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

Should you encounter any unexpected behaviour,
please let us know.


***  LIGASE 11-FEB-17 5N4W  ***

elNémo ID: 22060311222952297

Job options:

ID        	=	 22060311222952297
JOBID     	=	 LIGASE 11-FEB-17 5N4W
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    LIGASE                                  11-FEB-17   5N4W
TITLE     CRYSTAL STRUCTURE OF THE CUL2-RBX1-ELOBC-VHL UBIQUITIN
TITLE    2 LIGASE COMPLEX
EXPDTA    X-RAY DIFFRACTION
REMARK   2 RESOLUTION.    3.90 ANGSTROMS
REMARK   3  R VALUE : 0.302000
REMARK   3  FREE R VALUE : 0.346000
REMARK   4 5N4W COMPLIES WITH FORMAT V. 3.30,
REMARK 200  TEMPERATURE           (KELVIN) : 100.00
REMARK 200  PH                             : 7.60
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, V, R, B, C
REMARK 350   BIOMT1  1   1.000000 0.000000 0.000000   0.000000
REMARK 350   BIOMT2  1   0.000000 1.000000 0.000000   0.000000
REMARK 350   BIOMT3  1   0.000000 0.000000 1.000000   0.000000
REMARK 888
REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC)
CRYST1   86.038  190.962  238.885  90.00  90.00  90.00 C 2 2 21      8
ATOM      1  N   MET A   1     -30.158  17.108 -80.703  1.00256.96           N  
ANISOU    1  N   MET A   1    32803  34676  30153   3333  -2020  -2136
ATOM      2  CA  MET A   1     -30.400  18.416 -81.302  1.00258.45           C  
ANISOU    2  CA  MET A   1    33206  34796  30198   3603  -1429  -2328
ATOM      3  C   MET A   1     -29.633  19.510 -80.568  1.00260.86           C  
ANISOU    3  C   MET A   1    33214  35440  30461   3317   -661  -2439
ATOM      4  O   MET A   1     -28.525  19.285 -80.085  1.00261.63           O  
ANISOU    4  O   MET A   1    33137  35678  30594   3153   -504  -2438
ATOM      5  CB  MET A   1     -31.896  18.735 -81.306  1.00256.17           C  
ANISOU    5  CB  MET A   1    32869  34526  29939   3528  -1635  -2284
ATOM      6  CG  MET A   1     -32.716  17.839 -82.216  1.00253.14           C  
ANISOU    6  CG  MET A   1    32837  33758  29587   3889  -2342  -2222
ATOM      7  SD  MET A   1     -32.202  17.971 -83.939  1.00254.38           S  
ANISOU    7  SD  MET A   1    33742  33375  29535   4726  -2219  -2420
ATOM      8  CE  MET A   1     -32.727  19.641 -84.320  1.00254.53           C  
ANISOU    8  CE  MET A   1    33888  33429  29394   4913  -1505  -2614
ATOM      9  N   SER A   2     -30.228  20.696 -80.494  1.00259.13           N  
ANISOU    9  N   SER A   2    32941  35346  30169   3261   -191  -2538
ATOM     10  CA  SER A   2     -29.616  21.810 -79.789  1.00260.78           C  
ANISOU   10  CA  SER A   2    32871  35875  30338   2975    544  -2651
ATOM     11  C   SER A   2     -29.745  21.620 -78.279  1.00261.54           C  
ANISOU   11  C   SER A   2    32384  36430  30561   2288    437  -2500
ATOM     12  O   SER A   2     -30.408  20.701 -77.792  1.00259.32           O  
ANISOU   12  O   SER A   2    31916  36217  30398   2037   -173  -2304
ATOM     13  CB  SER A   2     -30.254  23.130 -80.218  1.00259.61           C  
ANISOU   13  CB  SER A   2    32880  35698  30063   3152   1075  -2801
ATOM     14  OG  SER A   2     -29.697  24.222 -79.506  1.00260.50           O  
ANISOU   14  OG  SER A   2    32717  36119  30141   2854   1787  -2913
ATOM     15  N   LEU A   3     -29.096  22.513 -77.531  1.00260.35           N  
ANISOU   15  N   LEU A   3    31951  36587  30384   1985   1047  -2596
ATOM     16  CA  LEU A   3     -29.199  22.477 -76.077  1.00260.17           C  
ANISOU   16  CA  LEU A   3    31395  37008  30449   1341   1017  -2473
ATOM     17  C   LEU A   3     -30.548  22.963 -75.565  1.00258.85           C  
ANISOU   17  C   LEU A   3    31033  37023  30294   1062    996  -2390
ATOM     18  O   LEU A   3     -30.749  22.985 -74.345  1.00257.72           O  
ANISOU   18  O   LEU A   3    30464  37244  30212    529    989  -2279
ATOM     19  CB  LEU A   3     -28.064  23.293 -75.448  1.00261.47           C  
ANISOU   19  CB  LEU A   3    31330  37436  30582   1112   1667  -2616
ATOM     20  CG  LEU A   3     -27.881  24.765 -75.826  1.00260.79           C  
ANISOU   20  CG  LEU A   3    31372  37342  30374   1275   2463  -2846
ATOM     21  CD1 LEU A   3     -28.782  25.667 -75.019  1.00259.93           C  
ANISOU   21  CD1 LEU A   3    30986  37539  30235    888   2742  -2830
ATOM     22  CD2 LEU A   3     -26.436  25.173 -75.624  1.00258.56           C  
ANISOU   22  CD2 LEU A   3    30994  37151  30097   1234   2965  -3000
ATOM     23  N   LYS A   4     -31.461  23.360 -76.449  1.00265.79           N  
ANISOU   23  N   LYS A   4    32214  37661  31115   1412    993  -2441
ATOM     24  CA  LYS A   4     -32.806  23.697 -76.019  1.00264.31           C  
ANISOU   24  CA  LYS A   4    31842  37619  30967   1173    899  -2344
ATOM     25  C   LYS A   4     -33.478  22.463 -75.421  1.00261.63           C  
ANISOU   25  C   LYS A   4    31266  37342  30799    873    154  -2092
ATOM     26  O   LYS A   4     -33.220  21.335 -75.852  1.00261.16           O  
ANISOU   26  O   LYS A   4    31366  37058  30803   1060   -384  -2014
ATOM     27  CB  LYS A   4     -33.630  24.237 -77.188  1.00264.17           C  
ANISOU   27  CB  LYS A   4    32222  37288  30861   1662    963  -2447
ATOM     28  CG  LYS A   4     -33.189  25.609 -77.673  1.00265.34           C  
ANISOU   28  CG  LYS A   4    32576  37403  30836   1913   1757  -2683
ATOM     29  CD  LYS A   4     -34.027  26.078 -78.851  1.00264.25           C  
ANISOU   29  CD  LYS A   4    32862  36941  30600   2426   1777  -2776
ATOM     30  CE  LYS A   4     -35.441  26.434 -78.415  1.00263.22           C  
ANISOU   30  CE  LYS A   4    32515  36967  30528   2189   1661  -2676
ATOM     31  NZ  LYS A   4     -35.469  27.642 -77.544  1.00263.75           N1+
ANISOU   31  NZ  LYS A   4    32283  37391  30541   1818   2332  -2734
ATOM     32  N   PRO A   5     -34.338  22.645 -74.419  1.00264.82           N  
ANISOU   32  N   PRO A   5    31295  38042  31283    408    121  -1957
ATOM     33  CA  PRO A   5     -34.902  21.487 -73.715  1.00262.33           C  
ANISOU   33  CA  PRO A   5    30718  37812  31144     72   -532  -1708
ATOM     34  C   PRO A   5     -35.817  20.656 -74.599  1.00260.91           C  
ANISOU   34  C   PRO A   5    30787  37280  31067    391  -1176  -1623
ATOM     35  O   PRO A   5     -36.905  21.101 -74.977  1.00260.57           O  
ANISOU   35  O   PRO A   5    30810  37149  31046    508  -1193  -1630
ATOM     36  CB  PRO A   5     -35.676  22.128 -72.558  1.00260.80           C  
ANISOU   36  CB  PRO A   5    30114  37989  30989   -440   -287  -1612
ATOM     37  CG  PRO A   5     -35.088  23.490 -72.400  1.00262.25           C  
ANISOU   37  CG  PRO A   5    30282  38353  31008   -465    509  -1813
ATOM     38  CD  PRO A   5     -34.741  23.913 -73.791  1.00264.44           C  
ANISOU   38  CD  PRO A   5    31029  38279  31168    139    717  -2020
ATOM     39  N   ARG A   6     -35.381  19.445 -74.930  1.00260.78           N  
ANISOU   39  N   ARG A   6    30908  37059  31118    534  -1717  -1545
ATOM     40  CA  ARG A   6     -36.137  18.537 -75.777  1.00258.24           C  
ANISOU   40  CA  ARG A   6    30838  36381  30899    840  -2380  -1469
ATOM     41  C   ARG A   6     -36.527  17.302 -74.978  1.00254.71           C  
ANISOU   41  C   ARG A   6    30100  36022  30655    455  -3008  -1217
ATOM     42  O   ARG A   6     -35.709  16.747 -74.236  1.00254.95           O  
ANISOU   42  O   ARG A   6    29937  36229  30703    183  -3063  -1132
ATOM     43  CB  ARG A   6     -35.327  18.126 -77.012  1.00259.19           C  
ANISOU   43  CB  ARG A   6    31449  36115  30917   1411  -2503  -1601
ATOM     44  CG  ARG A   6     -34.901  19.288 -77.897  1.00261.38           C  
ANISOU   44  CG  ARG A   6    32066  36254  30991   1843  -1884  -1849
ATOM     45  CD  ARG A   6     -36.092  19.928 -78.593  1.00259.90           C  
ANISOU   45  CD  ARG A   6    32069  35903  30779   2104  -1871  -1914
ATOM     46  NE  ARG A   6     -35.690  21.045 -79.443  1.00260.75           N  
ANISOU   46  NE  ARG A   6    32525  35869  30680   2530  -1262  -2148
ATOM     47  CZ  ARG A   6     -35.364  20.929 -80.726  1.00259.05           C  
ANISOU   47  CZ  ARG A   6    32830  35252  30345   3128  -1324  -2279
ATOM     48  NH1 ARG A   6     -35.391  19.740 -81.314  1.00256.58           N  
ANISOU   48  NH1 ARG A   6    32752  34641  30097   3369  -1983  -2204
ATOM     49  NH2 ARG A   6     -35.010  22.000 -81.422  1.00259.48           N1+
ANISOU   49  NH2 ARG A   6    33187  35193  30211   3492   -719  -2484
ATOM     50  N   VAL A   7     -37.780  16.877 -75.128  1.00249.62           N  
ANISOU   50  N   VAL A   7    29421  35252  30172    436  -3477  -1097
ATOM     51  CA  VAL A   7     -38.265  15.654 -74.494  1.00250.76           C  
ANISOU   51  CA  VAL A   7    29324  35419  30533    112  -4110   -854
ATOM     52  C   VAL A   7     -37.684  14.484 -75.284  1.00251.81           C  
ANISOU   52  C   VAL A   7    29786  35211  30680    453  -4640   -847
ATOM     53  O   VAL A   7     -38.145  14.166 -76.381  1.00252.94           O  
ANISOU   53  O   VAL A   7    30276  34986  30844    879  -4998   -905
ATOM     54  CB  VAL A   7     -39.793  15.601 -74.441  1.00251.83           C  
ANISOU   54  CB  VAL A   7    29310  35509  30865     -9  -4424   -738
ATOM     55  CG1 VAL A   7     -40.258  14.281 -73.844  1.00253.21           C  
ANISOU   55  CG1 VAL A   7    29256  35670  31281   -324  -5082   -488
ATOM     56  CG2 VAL A   7     -40.336  16.778 -73.642  1.00250.80           C  
ANISOU   56  CG2 VAL A   7    28861  35719  30713   -342  -3867   -741
ATOM     57  N   VAL A   8     -36.664  13.839 -74.723  1.00246.95           N  
ANISOU   57  N   VAL A   8    29069  34715  30047    275  -4698   -777
ATOM     58  CA  VAL A   8     -35.920  12.785 -75.404  1.00246.53           C  
ANISOU   58  CA  VAL A   8    29323  34366  29981    592  -5119   -775
ATOM     59  C   VAL A   8     -36.419  11.436 -74.904  1.00247.85           C  
ANISOU   59  C   VAL A   8    29316  34493  30363    323  -5816   -532
ATOM     60  O   VAL A   8     -36.952  11.319 -73.793  1.00247.86           O  
ANISOU   60  O   VAL A   8    28909  34772  30493   -176  -5865   -359
ATOM     61  CB  VAL A   8     -34.401  12.964 -75.174  1.00249.39           C  
ANISOU   61  CB  VAL A   8    29699  34869  30188    608  -4711   -867
ATOM     62  CG1 VAL A   8     -33.587  11.886 -75.885  1.00248.30           C  
ANISOU   62  CG1 VAL A   8    29885  34422  30035    952  -5117   -862
ATOM     63  CG2 VAL A   8     -33.955  14.351 -75.620  1.00252.89           C  
ANISOU   63  CG2 VAL A   8    30289  35355  30443    843  -3984  -1106
ATOM     64  N   ASP A   9     -36.262  10.409 -75.739  1.00249.92           N  
ANISOU   64  N   ASP A   9    29907  34391  30661    663  -6353   -516
ATOM     65  CA  ASP A   9     -36.671   9.057 -75.384  1.00247.87           C  
ANISOU   65  CA  ASP A   9    29535  34041  30605    456  -7037   -295
ATOM     66  C   ASP A   9     -35.966   8.588 -74.113  1.00247.23           C  
ANISOU   66  C   ASP A   9    29098  34292  30548    -13  -6990   -135
ATOM     67  O   ASP A   9     -34.960   9.154 -73.678  1.00248.75           O  
ANISOU   67  O   ASP A   9    29199  34727  30588    -96  -6496   -214
ATOM     68  CB  ASP A   9     -36.367   8.090 -76.530  1.00247.80           C  
ANISOU   68  CB  ASP A   9    29985  33584  30585    939  -7549   -334
ATOM     69  CG  ASP A   9     -37.228   8.343 -77.752  1.00248.19           C  
ANISOU   69  CG  ASP A   9    30390  33273  30637   1386  -7745   -462
ATOM     70  OD1 ASP A   9     -38.370   8.823 -77.590  1.00248.60           O  
ANISOU   70  OD1 ASP A   9    30260  33390  30805   1233  -7747   -440
ATOM     71  OD2 ASP A   9     -36.762   8.060 -78.876  1.00248.49           O1-
ANISOU   71  OD2 ASP A   9    30898  32958  30561   1900  -7898   -585
ATOM     72  N   PHE A  10     -36.508   7.524 -73.520  1.00240.94           N  
ANISOU   72  N   PHE A  10    28103  33494  29951   -316  -7521     92
ATOM     73  CA  PHE A  10     -36.000   6.999 -72.260  1.00240.79           C  
ANISOU   73  CA  PHE A  10    27744  33780  29966   -778  -7537    272
ATOM     74  C   PHE A  10     -35.137   5.754 -72.427  1.00241.68           C  
ANISOU   74  C   PHE A  10    28030  33719  30078   -649  -7967    350
ATOM     75  O   PHE A  10     -34.499   5.331 -71.457  1.00241.53           O  
ANISOU   75  O   PHE A  10    27776  33945  30049   -969  -7951    475
ATOM     76  CB  PHE A  10     -37.165   6.696 -71.306  1.00241.63           C  
ANISOU   76  CB  PHE A  10    27473  34043  30293  -1259  -7768    495
ATOM     77  CG  PHE A  10     -38.092   5.617 -71.793  1.00243.65           C  
ANISOU   77  CG  PHE A  10    27848  33954  30773  -1162  -8413    612
ATOM     78  CD1 PHE A  10     -39.152   5.922 -72.631  1.00244.38           C  
ANISOU   78  CD1 PHE A  10    28079  33805  30970   -932  -8580    539
ATOM     79  CD2 PHE A  10     -37.922   4.303 -71.389  1.00244.94           C  
ANISOU   79  CD2 PHE A  10    28045  34011  31010  -1241  -8532    732
ATOM     80  CE1 PHE A  10     -40.011   4.934 -73.075  1.00246.43           C  
ANISOU   80  CE1 PHE A  10    28494  33733  31404   -812  -8850    596
ATOM     81  CE2 PHE A  10     -38.779   3.312 -71.827  1.00246.92           C  
ANISOU   81  CE2 PHE A  10    28457  33928  31435  -1125  -8806    793
ATOM     82  CZ  PHE A  10     -39.824   3.627 -72.671  1.00247.70           C  
ANISOU   82  CZ  PHE A  10    28678  33797  31640   -925  -8962    728
ATOM     83  N   ASP A  11     -35.100   5.159 -73.619  1.00241.95           N  
ANISOU   83  N   ASP A  11    28478  33335  30115   -182  -8351    281
ATOM     84  CA  ASP A  11     -34.235   4.019 -73.893  1.00242.12           C  
ANISOU   84  CA  ASP A  11    28714  33162  30118     -2  -8734    340
ATOM     85  C   ASP A  11     -33.127   4.318 -74.889  1.00243.80           C  
ANISOU   85  C   ASP A  11    29322  33185  30127    508  -8480    131
ATOM     86  O   ASP A  11     -32.089   3.654 -74.852  1.00244.37           O  
ANISOU   86  O   ASP A  11    29483  33225  30141    590  -8576    163
ATOM     87  CB  ASP A  11     -35.055   2.831 -74.414  1.00243.98           C  
ANISOU   87  CB  ASP A  11    29159  33031  30510    112  -9026    440
ATOM     88  CG  ASP A  11     -35.907   2.192 -73.337  1.00244.66           C  
ANISOU   88  CG  ASP A  11    28907  33267  30783   -356  -9021    636
ATOM     89  OD1 ASP A  11     -35.520   2.259 -72.151  1.00244.23           O  
ANISOU   89  OD1 ASP A  11    28524  33560  30710   -733  -8823    724
ATOM     90  OD2 ASP A  11     -36.959   1.610 -73.678  1.00246.08           O1-
ANISOU   90  OD2 ASP A  11    29170  33198  31132   -330  -9213    689
ATOM     91  N   GLU A  12     -33.327   5.294 -75.780  1.00239.72           N  
ANISOU   91  N   GLU A  12    29047  32532  29502    859  -8152    -76
ATOM     92  CA  GLU A  12     -32.299   5.654 -76.752  1.00241.09           C  
ANISOU   92  CA  GLU A  12    29611  32510  29481   1360  -7855   -277
ATOM     93  C   GLU A  12     -30.992   6.015 -76.059  1.00242.84           C  
ANISOU   93  C   GLU A  12    29636  33042  29592   1197  -7366   -313
ATOM     94  O   GLU A  12     -29.943   5.417 -76.324  1.00243.56           O  
ANISOU   94  O   GLU A  12    29901  33017  29625   1402  -7444   -320
ATOM     95  CB  GLU A  12     -32.787   6.816 -77.620  1.00242.57           C  
ANISOU   95  CB  GLU A  12    30028  32571  29566   1690  -7486   -486
ATOM     96  CG  GLU A  12     -31.798   7.245 -78.690  1.00245.08           C  
ANISOU   96  CG  GLU A  12    30783  32654  29683   2238  -7145   -697
ATOM     97  CD  GLU A  12     -32.317   8.387 -79.539  1.00246.90           C  
ANISOU   97  CD  GLU A  12    31258  32752  29802   2572  -6780   -896
ATOM     98  OE1 GLU A  12     -33.446   8.856 -79.281  1.00246.94           O  
ANISOU   98  OE1 GLU A  12    31077  32860  29890   2372  -6797   -872
ATOM     99  OE2 GLU A  12     -31.596   8.820 -80.463  1.00248.65           O1-
ANISOU   99  OE2 GLU A  12    31862  32760  29855   3042  -6464  -1074
ATOM    100  N   THR A  13     -31.037   7.000 -75.161  1.00237.37           N  
ANISOU  100  N   THR A  13    28575  32743  28873    828  -6859   -339
ATOM    101  CA  THR A  13     -29.846   7.379 -74.413  1.00239.64           C  
ANISOU  101  CA  THR A  13    28634  33347  29071    630  -6407   -379
ATOM    102  C   THR A  13     -29.473   6.345 -73.360  1.00237.51           C  
ANISOU  102  C   THR A  13    28079  33274  28890    245  -6754   -164
ATOM    103  O   THR A  13     -28.313   6.301 -72.938  1.00238.76           O  
ANISOU  103  O   THR A  13    28135  33600  28982    184  -6543   -187
ATOM    104  CB  THR A  13     -30.053   8.741 -73.748  1.00241.24           C  
ANISOU  104  CB  THR A  13    28537  33906  29215    340  -5778   -474
ATOM    105  OG1 THR A  13     -31.143   8.661 -72.820  1.00238.33           O  
ANISOU  105  OG1 THR A  13    27827  33754  28971   -123  -5962   -303
ATOM    106  CG2 THR A  13     -30.363   9.803 -74.793  1.00242.96           C  
ANISOU  106  CG2 THR A  13    29051  33931  29331    738  -5396   -691
ATOM    107  N   TRP A  14     -30.422   5.506 -72.940  1.00235.99           N  
ANISOU  107  N   TRP A  14    27762  33053  28852     -6  -7283     42
ATOM    108  CA  TRP A  14     -30.162   4.582 -71.844  1.00234.79           C  
ANISOU  108  CA  TRP A  14    27323  33108  28780   -405  -7583    259
ATOM    109  C   TRP A  14     -29.437   3.322 -72.300  1.00234.19           C  
ANISOU  109  C   TRP A  14    27498  32766  28716   -150  -8049    332
ATOM    110  O   TRP A  14     -28.747   2.688 -71.495  1.00234.35           O  
ANISOU  110  O   TRP A  14    27331  32968  28742   -384  -8162    458
ATOM    111  CB  TRP A  14     -31.472   4.212 -71.147  1.00233.30           C  
ANISOU  111  CB  TRP A  14    26881  32999  28763   -799  -7919    462
ATOM    112  CG  TRP A  14     -31.277   3.323 -69.962  1.00232.32           C  
ANISOU  112  CG  TRP A  14    26476  33086  28710  -1209  -8132    679
ATOM    113  CD1 TRP A  14     -31.561   1.992 -69.878  1.00232.06           C  
ANISOU  113  CD1 TRP A  14    26565  32821  28785  -1163  -8338    783
ATOM    114  CD2 TRP A  14     -30.724   3.697 -68.695  1.00232.17           C  
ANISOU  114  CD2 TRP A  14    26090  33499  28624  -1628  -7812    732
ATOM    115  NE1 TRP A  14     -31.235   1.517 -68.631  1.00232.00           N  
ANISOU  115  NE1 TRP A  14    26314  33040  28795  -1497  -8207    887
ATOM    116  CE2 TRP A  14     -30.717   2.543 -67.886  1.00231.03           C  
ANISOU  116  CE2 TRP A  14    25906  33304  28571  -1767  -7885    847
ATOM    117  CE3 TRP A  14     -30.241   4.896 -68.164  1.00232.72           C  
ANISOU  117  CE3 TRP A  14    25946  33915  28560  -1800  -7216    605
ATOM    118  CZ2 TRP A  14     -30.246   2.554 -66.576  1.00230.40           C  
ANISOU  118  CZ2 TRP A  14    25555  33521  28466  -2119  -7641    906
ATOM    119  CZ3 TRP A  14     -29.774   4.905 -66.863  1.00231.45           C  
ANISOU  119  CZ3 TRP A  14    25447  34137  28358  -2226  -7067    703
ATOM    120  CH2 TRP A  14     -29.779   3.742 -66.084  1.00230.34           C  
ANISOU  120  CH2 TRP A  14    25292  33896  28329  -2351  -7273    841
ATOM    121  N   ASN A  15     -29.575   2.938 -73.570  1.00230.61           N  
ANISOU  121  N   ASN A  15    27479  31883  28261    333  -8326    258
ATOM    122  CA  ASN A  15     -28.843   1.776 -74.064  1.00230.60           C  
ANISOU  122  CA  ASN A  15    27751  31610  28256    609  -8740    317
ATOM    123  C   ASN A  15     -27.362   2.094 -74.226  1.00232.55           C  
ANISOU  123  C   ASN A  15    28077  31923  28357    826  -8327    183
ATOM    124  O   ASN A  15     -26.503   1.454 -73.606  1.00232.79           O  
ANISOU  124  O   ASN A  15    27967  32093  28388    680  -8422    284
ATOM    125  CB  ASN A  15     -29.445   1.294 -75.385  1.00230.07           C  
ANISOU  125  CB  ASN A  15    28147  31051  28219   1055  -9009    271
ATOM    126  CG  ASN A  15     -30.786   0.614 -75.199  1.00230.10           C  
ANISOU  126  CG  ASN A  15    28075  30948  28404    808  -9148    425
ATOM    127  OD1 ASN A  15     -30.977  -0.159 -74.260  1.00230.75           O  
ANISOU  127  OD1 ASN A  15    27904  31184  28586    436  -9164    599
ATOM    128  ND2 ASN A  15     -31.724   0.895 -76.096  1.00230.97           N  
ANISOU  128  ND2 ASN A  15    28419  30782  28555   1048  -9248    339
ATOM    129  N   LYS A  16     -27.043   3.090 -75.056  1.00223.69           N  
ANISOU  129  N   LYS A  16    27178  30698  27116   1180  -7857    -44
ATOM    130  CA  LYS A  16     -25.648   3.472 -75.246  1.00226.54           C  
ANISOU  130  CA  LYS A  16    27603  31108  27363   1392  -7416   -183
ATOM    131  C   LYS A  16     -25.053   4.029 -73.958  1.00227.53           C  
ANISOU  131  C   LYS A  16    27249  31722  27480    927  -7011   -171
ATOM    132  O   LYS A  16     -23.875   3.799 -73.659  1.00228.64           O  
ANISOU  132  O   LYS A  16    27307  31973  27593    930  -6889   -179
ATOM    133  CB  LYS A  16     -25.531   4.492 -76.379  1.00229.40           C  
ANISOU  133  CB  LYS A  16    28301  31253  27608   1851  -6961   -427
ATOM    134  CG  LYS A  16     -24.100   4.863 -76.721  1.00232.64           C  
ANISOU  134  CG  LYS A  16    28819  31651  27924   2125  -6499   -576
ATOM    135  CD  LYS A  16     -23.386   3.687 -77.368  1.00231.45           C  
ANISOU  135  CD  LYS A  16    28991  31173  27774   2482  -6900   -511
ATOM    136  CE  LYS A  16     -21.981   4.058 -77.801  1.00234.67           C  
ANISOU  136  CE  LYS A  16    29525  31531  28109   2794  -6428   -661
ATOM    137  NZ  LYS A  16     -21.110   4.317 -76.624  1.00237.04           N1+
ANISOU  137  NZ  LYS A  16    29349  32267  28449   2384  -6124   -642
ATOM    138  N   LEU A  17     -25.856   4.761 -73.180  1.00226.83           N  
ANISOU  138  N   LEU A  17    26842  31927  27415    530  -6806   -153
ATOM    139  CA  LEU A  17     -25.381   5.275 -71.900  1.00226.86           C  
ANISOU  139  CA  LEU A  17    26398  32396  27402     67  -6455   -136
ATOM    140  C   LEU A  17     -25.082   4.139 -70.931  1.00225.73           C  
ANISOU  140  C   LEU A  17    26029  32412  27327   -253  -6888     89
ATOM    141  O   LEU A  17     -24.065   4.163 -70.230  1.00226.25           O  
ANISOU  141  O   LEU A  17    25877  32733  27356   -419  -6698     81
ATOM    142  CB  LEU A  17     -26.412   6.241 -71.312  1.00225.87           C  
ANISOU  142  CB  LEU A  17    26018  32519  27285   -274  -6178   -148
ATOM    143  CG  LEU A  17     -26.059   7.080 -70.080  1.00225.52           C  
ANISOU  143  CG  LEU A  17    25545  32948  27193   -729  -5708   -176
ATOM    144  CD1 LEU A  17     -26.820   8.394 -70.117  1.00225.58           C  
ANISOU  144  CD1 LEU A  17    25484  33068  27157   -806  -5235   -305
ATOM    145  CD2 LEU A  17     -26.368   6.338 -68.787  1.00223.54           C  
ANISOU  145  CD2 LEU A  17    24956  32965  27014  -1227  -6050     66
ATOM    146  N   LEU A  18     -25.958   3.132 -70.880  1.00226.65           N  
ANISOU  146  N   LEU A  18    26196  32372  27549   -339  -7475    288
ATOM    147  CA  LEU A  18     -25.743   2.001 -69.982  1.00225.39           C  
ANISOU  147  CA  LEU A  18    25849  32335  27453   -632  -7903    515
ATOM    148  C   LEU A  18     -24.507   1.206 -70.386  1.00226.54           C  
ANISOU  148  C   LEU A  18    26189  32322  27564   -332  -8068    510
ATOM    149  O   LEU A  18     -23.660   0.885 -69.543  1.00227.33           O  
ANISOU  149  O   LEU A  18    26061  32669  27643   -545  -8052    579
ATOM    150  CB  LEU A  18     -26.986   1.107 -69.960  1.00223.33           C  
ANISOU  150  CB  LEU A  18    25651  31880  27326   -726  -8338    687
ATOM    151  CG  LEU A  18     -27.043  -0.043 -68.947  1.00221.13           C  
ANISOU  151  CG  LEU A  18    25243  31663  27114   -973  -8365    838
ATOM    152  CD1 LEU A  18     -28.478  -0.296 -68.525  1.00221.72           C  
ANISOU  152  CD1 LEU A  18    25241  31677  27325  -1195  -8387    927
ATOM    153  CD2 LEU A  18     -26.441  -1.321 -69.517  1.00222.50           C  
ANISOU  153  CD2 LEU A  18    25710  31540  27291   -668  -8607    894
ATOM    154  N   THR A  19     -24.390   0.871 -71.675  1.00225.49           N  
ANISOU  154  N   THR A  19    26486  31770  27420    173  -8233    430
ATOM    155  CA  THR A  19     -23.200   0.165 -72.140  1.00226.98           C  
ANISOU  155  CA  THR A  19    26885  31784  27573    496  -8349    418
ATOM    156  C   THR A  19     -21.940   0.991 -71.915  1.00230.19           C  
ANISOU  156  C   THR A  19    27138  32427  27897    525  -7768    251
ATOM    157  O   THR A  19     -20.855   0.429 -71.726  1.00231.59           O  
ANISOU  157  O   THR A  19    27285  32638  28068    589  -7827    285
ATOM    158  CB  THR A  19     -23.342  -0.200 -73.619  1.00227.22           C  
ANISOU  158  CB  THR A  19    27436  31309  27587   1058  -8569    342
ATOM    159  OG1 THR A  19     -23.516   0.991 -74.396  1.00229.05           O  
ANISOU  159  OG1 THR A  19    27832  31454  27744   1317  -8093    118
ATOM    160  CG2 THR A  19     -24.535  -1.123 -73.828  1.00224.31           C  
ANISOU  160  CG2 THR A  19    27212  30694  27321   1000  -8972    504
ATOM    161  N   THR A  20     -22.063   2.321 -71.923  1.00224.00           N  
ANISOU  161  N   THR A  20    26246  31804  27060    476  -7204     70
ATOM    162  CA  THR A  20     -20.919   3.163 -71.593  1.00227.79           C  
ANISOU  162  CA  THR A  20    26529  32536  27486    441  -6635    -92
ATOM    163  C   THR A  20     -20.582   3.073 -70.108  1.00226.43           C  
ANISOU  163  C   THR A  20    25888  32814  27329    -82  -6628     17
ATOM    164  O   THR A  20     -19.404   3.080 -69.734  1.00228.77           O  
ANISOU  164  O   THR A  20    26031  33275  27616   -102  -6446    -33
ATOM    165  CB  THR A  20     -21.195   4.611 -72.001  1.00230.23           C  
ANISOU  165  CB  THR A  20    26861  32882  27734    524  -6034   -314
ATOM    166  OG1 THR A  20     -21.467   4.668 -73.407  1.00230.26           O  
ANISOU  166  OG1 THR A  20    27332  32450  27704   1044  -6050   -417
ATOM    167  CG2 THR A  20     -19.991   5.491 -71.694  1.00233.80           C  
ANISOU  167  CG2 THR A  20    27110  33573  28150    491  -5436   -494
ATOM    168  N   ILE A  21     -21.602   2.984 -69.249  1.00225.65           N  
ANISOU  168  N   ILE A  21    25563  32914  27260   -502  -6826    168
ATOM    169  CA  ILE A  21     -21.362   2.755 -67.824  1.00223.29           C  
ANISOU  169  CA  ILE A  21    24863  33014  26962   -988  -6889    301
ATOM    170  C   ILE A  21     -20.607   1.448 -67.621  1.00222.20           C  
ANISOU  170  C   ILE A  21    24760  32812  26855   -932  -7347    458
ATOM    171  O   ILE A  21     -19.566   1.404 -66.953  1.00223.23           O  
ANISOU  171  O   ILE A  21    24674  33184  26959  -1056  -7229    444
ATOM    172  CB  ILE A  21     -22.690   2.757 -67.045  1.00220.21           C  
ANISOU  172  CB  ILE A  21    24282  32780  26608  -1404  -7065    462
ATOM    173  CG1 ILE A  21     -23.395   4.107 -67.163  1.00220.77           C  
ANISOU  173  CG1 ILE A  21    24290  32948  26643  -1477  -6577    307
ATOM    174  CG2 ILE A  21     -22.449   2.410 -65.583  1.00218.12           C  
ANISOU  174  CG2 ILE A  21    23649  32898  26329  -1881  -7166    620
ATOM    175  CD1 ILE A  21     -22.630   5.243 -66.546  1.00222.25           C  
ANISOU  175  CD1 ILE A  21    24213  33486  26746  -1662  -5978    133
ATOM    176  N   LYS A  22     -21.127   0.361 -68.198  1.00221.93           N  
ANISOU  176  N   LYS A  22    25000  32444  26880   -740  -7884    607
ATOM    177  CA  LYS A  22     -20.476  -0.938 -68.063  1.00221.24           C  
ANISOU  177  CA  LYS A  22    24992  32252  26819   -650  -8283    751
ATOM    178  C   LYS A  22     -19.081  -0.929 -68.677  1.00224.13           C  
ANISOU  178  C   LYS A  22    25484  32523  27154   -287  -8138    625
ATOM    179  O   LYS A  22     -18.207  -1.690 -68.245  1.00224.34           O  
ANISOU  179  O   LYS A  22    25429  32624  27186   -307  -8338    718
ATOM    180  CB  LYS A  22     -21.347  -2.018 -68.707  1.00220.36           C  
ANISOU  180  CB  LYS A  22    25231  31734  26763   -424  -8522    837
ATOM    181  CG  LYS A  22     -20.852  -3.441 -68.518  1.00220.12           C  
ANISOU  181  CG  LYS A  22    25318  31570  26747   -333  -8687    959
ATOM    182  CD  LYS A  22     -21.848  -4.440 -69.089  1.00219.43           C  
ANISOU  182  CD  LYS A  22    25528  31115  26732   -202  -8885   1061
ATOM    183  CE  LYS A  22     -21.315  -5.861 -69.026  1.00220.63           C  
ANISOU  183  CE  LYS A  22    25824  31105  26899    -96  -9054   1184
ATOM    184  NZ  LYS A  22     -21.173  -6.337 -67.622  1.00220.70           N1+
ANISOU  184  NZ  LYS A  22    25558  31386  26910   -430  -8992   1261
ATOM    185  N   ALA A  23     -18.850  -0.070 -69.674  1.00217.90           N  
ANISOU  185  N   ALA A  23    24901  31557  26335     64  -7728    403
ATOM    186  CA  ALA A  23     -17.515   0.068 -70.243  1.00221.86           C  
ANISOU  186  CA  ALA A  23    25510  31965  26822    416  -7451    255
ATOM    187  C   ALA A  23     -16.579   0.840 -69.321  1.00224.47           C  
ANISOU  187  C   ALA A  23    25436  32712  27140    143  -6999    146
ATOM    188  O   ALA A  23     -15.370   0.580 -69.315  1.00227.44           O  
ANISOU  188  O   ALA A  23    25766  33113  27540    286  -6929    107
ATOM    189  CB  ALA A  23     -17.593   0.756 -71.608  1.00224.75           C  
ANISOU  189  CB  ALA A  23    26246  31993  27157    887  -7133     56
ATOM    190  N   VAL A  24     -17.108   1.787 -68.544  1.00220.53           N  
ANISOU  190  N   VAL A  24    24643  32537  26612   -243  -6693     92
ATOM    191  CA  VAL A  24     -16.277   2.497 -67.578  1.00220.32           C  
ANISOU  191  CA  VAL A  24    24222  32920  26571   -540  -6303     -9
ATOM    192  C   VAL A  24     -15.942   1.589 -66.401  1.00221.46           C  
ANISOU  192  C   VAL A  24    24101  33324  26721   -872  -6693    188
ATOM    193  O   VAL A  24     -14.834   1.644 -65.852  1.00222.10           O  
ANISOU  193  O   VAL A  24    23952  33625  26810   -949  -6555    132
ATOM    194  CB  VAL A  24     -16.973   3.794 -67.124  1.00218.88           C  
ANISOU  194  CB  VAL A  24    23835  32988  26342   -841  -5854   -128
ATOM    195  CG1 VAL A  24     -16.189   4.460 -66.005  1.00218.85           C  
ANISOU  195  CG1 VAL A  24    23415  33421  26318  -1195  -5511   -219
ATOM    196  CG2 VAL A  24     -17.124   4.750 -68.296  1.00217.88           C  
ANISOU  196  CG2 VAL A  24    23972  32612  26201   -480  -5414   -343
ATOM    197  N   VAL A  25     -16.883   0.731 -66.003  1.00222.27           N  
ANISOU  197  N   VAL A  25    24234  33394  26824  -1066  -7189    421
ATOM    198  CA  VAL A  25     -16.610  -0.242 -64.954  1.00220.34           C  
ANISOU  198  CA  VAL A  25    23793  33350  26576  -1343  -7594    630
ATOM    199  C   VAL A  25     -15.605  -1.266 -65.469  1.00222.07           C  
ANISOU  199  C   VAL A  25    24194  33348  26833   -995  -7884    680
ATOM    200  O   VAL A  25     -15.611  -1.627 -66.654  1.00222.94           O  
ANISOU  200  O   VAL A  25    24665  33064  26976   -568  -7995    653
ATOM    201  CB  VAL A  25     -17.918  -0.909 -64.493  1.00217.41           C  
ANISOU  201  CB  VAL A  25    23569  32772  26264  -1476  -7760    744
ATOM    202  CG1 VAL A  25     -17.648  -1.971 -63.436  1.00215.70           C  
ANISOU  202  CG1 VAL A  25    23336  32536  26085  -1582  -7859    826
ATOM    203  CG2 VAL A  25     -18.884   0.140 -63.964  1.00215.72           C  
ANISOU  203  CG2 VAL A  25    23175  32756  26034  -1812  -7461    705
ATOM    204  N   MET A  26     -14.721  -1.722 -64.578  1.00222.59           N  
ANISOU  204  N   MET A  26    24063  33608  26905  -1127  -7920    709
ATOM    205  CA  MET A  26     -13.605  -2.624 -64.867  1.00224.97           C  
ANISOU  205  CA  MET A  26    24455  33788  27237   -846  -8149    753
ATOM    206  C   MET A  26     -12.551  -1.988 -65.762  1.00228.47           C  
ANISOU  206  C   MET A  26    24946  34145  27718   -496  -7800    554
ATOM    207  O   MET A  26     -11.667  -2.697 -66.261  1.00229.58           O  
ANISOU  207  O   MET A  26    25231  34095  27904   -173  -7954    576
ATOM    208  CB  MET A  26     -14.067  -3.945 -65.494  1.00224.45           C  
ANISOU  208  CB  MET A  26    24798  33296  27185   -538  -8462    869
ATOM    209  CG  MET A  26     -14.851  -4.849 -64.560  1.00221.86           C  
ANISOU  209  CG  MET A  26    24514  32935  26849   -739  -8505    962
ATOM    210  SD  MET A  26     -15.390  -6.360 -65.383  1.00221.15           S  
ANISOU  210  SD  MET A  26    24850  32416  26761   -435  -8790   1127
ATOM    211  CE  MET A  26     -13.823  -7.205 -65.591  1.00223.37           C  
ANISOU  211  CE  MET A  26    25174  32667  27028   -159  -8935   1175
ATOM    212  N   LEU A  27     -12.617  -0.672 -65.977  1.00219.22           N  
ANISOU  212  N   LEU A  27    23691  33063  26541   -517  -7249    331
ATOM    213  CA  LEU A  27     -11.668   0.052 -66.823  1.00223.96           C  
ANISOU  213  CA  LEU A  27    24365  33534  27196   -165  -6770     93
ATOM    214  C   LEU A  27     -11.621  -0.513 -68.240  1.00226.40           C  
ANISOU  214  C   LEU A  27    25142  33345  27533    378  -6906     98
ATOM    215  O   LEU A  27     -10.575  -0.489 -68.894  1.00230.83           O  
ANISOU  215  O   LEU A  27    25800  33749  28155    729  -6698    -13
ATOM    216  CB  LEU A  27     -10.267   0.069 -66.205  1.00226.31           C  
ANISOU  216  CB  LEU A  27    24352  34084  27553   -226  -6629     22
ATOM    217  CG  LEU A  27     -10.126   0.860 -64.904  1.00225.29           C  
ANISOU  217  CG  LEU A  27    23765  34441  27393   -716  -6386    -51
ATOM    218  CD1 LEU A  27      -8.730   0.697 -64.321  1.00227.56           C  
ANISOU  218  CD1 LEU A  27    23763  34948  27750   -748  -6347   -106
ATOM    219  CD2 LEU A  27     -10.449   2.328 -65.134  1.00227.26           C  
ANISOU  219  CD2 LEU A  27    23954  34763  27632   -780  -5785   -283
ATOM    220  N   GLU A  28     -12.750  -1.028 -68.722  1.00217.68           N  
ANISOU  220  N   GLU A  28    24334  31984  26392    456  -7257    226
ATOM    221  CA  GLU A  28     -12.832  -1.487 -70.099  1.00219.17           C  
ANISOU  221  CA  GLU A  28    25002  31685  26586    973  -7387    217
ATOM    222  C   GLU A  28     -12.659  -0.310 -71.055  1.00222.63           C  
ANISOU  222  C   GLU A  28    25602  31967  27020   1277  -6798    -37
ATOM    223  O   GLU A  28     -12.794   0.858 -70.679  1.00223.81           O  
ANISOU  223  O   GLU A  28    25518  32364  27157   1053  -6336   -188
ATOM    224  CB  GLU A  28     -14.169  -2.185 -70.356  1.00214.97           C  
ANISOU  224  CB  GLU A  28    24723  30930  26025    952  -7883    389
ATOM    225  CG  GLU A  28     -14.360  -3.489 -69.592  1.00211.29           C  
