A    O  
ANISOU 3021  O   ASP A 394     4864   4441   4502   -333    188     70  A    O  
ATOM   3022  CB  ASP A 394      38.444 114.359 270.845  1.00 34.04      A    C  
ANISOU 3022  CB  ASP A 394     4687   4149   4099   -333    206    283  A    C  
ATOM   3023  CG  ASP A 394      39.170 113.334 271.701  1.00 47.07      A    C  
ANISOU 3023  CG  ASP A 394     6393   5799   5692   -302    203    404  A    C  
ATOM   3024  OD1 ASP A 394      39.515 112.267 271.143  1.00 51.06      A    O  
ANISOU 3024  OD1 ASP A 394     6992   6170   6239   -270    189    464  A    O  
ATOM   3025  OD2 ASP A 394      39.455 113.603 272.888  1.00 48.33      A    O1-
ANISOU 3025  OD2 ASP A 394     6508   6089   5767   -301    211    437  A    O1-
ATOM   3026  N   GLY A 395      38.757 115.476 267.371  1.00 26.03      A    N  
ANISOU 3026  N   GLY A 395     3700   2943   3246   -249    155    101  A    N  
ATOM   3027  CA  GLY A 395      38.152 116.302 266.354  1.00 24.17      A    C  
ANISOU 3027  CA  GLY A 395     3431   2691   3061   -269    141     21  A    C  
ATOM   3028  C   GLY A 395      38.309 115.652 265.000  1.00 25.30      A    C  
ANISOU 3028  C   GLY A 395     3670   2710   3233   -241    120     14  A    C  
ATOM   3029  O   GLY A 395      39.041 114.668 264.846  1.00 26.73      A    O  
ANISOU 3029  O   GLY A 395     3938   2818   3402   -190    123     59  A    O  
ATOM   3030  N   MET A 396      37.636 116.216 264.008  1.00 16.42      A    N  
ANISOU 3030  N   MET A 396     2530   1565   2144   -269     98    -45  A    N  
ATOM   3031  CA  MET A 396      37.701 115.686 262.660  1.00 18.24      A    C  
ANISOU 3031  CA  MET A 396     2853   1693   2385   -248     74    -66  A    C  
ATOM   3032  C   MET A 396      37.358 116.800 261.697  1.00 16.32      A    C  
ANISOU 3032  C   MET A 396     2558   1476   2165   -251     51   -124  A    C  
ATOM   3033  O   MET A 396      36.491 117.628 261.991  1.00 18.46      A    O  
ANISOU 3033  O   MET A 396     2740   1807   2468   -305     42   -148  A    O  
ATOM   3034  CB  MET A 396      36.718 114.521 262.507  1.00 17.89      A    C  
ANISOU 3034  CB  MET A 396     2884   1556   2355   -328     53    -52  A    C  
ATOM   3035  CG  MET A 396      36.591 113.996 261.082  1.00 30.66      A    C  
ANISOU 3035  CG  MET A 396     4601   3070   3977   -322     18    -94  A    C  
ATOM   3036  SD  MET A 396      35.598 112.495 260.948  1.00 71.74      A    S  
ANISOU 3036  SD  MET A 396     9906   8143   9208   -418    -16    -82  A    S  
ATOM   3037  CE  MET A 396      33.974 113.114 261.366  1.00 34.49      A    C  
ANISOU 3037  CE  MET A 396     5071   3499   4534   -548    -40    -89  A    C  
ATOM   3038  N   THR A 397      38.034 116.816 260.553  1.00 23.60      A    N  
ANISOU 3038  N   THR A 397     3537   2356   3072   -188     45   -141  A    N  
ATOM   3039  CA  THR A 397      37.711 117.739 259.472  1.00 21.13      A    C  
ANISOU 3039  CA  THR A 397     3197   2060   2773   -190     18   -180  A    C  
ATOM   3040  C   THR A 397      37.230 116.911 258.306  1.00 23.34      A    C  
ANISOU 3040  C   THR A 397     3584   2254   3030   -211    -18   -205  A    C  
ATOM   3041  O   THR A 397      37.871 115.926 257.931  1.00 21.74      A    O  
ANISOU 3041  O   THR A 397     3487   1981   2793   -165     -4   -203  A    O  
ATOM   3042  CB  THR A 397      38.940 118.545 259.037  1.00 19.51      A    C  
ANISOU 3042  CB  THR A 397     2964   1892   2557   -101     45   -175  A    C  
ATOM   3043  CG2 THR A 397      38.618 119.410 257.809  1.00 19.60      A    C  
ANISOU 3043  CG2 THR A 397     2960   1912   2574   -103     16   -198  A    C  
ATOM   3044  OG1 THR A 397      39.343 119.407 260.108  1.00 19.38      A    O  
ANISOU 3044  OG1 THR A 397     2842   1954   2567    -92     66   -165  A    O  
ATOM   3045  N   LYS A 398      36.088 117.287 257.744  1.00 21.40      A    N  
ANISOU 3045  N   LYS A 398     3312   2013   2807   -280    -69   -233  A    N  
ATOM   3046  CA  LYS A 398      35.475 116.474 256.700  1.00 18.54      A    C  
ANISOU 3046  CA  LYS A 398     3050   1575   2420   -320   -119   -265  A    C  
ATOM   3047  C   LYS A 398      35.126 117.315 255.482  1.00 22.52      A    C  
ANISOU 3047  C   LYS A 398     3538   2110   2909   -319   -166   -291  A    C  
ATOM   3048  O   LYS A 398      34.521 118.379 255.609  1.00 23.60      A    O  
ANISOU 3048  O   LYS A 398     3566   2309   3092   -347   -187   -284  A    O  
ATOM   3049  CB  LYS A 398      34.226 115.781 257.252  1.00 16.53      A    C  
ANISOU 3049  CB  LYS A 398     2786   1286   2207   -429   -153   -264  A    C  
ATOM   3050  CG  LYS A 398      33.417 114.986 256.230  1.00 16.03      A    C  
ANISOU 3050  CG  LYS A 398     2813   1145   2133   -493   -222   -305  A    C  
ATOM   3051  CD  LYS A 398      32.359 114.144 256.927  1.00 21.26      A    C  
ANISOU 3051  CD  LYS A 398     3467   1762   2849   -603   -244   -290  A    C  
ATOM   3052  CE  LYS A 398      31.221 113.777 256.002  1.00 23.96      A    C  
ANISOU 3052  CE  LYS A 398     3839   2061   3205   -696   -333   -333  A    C  
ATOM   3053  NZ  LYS A 398      30.137 113.049 256.726  1.00 24.63      A    N1+
ANISOU 3053  NZ  LYS A 398     3891   2111   3357   -816   -351   -309  A    N1+
ATOM   3054  N   LEU A 399      35.532 116.839 254.308  1.00 22.43      A    N  
ANISOU 3054  N   LEU A 399     3637   2055   2829   -282   -180   -319  A    N  
ATOM   3055  CA  LEU A 399      35.157 117.468 253.048  1.00 20.78      A    C  
ANISOU 3055  CA  LEU A 399     3436   1876   2584   -286   -232   -337  A    C  
ATOM   3056  C   LEU A 399      34.350 116.503 252.196  1.00 25.58      A    C  
ANISOU 3056  C   LEU A 399     4148   2419   3151   -349   -304   -389  A    C  
ATOM   3057  O   LEU A 399      34.594 115.296 252.207  1.00 24.18      A    O  
ANISOU 3057  O   LEU A 399     4082   2157   2950   -348   -293   -420  A    O  
ATOM   3058  CB  LEU A 399      36.392 117.955 252.275  1.00 18.12      A    C  
ANISOU 3058  CB  LEU A 399     3130   1573   2182   -185   -184   -324  A    C  
ATOM   3059  CG  LEU A 399      37.200 119.099 252.893  1.00 20.68      A    C  
ANISOU 3059  CG  LEU A 399     3341   1964   2550   -130   -128   -273  A    C  
ATOM   3060  CD1 LEU A 399      38.406 119.458 252.020  1.00 20.37      A    C  
ANISOU 3060  CD1 LEU A 399     3336   1955   2448    -39    -79   -254  A    C  
ATOM   3061  CD2 LEU A 399      36.299 120.311 253.074  1.00 16.98      A    C  
ANISOU 3061  CD2 LEU A 399     2750   1548   2153   -182   -173   -254  A    C  
ATOM   3062  N   ILE A 400      33.381 117.038 251.462  1.00 23.61      A    N  
ANISOU 3062  N   ILE A 400     3865   2205   2900   -406   -384   -398  A    N  
ATOM   3063  CA  ILE A 400      32.571 116.223 250.565  1.00 26.35      A    C  
ANISOU 3063  CA  ILE A 400     4305   2503   3204   -474   -469   -453  A    C  
ATOM   3064  C   ILE A 400      32.749 116.723 249.134  1.00 26.27      A    C  
ANISOU 3064  C   ILE A 400     4348   2541   3094   -436   -510   -467  A    C  
ATOM   3065  O   ILE A 400      32.594 117.911 248.866  1.00 24.86      A    O  
ANISOU 3065  O   ILE A 400     4076   2442   2928   -422   -528   -420  A    O  
ATOM   3066  CB  ILE A 400      31.083 116.230 250.954  1.00 25.56      A    C  
ANISOU 3066  CB  ILE A 400     4117   2406   3188   -593   -548   -450  A    C  
ATOM   3067  CG1 ILE A 400      30.906 115.783 252.408  1.00 28.38      A    C  
ANISOU 3067  CG1 ILE A 400     4417   2733   3633   -632   -496   -424  A    C  
ATOM   3068  CG2 ILE A 400      30.290 115.315 250.024  1.00 24.57      A    C  
ANISOU 3068  CG2 ILE A 400     4090   2224   3021   -674   -646   -513  A    C  
ATOM   3069  CD1 ILE A 400      29.472 115.830 252.895  1.00 31.11      A    C  
ANISOU 3069  CD1 ILE A 400     4655   3095   4068   -747   -552   -413  A    C  
ATOM   3070  N   PHE A 401      33.108 115.816 248.231  1.00 25.29      A    N  
ANISOU 3070  N   PHE A 401     4375   2366   2869   -415   -521   -531  A    N  
ATOM   3071  CA  PHE A 401      33.401 116.168 246.847  1.00 25.61      A    C  
ANISOU 3071  CA  PHE A 401     4485   2460   2785   -371   -546   -549  A    C  
ATOM   3072  C   PHE A 401      32.440 115.501 245.879  1.00 31.93      A    C  
ANISOU 3072  C   PHE A 401     5377   3235   3519   -453   -663   -622  A    C  
ATOM   3073  O   PHE A 401      31.982 114.385 246.128  1.00 31.26      A    O  
ANISOU 3073  O   PHE A 401     5360   3055   3461   -517   -696   -685  A    O  
ATOM   3074  CB  PHE A 401      34.823 115.725 246.485  1.00 21.23      A    C  
ANISOU 3074  CB  PHE A 401     4038   1887   2141   -257   -445   -573  A    C  
ATOM   3075  CG  PHE A 401      35.896 116.452 247.240  1.00 22.28      A    C  
ANISOU 3075  CG  PHE A 401     4081   2060   2324   -172   -339   -500  A    C  
ATOM   3076  CD1 PHE A 401      36.472 115.888 248.364  1.00 18.39      A    C  
ANISOU 3076  CD1 PHE A 401     3578   1509   1902   -143   -269   -493  A    C  
ATOM   3077  CD2 PHE A 401      36.332 117.701 246.815  1.00 21.69      A    C  
ANISOU 3077  CD2 PHE A 401     3932   2082   2227   -125   -315   -433  A    C  
ATOM   3078  CE1 PHE A 401      37.462 116.558 249.058  1.00 23.02      A    C  
ANISOU 3078  CE1 PHE A 401     4078   2139   2531    -71   -184   -430  A    C  
ATOM   3079  CE2 PHE A 401      37.312 118.380 247.508  1.00 24.38      A    C  
ANISOU 3079  CE2 PHE A 401     4186   2455   2623    -58   -226   -370  A    C  
ATOM   3080  CZ  PHE A 401      37.884 117.807 248.628  1.00 25.44      A    C  
ANISOU 3080  CZ  PHE A 401     4308   2538   2821    -31   -163   -373  A    C  
ATOM   3081  N   ASP A 402      32.131 116.188 244.781  1.00 30.61      A    N  
ANISOU 3081  N   ASP A 402     5213   3153   3266   -455   -729   -611  A    N  
ATOM   3082  CA  ASP A 402      31.457 115.552 243.651  1.00 29.16      A    C  
ANISOU 3082  CA  ASP A 402     5142   2961   2977   -515   -839   -691  A    C  
ATOM   3083  C   ASP A 402      32.452 114.611 242.993  1.00 32.66      A    C  
ANISOU 3083  C   ASP A 402     5763   3354   3291   -441   -777   -779  A    C  
ATOM   3084  O   ASP A 402      33.538 115.032 242.606  1.00 29.90      A    O  
ANISOU 3084  O   ASP A 402     5441   3058   2861   -333   -685   -753  A    O  
ATOM   3085  CB  ASP A 402      30.991 116.594 242.632  1.00 33.62      A    C  
ANISOU 3085  CB  ASP A 402     5664   3644   3468   -522   -923   -640  A    C  
ATOM   3086  CG  ASP A 402      30.221 115.975 241.471  1.00 37.03      A    C  
ANISOU 3086  CG  ASP A 402     6205   4083   3780   -593  -1055   -724  A    C  
ATOM   3087  OD1 ASP A 402      28.975 115.949 241.506  1.00 35.93      A    O  
ANISOU 3087  OD1 ASP A 402     5992   3949   3711   -696  -1171   -722  A    O  
ATOM   3088  OD2 ASP A 402      30.872 115.510 240.514  1.00 43.63      A    O1-
ANISOU 3088  OD2 ASP A 402     7191   4929   4456   -540  -1034   -790  A    O1-
ATOM   3089  N   LYS A 403      32.104 113.337 242.878  1.00 39.20      A    N  
ANISOU 3089  N   LYS A 403     6653   4106   4137   -479   -795   -856  A    N  
ATOM   3090  CA  LYS A 403      33.090 112.353 242.446  1.00 43.24      A    C  
ANISOU 3090  CA  LYS A 403     7287   4566   4576   -392   -707   -926  A    C  
ATOM   3091  C   LYS A 403      33.607 112.557 241.021  1.00 42.88      A    C  
ANISOU 3091  C   LYS A 403     7347   4603   4345   -326   -704   -971  A    C  
ATOM   3092  O   LYS A 403      34.771 112.280 240.725  1.00 47.29      A    O  
ANISOU 3092  O   LYS A 403     7981   5156   4829   -216   -596   -998  A    O  
ATOM   3093  CB  LYS A 403      32.539 110.936 242.555  1.00 50.61      A    C  
ANISOU 3093  CB  LYS A 403     8248   5401   5579   -450   -733   -994  A    C  
ATOM   3094  CG  LYS A 403      33.621 109.895 242.365  1.00 55.59      A    C  
ANISOU 3094  CG  LYS A 403     8986   5959   6176   -353   -636  -1059  A    C  
ATOM   3095  CD  LYS A 403      33.072 108.497 242.406  1.00 60.81      A    C  
ANISOU 3095  CD  LYS A 403     9685   6513   6907   -413   -670  -1131  A    C  
ATOM   3096  CE  LYS A 403      34.192 107.486 242.361  1.00 65.28      A    C  
ANISOU 3096  CE  LYS A 403    10345   6995   7464   -311   -571  -1188  A    C  
ATOM   3097  NZ  LYS A 403      33.661 106.120 242.157  1.00 71.04      A    N1+
ANISOU 3097  NZ  LYS A 403    11131   7617   8245   -369   -615  -1276  A    N1+
ATOM   3098  N   GLU A 404      32.751 113.074 240.150  1.00 41.37      A    N  
ANISOU 3098  N   GLU A 404     7146   4497   4078   -389   -817   -969  A    N  
ATOM   3099  CA  GLU A 404      33.093 113.195 238.742  1.00 45.26      A    C  
ANISOU 3099  CA  GLU A 404     7734   5081   4381   -340   -824  -1008  A    C  
ATOM   3100  C   GLU A 404      33.838 114.479 238.431  1.00 42.21      A    C  
ANISOU 3100  C   GLU A 404     7345   4804   3888   -263   -777   -923  A    C  
ATOM   3101  O   GLU A 404      34.847 114.461 237.725  1.00 43.58      A    O  
ANISOU 3101  O   GLU A 404     7598   5030   3931   -164   -683   -939  A    O  
ATOM   3102  CB  GLU A 404      31.815 113.165 237.909  1.00 51.99      A    C  
ANISOU 3102  CB  GLU A 404     8573   5988   5193   -443   -975  -1034  A    C  
ATOM   3103  CG  GLU A 404      31.114 111.822 237.883  1.00 65.62      A    C  
ANISOU 3103  CG  GLU A 404    10325   7621   6985   -515  -1023  -1134  A    C  
ATOM   3104  CD  GLU A 404      29.889 111.833 236.989  1.00 78.61      A    C  
ANISOU 3104  CD  GLU A 404    11954   9334   8581   -612  -1173  -1163  A    C  
ATOM   3105  OE1 GLU A 404      29.499 112.930 236.527  1.00 83.02      A    O  
ANISOU 3105  OE1 GLU A 404    12462  10007   9075   -628  -1247  -1088  A    O  
ATOM   3106  OE2 GLU A 404      29.306 110.750 236.761  1.00 82.44      A    O1-
ANISOU 3106  OE2 GLU A 404    12471   9756   9096   -674  -1221  -1255  A    O1-
ATOM   3107  N   SER A 405      33.303 115.594 238.912  1.00 37.08      A    N  
ANISOU 3107  N   SER A 405     6577   4201   3310   -309   -836   -819  A    N  
ATOM   3108  CA  SER A 405      33.872 116.905 238.638  1.00 31.89      A    C  
ANISOU 3108  CA  SER A 405     5832   3663   2623   -241   -779   -689  A    C  
ATOM   3109  C   SER A 405      35.038 117.210 239.563  1.00 30.94      A    C  
ANISOU 3109  C   SER A 405     5640   3516   2598   -150   -623   -629  A    C  
ATOM   3110  O   SER A 405      35.863 118.072 239.258  1.00 32.88      A    O  
ANISOU 3110  O   SER A 405     5846   3846   2802    -74   -542   -541  A    O  
ATOM   3111  CB  SER A 405      32.802 117.979 238.807  1.00 35.50      A    C  
ANISOU 3111  CB  SER A 405     6137   4176   3175   -316   -890   -585  A    C  
ATOM   3112  OG  SER A 405      32.453 118.123 240.174  1.00 37.09      A    O  
ANISOU 3112  OG  SER A 405     6206   4307   3581   -353   -875   -551  A    O  
ATOM   3113  N   HIS A 406      35.084 116.497 240.690  1.00 33.23      A    N  
ANISOU 3113  N   HIS A 406     5913   3694   3020   -163   -587   -670  A    N  
ATOM   3114  CA  HIS A 406      36.028 116.742 241.791  1.00 33.65      A    C  
ANISOU 3114  CA  HIS A 406     5880   3717   3189    -95   -462   -611  A    C  
ATOM   3115  C   HIS A 406      35.769 118.046 242.554  1.00 26.32      A    C  
ANISOU 3115  C   HIS A 406     4769   2837   2395   -117   -468   -490  A    C  
ATOM   3116  O   HIS A 406      36.596 118.446 243.371  1.00 24.80      A    O  
ANISOU 3116  O   HIS A 406     4497   2641   2284    -61   -372   -435  A    O  
ATOM   3117  CB  HIS A 406      37.491 116.735 241.322  1.00 35.96      A    C  
ANISOU 3117  CB  HIS A 406     6231   4049   3383     31   -326   -605  A    C  
ATOM   3118  CG  HIS A 406      37.927 115.421 240.731  1.00 41.67      A    C  
ANISOU 3118  CG  HIS A 406     7131   4710   3993     78   -292   -735  A    C  
ATOM   3119  CD2 HIS A 406      39.107 115.085 240.142  1.00 44.64      A    C  
ANISOU 3119  CD2 HIS A 406     7593   5110   4259    193   -176   -769  A    C  
ATOM   3120  ND1 HIS A 406      37.135 114.317 240.708  1.00 40.94      A    N  
ANISOU 3120  ND1 HIS A 406     7137   4516   3900      8   -376   -847  A    N  
ATOM   3121  CE1 HIS A 406      37.798 113.316 240.119  1.00 45.43      A    C  
ANISOU 3121  CE1 HIS A 406     7822   5050   4390     77   -312   -938  A    C  
ATOM   3122  NE2 HIS A 406      38.978 113.759 239.777  1.00 48.35      A    N  
ANISOU 3122  NE2 HIS A 406     8207   5489   4675    193   -193   -905  A    N  
ATOM   3123  N   ARG A 407      34.646 118.716 242.303  1.00 23.30      A    N  
ANISOU 3123  N   ARG A 407     4316   2498   2039   -195   -582   -450  A    N  
ATOM   3124  CA  ARG A 407      34.353 119.945 243.052  1.00 28.13      A    C  
ANISOU 3124  CA  ARG A 407     4755   3142   2792   -210   -586   -347  A    C  
ATOM   3125  C   ARG A 407      33.940 119.694 244.488  1.00 23.71      A    C  
ANISOU 3125  C   ARG A 407     4107   2510   2393   -255   -577   -360  A    C  
ATOM   3126  O   ARG A 407      33.215 118.738 244.782  1.00 21.88      A    O  
ANISOU 3126  O   ARG A 407     3915   2213   2184   -324   -629   -429  A    O  
ATOM   3127  CB  ARG A 407      33.264 120.774 242.397  1.00 38.19      A    C  
ANISOU 3127  CB  ARG A 407     5967   4481   4063   -269   -709   -293  A    C  
ATOM   3128  CG  ARG A 407      33.667 121.396 241.107  1.00 56.67      A    C  
ANISOU 3128  CG  ARG A 407     8356   6914   6260   -222   -716   -237  A    C  
ATOM   3129  CD  ARG A 407      32.619 122.379 240.681  1.00 72.73      A    C  
ANISOU 3129  CD  ARG A 407    10297   9007   8331   -272   -836   -156  A    C  
ATOM   3130  NE  ARG A 407      31.372 121.673 240.433  1.00 87.63      A    N  
ANISOU 3130  NE  ARG A 407    12215  10877  10202   -365   -971   -227  A    N  
ATOM   3131  CZ  ARG A 407      31.091 121.071 239.290  1.00 97.02      A    C  
ANISOU 3131  CZ  ARG A 407    13533  12106  11225   -389  -1050   -284  A    C  
ATOM   3132  NH1 ARG A 407      32.014 121.039 238.338  1.00 99.20      A    N1+
ANISOU 3132  NH1 ARG A 407    13923  12441  11327   -320   -991   -282  A    N1+
ATOM   3133  NH2 ARG A 407      29.929 120.450 239.132  1.00 99.74      A    N  
ANISOU 3133  NH2 ARG A 407    13892  12431  11574   -485  -1182   -350  A    N  
ATOM   3134  N   VAL A 408      34.403 120.562 245.380  1.00 18.71      A    N  
ANISOU 3134  N   VAL A 408     3352   1891   1868   -221   -510   -292  A    N  
ATOM   3135  CA  VAL A 408      33.974 120.514 246.766  1.00 17.81      A    C  
ANISOU 3135  CA  VAL A 408     3140   1731   1895   -263   -499   -295  A    C  
ATOM   3136  C   VAL A 408      32.526 121.018 246.826  1.00 24.77      A    C  
ANISOU 3136  C   VAL A 408     3924   2631   2856   -348   -607   -278  A    C  
ATOM   3137  O   VAL A 408      32.190 122.058 246.252  1.00 24.23      A    O  
ANISOU 3137  O   VAL A 408     3791   2620   2797   -344   -655   -219  A    O  
ATOM   3138  CB  VAL A 408      34.945 121.300 247.692  1.00 21.43      A    C  
ANISOU 3138  CB  VAL A 408     3504   2205   2435   -200   -399   -240  A    C  
ATOM   3139  CG1 VAL A 408      34.985 122.786 247.335  1.00 21.54      A    C  
ANISOU 3139  CG1 VAL A 408     3417   2281   2487   -178   -410   -158  A    C  
ATOM   3140  CG2 VAL A 408      34.581 121.101 249.158  1.00 18.01      A    C  
ANISOU 3140  CG2 VAL A 408     2989   1733   2120   -238   -381   -255  A    C  
ATOM   3141  N   ILE A 409      31.659 120.244 247.472  1.00 24.68      A    N  
ANISOU 3141  N   ILE A 409     3903   2571   2905   -426   -646   -326  A    N  
ATOM   3142  CA  ILE A 409      30.237 120.566 247.546  1.00 23.71      A    C  
ANISOU 3142  CA  ILE A 409     3681   2467   2862   -511   -746   -316  A    C  
ATOM   3143  C   ILE A 409      29.766 120.700 248.992  1.00 22.69      A    C  
ANISOU 3143  C   ILE A 409     3428   2320   2873   -546   -709   -308  A    C  
ATOM   3144  O   ILE A 409      28.640 121.141 249.249  1.00 23.97      A    O  
ANISOU 3144  O   ILE A 409     3475   2507   3126   -604   -769   -292  A    O  
ATOM   3145  CB  ILE A 409      29.371 119.498 246.839  1.00 22.16      A    C  
ANISOU 3145  CB  ILE A 409     3575   2239   2604   -596   -849   -380  A    C  
ATOM   3146  CG1 ILE A 409      29.617 118.123 247.467  1.00 25.43      A    C  
ANISOU 3146  CG1 ILE A 409     4082   2562   3019   -624   -804   -447  A    C  
ATOM   3147  CG2 ILE A 409      29.667 119.462 245.347  1.00 22.29      A    C  
ANISOU 3147  CG2 ILE A 409     3710   2292   2467   -567   -901   -394  A    C  
ATOM   3148  CD1 ILE A 409      28.780 116.998 246.861  1.00 23.88      A    C  
ANISOU 3148  CD1 ILE A 409     3979   2314   2782   -719   -906   -520  A    C  
ATOM   3149  N   GLY A 410      30.624 120.311 249.931  1.00 20.49      A    N  
ANISOU 3149  N   GLY A 410     3169   2008   2608   -509   -608   -318  A    N  
ATOM   3150  CA  GLY A 410      30.283 120.382 251.340  1.00 21.84      A    C  
ANISOU 3150  CA  GLY A 410     3237   2175   2888   -538   -563   -312  A    C  
ATOM   3151  C   GLY A 410      31.480 120.153 252.245  1.00 23.46      A    C  
ANISOU 3151  C   GLY A 410     3467   2361   3085   -476   -455   -308  A    C  
ATOM   3152  O   GLY A 410      32.500 119.592 251.826  1.00 23.58      A    O  
ANISOU 3152  O   GLY A 410     3595   2347   3018   -421   -416   -320  A    O  
ATOM   3153  N   GLY A 411      31.368 120.606 253.488  1.00 21.89      A    N  
ANISOU 3153  N   GLY A 411     3161   2186   2969   -481   -406   -294  A    N  
ATOM   3154  CA  GLY A 411      32.433 120.405 254.451  1.00 14.34      A    C  
ANISOU 3154  CA  GLY A 411     2218   1224   2007   -430   -317   -287  A    C  
ATOM   3155  C   GLY A 411      31.930 120.503 255.873  1.00 15.64      A    C  
ANISOU 3155  C   GLY A 411     2283   1414   2245   -470   -281   -285  A    C  
ATOM   3156  O   GLY A 411      30.870 121.101 256.126  1.00 17.64      A    O  
ANISOU 3156  O   GLY A 411     2430   1703   2571   -517   -311   -287  A    O  
ATOM   3157  N   ALA A 412      32.685 119.917 256.799  1.00 15.59      A    N  
ANISOU 3157  N   ALA A 412     2309   1395   2217   -447   -216   -278  A    N  
ATOM   3158  CA  ALA A 412      32.327 119.940 258.218  1.00 17.75      A    C  
ANISOU 3158  CA  ALA A 412     2502   1707   2536   -481   -174   -272  A    C  
ATOM   3159  C   ALA A 412      33.556 119.788 259.120  1.00 21.25      A    C  
ANISOU 3159  C   ALA A 412     2966   2164   2945   -420   -105   -255  A    C  
ATOM   3160  O   ALA A 412      34.557 119.181 258.734  1.00 21.35      A    O  
ANISOU 3160  O   ALA A 412     3074   2135   2904   -366    -89   -243  A    O  
ATOM   3161  CB  ALA A 412      31.304 118.864 258.529  1.00 14.40      A    C  
ANISOU 3161  CB  ALA A 412     2098   1248   2124   -574   -194   -269  A    C  
ATOM   3162  N   ILE A 413      33.485 120.381 260.305  1.00 18.33      A    N  
ANISOU 3162  N   ILE A 413     2500   1859   2605   -424    -65   -257  A    N  
ATOM   3163  CA  ILE A 413      34.524 120.237 261.308  1.00 17.37      A    C  
ANISOU 3163  CA  ILE A 413     2386   1767   2448   -379    -11   -239  A    C  