ANISOU  225  CG  GLU A  28    24179  30528  25573    723  -8494    655
ATOM    226  CD  GLU A  28     -13.437  -4.592 -70.073  1.00212.32           C  
ANISOU  226  CD  GLU A  28    24529  30412  25730   1073  -8795    740
ATOM    227  OE1 GLU A  28     -13.104  -4.608 -71.277  1.00214.01           O  
ANISOU  227  OE1 GLU A  28    25106  30262  25947   1555  -8696    641
ATOM    228  OE2 GLU A  28     -13.048  -5.447 -69.249  1.00211.10           O1-
ANISOU  228  OE2 GLU A  28    24205  30423  25579    872  -9024    902
ATOM    229  N   TYR A  29     -12.353  -0.629 -72.309  1.00205.28           N  
ANISOU  229  N   TYR A  29    23829  29344  24826   1801  -6809    -82
ATOM    230  CA  TYR A  29     -12.093   0.411 -73.294  1.00207.97           C  
ANISOU  230  CA  TYR A  29    24370  29491  25156   2148  -6243   -316
ATOM    231  C   TYR A  29     -13.356   1.208 -73.594  1.00206.10           C  
ANISOU  231  C   TYR A  29    24254  29206  24848   2084  -6104   -387
ATOM    232  O   TYR A  29     -14.394   0.642 -73.952  1.00203.37           O  
ANISOU  232  O   TYR A  29    24163  28647  24462   2140  -6529   -268
ATOM    233  CB  TYR A  29     -11.534  -0.192 -74.580  1.00209.63           C  
ANISOU  233  CB  TYR A  29    25052  29228  25370   2745  -6318   -329
ATOM    234  CG  TYR A  29     -11.315   0.838 -75.663  1.00213.58           C  
ANISOU  234  CG  TYR A  29    25817  29487  25847   3140  -5738   -558
ATOM    235  CD1 TYR A  29     -10.289   1.768 -75.566  1.00218.80           C  
ANISOU  235  CD1 TYR A  29    26251  30305  26580   3157  -5121   -746
ATOM    236  CD2 TYR A  29     -12.137   0.883 -76.782  1.00211.84           C  
ANISOU  236  CD2 TYR A  29    26078  28873  25538   3501  -5808   -590
ATOM    237  CE1 TYR A  29     -10.090   2.717 -76.550  1.00221.86           C  
ANISOU  237  CE1 TYR A  29    26888  30461  26949   3519  -4564   -951
ATOM    238  CE2 TYR A  29     -11.942   1.826 -77.774  1.00215.00           C  
ANISOU  238  CE2 TYR A  29    26747  29043  25900   3879  -5268   -796
ATOM    239  CZ  TYR A  29     -10.916   2.740 -77.653  1.00219.84           C  
ANISOU  239  CZ  TYR A  29    27132  29814  26585   3887  -4635   -972
ATOM    240  OH  TYR A  29     -10.718   3.681 -78.638  1.00222.13           O  
ANISOU  240  OH  TYR A  29    27698  29862  26841   4267  -4072  -1172
ATOM    241  N   VAL A  30     -13.262   2.526 -73.444  1.00213.75           N  
ANISOU  241  N   VAL A  30    25032  30372  25810   1965  -5508   -583
ATOM    242  CA  VAL A  30     -14.330   3.445 -73.809  1.00212.89           C  
ANISOU  242  CA  VAL A  30    25043  30214  25633   1953  -5270   -682
ATOM    243  C   VAL A  30     -13.797   4.383 -74.884  1.00217.41           C  
ANISOU  243  C   VAL A  30    25870  30548  26188   2386  -4677   -917
ATOM    244  O   VAL A  30     -12.616   4.745 -74.893  1.00221.27           O  
ANISOU  244  O   VAL A  30    26234  31097  26741   2485  -4281  -1038
ATOM    245  CB  VAL A  30     -14.861   4.231 -72.587  1.00211.46           C  
ANISOU  245  CB  VAL A  30    24409  30494  25443   1383  -5081   -694
ATOM    246  CG1 VAL A  30     -13.796   5.168 -72.040  1.00216.01           C  
ANISOU  246  CG1 VAL A  30    24639  31373  26063   1225  -4506   -871
ATOM    247  CG2 VAL A  30     -16.132   4.991 -72.941  1.00209.98           C  
ANISOU  247  CG2 VAL A  30    24357  30237  25187   1362  -4947   -751
ATOM    248  N   GLU A  31     -14.675   4.760 -75.808  1.00217.59           N  
ANISOU  248  N   GLU A  31    26259  30285  26130   2656  -4623   -979
ATOM    249  CA  GLU A  31     -14.273   5.566 -76.950  1.00219.44           C  
ANISOU  249  CA  GLU A  31    26821  30230  26326   3127  -4097  -1186
ATOM    250  C   GLU A  31     -14.073   7.021 -76.544  1.00221.73           C  
ANISOU  250  C   GLU A  31    26820  30803  26623   2910  -3401  -1386
ATOM    251  O   GLU A  31     -14.692   7.517 -75.598  1.00220.56           O  
ANISOU  251  O   GLU A  31    26329  31007  26468   2443  -3359  -1371
ATOM    252  CB  GLU A  31     -15.316   5.461 -78.063  1.00217.74           C  
ANISOU  252  CB  GLU A  31    27114  29612  26007   3498  -4305  -1185
ATOM    253  CG  GLU A  31     -15.436   4.059 -78.643  1.00216.62           C  
ANISOU  253  CG  GLU A  31    27327  29123  25855   3787  -4957  -1016
ATOM    254  CD  GLU A  31     -16.497   3.954 -79.719  1.00214.85           C  
ANISOU  254  CD  GLU A  31    27600  28502  25531   4144  -5200  -1026
ATOM    255  OE1 GLU A  31     -17.219   4.947 -79.946  1.00214.37           O  
ANISOU  255  OE1 GLU A  31    27583  28459  25408   4139  -4893  -1148
ATOM    256  OE2 GLU A  31     -16.614   2.873 -80.333  1.00215.37           O1-
ANISOU  256  OE2 GLU A  31    28016  28236  25579   4433  -5709   -913
ATOM    257  N   ARG A  32     -13.192   7.708 -77.276  1.00222.13           N  
ANISOU  257  N   ARG A  32    27022  30684  26692   3260  -2837  -1574
ATOM    258  CA  ARG A  32     -12.860   9.090 -76.947  1.00221.25           C  
ANISOU  258  CA  ARG A  32    26647  30814  26605   3083  -2137  -1779
ATOM    259  C   ARG A  32     -14.000  10.059 -77.238  1.00219.91           C  
ANISOU  259  C   ARG A  32    26613  30620  26322   3067  -1893  -1871
ATOM    260  O   ARG A  32     -13.965  11.194 -76.752  1.00218.99           O  
ANISOU  260  O   ARG A  32    26229  30765  26213   2812  -1379  -2014
ATOM    261  CB  ARG A  32     -11.609   9.534 -77.711  1.00222.15           C  
ANISOU  261  CB  ARG A  32    26903  30715  26789   3486  -1587  -1952
ATOM    262  CG  ARG A  32     -10.314   8.878 -77.256  1.00223.48           C  
ANISOU  262  CG  ARG A  32    26814  30992  27105   3436  -1666  -1906
ATOM    263  CD  ARG A  32      -9.131   9.418 -78.050  1.00224.45           C  
ANISOU  263  CD  ARG A  32    27070  30889  27321   3838  -1063  -2086
ATOM    264  NE  ARG A  32      -7.860   8.837 -77.627  1.00225.88           N  
ANISOU  264  NE  ARG A  32    26981  31174  27667   3800  -1113  -2052
ATOM    265  CZ  ARG A  32      -6.688   9.118 -78.188  1.00227.09           C  
ANISOU  265  CZ  ARG A  32    27181  31153  27949   4117   -649  -2179
ATOM    266  NH1 ARG A  32      -6.623   9.974 -79.199  1.00227.03           N  
ANISOU  266  NH1 ARG A  32    27498  30850  27913   4500    -85  -2346
ATOM    267  NH2 ARG A  32      -5.580   8.545 -77.739  1.00228.48           N1+
ANISOU  267  NH2 ARG A  32    27079  31445  28289   4058   -742  -2136
ATOM    268  N   ALA A  33     -15.002   9.646 -78.012  1.00230.68           N  
ANISOU  268  N   ALA A  33    28385  31677  27587   3332  -2252  -1796
ATOM    269  CA  ALA A  33     -16.101  10.525 -78.399  1.00229.26           C  
ANISOU  269  CA  ALA A  33    28373  31436  27299   3376  -2047  -1883
ATOM    270  C   ALA A  33     -17.392  10.244 -77.641  1.00225.78           C  
ANISOU  270  C   ALA A  33    27738  31211  26839   2960  -2510  -1728
ATOM    271  O   ALA A  33     -18.112  11.184 -77.284  1.00225.25           O  
ANISOU  271  O   ALA A  33    27514  31339  26730   2720  -2231  -1797
ATOM    272  CB  ALA A  33     -16.362  10.411 -79.905  1.00227.51           C  
ANISOU  272  CB  ALA A  33    28778  30692  26976   4013  -2069  -1939
ATOM    273  N   THR A  34     -17.708   8.971 -77.394  1.00225.90           N  
ANISOU  273  N   THR A  34    27761  31181  26889   2874  -3201  -1517
ATOM    274  CA  THR A  34     -18.914   8.644 -76.640  1.00224.84           C  
ANISOU  274  CA  THR A  34    27424  31241  26763   2467  -3643  -1356
ATOM    275  C   THR A  34     -18.857   9.233 -75.236  1.00223.92           C  
ANISOU  275  C   THR A  34    26753  31639  26689   1871  -3404  -1349
ATOM    276  O   THR A  34     -19.868   9.728 -74.719  1.00223.03           O  
ANISOU  276  O   THR A  34    26469  31719  26553   1560  -3387  -1321
ATOM    277  CB  THR A  34     -19.102   7.129 -76.586  1.00225.99           C  
ANISOU  277  CB  THR A  34    27664  31244  26957   2476  -4398  -1131
ATOM    278  OG1 THR A  34     -17.987   6.529 -75.916  1.00226.65           O  
ANISOU  278  OG1 THR A  34    27495  31507  27113   2319  -4471  -1061
ATOM    279  CG2 THR A  34     -19.200   6.564 -77.994  1.00227.00           C  
ANISOU  279  CG2 THR A  34    28369  30849  27031   3074  -4645  -1146
ATOM    280  N   TRP A  35     -17.679   9.195 -74.608  1.00225.23           N  
ANISOU  280  N   TRP A  35    26636  32026  26915   1713  -3217  -1375
ATOM    281  CA  TRP A  35     -17.488   9.900 -73.345  1.00226.68           C  
ANISOU  281  CA  TRP A  35    26321  32685  27123   1190  -2912  -1412
ATOM    282  C   TRP A  35     -17.794  11.384 -73.497  1.00229.09           C  
ANISOU  282  C   TRP A  35    26602  33073  27369   1168  -2263  -1616
ATOM    283  O   TRP A  35     -18.345  12.010 -72.584  1.00228.96           O  
ANISOU  283  O   TRP A  35    26272  33391  27334    735  -2113  -1613
ATOM    284  CB  TRP A  35     -16.059   9.699 -72.841  1.00230.21           C  
ANISOU  284  CB  TRP A  35    26516  33302  27651   1114  -2775  -1449
ATOM    285  CG  TRP A  35     -15.791  10.368 -71.530  1.00231.00           C  
ANISOU  285  CG  TRP A  35    26114  33883  27772    586  -2499  -1494
ATOM    286  CD1 TRP A  35     -15.148  11.555 -71.332  1.00233.92           C  
ANISOU  286  CD1 TRP A  35    26289  34432  28158    500  -1852  -1711
ATOM    287  CD2 TRP A  35     -16.154   9.887 -70.230  1.00226.99           C  
ANISOU  287  CD2 TRP A  35    25251  33727  27267     77  -2863  -1320
ATOM    288  NE1 TRP A  35     -15.093  11.845 -69.991  1.00231.97           N  
ANISOU  288  NE1 TRP A  35    25591  34630  27918    -31  -1806  -1689
ATOM    289  CE2 TRP A  35     -15.702  10.837 -69.292  1.00227.73           C  
ANISOU  289  CE2 TRP A  35    24956  34207  27365   -292  -2416  -1448
ATOM    290  CE3 TRP A  35     -16.818   8.747 -69.767  1.00221.66           C  
ANISOU  290  CE3 TRP A  35    24561  33068  26593    -98  -3514  -1069
ATOM    291  CZ2 TRP A  35     -15.892  10.681 -67.921  1.00223.29           C  
ANISOU  291  CZ2 TRP A  35    24011  34042  26788   -814  -2605  -1333
ATOM    292  CZ3 TRP A  35     -17.006   8.594 -68.405  1.00217.67           C  
ANISOU  292  CZ3 TRP A  35    23668  32955  26081   -618  -3681   -948
ATOM    293  CH2 TRP A  35     -16.545   9.557 -67.498  1.00218.74           C  
ANISOU  293  CH2 TRP A  35    23440  33469  26203   -963  -3231  -1079
ATOM    294  N   ASN A  36     -17.447  11.962 -74.648  1.00228.77           N  
ANISOU  294  N   ASN A  36    26906  32723  27294   1640  -1860  -1791
ATOM    295  CA  ASN A  36     -17.795  13.348 -74.927  1.00229.98           C  
ANISOU  295  CA  ASN A  36    27100  32902  27380   1677  -1247  -1983
ATOM    296  C   ASN A  36     -19.278  13.525 -75.229  1.00227.50           C  
ANISOU  296  C   ASN A  36    26971  32488  26982   1692  -1439  -1927
ATOM    297  O   ASN A  36     -19.751  14.665 -75.273  1.00228.16           O  
ANISOU  297  O   ASN A  36    27037  32649  27003   1642   -978  -2058
ATOM    298  CB  ASN A  36     -16.960  13.875 -76.097  1.00232.06           C  
ANISOU  298  CB  ASN A  36    27705  32837  27631   2204   -752  -2180
ATOM    299  CG  ASN A  36     -15.482  13.969 -75.765  1.00234.01           C  
ANISOU  299  CG  ASN A  36    27713  33211  27989   2162   -428  -2274
ATOM    300  OD1 ASN A  36     -15.103  14.378 -74.668  1.00234.38           O  
ANISOU  300  OD1 ASN A  36    27307  33652  28094   1712   -241  -2305
ATOM    301  ND2 ASN A  36     -14.638  13.589 -76.717  1.00234.72           N  
ANISOU  301  ND2 ASN A  36    28111  32960  28114   2639   -362  -2320
ATOM    302  N   ASP A  37     -20.016  12.432 -75.436  1.00232.20           N  
ANISOU  302  N   ASP A  37    27735  32908  27583   1761  -2105  -1738
ATOM    303  CA  ASP A  37     -21.449  12.500 -75.694  1.00230.39           C  
ANISOU  303  CA  ASP A  37    27651  32579  27306   1762  -2353  -1673
ATOM    304  C   ASP A  37     -22.305  12.249 -74.459  1.00228.22           C  
ANISOU  304  C   ASP A  37    26978  32654  27082   1193  -2669  -1496
ATOM    305  O   ASP A  37     -23.460  12.693 -74.426  1.00227.20           O  
ANISOU  305  O   ASP A  37    26845  32553  26927   1086  -2680  -1477
ATOM    306  CB  ASP A  37     -21.843  11.484 -76.774  1.00229.43           C  
ANISOU  306  CB  ASP A  37    27991  32009  27173   2211  -2899  -1586
ATOM    307  CG  ASP A  37     -21.294  11.839 -78.140  1.00230.65           C  
ANISOU  307  CG  ASP A  37    28626  31764  27246   2827  -2577  -1762
ATOM    308  OD1 ASP A  37     -21.110  13.043 -78.415  1.00231.83           O  
ANISOU  308  OD1 ASP A  37    28814  31939  27332   2933  -1940  -1952
ATOM    309  OD2 ASP A  37     -21.047  10.911 -78.940  1.00230.24           O1-
ANISOU  309  OD2 ASP A  37    28929  31364  27189   3213  -2952  -1707
ATOM    310  N   ARG A  38     -21.773  11.557 -73.447  1.00233.45           N  
ANISOU  310  N   ARG A  38    27312  33574  27813    839  -2918  -1364
ATOM    311  CA  ARG A  38     -22.610  11.128 -72.329  1.00229.70           C  
ANISOU  311  CA  ARG A  38    26512  33378  27384    338  -3289  -1165
ATOM    312  C   ARG A  38     -23.116  12.309 -71.507  1.00229.92           C  
ANISOU  312  C   ARG A  38    26227  33758  27373    -57  -2833  -1233
ATOM    313  O   ARG A  38     -24.250  12.284 -71.016  1.00226.79           O  
ANISOU  313  O   ARG A  38    25701  33473  26994   -333  -3038  -1107
ATOM    314  CB  ARG A  38     -21.846  10.147 -71.442  1.00228.39           C  
ANISOU  314  CB  ARG A  38    26092  33403  27281     77  -3628  -1016
ATOM    315  CG  ARG A  38     -21.456   8.847 -72.132  1.00227.50           C  
ANISOU  315  CG  ARG A  38    26270  32959  27213    419  -4151   -909
ATOM    316  CD  ARG A  38     -22.650   7.916 -72.332  1.00224.14           C  
ANISOU  316  CD  ARG A  38    25999  32334  26831    423  -4785   -713
ATOM    317  NE  ARG A  38     -23.488   8.301 -73.465  1.00224.84           N  
ANISOU  317  NE  ARG A  38    26455  32093  26883    790  -4757   -802
ATOM    318  CZ  ARG A  38     -23.188   8.053 -74.736  1.00226.07           C  
ANISOU  318  CZ  ARG A  38    27057  31838  27000   1334  -4817   -888
ATOM    319  NH1 ARG A  38     -22.067   7.415 -75.043  1.00227.44           N  
ANISOU  319  NH1 ARG A  38    27360  31877  27179   1571  -4894   -891
ATOM    320  NH2 ARG A  38     -24.010   8.440 -75.702  1.00225.31           N1+
ANISOU  320  NH2 ARG A  38    27289  31461  26858   1651  -4802   -970
ATOM    321  N   PHE A  39     -22.292  13.346 -71.335  1.00231.44           N  
ANISOU  321  N   PHE A  39    26290  34124  27523    -94  -2209  -1429
ATOM    322  CA  PHE A  39     -22.733  14.512 -70.572  1.00232.02           C  
ANISOU  322  CA  PHE A  39    26086  34522  27550   -459  -1747  -1507
ATOM    323  C   PHE A  39     -23.942  15.173 -71.219  1.00231.72           C  
ANISOU  323  C   PHE A  39    26259  34323  27461   -301  -1621  -1549
ATOM    324  O   PHE A  39     -24.875  15.596 -70.525  1.00229.94           O  
ANISOU  324  O   PHE A  39    25823  34319  27226   -646  -1581  -1482
ATOM    325  CB  PHE A  39     -21.586  15.508 -70.418  1.00235.77           C  
ANISOU  325  CB  PHE A  39    26426  35158  27999   -475  -1094  -1733
ATOM    326  CG  PHE A  39     -20.553  15.083 -69.420  1.00234.69           C  
ANISOU  326  CG  PHE A  39    25953  35305  27914   -782  -1170  -1693
ATOM    327  CD1 PHE A  39     -20.832  14.080 -68.511  1.00230.85           C  
ANISOU  327  CD1 PHE A  39    25258  34993  27463  -1112  -1716  -1464
ATOM    328  CD2 PHE A  39     -19.311  15.684 -69.383  1.00237.47           C  
ANISOU  328  CD2 PHE A  39    26195  35744  28287   -739   -698  -1886
ATOM    329  CE1 PHE A  39     -19.892  13.688 -67.587  1.00229.89           C  
ANISOU  329  CE1 PHE A  39    24840  35133  27375  -1379  -1800  -1428
ATOM    330  CE2 PHE A  39     -18.366  15.289 -68.456  1.00236.19           C  
ANISOU  330  CE2 PHE A  39    25713  35848  28180  -1018   -794  -1856
ATOM    331  CZ  PHE A  39     -18.657  14.289 -67.561  1.00232.58           C  
ANISOU  331  CZ  PHE A  39    25067  35566  27736  -1330  -1353  -1627
ATOM    332  N   SER A  40     -23.944  15.272 -72.549  1.00236.32           N  
ANISOU  332  N   SER A  40    27267  34517  28009    229  -1556  -1659
ATOM    333  CA  SER A  40     -25.137  15.736 -73.244  1.00236.20           C  
ANISOU  333  CA  SER A  40    27489  34309  27948    427  -1540  -1683
ATOM    334  C   SER A  40     -26.285  14.751 -73.067  1.00232.01           C  
ANISOU  334  C   SER A  40    26947  33714  27494    296  -2225  -1453
ATOM    335  O   SER A  40     -27.434  15.154 -72.842  1.00230.01           O  
ANISOU  335  O   SER A  40    26607  33538  27247    124  -2237  -1403
ATOM    336  CB  SER A  40     -24.829  15.943 -74.725  1.00238.87           C  
ANISOU  336  CB  SER A  40    28321  34220  28219   1055  -1371  -1843
ATOM    337  OG  SER A  40     -23.864  16.964 -74.908  1.00242.93           O  
ANISOU  337  OG  SER A  40    28844  34781  28676   1172   -679  -2062
ATOM    338  N   ASP A  41     -25.987  13.452 -73.146  1.00237.69           N  
ANISOU  338  N   ASP A  41    27740  34288  28284    368  -2793  -1307
ATOM    339  CA  ASP A  41     -26.999  12.415 -72.978  1.00233.26           C  
ANISOU  339  CA  ASP A  41    27166  33643  27820    242  -3467  -1083
ATOM    340  C   ASP A  41     -27.496  12.288 -71.542  1.00230.37           C  
ANISOU  340  C   ASP A  41    26340  33672  27520   -366  -3585   -908
ATOM    341  O   ASP A  41     -28.331  11.417 -71.276  1.00227.32           O  
ANISOU  341  O   ASP A  41    25898  33239  27234   -523  -4125   -707
ATOM    342  CB  ASP A  41     -26.452  11.070 -73.460  1.00232.37           C  
ANISOU  342  CB  ASP A  41    27274  33259  27756    496  -4011   -983
ATOM    343  CG  ASP A  41     -26.273  11.023 -74.966  1.00233.67           C  
ANISOU  343  CG  ASP A  41    27956  32967  27860   1125  -4025  -1115
ATOM    344  OD1 ASP A  41     -27.030  11.716 -75.677  1.00233.76           O  
ANISOU  344  OD1 ASP A  41    28183  32815  27818   1356  -3858  -1219
ATOM    345  OD2 ASP A  41     -25.375  10.294 -75.438  1.00233.97           O1-
ANISOU  345  OD2 ASP A  41    28197  32806  27895   1400  -4199  -1114
ATOM    346  N   ILE A  42     -27.006  13.112 -70.619  1.00233.73           N  
ANISOU  346  N   ILE A  42    26446  34467  27893   -706  -3099   -978
ATOM    347  CA  ILE A  42     -27.539  13.186 -69.267  1.00233.53           C  
ANISOU  347  CA  ILE A  42    26011  34818  27900  -1268  -3123   -832
ATOM    348  C   ILE A  42     -28.209  14.530 -69.006  1.00232.44           C  
ANISOU  348  C   ILE A  42    25746  34869  27700  -1436  -2592   -938
ATOM    349  O   ILE A  42     -29.294  14.583 -68.419  1.00232.43           O  
ANISOU  349  O   ILE A  42    25566  34999  27747  -1735  -2711   -803
ATOM    350  CB  ILE A  42     -26.435  12.907 -68.223  1.00233.72           C  
ANISOU  350  CB  ILE A  42    25744  35149  27910  -1581  -3073   -798
ATOM    351  CG1 ILE A  42     -25.906  11.480 -68.374  1.00234.93           C  
ANISOU  351  CG1 ILE A  42    25999  35130  28132  -1454  -3655   -654
ATOM    352  CG2 ILE A  42     -26.959  13.131 -66.813  1.00233.54           C  
ANISOU  352  CG2 ILE A  42    25323  35523  27888  -2151  -3022   -667
ATOM    353  CD1 ILE A  42     -24.655  11.204 -67.570  1.00235.28           C  
ANISOU  353  CD1 ILE A  42    25815  35421  28158  -1651  -3598   -653
ATOM    354  N   TYR A  43     -27.579  15.625 -69.440  1.00239.96           N  
ANISOU  354  N   TYR A  43    26792  35828  28553  -1244  -1989  -1177
ATOM    355  CA  TYR A  43     -28.214  16.935 -69.345  1.00240.78           C  
ANISOU  355  CA  TYR A  43    26831  36065  28588  -1341  -1463  -1294
ATOM    356  C   TYR A  43     -29.543  16.957 -70.087  1.00239.75           C  
ANISOU  356  C   TYR A  43    26912  35688  28492  -1130  -1674  -1245
ATOM    357  O   TYR A  43     -30.511  17.569 -69.622  1.00238.69           O  
ANISOU  357  O   TYR A  43    26615  35716  28362  -1375  -1520  -1204
ATOM    358  CB  TYR A  43     -27.282  18.014 -69.893  1.00244.54           C  
ANISOU  358  CB  TYR A  43    27440  36510  28963  -1088   -808  -1565
ATOM    359  CG  TYR A  43     -27.866  19.410 -69.852  1.00244.95           C  
ANISOU  359  CG  TYR A  43    27454  36682  28932  -1158   -226  -1701
ATOM    360  CD1 TYR A  43     -27.923  20.127 -68.665  1.00242.75           C  
ANISOU  360  CD1 TYR A  43    26815  36801  28619  -1638    118  -1702
ATOM    361  CD2 TYR A  43     -28.359  20.012 -71.003  1.00247.00           C  
ANISOU  361  CD2 TYR A  43    28057  36653  29139   -731    -20  -1828
ATOM    362  CE1 TYR A  43     -28.455  21.403 -68.624  1.00242.45           C  
ANISOU  362  CE1 TYR A  43    26751  36868  28500  -1700    659  -1823
ATOM    363  CE2 TYR A  43     -28.892  21.287 -70.973  1.00247.18           C  
ANISOU  363  CE2 TYR A  43    28054  36782  29081   -783    518  -1949
ATOM    364  CZ  TYR A  43     -28.938  21.978 -69.781  1.00244.80           C  
ANISOU  364  CZ  TYR A  43    27384  36877  28752  -1272    860  -1945
ATOM    365  OH  TYR A  43     -29.468  23.247 -69.745  1.00243.63           O  
ANISOU  365  OH  TYR A  43    27218  36830  28520  -1323   1404  -2063
ATOM    366  N   ALA A  44     -29.608  16.298 -71.247  1.00242.46           N  
ANISOU  366  N   ALA A  44    27625  35635  28864   -668  -2032  -1253
ATOM    367  CA  ALA A  44     -30.872  16.219 -71.972  1.00241.50           C  
ANISOU  367  CA  ALA A  44    27709  35260  28788   -455  -2309  -1207
ATOM    368  C   ALA A  44     -31.926  15.461 -71.175  1.00237.39           C  
ANISOU  368  C   ALA A  44    26928  34855  28414   -839  -2817   -954
ATOM    369  O   ALA A  44     -33.123  15.743 -71.303  1.00236.48           O  
ANISOU  369  O   ALA A  44    26802  34694  28354   -864  -2889   -909
ATOM    370  CB  ALA A  44     -30.657  15.562 -73.335  1.00242.04           C  
ANISOU  370  CB  ALA A  44    28239  34873  28851    115  -2640  -1262
ATOM    371  N   LEU A  45     -31.504  14.503 -70.348  1.00235.73           N  
ANISOU  371  N   LEU A  45    26503  34791  28273  -1137  -3162   -786
ATOM    372  CA  LEU A  45     -32.453  13.737 -69.548  1.00236.53           C  
ANISOU  372  CA  LEU A  45    26357  34994  28521  -1512  -3628   -534
ATOM    373  C   LEU A  45     -32.938  14.524 -68.337  1.00235.87           C  
ANISOU  373  C   LEU A  45    25888  35307  28423  -2011  -3262   -478
ATOM    374  O   LEU A  45     -34.117  14.448 -67.977  1.00236.31           O  
ANISOU  374  O   LEU A  45    25795  35401  28590  -2228  -3443   -332
ATOM    375  CB  LEU A  45     -31.821  12.421 -69.093  1.00237.47           C  
ANISOU  375  CB  LEU A  45    26407  35116  28706  -1638  -4117   -369
ATOM    376  CG  LEU A  45     -31.477  11.389 -70.166  1.00238.45           C  
ANISOU  376  CG  LEU A  45    26894  34838  28869  -1196  -4601   -366
ATOM    377  CD1 LEU A  45     -30.756  10.203 -69.544  1.00239.28           C  
ANISOU  377  CD1 LEU A  45    26886  35008  29022  -1373  -5000   -204
ATOM    378  CD2 LEU A  45     -32.728  10.937 -70.899  1.00239.40           C  
ANISOU  378  CD2 LEU A  45    27200  34647  29116  -1007  -5058   -289
ATOM    379  N   CYS A  46     -32.047  15.282 -67.700  1.00245.80           N  
ANISOU  379  N   CYS A  46    26982  36857  29555  -2197  -2747   -593
ATOM    380  CA  CYS A  46     -32.354  15.932 -66.432  1.00244.92           C  
ANISOU  380  CA  CYS A  46    26506  37139  29411  -2696  -2422   -532
ATOM    381  C   CYS A  46     -33.104  17.254 -66.585  1.00246.39           C  
ANISOU  381  C   CYS A  46    26685  37393  29540  -2691  -1910   -653
ATOM    382  O   CYS A  46     -33.142  18.029 -65.621  1.00244.36           O  
ANISOU  382  O   CYS A  46    26167  37465  29214  -3056  -1502   -662
ATOM    383  CB  CYS A  46     -31.066  16.163 -65.636  1.00245.40           C  
ANISOU  383  CB  CYS A  46    26388  37488  29363  -2911  -2116   -610
ATOM    384  SG  CYS A  46     -30.236  14.654 -65.092  1.00243.89           S  
ANISOU  384  SG  CYS A  46    26114  37320  29233  -3037  -2690   -432
ATOM    385  N   VAL A  47     -33.698  17.551 -67.742  1.00256.94           N  
ANISOU  385  N   VAL A  47    28306  38429  30891  -2289  -1915   -748
ATOM    386  CA  VAL A  47     -34.343  18.850 -67.907  1.00259.13           C  
ANISOU  386  CA  VAL A  47    28588  38770  31098  -2260  -1398   -873
ATOM    387  C   VAL A  47     -35.816  18.734 -68.283  1.00258.28           C  
ANISOU  387  C   VAL A  47    28517  38496  31120  -2196  -1688   -761
ATOM    388  O   VAL A  47     -36.693  19.111 -67.499  1.00256.23           O  
ANISOU  388  O   VAL A  47    27995  38448  30913  -2543  -1574   -649
ATOM    389  CB  VAL A  47     -33.593  19.702 -68.950  1.00262.62           C  
ANISOU  389  CB  VAL A  47    29343  39041  31398  -1814   -937  -1150
ATOM    390  CG1 VAL A  47     -34.356  20.988 -69.231  1.00263.05           C  
ANISOU  390  CG1 VAL A  47    29445  39118  31382  -1738   -444  -1272
ATOM    391  CG2 VAL A  47     -32.190  20.022 -68.462  1.00262.84           C  
ANISOU  391  CG2 VAL A  47    29271  39276  31321  -1933   -554  -1276
ATOM    392  N   ALA A  48     -36.108  18.189 -69.461  1.00261.32           N  
ANISOU  392  N   ALA A  48    29222  38499  31567  -1758  -2078   -786
ATOM    393  CA  ALA A  48     -37.368  18.472 -70.151  1.00261.87           C  
ANISOU  393  CA  ALA A  48    29415  38368  31716  -1552  -2193   -785
ATOM    394  C   ALA A  48     -38.274  17.245 -70.232  1.00260.59           C  
ANISOU  394  C   ALA A  48    29219  38015  31778  -1591  -2934   -570
ATOM    395  O   ALA A  48     -38.161  16.434 -71.153  1.00260.77           O  
ANISOU  395  O   ALA A  48    29530  37703  31847  -1232  -3391   -583
ATOM    396  CB  ALA A  48     -37.084  19.018 -71.548  1.00263.92           C  
ANISOU  396  CB  ALA A  48    30110  38317  31850   -967  -1995  -1021
ATOM    397  N   TYR A  49     -39.181  17.111 -69.259  1.00265.68           N  
ANISOU  397  N   TYR A  49    29515  38864  32567  -2030  -3043   -370
ATOM    398  CA  TYR A  49     -40.381  16.315 -69.498  1.00262.96           C  
ANISOU  398  CA  TYR A  49    29139  38310  32462  -2026  -3630   -202
ATOM    399  C   TYR A  49     -41.656  16.937 -68.910  1.00261.76           C  
ANISOU  399  C   TYR A  49    28701  38325  32431  -2318  -3459   -100
ATOM    400  O   TYR A  49     -42.509  16.209 -68.391  1.00258.90           O  
ANISOU  400  O   TYR A  49    28110  37964  32295  -2590  -3863    121
ATOM    401  CB  TYR A  49     -40.129  14.900 -68.949  1.00261.47           C  
ANISOU  401  CB  TYR A  49    28830  38106  32412  -2253  -4195      9
ATOM    402  CG  TYR A  49     -41.271  13.907 -69.058  1.00257.79           C  
ANISOU  402  CG  TYR A  49    28295  37430  32225  -2311  -4842    206
ATOM    403  CD1 TYR A  49     -41.697  13.431 -70.290  1.00256.59           C  
ANISOU  403  CD1 TYR A  49    28453  36875  32163  -1875  -5290    143
ATOM    404  CD2 TYR A  49     -41.896  13.417 -67.914  1.00256.30           C  
ANISOU  404  CD2 TYR A  49    27735  37434  32213  -2803  -5011    456
ATOM    405  CE1 TYR A  49     -42.736  12.523 -70.382  1.00254.53           C  
ANISOU  405  CE1 TYR A  49    28114  36416  32178  -1940  -5892    314
ATOM    406  CE2 TYR A  49     -42.932  12.513 -67.996  1.00254.78           C  
ANISOU  406  CE2 TYR A  49    27461  37041  32301  -2871  -5584    637
ATOM    407  CZ  TYR A  49     -43.347  12.066 -69.231  1.00254.10           C  
ANISOU  407  CZ  TYR A  49    27668  36560  32319  -2445  -6031    561
ATOM    408  OH  TYR A  49     -44.378  11.159 -69.312  1.00253.75           O  
ANISOU  408  OH  TYR A  49    27530  36308  32577  -2522  -6616    731
ATOM    409  N   PRO A  50     -41.857  18.271 -68.951  1.00263.50           N  
ANISOU  409  N   PRO A  50    28914  38682  32519  -2279  -2860   -243
ATOM    410  CA  PRO A  50     -40.982  19.444 -69.021  1.00266.73           C  
ANISOU  410  CA  PRO A  50    29431  39246  32670  -2175  -2175   -466
ATOM    411  C   PRO A  50     -40.518  19.716 -67.594  1.00265.56           C  
ANISOU  411  C   PRO A  50    28936  39512  32455  -2700  -1824   -379
ATOM    412  O   PRO A  50     -40.573  20.836 -67.092  1.00265.25           O  
ANISOU  412  O   PRO A  50    28768  39718  32299  -2874  -1243   -453
ATOM    413  CB  PRO A  50     -41.896  20.548 -69.549  1.00267.83           C  
ANISOU  413  CB  PRO A  50    29644  39333  32786  -1985  -1839   -575
ATOM    414  CG  PRO A  50     -43.234  20.162 -69.064  1.00264.89           C  
ANISOU  414  CG  PRO A  50    28999  38986  32660  -2255  -2172   -355
ATOM    415  CD  PRO A  50     -43.273  18.657 -69.095  1.00262.91           C  
ANISOU  415  CD  PRO A  50    28738  38553  32604  -2291  -2906   -183
ATOM    416  N   GLU A  51     -40.133  18.632 -66.927  1.00267.08           N  
ANISOU  416  N   GLU A  51    28981  39770  32728  -2955  -2217   -208
ATOM    417  CA  GLU A  51     -39.770  18.559 -65.523  1.00264.77           C  
ANISOU  417  CA  GLU A  51    28363  39837  32402  -3464  -2060    -76
ATOM    418  C   GLU A  51     -38.474  17.775 -65.377  1.00264.70           C  
ANISOU  418  C   GLU A  51    28414  39839  32320  -3455  -2254    -87
ATOM    419  O   GLU A  51     -38.155  16.939 -66.229  1.00264.87           O  
ANISOU  419  O   GLU A  51    28678  39569  32394  -3128  -2684   -105
ATOM    420  CB  GLU A  51     -40.888  17.874 -64.722  1.00261.35           C  
ANISOU  420  CB  GLU A  51    27643  39466  32193  -3834  -2426    209
ATOM    421  CG  GLU A  51     -42.206  18.634 -64.727  1.00260.06           C  
ANISOU  421  CG  GLU A  51    27363  39320  32129  -3892  -2226    245
ATOM    422  CD  GLU A  51     -43.323  17.871 -64.043  1.00257.09           C  
ANISOU  422  CD  GLU A  51    26713  38954  32014  -4222  -2620    531
ATOM    423  OE1 GLU A  51     -43.106  16.697 -63.678  1.00255.87           O  
ANISOU  423  OE1 GLU A  51    26496  38756  31968  -4368  -3088    697
ATOM    424  OE2 GLU A  51     -44.421  18.443 -63.876  1.00256.64           O1-
ANISOU  424  OE2 GLU A  51    26505  38943  32065  -4331  -2453    592
ATOM    425  N   PRO A  52     -37.705  18.022 -64.316  1.00264.28           N  
ANISOU  425  N   PRO A  52    28155  40114  32144  -3797  -1953    -80
ATOM    426  CA  PRO A  52     -36.458  17.270 -64.124  1.00263.92           C  
ANISOU  426  CA  PRO A  52    28144  40095  32038  -3798  -2145    -86
ATOM    427  C   PRO A  52     -36.721  15.792 -63.873  1.00261.07           C  
ANISOU  427  C   PRO A  52    27727  39618  31849  -3909  -2832    160
ATOM    428  O   PRO A  52     -37.790  15.397 -63.400  1.00259.31           O  
ANISOU  428  O   PRO A  52    27333  39408  31785  -4149  -3083    369
ATOM    429  CB  PRO A  52     -35.821  17.942 -62.902  1.00262.51           C  
ANISOU  429  CB  PRO A  52    27711  40323  31708  -4198  -1675   -114
ATOM    430  CG  PRO A  52     -36.964  18.564 -62.173  1.00260.81           C  
ANISOU  430  CG  PRO A  52    27272  40294  31530  -4521  -1446     -1
ATOM    431  CD  PRO A  52     -37.933  18.998 -63.235  1.00262.83           C  
ANISOU  431  CD  PRO A  52    27704  40290  31869  -4195  -1431    -68
ATOM    432  N   LEU A  53     -35.718  14.966 -64.201  1.00248.94           N  
ANISOU  432  N   LEU A  53    26338  37958  30289  -3728  -3125    137
ATOM    433  CA  LEU A  53     -35.895  13.519 -64.159  1.00250.36           C  
ANISOU  433  CA  LEU A  53    26527  37970  30626  -3757  -3797    349
ATOM    434  C   LEU A  53     -34.704  12.762 -63.576  1.00250.63           C  
ANISOU  434  C   LEU A  53    26510  38127  30593  -3877  -3960    399
ATOM    435  O   LEU A  53     -34.678  11.528 -63.672  1.00251.79           O  
ANISOU  435  O   LEU A  53    26716  38102  30850  -3837  -4515    552
ATOM    436  CB  LEU A  53     -36.186  12.976 -65.564  1.00250.91           C  
ANISOU  436  CB  LEU A  53    26933  37604  30795  -3273  -4200    294
ATOM    437  CG  LEU A  53     -37.483  13.395 -66.256  1.00251.18           C  
ANISOU  437  CG  LEU A  53    27046  37444  30946  -3110  -4236    279
ATOM    438  CD1 LEU A  53     -37.505  12.848 -67.673  1.00251.78           C  
ANISOU  438  CD1 LEU A  53    27502  37088  31074  -2590  -4630    190
ATOM    439  CD2 LEU A  53     -38.698  12.924 -65.473  1.00252.38           C  
ANISOU  439  CD2 LEU A  53    26918  37667  31307  -3488  -4520    536
ATOM    440  N   GLY A  54     -33.720  13.444 -62.985  1.00249.60           N  
ANISOU  440  N   GLY A  54    26270  38279  30288  -4016  -3509    273
ATOM    441  CA  GLY A  54     -32.558  12.755 -62.440  1.00249.57           C  
ANISOU  441  CA  GLY A  54    26207  38396  30222  -4116  -3665    308
ATOM    442  C   GLY A  54     -32.887  11.745 -61.359  1.00246.88           C  
ANISOU  442  C   GLY A  54    25659  38177  29964  -4493  -4068    590
ATOM    443  O   GLY A  54     -32.095  10.820 -61.118  1.00246.99           O  
ANISOU  443  O   GLY A  54    25773  38075  29996  -4426  -4318    652
ATOM    444  N   GLU A  55     -34.041  11.902 -60.702  1.00245.63           N  
ANISOU  444  N   GLU A  55    25439  37976  29914  -4699  -3964    736
ATOM    445  CA  GLU A  55     -34.476  10.946 -59.689  1.00244.75           C  
ANISOU  445  CA  GLU A  55    25371  37683  29940  -4852  -4157    973
ATOM    446  C   GLU A  55     -34.528   9.527 -60.242  1.00244.69           C  
ANISOU  446  C   GLU A  55    25554  37312  30104  -4621  -4743   1080
ATOM    447  O   GLU A  55     -34.297   8.563 -59.503  1.00244.88           O  
ANISOU  447  O   GLU A  55    25635  37224  30183  -4685  -4918   1217
ATOM    448  CB  GLU A  55     -35.843  11.366 -59.145  1.00245.07           C  
ANISOU  448  CB  GLU A  55    25313  37721  30081  -5058  -3980   1098
ATOM    449  CG  GLU A  55     -36.375  10.514 -58.006  1.00246.29           C  
ANISOU  449  CG  GLU A  55    25479  37752  30349  -5247  -4101   1336
ATOM    450  CD  GLU A  55     -37.706  11.020 -57.478  1.00247.01           C  
ANISOU  450  CD  GLU A  55    25461  37863  30529  -5444  -3889   1452
ATOM    451  OE1 GLU A  55     -38.216  12.026 -58.015  1.00246.57           O  
ANISOU  451  OE1 GLU A  55    25324  37904  30458  -5427  -3654   1346
ATOM    452  OE2 GLU A  55     -38.242  10.413 -56.527  1.00247.90           O1-
ANISOU  452  OE2 GLU A  55    25564  37904  30724  -5613  -3950   1649
ATOM    453  N   ARG A  56     -34.819   9.379 -61.536  1.00240.81           N  
ANISOU  453  N   ARG A  56    25181  36633  29684  -4338  -5046   1013
ATOM    454  CA  ARG A  56     -34.787   8.062 -62.162  1.00241.34           C  
ANISOU  454  CA  ARG A  56    25475  36327  29896  -4071  -5587   1081
ATOM    455  C   ARG A  56     -33.356   7.559 -62.314  1.00241.49           C  
ANISOU  455  C   ARG A  56    25601  36359  29796  -3913  -5695   1009
ATOM    456  O   ARG A  56     -33.058   6.396 -62.011  1.00241.59           O  
ANISOU  456  O   ARG A  56    25732  36170  29890  -3856  -5973   1108
ATOM    457  CB  ARG A  56     -35.484   8.117 -63.522  1.00240.95           C  