ATOM   3164  C   ILE A 413      33.862 119.985 262.662  1.00 20.27      A    C  
ANISOU 3164  C   ILE A 413     2698   2186   2819   -435     22   -233  A    C  
ATOM   3165  O   ILE A 413      32.893 120.657 263.025  1.00 16.40      A    O  
ANISOU 3165  O   ILE A 413     2110   1745   2376   -477     23   -261  A    O  
ATOM   3166  CB  ILE A 413      35.414 121.505 261.419  1.00 25.03      A    C  
ANISOU 3166  CB  ILE A 413     3288   2786   3436   -312      7   -256  A    C  
ATOM   3167  CG1 ILE A 413      35.957 121.944 260.051  1.00 19.51      A    C  
ANISOU 3167  CG1 ILE A 413     2624   2051   2739   -264    -19   -252  A    C  
ATOM   3168  CG2 ILE A 413      36.551 121.285 262.412  1.00 12.06      A    C  
ANISOU 3168  CG2 ILE A 413     1653   1178   1751   -268     49   -237  A    C  
ATOM   3169  CD1 ILE A 413      35.100 122.994 259.367  1.00 24.02      A    C  
ANISOU 3169  CD1 ILE A 413     3125   2629   3372   -285    -60   -271  A    C  
ATOM   3170  N   VAL A 414      34.373 119.012 263.407  1.00 18.00      A    N  
ANISOU 3170  N   VAL A 414     2469   1890   2481   -433     51   -191  A    N  
ATOM   3171  CA  VAL A 414      34.070 118.941 264.830  1.00 19.01      A    C  
ANISOU 3171  CA  VAL A 414     2541   2093   2588   -468     94   -175  A    C  
ATOM   3172  C   VAL A 414      35.404 119.112 265.544  1.00 20.75      A    C  
ANISOU 3172  C   VAL A 414     2769   2358   2757   -397    120   -160  A    C  
ATOM   3173  O   VAL A 414      36.373 118.428 265.223  1.00 20.87      A    O  
ANISOU 3173  O   VAL A 414     2867   2320   2742   -346    115   -123  A    O  
ATOM   3174  CB  VAL A 414      33.348 117.623 265.236  1.00 18.43      A    C  
ANISOU 3174  CB  VAL A 414     2520   1982   2501   -544    101   -121  A    C  
ATOM   3175  CG1 VAL A 414      34.063 116.390 264.683  1.00 14.74      A    C  
ANISOU 3175  CG1 VAL A 414     2187   1405   2007   -518     83    -75  A    C  
ATOM   3176  CG2 VAL A 414      33.207 117.528 266.746  1.00 21.13      A    C  
ANISOU 3176  CG2 VAL A 414     2812   2416   2799   -572    155    -89  A    C  
ATOM   3177  N   GLY A 415      35.477 120.067 266.469  1.00 14.20      A    N  
ANISOU 3177  N   GLY A 415     1848   1625   1921   -389    145   -196  A    N  
ATOM   3178  CA  GLY A 415      36.728 120.314 267.163  1.00 16.23      A    C  
ANISOU 3178  CA  GLY A 415     2101   1935   2131   -329    157   -189  A    C  
ATOM   3179  C   GLY A 415      36.813 121.701 267.779  1.00 20.50      A    C  
ANISOU 3179  C   GLY A 415     2537   2562   2689   -317    167   -262  A    C  
ATOM   3180  O   GLY A 415      35.998 122.584 267.478  1.00 17.41      A    O  
ANISOU 3180  O   GLY A 415     2079   2175   2362   -338    164   -321  A    O  
ATOM   3181  N   THR A 416      37.797 121.882 268.658  1.00 16.97      A    N  
ANISOU 3181  N   THR A 416     2077   2183   2189   -282    173   -261  A    N  
ATOM   3182  CA  THR A 416      38.075 123.190 269.248  1.00 21.13      A    C  
ANISOU 3182  CA  THR A 416     2514   2782   2731   -268    174   -341  A    C  
ATOM   3183  C   THR A 416      38.403 124.159 268.128  1.00 17.41      A    C  
ANISOU 3183  C   THR A 416     2015   2248   2353   -234    147   -378  A    C  
ATOM   3184  O   THR A 416      39.116 123.796 267.185  1.00 13.85      A    O  
ANISOU 3184  O   THR A 416     1616   1732   1915   -196    129   -330  A    O  
ATOM   3185  CB  THR A 416      39.267 123.129 270.222  1.00 19.49      A    C  
ANISOU 3185  CB  THR A 416     2306   2650   2448   -234    167   -326  A    C  
ATOM   3186  CG2 THR A 416      39.556 124.501 270.815  1.00 25.98      A    C  
ANISOU 3186  CG2 THR A 416     3040   3540   3292   -228    160   -425  A    C  
ATOM   3187  OG1 THR A 416      38.947 122.236 271.292  1.00 20.21      A    O  
ANISOU 3187  OG1 THR A 416     2426   2808   2444   -266    192   -278  A    O  
ATOM   3188  N   ASN A 417      37.837 125.365 268.206  1.00 17.18      A    N  
ANISOU 3188  N   ASN A 417     1903   2235   2390   -246    149   -459  A    N  
ATOM   3189  CA  ASN A 417      38.010 126.383 267.174  1.00 17.38      A    C  
ANISOU 3189  CA  ASN A 417     1893   2196   2514   -221    122   -485  A    C  
ATOM   3190  C   ASN A 417      37.539 125.946 265.782  1.00 17.94      A    C  
ANISOU 3190  C   ASN A 417     2014   2181   2620   -223    104   -434  A    C  
ATOM   3191  O   ASN A 417      37.908 126.568 264.781  1.00 19.17      A    O  
ANISOU 3191  O   ASN A 417     2164   2285   2835   -196     81   -425  A    O  
ATOM   3192  CB  ASN A 417      39.473 126.843 267.086  1.00 21.82      A    C  
ANISOU 3192  CB  ASN A 417     2449   2758   3085   -176    104   -478  A    C  
ATOM   3193  CG  ASN A 417      39.937 127.581 268.328  1.00 25.91      A    C  
ANISOU 3193  CG  ASN A 417     2904   3355   3587   -179    104   -549  A    C  
ATOM   3194  ND2 ASN A 417      41.245 127.568 268.562  1.00 30.26      A    N  
ANISOU 3194  ND2 ASN A 417     3455   3930   4111   -150     85   -527  A    N  
ATOM   3195  OD1 ASN A 417      39.138 128.170 269.058  1.00 24.26      A    O  
ANISOU 3195  OD1 ASN A 417     2642   3186   3388   -205    121   -628  A    O  
ATOM   3196  N   GLY A 418      36.729 124.892 265.715  1.00 19.73      A    N  
ANISOU 3196  N   GLY A 418     2291   2396   2808   -260    111   -399  A    N  
ATOM   3197  CA  GLY A 418      36.326 124.337 264.435  1.00 17.54      A    C  
ANISOU 3197  CA  GLY A 418     2074   2042   2547   -267     84   -358  A    C  
ATOM   3198  C   GLY A 418      35.590 125.302 263.519  1.00 16.50      A    C  
ANISOU 3198  C   GLY A 418     1889   1876   2503   -273     54   -384  A    C  
ATOM   3199  O   GLY A 418      35.853 125.332 262.312  1.00 22.29      A    O  
ANISOU 3199  O   GLY A 418     2665   2556   3249   -250     24   -353  A    O  
ATOM   3200  N   GLY A 419      34.686 126.099 264.087  1.00 15.38      A    N  
ANISOU 3200  N   GLY A 419     1655   1770   2420   -296     63   -438  A    N  
ATOM   3201  CA  GLY A 419      33.917 127.071 263.319  1.00 14.32      A    C  
ANISOU 3201  CA  GLY A 419     1455   1601   2383   -295     31   -459  A    C  
ATOM   3202  C   GLY A 419      34.787 128.003 262.486  1.00 22.23      A    C  
ANISOU 3202  C   GLY A 419     2453   2559   3434   -247      5   -446  A    C  
ATOM   3203  O   GLY A 419      34.459 128.336 261.335  1.00 29.95      A    O  
ANISOU 3203  O   GLY A 419     3435   3490   4456   -240    -35   -414  A    O  
ATOM   3204  N   GLU A 420      35.929 128.386 263.046  1.00 21.13      A    N  
ANISOU 3204  N   GLU A 420     2307   2439   3282   -216     26   -462  A    N  
ATOM   3205  CA  GLU A 420      36.814 129.337 262.377  1.00 23.43      A    C  
ANISOU 3205  CA  GLU A 420     2580   2691   3631   -178      9   -445  A    C  
ATOM   3206  C   GLU A 420      37.377 128.785 261.071  1.00 25.31      A    C  
ANISOU 3206  C   GLU A 420     2900   2890   3827   -156     -8   -366  A    C  
ATOM   3207  O   GLU A 420      37.945 129.534 260.269  1.00 21.29      A    O  
ANISOU 3207  O   GLU A 420     2378   2348   3363   -130    -21   -333  A    O  
ATOM   3208  CB  GLU A 420      37.949 129.774 263.310  1.00 21.42      A    C  
ANISOU 3208  CB  GLU A 420     2296   2472   3371   -159     29   -480  A    C  
ATOM   3209  CG  GLU A 420      37.488 130.483 264.590  1.00 22.38      A    C  
ANISOU 3209  CG  GLU A 420     2339   2638   3529   -175     46   -577  A    C  
ATOM   3210  CD  GLU A 420      36.804 131.828 264.337  1.00 26.47      A    C  
ANISOU 3210  CD  GLU A 420     2773   3105   4179   -171     29   -626  A    C  
ATOM   3211  OE1 GLU A 420      36.750 132.271 263.168  1.00 21.49      A    O  
ANISOU 3211  OE1 GLU A 420     2143   2408   3615   -157     -1   -572  A    O  
ATOM   3212  OE2 GLU A 420      36.319 132.443 265.318  1.00 23.44      A    O1-
ANISOU 3212  OE2 GLU A 420     2325   2750   3831   -177     48   -719  A    O1-
ATOM   3213  N   LEU A 421      37.179 127.487 260.843  1.00 18.50      A    N  
ANISOU 3213  N   LEU A 421     2122   2028   2878   -169     -5   -337  A    N  
ATOM   3214  CA  LEU A 421      37.670 126.860 259.623  1.00 17.30      A    C  
ANISOU 3214  CA  LEU A 421     2060   1842   2673   -145    -16   -279  A    C  
ATOM   3215  C   LEU A 421      36.683 126.958 258.465  1.00 19.49      A    C  
ANISOU 3215  C   LEU A 421     2353   2084   2967   -165    -62   -259  A    C  
ATOM   3216  O   LEU A 421      37.045 126.662 257.321  1.00 18.72      A    O  
ANISOU 3216  O   LEU A 421     2326   1965   2823   -144    -75   -217  A    O  
ATOM   3217  CB  LEU A 421      38.020 125.382 259.873  1.00 20.53      A    C  
ANISOU 3217  CB  LEU A 421     2563   2251   2986   -142      5   -262  A    C  
ATOM   3218  CG  LEU A 421      39.398 125.036 260.451  1.00 21.11      A    C  
ANISOU 3218  CG  LEU A 421     2654   2348   3018    -96     42   -244  A    C  
ATOM   3219  CD1 LEU A 421      39.667 125.736 261.772  1.00 21.20      A    C  
ANISOU 3219  CD1 LEU A 421     2579   2415   3063   -103     56   -283  A    C  
ATOM   3220  CD2 LEU A 421      39.539 123.528 260.616  1.00 24.28      A    C  
ANISOU 3220  CD2 LEU A 421     3153   2731   3341    -91     57   -221  A    C  
ATOM   3221  N   LEU A 422      35.434 127.323 258.758  1.00 19.72      A    N  
ANISOU 3221  N   LEU A 422     2317   2118   3056   -205    -87   -291  A    N  
ATOM   3222  CA  LEU A 422      34.391 127.319 257.725  1.00 24.13      A    C  
ANISOU 3222  CA  LEU A 422     2884   2654   3631   -231   -144   -270  A    C  
ATOM   3223  C   LEU A 422      34.650 128.271 256.546  1.00 24.54      A    C  
ANISOU 3223  C   LEU A 422     2925   2682   3717   -198   -178   -222  A    C  
ATOM   3224  O   LEU A 422      34.355 127.933 255.391  1.00 27.37      A    O  
ANISOU 3224  O   LEU A 422     3343   3027   4028   -204   -222   -184  A    O  
ATOM   3225  CB  LEU A 422      33.017 127.624 258.328  1.00 25.14      A    C  
ANISOU 3225  CB  LEU A 422     2920   2798   3834   -274   -161   -309  A    C  
ATOM   3226  CG  LEU A 422      32.285 126.502 259.057  1.00 23.38      A    C  
ANISOU 3226  CG  LEU A 422     2714   2597   3570   -329   -146   -332  A    C  
ATOM   3227  CD1 LEU A 422      30.867 126.944 259.380  1.00 23.28      A    C  
ANISOU 3227  CD1 LEU A 422     2596   2607   3645   -368   -164   -359  A    C  
ATOM   3228  CD2 LEU A 422      32.270 125.206 258.244  1.00 13.94      A    C  
ANISOU 3228  CD2 LEU A 422     1638   1371   2289   -356   -175   -301  A    C  
ATOM   3229  N   GLY A 423      35.202 129.448 256.841  1.00 19.56      A    N  
ANISOU 3229  N   GLY A 423     2221   2044   3165   -168   -161   -222  A    N  
ATOM   3230  CA  GLY A 423      35.428 130.462 255.822  1.00 22.40      A    C  
ANISOU 3230  CA  GLY A 423     2559   2375   3576   -142   -190   -162  A    C  
ATOM   3231  C   GLY A 423      36.026 129.893 254.546  1.00 23.81      A    C  
ANISOU 3231  C   GLY A 423     2840   2557   3650   -124   -198    -97  A    C  
ATOM   3232  O   GLY A 423      35.383 129.930 253.481  1.00 26.70      A    O  
ANISOU 3232  O   GLY A 423     3231   2918   3995   -132   -252    -55  A    O  
ATOM   3233  N   GLU A 424      37.193 129.262 254.688  1.00 19.81      A    N  
ANISOU 3233  N   GLU A 424     2394   2065   3069    -98   -144    -94  A    N  
ATOM   3234  CA  GLU A 424      37.900 128.685 253.557  1.00 20.83      A    C  
ANISOU 3234  CA  GLU A 424     2620   2202   3092    -68   -132    -43  A    C  
ATOM   3235  C   GLU A 424      36.953 127.758 252.805  1.00 18.30      A    C  
ANISOU 3235  C   GLU A 424     2382   1879   2690    -97   -182    -53  A    C  
ATOM   3236  O   GLU A 424      36.712 127.938 251.596  1.00 22.99      A    O  
ANISOU 3236  O   GLU A 424     3015   2479   3240    -93   -221     -7  A    O  
ATOM   3237  CB  GLU A 424      39.146 127.916 254.030  1.00 14.07      A    C  
ANISOU 3237  CB  GLU A 424     1810   1362   2175    -33    -65    -54  A    C  
ATOM   3238  CG  GLU A 424      40.028 127.387 252.882  1.00 18.54      A    C  
ANISOU 3238  CG  GLU A 424     2468   1941   2637     13    -34     -7  A    C  
ATOM   3239  CD  GLU A 424      41.218 126.560 253.360  1.00 24.81      A    C  
ANISOU 3239  CD  GLU A 424     3299   2747   3382     58     32    -17  A    C  
ATOM   3240  OE1 GLU A 424      41.541 126.597 254.572  1.00 19.41      A    O  
ANISOU 3240  OE1 GLU A 424     2559   2069   2748     54     50    -45  A    O  
ATOM   3241  OE2 GLU A 424      41.831 125.868 252.517  1.00 25.87      A    O1-
ANISOU 3241  OE2 GLU A 424     3518   2888   3422    101     66      1  A    O1-
ATOM   3242  N   ILE A 425      36.348 126.829 253.543  1.00 13.72      A    N  
ANISOU 3242  N   ILE A 425     1823   1293   2095   -132   -186   -110  A    N  
ATOM   3243  CA  ILE A 425      35.493 125.838 252.907  1.00 16.94      A    C  
ANISOU 3243  CA  ILE A 425     2313   1691   2433   -170   -236   -127  A    C  
ATOM   3244  C   ILE A 425      34.383 126.569 252.168  1.00 22.19      A    C  
ANISOU 3244  C   ILE A 425     2928   2361   3142   -200   -316   -102  A    C  
ATOM   3245  O   ILE A 425      34.165 126.330 250.967  1.00 26.14      A    O  
ANISOU 3245  O   ILE A 425     3498   2868   3565   -203   -364    -77  A    O  
ATOM   3246  CB  ILE A 425      34.963 124.802 253.920  1.00 18.85      A    C  
ANISOU 3246  CB  ILE A 425     2570   1919   2675   -214   -227   -181  A    C  
ATOM   3247  CG1 ILE A 425      36.143 124.088 254.591  1.00 14.22      A    C  
ANISOU 3247  CG1 ILE A 425     2034   1327   2043   -174   -155   -189  A    C  
ATOM   3248  CG2 ILE A 425      34.088 123.763 253.229  1.00 16.23      A    C  
ANISOU 3248  CG2 ILE A 425     2321   1563   2282   -264   -286   -201  A    C  
ATOM   3249  CD1 ILE A 425      35.734 123.112 255.693  1.00 12.56      A    C  
ANISOU 3249  CD1 ILE A 425     1836   1103   1834   -215   -140   -223  A    C  
ATOM   3250  N   GLY A 426      33.764 127.534 252.850  1.00 18.15      A    N  
ANISOU 3250  N   GLY A 426     2295   1850   2751   -213   -328   -106  A    N  
ATOM   3251  CA  GLY A 426      32.682 128.288 252.248  1.00 18.05      A    C  
ANISOU 3251  CA  GLY A 426     2216   1839   2802   -232   -405    -76  A    C  
ATOM   3252  C   GLY A 426      33.172 128.915 250.955  1.00 21.15      A    C  
ANISOU 3252  C   GLY A 426     2643   2237   3154   -196   -432      2  A    C  
ATOM   3253  O   GLY A 426      32.564 128.740 249.881  1.00 18.72      A    O  
ANISOU 3253  O   GLY A 426     2378   1946   2789   -214   -505     34  A    O  
ATOM   3254  N   LEU A 427      34.317 129.593 251.044  1.00 16.88      A    N  
ANISOU 3254  N   LEU A 427     2089   1691   2634   -150   -373     36  A    N  
ATOM   3255  CA  LEU A 427      34.799 130.321 249.886  1.00 25.59      A    C  
ANISOU 3255  CA  LEU A 427     3210   2802   3711   -119   -387    126  A    C  
ATOM   3256  C   LEU A 427      35.028 129.293 248.792  1.00 26.47      A    C  
ANISOU 3256  C   LEU A 427     3456   2948   3654   -116   -398    137  A    C  
ATOM   3257  O   LEU A 427      34.599 129.485 247.644  1.00 15.77      A    O  
ANISOU 3257  O   LEU A 427     2134   1617   2241   -121   -462    192  A    O  
ATOM   3258  CB  LEU A 427      36.079 131.089 250.198  1.00 18.93      A    C  
ANISOU 3258  CB  LEU A 427     2330   1946   2917    -79   -314    161  A    C  
ATOM   3259  CG  LEU A 427      36.619 131.926 249.033  1.00 22.52      A    C  
ANISOU 3259  CG  LEU A 427     2792   2410   3357    -52   -320    273  A    C  
ATOM   3260  CD1 LEU A 427      35.614 132.986 248.570  1.00 18.07      A    C  
ANISOU 3260  CD1 LEU A 427     2155   1821   2891    -63   -402    335  A    C  
ATOM   3261  CD2 LEU A 427      37.945 132.581 249.403  1.00 21.35      A    C  
ANISOU 3261  CD2 LEU A 427     2601   2248   3263    -24   -243    305  A    C  
ATOM   3262  N   ALA A 428      35.624 128.167 249.185  1.00 14.59      A    N  
ANISOU 3262  N   ALA A 428     2029   1443   2070   -110   -343     77  A    N  
ATOM   3263  CA  ALA A 428      35.987 127.143 248.219  1.00 20.43      A    C  
ANISOU 3263  CA  ALA A 428     2904   2204   2653    -97   -338     68  A    C  
ATOM   3264  C   ALA A 428      34.746 126.721 247.458  1.00 21.27      A    C  
ANISOU 3264  C   ALA A 428     3055   2321   2707   -147   -440     53  A    C  
ATOM   3265  O   ALA A 428      34.795 126.546 246.238  1.00 23.45      A    O  
ANISOU 3265  O   ALA A 428     3415   2631   2864   -137   -472     80  A    O  
ATOM   3266  CB  ALA A 428      36.615 125.945 248.910  1.00 14.67      A    C  
ANISOU 3266  CB  ALA A 428     2243   1454   1877    -84   -273     -2  A    C  
ATOM   3267  N   ILE A 429      33.623 126.579 248.163  1.00 19.91      A    N  
ANISOU 3267  N   ILE A 429     2820   2126   2619   -202   -492     10  A    N  
ATOM   3268  CA  ILE A 429      32.441 126.080 247.476  1.00 18.37      A    C  
ANISOU 3268  CA  ILE A 429     2659   1942   2380   -258   -595     -8  A    C  
ATOM   3269  C   ILE A 429      31.889 127.151 246.547  1.00 21.41      A    C  
ANISOU 3269  C   ILE A 429     2990   2361   2782   -255   -676     75  A    C  
ATOM   3270  O   ILE A 429      31.444 126.842 245.443  1.00 18.90      A    O  
ANISOU 3270  O   ILE A 429     2742   2078   2361   -275   -755     88  A    O  
ATOM   3271  CB  ILE A 429      31.349 125.565 248.431  1.00 19.70      A    C  
ANISOU 3271  CB  ILE A 429     2768   2084   2635   -325   -628    -69  A    C  
ATOM   3272  CG1 ILE A 429      31.860 124.372 249.244  1.00 21.70      A    C  
ANISOU 3272  CG1 ILE A 429     3091   2300   2854   -333   -559   -137  A    C  
ATOM   3273  CG2 ILE A 429      30.119 125.142 247.638  1.00 17.33      A    C  
ANISOU 3273  CG2 ILE A 429     2486   1799   2299   -390   -747    -79  A    C  
ATOM   3274  CD1 ILE A 429      30.909 123.939 250.351  1.00 19.89      A    C  
ANISOU 3274  CD1 ILE A 429     2792   2050   2715   -398   -569   -180  A    C  
ATOM   3275  N   GLU A 430      31.951 128.412 246.975  1.00 20.49      A    N  
ANISOU 3275  N   GLU A 430     2756   2236   2796   -227   -659    132  A    N  
ATOM   3276  CA  GLU A 430      31.353 129.484 246.181  1.00 17.68      A    C  
ANISOU 3276  CA  GLU A 430     2336   1898   2482   -221   -740    223  A    C  
ATOM   3277  C   GLU A 430      32.132 129.685 244.893  1.00 19.58      A    C  
ANISOU 3277  C   GLU A 430     2668   2183   2589   -185   -737    303  A    C  
ATOM   3278  O   GLU A 430      31.562 130.042 243.857  1.00 21.96      A    O  
ANISOU 3278  O   GLU A 430     2979   2523   2842   -192   -828    372  A    O  
ATOM   3279  CB  GLU A 430      31.330 130.793 246.983  1.00 17.27      A    C  
ANISOU 3279  CB  GLU A 430     2142   1806   2614   -194   -714    259  A    C  
ATOM   3280  CG  GLU A 430      30.311 130.814 248.111  1.00 26.07      A    C  
ANISOU 3280  CG  GLU A 430     3147   2895   3865   -225   -729    191  A    C  
ATOM   3281  CD  GLU A 430      28.880 130.984 247.625  1.00 32.06      A    C  
ANISOU 3281  CD  GLU A 430     3842   3671   4670   -259   -846    216  A    C  
ATOM   3282  OE1 GLU A 430      28.677 131.262 246.425  1.00 36.90      A    O  
ANISOU 3282  OE1 GLU A 430     4486   4313   5220   -253   -926    296  A    O  
ATOM   3283  OE2 GLU A 430      27.955 130.851 248.455  1.00 36.43      A    O1-
ANISOU 3283  OE2 GLU A 430     4306   4216   5321   -290   -858    159  A    O1-
ATOM   3284  N   MET A 431      33.435 129.420 244.949  1.00 17.92      A    N  
ANISOU 3284  N   MET A 431     2524   1975   2312   -145   -633    297  A    N  
ATOM   3285  CA  MET A 431      34.291 129.638 243.786  1.00 19.52      A    C  
ANISOU 3285  CA  MET A 431     2803   2227   2385   -105   -606    377  A    C  
ATOM   3286  C   MET A 431      34.343 128.402 242.898  1.00 24.29      A    C  
ANISOU 3286  C   MET A 431     3561   2879   2791   -113   -622    321  A    C  
ATOM   3287  O   MET A 431      34.996 128.409 241.857  1.00 29.27      A    O  
ANISOU 3287  O   MET A 431     4274   3566   3282    -79   -596    372  A    O  
ATOM   3288  CB  MET A 431      35.709 130.014 244.214  1.00 18.75      A    C  
ANISOU 3288  CB  MET A 431     2689   2118   2318    -56   -483    404  A    C  
ATOM   3289  CG  MET A 431      35.807 131.315 244.995  1.00 25.78      A    C  
ANISOU 3289  CG  MET A 431     3439   2957   3400    -49   -467    456  A    C  
ATOM   3290  SD  MET A 431      35.194 132.718 244.048  1.00 29.83      A    S  
ANISOU 3290  SD  MET A 431     3885   3474   3974    -48   -553    602  A    S  
ATOM   3291  CE  MET A 431      36.394 132.800 242.720  1.00 60.29      A    C  
ANISOU 3291  CE  MET A 431     7838   7405   7664    -11   -492    713  A    C  
ATOM   3292  N   GLY A 432      33.670 127.337 243.316  1.00 21.42      A    N  
ANISOU 3292  N   GLY A 432     3237   2489   2414   -157   -659    215  A    N  
ATOM   3293  CA  GLY A 432      33.665 126.114 242.538  1.00 21.35      A    C  
ANISOU 3293  CA  GLY A 432     3377   2503   2231   -169   -680    142  A    C  
ATOM   3294  C   GLY A 432      35.010 125.414 242.516  1.00 21.15      A    C  
ANISOU 3294  C   GLY A 432     3451   2477   2110   -110   -558    102  A    C  
ATOM   3295  O   GLY A 432      35.351 124.776 241.527  1.00 21.52      A    O  
ANISOU 3295  O   GLY A 432     3625   2563   1988    -89   -551     74  A    O  
ATOM   3296  N   CYS A 433      35.774 125.524 243.602  1.00 21.32      A    N  
ANISOU 3296  N   CYS A 433     3411   2455   2235    -79   -462     95  A    N  
ATOM   3297  CA  CYS A 433      37.074 124.857 243.688  1.00 24.89      A    C  
ANISOU 3297  CA  CYS A 433     3937   2903   2617    -17   -345     61  A    C  
ATOM   3298  C   CYS A 433      36.957 123.343 243.637  1.00 25.90      A    C  
ANISOU 3298  C   CYS A 433     4193   2993   2653    -26   -348    -55  A    C  
ATOM   3299  O   CYS A 433      35.952 122.782 244.088  1.00 23.71      A    O  
ANISOU 3299  O   CYS A 433     3917   2670   2423    -91   -422   -115  A    O  
ATOM   3300  CB  CYS A 433      37.795 125.238 244.978  1.00 27.65      A    C  
ANISOU 3300  CB  CYS A 433     4185   3216   3106      8   -263     73  A    C  
ATOM   3301  SG  CYS A 433      38.290 126.953 245.078  1.00 33.58      A    S  
ANISOU 3301  SG  CYS A 433     4797   3991   3971     28   -235    197  A    S  
ATOM   3302  N   ASP A 434      37.981 122.689 243.083  1.00 23.18      A    N  
ANISOU 3302  N   ASP A 434     3955   2666   2188     40   -265    -84  A    N  
ATOM   3303  CA  ASP A 434      38.088 121.232 243.183  1.00 27.47      A    C  
ANISOU 3303  CA  ASP A 434     4619   3149   2669     48   -247   -198  A    C  
ATOM   3304  C   ASP A 434      39.111 120.849 244.243  1.00 26.71      A    C  
ANISOU 3304  C   ASP A 434     4493   3005   2650    104   -140   -210  A    C  
ATOM   3305  O   ASP A 434      39.781 121.717 244.804  1.00 21.96      A    O  
ANISOU 3305  O   ASP A 434     3782   2428   2133    135    -82   -136  A    O  
ATOM   3306  CB  ASP A 434      38.454 120.585 241.842  1.00 26.45      A    C  