ANISOU  457  CB  ARG A  56    25560  36058  29933  -3783  -5879   1021
ATOM    458  CG  ARG A  56     -35.533   6.789 -64.254  1.00241.19           C  
ANISOU  458  CG  ARG A  56    25864  35666  30110  -3472  -6421   1067
ATOM    459  CD  ARG A  56     -36.285   6.922 -65.567  1.00241.24           C  
ANISOU  459  CD  ARG A  56    26032  35433  30195  -3173  -6703   1004
ATOM    460  NE  ARG A  56     -36.290   5.676 -66.326  1.00241.92           N  
ANISOU  460  NE  ARG A  56    26417  35106  30397  -2844  -7182   1018
ATOM    461  CZ  ARG A  56     -36.890   5.523 -67.502  1.00242.23           C  
ANISOU  461  CZ  ARG A  56    26678  34842  30516  -2519  -7495    962
ATOM    462  NH1 ARG A  56     -37.536   6.541 -68.053  1.00242.60           N  
ANISOU  462  NH1 ARG A  56    26678  34945  30554  -2476  -7422    898
ATOM    463  NH2 ARG A  56     -36.845   4.354 -68.126  1.00242.65           N1+
ANISOU  463  NH2 ARG A  56    27010  34541  30645  -2234  -7860    971
ATOM    464  N   LEU A  57     -32.455   8.429 -62.782  1.00239.93           N  
ANISOU  464  N   LEU A  57    25346  36417  29397  -3840  -5457    827
ATOM    465  CA  LEU A  57     -31.076   8.018 -63.025  1.00241.40           C  
ANISOU  465  CA  LEU A  57    25616  36629  29475  -3669  -5555    747
ATOM    466  C   LEU A  57     -30.391   7.576 -61.738  1.00240.14           C  
ANISOU  466  C   LEU A  57    25374  36564  29302  -3891  -5436    827
ATOM    467  O   LEU A  57     -29.612   6.613 -61.741  1.00240.18           O  
ANISOU  467  O   LEU A  57    25503  36425  29330  -3749  -5701    862
ATOM    468  CB  LEU A  57     -30.300   9.158 -63.687  1.00243.65           C  
ANISOU  468  CB  LEU A  57    25950  37031  29595  -3457  -5093    474
ATOM    469  CG  LEU A  57     -28.841   8.881 -64.059  1.00245.97           C  
ANISOU  469  CG  LEU A  57    26375  37277  29805  -3199  -5074    346
ATOM    470  CD1 LEU A  57     -28.749   7.739 -65.053  1.00245.84           C  
ANISOU  470  CD1 LEU A  57    26663  36864  29879  -2821  -5607    406
ATOM    471  CD2 LEU A  57     -28.189  10.131 -64.627  1.00249.47           C  
ANISOU  471  CD2 LEU A  57    26904  37751  30133  -2972  -4471     57
ATOM    472  N   TYR A  58     -30.671   8.262 -60.627  1.00238.71           N  
ANISOU  472  N   TYR A  58    25005  36623  29073  -4222  -5043    858
ATOM    473  CA  TYR A  58     -30.079   7.864 -59.351  1.00238.30           C  
ANISOU  473  CA  TYR A  58    24898  36663  28982  -4424  -4946    946
ATOM    474  C   TYR A  58     -30.503   6.450 -58.965  1.00238.56           C  
ANISOU  474  C   TYR A  58    25068  36398  29175  -4396  -5346   1150
ATOM    475  O   TYR A  58     -29.661   5.597 -58.649  1.00239.20           O  
ANISOU  475  O   TYR A  58    25220  36419  29246  -4331  -5528   1186
ATOM    476  CB  TYR A  58     -30.466   8.862 -58.260  1.00237.89           C  
ANISOU  476  CB  TYR A  58    24665  36887  28835  -4759  -4472    958
ATOM    477  N   THR A  59     -31.810   6.180 -59.000  1.00238.44           N  
ANISOU  477  N   THR A  59    25081  36203  29312  -4442  -5477   1276
ATOM    478  CA  THR A  59     -32.317   4.874 -58.586  1.00239.73           C  
ANISOU  478  CA  THR A  59    25347  36113  29626  -4448  -5804   1463
ATOM    479  C   THR A  59     -31.812   3.767 -59.503  1.00240.25           C  
ANISOU  479  C   THR A  59    25627  35895  29762  -4115  -6235   1432
ATOM    480  O   THR A  59     -31.328   2.731 -59.033  1.00240.55           O  
ANISOU  480  O   THR A  59    25742  35843  29812  -4096  -6421   1519
ATOM    481  CB  THR A  59     -33.846   4.890 -58.554  1.00239.85           C  
ANISOU  481  CB  THR A  59    25326  36002  29805  -4557  -5840   1583
ATOM    482  OG1 THR A  59     -34.351   5.184 -59.862  1.00239.74           O  
ANISOU  482  OG1 THR A  59    25386  35832  29873  -4323  -5991   1476
ATOM    483  CG2 THR A  59     -34.348   5.936 -57.570  1.00239.83           C  
ANISOU  483  CG2 THR A  59    25126  36277  29722  -4883  -5400   1629
ATOM    484  N   GLU A  60     -31.925   3.966 -60.821  1.00240.22           N  
ANISOU  484  N   GLU A  60    25737  35748  29788  -3838  -6395   1312
ATOM    485  CA  GLU A  60     -31.436   2.962 -61.763  1.00240.64           C  
ANISOU  485  CA  GLU A  60    26028  35523  29880  -3489  -6788   1276
ATOM    486  C   GLU A  60     -29.951   2.686 -61.553  1.00240.80           C  
ANISOU  486  C   GLU A  60    26068  35654  29770  -3413  -6775   1217
ATOM    487  O   GLU A  60     -29.519   1.523 -61.537  1.00240.69           O  
ANISOU  487  O   GLU A  60    26195  35465  29792  -3276  -7040   1276
ATOM    488  CB  GLU A  60     -31.698   3.421 -63.198  1.00239.93           C  
ANISOU  488  CB  GLU A  60    26070  35300  29793  -3196  -6923   1148
ATOM    489  CG  GLU A  60     -33.170   3.523 -63.570  1.00239.66           C  
ANISOU  489  CG  GLU A  60    26049  35096  29914  -3205  -7021   1198
ATOM    490  CD  GLU A  60     -33.855   2.172 -63.629  1.00240.49           C  
ANISOU  490  CD  GLU A  60    26306  34875  30194  -3122  -7367   1322
ATOM    491  OE1 GLU A  60     -33.184   1.178 -63.978  1.00240.77           O  
ANISOU  491  OE1 GLU A  60    26531  34739  30212  -2906  -7611   1324
ATOM    492  OE2 GLU A  60     -35.066   2.105 -63.332  1.00240.56           O1-
ANISOU  492  OE2 GLU A  60    26237  34810  30356  -3280  -7380   1424
ATOM    493  N   THR A  61     -29.156   3.747 -61.384  1.00237.40           N  
ANISOU  493  N   THR A  61    25484  35530  29187  -3507  -6450   1099
ATOM    494  CA  THR A  61     -27.731   3.578 -61.120  1.00237.45           C  
ANISOU  494  CA  THR A  61    25466  35672  29081  -3461  -6408   1036
ATOM    495  C   THR A  61     -27.502   2.732 -59.873  1.00238.76           C  
ANISOU  495  C   THR A  61    25601  35847  29270  -3640  -6446   1175
ATOM    496  O   THR A  61     -26.670   1.816 -59.875  1.00239.67           O  
ANISOU  496  O   THR A  61    25817  35864  29382  -3488  -6663   1190
ATOM    497  CB  THR A  61     -27.061   4.946 -60.977  1.00236.03           C  
ANISOU  497  CB  THR A  61    25076  35868  28738  -3600  -5978    882
ATOM    498  OG1 THR A  61     -27.242   5.698 -62.183  1.00236.16           O  
ANISOU  498  OG1 THR A  61    25121  35906  28701  -3416  -5945    751
ATOM    499  CG2 THR A  61     -25.572   4.786 -60.705  1.00236.28           C  
ANISOU  499  CG2 THR A  61    25055  36046  28673  -3555  -5933    807
ATOM    500  N   LYS A  62     -28.247   3.014 -58.800  1.00234.33           N  
ANISOU  500  N   LYS A  62    24908  35407  28718  -3956  -6239   1287
ATOM    501  CA  LYS A  62     -28.100   2.227 -57.578  1.00235.55           C  
ANISOU  501  CA  LYS A  62    25044  35585  28869  -4133  -6281   1439
ATOM    502  C   LYS A  62     -28.477   0.767 -57.811  1.00235.95           C  
ANISOU  502  C   LYS A  62    25279  35318  29051  -3978  -6686   1568
ATOM    503  O   LYS A  62     -27.867  -0.141 -57.231  1.00236.59           O  
ANISOU  503  O   LYS A  62    25408  35376  29111  -3975  -6825   1646
ATOM    504  CB  LYS A  62     -28.945   2.836 -56.458  1.00236.10           C  
ANISOU  504  CB  LYS A  62    24960  35836  28910  -4486  -5989   1552
ATOM    505  CG  LYS A  62     -28.748   2.182 -55.099  1.00236.89           C  
ANISOU  505  CG  LYS A  62    25031  36015  28960  -4694  -5994   1715
ATOM    506  CD  LYS A  62     -29.490   2.941 -54.009  1.00237.01           C  
ANISOU  506  CD  LYS A  62    24903  36246  28906  -5033  -5668   1816
ATOM    507  CE  LYS A  62     -29.267   2.312 -52.643  1.00238.25           C  
ANISOU  507  CE  LYS A  62    25043  36501  28981  -5235  -5684   1986
ATOM    508  NZ  LYS A  62     -29.971   3.057 -51.562  1.00239.12           N1+
ANISOU  508  NZ  LYS A  62    25032  36829  28994  -5556  -5368   2091
ATOM    509  N   ILE A  63     -29.473   0.521 -58.667  1.00232.90           N  
ANISOU  509  N   ILE A  63    25001  34693  28798  -3847  -6874   1587
ATOM    510  CA  ILE A  63     -29.859  -0.851 -58.991  1.00234.46           C  
ANISOU  510  CA  ILE A  63    25382  34586  29118  -3692  -7240   1695
ATOM    511  C   ILE A  63     -28.706  -1.581 -59.669  1.00234.76           C  
ANISOU  511  C   ILE A  63    25584  34511  29101  -3381  -7463   1611
ATOM    512  O   ILE A  63     -28.340  -2.701 -59.283  1.00236.16           O  
ANISOU  512  O   ILE A  63    25847  34596  29289  -3349  -7647   1710
ATOM    513  CB  ILE A  63     -31.124  -0.862 -59.868  1.00234.54           C  
ANISOU  513  CB  ILE A  63    25471  34367  29277  -3597  -7385   1706
ATOM    514  CG1 ILE A  63     -32.313  -0.279 -59.102  1.00234.59           C  
ANISOU  514  CG1 ILE A  63    25303  34474  29358  -3917  -7181   1820
ATOM    515  CG2 ILE A  63     -31.433  -2.274 -60.342  1.00236.22           C  
ANISOU  515  CG2 ILE A  63    25889  34258  29605  -3415  -7754   1798
ATOM    516  CD1 ILE A  63     -33.518   0.001 -59.972  1.00234.48           C  
ANISOU  516  CD1 ILE A  63    25320  34284  29487  -3835  -7272   1798
ATOM    517  N   PHE A  64     -28.114  -0.955 -60.693  1.00233.04           N  
ANISOU  517  N   PHE A  64    25417  34307  28820  -3145  -7445   1437
ATOM    518  CA  PHE A  64     -26.968  -1.570 -61.360  1.00233.45           C  
ANISOU  518  CA  PHE A  64    25621  34268  28810  -2840  -7636   1363
ATOM    519  C   PHE A  64     -25.828  -1.818 -60.380  1.00233.69           C  
ANISOU  519  C   PHE A  64    25548  34492  28753  -2952  -7550   1380
ATOM    520  O   PHE A  64     -25.156  -2.856 -60.445  1.00233.52           O  
ANISOU  520  O   PHE A  64    25648  34358  28721  -2787  -7761   1416
ATOM    521  CB  PHE A  64     -26.498  -0.693 -62.520  1.00232.71           C  
ANISOU  521  CB  PHE A  64    25574  34200  28646  -2604  -7593   1190
ATOM    522  CG  PHE A  64     -25.333  -1.266 -63.277  1.00233.06           C  
ANISOU  522  CG  PHE A  64    25782  34146  28625  -2274  -7783   1127
ATOM    523  CD1 PHE A  64     -25.511  -2.326 -64.151  1.00233.61           C  
ANISOU  523  CD1 PHE A  64    26125  33899  28739  -1977  -8092   1174
ATOM    524  CD2 PHE A  64     -24.060  -0.744 -63.117  1.00233.07           C  
ANISOU  524  CD2 PHE A  64    25660  34375  28522  -2269  -7634   1031
ATOM    525  CE1 PHE A  64     -24.442  -2.856 -64.849  1.00234.06           C  
ANISOU  525  CE1 PHE A  64    26346  33858  28727  -1669  -8245   1138
ATOM    526  CE2 PHE A  64     -22.987  -1.270 -63.812  1.00234.31           C  
ANISOU  526  CE2 PHE A  64    25958  34440  28629  -1961  -7811    988
ATOM    527  CZ  PHE A  64     -23.179  -2.327 -64.679  1.00234.59           C  
ANISOU  527  CZ  PHE A  64    26283  34151  28699  -1653  -8114   1046
ATOM    528  N   LEU A  65     -25.602  -0.876 -59.459  1.00234.75           N  
ANISOU  528  N   LEU A  65    25459  34919  28815  -3231  -7233   1357
ATOM    529  CA  LEU A  65     -24.590  -1.071 -58.426  1.00234.55           C  
ANISOU  529  CA  LEU A  65    25328  35083  28705  -3359  -7147   1377
ATOM    530  C   LEU A  65     -24.870  -2.331 -57.616  1.00235.06           C  
ANISOU  530  C   LEU A  65    25468  35031  28814  -3439  -7343   1562
ATOM    531  O   LEU A  65     -23.980  -3.168 -57.420  1.00235.16           O  
ANISOU  531  O   LEU A  65    25541  35017  28793  -3325  -7500   1580
ATOM    532  CB  LEU A  65     -24.530   0.156 -57.513  1.00233.91           C  
ANISOU  532  CB  LEU A  65    25013  35328  28533  -3673  -6753   1340
ATOM    533  CG  LEU A  65     -24.029   1.462 -58.134  1.00232.86           C  
ANISOU  533  CG  LEU A  65    24762  35390  28324  -3642  -6490   1151
ATOM    534  CD1 LEU A  65     -24.195   2.618 -57.160  1.00232.00           C  
ANISOU  534  CD1 LEU A  65    24436  35595  28117  -3979  -6069   1129
ATOM    535  CD2 LEU A  65     -22.579   1.333 -58.573  1.00232.96           C  
ANISOU  535  CD2 LEU A  65    24774  35458  28282  -3432  -6557   1028
ATOM    536  N   GLU A  66     -26.111  -2.489 -57.145  1.00233.10           N  
ANISOU  536  N   GLU A  66    25209  34716  28643  -3638  -7336   1710
ATOM    537  CA  GLU A  66     -26.461  -3.667 -56.355  1.00235.14           C  
ANISOU  537  CA  GLU A  66    25528  34872  28945  -3745  -7513   1910
ATOM    538  C   GLU A  66     -26.230  -4.951 -57.142  1.00235.94           C  
ANISOU  538  C   GLU A  66    25844  34695  29106  -3455  -7857   1935
ATOM    539  O   GLU A  66     -25.611  -5.900 -56.640  1.00236.95           O  
ANISOU  539  O   GLU A  66    26025  34805  29199  -3430  -7997   2016
ATOM    540  CB  GLU A  66     -27.917  -3.579 -55.894  1.00235.54           C  
ANISOU  540  CB  GLU A  66    25527  34877  29091  -3993  -7459   2069
ATOM    541  CG  GLU A  66     -28.349  -4.743 -55.015  1.00237.48           C  
ANISOU  541  CG  GLU A  66    25817  35031  29384  -4145  -7627   2302
ATOM    542  CD  GLU A  66     -29.784  -4.621 -54.544  1.00238.40           C  
ANISOU  542  CD  GLU A  66    25862  35113  29607  -4405  -7568   2472
ATOM    543  OE1 GLU A  66     -30.453  -3.635 -54.918  1.00238.26           O  
ANISOU  543  OE1 GLU A  66    25763  35139  29628  -4454  -7395   2399
ATOM    544  OE2 GLU A  66     -30.244  -5.514 -53.801  1.00239.82           O1-
ANISOU  544  OE2 GLU A  66    26063  35223  29836  -4562  -7695   2686
ATOM    545  N   ASN A  67     -26.725  -5.000 -58.382  1.00234.89           N  
ANISOU  545  N   ASN A  67    25846  34346  29054  -3229  -7992   1869
ATOM    546  CA  ASN A  67     -26.579  -6.210 -59.186  1.00235.52           C  
ANISOU  546  CA  ASN A  67    26153  34151  29181  -2954  -8300   1902
ATOM    547  C   ASN A  67     -25.111  -6.564 -59.398  1.00235.41           C  
ANISOU  547  C   ASN A  67    26196  34191  29056  -2731  -8364   1815
ATOM    548  O   ASN A  67     -24.725  -7.736 -59.294  1.00236.21           O  
ANISOU  548  O   ASN A  67    26419  34173  29159  -2636  -8563   1908
ATOM    549  CB  ASN A  67     -27.293  -6.036 -60.525  1.00234.84           C  
ANISOU  549  CB  ASN A  67    26210  33843  29175  -2737  -8409   1830
ATOM    550  CG  ASN A  67     -28.801  -5.992 -60.378  1.00234.63           C  
ANISOU  550  CG  ASN A  67    26150  33705  29295  -2928  -8420   1940
ATOM    551  OD1 ASN A  67     -29.385  -6.759 -59.611  1.00235.63           O  
ANISOU  551  OD1 ASN A  67    26259  33765  29503  -3122  -8502   2120
ATOM    552  ND2 ASN A  67     -29.442  -5.090 -61.112  1.00233.29           N  
ANISOU  552  ND2 ASN A  67    25965  33512  29161  -2873  -8345   1839
ATOM    553  N   HIS A  68     -24.275  -5.562 -59.683  1.00233.11           N  
ANISOU  553  N   HIS A  68    25811  34083  28676  -2655  -8196   1645
ATOM    554  CA  HIS A  68     -22.852  -5.825 -59.878  1.00234.12           C  
ANISOU  554  CA  HIS A  68    25965  34278  28714  -2451  -8250   1562
ATOM    555  C   HIS A  68     -22.208  -6.333 -58.592  1.00234.73           C  
ANISOU  555  C   HIS A  68    25937  34509  28740  -2626  -8232   1646
ATOM    556  O   HIS A  68     -21.415  -7.287 -58.615  1.00235.53           O  
ANISOU  556  O   HIS A  68    26132  34547  28810  -2463  -8406   1680
ATOM    557  CB  HIS A  68     -22.158  -4.554 -60.372  1.00233.52           C  
ANISOU  557  CB  HIS A  68    25773  34381  28573  -2383  -8057   1376
ATOM    558  CG  HIS A  68     -20.735  -4.759 -60.788  1.00234.64           C  
ANISOU  558  CG  HIS A  68    25939  34567  28644  -2141  -8129   1288
ATOM    559  ND1 HIS A  68     -20.388  -5.373 -61.972  1.00235.43           N  
ANISOU  559  ND1 HIS A  68    26261  34454  28739  -1785  -8343   1274
ATOM    560  CD2 HIS A  68     -19.571  -4.420 -60.184  1.00235.08           C  
ANISOU  560  CD2 HIS A  68    25824  34856  28641  -2206  -8012   1218
ATOM    561  CE1 HIS A  68     -19.072  -5.407 -62.079  1.00236.07           C  
ANISOU  561  CE1 HIS A  68    26298  34638  28760  -1637  -8357   1207
ATOM    562  NE2 HIS A  68     -18.552  -4.837 -61.006  1.00235.82           N  
ANISOU  562  NE2 HIS A  68    26018  34877  28704  -1890  -8166   1164
ATOM    563  N   VAL A  69     -22.553  -5.716 -57.457  1.00229.13           N  
ANISOU  563  N   VAL A  69    25045  34002  28013  -2956  -8021   1693
ATOM    564  CA  VAL A  69     -22.014  -6.147 -56.168  1.00230.35           C  
ANISOU  564  CA  VAL A  69    25112  34309  28103  -3135  -8002   1786
ATOM    565  C   VAL A  69     -22.372  -7.601 -55.889  1.00232.01           C  
ANISOU  565  C   VAL A  69    25474  34323  28356  -3113  -8262   1974
ATOM    566  O   VAL A  69     -21.542  -8.375 -55.396  1.00233.35           O  
ANISOU  566  O   VAL A  69    25668  34525  28468  -3062  -8377   2019
ATOM    567  CB  VAL A  69     -22.505  -5.215 -55.044  1.00230.08           C  
ANISOU  567  CB  VAL A  69    24886  34509  28027  -3498  -7722   1831
ATOM    568  CG1 VAL A  69     -22.155  -5.789 -53.685  1.00231.63           C  
ANISOU  568  CG1 VAL A  69    25030  34832  28147  -3687  -7741   1967
ATOM    569  CG2 VAL A  69     -21.886  -3.836 -55.195  1.00228.84           C  
ANISOU  569  CG2 VAL A  69    24565  34580  27804  -3532  -7445   1643
ATOM    570  N   ARG A  70     -23.607  -8.003 -56.204  1.00232.74           N  
ANISOU  570  N   ARG A  70    25666  34207  28556  -3155  -8361   2090
ATOM    571  CA  ARG A  70     -23.999  -9.386 -55.943  1.00234.19           C  
ANISOU  571  CA  ARG A  70    25988  34195  28798  -3163  -8603   2283
ATOM    572  C   ARG A  70     -23.334 -10.354 -56.916  1.00235.18           C  
ANISOU  572  C   ARG A  70    26314  34118  28928  -2822  -8840   2247
ATOM    573  O   ARG A  70     -22.987 -11.480 -56.536  1.00236.11           O  
ANISOU  573  O   ARG A  70    26519  34160  29033  -2793  -9013   2367
ATOM    574  CB  ARG A  70     -25.519  -9.529 -55.985  1.00233.91           C  
ANISOU  574  CB  ARG A  70    25984  33991  28902  -3327  -8645   2423
ATOM    575  CG  ARG A  70     -26.213  -8.911 -54.785  1.00233.65           C  
ANISOU  575  CG  ARG A  70    25770  34146  28860  -3697  -8444   2538
ATOM    576  CD  ARG A  70     -27.705  -9.183 -54.798  1.00234.35           C  
ANISOU  576  CD  ARG A  70    25881  34055  29106  -3859  -8514   2701
ATOM    577  NE  ARG A  70     -28.370  -8.578 -53.648  1.00233.95           N  
ANISOU  577  NE  ARG A  70    25658  34197  29036  -4214  -8309   2829
ATOM    578  CZ  ARG A  70     -28.501  -9.174 -52.467  1.00235.25           C  
ANISOU  578  CZ  ARG A  70    25788  34428  29168  -4449  -8342   3042
ATOM    579  NH1 ARG A  70     -28.010 -10.392 -52.279  1.00236.22           N  
ANISOU  579  NH1 ARG A  70    26032  34437  29282  -4367  -8574   3144
ATOM    580  NH2 ARG A  70     -29.120  -8.553 -51.473  1.00235.08           N1+
ANISOU  580  NH2 ARG A  70    25618  34592  29111  -4765  -8141   3163
ATOM    581  N   HIS A  71     -23.147  -9.940 -58.174  1.00236.04           N  
ANISOU  581  N   HIS A  71    26505  34136  29043  -2563  -8850   2096
ATOM    582  CA  HIS A  71     -22.409 -10.779 -59.115  1.00236.88           C  
ANISOU  582  CA  HIS A  71    26806  34068  29128  -2230  -9047   2069
ATOM    583  C   HIS A  71     -20.998 -11.053 -58.610  1.00237.73           C  
ANISOU  583  C   HIS A  71    26854  34349  29124  -2152  -9049   2032
ATOM    584  O   HIS A  71     -20.558 -12.209 -58.549  1.00238.92           O  
ANISOU  584  O   HIS A  71    27127  34391  29261  -2043  -9233   2129
ATOM    585  CB  HIS A  71     -22.363 -10.124 -60.495  1.00235.27           C  
ANISOU  585  CB  HIS A  71    26695  33773  28925  -1971  -9029   1918
ATOM    586  CG  HIS A  71     -21.676 -10.958 -61.532  1.00236.12           C  
ANISOU  586  CG  HIS A  71    27030  33678  29009  -1627  -9222   1915
ATOM    587  ND1 HIS A  71     -20.312 -10.921 -61.730  1.00236.25           N  
ANISOU  587  ND1 HIS A  71    27030  33810  28924  -1432  -9210   1832
ATOM    588  CD2 HIS A  71     -22.160 -11.858 -62.420  1.00237.05           C  
ANISOU  588  CD2 HIS A  71    27399  33469  29199  -1450  -9427   1994
ATOM    589  CE1 HIS A  71     -19.987 -11.759 -62.699  1.00236.99           C  
ANISOU  589  CE1 HIS A  71    27364  33661  29022  -1145  -9390   1873
ATOM    590  NE2 HIS A  71     -21.090 -12.340 -63.135  1.00237.66           N  
ANISOU  590  NE2 HIS A  71    27623  33468  29210  -1152  -9523   1967
ATOM    591  N   LEU A  72     -20.273  -9.997 -58.233  1.00237.77           N  
ANISOU  591  N   LEU A  72    26666  34622  29055  -2215  -8849   1893
ATOM    592  CA  LEU A  72     -18.938 -10.202 -57.685  1.00238.25           C  
ANISOU  592  CA  LEU A  72    26642  34857  29026  -2160  -8854   1851
ATOM    593  C   LEU A  72     -18.964 -10.839 -56.302  1.00239.71           C  
ANISOU  593  C   LEU A  72    26766  35132  29182  -2393  -8887   1999
ATOM    594  O   LEU A  72     -17.917 -11.297 -55.832  1.00240.66           O  
ANISOU  594  O   LEU A  72    26854  35354  29232  -2326  -8950   1994
ATOM    595  CB  LEU A  72     -18.168  -8.880 -57.648  1.00236.19           C  
ANISOU  595  CB  LEU A  72    26179  34846  28717  -2188  -8634   1663
ATOM    596  CG  LEU A  72     -17.487  -8.478 -58.962  1.00234.64           C  
ANISOU  596  CG  LEU A  72    26038  34601  28512  -1880  -8652   1519
ATOM    597  CD1 LEU A  72     -18.495  -8.068 -60.023  1.00233.77           C  
ANISOU  597  CD1 LEU A  72    26054  34313  28456  -1797  -8646   1499
ATOM    598  CD2 LEU A  72     -16.483  -7.363 -58.727  1.00233.10           C  
ANISOU  598  CD2 LEU A  72    25613  34672  28280  -1931  -8459   1356
ATOM    599  N   HIS A  73     -20.125 -10.885 -55.645  1.00236.94           N  
ANISOU  599  N   HIS A  73    26400  34746  28882  -2660  -8853   2139
ATOM    600  CA  HIS A  73     -20.253 -11.670 -54.424  1.00238.41           C  
ANISOU  600  CA  HIS A  73    26573  34972  29040  -2862  -8928   2322
ATOM    601  C   HIS A  73     -20.378 -13.156 -54.720  1.00240.07           C  
ANISOU  601  C   HIS A  73    26990  34930  29295  -2724  -9201   2472
ATOM    602  O   HIS A  73     -19.912 -13.982 -53.927  1.00241.74           O  
ANISOU  602  O   HIS A  73    27219  35182  29451  -2764  -9310   2584
ATOM    603  CB  HIS A  73     -21.456 -11.204 -53.603  1.00237.81           C  
ANISOU  603  CB  HIS A  73    26406  34950  29002  -3208  -8796   2448
ATOM    604  CG  HIS A  73     -21.674 -12.002 -52.355  1.00240.24           C  
ANISOU  604  CG  HIS A  73    26711  35294  29275  -3430  -8880   2666
ATOM    605  ND1 HIS A  73     -20.865 -11.887 -51.245  1.00241.81           N  
ANISOU  605  ND1 HIS A  73    26799  35733  29345  -3545  -8814   2675
ATOM    606  CD2 HIS A  73     -22.604 -12.937 -52.046  1.00241.76           C  
ANISOU  606  CD2 HIS A  73    27002  35309  29546  -3559  -9035   2891
ATOM    607  CE1 HIS A  73     -21.289 -12.712 -50.304  1.00243.58           C  
ANISOU  607  CE1 HIS A  73    27063  35934  29553  -3728  -8925   2901
ATOM    608  NE2 HIS A  73     -22.344 -13.360 -50.765  1.00243.80           N  
ANISOU  608  NE2 HIS A  73    27213  35709  29711  -3748  -9058   3040
ATOM    609  N   LYS A  74     -21.006 -13.520 -55.840  1.00238.50           N  
ANISOU  609  N   LYS A  74    26956  34469  29194  -2565  -9316   2481
ATOM    610  CA  LYS A  74     -21.048 -14.928 -56.215  1.00240.18           C  
ANISOU  610  CA  LYS A  74    27378  34425  29454  -2421  -9571   2614
ATOM    611  C   LYS A  74     -19.725 -15.389 -56.813  1.00240.54           C  
ANISOU  611  C   LYS A  74    27508  34468  29417  -2104  -9661   2525
ATOM    612  O   LYS A  74     -19.318 -16.536 -56.593  1.00242.29           O  
ANISOU  612  O   LYS A  74    27839  34601  29621  -2032  -9834   2639
ATOM    613  CB  LYS A  74     -22.196 -15.187 -57.192  1.00239.95           C  
ANISOU  613  CB  LYS A  74    27507  34097  29569  -2372  -9674   2660
ATOM    614  CG  LYS A  74     -22.390 -16.659 -57.529  1.00241.86           C  
ANISOU  614  CG  LYS A  74    27970  34042  29886  -2271  -9939   2813
ATOM    615  CD  LYS A  74     -22.831 -17.441 -56.298  1.00243.75           C  
ANISOU  615  CD  LYS A  74    28176  34283  30154  -2544 -10026   3032
ATOM    616  CE  LYS A  74     -23.003 -18.921 -56.602  1.00245.77           C  
ANISOU  616  CE  LYS A  74    28650  34238  30495  -2460 -10295   3187
ATOM    617  NZ  LYS A  74     -24.135 -19.173 -57.534  1.00245.82           N1+
ANISOU  617  NZ  LYS A  74    28799  33926  30677  -2438 -10414   3221
ATOM    618  N   ARG A  75     -19.040 -14.519 -57.561  1.00240.88           N  
ANISOU  618  N   ARG A  75    27501  34609  29412  -1916  -9548   2335
ATOM    619  CA  ARG A  75     -17.695 -14.852 -58.023  1.00241.49           C  
ANISOU  619  CA  ARG A  75    27621  34724  29409  -1634  -9613   2260
ATOM    620  C   ARG A  75     -16.720 -14.935 -56.856  1.00242.89           C  
ANISOU  620  C   ARG A  75    27638  35157  29492  -1724  -9585   2257
ATOM    621  O   ARG A  75     -15.909 -15.865 -56.776  1.00244.79           O  
ANISOU  621  O   ARG A  75    27950  35373  29684  -1574  -9728   2312
ATOM    622  CB  ARG A  75     -17.214 -13.827 -59.049  1.00240.02           C  
ANISOU  622  CB  ARG A  75    27403  34592  29203  -1437  -9496   2074
ATOM    623  CG  ARG A  75     -15.771 -14.044 -59.491  1.00241.09           C  
ANISOU  623  CG  ARG A  75    27546  34792  29264  -1160  -9547   2005
ATOM    624  CD  ARG A  75     -15.591 -15.364 -60.225  1.00242.66           C  
ANISOU  624  CD  ARG A  75    28006  34717  29477   -917  -9764   2130
ATOM    625  NE  ARG A  75     -16.345 -15.407 -61.474  1.00242.16           N  
ANISOU  625  NE  ARG A  75    28161  34363  29485   -769  -9820   2142
ATOM    626  CZ  ARG A  75     -15.895 -14.928 -62.629  1.00241.39           C  
ANISOU  626  CZ  ARG A  75    28152  34189  29376   -512  -9796   2053
ATOM    627  NH1 ARG A  75     -14.692 -14.373 -62.696  1.00241.13           N  
ANISOU  627  NH1 ARG A  75    27987  34357  29274   -385  -9717   1952
ATOM    628  NH2 ARG A  75     -16.646 -15.007 -63.719  1.00240.94           N1+
ANISOU  628  NH2 ARG A  75    28321  33838  29386   -381  -9861   2069
ATOM    629  N   VAL A  76     -16.779 -13.964 -55.942  1.00239.49           N  
ANISOU  629  N   VAL A  76    26995  34966  29033  -1968  -9401   2194
ATOM    630  CA  VAL A  76     -15.892 -13.977 -54.784  1.00240.61           C  
ANISOU  630  CA  VAL A  76    26987  35346  29087  -2070  -9375   2187
ATOM    631  C   VAL A  76     -16.192 -15.178 -53.897  1.00242.73           C  
ANISOU  631  C   VAL A  76    27346  35543  29337  -2187  -9538   2399
ATOM    632  O   VAL A  76     -15.280 -15.809 -53.352  1.00244.31           O  
ANISOU  632  O   VAL A  76    27535  35830  29462  -2116  -9639   2426
ATOM    633  CB  VAL A  76     -16.009 -12.653 -54.009  1.00239.47           C  
ANISOU  633  CB  VAL A  76    26618  35448  28921  -2332  -9132   2091
ATOM    634  N   LEU A  77     -17.474 -15.517 -53.743  1.00242.50           N  
ANISOU  634  N   LEU A  77    27403  35353  29384  -2368  -9575   2557
ATOM    635  CA  LEU A  77     -17.840 -16.693 -52.961  1.00244.76           C  
ANISOU  635  CA  LEU A  77    27784  35543  29670  -2490  -9745   2780
ATOM    636  C   LEU A  77     -17.410 -17.979 -53.655  1.00246.47           C  
ANISOU  636  C   LEU A  77    28204  35540  29902  -2227  -9972   2846
ATOM    637  O   LEU A  77     -17.106 -18.972 -52.984  1.00248.92           O  
ANISOU  637  O   LEU A  77    28572  35837  30168  -2246 -10118   2984
ATOM    638  CB  LEU A  77     -19.348 -16.699 -52.704  1.00245.10           C  
ANISOU  638  CB  LEU A  77    27856  35454  29818  -2757  -9733   2940
ATOM    639  CG  LEU A  77     -19.906 -17.810 -51.812  1.00247.85           C  
ANISOU  639  CG  LEU A  77    28284  35702  30185  -2946  -9898   3200
ATOM    640  CD1 LEU A  77     -19.333 -17.711 -50.406  1.00248.86           C  
ANISOU  640  CD1 LEU A  77    28284  36098  30174  -3121  -9846   3256
ATOM    641  CD2 LEU A  77     -21.427 -17.761 -51.780  1.00247.58           C  
ANISOU  641  CD2 LEU A  77    28270  35510  30289  -3187  -9894   3349
ATOM    642  N   GLU A  78     -17.378 -17.980 -54.991  1.00242.65           N  
ANISOU  642  N   GLU A  78    27840  34882  29474  -1981 -10005   2758
ATOM    643  CA  GLU A  78     -16.894 -19.146 -55.724  1.00243.55           C  
ANISOU  643  CA  GLU A  78    28157  34786  29595  -1717 -10202   2818
ATOM    644  C   GLU A  78     -15.428 -19.423 -55.415  1.00244.52           C  
ANISOU  644  C   GLU A  78    28220  35089  29596  -1544 -10234   2762
ATOM    645  O   GLU A  78     -15.018 -20.584 -55.303  1.00246.53           O  
ANISOU  645  O   GLU A  78    28598  35246  29827  -1440 -10406   2879
ATOM    646  CB  GLU A  78     -17.089 -18.942 -57.226  1.00241.61           C  
ANISOU  646  CB  GLU A  78    28051  34333  29416  -1485 -10209   2729
ATOM    647  CG  GLU A  78     -16.632 -20.117 -58.074  1.00242.72           C  
ANISOU  647  CG  GLU A  78    28427  34226  29570  -1213 -10402   2798
ATOM    648  CD  GLU A  78     -16.832 -19.878 -59.557  1.00241.55           C  
ANISOU  648  CD  GLU A  78    28440  33857  29482   -984 -10409   2719
ATOM    649  OE1 GLU A  78     -17.317 -18.788 -59.925  1.00239.74           O  
ANISOU  649  OE1 GLU A  78    28132  33679  29277  -1030 -10267   2607
ATOM    650  OE2 GLU A  78     -16.498 -20.779 -60.355  1.00242.53           O1-
ANISOU  650  OE2 GLU A  78    28779  33746  29624   -756 -10557   2773
ATOM    651  N   SER A  79     -14.624 -18.368 -55.281  1.00240.62           N  
ANISOU  651  N   SER A  79    27533  34857  29036  -1512 -10077   2584
ATOM    652  CA  SER A  79     -13.207 -18.515 -54.978  1.00242.02           C  
ANISOU  652  CA  SER A  79    27619  35223  29115  -1354 -10107   2513
ATOM    653  C   SER A  79     -13.016 -19.179 -53.621  1.00244.34           C  
ANISOU  653  C   SER A  79    27869  35630  29339  -1514 -10193   2635
ATOM    654  O   SER A  79     -13.357 -18.599 -52.585  1.00244.00           O  
ANISOU  654  O   SER A  79    27686  35753  29269  -1779 -10092   2639
ATOM    655  CB  SER A  79     -12.509 -17.153 -55.011  1.00240.92           C  
ANISOU  655  CB  SER A  79    27255  35333  28949  -1345  -9919   2296
ATOM    656  OG  SER A  79     -12.558 -16.586 -56.309  1.00238.41           O  
ANISOU  656  OG  SER A  79    26989  34914  28682  -1166  -9857   2193
ATOM    657  N   GLU A  80     -12.477 -20.397 -53.618  1.00241.27           N  
ANISOU  657  N   GLU A  80    27610  35149  28913  -1356 -10378   2746
ATOM    658  CA  GLU A  80     -12.280 -21.154 -52.384  1.00243.40           C  
ANISOU  658  CA  GLU A  80    27868  35505  29106  -1478 -10488   2879
ATOM    659  C   GLU A  80     -11.066 -20.583 -51.662  1.00243.43           C  
ANISOU  659  C   GLU A  80    27661  35824  29009  -1447 -10429   2738
ATOM    660  O   GLU A  80      -9.921 -20.858 -52.029  1.00243.25           O  
ANISOU  660  O   GLU A  80    27618  35861  28944  -1195 -10494   2666
ATOM    661  CB  GLU A  80     -12.108 -22.638 -52.687  1.00245.80           C  
ANISOU  661  CB  GLU A  80    28387  35595  29411  -1309 -10705   3041
ATOM    662  CG  GLU A  80     -12.213 -23.546 -51.467  1.00248.93           C  
ANISOU  662  CG  GLU A  80    28819  36017  29744  -1463 -10840   3224
ATOM    663  CD  GLU A  80     -10.904 -23.686 -50.714  1.00250.86           C  
ANISOU  663  CD  GLU A  80    28946  36514  29855  -1356 -10884   3169
ATOM    664  OE1 GLU A  80      -9.834 -23.580 -51.349  1.00250.89           O  
ANISOU  664  OE1 GLU A  80    28906  36588  29833  -1093 -10881   3040
ATOM    665  OE2 GLU A  80     -10.946 -23.902 -49.484  1.00252.92           O1-
ANISOU  665  OE2 GLU A  80    29159  36901  30037  -1535 -10929   3263
ATOM    666  N   GLU A  81     -11.321 -19.760 -50.645  1.00239.07           N  
ANISOU  666  N   GLU A  81    26946  35466  28422  -1710 -10306   2702
ATOM    667  CA  GLU A  81     -10.333 -19.133 -49.770  1.00240.00           C  
ANISOU  667  CA  GLU A  81    26856  35877  28455  -1749 -10249   2572
ATOM    668  C   GLU A  81      -9.468 -18.103 -50.486  1.00238.50           C  
ANISOU  668  C   GLU A  81    26505  35812  28302  -1595 -10126   2330
ATOM    669  O   GLU A  81      -8.630 -17.465 -49.838  1.00239.88           O  
ANISOU  669  O   GLU A  81    26487  36220  28438  -1636 -10072   2198
ATOM    670  CB  GLU A  81      -9.423 -20.162 -49.084  1.00242.89           C  
ANISOU  670  CB  GLU A  81    27251  36316  28720  -1631 -10439   2649
ATOM    671  CG  GLU A  81     -10.149 -21.042 -48.081  1.00245.12           C  
ANISOU  671  CG  GLU A  81    27652  36535  28947  -1827 -10554   2885
ATOM    672  CD  GLU A  81      -9.238 -22.062 -47.433  1.00248.29           C  
ANISOU  672  CD  GLU A  81    28091  37008  29238  -1693 -10747   2960
ATOM    673  OE1 GLU A  81      -8.067 -22.166 -47.854  1.00248.78           O  
ANISOU  673  OE1 GLU A  81    28095  37150  29279  -1431 -10799   2835
ATOM    674  OE2 GLU A  81      -9.693 -22.759 -46.502  1.00250.63           O1-
ANISOU  674  OE2 GLU A  81    28473  37284  29470  -1850 -10850   3152
ATOM    675  N   GLN A  82      -9.638 -17.915 -51.793  1.00237.78           N  
ANISOU  675  N   GLN A  82    26488  35569  28290  -1425 -10087   2273
ATOM    676  CA  GLN A  82      -8.971 -16.846 -52.534  1.00235.11           C  
ANISOU  676  CA  GLN A  82    26001  35333  27999  -1306  -9957   2062
ATOM    677  C   GLN A  82      -9.928 -15.704 -52.836  1.00232.03           C  
ANISOU  677  C   GLN A  82    25560  34923  27676  -1489  -9757   1991
ATOM    678  O   GLN A  82      -9.872 -15.092 -53.907  1.00229.84           O  
ANISOU  678  O   GLN A  82    25278  34594  27458  -1355  -9678   1883
ATOM    679  CB  GLN A  82      -8.353 -17.385 -53.820  1.00235.13           C  
ANISOU  679  CB  GLN A  82    26118  35197  28025   -963 -10054   2057
ATOM    680  CG  GLN A  82      -7.168 -18.309 -53.601  1.00237.97           C  
ANISOU  680  CG  GLN A  82    26475  35622  28321   -756 -10222   2095
ATOM    681  CD  GLN A  82      -6.558 -18.791 -54.902  1.00238.48           C  
ANISOU  681  CD  GLN A  82    26655  35546  28409   -424 -10297   2117
ATOM    682  OE1 GLN A  82      -7.061 -18.491 -55.985  1.00237.42           O  
ANISOU  682  OE1 GLN A  82    26630  35245  28333   -342 -10238   2111
ATOM    683  NE2 GLN A  82      -5.464 -19.537 -54.802  1.00239.65           N  
ANISOU  683  NE2 GLN A  82    26789  35758  28511   -226 -10430   2153
ATOM    684  N   VAL A  83     -10.828 -15.408 -51.895  1.00230.68           N  
ANISOU  684  N   VAL A  83    25358  34797  27491  -1795  -9673   2065
ATOM    685  CA  VAL A  83     -11.780 -14.318 -52.079  1.00229.42           C  
ANISOU  685  CA  VAL A  83    25142  34637  27390  -1991  -9471   2013
ATOM    686  C   VAL A  83     -11.050 -12.984 -52.142  1.00228.65           C  
ANISOU  686  C   VAL A  83    24820  34746  27312  -2016  -9287   1795
ATOM    687  O   VAL A  83     -11.540 -12.022 -52.746  1.00226.81           O  
ANISOU  687  O   VAL A  83    24543  34498  27139  -2068  -9122   1706
ATOM    688  CB  VAL A  83     -12.826 -14.344 -50.945  1.00229.68           C  
ANISOU  688  CB  VAL A  83    25178  34697  27393  -2324  -9423   2171
ATOM    689  CG1 VAL A  83     -13.894 -13.277 -51.158  1.00227.89           C  