ANISOU 3306  CB  ASP A 434     4643   3060   2346     90   -232   -247  A    C  
ATOM   3307  CG  ASP A 434      39.781 121.087 241.281  1.00 31.35      A    C  
ANISOU 3307  CG  ASP A 434     5263   3755   2892    185   -112   -181  A    C  
ATOM   3308  OD1 ASP A 434      40.617 121.627 242.044  1.00 31.86      A    O  
ANISOU 3308  OD1 ASP A 434     5226   3818   3061    225    -29   -119  A    O  
ATOM   3309  OD2 ASP A 434      40.003 120.912 240.063  1.00 34.94      A    O1-
ANISOU 3309  OD2 ASP A 434     5821   4276   3178    217   -100   -194  A    O1-
ATOM   3310  N   ALA A 435      39.258 119.551 244.489  1.00 27.32      A    N  
ANISOU 3310  N   ALA A 435     4669   3011   2700    118   -119   -301  A    N  
ATOM   3311  CA  ALA A 435      40.166 119.078 245.528  1.00 23.72      A    C  
ANISOU 3311  CA  ALA A 435     4188   2506   2318    172    -31   -308  A    C  
ATOM   3312  C   ALA A 435      41.606 119.537 245.307  1.00 24.55      A    C  
ANISOU 3312  C   ALA A 435     4262   2670   2397    272     85   -251  A    C  
ATOM   3313  O   ALA A 435      42.311 119.868 246.258  1.00 27.47      A    O  
ANISOU 3313  O   ALA A 435     4536   3039   2864    301    141   -207  A    O  
ATOM   3314  CB  ALA A 435      40.107 117.561 245.626  1.00 24.45      A    C  
ANISOU 3314  CB  ALA A 435     4408   2503   2377    179    -30   -408  A    C  
ATOM   3315  N   GLU A 436      42.028 119.569 244.048  1.00 21.61      A    N  
ANISOU 3315  N   GLU A 436     3966   2358   1888    320    119   -251  A    N  
ATOM   3316  CA  GLU A 436      43.386 119.961 243.703  1.00 19.91      A    C  
ANISOU 3316  CA  GLU A 436     3720   2208   1637    414    237   -194  A    C  
ATOM   3317  C   GLU A 436      43.667 121.414 244.094  1.00 24.35      A    C  
ANISOU 3317  C   GLU A 436     4125   2828   2300    396    248    -74  A    C  
ATOM   3318  O   GLU A 436      44.740 121.724 244.623  1.00 24.94      A    O  
ANISOU 3318  O   GLU A 436     4117   2920   2440    448    332    -26  A    O  
ATOM   3319  CB  GLU A 436      43.620 119.747 242.206  1.00 27.57      A    C  
ANISOU 3319  CB  GLU A 436     4807   3245   2423    459    268   -216  A    C  
ATOM   3320  CG  GLU A 436      44.998 120.137 241.722  1.00 31.61      A    C  
ANISOU 3320  CG  GLU A 436     5286   3840   2884    555    401   -152  A    C  
ATOM   3321  CD  GLU A 436      45.158 119.983 240.218  1.00 38.80      A    C  
ANISOU 3321  CD  GLU A 436     6313   4835   3594    596    435   -171  A    C  
ATOM   3322  OE1 GLU A 436      45.318 121.012 239.530  1.00 43.79      A    O  
ANISOU 3322  OE1 GLU A 436     6895   5566   4176    589    451    -67  A    O  
ATOM   3323  OE2 GLU A 436      45.141 118.836 239.725  1.00 44.78      A    O1-
ANISOU 3323  OE2 GLU A 436     7213   5558   4242    636    449   -290  A    O1-
ATOM   3324  N   ASP A 437      42.700 122.296 243.843  1.00 23.06      A    N  
ANISOU 3324  N   ASP A 437     3917   2687   2159    321    158    -29  A    N  
ATOM   3325  CA  ASP A 437      42.818 123.702 244.223  1.00 23.03      A    C  
ANISOU 3325  CA  ASP A 437     3767   2714   2268    297    155     77  A    C  
ATOM   3326  C   ASP A 437      43.112 123.872 245.711  1.00 20.68      A    C  
ANISOU 3326  C   ASP A 437     3361   2367   2128    289    173     75  A    C  
ATOM   3327  O   ASP A 437      43.977 124.658 246.102  1.00 24.44      A    O  
ANISOU 3327  O   ASP A 437     3736   2869   2682    312    229    141  A    O  
ATOM   3328  CB  ASP A 437      41.539 124.469 243.881  1.00 24.77      A    C  
ANISOU 3328  CB  ASP A 437     3959   2942   2511    219     40    112  A    C  
ATOM   3329  CG  ASP A 437      41.358 124.673 242.397  1.00 28.61      A    C  
ANISOU 3329  CG  ASP A 437     4523   3501   2846    226     18    152  A    C  
ATOM   3330  OD1 ASP A 437      42.374 124.832 241.687  1.00 31.49      A    O  
ANISOU 3330  OD1 ASP A 437     4911   3930   3123    287    109    202  A    O  
ATOM   3331  OD2 ASP A 437      40.192 124.703 241.948  1.00 32.42      A    O1-
ANISOU 3331  OD2 ASP A 437     5037   3985   3295    168    -92    139  A    O1-
ATOM   3332  N   ILE A 438      42.377 123.133 246.533  1.00 19.67      A    N  
ANISOU 3332  N   ILE A 438     3256   2174   2045    249    122     -1  A    N  
ATOM   3333  CA  ILE A 438      42.528 123.215 247.979  1.00 17.42      A    C  
ANISOU 3333  CA  ILE A 438     2879   1852   1888    235    130     -9  A    C  
ATOM   3334  C   ILE A 438      43.839 122.576 248.431  1.00 23.79      A    C  
ANISOU 3334  C   ILE A 438     3692   2656   2691    314    224    -16  A    C  
ATOM   3335  O   ILE A 438      44.606 123.185 249.179  1.00 23.39      A    O  
ANISOU 3335  O   ILE A 438     3536   2625   2725    331    263     27  A    O  
ATOM   3336  CB  ILE A 438      41.344 122.531 248.684  1.00 19.08      A    C  
ANISOU 3336  CB  ILE A 438     3115   2002   2134    169     56    -77  A    C  
ATOM   3337  CG1 ILE A 438      40.023 123.142 248.210  1.00 16.36      A    C  
ANISOU 3337  CG1 ILE A 438     2750   1665   1801     95    -41    -69  A    C  
ATOM   3338  CG2 ILE A 438      41.485 122.611 250.203  1.00 15.80      A    C  
ANISOU 3338  CG2 ILE A 438     2609   1563   1832    154     69    -83  A    C  
ATOM   3339  CD1 ILE A 438      38.788 122.366 248.652  1.00 19.32      A    C  
ANISOU 3339  CD1 ILE A 438     3157   1988   2195     24   -115   -135  A    C  
ATOM   3340  N   ALA A 439      44.103 121.364 247.951  1.00 23.93      A    N  
ANISOU 3340  N   ALA A 439     3831   2648   2612    363    257    -72  A    N  
ATOM   3341  CA  ALA A 439      45.288 120.611 248.355  1.00 21.34      A    C  
ANISOU 3341  CA  ALA A 439     3517   2308   2285    448    342    -82  A    C  
ATOM   3342  C   ALA A 439      46.582 121.328 247.998  1.00 19.25      A    C  
ANISOU 3342  C   ALA A 439     3175   2118   2020    516    432     -9  A    C  
ATOM   3343  O   ALA A 439      47.514 121.351 248.794  1.00 23.42      A    O  
ANISOU 3343  O   ALA A 439     3625   2655   2619    557    481     19  A    O  
ATOM   3344  CB  ALA A 439      45.273 119.215 247.741  1.00 20.32      A    C  
ANISOU 3344  CB  ALA A 439     3541   2125   2054    494    361   -164  A    C  
ATOM   3345  N   LEU A 440      46.641 121.913 246.806  1.00 17.38      A    N  
ANISOU 3345  N   LEU A 440     2957   1942   1705    523    451     31  A    N  
ATOM   3346  CA  LEU A 440      47.874 122.551 246.346  1.00 24.38      A    C  
ANISOU 3346  CA  LEU A 440     3773   2906   2584    583    546    110  A    C  
ATOM   3347  C   LEU A 440      48.100 123.935 246.966  1.00 24.16      A    C  
ANISOU 3347  C   LEU A 440     3588   2905   2688    534    532    198  A    C  
ATOM   3348  O   LEU A 440      49.201 124.483 246.881  1.00 26.22      A    O  
ANISOU 3348  O   LEU A 440     3762   3219   2982    572    606    269  A    O  
ATOM   3349  CB  LEU A 440      47.943 122.612 244.816  1.00 27.59      A    C  
ANISOU 3349  CB  LEU A 440     4263   3377   2843    613    586    128  A    C  
ATOM   3350  CG  LEU A 440      48.047 121.250 244.120  1.00 34.56      A    C  
ANISOU 3350  CG  LEU A 440     5301   4241   3588    683    627     32  A    C  
ATOM   3351  CD1 LEU A 440      48.265 121.410 242.625  1.00 32.39      A    C  
ANISOU 3351  CD1 LEU A 440     5101   4055   3152    719    680     53  A    C  
ATOM   3352  CD2 LEU A 440      49.144 120.396 244.731  1.00 38.07      A    C  
ANISOU 3352  CD2 LEU A 440     5735   4659   4072    777    715      2  A    C  
ATOM   3353  N   THR A 441      47.058 124.511 247.561  1.00 20.51      A    N  
ANISOU 3353  N   THR A 441     3085   2404   2305    450    437    191  A    N  
ATOM   3354  CA  THR A 441      47.242 125.726 248.348  1.00 24.35      A    C  
ANISOU 3354  CA  THR A 441     3427   2893   2930    405    418    247  A    C  
ATOM   3355  C   THR A 441      48.055 125.339 249.577  1.00 25.01      A    C  
ANISOU 3355  C   THR A 441     3447   2966   3088    434    448    224  A    C  
ATOM   3356  O   THR A 441      47.748 124.344 250.242  1.00 21.58      A    O  
ANISOU 3356  O   THR A 441     3068   2490   2641    442    428    156  A    O  
ATOM   3357  CB  THR A 441      45.894 126.336 248.785  1.00 27.63      A    C  
ANISOU 3357  CB  THR A 441     3817   3267   3417    320    314    228  A    C  
ATOM   3358  CG2 THR A 441      46.115 127.565 249.666  1.00 27.94      A    C  
ANISOU 3358  CG2 THR A 441     3713   3298   3606    280    298    266  A    C  
ATOM   3359  OG1 THR A 441      45.154 126.740 247.626  1.00 25.68      A    O  
ANISOU 3359  OG1 THR A 441     3618   3036   3104    295    275    262  A    O  
ATOM   3360  N   ILE A 442      49.110 126.096 249.867  1.00 18.10      A    N  
ANISOU 3360  N   ILE A 442     2457   2129   2292    448    494    287  A    N  
ATOM   3361  CA  ILE A 442      49.966 125.769 251.008  1.00 17.13      A    C  
ANISOU 3361  CA  ILE A 442     2265   2010   2236    477    515    273  A    C  
ATOM   3362  C   ILE A 442      49.351 126.302 252.304  1.00 21.40      A    C  
ANISOU 3362  C   ILE A 442     2735   2516   2879    405    436    237  A    C  
ATOM   3363  O   ILE A 442      49.280 127.515 252.508  1.00 20.64      A    O  
ANISOU 3363  O   ILE A 442     2545   2421   2874    351    407    267  A    O  
ATOM   3364  CB  ILE A 442      51.408 126.312 250.836  1.00 19.67      A    C  
ANISOU 3364  CB  ILE A 442     2478   2392   2602    518    592    352  A    C  
ATOM   3365  CG1 ILE A 442      52.031 125.788 249.542  1.00 22.22      A    C  
ANISOU 3365  CG1 ILE A 442     2867   2763   2814    596    686    386  A    C  
ATOM   3366  CG2 ILE A 442      52.274 125.914 252.023  1.00 15.88      A    C  
ANISOU 3366  CG2 ILE A 442     1924   1923   2186    549    599    337  A    C  
ATOM   3367  CD1 ILE A 442      53.441 126.301 249.282  1.00 22.76      A    C  
ANISOU 3367  CD1 ILE A 442     2820   2902   2926    637    775    473  A    C  
ATOM   3368  N   HIS A 443      48.888 125.393 253.163  1.00 18.14      A    N  
ANISOU 3368  N   HIS A 443     2371   2072   2450    404    403    171  A    N  
ATOM   3369  CA  HIS A 443      48.309 125.775 254.444  1.00 22.75      A    C  
ANISOU 3369  CA  HIS A 443     2896   2638   3109    342    340    131  A    C  
ATOM   3370  C   HIS A 443      49.404 125.807 255.500  1.00 23.59      A    C  
ANISOU 3370  C   HIS A 443     2912   2780   3271    365    355    142  A    C  
ATOM   3371  O   HIS A 443      50.272 124.938 255.515  1.00 22.56      A    O  
ANISOU 3371  O   HIS A 443     2801   2667   3102    436    400    158  A    O  
ATOM   3372  CB  HIS A 443      47.216 124.779 254.851  1.00 20.14      A    C  
ANISOU 3372  CB  HIS A 443     2660   2263   2729    320    299     67  A    C  
ATOM   3373  CG  HIS A 443      46.051 124.738 253.912  1.00 22.78      A    C  
ANISOU 3373  CG  HIS A 443     3074   2566   3017    286    266     50  A    C  
ATOM   3374  CD2 HIS A 443      44.746 125.066 254.093  1.00 20.75      A    C  
ANISOU 3374  CD2 HIS A 443     2817   2283   2785    217    203     17  A    C  
ATOM   3375  ND1 HIS A 443      46.156 124.324 252.597  1.00 19.82      A    N  
ANISOU 3375  ND1 HIS A 443     2785   2191   2554    324    297     66  A    N  
ATOM   3376  CE1 HIS A 443      44.975 124.398 252.017  1.00 20.35      A    C  
ANISOU 3376  CE1 HIS A 443     2905   2235   2592    276    243     46  A    C  
ATOM   3377  NE2 HIS A 443      44.099 124.842 252.902  1.00 19.31      A    N  
ANISOU 3377  NE2 HIS A 443     2716   2085   2535    211    186     19  A    N  