ANISOU  689  CG1 VAL A  83    24899  34461  27226  -2525  -9213   2140
ATOM    690  CG2 VAL A  83     -13.440 -15.730 -50.809  1.00231.31           C  
ANISOU  690  CG2 VAL A  83    25590  34701  27596  -2312  -9626   2398
ATOM    691  N   LEU A  84      -9.861 -12.908 -51.540  1.00219.71           N  
ANISOU  691  N   LEU A  84    23538  33802  26140  -1980  -9317   1707
ATOM    692  CA  LEU A  84      -9.085 -11.676 -51.520  1.00218.92           C  
ANISOU  692  CA  LEU A  84    23202  33897  26079  -2028  -9151   1506
ATOM    693  C   LEU A  84      -8.319 -11.429 -52.815  1.00218.09           C  
ANISOU  693  C   LEU A  84    23067  33744  26054  -1746  -9167   1373
ATOM    694  O   LEU A  84      -7.887 -10.296 -53.053  1.00217.02           O  
ANISOU  694  O   LEU A  84    22743  33730  25982  -1797  -9002   1216
ATOM    695  CB  LEU A  84      -8.125 -11.695 -50.325  1.00220.91           C  
ANISOU  695  CB  LEU A  84    23298  34365  26273  -2113  -9192   1467
ATOM    696  CG  LEU A  84      -7.152 -12.873 -50.182  1.00223.25           C  
ANISOU  696  CG  LEU A  84    23645  34653  26526  -1877  -9444   1508
ATOM    697  CD1 LEU A  84      -5.855 -12.658 -50.950  1.00223.47           C  
ANISOU  697  CD1 LEU A  84    23540  34735  26632  -1623  -9487   1346
ATOM    698  CD2 LEU A  84      -6.868 -13.151 -48.712  1.00225.38           C  
ANISOU  698  CD2 LEU A  84    23855  35086  26694  -2044  -9509   1564
ATOM    699  N   VAL A  85      -8.141 -12.449 -53.653  1.00222.31           N  
ANISOU  699  N   VAL A  85    23780  34107  26581  -1459  -9351   1449
ATOM    700  CA  VAL A  85      -7.459 -12.255 -54.931  1.00221.37           C  
ANISOU  700  CA  VAL A  85    23655  33937  26521  -1178  -9370   1359
ATOM    701  C   VAL A  85      -8.414 -11.663 -55.961  1.00219.64           C  
ANISOU  701  C   VAL A  85    23539  33569  26345  -1167  -9258   1348
ATOM    702  O   VAL A  85      -8.180 -10.574 -56.500  1.00217.93           O  
ANISOU  702  O   VAL A  85    23185  33425  26192  -1169  -9113   1211
ATOM    703  CB  VAL A  85      -6.848 -13.579 -55.424  1.00222.24           C  
ANISOU  703  CB  VAL A  85    23925  33930  26587   -872  -9594   1470
ATOM    704  CG1 VAL A  85      -6.229 -13.396 -56.801  1.00221.43           C  
ANISOU  704  CG1 VAL A  85    23842  33756  26534   -576  -9607   1421
ATOM    705  CG2 VAL A  85      -5.814 -14.085 -54.432  1.00224.57           C  
ANISOU  705  CG2 VAL A  85    24095  34392  26838   -864  -9707   1462
ATOM    706  N   MET A  86      -9.507 -12.376 -56.251  1.00225.59           N  
ANISOU  706  N   MET A  86    24530  34109  27074  -1161  -9329   1496
ATOM    707  CA  MET A  86     -10.565 -11.809 -57.079  1.00223.93           C  
ANISOU  707  CA  MET A  86    24419  33757  26907  -1185  -9231   1490
ATOM    708  C   MET A  86     -11.185 -10.575 -56.440  1.00222.26           C  
ANISOU  708  C   MET A  86    24034  33690  26722  -1503  -9002   1405
ATOM    709  O   MET A  86     -11.780  -9.755 -57.148  1.00220.84           O  
ANISOU  709  O   MET A  86    23862  33464  26585  -1519  -8879   1343
ATOM    710  CB  MET A  86     -11.647 -12.856 -57.353  1.00223.45           C  
ANISOU  710  CB  MET A  86    24625  33435  26840  -1160  -9362   1673
ATOM    711  CG  MET A  86     -11.207 -13.983 -58.271  1.00224.32           C  
ANISOU  711  CG  MET A  86    24952  33343  26935   -841  -9556   1772
ATOM    712  SD  MET A  86     -10.760 -13.389 -59.915  1.00222.85           S  
ANISOU  712  SD  MET A  86    24839  33052  26782   -530  -9526   1684
ATOM    713  CE  MET A  86     -12.362 -12.883 -60.538  1.00220.76           C  
ANISOU  713  CE  MET A  86    24719  32589  26570   -635  -9450   1697
ATOM    714  N   TYR A  87     -11.066 -10.431 -55.119  1.00217.78           N  
ANISOU  714  N   TYR A  87    23324  33298  26123  -1753  -8940   1415
ATOM    715  CA  TYR A  87     -11.480  -9.203 -54.456  1.00216.63           C  
ANISOU  715  CA  TYR A  87    22999  33322  25988  -2061  -8692   1344
ATOM    716  C   TYR A  87     -10.482  -8.077 -54.690  1.00215.94           C  
ANISOU  716  C   TYR A  87    22682  33423  25945  -2053  -8535   1153
ATOM    717  O   TYR A  87     -10.877  -6.907 -54.755  1.00214.36           O  
ANISOU  717  O   TYR A  87    22363  33317  25768  -2229  -8298   1073
ATOM    718  CB  TYR A  87     -11.662  -9.458 -52.958  1.00218.01           C  
ANISOU  718  CB  TYR A  87    23118  33622  26093  -2324  -8680   1443
ATOM    719  CG  TYR A  87     -12.141  -8.261 -52.171  1.00217.04           C  
ANISOU  719  CG  TYR A  87    22831  33685  25951  -2657  -8410   1405
ATOM    720  CD1 TYR A  87     -13.459  -7.834 -52.254  1.00215.65           C  
ANISOU  720  CD1 TYR A  87    22710  33439  25788  -2831  -8279   1476
ATOM    721  CD2 TYR A  87     -11.280  -7.567 -51.331  1.00217.67           C  
ANISOU  721  CD2 TYR A  87    22697  34012  25994  -2799  -8283   1304
ATOM    722  CE1 TYR A  87     -13.903  -6.743 -51.533  1.00214.82           C  
ANISOU  722  CE1 TYR A  87    22459  33517  25646  -3133  -8013   1454
ATOM    723  CE2 TYR A  87     -11.715  -6.476 -50.605  1.00216.88           C  
ANISOU  723  CE2 TYR A  87    22458  34094  25852  -3104  -8015   1277
ATOM    724  CZ  TYR A  87     -13.028  -6.069 -50.709  1.00215.42           C  
ANISOU  724  CZ  TYR A  87    22338  33846  25666  -3268  -7874   1357
ATOM    725  OH  TYR A  87     -13.468  -4.983 -49.988  1.00214.68           O  
ANISOU  725  OH  TYR A  87    22112  33947  25511  -3565  -7590   1338
ATOM    726  N   HIS A  88      -9.195  -8.408 -54.825  1.00212.84           N  
ANISOU  726  N   HIS A  88    22211  33091  25568  -1858  -8653   1088
ATOM    727  CA  HIS A  88      -8.200  -7.396 -55.166  1.00212.97           C  
ANISOU  727  CA  HIS A  88    21989  33272  25657  -1839  -8516    920
ATOM    728  C   HIS A  88      -8.373  -6.924 -56.603  1.00212.02           C  
ANISOU  728  C   HIS A  88    21924  33042  25592  -1651  -8475    869
ATOM    729  O   HIS A  88      -8.360  -5.718 -56.877  1.00211.16           O  
ANISOU  729  O   HIS A  88    21644  33061  25524  -1773  -8241    762
ATOM    730  CB  HIS A  88      -6.789  -7.944 -54.947  1.00214.82           C  
ANISOU  730  CB  HIS A  88    22115  33592  25916  -1671  -8676    879
ATOM    731  CG  HIS A  88      -5.706  -6.975 -55.307  1.00215.21           C  
ANISOU  731  CG  HIS A  88    21887  33812  26069  -1654  -8543    722
ATOM    732  ND1 HIS A  88      -5.403  -5.875 -54.534  1.00214.83           N  
ANISOU  732  ND1 HIS A  88    21572  34009  26045  -1939  -8293    611
ATOM    733  CD2 HIS A  88      -4.857  -6.939 -56.362  1.00216.29           C  
ANISOU  733  CD2 HIS A  88    21959  33929  26294  -1391  -8605    670
ATOM    734  CE1 HIS A  88      -4.413  -5.204 -55.095  1.00216.29           C  
ANISOU  734  CE1 HIS A  88    21517  34327  26334  -1867  -8190    488
ATOM    735  NE2 HIS A  88      -4.064  -5.829 -56.206  1.00217.39           N  
ANISOU  735  NE2 HIS A  88    21766  34309  26522  -1535  -8383    530
ATOM    736  N   ARG A  89      -8.528  -7.865 -57.539  1.00219.29           N  
ANISOU  736  N   ARG A  89    23087  33739  26496  -1350  -8686    956
ATOM    737  CA  ARG A  89      -8.837  -7.479 -58.912  1.00218.30           C  
ANISOU  737  CA  ARG A  89    23067  33478  26397  -1155  -8670    935
ATOM    738  C   ARG A  89     -10.185  -6.775 -58.992  1.00216.52           C  
ANISOU  738  C   ARG A  89    22901  33203  26164  -1354  -8508    938
ATOM    739  O   ARG A  89     -10.394  -5.927 -59.867  1.00216.04           O  
ANISOU  739  O   ARG A  89    22822  33132  26130  -1304  -8398    871
ATOM    740  CB  ARG A  89      -8.819  -8.706 -59.824  1.00218.84           C  
ANISOU  740  CB  ARG A  89    23422  33301  26424   -807  -8915   1062
ATOM    741  CG  ARG A  89      -7.476  -9.420 -59.878  1.00221.11           C  
ANISOU  741  CG  ARG A  89    23661  33635  26716   -577  -9069   1080
ATOM    742  CD  ARG A  89      -6.417  -8.570 -60.564  1.00223.84           C  
ANISOU  742  CD  ARG A  89    23801  34095  27155   -438  -9005    966
ATOM    743  NE  ARG A  89      -5.136  -9.267 -60.660  1.00226.29           N  
ANISOU  743  NE  ARG A  89    24052  34439  27488   -202  -9157    999
ATOM    744  CZ  ARG A  89      -4.022  -8.721 -61.137  1.00229.56           C  
ANISOU  744  CZ  ARG A  89    24245  34962  28016    -64  -9133    927
ATOM    745  NH1 ARG A  89      -4.025  -7.466 -61.564  1.00230.50           N  
ANISOU  745  NH1 ARG A  89    24172  35182  28224   -152  -8947    824
ATOM    746  NH2 ARG A  89      -2.902  -9.430 -61.185  1.00232.54           N1+
ANISOU  746  NH2 ARG A  89    24569  35361  28425    154  -9280    977
ATOM    747  N   TYR A  90     -11.102  -7.103 -58.080  1.00218.15           N  
ANISOU  747  N   TYR A  90    23169  33386  26334  -1580  -8492   1026
ATOM    748  CA  TYR A  90     -12.403  -6.444 -58.049  1.00216.61           C  
ANISOU  748  CA  TYR A  90    23005  33156  26142  -1789  -8333   1043
ATOM    749  C   TYR A  90     -12.264  -4.978 -57.656  1.00216.27           C  
ANISOU  749  C   TYR A  90    22697  33365  26111  -2048  -8022    917
ATOM    750  O   TYR A  90     -12.722  -4.081 -58.375  1.00215.49           O  
ANISOU  750  O   TYR A  90    22575  33273  26026  -2061  -7870    852
ATOM    751  CB  TYR A  90     -13.332  -7.178 -57.080  1.00216.09           C  
ANISOU  751  CB  TYR A  90    23036  33025  26044  -1980  -8390   1194
ATOM    752  N   TRP A  91     -11.631  -4.715 -56.509  1.00214.54           N  
ANISOU  752  N   TRP A  91    22279  33367  25871  -2257  -7909    883
ATOM    753  CA  TRP A  91     -11.488  -3.338 -56.046  1.00213.89           C  
ANISOU  753  CA  TRP A  91    21941  33551  25777  -2526  -7570    768
ATOM    754  C   TRP A  91     -10.602  -2.524 -56.980  1.00214.59           C  
ANISOU  754  C   TRP A  91    21860  33764  25910  -2398  -7442    617
ATOM    755  O   TRP A  91     -10.920  -1.371 -57.295  1.00213.87           O  
ANISOU  755  O   TRP A  91    21642  33817  25801  -2526  -7153    522
ATOM    756  CB  TRP A  91     -10.925  -3.310 -54.626  1.00214.17           C  
ANISOU  756  CB  TRP A  91    21819  33789  25766  -2747  -7499    765
ATOM    757  CG  TRP A  91     -10.769  -1.921 -54.093  1.00213.25           C  
ANISOU  757  CG  TRP A  91    21453  33958  25616  -3023  -7127    640
ATOM    758  CD1 TRP A  91     -11.767  -1.037 -53.804  1.00211.17           C  
ANISOU  758  CD1 TRP A  91    21162  33777  25295  -3269  -6855    643
ATOM    759  CD2 TRP A  91      -9.539  -1.244 -53.806  1.00214.96           C  
ANISOU  759  CD2 TRP A  91    21404  34422  25850  -3075  -6966    484
ATOM    760  NE1 TRP A  91     -11.236   0.144 -53.344  1.00210.67           N  
ANISOU  760  NE1 TRP A  91    20852  33999  25194  -3466  -6522    493
ATOM    761  CE2 TRP A  91      -9.869   0.042 -53.337  1.00213.82           C  
ANISOU  761  CE2 TRP A  91    21095  34503  25643  -3356  -6581    388
ATOM    762  CE3 TRP A  91      -8.190  -1.604 -53.896  1.00217.50           C  
ANISOU  762  CE3 TRP A  91    21602  34799  26239  -2910  -7102    413
ATOM    763  CZ2 TRP A  91      -8.900   0.971 -52.959  1.00215.81           C  
ANISOU  763  CZ2 TRP A  91    21073  35030  25897  -3476  -6322    209
ATOM    764  CZ3 TRP A  91      -7.229  -0.681 -53.520  1.00218.27           C  
ANISOU  764  CZ3 TRP A  91    21405  35172  26357  -3036  -6856    244
ATOM    765  CH2 TRP A  91      -7.590   0.591 -53.057  1.00217.69           C  
ANISOU  765  CH2 TRP A  91    21180  35314  26218  -3316  -6466    136
ATOM    766  N   GLU A  92      -9.485  -3.100 -57.431  1.00215.15           N  
ANISOU  766  N   GLU A  92    21910  33806  26030  -2144  -7633    594
ATOM    767  CA  GLU A  92      -8.595  -2.366 -58.323  1.00217.53           C  
ANISOU  767  CA  GLU A  92    22016  34258  26376  -2013  -7503    467
ATOM    768  C   GLU A  92      -9.191  -2.218 -59.718  1.00218.48           C  
ANISOU  768  C   GLU A  92    22302  34222  26488  -1790  -7547    486
ATOM    769  O   GLU A  92      -8.742  -1.359 -60.485  1.00220.51           O  
ANISOU  769  O   GLU A  92    22375  34670  26738  -1715  -7346    369
ATOM    770  CB  GLU A  92      -7.226  -3.051 -58.372  1.00219.72           C  
ANISOU  770  CB  GLU A  92    22207  34555  26720  -1799  -7702    459
ATOM    771  CG  GLU A  92      -6.142  -2.255 -59.087  1.00222.95           C  
ANISOU  771  CG  GLU A  92    22317  35208  27185  -1689  -7513    315
ATOM    772  CD  GLU A  92      -4.770  -2.888 -58.959  1.00225.50           C  
ANISOU  772  CD  GLU A  92    22505  35579  27596  -1514  -7688    309
ATOM    773  OE1 GLU A  92      -4.664  -3.961 -58.328  1.00225.07           O  
ANISOU  773  OE1 GLU A  92    22614  35359  27543  -1472  -7970    414
ATOM    774  OE2 GLU A  92      -3.795  -2.308 -59.482  1.00228.17           O1-
ANISOU  774  OE2 GLU A  92    22547  36155  27994  -1401  -7516    176
ATOM    775  N   GLU A  93     -10.198  -3.025 -60.059  1.00222.23           N  
ANISOU  775  N   GLU A  93    23105  34386  26946  -1671  -7781    615
ATOM    776  CA  GLU A  93     -11.013  -2.808 -61.246  1.00222.46           C  
ANISOU  776  CA  GLU A  93    23327  34241  26958  -1502  -7818    638
ATOM    777  C   GLU A  93     -12.356  -2.161 -60.917  1.00220.14           C  
ANISOU  777  C   GLU A  93    23058  33955  26630  -1766  -7629    640
ATOM    778  O   GLU A  93     -13.291  -2.253 -61.718  1.00220.55           O  
ANISOU  778  O   GLU A  93    23330  33792  26675  -1639  -7727    688
ATOM    779  CB  GLU A  93     -11.241  -4.123 -61.995  1.00222.04           C  
ANISOU  779  CB  GLU A  93    23631  33825  26908  -1155  -8183    764
ATOM    780  CG  GLU A  93     -10.020  -4.680 -62.710  1.00225.49           C  
ANISOU  780  CG  GLU A  93    24101  34200  27374   -812  -8372    783
ATOM    781  CD  GLU A  93     -10.318  -5.986 -63.426  1.00225.25           C  
ANISOU  781  CD  GLU A  93    24453  33820  27314   -488  -8659    921
ATOM    782  OE1 GLU A  93     -11.438  -6.515 -63.258  1.00222.58           O  
ANISOU  782  OE1 GLU A  93    24310  33326  26936   -562  -8707   1000
ATOM    783  OE2 GLU A  93      -9.436  -6.482 -64.157  1.00228.01           O1-
ANISOU  783  OE2 GLU A  93    24900  34045  27689   -169  -8811    968
ATOM    784  N   TYR A  94     -12.477  -1.521 -59.753  1.00220.32           N  
ANISOU  784  N   TYR A  94    22870  34210  26631  -2118  -7365    596
ATOM    785  CA  TYR A  94     -13.740  -0.899 -59.373  1.00217.56           C  
ANISOU  785  CA  TYR A  94    22532  33880  26250  -2373  -7170    615
ATOM    786  C   TYR A  94     -13.570   0.549 -58.925  1.00217.49           C  
ANISOU  786  C   TYR A  94    22225  34225  26186  -2653  -6728    468
ATOM    787  O   TYR A  94     -14.479   1.368 -59.104  1.00215.70           O  
ANISOU  787  O   TYR A  94    21982  34053  25920  -2786  -6511    436
ATOM    788  CB  TYR A  94     -14.417  -1.710 -58.265  1.00215.89           C  
ANISOU  788  CB  TYR A  94    22427  33560  26041  -2536  -7285    755
ATOM    789  CG  TYR A  94     -15.749  -1.144 -57.826  1.00214.77           C  
ANISOU  789  CG  TYR A  94    22291  33435  25879  -2797  -7098    806
ATOM    790  CD1 TYR A  94     -16.882  -1.289 -58.616  1.00214.22           C  
ANISOU  790  CD1 TYR A  94    22407  33143  25842  -2699  -7200    863
ATOM    791  CD2 TYR A  94     -15.873  -0.462 -56.622  1.00215.34           C  
ANISOU  791  CD2 TYR A  94    22183  33744  25894  -3131  -6822    800
ATOM    792  CE1 TYR A  94     -18.101  -0.771 -58.219  1.00213.75           C  
ANISOU  792  CE1 TYR A  94    22332  33103  25780  -2935  -7033    915
ATOM    793  CE2 TYR A  94     -17.088   0.058 -56.216  1.00214.55           C  
ANISOU  793  CE2 TYR A  94    22084  33665  25770  -3363  -6644    861
ATOM    794  CZ  TYR A  94     -18.199  -0.099 -57.019  1.00213.24           C  
ANISOU  794  CZ  TYR A  94    22082  33283  25658  -3268  -6750    920
ATOM    795  OH  TYR A  94     -19.411   0.417 -56.619  1.00210.86           O  
ANISOU  795  OH  TYR A  94    21763  33008  25348  -3498  -6577    986
ATOM    796  N   SER A  95     -12.415   0.879 -58.345  1.00215.52           N  
ANISOU  796  N   SER A  95    21736  34222  25932  -2737  -6577    363
ATOM    797  CA  SER A  95     -12.229   2.202 -57.755  1.00214.86           C  
ANISOU  797  CA  SER A  95    21373  34475  25790  -3017  -6129    202
ATOM    798  C   SER A  95     -12.169   3.286 -58.826  1.00213.38           C  
ANISOU  798  C   SER A  95    21039  34469  25565  -2939  -5839     14
ATOM    799  O   SER A  95     -12.934   4.260 -58.788  1.00212.00           O  
ANISOU  799  O   SER A  95    20805  34416  25328  -3120  -5527    -62
ATOM    800  CB  SER A  95     -10.963   2.216 -56.895  1.00216.44           C  
ANISOU  800  CB  SER A  95    21360  34869  26009  -3098  -6067    120
ATOM    801  OG  SER A  95      -9.804   2.031 -57.689  1.00217.12           O  
ANISOU  801  OG  SER A  95    21331  35007  26158  -2843  -6152     27
ATOM    802  N   LYS A  96     -11.255   3.137 -59.791  1.00213.59           N  
ANISOU  802  N   LYS A  96    20994  34542  25618  -2651  -5918    -76
ATOM    803  CA  LYS A  96     -11.117   4.140 -60.844  1.00217.06           C  
ANISOU  803  CA  LYS A  96    21489  34884  26101  -2414  -5453   -311
ATOM    804  C   LYS A  96     -12.412   4.300 -61.628  1.00216.50           C  
ANISOU  804  C   LYS A  96    21716  34544  26000  -2300  -5436   -258
ATOM    805  O   LYS A  96     -12.780   5.417 -62.013  1.00217.46           O  
ANISOU  805  O   LYS A  96    21860  34652  26114  -2289  -4970   -433
ATOM    806  CB  LYS A  96      -9.966   3.766 -61.779  1.00221.41           C  
ANISOU  806  CB  LYS A  96    22165  35182  26780  -1966  -5426   -401
ATOM    807  CG  LYS A  96      -8.590   3.809 -61.131  1.00222.58           C  
ANISOU  807  CG  LYS A  96    21991  35584  26996  -2042  -5349   -507
ATOM    808  CD  LYS A  96      -7.500   3.455 -62.131  1.00226.64           C  
ANISOU  808  CD  LYS A  96    22638  35816  27657  -1576  -5292   -589
ATOM    809  CE  LYS A  96      -6.116   3.580 -61.515  1.00227.19           C  
ANISOU  809  CE  LYS A  96    22356  36138  27827  -1648  -5185   -714
ATOM    810  NZ  LYS A  96      -5.884   2.561 -60.455  1.00224.03           N1+
ANISOU  810  NZ  LYS A  96    21790  35965  27367  -1870  -5718   -513
ATOM    811  N   GLY A  97     -13.120   3.196 -61.873  1.00220.48           N  
ANISOU  811  N   GLY A  97    22450  34829  26493  -2212  -5946    -21
ATOM    812  CA  GLY A  97     -14.407   3.289 -62.540  1.00219.04           C  
ANISOU  812  CA  GLY A  97    22527  34402  26294  -2130  -5987     39
ATOM    813  C   GLY A  97     -15.446   4.004 -61.698  1.00215.43           C  
ANISOU  813  C   GLY A  97    21888  34208  25758  -2558  -5830     67
ATOM    814  O   GLY A  97     -16.292   4.731 -62.226  1.00215.73           O  
ANISOU  814  O   GLY A  97    22047  34134  25788  -2512  -5578     -8
ATOM    815  N   ALA A  98     -15.396   3.812 -60.378  1.00215.36           N  
ANISOU  815  N   ALA A  98    21718  34369  25740  -2890  -5866    157
ATOM    816  CA  ALA A  98     -16.320   4.511 -59.492  1.00213.32           C  
ANISOU  816  CA  ALA A  98    21398  34206  25449  -3224  -5589    172
ATOM    817  C   ALA A  98     -16.072   6.013 -59.518  1.00213.47           C  
ANISOU  817  C   ALA A  98    21142  34589  25379  -3382  -5068    -74
ATOM    818  O   ALA A  98     -17.015   6.809 -59.617  1.00212.47           O  
ANISOU  818  O   ALA A  98    21002  34523  25203  -3512  -4829   -113
ATOM    819  CB  ALA A  98     -16.198   3.966 -58.069  1.00212.96           C  
ANISOU  819  CB  ALA A  98    21347  34143  25425  -3436  -5648    294
ATOM    820  N   ASP A  99     -14.803   6.422 -59.437  1.00213.12           N  
ANISOU  820  N   ASP A  99    20865  34784  25328  -3367  -4868   -260
ATOM    821  CA  ASP A  99     -14.486   7.845 -59.502  1.00215.28           C  
ANISOU  821  CA  ASP A  99    20975  35237  25583  -3434  -4262   -536
ATOM    822  C   ASP A  99     -14.855   8.431 -60.859  1.00218.92           C  
ANISOU  822  C   ASP A  99    21718  35363  26099  -3066  -3950   -672
ATOM    823  O   ASP A  99     -15.366   9.555 -60.942  1.00219.53           O  
ANISOU  823  O   ASP A  99    21773  35500  26138  -3156  -3503   -811
ATOM    824  CB  ASP A  99     -13.003   8.070 -59.205  1.00216.53           C  
ANISOU  824  CB  ASP A  99    20908  35568  25796  -3415  -4082   -713
ATOM    825  CG  ASP A  99     -12.643   9.540 -59.125  1.00217.96           C  
ANISOU  825  CG  ASP A  99    20916  35920  25981  -3520  -3437   -999
ATOM    826  OD1 ASP A  99     -12.998  10.188 -58.118  1.00215.04           O  
ANISOU  826  OD1 ASP A  99    20328  35867  25510  -3919  -3271  -1023
ATOM    827  OD2 ASP A  99     -12.005  10.050 -60.071  1.00222.05           O1-
ANISOU  827  OD2 ASP A  99    21525  36245  26601  -3200  -3084  -1199
ATOM    828  N   TYR A 100     -14.604   7.682 -61.937  1.00215.06           N  
ANISOU  828  N   TYR A 100    21512  34511  25689  -2637  -4177   -633
ATOM    829  CA  TYR A 100     -14.988   8.151 -63.265  1.00218.46           C  
ANISOU  829  CA  TYR A 100    22258  34594  26153  -2253  -3924   -748
ATOM    830  C   TYR A 100     -16.499   8.291 -63.396  1.00216.17           C  
ANISOU  830  C   TYR A 100    22110  34217  25807  -2348  -4013   -638
ATOM    831  O   TYR A 100     -16.978   9.193 -64.094  1.00218.76           O  
ANISOU  831  O   TYR A 100    22582  34416  26123  -2198  -3632   -780
ATOM    832  CB  TYR A 100     -14.440   7.209 -64.337  1.00221.99           C  
ANISOU  832  CB  TYR A 100    23004  34662  26680  -1776  -4205   -705
ATOM    833  CG  TYR A 100     -12.941   7.296 -64.525  1.00226.19           C  
ANISOU  833  CG  TYR A 100    23440  35204  27298  -1582  -3985   -863
ATOM    834  CD1 TYR A 100     -12.218   8.369 -64.021  1.00227.02           C  
ANISOU  834  CD1 TYR A 100    23251  35582  27423  -1767  -3477  -1081
ATOM    835  CD2 TYR A 100     -12.248   6.304 -65.209  1.00228.65           C  
ANISOU  835  CD2 TYR A 100    23950  35244  27683  -1214  -4282   -796
ATOM    836  CE1 TYR A 100     -10.848   8.453 -64.191  1.00230.52           C  
ANISOU  836  CE1 TYR A 100    23581  36029  27978  -1596  -3273  -1229
ATOM    837  CE2 TYR A 100     -10.879   6.379 -65.383  1.00232.44           C  
ANISOU  837  CE2 TYR A 100    24326  35727  28263  -1032  -4070   -935
ATOM    838  CZ  TYR A 100     -10.184   7.456 -64.873  1.00233.65           C  
ANISOU  838  CZ  TYR A 100    24167  36156  28455  -1226  -3567  -1152
ATOM    839  OH  TYR A 100      -8.821   7.534 -65.045  1.00237.46           O  
ANISOU  839  OH  TYR A 100    24521  36635  29068  -1051  -3355  -1293
ATOM    840  N   MET A 101     -17.267   7.416 -62.741  1.00222.95           N  
ANISOU  840  N   MET A 101    22931  35140  26640  -2588  -4503   -385
ATOM    841  CA  MET A 101     -18.717   7.580 -62.740  1.00220.13           C  
ANISOU  841  CA  MET A 101    22652  34733  26255  -2727  -4576   -276
ATOM    842  C   MET A 101     -19.135   8.790 -61.915  1.00219.15           C  
ANISOU  842  C   MET A 101    22274  34941  26054  -3104  -4121   -372
ATOM    843  O   MET A 101     -20.109   9.472 -62.255  1.00219.14           O  
ANISOU  843  O   MET A 101    22358  34871  26035  -3106  -3906   -409
ATOM    844  CB  MET A 101     -19.403   6.317 -62.218  1.00216.20           C  
ANISOU  844  CB  MET A 101    22162  34210  25773  -2899  -5200     24
ATOM    845  CG  MET A 101     -19.306   5.121 -63.147  1.00217.14           C  
ANISOU  845  CG  MET A 101    22590  33945  25968  -2518  -5678    137
ATOM    846  SD  MET A 101     -20.264   3.714 -62.553  1.00213.87           S  
ANISOU  846  SD  MET A 101    22254  33385  25622  -2694  -6309    463
ATOM    847  CE  MET A 101     -19.247   3.154 -61.191  1.00213.61           C  
ANISOU  847  CE  MET A 101    22087  33459  25617  -2874  -6283    504
ATOM    848  N   ASP A 102     -18.416   9.070 -60.824  1.00221.39           N  
ANISOU  848  N   ASP A 102    22249  35584  26286  -3421  -3977   -416
ATOM    849  CA  ASP A 102     -18.725  10.259 -60.035  1.00220.26           C  
ANISOU  849  CA  ASP A 102    21875  35756  26058  -3773  -3522   -526
ATOM    850  C   ASP A 102     -18.464  11.526 -60.841  1.00223.67           C  
ANISOU  850  C   ASP A 102    22383  36102  26499  -3557  -2914   -809
ATOM    851  O   ASP A 102     -19.231  12.493 -60.759  1.00222.76           O  
ANISOU  851  O   ASP A 102    22244  36065  26330  -3695  -2558   -878
ATOM    852  CB  ASP A 102     -17.910  10.259 -58.741  1.00218.28           C  
ANISOU  852  CB  ASP A 102    21304  35886  25746  -4124  -3518   -531
ATOM    853  CG  ASP A 102     -18.412  11.279 -57.733  1.00216.32           C  
ANISOU  853  CG  ASP A 102    20978  35789  25423  -4445  -3083   -566
ATOM    854  OD1 ASP A 102     -19.396  11.989 -58.031  1.00216.38           O  
ANISOU  854  OD1 ASP A 102    21001  35819  25392  -4512  -2862   -597
ATOM    855  OD2 ASP A 102     -17.822  11.370 -56.636  1.00214.99           O1-
ANISOU  855  OD2 ASP A 102    20746  35715  25223  -4617  -2974   -562
ATOM    856  N   CYS A 103     -17.388  11.537 -61.632  1.00225.33           N  
ANISOU  856  N   CYS A 103    22693  36141  26780  -3209  -2774   -969
ATOM    857  CA  CYS A 103     -17.163  12.655 -62.542  1.00224.36           C  
ANISOU  857  CA  CYS A 103    22696  35873  26677  -2946  -2205  -1225
ATOM    858  C   CYS A 103     -18.176  12.659 -63.680  1.00223.43           C  
ANISOU  858  C   CYS A 103    22930  35400  26563  -2625  -2243  -1191
ATOM    859  O   CYS A 103     -18.453  13.715 -64.260  1.00223.68           O  
ANISOU  859  O   CYS A 103    23066  35351  26571  -2495  -1766  -1364
ATOM    860  CB  CYS A 103     -15.742  12.606 -63.103  1.00225.15           C  
ANISOU  860  CB  CYS A 103    22816  35860  26870  -2644  -2047  -1391
ATOM    861  SG  CYS A 103     -14.440  12.873 -61.879  1.00226.37           S  
ANISOU  861  SG  CYS A 103    22538  36427  27044  -2987  -1895  -1505
ATOM    862  N   LEU A 104     -18.739  11.494 -64.008  1.00227.43           N  
ANISOU  862  N   LEU A 104    23626  35688  27100  -2492  -2809   -973
ATOM    863  CA  LEU A 104     -19.714  11.397 -65.085  1.00228.50           C  
ANISOU  863  CA  LEU A 104    24099  35473  27246  -2181  -2920   -936
ATOM    864  C   LEU A 104     -21.095  11.890 -64.669  1.00225.62           C  
ANISOU  864  C   LEU A 104    23670  35221  26835  -2457  -2873   -855
ATOM    865  O   LEU A 104     -21.936  12.150 -65.537  1.00227.14           O  
ANISOU  865  O   LEU A 104    24108  35163  27030  -2219  -2834   -877
ATOM    866  CB  LEU A 104     -19.792   9.948 -65.581  1.00227.57           C  
ANISOU  866  CB  LEU A 104    24205  35071  27191  -1944  -3561   -739
ATOM    867  CG  LEU A 104     -20.652   9.600 -66.800  1.00228.28           C  
ANISOU  867  CG  LEU A 104    24687  34744  27307  -1560  -3792   -696
ATOM    868  CD1 LEU A 104     -20.158  10.312 -68.045  1.00231.13           C  
ANISOU  868  CD1 LEU A 104    25333  34832  27656  -1090  -3369   -930
ATOM    869  CD2 LEU A 104     -20.645   8.105 -67.022  1.00227.91           C  
ANISOU  869  CD2 LEU A 104    24799  34477  27321  -1417  -4454   -488
ATOM    870  N   TYR A 105     -21.341  12.042 -63.371  1.00235.06           N  
ANISOU  870  N   TYR A 105    24546  36782  27986  -2939  -2866   -765
ATOM    871  CA  TYR A 105     -22.627  12.482 -62.844  1.00232.26           C  
ANISOU  871  CA  TYR A 105    24096  36559  27593  -3237  -2813   -669
ATOM    872  C   TYR A 105     -22.499  13.830 -62.144  1.00231.98           C  
ANISOU  872  C   TYR A 105    23827  36847  27469  -3525  -2212   -839
ATOM    873  O   TYR A 105     -23.058  14.047 -61.067  1.00229.36           O  
ANISOU  873  O   TYR A 105    23266  36797  27082  -3941  -2187   -738
ATOM    874  CB  TYR A 105     -23.210  11.438 -61.894  1.00228.11           C  
ANISOU  874  CB  TYR A 105    23425  36158  27087  -3565  -3344   -382
ATOM    875  CG  TYR A 105     -23.659  10.165 -62.574  1.00228.04           C  
ANISOU  875  CG  TYR A 105    23655  35814  27175  -3319  -3942   -196
ATOM    876  CD1 TYR A 105     -23.850  10.117 -63.949  1.00229.86           C  
ANISOU  876  CD1 TYR A 105    24221  35660  27455  -2858  -3981   -278
ATOM    877  CD2 TYR A 105     -23.888   9.008 -61.841  1.00227.25           C  
ANISOU  877  CD2 TYR A 105    23460  35772  27111  -3543  -4467     60
ATOM    878  CE1 TYR A 105     -24.259   8.956 -64.573  1.00229.89           C  
ANISOU  878  CE1 TYR A 105    24454  35347  27545  -2633  -4541   -118
ATOM    879  CE2 TYR A 105     -24.297   7.842 -62.457  1.00228.03           C  
ANISOU  879  CE2 TYR A 105    23778  35556  27307  -3328  -5014    225
ATOM    880  CZ  TYR A 105     -24.481   7.821 -63.823  1.00228.59           C  
ANISOU  880  CZ  TYR A 105    24176  35248  27429  -2876  -5056    132
ATOM    881  OH  TYR A 105     -24.889   6.662 -64.440  1.00228.75           O  
ANISOU  881  OH  TYR A 105    24426  34945  27544  -2661  -5613    287
ATOM    882  N   ARG A 106     -21.753  14.755 -62.751  1.00238.91           N  
ANISOU  882  N   ARG A 106    24770  37675  28332  -3302  -1707  -1100
ATOM    883  CA  ARG A 106     -21.566  16.068 -62.142  1.00238.64           C  
ANISOU  883  CA  ARG A 106    24526  37926  28219  -3560  -1114  -1282
ATOM    884  C   ARG A 106     -22.858  16.877 -62.170  1.00237.80           C  
ANISOU  884  C   ARG A 106    24458  37835  28061  -3665   -868  -1271
ATOM    885  O   ARG A 106     -23.320  17.366 -61.132  1.00235.32           O  
ANISOU  885  O   ARG A 106    23914  37821  27676  -4073   -715  -1226
ATOM    886  CB  ARG A 106     -20.439  16.820 -62.851  1.00242.54           C  
ANISOU  886  CB  ARG A 106    25090  38328  28736  -3276   -632  -1563
ATOM    887  CG  ARG A 106     -20.121  18.172 -62.239  1.00241.10           C  
ANISOU  887  CG  ARG A 106    24689  38430  28488  -3537     -9  -1773
ATOM    888  CD  ARG A 106     -19.598  18.019 -60.820  1.00237.83           C  
ANISOU  888  CD  ARG A 106    23923  38405  28035  -3992   -109  -1726
ATOM    889  NE  ARG A 106     -18.385  17.208 -60.769  1.00238.47           N  
ANISOU  889  NE  ARG A 106    23934  38478  28194  -3894   -378  -1730
ATOM    890  CZ  ARG A 106     -17.160  17.683 -60.965  1.00238.57           C  
ANISOU  890  CZ  ARG A 106    23867  38511  28269  -3781    -44  -1956
ATOM    891  NH1 ARG A 106     -16.979  18.971 -61.223  1.00237.10           N  
ANISOU  891  NH1 ARG A 106    23666  38349  28072  -3759    582  -2199
ATOM    892  NH2 ARG A 106     -16.114  16.870 -60.900  1.00239.64           N1+
ANISOU  892  NH2 ARG A 106    23928  38636  28486  -3691   -329  -1937
ATOM    893  N   TYR A 107     -23.459  17.028 -63.354  1.00247.55           N  
ANISOU  893  N   TYR A 107    25992  38743  29325  -3290   -830  -1310
ATOM    894  CA  TYR A 107     -24.724  17.747 -63.446  1.00247.18           C  
ANISOU  894  CA  TYR A 107    25988  38688  29240  -3357   -630  -1292
ATOM    895  C   TYR A 107     -25.858  17.000 -62.758  1.00243.94           C  
ANISOU  895  C   TYR A 107    25470  38355  28863  -3645  -1097  -1012
ATOM    896  O   TYR A 107     -26.839  17.629 -62.348  1.00242.17           O  
ANISOU  896  O   TYR A 107    25153  38257  28605  -3867   -906   -970
ATOM    897  CB  TYR A 107     -25.089  18.012 -64.908  1.00251.94           C  
ANISOU  897  CB  TYR A 107    26956  38906  29864  -2858   -528  -1398
ATOM    898  CG  TYR A 107     -26.344  18.843 -65.068  1.00251.38           C  
ANISOU  898  CG  TYR A 107    26935  38822  29755  -2893   -285  -1404
ATOM    899  CD1 TYR A 107     -26.321  20.215 -64.855  1.00250.07           C  
ANISOU  899  CD1 TYR A 107    26685  38831  29501  -3006    363  -1589
ATOM    900  CD2 TYR A 107     -27.553  18.254 -65.416  1.00251.00           C  
ANISOU  900  CD2 TYR A 107    27008  38590  29771  -2818   -707  -1224
ATOM    901  CE1 TYR A 107     -27.464  20.980 -64.992  1.00249.39           C  
ANISOU  901  CE1 TYR A 107    26642  38736  29377  -3031    592  -1590
ATOM    902  CE2 TYR A 107     -28.702  19.011 -65.554  1.00250.42           C  
ANISOU  902  CE2 TYR A 107    26962  38508  29678  -2845   -493  -1228
ATOM    903  CZ  TYR A 107     -28.651  20.373 -65.342  1.00250.25           C  
ANISOU  903  CZ  TYR A 107    26863  38665  29555  -2947    160  -1408
ATOM    904  OH  TYR A 107     -29.791  21.131 -65.480  1.00250.96           O  
ANISOU  904  OH  TYR A 107    26982  38747  29624  -2964    380  -1407
ATOM    905  N   LEU A 108     -25.744  15.676 -62.624  1.00244.77           N  
ANISOU  905  N   LEU A 108    25585  38378  29040  -3644  -1690   -818
ATOM    906  CA  LEU A 108     -26.747  14.916 -61.887  1.00240.96           C  
ANISOU  906  CA  LEU A 108    24979  37971  28603  -3943  -2126   -543
ATOM    907  C   LEU A 108     -26.820  15.351 -60.431  1.00237.20           C  
ANISOU  907  C   LEU A 108    24175  37909  28043  -4458  -1924   -483
ATOM    908  O   LEU A 108     -27.866  15.201 -59.788  1.00234.86           O  
ANISOU  908  O   LEU A 108    23763  37708  27765  -4738  -2066   -293
ATOM    909  CB  LEU A 108     -26.441  13.419 -61.980  1.00240.31           C  
ANISOU  909  CB  LEU A 108    24971  37730  28607  -3846  -2768   -360
ATOM    910  CG  LEU A 108     -27.416  12.460 -61.292  1.00237.03           C  
ANISOU  910  CG  LEU A 108    24452  37342  28265  -4123  -3271    -61
ATOM    911  CD1 LEU A 108     -28.798  12.548 -61.921  1.00237.54           C  
ANISOU  911  CD1 LEU A 108    24650  37184  28420  -4014  -3375     12
ATOM    912  CD2 LEU A 108     -26.890  11.032 -61.328  1.00235.70           C  
ANISOU  912  CD2 LEU A 108    24353  37039  28164  -4029  -3852     94
ATOM    913  N   ASN A 109     -25.730  15.906 -59.896  1.00243.70           N  
ANISOU  913  N   ASN A 109    24846  38971  28777  -4586  -1588   -645
ATOM    914  CA  ASN A 109     -25.673  16.277 -58.491  1.00241.51           C  
ANISOU  914  CA  ASN A 109    24277  39086  28401  -5062  -1422   -602
ATOM    915  C   ASN A 109     -25.562  17.774 -58.243  1.00241.02           C  
ANISOU  915  C   ASN A 109    24158  39184  28236  -5164   -741   -823
ATOM    916  O   ASN A 109     -25.805  18.208 -57.112  1.00239.09           O  
ANISOU  916  O   ASN A 109    23982  38958  27902  -5358   -534   -751
ATOM    917  CB  ASN A 109     -24.495  15.569 -57.804  1.00241.54           C  
ANISOU  917  CB  ASN A 109    24273  39108  28395  -5086  -1621   -564
ATOM    918  CG  ASN A 109     -24.652  14.060 -57.788  1.00240.76           C  
ANISOU  918  CG  ASN A 109    24295  38787  28394  -4993  -2254   -307
ATOM    919  OD1 ASN A 109     -23.873  13.337 -58.408  1.00242.72           O  
ANISOU  919  OD1 ASN A 109    24558  38973  28692  -4790  -2559   -338
ATOM    920  ND2 ASN A 109     -25.667  13.579 -57.080  1.00238.27           N  
ANISOU  920  ND2 ASN A 109    24081  38334  28117  -5126  -2434    -56
ATOM    921  N   THR A 110     -25.207  18.576 -59.253  1.00247.43           N  