ATOM   3378  N   ALA A 444      49.359 126.793 256.393  1.00 19.63      A    N  
ANISOU 3378  N   ALA A 444     2309   2289   2859    309    312    128  A    N  
ATOM   3379  CA  ALA A 444      50.391 126.912 257.423  1.00 22.46      A    C  
ANISOU 3379  CA  ALA A 444     2575   2691   3267    321    311    134  A    C  
ATOM   3380  C   ALA A 444      50.399 125.715 258.373  1.00 23.05      A    C  
ANISOU 3380  C   ALA A 444     2697   2773   3288    351    299    104  A    C  
ATOM   3381  O   ALA A 444      49.347 125.164 258.711  1.00 21.56      A    O  
ANISOU 3381  O   ALA A 444     2583   2552   3058    325    271     60  A    O  
ATOM   3382  CB  ALA A 444      50.215 128.195 258.205  1.00 19.06      A    C  
ANISOU 3382  CB  ALA A 444     2042   2263   2937    249    259    105  A    C  
ATOM   3383  N   HIS A 445      51.597 125.326 258.799  1.00 22.64      A    N  
ANISOU 3383  N   HIS A 445     2595   2765   3243    406    321    138  A    N  
ATOM   3384  CA  HIS A 445      51.792 124.224 259.738  1.00 22.09      A    C  
ANISOU 3384  CA  HIS A 445     2558   2706   3130    443    308    132  A    C  
ATOM   3385  C   HIS A 445      52.605 124.739 260.922  1.00 25.96      A    C  
ANISOU 3385  C   HIS A 445     2929   3262   3672    427    268    137  A    C  
ATOM   3386  O   HIS A 445      53.561 125.490 260.737  1.00 26.95      A    O  
ANISOU 3386  O   HIS A 445     2952   3427   3862    431    279    169  A    O  
ATOM   3387  CB  HIS A 445      52.544 123.081 259.057  1.00 20.61      A    C  
ANISOU 3387  CB  HIS A 445     2429   2506   2895    545    370    175  A    C  
ATOM   3388  CG  HIS A 445      52.844 121.924 259.958  1.00 27.74      A    C  
ANISOU 3388  CG  HIS A 445     3363   3407   3768    595    357    185  A    C  
ATOM   3389  CD2 HIS A 445      53.949 121.618 260.684  1.00 31.59      A    C  
ANISOU 3389  CD2 HIS A 445     3778   3946   4279    650    352    229  A    C  
ATOM   3390  ND1 HIS A 445      51.946 120.898 260.186  1.00 28.46      A    N  
ANISOU 3390  ND1 HIS A 445     3572   3438   3804    591    342    160  A    N  
ATOM   3391  CE1 HIS A 445      52.485 120.016 261.007  1.00 28.47      A    C  
ANISOU 3391  CE1 HIS A 445     3576   3446   3794    643    332    193  A    C  
ATOM   3392  NE2 HIS A 445      53.699 120.426 261.324  1.00 29.74      A    N  
ANISOU 3392  NE2 HIS A 445     3622   3678   4000    683    335    235  A    N  
ATOM   3393  N   PRO A 446      52.217 124.365 262.149  1.00 26.51      A    N  
ANISOU 3393  N   PRO A 446     3009   3351   3712    401    218    105  A    N  
ATOM   3394  CA  PRO A 446      51.081 123.509 262.493  1.00 24.05      A    C  
ANISOU 3394  CA  PRO A 446     2806   2999   3333    383    205     76  A    C  
ATOM   3395  C   PRO A 446      49.847 124.313 262.905  1.00 22.26      A    C  
ANISOU 3395  C   PRO A 446     2575   2765   3120    291    168      7  A    C  
ATOM   3396  O   PRO A 446      49.883 125.080 263.870  1.00 16.15      A    O  
ANISOU 3396  O   PRO A 446     1723   2041   2372    245    128    -31  A    O  
ATOM   3397  CB  PRO A 446      51.616 122.722 263.686  1.00 23.24      A    C  
ANISOU 3397  CB  PRO A 446     2693   2943   3195    414    178    103  A    C  
ATOM   3398  CG  PRO A 446      52.552 123.695 264.378  1.00 23.00      A    C  
ANISOU 3398  CG  PRO A 446     2528   2994   3216    395    141    101  A    C  
ATOM   3399  CD  PRO A 446      53.058 124.659 263.326  1.00 24.28      A    C  
ANISOU 3399  CD  PRO A 446     2625   3145   3453    394    172    110  A    C  
ATOM   3400  N   THR A 447      48.753 124.126 262.171  1.00 20.20      A    N  
ANISOU 3400  N   THR A 447     2393   2443   2839    268    180    -14  A    N  
ATOM   3401  CA  THR A 447      47.492 124.789 262.482  1.00 19.33      A    C  
ANISOU 3401  CA  THR A 447     2277   2322   2747    191    150    -75  A    C  
ATOM   3402  C   THR A 447      46.378 123.766 262.466  1.00 18.44      A    C  
ANISOU 3402  C   THR A 447     2265   2166   2576    174    151    -84  A    C  
ATOM   3403  O   THR A 447      46.563 122.652 261.981  1.00 16.37      A    O  
ANISOU 3403  O   THR A 447     2087   1865   2267    219    173    -49  A    O  
ATOM   3404  CB  THR A 447      47.137 125.862 261.434  1.00 20.68      A    C  
ANISOU 3404  CB  THR A 447     2420   2457   2980    167    153    -84  A    C  
ATOM   3405  CG2 THR A 447      48.204 126.925 261.370  1.00 11.95      A    C  
ANISOU 3405  CG2 THR A 447     1211   1380   1948    173    154    -66  A    C  
ATOM   3406  OG1 THR A 447      47.010 125.242 260.145  1.00 18.81      A    O  
ANISOU 3406  OG1 THR A 447     2268   2174   2705    203    184    -48  A    O  
ATOM   3407  N   LEU A 448      45.216 124.142 262.984  1.00 19.99      A    N  
ANISOU 3407  N   LEU A 448     2449   2366   2780    108    128   -135  A    N  
ATOM   3408  CA  LEU A 448      44.044 123.285 262.870  1.00 17.00      A    C  
ANISOU 3408  CA  LEU A 448     2152   1945   2362     76    126   -142  A    C  
ATOM   3409  C   LEU A 448      43.478 123.363 261.453  1.00 22.58      A    C  
ANISOU 3409  C   LEU A 448     2907   2590   3083     73    127   -142  A    C  
ATOM   3410  O   LEU A 448      42.974 122.368 260.921  1.00 19.70      A    O  
ANISOU 3410  O   LEU A 448     2634   2174   2677     72    129   -132  A    O  
ATOM   3411  CB  LEU A 448      42.977 123.696 263.887  1.00 20.29      A    C  
ANISOU 3411  CB  LEU A 448     2526   2399   2786      8    109   -194  A    C  
ATOM   3412  CG  LEU A 448      43.417 123.638 265.356  1.00 22.63      A    C  
ANISOU 3412  CG  LEU A 448     2780   2773   3044      3    105   -202  A    C  
ATOM   3413  CD1 LEU A 448      42.336 124.173 266.291  1.00 18.18      A    C  
ANISOU 3413  CD1 LEU A 448     2169   2257   2481    -61    101   -265  A    C  
ATOM   3414  CD2 LEU A 448      43.781 122.198 265.736  1.00 19.88      A    C  
ANISOU 3414  CD2 LEU A 448     2510   2420   2625     32    115   -137  A    C  
ATOM   3415  N   HIS A 449      43.575 124.538 260.832  1.00 16.97      A    N  
ANISOU 3415  N   HIS A 449     2137   1881   2430     70    121   -150  A    N  
ATOM   3416  CA  HIS A 449      42.925 124.721 259.538  1.00 17.98      A    C  
ANISOU 3416  CA  HIS A 449     2305   1964   2564     61    112   -144  A    C  
ATOM   3417  C   HIS A 449      43.636 124.004 258.387  1.00 17.34      A    C  
ANISOU 3417  C   HIS A 449     2306   1856   2428    120    141   -102  A    C  
ATOM   3418  O   HIS A 449      43.025 123.751 257.347  1.00 19.11      A    O  
ANISOU 3418  O   HIS A 449     2596   2044   2621    112    130   -102  A    O  
ATOM   3419  CB  HIS A 449      42.666 126.210 259.212  1.00 19.42      A    C  
ANISOU 3419  CB  HIS A 449     2401   2148   2830     36     92   -154  A    C  
ATOM   3420  CG  HIS A 449      43.863 126.946 258.699  1.00 17.21      A    C  
ANISOU 3420  CG  HIS A 449     2075   1880   2585     75    114   -112  A    C  
ATOM   3421  CD2 HIS A 449      44.374 127.048 257.445  1.00 14.98      A    C  
ANISOU 3421  CD2 HIS A 449     1821   1585   2286    109    135    -58  A    C  
ATOM   3422  ND1 HIS A 449      44.695 127.687 259.514  1.00 17.76      A    N  
ANISOU 3422  ND1 HIS A 449     2054   1983   2711     75    116   -121  A    N  
ATOM   3423  CE1 HIS A 449      45.662 128.219 258.783  1.00 19.67      A    C  
ANISOU 3423  CE1 HIS A 449     2264   2227   2983    104    138    -69  A    C  
ATOM   3424  NE2 HIS A 449      45.494 127.844 257.528  1.00 16.23      A    N  
ANISOU 3424  NE2 HIS A 449     1900   1768   2500    128    156    -26  A    N  
ATOM   3425  N   GLU A 450      44.906 123.646 258.574  1.00 15.45      A    N  
ANISOU 3425  N   GLU A 450     2062   1638   2172    180    177    -70  A    N  
ATOM   3426  CA  GLU A 450      45.610 122.906 257.528  1.00 21.08      A    C  
ANISOU 3426  CA  GLU A 450     2851   2327   2830    248    218    -39  A    C  
ATOM   3427  C   GLU A 450      44.937 121.563 257.253  1.00 20.47      A    C  
ANISOU 3427  C   GLU A 450     2898   2190   2688    249    212    -61  A    C  
ATOM   3428  O   GLU A 450      45.065 121.009 256.157  1.00 21.11      A    O  
ANISOU 3428  O   GLU A 450     3064   2239   2717    287    234    -61  A    O  
ATOM   3429  CB  GLU A 450      47.106 122.736 257.844  1.00 23.10      A    C  
ANISOU 3429  CB  GLU A 450     3065   2621   3093    321    261      1  A    C  
ATOM   3430  CG  GLU A 450      47.427 121.774 258.975  1.00 30.23      A    C  
ANISOU 3430  CG  GLU A 450     3982   3526   3979    344    257      5  A    C  
ATOM   3431  CD  GLU A 450      48.926 121.553 259.143  1.00 34.76      A    C  
ANISOU 3431  CD  GLU A 450     4510   4138   4562    426    295     52  A    C  
ATOM   3432  OE1 GLU A 450      49.589 121.179 258.148  1.00 32.68      A    O  
ANISOU 3432  OE1 GLU A 450     4282   3859   4275    496    346     75  A    O  
ATOM   3433  OE2 GLU A 450      49.440 121.764 260.265  1.00 33.01      A    O1-
ANISOU 3433  OE2 GLU A 450     4210   3966   4367    422    273     64  A    O1-
ATOM   3434  N   SER A 451      44.187 121.072 258.238  1.00 19.89      A    N  
ANISOU 3434  N   SER A 451     2835   2103   2619    200    183    -82  A    N  
ATOM   3435  CA  SER A 451      43.397 119.860 258.068  1.00 20.96      A    C  
ANISOU 3435  CA  SER A 451     3080   2171   2713    179    169   -101  A    C  
ATOM   3436  C   SER A 451      42.514 119.949 256.819  1.00 22.56      A    C  
ANISOU 3436  C   SER A 451     3340   2339   2893    145    142   -129  A    C  
ATOM   3437  O   SER A 451      42.339 118.947 256.116  1.00 24.07      A    O  
ANISOU 3437  O   SER A 451     3642   2469   3034    159    142   -148  A    O  
ATOM   3438  CB  SER A 451      42.586 119.537 259.334  1.00 17.98      A    C  
ANISOU 3438  CB  SER A 451     2683   1797   2351    113    143   -108  A    C  
ATOM   3439  OG  SER A 451      41.628 120.543 259.623  1.00 15.87      A    O  
ANISOU 3439  OG  SER A 451     2337   1567   2126     42    113   -136  A    O  
ATOM   3440  N   VAL A 452      42.007 121.150 256.520  1.00 24.51      A    N  
ANISOU 3440  N   VAL A 452     3514   2622   3177    106    116   -133  A    N  
ATOM   3441  CA  VAL A 452      41.209 121.355 255.306  1.00 12.47      A    C  
ANISOU 3441  CA  VAL A 452     2033   1079   1627     78     81   -147  A    C  
ATOM   3442  C   VAL A 452      42.023 120.889 254.102  1.00 17.67      A    C  
ANISOU 3442  C   VAL A 452     2779   1725   2211    148    117   -138  A    C  
ATOM   3443  O   VAL A 452      41.619 119.943 253.387  1.00 20.52      A    O  
ANISOU 3443  O   VAL A 452     3253   2037   2508    145    102   -171  A    O  
ATOM   3444  CB  VAL A 452      40.767 122.836 255.156  1.00 18.08      A    C  
ANISOU 3444  CB  VAL A 452     2640   1830   2401     44     53   -135  A    C  
ATOM   3445  CG1 VAL A 452      40.068 123.073 253.818  1.00 12.52      A    C  
ANISOU 3445  CG1 VAL A 452     1978   1116   1662     26     11   -131  A    C  
ATOM   3446  CG2 VAL A 452      39.844 123.213 256.297  1.00 15.20      A    C  
ANISOU 3446  CG2 VAL A 452     2196   1476   2105    -19     23   -161  A    C  
ATOM   3447  N   GLY A 453      43.211 121.471 253.949  1.00 17.63      A    N  
ANISOU 3447  N   GLY A 453     2724   1763   2213    211    168    -99  A    N  
ATOM   3448  CA  GLY A 453      44.117 121.055 252.896  1.00 20.27      A    C  
ANISOU 3448  CA  GLY A 453     3127   2100   2474    288    222    -86  A    C  
ATOM   3449  C   GLY A 453      44.358 119.557 252.966  1.00 21.21      A    C  
ANISOU 3449  C   GLY A 453     3356   2158   2544    332    246   -122  A    C  
ATOM   3450  O   GLY A 453      44.316 118.850 251.945  1.00 23.19      A    O  
ANISOU 3450  O   GLY A 453     3719   2376   2716    362    257   -155  A    O  
ATOM   3451  N   LEU A 454      44.561 119.050 254.179  1.00 17.43      A    N  
ANISOU 3451  N   LEU A 454     2853   1659   2110    335    248   -117  A    N  
ATOM   3452  CA  LEU A 454      44.963 117.659 254.285  1.00 21.97      A    C  
ANISOU 3452  CA  LEU A 454     3526   2167   2655    390    275   -135  A    C  
ATOM   3453  C   LEU A 454      43.807 116.791 253.826  1.00 21.55      A    C  
ANISOU 3453  C   LEU A 454     3590   2033   2565    333    227   -191  A    C  
ATOM   3454  O   LEU A 454      44.025 115.787 253.137  1.00 18.74      A    O  
ANISOU 3454  O   LEU A 454     3351   1611   2158    382    248   -229  A    O  
ATOM   3455  CB  LEU A 454      45.463 117.318 255.693  1.00 22.28      A    C  
ANISOU 3455  CB  LEU A 454     3511   2207   2746    407    283   -100  A    C  
ATOM   3456  CG  LEU A 454      46.780 118.035 256.029  1.00 25.34      A    C  
ANISOU 3456  CG  LEU A 454     3790   2673   3166    472    328    -49  A    C  
ATOM   3457  CD1 LEU A 454      47.133 117.945 257.501  1.00 23.46      A    C  
ANISOU 3457  CD1 LEU A 454     3480   2461   2973    468    314    -14  A    C  
ATOM   3458  CD2 LEU A 454      47.913 117.461 255.190  1.00 20.02      A    C  
ANISOU 3458  CD2 LEU A 454     3163   1988   2456    585    398    -41  A    C  
ATOM   3459  N   ALA A 455      42.581 117.234 254.113  1.00 19.26      A    N  
ANISOU 3459  N   ALA A 455     3265   1748   2303    232    163   -202  A    N  
ATOM   3460  CA  ALA A 455      41.428 116.430 253.727  1.00 18.77      A    C  
ANISOU 3460  CA  ALA A 455     3299   1614   2220    163    107   -252  A    C  
ATOM   3461  C   ALA A 455      41.433 116.353 252.218  1.00 22.50      A    C  
ANISOU 3461  C   ALA A 455     3860   2079   2608    190    103   -293  A    C  
ATOM   3462  O   ALA A 455      41.234 115.274 251.641  1.00 22.54      A    O  
ANISOU 3462  O   ALA A 455     3991   2006   2566    195     92   -348  A    O  
ATOM   3463  CB  ALA A 455      40.137 117.050 254.232  1.00 20.41      A    C  
ANISOU 3463  CB  ALA A 455     3431   1847   2478     55     44   -251  A    C  
ATOM   3464  N   ALA A 456      41.743 117.483 251.581  1.00 19.00      A    N  
ANISOU 3464  N   ALA A 456     3356   1718   2145    210    116   -265  A    N  
ATOM   3465  CA  ALA A 456      41.743 117.529 250.128  1.00 20.18      A    C  
ANISOU 3465  CA  ALA A 456     3585   1885   2199    233    114   -291  A    C  
ATOM   3466  C   ALA A 456      42.762 116.526 249.616  1.00 23.89      A    C  
ANISOU 3466  C   ALA A 456     4161   2315   2601    333    185   -326  A    C  
ATOM   3467  O   ALA A 456      42.486 115.774 248.667  1.00 27.18      A    O  
ANISOU 3467  O   ALA A 456     4705   2690   2933    340    171   -394  A    O  
ATOM   3468  CB  ALA A 456      42.067 118.931 249.634  1.00 20.33      A    C  
ANISOU 3468  CB  ALA A 456     3510   1998   2215    246    128   -231  A    C  
ATOM   3469  N   GLU A 457      43.913 116.468 250.288  1.00 21.78      A    N  
ANISOU 3469  N   GLU A 457     3842   2060   2376    412    259   -286  A    N  
ATOM   3470  CA  GLU A 457      44.961 115.544 249.867  1.00 22.12      A    C  
ANISOU 3470  CA  GLU A 457     3967   2066   2370    523    337   -314  A    C  
ATOM   3471  C   GLU A 457      44.478 114.097 249.955  1.00 23.95      A    C  
ANISOU 3471  C   GLU A 457     4332   2171   2595    515    309   -386  A    C  
ATOM   3472  O   GLU A 457      44.815 113.268 249.098  1.00 25.35      A    O  
ANISOU 3472  O   GLU A 457     4630   2298   2702    580    344   -452  A    O  
ATOM   3473  CB  GLU A 457      46.245 115.738 250.681  1.00 21.75      A    C  
ANISOU 3473  CB  GLU A 457     3821   2056   2386    605    409   -249  A    C  
ATOM   3474  CG  GLU A 457      47.025 117.000 250.333  1.00 30.92      A    C  
ANISOU 3474  CG  GLU A 457     4869   3332   3548    635    457   -184  A    C  
ATOM   3475  CD  GLU A 457      48.322 117.119 251.121  1.00 45.74      A    C  
ANISOU 3475  CD  GLU A 457     6643   5245   5490    712    520   -125  A    C  
ATOM   3476  OE1 GLU A 457      48.860 116.073 251.553  1.00 51.34      A    O  
ANISOU 3476  OE1 GLU A 457     7396   5897   6216    782    550   -138  A    O  
ATOM   3477  OE2 GLU A 457      48.814 118.257 251.292  1.00 48.97      A    O1-
ANISOU 3477  OE2 GLU A 457     6927   5736   5941    703    535    -62  A    O1-
ATOM   3478  N   VAL A 458      43.663 113.804 250.967  1.00 23.57      A    N  
ANISOU 3478  N   VAL A 458     4264   2069   2621    431    248   -377  A    N  
ATOM   3479  CA  VAL A 458      43.165 112.445 251.129  1.00 21.08      A    C  
ANISOU 3479  CA  VAL A 458     4068   1622   2318    409    218   -432  A    C  
ATOM   3480  C   VAL A 458      42.378 112.107 249.872  1.00 24.58      A    C  
ANISOU 3480  C   VAL A 458     4631   2031   2678    365    168   -522  A    C  
ATOM   3481  O   VAL A 458      42.515 111.007 249.324  1.00 25.29      A    O  
ANISOU 3481  O   VAL A 458     4842   2032   2734    401    177   -592  A    O  
ATOM   3482  CB  VAL A 458      42.278 112.291 252.381  1.00 23.87      A    C  
ANISOU 3482  CB  VAL A 458     4371   1941   2759    307    159   -394  A    C  
ATOM   3483  CG1 VAL A 458      41.548 110.950 252.355  1.00 24.26      A    C  
ANISOU 3483  CG1 VAL A 458     4547   1848   2822    256    115   -449  A    C  
ATOM   3484  CG2 VAL A 458      43.129 112.389 253.648  1.00 19.89      A    C  
ANISOU 3484  CG2 VAL A 458     3774   1464   2319    358    205   -314  A    C  
ATOM   3485  N   PHE A 459      41.604 113.074 249.377  1.00 22.04      A    N  
ANISOU 3485  N   PHE A 459     4259   1790   2324    290    113   -516  A    N  
ATOM   3486  CA  PHE A 459      40.860 112.843 248.146  1.00 26.45      A    C  
ANISOU 3486  CA  PHE A 459     4923   2336   2790    246     54   -595  A    C  
ATOM   3487  C   PHE A 459      41.802 112.715 246.961  1.00 25.87      A    C  
ANISOU 3487  C   PHE A 459     4937   2295   2600    355    124   -639  A    C  
ATOM   3488  O   PHE A 459      41.603 111.858 246.100  1.00 30.04      A    O  
ANISOU 3488  O   PHE A 459     5599   2765   3051    361    106   -733  A    O  
ATOM   3489  CB  PHE A 459      39.832 113.947 247.885  1.00 23.11      A    C  
ANISOU 3489  CB  PHE A 459     4417   1999   2365    148    -27   -564  A    C  
ATOM   3490  CG  PHE A 459      39.049 113.751 246.612  1.00 21.98      A    C  
ANISOU 3490  CG  PHE A 459     4375   1859   2119     99   -102   -637  A    C  
ATOM   3491  CD1 PHE A 459      37.892 112.986 246.601  1.00 25.12      A    C  
ANISOU 3491  CD1 PHE A 459     4835   2174   2536     -4   -198   -700  A    C  
ATOM   3492  CD2 PHE A 459      39.469 114.338 245.428  1.00 21.23      A    C  
ANISOU 3492  CD2 PHE A 459     4308   1854   1903    152    -80   -639  A    C  
ATOM   3493  CE1 PHE A 459      37.168 112.804 245.419  1.00 26.32      A    C  
ANISOU 3493  CE1 PHE A 459     5079   2335   2588    -55   -282   -773  A    C  
ATOM   3494  CE2 PHE A 459      38.752 114.169 244.249  1.00 26.60      A    C  
ANISOU 3494  CE2 PHE A 459     5086   2550   2472    106   -158   -706  A    C  
ATOM   3495  CZ  PHE A 459      37.598 113.401 244.246  1.00 25.83      A    C  
ANISOU 3495  CZ  PHE A 459     5050   2370   2393      2   -264   -778  A    C  
ATOM   3496  N   GLU A 460      42.854 113.530 246.937  1.00 24.93      A    N  
ANISOU 3496  N   GLU A 460     4731   2271   2471    439    208   -572  A    N  
ATOM   3497  CA  GLU A 460      43.728 113.560 245.769  1.00 27.80      A    C  
ANISOU 3497  CA  GLU A 460     5158   2692   2715    539    286   -600  A    C  
ATOM   3498  C   GLU A 460      44.594 112.306 245.711  1.00 31.07      A    C  
ANISOU 3498  C   GLU A 460     5675   3013   3116    649    364   -667  A    C  
ATOM   3499  O   GLU A 460      45.108 111.943 244.652  1.00 29.85      A    O  
ANISOU 3499  O   GLU A 460     5579   2893   2868    713    412   -714  A    O  
ATOM   3500  CB  GLU A 460      44.611 114.816 245.781  1.00 27.28      A    C  
ANISOU 3500  CB  GLU A 460     4956   2754   2657    589    357   -496  A    C  
ATOM   3501  CG  GLU A 460      43.869 116.092 245.387  1.00 26.97      A    C  
ANISOU 3501  CG  GLU A 460     4841   2807   2599    504    291   -438  A    C  
ATOM   3502  CD  GLU A 460      43.513 116.107 243.907  1.00 39.22      A    C  
ANISOU 3502  CD  GLU A 460     6499   4408   3994    500    269   -486  A    C  
ATOM   3503  OE1 GLU A 460      44.393 116.434 243.081  1.00 43.27      A    O  
ANISOU 3503  OE1 GLU A 460     7023   5004   4415    581    355   -462  A    O  
ATOM   3504  OE2 GLU A 460      42.358 115.767 243.566  1.00 41.18      A    O1-
ANISOU 3504  OE2 GLU A 460     6820   4618   4208    416    166   -546  A    O1-
ATOM   3505  N   GLY A 461      44.745 111.652 246.857  1.00 28.19      A    N  
ANISOU 3505  N   GLY A 461     5270   2567   2873    649    362   -640  A    N  
ATOM   3506  CA  GLY A 461      45.580 110.473 246.962  1.00 28.90      A    C  
ANISOU 3506  CA  GLY A 461     5384   2596   3002    733    415   -658  A    C  
ATOM   3507  C   GLY A 461      47.043 110.831 247.132  1.00 27.75      A    C  
ANISOU 3507  C   GLY A 461     5156   2518   2870    862    528   -596  A    C  
ATOM   3508  O   GLY A 461      47.921 110.009 246.869  1.00 30.89      A    O  
ANISOU 3508  O   GLY A 461     5571   2893   3272    953    589   -617  A    O  
ATOM   3509  N   SER A 462      47.311 112.046 247.604  1.00 28.15      A    N  
ANISOU 3509  N   SER A 462     5107   2650   2939    869    555   -519  A    N  
ATOM   3510  CA  SER A 462      48.689 112.504 247.737  1.00 29.31      A    C  
ANISOU 3510  CA  SER A 462     5152   2879   3106    980    658   -451  A    C  
ATOM   3511  C   SER A 462      49.101 112.627 249.195  1.00 27.28      A    C  
ANISOU 3511  C   SER A 462     4782   2608   2974    988    654   -369  A    C  
ATOM   3512  O   SER A 462      50.273 112.868 249.491  1.00 26.70      A    O  
ANISOU 3512  O   SER A 462     4611   2593   2940   1077    727   -308  A    O  
ATOM   3513  CB  SER A 462      48.850 113.877 247.085  1.00 28.67      A    C  
ANISOU 3513  CB  SER A 462     4990   2937   2966    964    685   -398  A    C  
ATOM   3514  OG  SER A 462      47.978 114.816 247.688  1.00 28.19      A    O  
ANISOU 3514  OG  SER A 462     4841   2910   2962    840    596   -344  A    O  
ATOM   3515  N   ILE A 463      48.135 112.452 250.093  1.00 22.56      A    N  
ANISOU 3515  N   ILE A 463     4185   1949   2439    885    564   -362  A    N  
ATOM   3516  CA  ILE A 463      48.346 112.623 251.529  1.00 24.26      A    C  
ANISOU 3516  CA  ILE A 463     4290   2172   2758    866    542   -281  A    C  
ATOM   3517  C   ILE A 463      49.531 111.797 252.038  1.00 25.20      A    C  
ANISOU 3517  C   ILE A 463     4401   2247   2926    993    606   -252  A    C  
ATOM   3518  O   ILE A 463      49.683 110.622 251.684  1.00 24.89      A    O  
ANISOU 3518  O   ILE A 463     4441   2135   2882   1028    612   -295  A    O  
ATOM   3519  CB  ILE A 463      47.068 112.225 252.305  1.00 28.10      A    C  
ANISOU 3519  CB  ILE A 463     4813   2579   3285    746    447   -292  A    C  
ATOM   3520  CG1 ILE A 463      47.244 112.397 253.816  1.00 28.24      A    C  