ANISOU  921  N   THR A 110    25091  39869  29054  -4868   -352  -1066
ATOM    922  CA  THR A 110     -25.155  20.019 -59.031  1.00246.30           C  
ANISOU  922  CA  THR A 110    24865  39903  28815  -4994    304  -1279
ATOM    923  C   THR A 110     -26.554  20.616 -58.918  1.00245.73           C  
ANISOU  923  C   THR A 110    24831  39824  28710  -5107    475  -1191
ATOM    924  O   THR A 110     -26.733  21.650 -58.264  1.00243.45           O  
ANISOU  924  O   THR A 110    24689  39492  28320  -5174    887  -1253
ATOM    925  CB  THR A 110     -24.362  20.713 -60.141  1.00248.80           C  
ANISOU  925  CB  THR A 110    25359  40020  29154  -4604    707  -1556
ATOM    926  OG1 THR A 110     -24.135  22.081 -59.780  1.00246.76           O  
ANISOU  926  OG1 THR A 110    24988  39965  28805  -4771   1348  -1770
ATOM    927  CG2 THR A 110     -25.117  20.674 -61.458  1.00252.39           C  
ANISOU  927  CG2 THR A 110    26128  40103  29665  -4183    654  -1550
ATOM    928  N   GLN A 111     -27.550  19.986 -59.542  1.00254.29           N  
ANISOU  928  N   GLN A 111    26047  40687  29886  -4945    118  -1026
ATOM    929  CA  GLN A 111     -28.951  20.334 -59.353  1.00253.35           C  
ANISOU  929  CA  GLN A 111    25904  40585  29771  -5091    174   -897
ATOM    930  C   GLN A 111     -29.631  19.415 -58.345  1.00250.85           C  
ANISOU  930  C   GLN A 111    25562  40255  29496  -5333   -264   -587
ATOM    931  O   GLN A 111     -30.865  19.381 -58.272  1.00249.86           O  
ANISOU  931  O   GLN A 111    25466  40040  29429  -5388   -353   -427
ATOM    932  CB  GLN A 111     -29.693  20.301 -60.690  1.00256.41           C  
ANISOU  932  CB  GLN A 111    26569  40607  30248  -4670     82   -913
ATOM    933  CG  GLN A 111     -29.250  21.374 -61.671  1.00258.76           C  
ANISOU  933  CG  GLN A 111    27062  40767  30490  -4328    605  -1198
ATOM    934  CD  GLN A 111     -29.523  22.777 -61.162  1.00256.23           C  
ANISOU  934  CD  GLN A 111    26621  40680  30054  -4552   1242  -1330
ATOM    935  OE1 GLN A 111     -28.600  23.513 -60.812  1.00254.37           O  
ANISOU  935  OE1 GLN A 111    26295  40624  29731  -4653   1671  -1520
ATOM    936  NE2 GLN A 111     -30.796  23.154 -61.119  1.00255.64           N  
ANISOU  936  NE2 GLN A 111    26541  40601  29990  -4629   1308  -1231
ATOM    937  N   PHE A 112     -28.844  18.668 -57.572  1.00248.20           N  
ANISOU  937  N   PHE A 112    25236  39928  29139  -5415   -513   -497
ATOM    938  CA  PHE A 112     -29.354  17.749 -56.570  1.00245.88           C  
ANISOU  938  CA  PHE A 112    25004  39538  28880  -5566   -875   -207
ATOM    939  C   PHE A 112     -28.827  18.049 -55.174  1.00245.42           C  
ANISOU  939  C   PHE A 112    24995  39577  28677  -5748   -668   -193
ATOM    940  O   PHE A 112     -29.368  17.516 -54.198  1.00245.68           O  
ANISOU  940  O   PHE A 112    25078  39565  28705  -5895   -847     30
ATOM    941  CB  PHE A 112     -29.000  16.302 -56.958  1.00246.83           C  
ANISOU  941  CB  PHE A 112    25132  39527  29125  -5450  -1477    -70
ATOM    942  CG  PHE A 112     -29.599  15.259 -56.060  1.00245.91           C  
ANISOU  942  CG  PHE A 112    25095  39260  29080  -5567  -1843    229
ATOM    943  CD1 PHE A 112     -30.946  14.947 -56.142  1.00245.68           C  
ANISOU  943  CD1 PHE A 112    25103  39072  29174  -5596  -2021    415
ATOM    944  CD2 PHE A 112     -28.812  14.574 -55.148  1.00246.00           C  
ANISOU  944  CD2 PHE A 112    25133  39287  29047  -5642  -2003    315
ATOM    945  CE1 PHE A 112     -31.500  13.983 -55.323  1.00246.27           C  
ANISOU  945  CE1 PHE A 112    25238  39003  29330  -5702  -2321    677
ATOM    946  CE2 PHE A 112     -29.360  13.608 -54.326  1.00246.66           C  
ANISOU  946  CE2 PHE A 112    25286  39242  29193  -5744  -2305    577
ATOM    947  CZ  PHE A 112     -30.705  13.312 -54.414  1.00246.75           C  
ANISOU  947  CZ  PHE A 112    25330  39092  29330  -5776  -2452    756
ATOM    948  N   ILE A 113     -27.802  18.897 -55.049  1.00247.58           N  
ANISOU  948  N   ILE A 113    25260  39975  28834  -5732   -300   -433
ATOM    949  CA  ILE A 113     -27.274  19.253 -53.737  1.00247.45           C  
ANISOU  949  CA  ILE A 113    25300  40053  28668  -5889   -134   -446
ATOM    950  C   ILE A 113     -28.296  20.053 -52.938  1.00248.12           C  
ANISOU  950  C   ILE A 113    25499  40119  28657  -6013    126   -385
ATOM    951  O   ILE A 113     -28.308  20.001 -51.702  1.00250.25           O  
ANISOU  951  O   ILE A 113    25821  40449  28815  -6175    110   -287
ATOM    952  CB  ILE A 113     -25.946  20.021 -53.893  1.00246.77           C  
ANISOU  952  CB  ILE A 113    25187  40062  28512  -5816    182   -738
ATOM    953  CG1 ILE A 113     -25.267  20.219 -52.536  1.00246.99           C  
ANISOU  953  CG1 ILE A 113    25254  40194  28396  -5974    247   -752
ATOM    954  CG2 ILE A 113     -26.160  21.356 -54.598  1.00245.70           C  
ANISOU  954  CG2 ILE A 113    25124  39874  28358  -5692    667   -970
ATOM    955  CD1 ILE A 113     -23.832  20.691 -52.634  1.00246.63           C  
ANISOU  955  CD1 ILE A 113    25154  40227  28327  -5909    441  -1011
ATOM    956  N   LYS A 114     -29.174  20.788 -53.616  1.00253.65           N  
ANISOU  956  N   LYS A 114    26243  40735  29398  -5929    358   -442
ATOM    957  CA  LYS A 114     -30.180  21.594 -52.937  1.00252.60           C  
ANISOU  957  CA  LYS A 114    26230  40548  29198  -6007    598   -393
ATOM    958  C   LYS A 114     -31.361  20.777 -52.409  1.00253.20           C  
ANISOU  958  C   LYS A 114    26289  40570  29347  -6136    305    -90
ATOM    959  O   LYS A 114     -32.256  21.356 -51.788  1.00252.30           O  
ANISOU  959  O   LYS A 114    26258  40410  29194  -6205    479    -28
ATOM    960  CB  LYS A 114     -30.696  22.688 -53.878  1.00250.03           C  
ANISOU  960  CB  LYS A 114    25972  40118  28910  -5840    952   -563
ATOM    961  CG  LYS A 114     -31.471  22.164 -55.073  1.00249.71           C  
ANISOU  961  CG  LYS A 114    25829  40023  29026  -5740    769   -480
ATOM    962  CD  LYS A 114     -31.940  23.282 -55.983  1.00248.43           C  
ANISOU  962  CD  LYS A 114    25743  39771  28879  -5562   1151   -657
ATOM    963  CE  LYS A 114     -32.742  22.739 -57.154  1.00249.58           C  
ANISOU  963  CE  LYS A 114    25757  39901  29170  -5473    940   -579
ATOM    964  NZ  LYS A 114     -33.209  23.822 -58.061  1.00250.81           N1+
ANISOU  964  NZ  LYS A 114    25992  39980  29323  -5279   1335   -752
ATOM    965  N   LYS A 115     -31.399  19.463 -52.644  1.00249.21           N  
ANISOU  965  N   LYS A 115    25692  40031  28967  -6151   -142     98
ATOM    966  CA  LYS A 115     -32.520  18.616 -52.276  1.00249.89           C  
ANISOU  966  CA  LYS A 115    25767  40010  29169  -6245   -442    383
ATOM    967  C   LYS A 115     -32.191  17.649 -51.150  1.00251.59           C  
ANISOU  967  C   LYS A 115    25991  40262  29338  -6394   -716    571
ATOM    968  O   LYS A 115     -33.119  17.188 -50.487  1.00252.45           O  
ANISOU  968  O   LYS A 115    26117  40309  29495  -6512   -845    794
ATOM    969  CB  LYS A 115     -33.003  17.822 -53.506  1.00249.09           C  
ANISOU  969  CB  LYS A 115    25592  39762  29288  -6110   -794    461
ATOM    970  CG  LYS A 115     -33.638  18.643 -54.602  1.00247.43           C  
ANISOU  970  CG  LYS A 115    25356  39517  29141  -5981   -577    329
ATOM    971  CD  LYS A 115     -33.997  17.776 -55.797  1.00247.38           C  
ANISOU  971  CD  LYS A 115    25280  39377  29336  -5837  -1005    393
ATOM    972  CE  LYS A 115     -35.174  16.860 -55.479  1.00248.75           C  
ANISOU  972  CE  LYS A 115    25456  39365  29691  -5911  -1374    677
ATOM    973  NZ  LYS A 115     -35.634  16.104 -56.677  1.00248.71           N1+
ANISOU  973  NZ  LYS A 115    25426  39182  29892  -5737  -1816    724
ATOM    974  N   ASN A 116     -30.917  17.296 -50.945  1.00248.72           N  
ANISOU  974  N   ASN A 116    25610  39993  28897  -6383   -812    491
ATOM    975  CA  ASN A 116     -30.487  16.596 -49.724  1.00250.35           C  
ANISOU  975  CA  ASN A 116    25835  40277  29008  -6534   -989    635
ATOM    976  C   ASN A 116     -30.150  17.687 -48.681  1.00251.44           C  
ANISOU  976  C   ASN A 116    26032  40595  28910  -6659   -604    502
ATOM    977  O   ASN A 116     -28.992  17.878 -48.313  1.00252.41           O  
ANISOU  977  O   ASN A 116    26143  40850  28911  -6673   -537    360
ATOM    978  CB  ASN A 116     -29.236  15.676 -49.904  1.00249.69           C  
ANISOU  978  CB  ASN A 116    25710  40204  28957  -6456  -1296    614
ATOM    979  CG  ASN A 116     -29.430  14.348 -49.153  1.00250.11           C  
ANISOU  979  CG  ASN A 116    25786  40185  29059  -6545  -1695    886
ATOM    980  OD1 ASN A 116     -28.461  13.644 -48.824  1.00251.23           O  
ANISOU  980  OD1 ASN A 116    25919  40360  29176  -6531  -1910    900
ATOM    981  ND2 ASN A 116     -30.708  13.943 -49.041  1.00249.36           N  
ANISOU  981  ND2 ASN A 116    25717  39960  29071  -6607  -1816   1098
ATOM    982  N   PRO A 135     -31.104  11.564 -47.448  1.00249.13           N  
ANISOU  982  N   PRO A 135    25746  39808  29103  -6807  -2463   1601
ATOM    983  CA  PRO A 135     -30.365  10.329 -47.174  1.00250.49           C  
ANISOU  983  CA  PRO A 135    25948  39920  29308  -6770  -2834   1707
ATOM    984  C   PRO A 135     -29.637   9.778 -48.400  1.00249.81           C  
ANISOU  984  C   PRO A 135    25873  39660  29382  -6505  -3100   1592
ATOM    985  O   PRO A 135     -30.259   9.559 -49.441  1.00249.11           O  
ANISOU  985  O   PRO A 135    25802  39367  29482  -6361  -3245   1598
ATOM    986  CB  PRO A 135     -31.461   9.363 -46.712  1.00251.98           C  
ANISOU  986  CB  PRO A 135    26169  39961  29610  -6876  -3077   1999
ATOM    987  CG  PRO A 135     -32.705   9.872 -47.354  1.00251.06           C  
ANISOU  987  CG  PRO A 135    26030  39728  29635  -6859  -2955   2013
ATOM    988  CD  PRO A 135     -32.563  11.366 -47.385  1.00249.56           C  
ANISOU  988  CD  PRO A 135    25805  39730  29287  -6886  -2502   1797
ATOM    989  N   LEU A 136     -28.326   9.571 -48.261  1.00248.06           N  
ANISOU  989  N   LEU A 136    25644  39523  29083  -6438  -3168   1483
ATOM    990  CA  LEU A 136     -27.503   8.880 -49.254  1.00247.82           C  
ANISOU  990  CA  LEU A 136    25640  39332  29189  -6183  -3460   1395
ATOM    991  C   LEU A 136     -27.524   9.587 -50.614  1.00245.99           C  
ANISOU  991  C   LEU A 136    25379  39045  29043  -6005  -3341   1198
ATOM    992  O   LEU A 136     -28.000   9.055 -51.619  1.00245.65           O  
ANISOU  992  O   LEU A 136    25389  38772  29174  -5832  -3594   1233
ATOM    993  CB  LEU A 136     -27.933   7.415 -49.388  1.00249.08           C  
ANISOU  993  CB  LEU A 136    25896  39224  29518  -6097  -3915   1609
ATOM    994  N   MET A 137     -26.995  10.808 -50.625  1.00243.55           N  
ANISOU  994  N   MET A 137    24989  38952  28598  -6047  -2948    983
ATOM    995  CA  MET A 137     -26.679  11.511 -51.859  1.00241.99           C  
ANISOU  995  CA  MET A 137    24744  38757  28442  -5877  -2802    760
ATOM    996  C   MET A 137     -25.234  11.185 -52.241  1.00242.22           C  
ANISOU  996  C   MET A 137    24740  38813  28477  -5717  -2929    615
ATOM    997  O   MET A 137     -24.636  10.247 -51.707  1.00243.57           O  
ANISOU  997  O   MET A 137    24946  38937  28660  -5702  -3205    713
ATOM    998  CB  MET A 137     -26.925  13.009 -51.695  1.00240.82           C  
ANISOU  998  CB  MET A 137    24534  38811  28155  -6001  -2283    596
ATOM    999  N   GLU A 138     -24.653  11.948 -53.174  1.00240.19           N  
ANISOU  999  N   GLU A 138    24410  38637  28215  -5592  -2723    376
ATOM   1000  CA  GLU A 138     -23.251  11.772 -53.567  1.00240.45           C  
ANISOU 1000  CA  GLU A 138    24381  38722  28257  -5443  -2790    215
ATOM   1001  C   GLU A 138     -22.999  10.359 -54.106  1.00241.30           C  
ANISOU 1001  C   GLU A 138    24586  38588  28507  -5229  -3318    346
ATOM   1002  O   GLU A 138     -22.425   9.502 -53.437  1.00242.68           O  
ANISOU 1002  O   GLU A 138    24797  38721  28690  -5232  -3559    447
ATOM   1003  CB  GLU A 138     -22.288  12.102 -52.416  1.00241.40           C  
ANISOU 1003  CB  GLU A 138    24430  39045  28247  -5596  -2602    143
ATOM   1004  CG  GLU A 138     -22.094  13.592 -52.153  1.00240.56           C  
ANISOU 1004  CG  GLU A 138    24234  39164  28003  -5726  -2064    -80
ATOM   1005  CD  GLU A 138     -23.121  14.178 -51.207  1.00240.48           C  
ANISOU 1005  CD  GLU A 138    24284  39221  27867  -5949  -1833     22
ATOM   1006  OE1 GLU A 138     -23.944  13.412 -50.667  1.00241.22           O  
ANISOU 1006  OE1 GLU A 138    24458  39215  27980  -6028  -2081    271
ATOM   1007  OE2 GLU A 138     -23.099  15.410 -51.000  1.00239.77           O1-
ANISOU 1007  OE2 GLU A 138    24169  39273  27659  -6036  -1398   -153
ATOM   1008  N   ILE A 139     -23.492  10.140 -55.329  1.00231.37           N  
ANISOU 1008  N   ILE A 139    23390  37165  27355  -5032  -3496    340
ATOM   1009  CA  ILE A 139     -23.462   8.853 -56.026  1.00232.14           C  
ANISOU 1009  CA  ILE A 139    23632  36983  27588  -4790  -4003    459
ATOM   1010  C   ILE A 139     -22.176   8.079 -55.750  1.00233.32           C  
ANISOU 1010  C   ILE A 139    23784  37123  27745  -4690  -4215    449
ATOM   1011  O   ILE A 139     -22.210   6.861 -55.534  1.00233.73           O  
ANISOU 1011  O   ILE A 139    23967  36962  27878  -4608  -4598    619
ATOM   1012  CB  ILE A 139     -23.637   9.064 -57.542  1.00232.59           C  
ANISOU 1012  CB  ILE A 139    23723  36959  27693  -4544  -4080    341
ATOM   1013  CG1 ILE A 139     -24.958   9.776 -57.838  1.00232.99           C  
ANISOU 1013  CG1 ILE A 139    23770  37005  27748  -4629  -3904    355
ATOM   1014  CG2 ILE A 139     -23.561   7.739 -58.287  1.00233.22           C  
ANISOU 1014  CG2 ILE A 139    23994  36724  27895  -4262  -4613    457
ATOM   1015  CD1 ILE A 139     -26.179   8.999 -57.407  1.00231.54           C  
ANISOU 1015  CD1 ILE A 139    23712  36584  27680  -4702  -4169    608
ATOM   1016  N   GLY A 140     -21.035   8.772 -55.764  1.00225.21           N  
ANISOU 1016  N   GLY A 140    22604  36323  26642  -4690  -3957    241
ATOM   1017  CA  GLY A 140     -19.788   8.128 -55.378  1.00226.26           C  
ANISOU 1017  CA  GLY A 140    22708  36476  26786  -4621  -4128    227
ATOM   1018  C   GLY A 140     -19.844   7.550 -53.976  1.00227.34           C  
ANISOU 1018  C   GLY A 140    22883  36610  26886  -4805  -4227    398
ATOM   1019  O   GLY A 140     -19.516   6.380 -53.756  1.00228.29           O  
ANISOU 1019  O   GLY A 140    23101  36571  27069  -4702  -4591    527
ATOM   1020  N   GLU A 141     -20.264   8.367 -53.004  1.00224.66           N  
ANISOU 1020  N   GLU A 141    22475  36456  26429  -5072  -3898    397
ATOM   1021  CA  GLU A 141     -20.471   7.875 -51.645  1.00226.33           C  
ANISOU 1021  CA  GLU A 141    22729  36695  26572  -5260  -3981    572
ATOM   1022  C   GLU A 141     -21.514   6.764 -51.604  1.00226.09           C  
ANISOU 1022  C   GLU A 141    22861  36411  26633  -5231  -4324    824
ATOM   1023  O   GLU A 141     -21.461   5.895 -50.727  1.00227.29           O  
ANISOU 1023  O   GLU A 141    23070  36521  26767  -5293  -4535    983
ATOM   1024  CB  GLU A 141     -20.885   9.034 -50.732  1.00226.63           C  
ANISOU 1024  CB  GLU A 141    22688  36972  26448  -5534  -3556    527
ATOM   1025  CG  GLU A 141     -21.159   8.654 -49.283  1.00228.20           C  
ANISOU 1025  CG  GLU A 141    22926  37245  26535  -5749  -3607    707
ATOM   1026  CD  GLU A 141     -19.920   8.180 -48.552  1.00229.70           C  
ANISOU 1026  CD  GLU A 141    23072  37526  26677  -5741  -3748    676
ATOM   1027  OE1 GLU A 141     -18.805   8.583 -48.943  1.00230.21           O  
ANISOU 1027  OE1 GLU A 141    23031  37679  26760  -5641  -3657    469
ATOM   1028  OE2 GLU A 141     -20.063   7.405 -47.583  1.00230.47           O1-
ANISOU 1028  OE2 GLU A 141    23231  37614  26723  -5837  -3947    858
ATOM   1029  N   LEU A 142     -22.462   6.771 -52.543  1.00225.23           N  
ANISOU 1029  N   LEU A 142    22821  36133  26621  -5137  -4384    857
ATOM   1030  CA  LEU A 142     -23.479   5.726 -52.578  1.00225.90           C  
ANISOU 1030  CA  LEU A 142    23053  35959  26818  -5102  -4707   1078
ATOM   1031  C   LEU A 142     -22.937   4.442 -53.198  1.00226.77           C  
ANISOU 1031  C   LEU A 142    23292  35822  27050  -4832  -5143   1119
ATOM   1032  O   LEU A 142     -23.284   3.342 -52.753  1.00228.11           O  
ANISOU 1032  O   LEU A 142    23570  35829  27273  -4831  -5420   1299
ATOM   1033  CB  LEU A 142     -24.712   6.227 -53.335  1.00224.61           C  
ANISOU 1033  CB  LEU A 142    22914  35703  26727  -5098  -4621   1089
ATOM   1034  CG  LEU A 142     -25.992   5.389 -53.306  1.00225.29           C  
ANISOU 1034  CG  LEU A 142    23116  35546  26940  -5115  -4877   1307
ATOM   1035  CD1 LEU A 142     -27.209   6.294 -53.400  1.00224.28           C  
ANISOU 1035  CD1 LEU A 142    22933  35468  26816  -5259  -4621   1322
ATOM   1036  CD2 LEU A 142     -26.009   4.379 -54.440  1.00225.52           C  
ANISOU 1036  CD2 LEU A 142    23297  35262  27128  -4815  -5289   1321
ATOM   1037  N   ALA A 143     -22.093   4.559 -54.226  1.00219.25           N  
ANISOU 1037  N   ALA A 143    22331  34843  26130  -4600  -5197    955
ATOM   1038  CA  ALA A 143     -21.465   3.373 -54.802  1.00220.16           C  
ANISOU 1038  CA  ALA A 143    22577  34737  26338  -4326  -5595    983
ATOM   1039  C   ALA A 143     -20.518   2.722 -53.803  1.00221.80           C  
ANISOU 1039  C   ALA A 143    22759  35019  26498  -4372  -5697   1028
ATOM   1040  O   ALA A 143     -20.529   1.497 -53.623  1.00223.14           O  
ANISOU 1040  O   ALA A 143    23060  34999  26723  -4274  -6022   1162
ATOM   1041  CB  ALA A 143     -20.727   3.742 -56.089  1.00219.20           C  
ANISOU 1041  CB  ALA A 143    22439  34612  26237  -4076  -5602    801
ATOM   1042  N   LEU A 144     -19.690   3.532 -53.138  1.00217.77           N  
ANISOU 1042  N   LEU A 144    22077  34788  25878  -4518  -5418    909
ATOM   1043  CA  LEU A 144     -18.850   3.004 -52.070  1.00218.76           C  
ANISOU 1043  CA  LEU A 144    22168  35008  25944  -4586  -5506    951
ATOM   1044  C   LEU A 144     -19.692   2.491 -50.909  1.00219.44           C  
ANISOU 1044  C   LEU A 144    22320  35083  25976  -4796  -5563   1164
ATOM   1045  O   LEU A 144     -19.267   1.582 -50.187  1.00220.42           O  
ANISOU 1045  O   LEU A 144    22489  35182  26077  -4793  -5778   1266
ATOM   1046  CB  LEU A 144     -17.870   4.076 -51.599  1.00218.48           C  
ANISOU 1046  CB  LEU A 144    21931  35276  25806  -4710  -5178    764
ATOM   1047  CG  LEU A 144     -16.817   4.496 -52.626  1.00217.49           C  
ANISOU 1047  CG  LEU A 144    21702  35200  25735  -4511  -5121    552
ATOM   1048  CD1 LEU A 144     -15.980   5.652 -52.102  1.00217.86           C  
ANISOU 1048  CD1 LEU A 144    21532  35556  25689  -4669  -4746    354
ATOM   1049  CD2 LEU A 144     -15.935   3.315 -53.001  1.00217.87           C  
ANISOU 1049  CD2 LEU A 144    21823  35082  25874  -4253  -5508    584
ATOM   1050  N   ASP A 145     -20.884   3.062 -50.713  1.00217.33           N  
ANISOU 1050  N   ASP A 145    22050  34845  25680  -4982  -5369   1239
ATOM   1051  CA  ASP A 145     -21.834   2.491 -49.765  1.00218.44           C  
ANISOU 1051  CA  ASP A 145    22258  34949  25789  -5169  -5449   1470
ATOM   1052  C   ASP A 145     -22.255   1.094 -50.204  1.00219.34           C  
ANISOU 1052  C   ASP A 145    22539  34757  26042  -4997  -5848   1623
ATOM   1053  O   ASP A 145     -22.477   0.210 -49.368  1.00220.97           O  
ANISOU 1053  O   ASP A 145    22808  34927  26225  -5087  -6017   1805
ATOM   1054  CB  ASP A 145     -23.051   3.410 -49.630  1.00217.32           C  
ANISOU 1054  CB  ASP A 145    22074  34886  25613  -5376  -5162   1512
ATOM   1055  CG  ASP A 145     -23.960   3.026 -48.474  1.00218.60           C  
ANISOU 1055  CG  ASP A 145    22264  35084  25711  -5623  -5173   1749
ATOM   1056  OD1 ASP A 145     -23.653   2.055 -47.752  1.00220.37           O  
ANISOU 1056  OD1 ASP A 145    22542  35282  25906  -5644  -5398   1883
ATOM   1057  OD2 ASP A 145     -24.994   3.702 -48.290  1.00217.92           O1-
ANISOU 1057  OD2 ASP A 145    22143  35059  25598  -5797  -4952   1805
ATOM   1058  N   MET A 146     -22.359   0.873 -51.517  1.00222.66           N  
ANISOU 1058  N   MET A 146    23043  34961  26596  -4746  -6001   1549
ATOM   1059  CA  MET A 146     -22.687  -0.461 -52.005  1.00223.88           C  
ANISOU 1059  CA  MET A 146    23373  34818  26875  -4556  -6379   1669
ATOM   1060  C   MET A 146     -21.511  -1.417 -51.842  1.00224.64           C  
ANISOU 1060  C   MET A 146    23522  34877  26955  -4388  -6621   1658
ATOM   1061  O   MET A 146     -21.715  -2.616 -51.619  1.00225.69           O  
ANISOU 1061  O   MET A 146    23778  34845  27128  -4335  -6889   1808
ATOM   1062  CB  MET A 146     -23.129  -0.395 -53.467  1.00223.40           C  
ANISOU 1062  CB  MET A 146    23402  34540  26938  -4321  -6481   1585
ATOM   1063  CG  MET A 146     -24.350   0.483 -53.695  1.00222.46           C  
ANISOU 1063  CG  MET A 146    23236  34437  26851  -4465  -6273   1598
ATOM   1064  SD  MET A 146     -25.763   0.016 -52.678  1.00222.52           S  
ANISOU 1064  SD  MET A 146    23257  34398  26891  -4743  -6290   1862
ATOM   1065  CE  MET A 146     -26.192  -1.565 -53.392  1.00222.02           C  
ANISOU 1065  CE  MET A 146    23404  33956  26996  -4507  -6745   1980
ATOM   1066  N   TRP A 147     -20.279  -0.911 -51.954  1.00216.56           N  
ANISOU 1066  N   TRP A 147    22398  34008  25878  -4307  -6524   1484
ATOM   1067  CA  TRP A 147     -19.122  -1.727 -51.596  1.00218.12           C  
ANISOU 1067  CA  TRP A 147    22612  34215  26050  -4184  -6725   1476
ATOM   1068  C   TRP A 147     -19.156  -2.094 -50.117  1.00219.82           C  
ANISOU 1068  C   TRP A 147    22798  34567  26157  -4417  -6723   1624
ATOM   1069  O   TRP A 147     -18.806  -3.220 -49.735  1.00221.52           O  
ANISOU 1069  O   TRP A 147    23101  34697  26369  -4337  -6980   1725
ATOM   1070  CB  TRP A 147     -17.829  -0.988 -51.940  1.00217.61           C  
ANISOU 1070  CB  TRP A 147    22406  34316  25961  -4087  -6593   1260
ATOM   1071  N   ARG A 148     -19.578  -1.152 -49.269  1.00215.01           N  
ANISOU 1071  N   ARG A 148    22072  34180  25442  -4703  -6430   1641
ATOM   1072  CA  ARG A 148     -19.827  -1.483 -47.871  1.00217.11           C  
ANISOU 1072  CA  ARG A 148    22331  34574  25587  -4942  -6430   1813
ATOM   1073  C   ARG A 148     -20.882  -2.575 -47.758  1.00218.42           C  
ANISOU 1073  C   ARG A 148    22643  34528  25817  -4969  -6658   2052
ATOM   1074  O   ARG A 148     -20.778  -3.461 -46.906  1.00220.49           O  
ANISOU 1074  O   ARG A 148    22959  34796  26022  -5032  -6830   2207
ATOM   1075  CB  ARG A 148     -20.261  -0.238 -47.098  1.00216.56           C  
ANISOU 1075  CB  ARG A 148    22133  34767  25383  -5238  -6063   1797
ATOM   1076  CG  ARG A 148     -20.421  -0.463 -45.602  1.00218.40           C  
ANISOU 1076  CG  ARG A 148    22354  35176  25454  -5494  -6046   1965
ATOM   1077  CD  ARG A 148     -20.816   0.821 -44.888  1.00218.47           C  
ANISOU 1077  CD  ARG A 148    22246  35452  25309  -5771  -5670   1933
ATOM   1078  NE  ARG A 148     -21.012   0.613 -43.456  1.00220.53           N  
ANISOU 1078  NE  ARG A 148    22507  35891  25392  -6020  -5662   2106
ATOM   1079  CZ  ARG A 148     -20.046   0.714 -42.549  1.00222.03           C  
ANISOU 1079  CZ  ARG A 148    22640  36289  25434  -6082  -5654   2048
ATOM   1080  NH1 ARG A 148     -18.814   1.028 -42.925  1.00221.35           N  
ANISOU 1080  NH1 ARG A 148    22475  36253  25375  -5918  -5644   1819
ATOM   1081  NH2 ARG A 148     -20.312   0.508 -41.267  1.00224.07           N1+
ANISOU 1081  NH2 ARG A 148    22912  36709  25516  -6312  -5662   2220
ATOM   1082  N   LYS A 149     -21.898  -2.536 -48.623  1.00219.47           N  
ANISOU 1082  N   LYS A 149    22840  34474  26075  -4921  -6669   2083
ATOM   1083  CA  LYS A 149     -22.875  -3.617 -48.665  1.00219.93           C  
ANISOU 1083  CA  LYS A 149    23032  34301  26229  -4924  -6905   2295
ATOM   1084  C   LYS A 149     -22.253  -4.921 -49.153  1.00220.77           C  
ANISOU 1084  C   LYS A 149    23281  34195  26406  -4655  -7248   2309
ATOM   1085  O   LYS A 149     -22.806  -5.995 -48.894  1.00222.02           O  
ANISOU 1085  O   LYS A 149    23548  34198  26610  -4681  -7461   2504
ATOM   1086  CB  LYS A 149     -24.058  -3.214 -49.549  1.00218.54           C  
ANISOU 1086  CB  LYS A 149    22881  33971  26184  -4916  -6843   2297
ATOM   1087  CG  LYS A 149     -25.241  -4.167 -49.512  1.00219.46           C  
ANISOU 1087  CG  LYS A 149    23103  33866  26414  -4978  -7044   2524
ATOM   1088  CD  LYS A 149     -26.411  -3.613 -50.308  1.00218.22           C  
ANISOU 1088  CD  LYS A 149    22940  33587  26386  -4989  -6961   2510
ATOM   1089  CE  LYS A 149     -27.609  -4.547 -50.260  1.00219.29           C  
ANISOU 1089  CE  LYS A 149    23161  33499  26660  -5066  -7163   2736
ATOM   1090  NZ  LYS A 149     -28.766  -4.004 -51.026  1.00218.23           N1+
ANISOU 1090  NZ  LYS A 149    23009  33244  26665  -5072  -7096   2716
ATOM   1091  N   LEU A 150     -21.111  -4.851 -49.841  1.00218.89           N  
ANISOU 1091  N   LEU A 150    23040  33953  26174  -4404  -7299   2115
ATOM   1092  CA  LEU A 150     -20.368  -6.061 -50.170  1.00220.17           C  
ANISOU 1092  CA  LEU A 150    23326  33958  26369  -4152  -7603   2125
ATOM   1093  C   LEU A 150     -19.562  -6.569 -48.982  1.00222.66           C  
ANISOU 1093  C   LEU A 150    23607  34430  26564  -4236  -7672   2195
ATOM   1094  O   LEU A 150     -19.352  -7.781 -48.856  1.00223.74           O  
ANISOU 1094  O   LEU A 150    23862  34439  26709  -4126  -7929   2305
ATOM   1095  CB  LEU A 150     -19.443  -5.809 -51.367  1.00218.63           C  
ANISOU 1095  CB  LEU A 150    23139  33707  26224  -3847  -7638   1905
ATOM   1096  CG  LEU A 150     -18.719  -6.989 -52.029  1.00219.35           C  
ANISOU 1096  CG  LEU A 150    23375  33611  26355  -3530  -7940   1895
ATOM   1097  CD1 LEU A 150     -18.502  -6.704 -53.505  1.00218.57           C  
ANISOU 1097  CD1 LEU A 150    23335  33379  26332  -3251  -7972   1738
ATOM   1098  CD2 LEU A 150     -17.383  -7.287 -51.361  1.00220.23           C  
ANISOU 1098  CD2 LEU A 150    23417  33879  26383  -3479  -8000   1846
ATOM   1099  N   MET A 151     -19.107  -5.674 -48.102  1.00216.87           N  
ANISOU 1099  N   MET A 151    22717  33973  25709  -4426  -7450   2133
ATOM   1100  CA  MET A 151     -18.262  -6.105 -46.994  1.00218.17           C  
ANISOU 1100  CA  MET A 151    22848  34297  25751  -4487  -7530   2177
ATOM   1101  C   MET A 151     -19.036  -6.471 -45.732  1.00219.18           C  
ANISOU 1101  C   MET A 151    22999  34505  25775  -4771  -7535   2421
ATOM   1102  O   MET A 151     -18.543  -7.276 -44.934  1.00220.42           O  
ANISOU 1102  O   MET A 151    23195  34706  25849  -4778  -7706   2520
ATOM   1103  CB  MET A 151     -17.228  -5.027 -46.661  1.00217.71           C  
ANISOU 1103  CB  MET A 151    22613  34500  25609  -4530  -7319   1976
ATOM   1104  CG  MET A 151     -16.186  -4.839 -47.746  1.00216.75           C  
ANISOU 1104  CG  MET A 151    22452  34324  25580  -4247  -7359   1755
ATOM   1105  SD  MET A 151     -15.368  -6.399 -48.133  1.00218.20           S  
ANISOU 1105  SD  MET A 151    22778  34309  25817  -3925  -7753   1791
ATOM   1106  CE  MET A 151     -14.539  -6.744 -46.586  1.00219.93           C  
ANISOU 1106  CE  MET A 151    22927  34751  25885  -4056  -7822   1846
ATOM   1107  N   VAL A 152     -20.232  -5.911 -45.525  1.00218.12           N  
ANISOU 1107  N   VAL A 152    22840  34397  25640  -5005  -7356   2528
ATOM   1108  CA  VAL A 152     -21.041  -6.261 -44.359  1.00219.57           C  
ANISOU 1108  CA  VAL A 152    23042  34656  25727  -5289  -7362   2786
ATOM   1109  C   VAL A 152     -21.453  -7.728 -44.397  1.00221.20           C  
ANISOU 1109  C   VAL A 152    23406  34627  26013  -5221  -7675   2996
ATOM   1110  O   VAL A 152     -21.791  -8.309 -43.358  1.00223.85           O  
ANISOU 1110  O   VAL A 152    23773  35022  26259  -5415  -7757   3221
ATOM   1111  CB  VAL A 152     -22.263  -5.313 -44.267  1.00218.27           C  
ANISOU 1111  CB  VAL A 152    22809  34560  25565  -5536  -7096   2850
ATOM   1112  CG1 VAL A 152     -23.210  -5.722 -43.148  1.00219.96           C  
ANISOU 1112  CG1 VAL A 152    23044  34835  25696  -5836  -7113   3144
ATOM   1113  CG2 VAL A 152     -21.803  -3.884 -44.039  1.00216.99           C  
ANISOU 1113  CG2 VAL A 152    22495  34665  25287  -5634  -6769   2657
ATOM   1114  N   GLU A 153     -21.382  -8.357 -45.570  1.00220.64           N  
ANISOU 1114  N   GLU A 153    23440  34293  26098  -4946  -7856   2930
ATOM   1115  CA  GLU A 153     -21.677  -9.768 -45.790  1.00222.16           C  
ANISOU 1115  CA  GLU A 153    23794  34237  26379  -4841  -8155   3098
ATOM   1116  C   GLU A 153     -20.854 -10.631 -44.838  1.00223.87           C  
ANISOU 1116  C   GLU A 153    24049  34541  26469  -4838  -8328   3193
ATOM   1117  O   GLU A 153     -19.873 -10.139 -44.265  1.00223.32           O  
ANISOU 1117  O   GLU A 153    23885  34700  26268  -4839  -8244   3071
ATOM   1118  CB  GLU A 153     -21.374 -10.128 -47.247  1.00221.74           C  
ANISOU 1118  CB  GLU A 153    23839  33943  26469  -4499  -8293   2943
ATOM   1119  CG  GLU A 153     -22.171  -9.324 -48.256  1.00220.62           C  
ANISOU 1119  CG  GLU A 153    23677  33701  26449  -4473  -8153   2843
ATOM   1120  CD  GLU A 153     -23.660  -9.574 -48.159  1.00220.88           C  
ANISOU 1120  CD  GLU A 153    23749  33592  26583  -4672  -8173   3055
ATOM   1121  OE1 GLU A 153     -24.056 -10.707 -47.814  1.00222.59           O  
ANISOU 1121  OE1 GLU A 153    24069  33666  26839  -4722  -8386   3265
ATOM   1122  OE2 GLU A 153     -24.435  -8.631 -48.422  1.00220.06           O1-
ANISOU 1122  OE2 GLU A 153    23565  33521  26525  -4785  -7977   3015
ATOM   1123  N   PRO A 154     -21.192 -11.913 -44.645  1.00219.96           N  
ANISOU 1123  N   PRO A 154    23690  33874  26011  -4832  -8576   3405
ATOM   1124  CA  PRO A 154     -20.353 -12.766 -43.782  1.00222.29           C  
ANISOU 1124  CA  PRO A 154    24031  34250  26178  -4803  -8753   3488
ATOM   1125  C   PRO A 154     -18.893 -12.814 -44.205  1.00222.19           C  
ANISOU 1125  C   PRO A 154    24005  34284  26131  -4499  -8820   3251
ATOM   1126  O   PRO A 154     -18.075 -13.393 -43.478  1.00224.10           O  
ANISOU 1126  O   PRO A 154    24264  34624  26259  -4457  -8953   3285
ATOM   1127  CB  PRO A 154     -21.018 -14.146 -43.890  1.00223.89           C  
ANISOU 1127  CB  PRO A 154    24401  34191  26477  -4795  -9012   3729
ATOM   1128  CG  PRO A 154     -21.807 -14.098 -45.155  1.00222.23           C  
ANISOU 1128  CG  PRO A 154    24244  33728  26464  -4690  -9014   3681
ATOM   1129  CD  PRO A 154     -22.286 -12.681 -45.266  1.00220.13           C  
ANISOU 1129  CD  PRO A 154    23833  33605  26201  -4831  -8723   3566
ATOM   1130  N   LEU A 155     -18.552 -12.229 -45.358  1.00219.61           N  
ANISOU 1130  N   LEU A 155    23646  33894  25901  -4288  -8739   3022
ATOM   1131  CA  LEU A 155     -17.157 -12.014 -45.720  1.00219.39           C  
ANISOU 1131  CA  LEU A 155    23560  33956  25844  -4039  -8756   2787
ATOM   1132  C   LEU A 155     -16.393 -11.322 -44.598  1.00220.19           C  
ANISOU 1132  C   LEU A 155    23509  34362  25790  -4184  -8633   2718
ATOM   1133  O   LEU A 155     -15.261 -11.703 -44.283  1.00221.59           O  
ANISOU 1133  O   LEU A 155    23667  34623  25902  -4041  -8757   2644
ATOM   1134  CB  LEU A 155     -17.083 -11.187 -47.004  1.00216.93           C  
ANISOU 1134  CB  LEU A 155    23205  33576  25644  -3873  -8626   2570
ATOM   1135  CG  LEU A 155     -17.670 -11.808 -48.273  1.00216.14           C  
ANISOU 1135  CG  LEU A 155    23260  33176  25687  -3673  -8759   2592
ATOM   1136  CD1 LEU A 155     -17.665 -10.797 -49.410  1.00213.73           C  
ANISOU 1136  CD1 LEU A 155    22900  32846  25463  -3551  -8602   2385
ATOM   1137  CD2 LEU A 155     -16.909 -13.063 -48.665  1.00217.59           C  
ANISOU 1137  CD2 LEU A 155    23580  33219  25877  -3395  -9025   2611
ATOM   1138  N   GLN A 156     -16.999 -10.307 -43.973  1.00218.54           N  
ANISOU 1138  N   GLN A 156    23194  34326  25518  -4468  -8392   2742
ATOM   1139  CA  GLN A 156     -16.327  -9.605 -42.883  1.00219.40           C  
ANISOU 1139  CA  GLN A 156    23166  34730  25466  -4623  -8265   2677
ATOM   1140  C   GLN A 156     -16.031 -10.522 -41.707  1.00222.22           C  
ANISOU 1140  C   GLN A 156    23586  35168  25682  -4693  -8460   2850
ATOM   1141  O   GLN A 156     -15.145 -10.215 -40.904  1.00223.44           O  
ANISOU 1141  O   GLN A 156    23651  35540  25707  -4723  -8446   2765
ATOM   1142  CB  GLN A 156     -17.162  -8.415 -42.407  1.00218.22           C  
ANISOU 1142  CB  GLN A 156    22913  34749  25251  -4929  -7964   2702
ATOM   1143  CG  GLN A 156     -18.476  -8.789 -41.746  1.00218.99           C  
ANISOU 1143  CG  GLN A 156    23085  34815  25307  -5195  -7967   2990
ATOM   1144  CD  GLN A 156     -19.285  -7.573 -41.341  1.00217.78           C  
ANISOU 1144  CD  GLN A 156    22824  34838  25085  -5484  -7654   3007
ATOM   1145  OE1 GLN A 156     -18.841  -6.436 -41.501  1.00216.40           O  
ANISOU 1145  OE1 GLN A 156    22524  34817  24880  -5492  -7425   2799
ATOM   1146  NE2 GLN A 156     -20.482  -7.807 -40.815  1.00218.39           N  
ANISOU 1146  NE2 GLN A 156    22945  34895  25138  -5729  -7638   3262
ATOM   1147  N   ALA A 157     -16.760 -11.628 -41.576  1.00211.01           N  
ANISOU 1147  N   ALA A 157    22315  33577  24283  -4725  -8644   3091
ATOM   1148  CA  ALA A 157     -16.378 -12.666 -40.631  1.00213.81           C  
ANISOU 1148  CA  ALA A 157    22752  33969  24516  -4733  -8870   3253
ATOM   1149  C   ALA A 157     -15.399 -13.649 -41.258  1.00214.64           C  
ANISOU 1149  C   ALA A 157    22940  33930  24683  -4388  -9114   3166
ATOM   1150  O   ALA A 157     -14.461 -14.097 -40.595  1.00216.64           O  
ANISOU 1150  O   ALA A 157    23192  34297  24824  -4304  -9255   3147
ATOM   1151  CB  ALA A 157     -17.617 -13.407 -40.123  1.00214.96           C  
ANISOU 1151  CB  ALA A 157    23015  34008  24654  -4957  -8952   3577
ATOM   1152  N   ILE A 158     -15.595 -13.975 -42.534  1.00217.11           N  
ANISOU 1152  N   ILE A 158    23328  34002  25162  -4181  -9166   3108
ATOM   1153  CA  ILE A 158     -14.710 -14.910 -43.220  1.00217.84           C  
ANISOU 1153  CA  ILE A 158    23508  33955  25305  -3847  -9384   3034
ATOM   1154  C   ILE A 158     -13.383 -14.246 -43.569  1.00217.26           C  
ANISOU 1154  C   ILE A 158    23296  34023  25228  -3644  -9330   2751
ATOM   1155  O   ILE A 158     -12.316 -14.701 -43.142  1.00219.04           O  
ANISOU 1155  O   ILE A 158    23504  34344  25379  -3505  -9473   2700
ATOM   1156  CB  ILE A 158     -15.400 -15.476 -44.476  1.00216.65           C  
ANISOU 1156  CB  ILE A 158    23495  33502  25319  -3700  -9459   3077
ATOM   1157  CG1 ILE A 158     -16.640 -16.284 -44.090  1.00217.70           C  
ANISOU 1157  CG1 ILE A 158    23761  33477  25480  -3900  -9557   3372
ATOM   1158  CG2 ILE A 158     -14.430 -16.329 -45.280  1.00217.23           C  
ANISOU 1158  CG2 ILE A 158    23655  33453  25430  -3343  -9652   2984
ATOM   1159  CD1 ILE A 158     -17.515 -16.656 -45.268  1.00216.49           C  
ANISOU 1159  CD1 ILE A 158    23725  33027  25503  -3813  -9605   3413
ATOM   1160  N   LEU A 159     -13.440 -13.151 -44.337  1.00217.36           N  
ANISOU 1160  N   LEU A 159    23205  34052  25329  -3632  -9126   2570
ATOM   1161  CA  LEU A 159     -12.238 -12.586 -44.949  1.00216.66           C  
ANISOU 1161  CA  LEU A 159    22993  34043  25285  -3417  -9089   2310
ATOM   1162  C   LEU A 159     -11.149 -12.302 -43.925  1.00218.38           C  
ANISOU 1162  C   LEU A 159    23073  34513  25391  -3457  -9103   2218
ATOM   1163  O   LEU A 159     -10.001 -12.725 -44.097  1.00219.54           O  
ANISOU 1163  O   LEU A 159    23189  34680  25546  -3223  -9255   2111
ATOM   1164  CB  LEU A 159     -12.578 -11.308 -45.719  1.00213.98           C  
ANISOU 1164  CB  LEU A 159    22548  33717  25036  -3471  -8835   2155
ATOM   1165  CG  LEU A 159     -13.393 -11.495 -46.995  1.00212.20           C  
ANISOU 1165  CG  LEU A 159    22447  33240  24940  -3348  -8842   2176
ATOM   1166  CD1 LEU A 159     -13.722 -10.153 -47.625  1.00209.72           C  
ANISOU 1166  CD1 LEU A 159    22020  32972  24693  -3421  -8582   2026
ATOM   1167  CD2 LEU A 159     -12.615 -12.366 -47.954  1.00212.65           C  
ANISOU 1167  CD2 LEU A 159    22600  33143  25056  -2996  -9051   2116
ATOM   1168  N   ILE A 160     -11.486 -11.578 -42.853  1.00210.73           N  
ANISOU 1168  N   ILE A 160    22016  33741  24311  -3749  -8949   2260
ATOM   1169  CA  ILE A 160     -10.469 -11.247 -41.859  1.00212.50           C  
ANISOU 1169  CA  ILE A 160    22109  34209  24422  -3794  -8964   2162
ATOM   1170  C   ILE A 160      -9.870 -12.520 -41.275  1.00215.29           C  
ANISOU 1170  C   ILE A 160    22562  34547  24692  -3653  -9259   2266
ATOM   1171  O   ILE A 160      -8.648 -12.628 -41.122  1.00216.69           O  
ANISOU 1171  O   ILE A 160    22654  34820  24859  -3485  -9377   2124
ATOM   1172  CB  ILE A 160     -11.041 -10.307 -40.776  1.00212.52           C  
ANISOU 1172  CB  ILE A 160    22029  34428  24289  -4143  -8749   2214
ATOM   1173  CG1 ILE A 160     -12.247 -10.913 -40.049  1.00213.36           C  
ANISOU 1173  CG1 ILE A 160    22280  34492  24293  -4360  -8788   2507
ATOM   1174  CG2 ILE A 160     -11.407  -8.958 -41.382  1.00209.84           C  
ANISOU 1174  CG2 ILE A 160    21568  34135  24029  -4253  -8441   2071
ATOM   1175  CD1 ILE A 160     -11.911 -11.648 -38.761  1.00216.41           C  
ANISOU 1175  CD1 ILE A 160    22722  35004  24500  -4426  -8977   2648
ATOM   1176  N   ARG A 161     -10.710 -13.524 -40.997  1.00220.80           N  
ANISOU 1176  N   ARG A 161    23439  35114  25342  -3709  -9387   2516
ATOM   1177  CA  ARG A 161     -10.194 -14.809 -40.536  1.00223.44           C  
ANISOU 1177  CA  ARG A 161    23887  35412  25597  -3560  -9666   2630
ATOM   1178  C   ARG A 161      -9.279 -15.430 -41.580  1.00223.41           C  
ANISOU 1178  C   ARG A 161    23907  35277  25703  -3197  -9820   2501
ATOM   1179  O   ARG A 161      -8.235 -16.003 -41.245  1.00225.48           O  
ANISOU 1179  O   ARG A 161    24154  35611  25907  -3020 -10003   2451
ATOM   1180  CB  ARG A 161     -11.346 -15.761 -40.210  1.00224.24           C  
ANISOU 1180  CB  ARG A 161    24178  35364  25660  -3695  -9762   2933
ATOM   1181  CG  ARG A 161     -12.158 -15.390 -38.982  1.00225.06           C  
ANISOU 1181  CG  ARG A 161    24274  35620  25619  -4050  -9664   3111
ATOM   1182  CD  ARG A 161     -13.299 -16.378 -38.787  1.00225.91           C  
ANISOU 1182  CD  ARG A 161    24559  35550  25725  -4180  -9773   3423
ATOM   1183  NE  ARG A 161     -14.159 -16.028 -37.660  1.00226.71           N  
ANISOU 1183  NE  ARG A 161    24654  35795  25691  -4534  -9676   3622
ATOM   1184  CZ  ARG A 161     -15.273 -16.681 -37.345  1.00227.49           C  
ANISOU 1184  CZ  ARG A 161    24875  35774  25789  -4727  -9736   3914
ATOM   1185  NH1 ARG A 161     -15.668 -17.715 -38.075  1.00227.57           N  
ANISOU 1185  NH1 ARG A 161    25024  35507  25935  -4599  -9895   4031
ATOM   1186  NH2 ARG A 161     -15.997 -16.296 -36.303  1.00228.32           N1+
ANISOU 1186  NH2 ARG A 161    24958  36036  25756  -5055  -9639   4096
ATOM   1187  N   MET A 162      -9.655 -15.324 -42.855  1.00222.59           N  
ANISOU 1187  N   MET A 162    23841  34987  25746  -3079  -9752   2448
ATOM   1188  CA  MET A 162      -8.795 -15.787 -43.932  1.00222.41           C  
ANISOU 1188  CA  MET A 162    23834  34855  25816  -2739  -9869   2323
ATOM   1189  C   MET A 162      -7.630 -14.839 -44.178  1.00221.95           C  
ANISOU 1189  C   MET A 162    23562  34958  25810  -2637  -9787   2055
ATOM   1190  O   MET A 162      -6.625 -15.250 -44.769  1.00222.60           O  
ANISOU 1190  O   MET A 162    23619  35018  25940  -2359  -9916   1951
ATOM   1191  CB  MET A 162      -9.608 -15.950 -45.219  1.00220.31           C  
ANISOU 1191  CB  MET A 162    23691  34341  25677  -2649  -9827   2359
ATOM   1192  CG  MET A 162     -10.802 -16.892 -45.101  1.00220.78           C  
ANISOU 1192  CG  MET A 162    23953  34205  25729  -2755  -9917   2622
ATOM   1193  SD  MET A 162     -10.397 -18.568 -44.575  1.00223.89           S  
ANISOU 1193  SD  MET A 162    24514  34525  26029  -2614 -10217   2815
ATOM   1194  CE  MET A 162     -10.969 -18.536 -42.876  1.00225.69           C  
ANISOU 1194  CE  MET A 162    24729  34917  26107  -2967 -10210   3007
ATOM   1195  N   LEU A 163      -7.741 -13.584 -43.733  1.00212.83           N  
ANISOU 1195  N   LEU A 163    22248  33968  24651  -2864  -9572   1952
ATOM   1196  CA  LEU A 163      -6.685 -12.604 -43.964  1.00212.42           C  
ANISOU 1196  CA  LEU A 163    21975  34061  24672  -2806  -9476   1703
ATOM   1197  C   LEU A 163      -5.605 -12.694 -42.894  1.00215.08           C  
ANISOU 1197  C   LEU A 163    22197  34602  24922  -2803  -9603   1637
ATOM   1198  O   LEU A 163      -4.412 -12.770 -43.210  1.00216.03           O  
ANISOU 1198  O   LEU A 163    22203  34764  25114  -2591  -9712   1486
ATOM   1199  CB  LEU A 163      -7.283 -11.198 -44.011  1.00210.21           C  
ANISOU 1199  CB  LEU A 163    21576  33866  24427  -3055  -9171   1621
ATOM   1200  CG  LEU A 163      -6.344 -10.031 -44.311  1.00209.51           C  
ANISOU 1200  CG  LEU A 163    21249  33921  24434  -3046  -9020   1375
ATOM   1201  CD1 LEU A 163      -5.725 -10.180 -45.690  1.00208.55           C  
ANISOU 1201  CD1 LEU A 163    21108  33663  24469  -2752  -9081   1259
ATOM   1202  CD2 LEU A 163      -7.105  -8.722 -44.201  1.00207.50           C  
ANISOU 1202  CD2 LEU A 163    20905  33761  24173  -3326  -8700   1335
ATOM   1203  N   LEU A 164      -6.008 -12.684 -41.620  1.00208.46           N  
ANISOU 1203  N   LEU A 164    28470  28018  22718  -2655  -1765  -4588
ATOM   1204  CA  LEU A 164      -5.047 -12.842 -40.534  1.00208.15           C  
ANISOU 1204  CA  LEU A 164    28469  27847  22771  -2610  -1829  -4578
ATOM   1205  C   LEU A 164      -4.297 -14.163 -40.639  1.00213.30           C  
ANISOU 1205  C   LEU A 164    29566  28064  23415  -2563  -2039  -4989
ATOM   1206  O   LEU A 164      -3.167 -14.274 -40.151  1.00213.00           O  
ANISOU 1206  O   LEU A 164    29624  27883  23424  -2415  -2056  -5086
ATOM   1207  CB  LEU A 164      -5.760 -12.729 -39.183  1.00207.34           C  
ANISOU 1207  CB  LEU A 164    28158  27846  22775  -2904  -1881  -4278
ATOM   1208  CG  LEU A 164      -6.890 -13.721 -38.871  1.00212.13           C  
ANISOU 1208  CG  LEU A 164    28896  28328  23377  -3287  -2057  -4303
ATOM   1209  CD1 LEU A 164      -6.394 -15.019 -38.240  1.00216.96           C  
ANISOU 1209  CD1 LEU A 164    29840  28538  24058  -3457  -2310  -4515
ATOM   1210  CD2 LEU A 164      -7.964 -13.067 -38.007  1.00209.54           C  
ANISOU 1210  CD2 LEU A 164    28240  28301  23074  -3531  -1943  -3920
ATOM   1211  N   ARG A 165      -4.909 -15.172 -41.266  1.00205.66           N  
ANISOU 1211  N   ARG A 165    28870  26867  22403  -2690  -2194  -5254
ATOM   1212  CA  ARG A 165      -4.227 -16.447 -41.461  1.00211.75           C  
ANISOU 1212  CA  ARG A 165    30072  27169  23213  -2616  -2380  -5707
ATOM   1213  C   ARG A 165      -2.974 -16.281 -42.311  1.00212.63           C  
ANISOU 1213  C   ARG A 165    30399  27175  23216  -2183  -2230  -5959
ATOM   1214  O   ARG A 165      -2.011 -17.040 -42.154  1.00216.07           O  
ANISOU 1214  O   ARG A 165    31153  27224  23720  -2017  -2310  -6288
ATOM   1215  CB  ARG A 165      -5.179 -17.458 -42.103  1.00216.71           C  
ANISOU 1215  CB  ARG A 165    30914  27612  23814  -2841  -2529  -5937
ATOM   1216  CG  ARG A 165      -4.616 -18.866 -42.212  1.00223.04           C  
ANISOU 1216  CG  ARG A 165    32128  27887  24731  -2835  -2698  -6428
ATOM   1217  CD  ARG A 165      -5.601 -19.809 -42.882  1.00227.39           C  
ANISOU 1217  CD  ARG A 165    32884  28276  25236  -3112  -2811  -6617
ATOM   1218  NE  ARG A 165      -5.845 -19.441 -44.274  1.00227.00           N  
ANISOU 1218  NE  ARG A 165    32849  28410  24991  -2872  -2719  -6740
ATOM   1219  CZ  ARG A 165      -5.057 -19.792 -45.285  1.00230.18           C  
ANISOU 1219  CZ  ARG A 165    33521  28606  25333  -2495  -2684  -7159
ATOM   1220  NH1 ARG A 165      -3.973 -20.522 -45.062  1.00233.48           N  
ANISOU 1220  NH1 ARG A 165    34157  28639  25917  -2281  -2702  -7559
ATOM   1221  NH2 ARG A 165      -5.353 -19.414 -46.521  1.00229.90           N1+
ANISOU 1221  NH2 ARG A 165    33527  28747  25077  -2347  -2593  -7182
ATOM   1222  N   GLU A 166      -2.964 -15.293 -43.208  1.00210.73           N  
ANISOU 1222  N   GLU A 166    29978  27266  22823  -2022  -1966  -5802
ATOM   1223  CA  GLU A 166      -1.768 -14.997 -43.984  1.00211.36           C  
ANISOU 1223  CA  GLU A 166    30162  27358  22788  -1688  -1697  -5962
ATOM   1224  C   GLU A 166      -0.802 -14.090 -43.233  1.00206.94           C  
ANISOU 1224  C   GLU A 166    29268  27052  22307  -1562  -1499  -5751
ATOM   1225  O   GLU A 166       0.365 -13.988 -43.626  1.00207.74           O  
ANISOU 1225  O   GLU A 166    29365  27184  22384  -1281  -1260  -5938
ATOM   1226  CB  GLU A 166      -2.156 -14.368 -45.324  1.00210.96           C  
ANISOU 1226  CB  GLU A 166    29978  27588  22589  -1611  -1496  -5909
ATOM   1227  CG  GLU A 166      -2.886 -15.332 -46.251  1.00216.10           C  
ANISOU 1227  CG  GLU A 166    30991  27988  23127  -1680  -1666  -6197
ATOM   1228  CD  GLU A 166      -3.298 -14.694 -47.563  1.00215.52           C  
ANISOU 1228  CD  GLU A 166    30778  28202  22907  -1640  -1486  -6133
ATOM   1229  OE1 GLU A 166      -3.136 -13.465 -47.707  1.00210.78           O  
ANISOU 1229  OE1 GLU A 166    29765  27990  22333  -1582  -1258  -5841
ATOM   1230  OE2 GLU A 166      -3.786 -15.424 -48.452  1.00220.44           O1-
ANISOU 1230  OE2 GLU A 166    31691  28655  23410  -1670  -1596  -6387
ATOM   1231  N   ILE A 167      -1.261 -13.435 -42.169  1.00205.75           N  
ANISOU 1231  N   ILE A 167    28784  27119  22273  -1747  -1571  -5386
ATOM   1232  CA  ILE A 167      -0.358 -12.722 -41.274  1.00201.58           C  
ANISOU 1232  CA  ILE A 167    27974  26784  21835  -1652  -1460  -5206
ATOM   1233  C   ILE A 167       0.078 -13.613 -40.113  1.00203.78           C  
ANISOU 1233  C   ILE A 167    28488  26720  22220  -1768  -1705  -5341
ATOM   1234  O   ILE A 167       1.205 -13.483 -39.624  1.00202.89           O  
ANISOU 1234  O   ILE A 167    28299  26629  22161  -1607  -1625  -5413
ATOM   1235  CB  ILE A 167      -1.015 -11.424 -40.770  1.00194.80           C  
ANISOU 1235  CB  ILE A 167    26637  26326  21052  -1763  -1371  -4730
ATOM   1236  CG1 ILE A 167      -1.287 -10.476 -41.938  1.00192.35           C  
ANISOU 1236  CG1 ILE A 167    26088  26307  20691  -1637  -1140  -4618
ATOM   1237  CG2 ILE A 167      -0.139 -10.728 -39.739  1.00191.22           C  
ANISOU 1237  CG2 ILE A 167    25912  26051  20693  -1690  -1304  -4532
ATOM   1238  CD1 ILE A 167      -2.131  -9.278 -41.565  1.00186.90           C  
ANISOU 1238  CD1 ILE A 167    24993  25911  20110  -1749  -1060  -4207
ATOM   1239  N   LYS A 168      -0.794 -14.529 -39.672  1.00198.37           N  
ANISOU 1239  N   LYS A 168    28022  25741  21608  -2045  -2008  -5395
ATOM   1240  CA  LYS A 168      -0.419 -15.506 -38.654  1.00201.98           C  
ANISOU 1240  CA  LYS A 168    28704  25806  22234  -2197  -2277  -5558
ATOM   1241  C   LYS A 168       0.865 -16.235 -39.022  1.00206.68           C  
ANISOU 1241  C   LYS A 168    29714  25974  22840  -1912  -2246  -6008
ATOM   1242  O   LYS A 168       1.654 -16.594 -38.140  1.00207.95           O  
ANISOU 1242  O   LYS A 168    29971  25884  23157  -1933  -2353  -6099
ATOM   1243  CB  LYS A 168      -1.555 -16.512 -38.449  1.00206.47           C  
ANISOU 1243  CB  LYS A 168    29393  26148  22910  -2563  -2511  -5619
ATOM   1244  CG  LYS A 168      -1.285 -17.558 -37.378  1.00210.87           C  
ANISOU 1244  CG  LYS A 168    30182  26268  23671  -2885  -2720  -5678
ATOM   1245  CD  LYS A 168      -2.488 -18.468 -37.183  1.00214.05           C  
ANISOU 1245  CD  LYS A 168    30748  26471  24112  -3345  -2884  -5580
ATOM   1246  CE  LYS A 168      -2.642 -19.429 -38.353  1.00219.18           C  
ANISOU 1246  CE  LYS A 168    31742  26787  24747  -3264  -2909  -6036
ATOM   1247  NZ  LYS A 168      -3.744 -20.406 -38.133  1.00223.12           N1+
ANISOU 1247  NZ  LYS A 168    32476  27037  25264  -3744  -3096  -5920
ATOM   1248  N   ASN A 169       1.100 -16.450 -40.316  1.00200.35           N  
ANISOU 1248  N   ASN A 169    29155  25082  21887  -1678  -2025  -6278
ATOM   1249  CA  ASN A 169       2.374 -16.984 -40.775  1.00204.77           C  
ANISOU 1249  CA  ASN A 169    29863  25402  22539  -1330  -1760  -6731
ATOM   1250  C   ASN A 169       3.430 -15.891 -40.687  1.00200.61           C  
ANISOU 1250  C   ASN A 169    28757  25390  22074   -888  -1514  -6644
ATOM   1251  O   ASN A 169       3.960 -15.439 -41.706  1.00199.68           O  
ANISOU 1251  O   ASN A 169    28437  25553  21881   -519  -1209  -6748
ATOM   1252  CB  ASN A 169       2.253 -17.513 -42.206  1.00208.65           C  
ANISOU 1252  CB  ASN A 169    30658  25729  22890  -1180  -1569  -7040
ATOM   1253  CG  ASN A 169       1.373 -18.744 -42.300  1.00213.78           C  
ANISOU 1253  CG  ASN A 169    31850  25846  23531  -1601  -1776  -7157
ATOM   1254  OD1 ASN A 169       1.441 -19.636 -41.455  1.00217.57           O  
ANISOU 1254  OD1 ASN A 169    32226  26059  24380  -1806  -1904  -7459
ATOM   1255  ND2 ASN A 169       0.539 -18.798 -43.332  1.00214.73           N  
ANISOU 1255  ND2 ASN A 169    32117  25992  23477  -1496  -1928  -7111
ATOM   1256  N   ASP A 170       3.731 -15.455 -39.464  1.00200.45           N  
ANISOU 1256  N   ASP A 170    28477  25509  22176   -959  -1667  -6423
ATOM   1257  CA  ASP A 170       4.668 -14.363 -39.228  1.00197.14           C  
ANISOU 1257  CA  ASP A 170    27521  25603  21780   -611  -1486  -6273
ATOM   1258  C   ASP A 170       6.104 -14.878 -39.188  1.00202.11           C  
ANISOU 1258  C   ASP A 170    28132  25948  22712     60  -1476  -6506
ATOM   1259  O   ASP A 170       6.956 -14.428 -39.962  1.00202.84           O  
ANISOU 1259  O   ASP A 170    27954  26360  22756    552  -1198  -6683
ATOM   1260  CB  ASP A 170       4.300 -13.642 -37.924  1.00192.47           C  
ANISOU 1260  CB  ASP A 170    26680  25274  21177  -1008  -1645  -5809
ATOM   1261  CG  ASP A 170       5.066 -12.345 -37.728  1.00188.07           C  
ANISOU 1261  CG  ASP A 170    25581  25297  20581   -760  -1443  -5547
ATOM   1262  OD1 ASP A 170       5.922 -12.012 -38.572  1.00189.31           O  
ANISOU 1262  OD1 ASP A 170    25534  25675  20722   -284  -1197  -5722
ATOM   1263  OD2 ASP A 170       4.803 -11.651 -36.723  1.00183.74           O1-
ANISOU 1263  OD2 ASP A 170    24816  24977  20018  -1056  -1528  -5127
ATOM   1264  N   ARG A 171       6.382 -15.822 -38.293  1.00196.75           N  
ANISOU 1264  N   ARG A 171    27727  24629  22400     72  -1743  -6299
ATOM   1265  CA  ARG A 171       7.710 -16.415 -38.183  1.00205.55           C  
ANISOU 1265  CA  ARG A 171    28840  25348  23911    710  -1728  -6282
ATOM   1266  C   ARG A 171       7.902 -17.429 -39.308  1.00211.70           C  
ANISOU 1266  C   ARG A 171    30012  25684  24742   1103  -1653  -6858
ATOM   1267  O   ARG A 171       7.247 -18.476 -39.339  1.00214.90           O  
ANISOU 1267  O   ARG A 171    30953  25491  25208    865  -1888  -7049
ATOM   1268  CB  ARG A 171       7.897 -17.038 -36.800  1.00210.28           C  
ANISOU 1268  CB  ARG A 171    29599  25417  24882    553  -2074  -5827
ATOM   1269  CG  ARG A 171       6.848 -18.073 -36.404  1.00212.01           C  
ANISOU 1269  CG  ARG A 171    30381  25038  25136     21  -2424  -5854
ATOM   1270  CD  ARG A 171       7.084 -18.610 -35.000  1.00215.98           C  
ANISOU 1270  CD  ARG A 171    31007  25067  25987   -163  -2775  -5355
ATOM   1271  NE  ARG A 171       8.295 -19.421 -34.911  1.00226.64           N  
ANISOU 1271  NE  ARG A 171    32470  25851  27792    468  -2851  -5354
ATOM   1272  CZ  ARG A 171       8.869 -19.782 -33.768  1.00232.05           C  
ANISOU 1272  CZ  ARG A 171    33159  26172  28837    491  -3116  -4894
ATOM   1273  NH1 ARG A 171       8.343 -19.406 -32.611  1.00225.82           N  
ANISOU 1273  NH1 ARG A 171    32283  25537  27983   -107  -3318  -4409
ATOM   1274  NH2 ARG A 171       9.969 -20.522 -33.782  1.00243.05           N1+
ANISOU 1274  NH2 ARG A 171    34639  27059  30651   1114  -3180  -4922
ATOM   1275  N   GLY A 172       8.787 -17.106 -40.250  1.00211.51           N  
ANISOU 1275  N   GLY A 172    29726  25971  24666   1685  -1326  -7142
ATOM   1276  CA  GLY A 172       9.082 -18.006 -41.349  1.00217.34           C  
ANISOU 1276  CA  GLY A 172    30799  26343  25438   2124  -1208  -7721
ATOM   1277  C   GLY A 172       7.921 -18.294 -42.271  1.00214.55           C  
ANISOU 1277  C   GLY A 172    30828  25958  24731   1724  -1198  -8147
ATOM   1278  O   GLY A 172       7.925 -19.323 -42.953  1.00220.66           O  
ANISOU 1278  O   GLY A 172    32018  26227  25595   1884  -1175  -8460
ATOM   1279  N   GLY A 173       6.922 -17.417 -42.317  1.00215.51           N  
ANISOU 1279  N   GLY A 173    30748  26611  24526   1094  -1123  -7829
ATOM   1280  CA  GLY A 173       5.774 -17.622 -43.179  1.00215.22           C  
ANISOU 1280  CA  GLY A 173    30987  26575  24214    584  -1030  -7825
ATOM   1281  C   GLY A 173       5.635 -16.543 -44.233  1.00210.86           C  
ANISOU 1281  C   GLY A 173    30085  26676  23358    541   -682  -7627
ATOM   1282  O   GLY A 173       4.529 -16.065 -44.505  1.00206.14           O  
ANISOU 1282  O   GLY A 173    29521  26288  22515     57   -705  -7337
ATOM   1283  N   GLU A 174       6.755 -16.155 -44.834  1.00221.32           N  
ANISOU 1283  N   GLU A 174    31079  28288  24726   1084   -407  -7740
ATOM   1284  CA  GLU A 174       6.814 -15.022 -45.742  1.00218.46           C  
ANISOU 1284  CA  GLU A 174    30324  28541  24142   1072   -130  -7496
ATOM   1285  C   GLU A 174       7.323 -15.480 -47.105  1.00224.01           C  
ANISOU 1285  C   GLU A 174    31150  29187  24776   1401    134  -7822
ATOM   1286  O   GLU A 174       8.113 -16.425 -47.197  1.00231.25           O  
ANISOU 1286  O   GLU A 174    32251  29728  25884   1853    178  -8208
ATOM   1287  CB  GLU A 174       7.725 -13.930 -45.163  1.00214.73           C  
ANISOU 1287  CB  GLU A 174    29263  28578  23745   1327    -48  -7231
ATOM   1288  CG  GLU A 174       7.280 -13.439 -43.795  1.00210.01           C  
ANISOU 1288  CG  GLU A 174    28537  28060  23195   1001   -292  -6908
ATOM   1289  CD  GLU A 174       5.909 -12.794 -43.817  1.00205.95           C  
ANISOU 1289  CD  GLU A 174    28047  27704  22501    401   -371  -6515
ATOM   1290  OE1 GLU A 174       5.557 -12.161 -44.834  1.00205.48           O  
ANISOU 1290  OE1 GLU A 174    27869  27907  22298    323   -213  -6362
ATOM   1291  OE2 GLU A 174       5.178 -12.925 -42.811  1.00203.50           O1-
ANISOU 1291  OE2 GLU A 174    27869  27233  22219     35   -616  -6344
ATOM   1292  N   ASP A 175       6.871 -14.816 -48.172  1.00223.47           N  
ANISOU 1292  N   ASP A 175    30988  29461  24460   1200    288  -7656
ATOM   1293  CA  ASP A 175       5.940 -13.690 -48.103  1.00216.22           C  
ANISOU 1293  CA  ASP A 175    29843  28913  23396    761    205  -7180
ATOM   1294  C   ASP A 175       4.899 -13.708 -49.222  1.00216.68           C  
ANISOU 1294  C   ASP A 175    30161  28946  23220    465    201  -7145
ATOM   1295  O   ASP A 175       5.216 -13.995 -50.376  1.00220.79           O  
ANISOU 1295  O   ASP A 175    30802  29464  23625    639    383  -7386
ATOM   1296  CB  ASP A 175       6.708 -12.360 -48.133  1.00212.09           C  
ANISOU 1296  CB  ASP A 175    28710  28972  22903    931    357  -6870
ATOM   1297  CG  ASP A 175       7.615 -12.225 -49.347  1.00215.91           C  
ANISOU 1297  CG  ASP A 175    29032  29686  23316   1271    628  -7041
ATOM   1298  OD1 ASP A 175       7.749 -13.197 -50.119  1.00222.40           O  
ANISOU 1298  OD1 ASP A 175    30203  30217  24083   1438    731  -7430
ATOM   1299  OD2 ASP A 175       8.196 -11.135 -49.531  1.00213.46           O1-
ANISOU 1299  OD2 ASP A 175    28257  29844  23004   1353    729  -6778
ATOM   1300  N   PRO A 176       3.654 -13.415 -48.876  1.00215.87           N  
ANISOU 1300  N   PRO A 176    30134  28831  23056     47    -22  -6847
ATOM   1301  CA  PRO A 176       2.617 -13.208 -49.890  1.00215.73           C  
ANISOU 1301  CA  PRO A 176    30239  28878  22852   -186    -71  -6742
ATOM   1302  C   PRO A 176       2.765 -11.824 -50.515  1.00211.56           C  
ANISOU 1302  C   PRO A 176    29202  28865  22315   -154     80  -6430
ATOM   1303  O   PRO A 176       3.638 -11.038 -50.151  1.00208.89           O  
ANISOU 1303  O   PRO A 176    28447  28824  22096     21    201  -6278
ATOM   1304  CB  PRO A 176       1.318 -13.336 -49.092  1.00212.88           C  
ANISOU 1304  CB  PRO A 176    30022  28355  22510   -561   -388  -6514
ATOM   1305  CG  PRO A 176       1.697 -12.933 -47.709  1.00208.67           C  
ANISOU 1305  CG  PRO A 176    29218  27904  22164   -569   -442  -6307
ATOM   1306  CD  PRO A 176       3.107 -13.397 -47.508  1.00211.94           C  
ANISOU 1306  CD  PRO A 176    29633  28221  22673   -206   -271  -6625
ATOM   1307  N   ASN A 177       1.890 -11.534 -51.475  1.00211.64           N  
ANISOU 1307  N   ASN A 177    29255  28966  22193   -331     42  -6338
ATOM   1308  CA  ASN A 177       1.913 -10.244 -52.155  1.00207.78           C  
ANISOU 1308  CA  ASN A 177    28329  28905  21715   -344    148  -6057
ATOM   1309  C   ASN A 177       1.509  -9.143 -51.183  1.00201.01           C  
ANISOU 1309  C   ASN A 177    27024  28301  21051   -505     58  -5649
ATOM   1310  O   ASN A 177       0.353  -9.077 -50.754  1.00199.25           O  
ANISOU 1310  O   ASN A 177    26777  28061  20866   -774   -102  -5513
ATOM   1311  CB  ASN A 177       0.983 -10.261 -53.365  1.00210.20           C  
ANISOU 1311  CB  ASN A 177    28705  29308  21854   -530    115  -6153
ATOM   1312  CG  ASN A 177       1.458 -11.198 -54.454  1.00216.49           C  
ANISOU 1312  CG  ASN A 177    29931  29886  22439   -351    232  -6537
ATOM   1313  OD1 ASN A 177       0.809 -12.199 -54.753  1.00221.06           O  
ANISOU 1313  OD1 ASN A 177    30997  30116  22879   -438    103  -6752
ATOM   1314  ND2 ASN A 177       2.594 -10.872 -55.060  1.00217.21           N  
ANISOU 1314  ND2 ASN A 177    29838  30190  22503    -97    469  -6630
ATOM   1315  N   GLN A 178       2.462  -8.276 -50.829  1.00204.85           N  
ANISOU 1315  N   GLN A 178    27120  29053  21659   -344    170  -5478
ATOM   1316  CA  GLN A 178       2.113  -7.064 -50.099  1.00199.65           C  
ANISOU 1316  CA  GLN A 178    25975  28707  21176   -494    114  -5125
ATOM   1317  C   GLN A 178       1.185  -6.174 -50.911  1.00198.61           C  
ANISOU 1317  C   GLN A 178    25507  28923  21033   -721    117  -5022
ATOM   1318  O   GLN A 178       0.491  -5.328 -50.339  1.00194.57           O  
ANISOU 1318  O   GLN A 178    24676  28595  20657   -904     65  -4764
ATOM   1319  CB  GLN A 178       3.374  -6.284 -49.721  1.00197.41           C  
ANISOU 1319  CB  GLN A 178    25352  28654  21001   -273    213  -4979
ATOM   1320  CG  GLN A 178       4.125  -5.712 -50.914  1.00199.65           C  
ANISOU 1320  CG  GLN A 178    25378  29272  21208   -134    356  -5056
ATOM   1321  CD  GLN A 178       5.370  -4.949 -50.511  1.00197.83           C  
ANISOU 1321  CD  GLN A 178    24805  29285  21075     70    418  -4895
ATOM   1322  OE1 GLN A 178       5.663  -4.797 -49.325  1.00195.46           O  
ANISOU 1322  OE1 GLN A 178    24452  28910  20905    105    361  -4716
ATOM   1323  NE2 GLN A 178       6.110  -4.459 -51.501  1.00199.16           N  
ANISOU 1323  NE2 GLN A 178    24742  29763  21167    188    523  -4953
ATOM   1324  N   LYS A 179       1.171  -6.345 -52.232  1.00202.47           N  
ANISOU 1324  N   LYS A 179    26068  29502  21359   -710    191  -5228
ATOM   1325  CA  LYS A 179       0.251  -5.604 -53.086  1.00202.46           C  
ANISOU 1325  CA  LYS A 179    25797  29804  21324   -943    187  -5157
ATOM   1326  C   LYS A 179      -1.187  -6.061 -52.868  1.00202.95           C  
ANISOU 1326  C   LYS A 179    26036  29711  21364  -1218     63  -5145
ATOM   1327  O   LYS A 179      -2.099  -5.237 -52.727  1.00200.88           O  
ANISOU 1327  O   LYS A 179    25452  29680  21194  -1434     41  -4933
ATOM   1328  CB  LYS A 179       0.675  -5.780 -54.544  1.00206.92           C  
ANISOU 1328  CB  LYS A 179    26439  30489  21692   -864    293  -5401
ATOM   1329  CG  LYS A 179      -0.190  -5.101 -55.582  1.00207.38           C  
ANISOU 1329  CG  LYS A 179    26264  30851  21679  -1104    292  -5362
ATOM   1330  CD  LYS A 179       0.471  -5.243 -56.942  1.00211.08           C  
ANISOU 1330  CD  LYS A 179    26796  31460  21946   -999    408  -5600
ATOM   1331  CE  LYS A 179       0.445  -6.691 -57.408  1.00216.43           C  
ANISOU 1331  CE  LYS A 179    28050  31765  22418   -919    423  -5953
ATOM   1332  NZ  LYS A 179       1.066  -6.863 -58.748  1.00220.74           N1+
ANISOU 1332  NZ  LYS A 179    28674  32450  22747   -812    561  -6209
ATOM   1333  N   VAL A 180      -1.404  -7.377 -52.818  1.00203.79           N  
ANISOU 1333  N   VAL A 180    26659  29423  21349  -1211    -22  -5372
ATOM   1334  CA  VAL A 180      -2.757  -7.905 -52.669  1.00204.71           C  
ANISOU 1334  CA  VAL A 180    26958  29398  21423  -1485   -169  -5376
ATOM   1335  C   VAL A 180      -3.286  -7.639 -51.264  1.00201.06           C  
ANISOU 1335  C   VAL A 180    26341  28909  21142  -1612   -260  -5115
ATOM   1336  O   VAL A 180      -4.371  -7.072 -51.091  1.00199.32           O  
ANISOU 1336  O   VAL A 180    25853  28897  20981  -1859   -276  -4934
ATOM   1337  CB  VAL A 180      -2.787  -9.406 -53.009  1.00209.51           C  
ANISOU 1337  CB  VAL A 180    28191  29563  21850  -1434   -279  -5704
ATOM   1338  CG1 VAL A 180      -4.163  -9.981 -52.730  1.00210.51           C  
ANISOU 1338  CG1 VAL A 180    28487  29549  21950  -1731   -475  -5692
ATOM   1339  CG2 VAL A 180      -2.404  -9.624 -54.464  1.00213.85           C  
ANISOU 1339  CG2 VAL A 180    28883  30172  22198  -1336   -166  -5970
ATOM   1340  N   ILE A 181      -2.530  -8.044 -50.240  1.00204.72           N  
ANISOU 1340  N   ILE A 181    26973  29125  21685  -1447   -306  -5095
ATOM   1341  CA  ILE A 181      -2.982  -7.846 -48.865  1.00200.90           C  
ANISOU 1341  CA  ILE A 181    26368  28610  21357  -1574   -396  -4857
ATOM   1342  C   ILE A 181      -3.035  -6.362 -48.527  1.00196.41           C  
ANISOU 1342  C   ILE A 181    25222  28452  20952  -1613   -270  -4559
ATOM   1343  O   ILE A 181      -3.945  -5.904 -47.825  1.00194.41           O  
ANISOU 1343  O   ILE A 181    24752  28322  20794  -1814   -288  -4357
ATOM   1344  CB  ILE A 181      -2.083  -8.619 -47.884  1.00200.54           C  
ANISOU 1344  CB  ILE A 181    26653  28197  21347  -1391   -489  -4910
ATOM   1345  CG1 ILE A 181      -2.184 -10.122 -48.141  1.00205.54           C  
ANISOU 1345  CG1 ILE A 181    27902  28360  21834  -1369   -658  -5211
ATOM   1346  CG2 ILE A 181      -2.468  -8.315 -46.446  1.00196.70           C  
ANISOU 1346  CG2 ILE A 181    26001  27719  21016  -1527   -575  -4647
ATOM   1347  CD1 ILE A 181      -1.181 -10.927 -47.359  1.00206.85           C  
ANISOU 1347  CD1 ILE A 181    28376  28200  22020  -1197   -713  -5369
ATOM   1348  N   HIS A 182      -2.067  -5.585 -49.019  1.00200.45           N  
ANISOU 1348  N   HIS A 182    25481  29183  21498  -1421   -144  -4534
ATOM   1349  CA  HIS A 182      -2.104  -4.143 -48.799  1.00196.73           C  
ANISOU 1349  CA  HIS A 182    24488  29078  21182  -1452    -58  -4270
ATOM   1350  C   HIS A 182      -3.306  -3.509 -49.484  1.00196.94           C  
ANISOU 1350  C   HIS A 182    24274  29362  21192  -1682    -24  -4206
ATOM   1351  O   HIS A 182      -3.838  -2.505 -48.999  1.00194.13           O  
ANISOU 1351  O   HIS A 182    23569  29225  20967  -1779     19  -3981
ATOM   1352  CB  HIS A 182      -0.807  -3.499 -49.291  1.00195.97           C  
ANISOU 1352  CB  HIS A 182    24187  29165  21107  -1217     32  -4270
ATOM   1353  CG  HIS A 182      -0.739  -2.023 -49.055  1.00192.48           C  
ANISOU 1353  CG  HIS A 182    23251  29058  20824  -1236     84  -4007
ATOM   1354  ND1 HIS A 182      -0.535  -1.478 -47.806  1.00189.16           N  
ANISOU 1354  ND1 HIS A 182    22662  28644  20565  -1213     72  -3785
ATOM   1355  CD2 HIS A 182      -0.849  -0.978 -49.908  1.00192.02           C  
ANISOU 1355  CD2 HIS A 182    22860  29320  20779  -1278    139  -3938
ATOM   1356  CE1 HIS A 182      -0.521  -0.160 -47.900  1.00186.96           C  
ANISOU 1356  CE1 HIS A 182    21982  28658  20396  -1228    122  -3599
ATOM   1357  NE2 HIS A 182      -0.709   0.169 -49.165  1.00188.49           N  
ANISOU 1357  NE2 HIS A 182    22071  29042  20504  -1267    156  -3684
ATOM   1358  N   GLY A 183      -3.749  -4.078 -50.607  1.00200.88           N  
ANISOU 1358  N   GLY A 183    24971  29834  21521  -1765    -37  -4409
ATOM   1359  CA  GLY A 183      -4.972  -3.603 -51.227  1.00202.11           C  
ANISOU 1359  CA  GLY A 183    24940  30214  21639  -2005    -18  -4354
ATOM   1360  C   GLY A 183      -6.218  -4.001 -50.462  1.00202.03           C  
ANISOU 1360  C   GLY A 183    25004  30117  21642  -2240    -86  -4274
ATOM   1361  O   GLY A 183      -7.190  -3.242 -50.419  1.00200.36           O  
ANISOU 1361  O   GLY A 183    24501  30150  21477  -2411    -37  -4117
ATOM   1362  N   VAL A 184      -6.209  -5.185 -49.845  1.00200.30           N  
ANISOU 1362  N   VAL A 184    25176  29556  21374  -2250   -203  -4383
ATOM   1363  CA  VAL A 184      -7.373  -5.642 -49.091  1.00200.23           C  
ANISOU 1363  CA  VAL A 184    25243  29472  21362  -2499   -285  -4307
ATOM   1364  C   VAL A 184      -7.532  -4.829 -47.811  1.00196.23           C  
ANISOU 1364  C   VAL A 184    24421  29105  21033  -2522   -224  -4037
ATOM   1365  O   VAL A 184      -8.622  -4.332 -47.505  1.00195.46           O  
ANISOU 1365  O   VAL A 184    24088  29217  20961  -2723   -172  -3889
ATOM   1366  CB  VAL A 184      -7.266  -7.148 -48.793  1.00203.41           C  
ANISOU 1366  CB  VAL A 184    26172  29447  21667  -2506   -468  -4505
ATOM   1367  CG1 VAL A 184      -8.400  -7.587 -47.878  1.00203.64           C  
ANISOU 1367  CG1 VAL A 184    26242  29423  21708  -2783   -567  -4396
ATOM   1368  CG2 VAL A 184      -7.288  -7.948 -50.085  1.00208.14           C  
ANISOU 1368  CG2 VAL A 184    27102  29910  22073  -2504   -526  -4790
ATOM   1369  N   ILE A 185      -6.450  -4.685 -47.043  1.00198.17           N  
ANISOU 1369  N   ILE A 185    24665  29242  21388  -2314   -220  -3976
ATOM   1370  CA  ILE A 185      -6.522  -3.926 -45.799  1.00194.53           C  
ANISOU 1370  CA  ILE A 185    23932  28897  21083  -2330   -162  -3731
ATOM   1371  C   ILE A 185      -6.674  -2.438 -46.089  1.00191.92           C  
ANISOU 1371  C   ILE A 185    23133  28933  20855  -2300    -12  -3569
ATOM   1372  O   ILE A 185      -7.482  -1.748 -45.455  1.00190.08           O  
ANISOU 1372  O   ILE A 185    22647  28883  20690  -2419     61  -3400
ATOM   1373  CB  ILE A 185      -5.286  -4.209 -44.926  1.00192.86           C  
ANISOU 1373  CB  ILE A 185    23869  28463  20946  -2126   -216  -3712
ATOM   1374  CG1 ILE A 185      -5.238  -5.685 -44.530  1.00195.12           C  
ANISOU 1374  CG1 ILE A 185    24645  28354  21140  -2164   -400  -3869
ATOM   1375  CG2 ILE A 185      -5.296  -3.334 -43.683  1.00189.35           C  
ANISOU 1375  CG2 ILE A 185    23135  28155  20653  -2143   -145  -3456
ATOM   1376  CD1 ILE A 185      -3.939  -6.100 -43.878  1.00194.20           C  
ANISOU 1376  CD1 ILE A 185    24740  27983  21064  -1936   -474  -3899
ATOM   1377  N   ASN A 186      -5.907  -1.921 -47.052  1.00197.87           N  
ANISOU 1377  N   ASN A 186    23774  29800  21608  -2138     31  -3628
ATOM   1378  CA  ASN A 186      -6.020  -0.515 -47.421  1.00195.87           C  
ANISOU 1378  CA  ASN A 186    23109  29870  21444  -2109    136  -3486
ATOM   1379  C   ASN A 186      -7.380  -0.197 -48.029  1.00197.03           C  
ANISOU 1379  C   ASN A 186    23121  30219  21521  -2316    175  -3475
ATOM   1380  O   ASN A 186      -7.803   0.963 -48.006  1.00195.42           O  
ANISOU 1380  O   ASN A 186    22593  30262  21395  -2323    256  -3331
ATOM   1381  CB  ASN A 186      -4.902  -0.143 -48.400  1.00196.44           C  
ANISOU 1381  CB  ASN A 186    23115  30023  21500  -1923    150  -3561
ATOM   1382  CG  ASN A 186      -4.721   1.360 -48.545  1.00193.80           C  
ANISOU 1382  CG  ASN A 186    22378  29975  21282  -1860    225  -3387
ATOM   1383  OD1 ASN A 186      -5.405   2.150 -47.897  1.00191.15           O  
ANISOU 1383  OD1 ASN A 186    21829  29759  21042  -1924    277  -3221
ATOM   1384  ND2 ASN A 186      -3.790   1.759 -49.405  1.00194.82           N  
ANISOU 1384  ND2 ASN A 186    22421  30216  21388  -1731    232  -3431
ATOM   1385  N   SER A 187      -8.078  -1.203 -48.559  1.00197.58           N  
ANISOU 1385  N   SER A 187    23453  30183  21437  -2481    111  -3627