ANISOU 3520  CG1 ILE A 463     4723   2619   3389    723    426   -210  A    C  
ATOM   3521  CG2 ILE A 463      46.653 110.800 251.962  1.00 25.79      A    C  
ANISOU 3521  CG2 ILE A 463     4677   2142   2980    754    431   -366  A    C  
ATOM   3522  CD1 ILE A 463      46.944 113.796 254.315  1.00 22.61      A    C  
ANISOU 3522  CD1 ILE A 463     3872   2022   2698    643    394   -164  A    C  
ATOM   3523  N   THR A 464      50.392 112.424 252.838  1.00 23.39      A    N  
ANISOU 3523  N   THR A 464     4028   2103   2756   1027    628   -166  A    N  
ATOM   3524  CA  THR A 464      51.501 111.702 253.459  1.00 25.61      A    C  
ANISOU 3524  CA  THR A 464     4270   2364   3096   1134    668   -119  A    C  
ATOM   3525  C   THR A 464      51.473 111.797 254.988  1.00 27.87      A    C  
ANISOU 3525  C   THR A 464     4474   2655   3458   1099    614    -40  A    C  
ATOM   3526  O   THR A 464      52.249 111.122 255.673  1.00 30.88      A    O  
ANISOU 3526  O   THR A 464     4830   3012   3893   1177    627     10  A    O  
ATOM   3527  CB  THR A 464      52.890 112.162 252.928  1.00 31.34      A    C  
ANISOU 3527  CB  THR A 464     4893   3197   3818   1235    755    -83  A    C  
ATOM   3528  CG2 THR A 464      53.073 111.784 251.451  1.00 22.28      A    C  
ANISOU 3528  CG2 THR A 464     3829   2049   2586   1278    813   -155  A    C  
ATOM   3529  OG1 THR A 464      53.028 113.579 253.095  1.00 23.96      A    O  
ANISOU 3529  OG1 THR A 464     3835   2376   2894   1198    759    -32  A    O  
ATOM   3530  N   ASP A 465      50.581 112.626 255.523  1.00 26.52      A    N  
ANISOU 3530  N   ASP A 465     4251   2535   3290    969    547    -28  A    N  
ATOM   3531  CA  ASP A 465      50.414 112.724 256.976  1.00 35.47      A    C  
ANISOU 3531  CA  ASP A 465     5312   3692   4475    915    490     35  A    C  
ATOM   3532  C   ASP A 465      49.425 111.690 257.527  1.00 31.54      A    C  
ANISOU 3532  C   ASP A 465     4920   3079   3986    855    439     26  A    C  
ATOM   3533  O   ASP A 465      49.255 111.573 258.737  1.00 32.32      A    O  
ANISOU 3533  O   ASP A 465     4977   3189   4115    815    398     84  A    O  
ATOM   3534  CB  ASP A 465      50.027 114.144 257.408  1.00 43.69      A    C  
ANISOU 3534  CB  ASP A 465     6233   4846   5521    815    451     51  A    C  
ATOM   3535  CG  ASP A 465      51.236 114.995 257.783  1.00 53.94      A    C  
ANISOU 3535  CG  ASP A 465     7383   6256   6854    865    476    108  A    C  
ATOM   3536  OD1 ASP A 465      52.352 114.445 257.910  1.00 56.28      A    O  
ANISOU 3536  OD1 ASP A 465     7656   6553   7176    975    517    148  A    O  
ATOM   3537  OD2 ASP A 465      51.067 116.218 257.965  1.00 60.72      A    O1-
ANISOU 3537  OD2 ASP A 465     8146   7199   7726    795    453    112  A    O1-
ATOM   3538  N   LEU A 466      48.773 110.958 256.625  1.00 27.86      A    N  
ANISOU 3538  N   LEU A 466     4590   2505   3490    844    440    -46  A    N  
ATOM   3539  CA  LEU A 466      47.976 109.785 256.983  1.00 25.94      A    C  
ANISOU 3539  CA  LEU A 466     4461   2126   3268    800    401    -57  A    C  
ATOM   3540  C   LEU A 466      48.413 108.624 256.122  1.00 28.92      A    C  
ANISOU 3540  C   LEU A 466     4948   2397   3643    887    437   -110  A    C  
ATOM   3541  O   LEU A 466      49.036 108.836 255.077  1.00 28.74      A    O  
ANISOU 3541  O   LEU A 466     4922   2421   3579    953    487   -157  A    O  
ATOM   3542  CB  LEU A 466      46.488 110.020 256.727  1.00 23.68      A    C  
ANISOU 3542  CB  LEU A 466     4219   1821   2959    656    340   -109  A    C  
ATOM   3543  CG  LEU A 466      45.771 111.076 257.545  1.00 25.30      A    C  
ANISOU 3543  CG  LEU A 466     4310   2133   3171    543    295    -73  A    C  
ATOM   3544  CD1 LEU A 466      44.349 111.232 257.038  1.00 22.95      A    C  
ANISOU 3544  CD1 LEU A 466     4057   1809   2854    421    243   -132  A    C  
ATOM   3545  CD2 LEU A 466      45.783 110.632 258.988  1.00 23.62      A    C  
ANISOU 3545  CD2 LEU A 466     4062   1914   2999    523    275      9  A    C  
ATOM   3546  N   PRO A 467      48.066 107.390 256.536  1.00 30.57      A    N  
ANISOU 3546  N   PRO A 467     5228   2490   3896    864    404   -101  A    N  
ATOM   3547  CA  PRO A 467      48.211 106.262 255.614  1.00 31.78      A    C  
ANISOU 3547  CA  PRO A 467     5471   2554   4051    903    417   -173  A    C  
ATOM   3548  C   PRO A 467      47.383 106.558 254.369  1.00 32.04      A    C  
ANISOU 3548  C   PRO A 467     5568   2594   4011    835    401   -279  A    C  
ATOM   3549  O   PRO A 467      46.333 107.195 254.488  1.00 33.21      A    O  
ANISOU 3549  O   PRO A 467     5716   2765   4139    723    352   -287  A    O  
ATOM   3550  CB  PRO A 467      47.613 105.089 256.401  1.00 34.23      A    C  
ANISOU 3550  CB  PRO A 467     5841   2735   4431    849    367   -139  A    C  
ATOM   3551  CG  PRO A 467      47.800 105.467 257.835  1.00 30.57      A    C  
ANISOU 3551  CG  PRO A 467     5302   2311   4003    845    354    -18  A    C  
ATOM   3552  CD  PRO A 467      47.606 106.960 257.870  1.00 28.79      A    C  
ANISOU 3552  CD  PRO A 467     5003   2211   3725    809    359    -17  A    C  
ATOM   3553  N   ASN A 468      47.880 106.175 253.196  1.00 29.04      A    N  
ANISOU 3553  N   ASN A 468     5238   2208   3588    904    442   -355  A    N  
ATOM   3554  CA  ASN A 468      47.249 106.563 251.938  1.00 30.01      A    C  
ANISOU 3554  CA  ASN A 468     5419   2362   3623    855    430   -448  A    C  
ATOM   3555  C   ASN A 468      46.734 105.339 251.189  1.00 32.66      A    C  
ANISOU 3555  C   ASN A 468     5871   2583   3956    829    400   -543  A    C  
ATOM   3556  O   ASN A 468      47.503 104.650 250.517  1.00 37.48      A    O  
ANISOU 3556  O   ASN A 468     6522   3162   4556    925    451   -593  A    O  
ATOM   3557  CB  ASN A 468      48.244 107.339 251.076  1.00 24.35      A    C  
ANISOU 3557  CB  ASN A 468     4660   1759   2835    953    510   -460  A    C  
ATOM   3558  CG  ASN A 468      47.632 107.845 249.785  1.00 30.89      A    C  
ANISOU 3558  CG  ASN A 468     5547   2633   3555    908    499   -541  A    C  
ATOM   3559  ND2 ASN A 468      48.477 108.334 248.886  1.00 33.22      A    N  
ANISOU 3559  ND2 ASN A 468     5825   3018   3779    994    574   -555  A    N  
ATOM   3560  OD1 ASN A 468      46.413 107.820 249.605  1.00 34.66      A    O  
ANISOU 3560  OD1 ASN A 468     6080   3074   4014    794    421   -583  A    O  
ATOM   3561  N   PRO A 469      45.433 105.040 251.326  1.00 34.05      A    N  
ANISOU 3561  N   PRO A 469     6094   2694   4150    699    318   -568  A    N  
ATOM   3562  CA  PRO A 469      44.918 103.848 250.638  1.00 41.38      A    C  
ANISOU 3562  CA  PRO A 469     7127   3508   5089    668    283   -661  A    C  
ATOM   3563  C   PRO A 469      44.811 104.025 249.125  1.00 37.23      A    C  
ANISOU 3563  C   PRO A 469     6666   3027   4453    678    290   -772  A    C  
ATOM   3564  O   PRO A 469      44.553 103.052 248.425  1.00 36.63      A    O  
ANISOU 3564  O   PRO A 469     6679   2865   4376    671    271   -864  A    O  
ATOM   3565  CB  PRO A 469      43.504 103.700 251.219  1.00 40.77      A    C  
ANISOU 3565  CB  PRO A 469     7054   3377   5059    513    193   -644  A    C  
ATOM   3566  CG  PRO A 469      43.532 104.457 252.513  1.00 38.26      A    C  
ANISOU 3566  CG  PRO A 469     6641   3114   4781    491    195   -528  A    C  
ATOM   3567  CD  PRO A 469      44.459 105.605 252.272  1.00 32.35      A    C  
ANISOU 3567  CD  PRO A 469     5830   2494   3969    581    258   -506  A    C  
ATOM   3568  N   LYS A 470      45.034 105.234 248.623  1.00 36.70      A    N  
ANISOU 3568  N   LYS A 470     6558   3092   4296    697    318   -762  A    N  
ATOM   3569  CA  LYS A 470      45.013 105.452 247.179  1.00 38.65      A    C  
ANISOU 3569  CA  LYS A 470     6868   3395   4422    715    330   -855  A    C  
ATOM   3570  C   LYS A 470      46.398 105.237 246.572  1.00 39.27      A    C  
ANISOU 3570  C   LYS A 470     6951   3507   4461    866    437   -877  A    C  
ATOM   3571  O   LYS A 470      46.602 105.395 245.367  1.00 40.52      A    O  
ANISOU 3571  O   LYS A 470     7158   3726   4512    903    469   -949  A    O  
ATOM   3572  CB  LYS A 470      44.465 106.840 246.844  1.00 36.15      A    C  
ANISOU 3572  CB  LYS A 470     6512   3198   4023    653    302   -832  A    C  
ATOM   3573  CG  LYS A 470      42.994 107.021 247.220  1.00 37.12      A    C  
ANISOU 3573  CG  LYS A 470     6633   3295   4178    499    192   -829  A    C  
ATOM   3574  CD  LYS A 470      42.402 108.283 246.589  1.00 38.81      A    C  
ANISOU 3574  CD  LYS A 470     6828   3618   4299    443    155   -829  A    C  
ATOM   3575  CE  LYS A 470      40.900 108.378 246.847  1.00 41.71      A    C  
ANISOU 3575  CE  LYS A 470     7185   3960   4703    290     40   -834  A    C  
ATOM   3576  NZ  LYS A 470      40.573 108.168 248.283  1.00 49.08      A    N1+
ANISOU 3576  NZ  LYS A 470     8050   4836   5764    236     22   -761  A    N1+
ATOM   3577  N   ALA A 471      47.349 104.890 247.430  1.00 37.33      A    N  
ANISOU 3577  N   ALA A 471     6647   3232   4304    953    490   -811  A    N  
ATOM   3578  CA  ALA A 471      48.717 104.637 247.008  1.00 41.83      A    C  
ANISOU 3578  CA  ALA A 471     7199   3833   4862   1098    592   -819  A    C  
ATOM   3579  C   ALA A 471      48.800 103.364 246.181  1.00 52.97      A    C  
ANISOU 3579  C   ALA A 471     8716   5143   6266   1140    603   -938  A    C  
ATOM   3580  O   ALA A 471      47.869 102.555 246.172  1.00 53.68      A    O  
ANISOU 3580  O   ALA A 471     8885   5119   6391   1057    528   -999  A    O  
ATOM   3581  CB  ALA A 471      49.624 104.527 248.213  1.00 40.15      A    C  
ANISOU 3581  CB  ALA A 471     6891   3608   4757   1171    629   -714  A    C  
ATOM   3582  N   LYS A 472      49.903 103.206 245.460  1.00 59.79      A    N  
ANISOU 3582  N   LYS A 472     9577   6051   7089   1264    697   -974  A    N  
ATOM   3583  CA  LYS A 472      50.219 101.918 244.863  1.00 66.25      A    C  
ANISOU 3583  CA  LYS A 472    10481   6762   7928   1330    723  -1083  A    C  
ATOM   3584  C   LYS A 472      51.725 101.699 244.871  1.00 66.90      A    C  
ANISOU 3584  C   LYS A 472    10498   6874   8045   1488    833  -1057  A    C  
ATOM   3585  O   LYS A 472      52.341 101.654 245.936  1.00 68.51      A    O  
ANISOU 3585  O   LYS A 472    10616   7062   8354   1535    847   -955  A    O  
ATOM   3586  CB  LYS A 472      49.658 101.777 243.452  1.00 69.61      A    C  
ANISOU 3586  CB  LYS A 472    11014   7207   8228   1296    711  -1221  A    C  
ATOM   3587  CG  LYS A 472      49.956 100.411 242.864  1.00 73.86      A    C  
ANISOU 3587  CG  LYS A 472    11644   7624   8796   1363    737  -1349  A    C  
ATOM   3588  CD  LYS A 472      49.628  99.312 243.874  1.00 71.44      A    C  
ANISOU 3588  CD  LYS A 472    11356   7136   8652   1334    678  -1333  A    C  
ATOM   3589  CE  LYS A 472      50.436  98.062 243.603  1.00 71.54      A    C  
ANISOU 3589  CE  LYS A 472    11415   7031   8737   1453    737  -1418  A    C  
ATOM   3590  NZ  LYS A 472      50.281  97.639 242.188  1.00 76.28      A    N1+
ANISOU 3590  NZ  LYS A 472    12120   7630   9231   1465    757  -1587  A    N1+
TER   
END



If you find results from this site helpful for your research, please cite one of our papers:

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.