ATOM   1386  CA  SER A 187      -9.408  -0.994 -49.115  1.00199.53           C  
ANISOU 1386  CA  SER A 187    23589  30629  21596  -2699    138  -3614
ATOM   1387  C   SER A 187     -10.436  -0.610 -48.059  1.00197.70           C  
ANISOU 1387  C   SER A 187    23176  30519  21423  -2835    192  -3445
ATOM   1388  O   SER A 187     -11.523  -0.147 -48.420  1.00198.82           O  
ANISOU 1388  O   SER A 187    23141  30892  21508  -2980    240  -3398
ATOM   1389  CB  SER A 187      -9.872  -2.253 -49.850  1.00203.73           C  
ANISOU 1389  CB  SER A 187    24479  30994  21937  -2860     38  -3819
ATOM   1390  OG  SER A 187     -11.181  -2.091 -50.367  1.00206.95           O  
ANISOU 1390  OG  SER A 187    24781  31607  22245  -3095     56  -3796
ATOM   1391  N   PHE A 188     -10.124  -0.785 -46.773  1.00192.63           N  
ANISOU 1391  N   PHE A 188    22574  29742  20875  -2793    188  -3356
ATOM   1392  CA  PHE A 188     -11.100  -0.473 -45.737  1.00191.60           C  
ANISOU 1392  CA  PHE A 188    22283  29744  20773  -2931    253  -3209
ATOM   1393  C   PHE A 188     -11.145   1.020 -45.437  1.00188.74           C  
ANISOU 1393  C   PHE A 188    21537  29639  20537  -2806    380  -3053
ATOM   1394  O   PHE A 188     -12.231   1.581 -45.256  1.00188.76           O  
ANISOU 1394  O   PHE A 188    21336  29873  20511  -2908    458  -2981
ATOM   1395  CB  PHE A 188     -10.799  -1.271 -44.467  1.00191.20           C  
ANISOU 1395  CB  PHE A 188    22444  29455  20749  -2965    194  -3174
ATOM   1396  CG  PHE A 188     -11.044  -2.747 -44.609  1.00194.44           C  
ANISOU 1396  CG  PHE A 188    23250  29606  21020  -3129     46  -3318
ATOM   1397  CD1 PHE A 188     -11.742  -3.245 -45.697  1.00197.49           C  
ANISOU 1397  CD1 PHE A 188    23754  30023  21260  -3278     -4  -3450
ATOM   1398  CD2 PHE A 188     -10.586  -3.637 -43.651  1.00194.65           C  
ANISOU 1398  CD2 PHE A 188    23551  29349  21057  -3140    -61  -3322
ATOM   1399  CE1 PHE A 188     -11.967  -4.597 -45.833  1.00200.76           C  
ANISOU 1399  CE1 PHE A 188    24557  30177  21546  -3429   -161  -3593
ATOM   1400  CE2 PHE A 188     -10.813  -4.994 -43.781  1.00197.92           C  
ANISOU 1400  CE2 PHE A 188    24356  29496  21349  -3283   -231  -3465
ATOM   1401  CZ  PHE A 188     -11.505  -5.474 -44.873  1.00201.02           C  
ANISOU 1401  CZ  PHE A 188    24868  29910  21601  -3426   -282  -3606
ATOM   1402  N   VAL A 189      -9.993   1.682 -45.374  1.00201.44           N  
ANISOU 1402  N   VAL A 189    23053  31214  22272  -2581    395  -3005
ATOM   1403  CA  VAL A 189      -9.965   3.142 -45.177  1.00199.72           C  
ANISOU 1403  CA  VAL A 189    22509  31209  22166  -2450    491  -2868
ATOM   1404  C   VAL A 189      -9.984   3.752 -46.575  1.00200.82           C  
ANISOU 1404  C   VAL A 189    22534  31509  22261  -2406    492  -2919
ATOM   1405  O   VAL A 189      -8.971   4.195 -47.122  1.00200.79           O  
ANISOU 1405  O   VAL A 189    22488  31497  22306  -2255    473  -2921
ATOM   1406  CB  VAL A 189      -8.755   3.594 -44.352  1.00197.56           C  
ANISOU 1406  CB  VAL A 189    22197  30829  22039  -2263    497  -2770
ATOM   1407  CG1 VAL A 189      -8.764   5.110 -44.164  1.00195.60           C  
ANISOU 1407  CG1 VAL A 189    21656  30774  21889  -2136    580  -2638
ATOM   1408  CG2 VAL A 189      -8.725   2.886 -43.018  1.00197.51           C  
ANISOU 1408  CG2 VAL A 189    22341  30653  22050  -2332    484  -2723
ATOM   1409  N   HIS A 190     -11.170   3.755 -47.177  1.00203.93           N  
ANISOU 1409  N   HIS A 190    22879  32066  22539  -2561    509  -2956
ATOM   1410  CA  HIS A 190     -11.436   4.593 -48.341  1.00204.87           C  
ANISOU 1410  CA  HIS A 190    22843  32389  22607  -2536    524  -2961
ATOM   1411  C   HIS A 190     -12.825   5.209 -48.342  1.00205.21           C  
ANISOU 1411  C   HIS A 190    22711  32676  22583  -2630    582  -2908
ATOM   1412  O   HIS A 190     -13.025   6.227 -49.014  1.00205.44           O  
ANISOU 1412  O   HIS A 190    22580  32882  22596  -2559    603  -2867
ATOM   1413  CB  HIS A 190     -11.240   3.800 -49.639  1.00207.32           C  
ANISOU 1413  CB  HIS A 190    23341  32646  22786  -2626    449  -3116
ATOM   1414  CG  HIS A 190     -11.171   4.659 -50.863  1.00207.96           C  
ANISOU 1414  CG  HIS A 190    23284  32915  22816  -2589    455  -3114
ATOM   1415  ND1 HIS A 190     -12.292   5.058 -51.559  1.00209.81           N  
ANISOU 1415  ND1 HIS A 190    23422  33360  22936  -2717    467  -3105
ATOM   1416  CD2 HIS A 190     -10.113   5.204 -51.509  1.00207.10           C  
ANISOU 1416  CD2 HIS A 190    23120  32828  22740  -2451    444  -3112
ATOM   1417  CE1 HIS A 190     -11.927   5.808 -52.585  1.00209.91           C  
ANISOU 1417  CE1 HIS A 190    23346  33499  22913  -2662    460  -3095
ATOM   1418  NE2 HIS A 190     -10.610   5.912 -52.577  1.00208.72           N  
ANISOU 1418  NE2 HIS A 190    23213  33243  22848  -2508    450  -3099
ATOM   1419  N   VAL A 191     -13.784   4.645 -47.611  1.00204.38           N  
ANISOU 1419  N   VAL A 191    22637  32597  22421  -2786    605  -2905
ATOM   1420  CA  VAL A 191     -15.197   4.978 -47.739  1.00205.68           C  
ANISOU 1420  CA  VAL A 191    22663  33016  22470  -2909    648  -2887
ATOM   1421  C   VAL A 191     -15.621   5.763 -46.507  1.00204.07           C  
ANISOU 1421  C   VAL A 191    22340  32846  22351  -2782    699  -2769
ATOM   1422  O   VAL A 191     -15.609   5.232 -45.390  1.00203.60           O  
ANISOU 1422  O   VAL A 191    22353  32679  22328  -2830    715  -2739
ATOM   1423  CB  VAL A 191     -16.054   3.713 -47.898  1.00208.09           C  
ANISOU 1423  CB  VAL A 191    23147  33304  22615  -3191    599  -2967
ATOM   1424  CG1 VAL A 191     -17.530   4.074 -47.983  1.00210.38           C  
ANISOU 1424  CG1 VAL A 191    23267  33896  22770  -3324    643  -2936
ATOM   1425  CG2 VAL A 191     -15.604   2.912 -49.112  1.00209.90           C  
ANISOU 1425  CG2 VAL A 191    23604  33390  22760  -3274    498  -3093
ATOM   1426  N   GLU A 192     -16.001   7.023 -46.712  1.00212.17           N  
ANISOU 1426  N   GLU A 192    23313  33889  23413  -2581    652  -2685
ATOM   1427  CA  GLU A 192     -16.559   7.842 -45.646  1.00211.85           C  
ANISOU 1427  CA  GLU A 192    23281  33766  23446  -2412    625  -2580
ATOM   1428  C   GLU A 192     -17.215   9.072 -46.254  1.00212.55           C  
ANISOU 1428  C   GLU A 192    23274  33990  23494  -2273    589  -2552
ATOM   1429  O   GLU A 192     -16.737   9.601 -47.261  1.00211.62           O  
ANISOU 1429  O   GLU A 192    23131  33907  23368  -2209    566  -2556
ATOM   1430  CB  GLU A 192     -15.485   8.258 -44.629  1.00209.67           C  
ANISOU 1430  CB  GLU A 192    23121  33184  23359  -2204    593  -2480
ATOM   1431  CG  GLU A 192     -16.013   9.125 -43.491  1.00209.71           C  
ANISOU 1431  CG  GLU A 192    23137  33110  23434  -2046    571  -2390
ATOM   1432  CD  GLU A 192     -17.059   8.418 -42.644  1.00211.23           C  
ANISOU 1432  CD  GLU A 192    23303  33417  23539  -2215    611  -2414
ATOM   1433  OE1 GLU A 192     -17.028   7.172 -42.564  1.00212.14           O  
ANISOU 1433  OE1 GLU A 192    23448  33574  23580  -2448    654  -2466
ATOM   1434  OE2 GLU A 192     -17.920   9.113 -42.064  1.00211.95           O1-
ANISOU 1434  OE2 GLU A 192    23338  33578  23615  -2127    602  -2389
ATOM   1435  N   GLN A 193     -18.313   9.505 -45.639  1.00220.45           N  
ANISOU 1435  N   GLN A 193    24214  35096  24449  -2237    586  -2533
ATOM   1436  CA  GLN A 193     -19.037  10.707 -46.041  1.00222.42           C  
ANISOU 1436  CA  GLN A 193    24360  35505  24644  -2092    550  -2523
ATOM   1437  C   GLN A 193     -18.117  11.917 -46.163  1.00221.23           C  
ANISOU 1437  C   GLN A 193    24260  35180  24619  -1838    499  -2455
ATOM   1438  O   GLN A 193     -17.327  12.201 -45.263  1.00219.04           O  
ANISOU 1438  O   GLN A 193    24090  34643  24493  -1700    483  -2386
ATOM   1439  CB  GLN A 193     -20.152  11.002 -45.035  1.00222.90           C  
ANISOU 1439  CB  GLN A 193    24359  35666  24668  -2047    553  -2522
ATOM   1440  CG  GLN A 193     -21.015  12.202 -45.380  1.00224.08           C  
ANISOU 1440  CG  GLN A 193    24377  36031  24733  -1894    516  -2543
ATOM   1441  CD  GLN A 193     -22.112  12.435 -44.359  1.00224.66           C  
ANISOU 1441  CD  GLN A 193    24372  36235  24754  -1848    522  -2567
ATOM   1442  OE1 GLN A 193     -22.212  11.716 -43.364  1.00224.24           O  
ANISOU 1442  OE1 GLN A 193    24368  36101  24732  -1941    557  -2552
ATOM   1443  NE2 GLN A 193     -22.938  13.446 -44.598  1.00225.22           N  
ANISOU 1443  NE2 GLN A 193    24308  36535  24729  -1707    487  -2611
ATOM   1444  N   PHE A 198     -15.028  10.738 -38.234  1.00193.99           N  
ANISOU 1444  N   PHE A 198    21424  30441  21845  -1640    526  -2065
ATOM   1445  CA  PHE A 198     -14.827   9.337 -37.873  1.00194.71           C  
ANISOU 1445  CA  PHE A 198    21564  30523  21894  -1852    564  -2079
ATOM   1446  C   PHE A 198     -14.601   8.410 -39.078  1.00195.86           C  
ANISOU 1446  C   PHE A 198    21691  30761  21966  -1992    582  -2160
ATOM   1447  O   PHE A 198     -15.328   7.436 -39.262  1.00199.08           O  
ANISOU 1447  O   PHE A 198    22056  31341  22243  -2212    624  -2235
ATOM   1448  CB  PHE A 198     -16.018   8.852 -37.029  1.00196.85           C  
ANISOU 1448  CB  PHE A 198    21781  30952  22060  -2005    604  -2107
ATOM   1449  CG  PHE A 198     -17.369   9.118 -37.653  1.00199.36           C  
ANISOU 1449  CG  PHE A 198    21958  31536  22254  -2032    616  -2186
ATOM   1450  CD1 PHE A 198     -18.012  10.328 -37.439  1.00199.00           C  
ANISOU 1450  CD1 PHE A 198    21834  31557  22220  -1851    593  -2191
ATOM   1451  CD2 PHE A 198     -18.012   8.155 -38.416  1.00201.57           C  
ANISOU 1451  CD2 PHE A 198    22179  32022  22385  -2253    651  -2264
ATOM   1452  CE1 PHE A 198     -19.251  10.583 -37.996  1.00200.79           C  
ANISOU 1452  CE1 PHE A 198    21920  32055  22317  -1867    600  -2270
ATOM   1453  CE2 PHE A 198     -19.253   8.405 -38.976  1.00203.17           C  
ANISOU 1453  CE2 PHE A 198    22245  32493  22456  -2289    660  -2329
ATOM   1454  CZ  PHE A 198     -19.873   9.619 -38.764  1.00203.01           C  
ANISOU 1454  CZ  PHE A 198    22141  32543  22451  -2087    634  -2331
ATOM   1455  N   PRO A 199     -13.568   8.689 -39.882  1.00196.42           N  
ANISOU 1455  N   PRO A 199    21793  30734  22104  -1886    552  -2151
ATOM   1456  CA  PRO A 199     -13.334   7.843 -41.063  1.00197.24           C  
ANISOU 1456  CA  PRO A 199    21862  30953  22127  -2019    572  -2253
ATOM   1457  C   PRO A 199     -12.755   6.481 -40.722  1.00197.05           C  
ANISOU 1457  C   PRO A 199    21899  30901  22071  -2205    606  -2304
ATOM   1458  O   PRO A 199     -13.045   5.505 -41.425  1.00197.83           O  
ANISOU 1458  O   PRO A 199    21957  31164  22047  -2415    647  -2427
ATOM   1459  CB  PRO A 199     -12.354   8.678 -41.898  1.00195.93           C  
ANISOU 1459  CB  PRO A 199    21705  30700  22040  -1835    528  -2219
ATOM   1460  CG  PRO A 199     -11.597   9.460 -40.885  1.00194.06           C  
ANISOU 1460  CG  PRO A 199    21561  30235  21939  -1663    493  -2090
ATOM   1461  CD  PRO A 199     -12.568   9.768 -39.775  1.00194.27           C  
ANISOU 1461  CD  PRO A 199    21581  30270  21962  -1665    504  -2056
ATOM   1462  N   LEU A 200     -11.950   6.384 -39.665  1.00189.90           N  
ANISOU 1462  N   LEU A 200    21090  29809  21256  -2155    594  -2223
ATOM   1463  CA  LEU A 200     -11.299   5.139 -39.277  1.00190.36           C  
ANISOU 1463  CA  LEU A 200    21211  29841  21274  -2325    624  -2273
ATOM   1464  C   LEU A 200     -12.212   4.207 -38.488  1.00191.85           C  
ANISOU 1464  C   LEU A 200    21422  30134  21340  -2590    674  -2295
ATOM   1465  O   LEU A 200     -11.715   3.260 -37.871  1.00191.82           O  
ANISOU 1465  O   LEU A 200    21498  30090  21296  -2750    698  -2307
ATOM   1466  CB  LEU A 200     -10.042   5.442 -38.454  1.00188.25           C  
ANISOU 1466  CB  LEU A 200    21039  29353  21135  -2175    587  -2164
ATOM   1467  CG  LEU A 200      -8.904   6.184 -39.159  1.00186.70           C  
ANISOU 1467  CG  LEU A 200    20841  29058  21039  -1957    538  -2132
ATOM   1468  CD1 LEU A 200      -7.809   6.542 -38.168  1.00184.78           C  
ANISOU 1468  CD1 LEU A 200    20695  28610  20903  -1836    505  -2002
ATOM   1469  CD2 LEU A 200      -8.341   5.356 -40.302  1.00188.82           C  
ANISOU 1469  CD2 LEU A 200    21053  29448  21242  -2030    554  -2287
ATOM   1470  N   LYS A 201     -13.524   4.451 -38.495  1.00189.31           N  
ANISOU 1470  N   LYS A 201    21032  29960  20939  -2654    690  -2298
ATOM   1471  CA  LYS A 201     -14.437   3.667 -37.668  1.00190.89           C  
ANISOU 1471  CA  LYS A 201    21251  30273  21006  -2910    733  -2294
ATOM   1472  C   LYS A 201     -14.530   2.223 -38.154  1.00193.11           C  
ANISOU 1472  C   LYS A 201    21565  30694  21115  -3257    788  -2411
ATOM   1473  O   LYS A 201     -14.341   1.281 -37.374  1.00192.96           O  
ANISOU 1473  O   LYS A 201    21675  30618  21024  -3469    797  -2392
ATOM   1474  CB  LYS A 201     -15.816   4.327 -37.656  1.00192.01           C  
ANISOU 1474  CB  LYS A 201    21285  30579  21090  -2882    735  -2284
ATOM   1475  CG  LYS A 201     -16.836   3.648 -36.761  1.00194.59           C  
ANISOU 1475  CG  LYS A 201    21613  31054  21268  -3135    774  -2267
ATOM   1476  CD  LYS A 201     -18.137   4.434 -36.732  1.00196.42           C  
ANISOU 1476  CD  LYS A 201    21712  31471  21450  -3060    772  -2269
ATOM   1477  CE  LYS A 201     -19.219   3.696 -35.961  1.00199.00           C  
ANISOU 1477  CE  LYS A 201    22019  31999  21594  -3339    811  -2259
ATOM   1478  NZ  LYS A 201     -18.890   3.584 -34.513  1.00198.16           N1+
ANISOU 1478  NZ  LYS A 201    22000  31765  21528  -3357    812  -2168
ATOM   1479  N   PHE A 202     -14.826   2.032 -39.442  1.00190.03           N  
ANISOU 1479  N   PHE A 202    21111  30443  20648  -3327    799  -2527
ATOM   1480  CA  PHE A 202     -14.949   0.685 -39.994  1.00193.21           C  
ANISOU 1480  CA  PHE A 202    21812  30661  20937  -3520    667  -2612
ATOM   1481  C   PHE A 202     -13.637  -0.080 -39.859  1.00192.72           C  
ANISOU 1481  C   PHE A 202    22049  30222  20952  -3433    538  -2641
ATOM   1482  O   PHE A 202     -13.622  -1.253 -39.465  1.00193.64           O  
ANISOU 1482  O   PHE A 202    22454  30130  20992  -3599    425  -2662
ATOM   1483  CB  PHE A 202     -15.382   0.767 -41.459  1.00194.63           C  
ANISOU 1483  CB  PHE A 202    21957  30939  21053  -3523    636  -2717
ATOM   1484  CG  PHE A 202     -15.653  -0.567 -42.095  1.00197.56           C  
ANISOU 1484  CG  PHE A 202    22635  31141  21286  -3738    497  -2821
ATOM   1485  CD1 PHE A 202     -16.845  -1.233 -41.859  1.00200.00           C  
ANISOU 1485  CD1 PHE A 202    22991  31574  21424  -4038    485  -2809
ATOM   1486  CD2 PHE A 202     -14.717  -1.156 -42.930  1.00197.78           C  
ANISOU 1486  CD2 PHE A 202    22913  30892  21340  -3642    372  -2940
ATOM   1487  CE1 PHE A 202     -17.101  -2.457 -42.448  1.00202.73           C  
ANISOU 1487  CE1 PHE A 202    23643  31745  21640  -4249    335  -2906
ATOM   1488  CE2 PHE A 202     -14.966  -2.383 -43.518  1.00200.41           C  
ANISOU 1488  CE2 PHE A 202    23561  31045  21539  -3825    230  -3062
ATOM   1489  CZ  PHE A 202     -16.159  -3.034 -43.275  1.00202.93           C  
ANISOU 1489  CZ  PHE A 202    23939  31463  21701  -4134    203  -3042
ATOM   1490  N   TYR A 203     -12.522   0.578 -40.185  1.00186.24           N  
ANISOU 1490  N   TYR A 203    21170  29318  20275  -3169    538  -2642
ATOM   1491  CA  TYR A 203     -11.206  -0.035 -40.035  1.00185.04           C  
ANISOU 1491  CA  TYR A 203    21271  28844  20190  -3047    424  -2671
ATOM   1492  C   TYR A 203     -10.940  -0.450 -38.595  1.00183.65           C  
ANISOU 1492  C   TYR A 203    21215  28534  20028  -3121    405  -2565
ATOM   1493  O   TYR A 203     -10.420  -1.543 -38.341  1.00183.85           O  
ANISOU 1493  O   TYR A 203    21561  28274  20020  -3166    261  -2610
ATOM   1494  CB  TYR A 203     -10.134   0.942 -40.514  1.00182.24           C  
ANISOU 1494  CB  TYR A 203    20762  28506  19975  -2769    454  -2655
ATOM   1495  CG  TYR A 203      -8.709   0.481 -40.314  1.00181.27           C  
ANISOU 1495  CG  TYR A 203    20849  28108  19917  -2611    355  -2674
ATOM   1496  CD1 TYR A 203      -8.139  -0.474 -41.146  1.00182.99           C  
ANISOU 1496  CD1 TYR A 203    21343  28113  20072  -2566    228  -2833
ATOM   1497  CD2 TYR A 203      -7.927   1.016 -39.298  1.00179.20           C  
ANISOU 1497  CD2 TYR A 203    20515  27808  19764  -2499    388  -2541
ATOM   1498  CE1 TYR A 203      -6.831  -0.888 -40.964  1.00181.91           C  
ANISOU 1498  CE1 TYR A 203    21396  27744  19977  -2394    139  -2866
ATOM   1499  CE2 TYR A 203      -6.623   0.609 -39.109  1.00178.55           C  
ANISOU 1499  CE2 TYR A 203    20615  27500  19727  -2352    294  -2552
ATOM   1500  CZ  TYR A 203      -6.079  -0.343 -39.943  1.00179.86           C  
ANISOU 1500  CZ  TYR A 203    21043  27469  19826  -2290    171  -2718
ATOM   1501  OH  TYR A 203      -4.777  -0.747 -39.753  1.00179.29           O  
ANISOU 1501  OH  TYR A 203    21152  27189  19780  -2119     80  -2745
ATOM   1502  N   GLN A 204     -11.289   0.410 -37.638  1.00186.54           N  
ANISOU 1502  N   GLN A 204    21344  29098  20435  -3133    539  -2432
ATOM   1503  CA  GLN A 204     -10.993   0.123 -36.238  1.00186.25           C  
ANISOU 1503  CA  GLN A 204    21405  28959  20404  -3212    534  -2315
ATOM   1504  C   GLN A 204     -11.845  -1.028 -35.718  1.00189.23           C  
ANISOU 1504  C   GLN A 204    21985  29292  20622  -3517    470  -2312
ATOM   1505  O   GLN A 204     -11.331  -1.954 -35.079  1.00189.88           O  
ANISOU 1505  O   GLN A 204    22348  29115  20684  -3595    338  -2286
ATOM   1506  CB  GLN A 204     -11.205   1.381 -35.396  1.00184.09           C  
ANISOU 1506  CB  GLN A 204    20827  28925  20195  -3152    699  -2194
ATOM   1507  CG  GLN A 204     -10.832   1.236 -33.934  1.00183.51           C  
ANISOU 1507  CG  GLN A 204    20833  28769  20122  -3232    711  -2061
ATOM   1508  CD  GLN A 204     -10.981   2.537 -33.172  1.00181.64           C  
ANISOU 1508  CD  GLN A 204    20546  28451  20019  -2987    690  -1931
ATOM   1509  OE1 GLN A 204     -11.391   3.554 -33.732  1.00180.11           O  
ANISOU 1509  OE1 GLN A 204    20255  28270  19907  -2773    673  -1942
ATOM   1510  NE2 GLN A 204     -10.649   2.513 -31.886  1.00181.17           N  
ANISOU 1510  NE2 GLN A 204    20579  28286  19972  -3028    677  -1810
ATOM   1511  N   GLU A 205     -13.151  -0.993 -35.990  1.00185.59           N  
ANISOU 1511  N   GLU A 205    21390  29086  20040  -3700    544  -2333
ATOM   1512  CA  GLU A 205     -14.043  -2.018 -35.456  1.00188.21           C  
ANISOU 1512  CA  GLU A 205    21885  29426  20202  -4027    490  -2306
ATOM   1513  C   GLU A 205     -13.813  -3.363 -36.135  1.00190.21           C  
ANISOU 1513  C   GLU A 205    22512  29359  20400  -4119    268  -2423
ATOM   1514  O   GLU A 205     -13.688  -4.395 -35.465  1.00191.45           O  
ANISOU 1514  O   GLU A 205    22949  29294  20501  -4289    123  -2391
ATOM   1515  CB  GLU A 205     -15.499  -1.582 -35.616  1.00189.31           C  
ANISOU 1515  CB  GLU A 205    21760  29962  20207  -4191    631  -2301
ATOM   1516  CG  GLU A 205     -15.891  -0.388 -34.763  1.00187.29           C  
ANISOU 1516  CG  GLU A 205    21163  30027  19971  -4126    833  -2211
ATOM   1517  CD  GLU A 205     -17.340   0.010 -34.960  1.00189.92           C  
ANISOU 1517  CD  GLU A 205    21327  30635  20198  -4179    873  -2223
ATOM   1518  OE1 GLU A 205     -17.999  -0.565 -35.852  1.00192.51           O  
ANISOU 1518  OE1 GLU A 205    21637  31135  20373  -4401    891  -2304
ATOM   1519  OE2 GLU A 205     -17.819   0.897 -34.224  1.00189.80           O1-
ANISOU 1519  OE2 GLU A 205    21232  30626  20257  -3982    855  -2155
ATOM   1520  N   ILE A 206     -13.754  -3.372 -37.468  1.00186.05           N  
ANISOU 1520  N   ILE A 206    22008  28799  19884  -4012    224  -2565
ATOM   1521  CA  ILE A 206     -13.709  -4.636 -38.194  1.00189.37           C  
ANISOU 1521  CA  ILE A 206    22786  28941  20226  -4114     16  -2709
ATOM   1522  C   ILE A 206     -12.343  -5.300 -38.078  1.00188.60           C  
ANISOU 1522  C   ILE A 206    23005  28434  20221  -3928   -161  -2784
ATOM   1523  O   ILE A 206     -12.250  -6.533 -38.009  1.00190.13           O  
ANISOU 1523  O   ILE A 206    23553  28329  20359  -4047   -372  -2868
ATOM   1524  CB  ILE A 206     -14.100  -4.406 -39.666  1.00191.43           C  
ANISOU 1524  CB  ILE A 206    22973  29318  20444  -4069     36  -2842
ATOM   1525  CG1 ILE A 206     -15.519  -3.844 -39.750  1.00193.36           C  
ANISOU 1525  CG1 ILE A 206    22922  29968  20578  -4265    182  -2773
ATOM   1526  CG2 ILE A 206     -13.988  -5.695 -40.468  1.00195.42           C  
ANISOU 1526  CG2 ILE A 206    23873  29516  20862  -4155   -181  -3020
ATOM   1527  CD1 ILE A 206     -16.576  -4.767 -39.184  1.00197.66           C  
ANISOU 1527  CD1 ILE A 206    23595  30560  20948  -4634    121  -2722
ATOM   1528  N   PHE A 207     -11.275  -4.521 -38.037  1.00184.68           N  
ANISOU 1528  N   PHE A 207    22391  27915  19865  -3638    -97  -2760
ATOM   1529  CA  PHE A 207      -9.959  -5.116 -38.243  1.00185.17           C  
ANISOU 1529  CA  PHE A 207    22740  27624  19992  -3421   -263  -2872
ATOM   1530  C   PHE A 207      -8.966  -4.836 -37.124  1.00182.05           C  
ANISOU 1530  C   PHE A 207    22338  27126  19705  -3289   -268  -2744
ATOM   1531  O   PHE A 207      -8.149  -5.705 -36.812  1.00181.62           O  
ANISOU 1531  O   PHE A 207    22594  26745  19670  -3222   -462  -2807
ATOM   1532  CB  PHE A 207      -9.393  -4.615 -39.581  1.00184.60           C  
ANISOU 1532  CB  PHE A 207    22593  27593  19955  -3178   -218  -3005
ATOM   1533  CG  PHE A 207      -8.085  -5.242 -39.962  1.00184.18           C  
ANISOU 1533  CG  PHE A 207    22836  27217  19928  -2941   -369  -3156
ATOM   1534  CD1 PHE A 207      -8.043  -6.525 -40.478  1.00187.51           C  
ANISOU 1534  CD1 PHE A 207    23660  27332  20254  -2976   -571  -3363
ATOM   1535  CD2 PHE A 207      -6.899  -4.548 -39.808  1.00180.96           C  
ANISOU 1535  CD2 PHE A 207    22312  26815  19630  -2679   -312  -3102
ATOM   1536  CE1 PHE A 207      -6.841  -7.105 -40.833  1.00187.40           C  
ANISOU 1536  CE1 PHE A 207    23937  27021  20246  -2726   -702  -3532
ATOM   1537  CE2 PHE A 207      -5.696  -5.123 -40.160  1.00181.58           C  
ANISOU 1537  CE2 PHE A 207    22656  26629  19706  -2453   -434  -3246
ATOM   1538  CZ  PHE A 207      -5.665  -6.402 -40.673  1.00184.08           C  
ANISOU 1538  CZ  PHE A 207    23385  26638  19918  -2464   -622  -3471
ATOM   1539  N   GLU A 208      -9.012  -3.652 -36.511  1.00181.38           N  
ANISOU 1539  N   GLU A 208    21921  27302  19693  -3247    -75  -2576
ATOM   1540  CA  GLU A 208      -7.931  -3.258 -35.614  1.00178.75           C  
ANISOU 1540  CA  GLU A 208    21572  26881  19465  -3094    -73  -2459
ATOM   1541  C   GLU A 208      -8.026  -3.954 -34.259  1.00179.28           C  
ANISOU 1541  C   GLU A 208    21815  26811  19492  -3294   -168  -2341
ATOM   1542  O   GLU A 208      -6.997  -4.293 -33.663  1.00179.22           O  
ANISOU 1542  O   GLU A 208    21980  26573  19541  -3194   -295  -2307
ATOM   1543  CB  GLU A 208      -7.919  -1.738 -35.445  1.00176.13           C  
ANISOU 1543  CB  GLU A 208    20846  26849  19225  -2979    145  -2335
ATOM   1544  CG  GLU A 208      -6.729  -1.208 -34.660  1.00173.96           C  
ANISOU 1544  CG  GLU A 208    20539  26498  19059  -2812    152  -2215
ATOM   1545  CD  GLU A 208      -6.667   0.308 -34.644  1.00171.36           C  
ANISOU 1545  CD  GLU A 208    19847  26429  18831  -2683    333  -2119
ATOM   1546  OE1 GLU A 208      -7.569   0.949 -35.224  1.00171.82           O  
ANISOU 1546  OE1 GLU A 208    19677  26725  18880  -2710    445  -2152
ATOM   1547  OE2 GLU A 208      -5.710   0.859 -34.061  1.00168.65           O1-
ANISOU 1547  OE2 GLU A 208    19459  26046  18574  -2555    345  -2014
ATOM   1548  N   SER A 209      -9.243  -4.182 -33.756  1.00169.27           N  
ANISOU 1548  N   SER A 209    20502  25699  18116  -3589   -114  -2270
ATOM   1549  CA  SER A 209      -9.374  -4.901 -32.490  1.00170.37           C  
ANISOU 1549  CA  SER A 209    20812  25723  18198  -3822   -212  -2144
ATOM   1550  C   SER A 209      -9.016  -6.378 -32.626  1.00172.91           C  
ANISOU 1550  C   SER A 209    21543  25647  18506  -3883   -518  -2263
ATOM   1551  O   SER A 209      -8.231  -6.877 -31.801  1.00172.88           O  
ANISOU 1551  O   SER A 209    21725  25403  18560  -3870   -679  -2202
ATOM   1552  CB  SER A 209     -10.781  -4.704 -31.916  1.00171.67           C  
ANISOU 1552  CB  SER A 209    20796  26209  18222  -4131    -54  -2031
ATOM   1553  OG  SER A 209     -11.008  -3.348 -31.577  1.00170.25           O  
ANISOU 1553  OG  SER A 209    20256  26360  18073  -4048    200  -1937
ATOM   1554  N   PRO A 210      -9.535  -7.128 -33.610  1.00173.46           N  
ANISOU 1554  N   PRO A 210    21775  25619  18512  -3950   -630  -2438
ATOM   1555  CA  PRO A 210      -9.137  -8.547 -33.707  1.00176.95           C  
ANISOU 1555  CA  PRO A 210    22625  25641  18967  -3986   -950  -2585
ATOM   1556  C   PRO A 210      -7.653  -8.734 -33.967  1.00176.18           C  
ANISOU 1556  C   PRO A 210    22707  25234  18998  -3635  -1109  -2722
ATOM   1557  O   PRO A 210      -7.017  -9.586 -33.332  1.00178.26           O  
ANISOU 1557  O   PRO A 210    23216  25178  19334  -3634  -1353  -2750
ATOM   1558  CB  PRO A 210      -9.995  -9.070 -34.868  1.00180.47           C  
ANISOU 1558  CB  PRO A 210    23165  26094  19311  -4096   -990  -2761
ATOM   1559  CG  PRO A 210     -11.146  -8.135 -34.947  1.00180.28           C  
ANISOU 1559  CG  PRO A 210    22787  26523  19190  -4257   -714  -2632
ATOM   1560  CD  PRO A 210     -10.581  -6.797 -34.595  1.00175.36           C  
ANISOU 1560  CD  PRO A 210    21849  26118  18663  -4031   -493  -2511
ATOM   1561  N   PHE A 211      -7.083  -7.964 -34.896  1.00170.52           N  
ANISOU 1561  N   PHE A 211    21863  24617  18311  -3345   -981  -2811
ATOM   1562  CA  PHE A 211      -5.646  -8.038 -35.138  1.00169.77           C  
ANISOU 1562  CA  PHE A 211    21916  24288  18300  -3008  -1095  -2922
ATOM   1563  C   PHE A 211      -4.862  -7.643 -33.893  1.00167.18           C  
ANISOU 1563  C   PHE A 211    21508  23950  18063  -2961  -1101  -2723
ATOM   1564  O   PHE A 211      -3.831  -8.250 -33.577  1.00167.06           O  
ANISOU 1564  O   PHE A 211    21721  23638  18118  -2808  -1323  -2795
ATOM   1565  CB  PHE A 211      -5.267  -7.140 -36.315  1.00167.85           C  
ANISOU 1565  CB  PHE A 211    21489  24236  18048  -2761   -905  -2998
ATOM   1566  CG  PHE A 211      -3.814  -7.201 -36.680  1.00166.62           C  
ANISOU 1566  CG  PHE A 211    21482  23893  17932  -2428   -983  -3112
ATOM   1567  CD1 PHE A 211      -3.317  -8.257 -37.424  1.00169.64           C  
ANISOU 1567  CD1 PHE A 211    22251  23943  18260  -2282  -1181  -3384
ATOM   1568  CD2 PHE A 211      -2.941  -6.209 -36.270  1.00163.24           C  
ANISOU 1568  CD2 PHE A 211    20820  23623  17582  -2262   -851  -2955
ATOM   1569  CE1 PHE A 211      -1.979  -8.317 -37.760  1.00169.92           C  
ANISOU 1569  CE1 PHE A 211    22386  23908  18268  -2034  -1176  -3533
ATOM   1570  CE2 PHE A 211      -1.602  -6.266 -36.600  1.00163.04           C  
ANISOU 1570  CE2 PHE A 211    20918  23466  17566  -1974   -903  -3045
ATOM   1571  CZ  PHE A 211      -1.121  -7.320 -37.347  1.00166.57           C  
ANISOU 1571  CZ  PHE A 211    21702  23674  17914  -1875  -1038  -3348
ATOM   1572  N   LEU A 212      -5.345  -6.632 -33.169  1.00169.14           N  
ANISOU 1572  N   LEU A 212    21438  24518  18310  -3091   -867  -2486
ATOM   1573  CA  LEU A 212      -4.657  -6.158 -31.974  1.00166.53           C  
ANISOU 1573  CA  LEU A 212    21020  24207  18047  -3070   -844  -2280
ATOM   1574  C   LEU A 212      -4.596  -7.247 -30.908  1.00168.69           C  
ANISOU 1574  C   LEU A 212    21542  24215  18336  -3268  -1093  -2222
ATOM   1575  O   LEU A 212      -3.513  -7.626 -30.444  1.00168.81           O  
ANISOU 1575  O   LEU A 212    21703  23992  18444  -3133  -1289  -2225
ATOM   1576  CB  LEU A 212      -5.361  -4.909 -31.439  1.00163.98           C  
ANISOU 1576  CB  LEU A 212    20334  24272  17701  -3190   -539  -2075
ATOM   1577  CG  LEU A 212      -4.735  -4.183 -30.249  1.00161.92           C  
ANISOU 1577  CG  LEU A 212    19945  24085  17491  -3177   -457  -1854
ATOM   1578  CD1 LEU A 212      -3.377  -3.613 -30.625  1.00159.47           C  
ANISOU 1578  CD1 LEU A 212    19592  23719  17282  -2853   -468  -1875
ATOM   1579  CD2 LEU A 212      -5.661  -3.086 -29.746  1.00161.01           C  
ANISOU 1579  CD2 LEU A 212    19510  24333  17332  -3321   -172  -1707
ATOM   1580  N   THR A 213      -5.760  -7.773 -30.514  1.00164.72           N  
ANISOU 1580  N   THR A 213    21077  23765  17746  -3604  -1097  -2163
ATOM   1581  CA  THR A 213      -5.788  -8.784 -29.461  1.00167.01           C  
ANISOU 1581  CA  THR A 213    21573  23830  18053  -3851  -1320  -2071
ATOM   1582  C   THR A 213      -5.158 -10.095 -29.916  1.00170.45           C  
ANISOU 1582  C   THR A 213    22344  23855  18565  -3803  -1658  -2321
ATOM   1583  O   THR A 213      -4.610 -10.836 -29.090  1.00172.91           O  
ANISOU 1583  O   THR A 213    22825  23968  18905  -4002  -1853  -2266
ATOM   1584  CB  THR A 213      -7.223  -9.025 -28.995  1.00168.83           C  
ANISOU 1584  CB  THR A 213    21761  24258  18127  -4260  -1222  -1937
ATOM   1585  OG1 THR A 213      -8.013  -9.498 -30.094  1.00171.55           O  
ANISOU 1585  OG1 THR A 213    22181  24595  18405  -4314  -1251  -2129
ATOM   1586  CG2 THR A 213      -7.831  -7.738 -28.454  1.00166.45           C  
ANISOU 1586  CG2 THR A 213    21121  24398  17724  -4342   -873  -1731
ATOM   1587  N   GLU A 214      -5.215 -10.398 -31.215  1.00166.90           N  
ANISOU 1587  N   GLU A 214    22006  23321  18089  -3652  -1699  -2598
ATOM   1588  CA  GLU A 214      -4.666 -11.661 -31.691  1.00171.53           C  
ANISOU 1588  CA  GLU A 214    22940  23560  18676  -3708  -1965  -2895
ATOM   1589  C   GLU A 214      -3.144 -11.621 -31.761  1.00171.15           C  
ANISOU 1589  C   GLU A 214    22973  23382  18674  -3467  -2047  -3038
ATOM   1590  O   GLU A 214      -2.483 -12.614 -31.438  1.00174.62           O  
ANISOU 1590  O   GLU A 214    23687  23501  19158  -3603  -2288  -3173
ATOM   1591  CB  GLU A 214      -5.255 -12.019 -33.054  1.00173.83           C  
ANISOU 1591  CB  GLU A 214    23349  23802  18898  -3630  -1968  -3160
ATOM   1592  CG  GLU A 214      -4.837 -13.394 -33.540  1.00179.57           C  
ANISOU 1592  CG  GLU A 214    24478  24123  19628  -3709  -2229  -3506
ATOM   1593  CD  GLU A 214      -5.499 -13.775 -34.841  1.00181.98           C  
ANISOU 1593  CD  GLU A 214    24913  24382  19849  -3659  -2229  -3756
ATOM   1594  OE1 GLU A 214      -6.252 -12.943 -35.386  1.00179.13           O  
ANISOU 1594  OE1 GLU A 214    24317  24316  19428  -3572  -2036  -3638
ATOM   1595  OE2 GLU A 214      -5.273 -14.909 -35.309  1.00186.43           O1-
ANISOU 1595  OE2 GLU A 214    25826  24591  20418  -3722  -2422  -4070
ATOM   1596  N   THR A 215      -2.568 -10.492 -32.185  1.00165.55           N  
ANISOU 1596  N   THR A 215    22043  22902  17956  -3134  -1850  -2999
ATOM   1597  CA  THR A 215      -1.122 -10.341 -32.057  1.00165.22           C  
ANISOU 1597  CA  THR A 215    22024  22823  17929  -2940  -1900  -3072
ATOM   1598  C   THR A 215      -0.710 -10.232 -30.594  1.00163.72           C  
ANISOU 1598  C   THR A 215    21750  22646  17811  -3132  -1979  -2780
ATOM   1599  O   THR A 215       0.411 -10.612 -30.236  1.00164.86           O  
ANISOU 1599  O   THR A 215    22011  22653  17977  -3129  -2148  -2842
ATOM   1600  CB  THR A 215      -0.632  -9.125 -32.844  1.00161.24           C  
ANISOU 1600  CB  THR A 215    21285  22588  17392  -2580  -1646  -3046
ATOM   1601  OG1 THR A 215      -1.293  -7.945 -32.371  1.00156.78           O  
ANISOU 1601  OG1 THR A 215    20406  22275  16887  -2585  -1429  -2711
ATOM   1602  CG2 THR A 215      -0.898  -9.305 -34.333  1.00161.64           C  
ANISOU 1602  CG2 THR A 215    21448  22606  17359  -2412  -1574  -3316
ATOM   1603  N   GLY A 216      -1.603  -9.728 -29.738  1.00158.36           N  
ANISOU 1603  N   GLY A 216    20885  22128  17155  -3310  -1853  -2463
ATOM   1604  CA  GLY A 216      -1.336  -9.759 -28.308  1.00158.42           C  
ANISOU 1604  CA  GLY A 216    20863  22121  17210  -3542  -1925  -2168
ATOM   1605  C   GLY A 216      -1.188 -11.174 -27.781  1.00163.51           C  
ANISOU 1605  C   GLY A 216    21834  22406  17888  -3887  -2245  -2199
ATOM   1606  O   GLY A 216      -0.230 -11.490 -27.070  1.00165.08           O  
ANISOU 1606  O   GLY A 216    22135  22441  18148  -3987  -2436  -2086
ATOM   1607  N   GLU A 217      -2.142 -12.047 -28.121  1.00159.97           N  
ANISOU 1607  N   GLU A 217    21573  21795  17411  -4099  -2327  -2317
ATOM   1608  CA  GLU A 217      -2.011 -13.460 -27.774  1.00165.21           C  
ANISOU 1608  CA  GLU A 217    22623  22018  18132  -4432  -2650  -2354
ATOM   1609  C   GLU A 217      -0.764 -14.068 -28.403  1.00167.88           C  
ANISOU 1609  C   GLU A 217    23251  21994  18544  -4272  -2872  -2671
ATOM   1610  O   GLU A 217      -0.060 -14.861 -27.765  1.00171.84           O  
ANISOU 1610  O   GLU A 217    24054  22078  19159  -4471  -3170  -2571
ATOM   1611  CB  GLU A 217      -3.258 -14.229 -28.214  1.00168.85           C  
ANISOU 1611  CB  GLU A 217    23238  22385  18534  -4655  -2679  -2451
ATOM   1612  CG  GLU A 217      -4.498 -13.941 -27.387  1.00168.29           C  
ANISOU 1612  CG  GLU A 217    22985  22590  18368  -4923  -2528  -2120
ATOM   1613  CD  GLU A 217      -4.401 -14.508 -25.984  1.00170.76           C  
ANISOU 1613  CD  GLU A 217    23440  22743  18697  -5303  -2696  -1772
ATOM   1614  OE1 GLU A 217      -3.761 -15.567 -25.813  1.00175.50           O  
ANISOU 1614  OE1 GLU A 217    24397  22887  19400  -5477  -3014  -1794
ATOM   1615  OE2 GLU A 217      -4.962 -13.896 -25.051  1.00168.27           O1-
ANISOU 1615  OE2 GLU A 217    22913  22730  18292  -5424  -2517  -1468
ATOM   1616  N   TYR A 218      -0.478 -13.707 -29.657  1.00155.69           N  
ANISOU 1616  N   TYR A 218    21658  20561  16936  -3903  -2739  -3033
ATOM   1617  CA  TYR A 218       0.686 -14.247 -30.352  1.00159.10           C  
ANISOU 1617  CA  TYR A 218    22399  20663  17389  -3700  -2889  -3408
ATOM   1618  C   TYR A 218       1.974 -13.946 -29.594  1.00158.74           C  
ANISOU 1618  C   TYR A 218    22345  20576  17393  -3662  -3023  -3230
ATOM   1619  O   TYR A 218       2.812 -14.833 -29.394  1.00162.94           O  
ANISOU 1619  O   TYR A 218    23241  20537  18132  -3593  -3291  -3237
ATOM   1620  CB  TYR A 218       0.748 -13.681 -31.771  1.00157.42           C  
ANISOU 1620  CB  TYR A 218    22058  20705  17051  -3274  -2643  -3769
ATOM   1621  CG  TYR A 218       1.932 -14.159 -32.580  1.00160.95           C  
ANISOU 1621  CG  TYR A 218    22815  20873  17467  -2992  -2688  -4232
ATOM   1622  CD1 TYR A 218       1.965 -15.441 -33.111  1.00167.31           C  
ANISOU 1622  CD1 TYR A 218    24163  21066  18341  -3019  -2870  -4588
ATOM   1623  CD2 TYR A 218       3.015 -13.324 -32.819  1.00159.06           C  
ANISOU 1623  CD2 TYR A 218    22311  20954  17171  -2618  -2498  -4290
ATOM   1624  CE1 TYR A 218       3.046 -15.879 -33.854  1.00171.46           C  
ANISOU 1624  CE1 TYR A 218    24813  21258  19077  -2402  -2775  -4851
ATOM   1625  CE2 TYR A 218       4.099 -13.752 -33.560  1.00163.09           C  
ANISOU 1625  CE2 TYR A 218    22881  21178  17907  -1996  -2389  -4505
ATOM   1626  CZ  TYR A 218       4.110 -15.030 -34.075  1.00169.20           C  
ANISOU 1626  CZ  TYR A 218    24114  21323  18852  -1871  -2517  -4798
ATOM   1627  OH  TYR A 218       5.189 -15.460 -34.813  1.00174.30           O  
ANISOU 1627  OH  TYR A 218    24808  21699  19719  -1216  -2390  -5042
ATOM   1628  N   TYR A 219       2.145 -12.699 -29.152  1.00155.91           N  
ANISOU 1628  N   TYR A 219    21529  20730  16979  -3534  -2807  -2960
ATOM   1629  CA  TYR A 219       3.373 -12.325 -28.463  1.00154.84           C  
ANISOU 1629  CA  TYR A 219    21321  20643  16869  -3499  -2935  -2751
ATOM   1630  C   TYR A 219       3.354 -12.640 -26.973  1.00155.62           C  
ANISOU 1630  C   TYR A 219    21472  20541  17115  -3876  -3172  -2259
ATOM   1631  O   TYR A 219       4.415 -12.599 -26.340  1.00156.66           O  
ANISOU 1631  O   TYR A 219    21542  20537  17445  -3715  -3284  -1966
ATOM   1632  CB  TYR A 219       3.674 -10.843 -28.693  1.00149.22           C  
ANISOU 1632  CB  TYR A 219    20112  20532  16053  -3156  -2594  -2664
ATOM   1633  CG  TYR A 219       4.183 -10.568 -30.091  1.00149.06           C  
ANISOU 1633  CG  TYR A 219    20029  20702  15903  -2738  -2402  -3104
ATOM   1634  CD1 TYR A 219       5.505 -10.829 -30.424  1.00151.88           C  
ANISOU 1634  CD1 TYR A 219    20345  20838  16523  -2180  -2348  -3112
ATOM   1635  CD2 TYR A 219       3.347 -10.063 -31.077  1.00147.02           C  
ANISOU 1635  CD2 TYR A 219    19667  20596  15600  -2530  -2132  -3209
ATOM   1636  CE1 TYR A 219       5.985 -10.588 -31.694  1.00151.92           C  
ANISOU 1636  CE1 TYR A 219    20239  21008  16476  -1698  -2104  -3460
ATOM   1637  CE2 TYR A 219       3.819  -9.819 -32.355  1.00147.36           C  
ANISOU 1637  CE2 TYR A 219    19658  20785  15548  -2149  -1934  -3534
ATOM   1638  CZ  TYR A 219       5.139 -10.084 -32.656  1.00149.36           C  
ANISOU 1638  CZ  TYR A 219    19870  21059  15820  -1806  -1938  -3807
ATOM   1639  OH  TYR A 219       5.620  -9.846 -33.922  1.00149.29           O  
ANISOU 1639  OH  TYR A 219    19755  21234  15734  -1362  -1701  -4144
ATOM   1640  N   LYS A 220       2.194 -12.953 -26.394  1.00155.62           N  
ANISOU 1640  N   LYS A 220    21479  20507  17144  -4169  -3120  -2068
ATOM   1641  CA  LYS A 220       2.193 -13.589 -25.080  1.00158.11           C  
ANISOU 1641  CA  LYS A 220    21961  20528  17585  -4557  -3377  -1654
ATOM   1642  C   LYS A 220       2.713 -15.017 -25.177  1.00164.54           C  
ANISOU 1642  C   LYS A 220    23332  20590  18596  -4706  -3856  -1746
ATOM   1643  O   LYS A 220       3.649 -15.404 -24.462  1.00166.91           O  
ANISOU 1643  O   LYS A 220    23772  20513  19133  -4710  -4159  -1459
ATOM   1644  CB  LYS A 220       0.789 -13.578 -24.477  1.00157.41           C  
ANISOU 1644  CB  LYS A 220    21765  20630  17413  -4821  -3181  -1448
ATOM   1645  CG  LYS A 220       0.725 -14.230 -23.101  1.00160.00           C  
ANISOU 1645  CG  LYS A 220    22267  20715  17812  -5229  -3406  -1008
ATOM   1646  CD  LYS A 220      -0.682 -14.225 -22.526  1.00159.72           C  
ANISOU 1646  CD  LYS A 220    22148  20916  17623  -5488  -3204   -830
ATOM   1647  CE  LYS A 220      -0.720 -14.939 -21.181  1.00162.52           C  
ANISOU 1647  CE  LYS A 220    22707  21045  17998  -5897  -3434   -394
ATOM   1648  NZ  LYS A 220      -2.091 -14.993 -20.599  1.00162.32           N1+
ANISOU 1648  NZ  LYS A 220    22631  21277  17767  -6171  -3253   -226
ATOM   1649  N   GLN A 221       2.118 -15.810 -26.073  1.00154.98           N  
ANISOU 1649  N   GLN A 221    22418  19094  17374  -4704  -3881  -2105
ATOM   1650  CA  GLN A 221       2.521 -17.203 -26.233  1.00161.80           C  
ANISOU 1650  CA  GLN A 221    23878  19115  18485  -4743  -4307  -2222
ATOM   1651  C   GLN A 221       3.986 -17.308 -26.637  1.00163.31           C  
ANISOU 1651  C   GLN A 221    23996  19005  19049  -3952  -4216  -2256
ATOM   1652  O   GLN A 221       4.750 -18.081 -26.048  1.00168.66           O  
ANISOU 1652  O   GLN A 221    24869  19120  20094  -3806  -4474  -1995
ATOM   1653  CB  GLN A 221       1.625 -17.890 -27.265  1.00165.33           C  
ANISOU 1653  CB  GLN A 221    24575  19401  18843  -4760  -4226  -2625
ATOM   1654  CG  GLN A 221       0.159 -17.986 -26.861  1.00164.69           C  
ANISOU 1654  CG  GLN A 221    24302  19657  18615  -5138  -4046  -2410
ATOM   1655  CD  GLN A 221      -0.058 -18.846 -25.631  1.00167.73           C  
ANISOU 1655  CD  GLN A 221    24926  19681  19122  -5569  -4349  -1963
ATOM   1656  OE1 GLN A 221      -0.367 -18.340 -24.552  1.00164.66           O  
ANISOU 1656  OE1 GLN A 221    24249  19660  18654  -5782  -4247  -1550
ATOM   1657  NE2 GLN A 221       0.092 -20.156 -25.791  1.00173.94           N  
ANISOU 1657  NE2 GLN A 221    26265  19727  20099  -5670  -4714  -2044
ATOM   1658  N   GLU A 222       4.402 -16.526 -27.636  1.00152.45           N  
ANISOU 1658  N   GLU A 222    22322  18020  17582  -3439  -3857  -2562
ATOM   1659  CA  GLU A 222       5.798 -16.558 -28.051  1.00158.78           C  
ANISOU 1659  CA  GLU A 222    22992  18634  18701  -2687  -3738  -2599
ATOM   1660  C   GLU A 222       6.706 -15.806 -27.085  1.00156.30           C  
ANISOU 1660  C   GLU A 222    22294  18585  18508  -2574  -3722  -2118
ATOM   1661  O   GLU A 222       7.919 -16.038 -27.087  1.00161.97           O  
ANISOU 1661  O   GLU A 222    22931  19053  19559  -2036  -3729  -2009
ATOM   1662  CB  GLU A 222       5.946 -16.000 -29.471  1.00158.47           C  
ANISOU 1662  CB  GLU A 222    22767  18951  18493  -2213  -3367  -3082
ATOM   1663  CG  GLU A 222       7.338 -16.186 -30.067  1.00165.74           C  
ANISOU 1663  CG  GLU A 222    23578  19672  19722  -1418  -3228  -3201
ATOM   1664  CD  GLU A 222       7.426 -15.748 -31.513  1.00165.35           C  
ANISOU 1664  CD  GLU A 222    23389  19962  19475  -1003  -2875  -3702
ATOM   1665  OE1 GLU A 222       6.406 -15.274 -32.055  1.00159.64           O  
ANISOU 1665  OE1 GLU A 222    22655  19617  18385  -1332  -2752  -3942
ATOM   1666  OE2 GLU A 222       8.514 -15.884 -32.111  1.00171.36           O1-
ANISOU 1666  OE2 GLU A 222    24038  20629  20441   -351  -2725  -3852
ATOM   1667  N   ALA A 223       6.154 -14.921 -26.253  1.00150.96           N  
ANISOU 1667  N   ALA A 223    21380  18413  17564  -3067  -3704  -1831
ATOM   1668  CA  ALA A 223       6.942 -14.352 -25.165  1.00148.67           C  
ANISOU 1668  CA  ALA A 223    20812  18291  17385  -3074  -3760  -1331
ATOM   1669  C   ALA A 223       7.357 -15.438 -24.180  1.00155.36           C  
ANISOU 1669  C   ALA A 223    21952  18491  18587  -3217  -4153   -955
ATOM   1670  O   ALA A 223       8.543 -15.582 -23.853  1.00160.12           O  
ANISOU 1670  O   ALA A 223    22448  18875  19516  -2817  -4227   -693
ATOM   1671  CB  ALA A 223       6.150 -13.253 -24.458  1.00142.08           C  
ANISOU 1671  CB  ALA A 223    19725  18091  16167  -3612  -3675  -1143
ATOM   1672  N   SER A 224       6.387 -16.230 -23.710  1.00151.18           N  
ANISOU 1672  N   SER A 224    21793  17652  17998  -3799  -4428   -909
ATOM   1673  CA  SER A 224       6.712 -17.334 -22.811  1.00157.54           C  
ANISOU 1673  CA  SER A 224    22929  17795  19133  -3981  -4846   -549
ATOM   1674  C   SER A 224       7.531 -18.412 -23.511  1.00168.08           C  
ANISOU 1674  C   SER A 224    24548  18417  20897  -3365  -4961   -752
ATOM   1675  O   SER A 224       8.347 -19.082 -22.868  1.00173.92           O  
ANISOU 1675  O   SER A 224    25411  18652  22018  -3209  -5243   -419
ATOM   1676  CB  SER A 224       5.432 -17.935 -22.229  1.00157.39           C  
ANISOU 1676  CB  SER A 224    23251  17638  18911  -4783  -5117   -470
ATOM   1677  OG  SER A 224       4.761 -17.001 -21.401  1.00151.89           O  
ANISOU 1677  OG  SER A 224    22281  17580  17849  -5345  -5036   -234
ATOM   1678  N   ASN A 225       7.331 -18.598 -24.819  1.00148.21           N  
ANISOU 1678  N   ASN A 225    22141  15847  18326  -3005  -4754  -1297
ATOM   1679  CA  ASN A 225       8.111 -19.593 -25.549  1.00158.60           C  
ANISOU 1679  CA  ASN A 225    23725  16506  20029  -2371  -4826  -1553
ATOM   1680  C   ASN A 225       9.570 -19.168 -25.678  1.00164.39           C  
ANISOU 1680  C   ASN A 225    24071  17350  21038  -1633  -4649  -1443
ATOM   1681  O   ASN A 225      10.477 -19.999 -25.553  1.00174.70           O  
ANISOU 1681  O   ASN A 225    25527  18072  22779  -1197  -4847  -1341
ATOM   1682  CB  ASN A 225       7.499 -19.836 -26.929  1.00159.22           C  
ANISOU 1682  CB  ASN A 225    24012  16559  19924  -2207  -4626  -2182
ATOM   1683  CG  ASN A 225       6.180 -20.579 -26.859  1.00158.09           C  
ANISOU 1683  CG  ASN A 225    24343  16129  19594  -2883  -4879  -2293
ATOM   1684  OD1 ASN A 225       6.024 -21.517 -26.078  1.00161.94           O  
ANISOU 1684  OD1 ASN A 225    25210  16043  20278  -3227  -5286  -2020
ATOM   1685  ND2 ASN A 225       5.221 -20.163 -27.679  1.00152.85           N  
ANISOU 1685  ND2 ASN A 225    23658  15875  18543  -3097  -4656  -2674
ATOM   1686  N   LEU A 226       9.816 -17.881 -25.933  1.00153.32           N  
ANISOU 1686  N   LEU A 226    22168  16695  19389  -1484  -4291  -1455
ATOM   1687  CA  LEU A 226      11.189 -17.398 -26.029  1.00153.05           C  
ANISOU 1687  CA  LEU A 226    21729  16851  19573   -843  -4123  -1313
ATOM   1688  C   LEU A 226      11.865 -17.373 -24.665  1.00153.32           C  
ANISOU 1688  C   LEU A 226    21633  16783  19841   -999  -4391   -674
ATOM   1689  O   LEU A 226      13.046 -17.721 -24.547  1.00158.40           O  
ANISOU 1689  O   LEU A 226    22162  17158  20864   -474  -4466   -493
ATOM   1690  CB  LEU A 226      11.222 -16.007 -26.661  1.00147.18           C  
ANISOU 1690  CB  LEU A 226    20516  16935  18471   -712  -3701  -1475
ATOM   1691  CG  LEU A 226      10.883 -15.883 -28.146  1.00146.98           C  
ANISOU 1691  CG  LEU A 226    20510  17100  18235   -408  -3385  -2090
ATOM   1692  CD1 LEU A 226      10.799 -14.420 -28.547  1.00140.80           C  
ANISOU 1692  CD1 LEU A 226    19274  17151  17072   -425  -3040  -2141
ATOM   1693  CD2 LEU A 226      11.917 -16.609 -28.989  1.00153.80           C  
ANISOU 1693  CD2 LEU A 226    21420  17587  19431    366  -3307  -2371
ATOM   1694  N   LEU A 227      11.135 -16.963 -23.622  1.00156.03           N  
ANISOU 1694  N   LEU A 227    21977  17356  19953  -1716  -4535   -324
ATOM   1695  CA  LEU A 227      11.760 -16.810 -22.311  1.00155.63           C  
ANISOU 1695  CA  LEU A 227    21778  17293  20062  -1917  -4770    294
ATOM   1696  C   LEU A 227      12.211 -18.150 -21.739  1.00165.39           C  
ANISOU 1696  C   LEU A 227    23376  17706  21760  -1855  -5204    549
ATOM   1697  O   LEU A 227      13.166 -18.197 -20.954  1.00168.81           O  
ANISOU 1697  O   LEU A 227    23653  18018  22470  -1715  -5384   1012
ATOM   1698  CB  LEU A 227      10.798 -16.106 -21.352  1.00143.62           C  
ANISOU 1698  CB  LEU A 227    20205  16210  18153  -2720  -4814    560
ATOM   1699  CG  LEU A 227      11.339 -15.747 -19.966  1.00140.02           C  
ANISOU 1699  CG  LEU A 227    19573  15871  17759  -3024  -5016   1192
ATOM   1700  CD1 LEU A 227      12.520 -14.795 -20.083  1.00138.84           C  
ANISOU 1700  CD1 LEU A 227    18945  16144  17663  -2529  -4788   1348
ATOM   1701  CD2 LEU A 227      10.244 -15.135 -19.105  1.00130.51           C  
ANISOU 1701  CD2 LEU A 227    18365  15091  16132  -3828  -5038   1361
ATOM   1702  N   GLN A 228      11.553 -19.246 -22.123  1.00143.90           N  
ANISOU 1702  N   GLN A 228    21148  14400  19128  -1959  -5396    267
ATOM   1703  CA  GLN A 228      11.971 -20.572 -21.687  1.00154.26           C  
ANISOU 1703  CA  GLN A 228    22859  14857  20897  -1858  -5832    467
ATOM   1704  C   GLN A 228      13.220 -21.057 -22.416  1.00165.65           C  
ANISOU 1704  C   GLN A 228    24229  15929  22780   -924  -5768    285
ATOM   1705  O   GLN A 228      13.876 -21.995 -21.947  1.00173.79           O  
ANISOU 1705  O   GLN A 228    25472  16301  24258   -706  -6123    541
ATOM   1706  CB  GLN A 228      10.822 -21.569 -21.894  1.00156.37           C  
ANISOU 1706  CB  GLN A 228    23711  14616  21088  -2306  -6072    212
ATOM   1707  CG  GLN A 228      11.071 -22.974 -21.351  1.00167.33           C  
ANISOU 1707  CG  GLN A 228    25598  15068  22913  -2340  -6594    449
ATOM   1708  CD  GLN A 228       9.895 -23.911 -21.568  1.00168.06           C  
ANISOU 1708  CD  GLN A 228    26284  14687  22885  -2847  -6843    207
ATOM   1709  OE1 GLN A 228       8.889 -23.537 -22.171  1.00161.16           O  
ANISOU 1709  OE1 GLN A 228    25434  14197  21605  -3153  -6612   -155
ATOM   1710  NE2 GLN A 228      10.019 -25.138 -21.075  1.00175.81           N  
ANISOU 1710  NE2 GLN A 228    27753  14827  24220  -2953  -7339    425
ATOM   1711  N   GLU A 229      13.582 -20.421 -23.529  1.00152.55           N  
ANISOU 1711  N   GLU A 229    22257  14702  21003   -368  -5329   -135
ATOM   1712  CA  GLU A 229      14.612 -20.926 -24.429  1.00164.03           C  
ANISOU 1712  CA  GLU A 229    23663  15851  22812    528  -5209   -439
ATOM   1713  C   GLU A 229      15.986 -20.307 -24.201  1.00164.99           C  
ANISOU 1713  C   GLU A 229    23231  16321  23136   1060  -5076   -121
ATOM   1714  O   GLU A 229      16.982 -21.031 -24.115  1.00174.10           O  
ANISOU 1714  O   GLU A 229    24392  17002  24755   1615  -5248     -1
ATOM   1715  CB  GLU A 229      14.185 -20.689 -25.883  1.00164.42           C  
ANISOU 1715  CB  GLU A 229    23721  16164  22589    817  -4808  -1127
ATOM   1716  CG  GLU A 229      15.181 -21.192 -26.915  1.00176.13           C  
ANISOU 1716  CG  GLU A 229    25154  17390  24377   1743  -4632  -1522
ATOM   1717  CD  GLU A 229      14.723 -20.938 -28.339  1.00175.58           C  
ANISOU 1717  CD  GLU A 229    25104  17615  23992   1964  -4238  -2195
ATOM   1718  OE1 GLU A 229      13.633 -20.354 -28.518  1.00165.52           O  
ANISOU 1718  OE1 GLU A 229    23870  16741  22279   1403  -4116  -2331
ATOM   1719  OE2 GLU A 229      15.454 -21.318 -29.278  1.00183.86           O1-
ANISOU 1719  OE2 GLU A 229    26118  18515  25227   2701  -4049  -2587
ATOM   1720  N   SER A 230      16.065 -18.984 -24.102  1.00158.90           N  
ANISOU 1720  N   SER A 230    21982  16365  22029    904  -4786     24
ATOM   1721  CA  SER A 230      17.318 -18.267 -24.289  1.00158.74           C  
ANISOU 1721  CA  SER A 230    21405  16804  22105   1470  -4550    172
ATOM   1722  C   SER A 230      17.876 -17.741 -22.971  1.00152.46           C  
ANISOU 1722  C   SER A 230    20327  16225  21375   1166  -4754    878
ATOM   1723  O   SER A 230      17.200 -17.702 -21.939  1.00146.35           O  
ANISOU 1723  O   SER A 230    19739  15390  20476    459  -5009   1226
ATOM   1724  CB  SER A 230      17.123 -17.108 -25.273  1.00152.93           C  
ANISOU 1724  CB  SER A 230    20327  16845  20934   1574  -4067   -196
ATOM   1725  OG  SER A 230      16.748 -17.585 -26.554  1.00158.65           O  
ANISOU 1725  OG  SER A 230    21277  17400  21603   1910  -3864   -846
ATOM   1726  N   ASN A 231      19.146 -17.340 -23.032  1.00152.21           N  
ANISOU 1726  N   ASN A 231    19831  16474  21528   1706  -4634   1085
ATOM   1727  CA  ASN A 231      19.799 -16.624 -21.949  1.00145.50           C  
ANISOU 1727  CA  ASN A 231    18625  15979  20680   1469  -4753   1728
ATOM   1728  C   ASN A 231      19.283 -15.184 -21.902  1.00134.38           C  
ANISOU 1728  C   ASN A 231    16952  15375  18733   1004  -4475   1753
ATOM   1729  O   ASN A 231      18.602 -14.711 -22.816  1.00133.40           O  
ANISOU 1729  O   ASN A 231    16841  15569  18276    990  -4165   1275
ATOM   1730  CB  ASN A 231      21.317 -16.663 -22.139  1.00149.64           C  
ANISOU 1730  CB  ASN A 231    18717  16580  21558   2216  -4702   1914
ATOM   1731  CG  ASN A 231      22.079 -16.213 -20.907  1.00145.12           C  
ANISOU 1731  CG  ASN A 231    17846  16207  21087   1980  -4933   2645
ATOM   1732  OD1 ASN A 231      21.485 -15.843 -19.895  1.00138.60           O  
ANISOU 1732  OD1 ASN A 231    17143  15468  20050   1252  -5120   3004
ATOM   1733  ND2 ASN A 231      23.405 -16.246 -20.987  1.00148.53           N  
ANISOU 1733  ND2 ASN A 231    17872  16734  21829   2591  -4918   2867
ATOM   1734  N   CYS A 232      19.615 -14.481 -20.816  1.00136.44           N  
ANISOU 1734  N   CYS A 232    16983  15952  18907    619  -4603   2321
ATOM   1735  CA  CYS A 232      19.080 -13.138 -20.601  1.00129.54           C  
ANISOU 1735  CA  CYS A 232    15917  15769  17531    125  -4396   2381
ATOM   1736  C   CYS A 232      19.471 -12.195 -21.735  1.00126.72           C  
ANISOU 1736  C   CYS A 232    15179  16021  16946    559  -3968   2053
ATOM   1737  O   CYS A 232      18.608 -11.621 -22.412  1.00122.88           O  
ANISOU 1737  O   CYS A 232    14744  15851  16093    393  -3716   1651
ATOM   1738  CB  CYS A 232      19.557 -12.592 -19.254  1.00127.95           C  
ANISOU 1738  CB  CYS A 232    15534  15773  17309   -292  -4618   3057
ATOM   1739  SG  CYS A 232      18.878 -10.968 -18.838  1.00120.04           S  
ANISOU 1739  SG  CYS A 232    14360  15550  15700   -927  -4409   3147
ATOM   1740  N   SER A 233      20.778 -12.021 -21.954  1.00128.19           N  
ANISOU 1740  N   SER A 233    14967  16400  17340   1103  -3893   2238
ATOM   1741  CA  SER A 233      21.239 -11.158 -23.037  1.00125.97           C  
ANISOU 1741  CA  SER A 233    14304  16719  16839   1510  -3502   1959
ATOM   1742  C   SER A 233      20.760 -11.658 -24.392  1.00132.58           C  
ANISOU 1742  C   SER A 233    15317  17411  17647   1895  -3258   1271
ATOM   1743  O   SER A 233      20.453 -10.853 -25.281  1.00127.52           O  
ANISOU 1743  O   SER A 233    14534  17265  16653   1929  -2939    931
ATOM   1744  CB  SER A 233      22.763 -11.061 -23.015  1.00128.11           C  
ANISOU 1744  CB  SER A 233    14113  17189  17374   2042  -3493   2294
ATOM   1745  OG  SER A 233      23.364 -12.310 -23.309  1.00140.21           O  
ANISOU 1745  OG  SER A 233    15720  18167  19386   2635  -3605   2179
ATOM   1746  N   GLN A 234      20.687 -12.978 -24.564  1.00128.15           N  
ANISOU 1746  N   GLN A 234    15085  16161  17443   2169  -3421   1063
ATOM   1747  CA  GLN A 234      20.161 -13.542 -25.801  1.00133.48           C  
ANISOU 1747  CA  GLN A 234    16002  16633  18083   2483  -3220    396
ATOM   1748  C   GLN A 234      18.673 -13.248 -25.945  1.00128.01           C  
ANISOU 1748  C   GLN A 234    15634  16009  16997   1879  -3169    110
ATOM   1749  O   GLN A 234      18.186 -13.000 -27.056  1.00126.66           O  
ANISOU 1749  O   GLN A 234    15487  16069  16569   2002  -2886   -398
ATOM   1750  CB  GLN A 234      20.427 -15.046 -25.830  1.00144.98           C  
ANISOU 1750  CB  GLN A 234    17787  17271  20028   2882  -3458    276
ATOM   1751  CG  GLN A 234      21.907 -15.396 -25.826  1.00149.88           C  
ANISOU 1751  CG  GLN A 234    18059  17825  21064   3583  -3484    494
ATOM   1752  CD  GLN A 234      22.159 -16.888 -25.763  1.00160.65           C  
ANISOU 1752  CD  GLN A 234    19776  18321  22941   3984  -3764    400
ATOM   1753  OE1 GLN A 234      21.226 -17.685 -25.664  1.00164.24           O  
ANISOU 1753  OE1 GLN A 234    20771  18194  23441   3685  -3971    206
ATOM   1754  NE2 GLN A 234      23.429 -17.274 -25.812  1.00165.29           N  
ANISOU 1754  NE2 GLN A 234    20059  18819  23923   4662  -3788    549
ATOM   1755  N   TYR A 235      17.938 -13.266 -24.830  1.00133.90           N  
ANISOU 1755  N   TYR A 235    16613  16585  17676   1215  -3443    437
ATOM   1756  CA  TYR A 235      16.527 -12.895 -24.864  1.00129.66           C  
ANISOU 1756  CA  TYR A 235    16320  16199  16747    615  -3394    216
ATOM   1757  C   TYR A 235      16.351 -11.443 -25.284  1.00123.62           C  
ANISOU 1757  C   TYR A 235    15212  16219  15540    497  -3075    135
ATOM   1758  O   TYR A 235      15.504 -11.128 -26.127  1.00121.31           O  
ANISOU 1758  O   TYR A 235    15001  16142  14948    407  -2865   -301
ATOM   1759  CB  TYR A 235      15.882 -13.139 -23.499  1.00128.95           C  
ANISOU 1759  CB  TYR A 235    16483  15852  16658    -74  -3740    630
ATOM   1760  CG  TYR A 235      14.438 -12.695 -23.425  1.00124.70           C  
ANISOU 1760  CG  TYR A 235    16134  15543  15701   -711  -3687    443
ATOM   1761  CD1 TYR A 235      13.431 -13.432 -24.033  1.00126.36           C  
ANISOU 1761  CD1 TYR A 235    16725  15432  15853   -837  -3702      8
ATOM   1762  CD2 TYR A 235      14.083 -11.536 -22.749  1.00119.33           C  
ANISOU 1762  CD2 TYR A 235    15249  15410  14679  -1182  -3624    699
ATOM   1763  CE1 TYR A 235      12.111 -13.026 -23.970  1.00122.77           C  
ANISOU 1763  CE1 TYR A 235    16402  15229  15015  -1413  -3654   -148
ATOM   1764  CE2 TYR A 235      12.767 -11.122 -22.680  1.00115.83           C  
ANISOU 1764  CE2 TYR A 235    14944  15202  13863  -1722  -3566    518
ATOM   1765  CZ  TYR A 235      11.785 -11.871 -23.292  1.00117.56           C  
ANISOU 1765  CZ  TYR A 235    15502  15129  14036  -1835  -3580    104
ATOM   1766  OH  TYR A 235      10.472 -11.464 -23.226  1.00114.37           O  
ANISOU 1766  OH  TYR A 235    15196  14997  13261  -2368  -3524    -62
ATOM   1767  N   MET A 236      17.147 -10.540 -24.706  1.00131.16           N  
ANISOU 1767  N   MET A 236    15791  17597  16445    484  -3055    567
ATOM   1768  CA  MET A 236      17.009  -9.126 -25.041  1.00119.85           C  
ANISOU 1768  CA  MET A 236    14063  16877  14596    349  -2794    528
ATOM   1769  C   MET A 236      17.392  -8.863 -26.492  1.00122.33           C  
ANISOU 1769  C   MET A 236    14169  17496  14816    889  -2461     88
ATOM   1770  O   MET A 236      16.686  -8.141 -27.207  1.00116.05           O  
ANISOU 1770  O   MET A 236    13354  17079  13662    754  -2246   -230
ATOM   1771  CB  MET A 236      17.853  -8.282 -24.086  1.00112.76           C  
ANISOU 1771  CB  MET A 236    12844  16321  13679    211  -2879   1106
ATOM   1772  CG  MET A 236      17.379  -8.362 -22.643  1.00108.58           C  
ANISOU 1772  CG  MET A 236    12513  15595  13149   -407  -3181   1531
ATOM   1773  SD  MET A 236      18.311  -7.310 -21.521  1.00103.59           S  
ANISOU 1773  SD  MET A 236    11540  15382  12438   -631  -3283   2195
ATOM   1774  CE  MET A 236      19.852  -8.210 -21.405  1.00111.08           C  
ANISOU 1774  CE  MET A 236    12290  15998  13915    -49  -3447   2519
ATOM   1775  N   GLU A 237      18.503  -9.450 -26.946  1.00123.85           N  
ANISOU 1775  N   GLU A 237    14197  17540  15322   1504  -2419     63
ATOM   1776  CA  GLU A 237      18.889  -9.352 -28.350  1.00126.44           C  
ANISOU 1776  CA  GLU A 237    14341  18133  15566   2037  -2098   -388
ATOM   1777  C   GLU A 237      17.755  -9.825 -29.253  1.00128.33           C  
ANISOU 1777  C   GLU A 237    14943  18164  15652   1967  -1991   -978
ATOM   1778  O   GLU A 237      17.374  -9.145 -30.218  1.00123.74           O  
ANISOU 1778  O   GLU A 237    14266  18017  14732   1980  -1729  -1318
ATOM   1779  CB  GLU A 237      20.151 -10.186 -28.587  1.00136.78           C  
ANISOU 1779  CB  GLU A 237    15484  19192  17295   2716  -2106   -355
ATOM   1780  CG  GLU A 237      20.797 -10.019 -29.951  1.00139.19           C  
ANISOU 1780  CG  GLU A 237    15505  19868  17513   3309  -1757   -755
ATOM   1781  CD  GLU A 237      21.517  -8.692 -30.094  1.00130.82           C  
ANISOU 1781  CD  GLU A 237    13937  19593  16178   3318  -1569   -496
ATOM   1782  OE1 GLU A 237      21.962  -8.145 -29.062  1.00126.05           O  
ANISOU 1782  OE1 GLU A 237    13143  19147  15603   3063  -1740     60
ATOM   1783  OE2 GLU A 237      21.647  -8.200 -31.235  1.00128.58           O1-
ANISOU 1783  OE2 GLU A 237    13455  19765  15636   3556  -1266   -839
ATOM   1784  N   LYS A 238      17.178 -10.984 -28.921  1.00137.51           N  
ANISOU 1784  N   LYS A 238    16539  18660  17047   1848  -2219  -1079
ATOM   1785  CA  LYS A 238      16.146 -11.581 -29.762  1.00140.42           C  
ANISOU 1785  CA  LYS A 238    17286  18767  17298   1782  -2154  -1627
ATOM   1786  C   LYS A 238      14.895 -10.712 -29.812  1.00128.91           C  
ANISOU 1786  C   LYS A 238    15891  17695  15395   1197  -2079  -1731
ATOM   1787  O   LYS A 238      14.345 -10.464 -30.889  1.00125.87           O  
ANISOU 1787  O   LYS A 238    15539  17542  14744   1244  -1858  -2179
ATOM   1788  CB  LYS A 238      15.809 -12.984 -29.257  1.00149.10           C  
ANISOU 1788  CB  LYS A 238    18857  19054  18740   1707  -2471  -1636
ATOM   1789  N   VAL A 239      14.424 -10.240 -28.653  1.00137.97           N  
ANISOU 1789  N   VAL A 239    17051  18924  16449    645  -2264  -1328
ATOM   1790  CA  VAL A 239      13.199  -9.445 -28.642  1.00129.96           C  
ANISOU 1790  CA  VAL A 239    16087  18264  15027    111  -2201  -1433
ATOM   1791  C   VAL A 239      13.422  -8.104 -29.331  1.00125.84           C  
ANISOU 1791  C   VAL A 239    15193  18442  14179    231  -1916  -1511
ATOM   1792  O   VAL A 239      12.506  -7.565 -29.968  1.00123.01           O  
ANISOU 1792  O   VAL A 239    14868  18377  13494     29  -1776  -1812
ATOM   1793  CB  VAL A 239      12.673  -9.264 -27.204  1.00127.71           C  
ANISOU 1793  CB  VAL A 239    15893  17922  14709   -493  -2452   -996
ATOM   1794  CG1 VAL A 239      12.372 -10.614 -26.571  1.00132.04           C  
ANISOU 1794  CG1 VAL A 239    16839  17778  15551   -670  -2759   -918
ATOM   1795  CG2 VAL A 239      13.655  -8.482 -26.355  1.00125.88           C  
ANISOU 1795  CG2 VAL A 239    15328  17975  14523   -472  -2492   -483
ATOM   1796  N   LEU A 240      14.633  -7.549 -29.232  1.00137.10           N  
ANISOU 1796  N   LEU A 240    16260  20149  15682    547  -1844  -1230
ATOM   1797  CA  LEU A 240      14.928  -6.306 -29.937  1.00131.29           C  
ANISOU 1797  CA  LEU A 240    15183  20064  14636    663  -1596  -1289
ATOM   1798  C   LEU A 240      14.855  -6.514 -31.446  1.00134.60           C  
ANISOU 1798  C   LEU A 240    15608  20589  14944   1033  -1345  -1830
ATOM   1799  O   LEU A 240      14.229  -5.725 -32.167  1.00128.78           O  
ANISOU 1799  O   LEU A 240    14817  20255  13859    892  -1185  -2070
ATOM   1800  CB  LEU A 240      16.304  -5.781 -29.522  1.00131.22           C  
ANISOU 1800  CB  LEU A 240    14796  20319  14743    915  -1594   -855
ATOM   1801  CG  LEU A 240      16.706  -4.400 -30.043  1.00125.86           C  
ANISOU 1801  CG  LEU A 240    13759  20328  13736    954  -1395   -795
ATOM   1802  CD1 LEU A 240      15.783  -3.329 -29.478  1.00119.91           C  
ANISOU 1802  CD1 LEU A 240    13057  19850  12654    397  -1452   -661
ATOM   1803  CD2 LEU A 240      18.156  -4.096 -29.704  1.00127.50           C  
ANISOU 1803  CD2 LEU A 240    13597  20754  14092   1238  -1407   -375
ATOM   1804  N   GLY A 241      15.479  -7.589 -31.940  1.00140.63           N  
ANISOU 1804  N   GLY A 241    16448  20984  16000   1509  -1317  -2037
ATOM   1805  CA  GLY A 241      15.350  -7.912 -33.353  1.00144.67           C  
ANISOU 1805  CA  GLY A 241    17020  21548  16400   1840  -1084  -2592
ATOM   1806  C   GLY A 241      13.909  -8.148 -33.769  1.00140.90           C  
ANISOU 1806  C   GLY A 241    16905  20922  15708   1465  -1100  -2970
ATOM   1807  O   GLY A 241      13.487  -7.730 -34.853  1.00138.07           O  
ANISOU 1807  O   GLY A 241    16516  20893  15053   1491   -895  -3337
ATOM   1808  N   ARG A 242      13.133  -8.813 -32.908  1.00151.86           N  
ANISOU 1808  N   ARG A 242    18630  21840  17229   1085  -1355  -2863
ATOM   1809  CA  ARG A 242      11.726  -9.072 -33.204  1.00148.95           C  
ANISOU 1809  CA  ARG A 242    18595  21345  16656    676  -1399  -3175
ATOM   1810  C   ARG A 242      10.937  -7.779 -33.351  1.00137.82           C  
ANISOU 1810  C   ARG A 242    17005  20530  14831    302  -1292  -3168
ATOM   1811  O   ARG A 242      10.093  -7.660 -34.247  1.00136.46           O  
ANISOU 1811  O   ARG A 242    16935  20512  14401    188  -1181  -3547
ATOM   1812  CB  ARG A 242      11.109  -9.949 -32.114  1.00151.21           C  
ANISOU 1812  CB  ARG A 242    19231  21076  17145    285  -1715  -2978
ATOM   1813  CG  ARG A 242      11.599 -11.381 -32.112  1.00164.16           C  
ANISOU 1813  CG  ARG A 242    21171  22019  19183    604  -1865  -3077
ATOM   1814  CD  ARG A 242      11.093 -12.105 -33.345  1.00167.82           C  
ANISOU 1814  CD  ARG A 242    21933  22259  19572    770  -1758  -3662
ATOM   1815  NE  ARG A 242       9.635 -12.172 -33.356  1.00161.14           N  
ANISOU 1815  NE  ARG A 242    21367  21390  18469    190  -1851  -3822
ATOM   1816  CZ  ARG A 242       8.905 -12.436 -34.434  1.00160.69           C  
ANISOU 1816  CZ  ARG A 242    21520  21333  18202    157  -1741  -4304
ATOM   1817  NH1 ARG A 242       9.496 -12.661 -35.599  1.00165.98           N  
ANISOU 1817  NH1 ARG A 242    22171  22018  18877    671  -1523  -4697
ATOM   1818  NH2 ARG A 242       7.582 -12.474 -34.347  1.00154.85           N1+
ANISOU 1818  NH2 ARG A 242    20998  20607  17233   -402  -1848  -4391
ATOM   1819  N   LEU A 243      11.179  -6.805 -32.471  1.00137.49           N  
ANISOU 1819  N   LEU A 243    16708  20812  14719    102  -1339  -2739
ATOM   1820  CA  LEU A 243      10.483  -5.528 -32.597  1.00132.44           C  
ANISOU 1820  CA  LEU A 243    15901  20717  13702   -207  -1249  -2730
ATOM   1821  C   LEU A 243      10.918  -4.786 -33.855  1.00131.65           C  
ANISOU 1821  C   LEU A 243    15553  21088  13380    115   -994  -2968
ATOM   1822  O   LEU A 243      10.076  -4.258 -34.598  1.00129.60           O  
ANISOU 1822  O   LEU A 243    15319  20886  13036    -37   -834  -3064
ATOM   1823  CB  LEU A 243      10.725  -4.677 -31.351  1.00129.08           C  
ANISOU 1823  CB  LEU A 243    15294  20493  13257   -470  -1366  -2227
ATOM   1824  CG  LEU A 243      10.118  -5.242 -30.066  1.00129.32           C  
ANISOU 1824  CG  LEU A 243    15559  20160  13419   -899  -1615  -1983
ATOM   1825  CD1 LEU A 243      10.525  -4.416 -28.859  1.00126.52           C  
ANISOU 1825  CD1 LEU A 243    15019  20011  13042  -1119  -1716  -1489
ATOM   1826  CD2 LEU A 243       8.607  -5.309 -30.185  1.00128.02           C  
ANISOU 1826  CD2 LEU A 243    15615  19958  13068  -1308  -1624  -2217
ATOM   1827  N   LYS A 244      12.230  -4.754 -34.121  1.00143.40           N  
ANISOU 1827  N   LYS A 244    16803  22678  15006    562   -891  -2863
ATOM   1828  CA  LYS A 244      12.728  -4.065 -35.308  1.00143.25           C  
ANISOU 1828  CA  LYS A 244    16527  23144  14758    852   -649  -3063
ATOM   1829  C   LYS A 244      12.133  -4.656 -36.581  1.00145.29           C  
ANISOU 1829  C   LYS A 244    16985  23325  14893    970   -509  -3621
ATOM   1830  O   LYS A 244      11.863  -3.928 -37.544  1.00143.29           O  
ANISOU 1830  O   LYS A 244    16609  23193  14641    907   -335  -3572
ATOM   1831  CB  LYS A 244      14.254  -4.120 -35.350  1.00146.49           C  
ANISOU 1831  CB  LYS A 244    16643  23657  15359   1322   -565  -2864
ATOM   1832  CG  LYS A 244      14.863  -3.362 -36.519  1.00146.80           C  
ANISOU 1832  CG  LYS A 244    16376  24264  15137   1591   -317  -3020
ATOM   1833  CD  LYS A 244      14.638  -1.862 -36.371  1.00141.62           C  
ANISOU 1833  CD  LYS A 244    15513  24018  14277   1244   -324  -2697
ATOM   1834  CE  LYS A 244      15.362  -1.074 -37.454  1.00142.51           C  
ANISOU 1834  CE  LYS A 244    15308  24427  14413   1416   -162  -2621
ATOM   1835  NZ  LYS A 244      14.792  -1.328 -38.807  1.00144.26           N1+
ANISOU 1835  NZ  LYS A 244    15660  24455  14699   1426    -62  -2936
ATOM   1836  N   ASP A 245      11.918  -5.975 -36.607  1.00151.31           N  
ANISOU 1836  N   ASP A 245    18072  23525  15895   1070   -580  -3853
ATOM   1837  CA  ASP A 245      11.217  -6.577 -37.738  1.00153.97           C  
ANISOU 1837  CA  ASP A 245    18664  23742  16095   1103   -479  -4387
ATOM   1838  C   ASP A 245       9.735  -6.216 -37.724  1.00150.21           C  
ANISOU 1838  C   ASP A 245    18360  23128  15586    541   -533  -4229
ATOM   1839  O   ASP A 245       9.143  -5.937 -38.776  1.00149.66           O  
ANISOU 1839  O   ASP A 245    18313  23012  15538    454   -384  -4220
ATOM   1840  CB  ASP A 245      11.392  -8.097 -37.721  1.00161.14           C  
ANISOU 1840  CB  ASP A 245    19914  23975  17338   1343   -565  -4599
ATOM   1841  CG  ASP A 245      12.815  -8.526 -38.020  1.00169.92           C  
ANISOU 1841  CG  ASP A 245    20846  25022  18696   1966   -436  -4618
ATOM   1842  OD1 ASP A 245      13.517  -7.792 -38.747  1.00168.93           O  
ANISOU 1842  OD1 ASP A 245    20375  25421  18390   2235   -205  -4665
ATOM   1843  OD2 ASP A 245      13.230  -9.598 -37.531  1.00178.28           O1-
ANISOU 1843  OD2 ASP A 245    22099  25513  20125   2184   -573  -4580
ATOM   1844  N   GLU A 246       9.126  -6.210 -36.535  1.00156.26           N  
ANISOU 1844  N   GLU A 246    19235  23755  16384    163   -742  -3988
ATOM   1845  CA  GLU A 246       7.685  -6.007 -36.424  1.00153.84           C  
ANISOU 1845  CA  GLU A 246    19106  23196  16150   -295   -762  -3758
ATOM   1846  C   GLU A 246       7.272  -4.647 -36.967  1.00149.41           C  
ANISOU 1846  C   GLU A 246    18296  22802  15671   -364   -569  -3405
ATOM   1847  O   GLU A 246       6.224  -4.521 -37.613  1.00148.97           O  
ANISOU 1847  O   GLU A 246    18344  22598  15660   -516   -512  -3378
ATOM   1848  CB  GLU A 246       7.247  -6.161 -34.967  1.00153.01           C  
ANISOU 1848  CB  GLU A 246    19109  22940  16089   -653   -994  -3504
ATOM   1849  CG  GLU A 246       5.745  -6.045 -34.739  1.00151.18           C  
ANISOU 1849  CG  GLU A 246    19049  22455  15938  -1037  -1011  -3281
ATOM   1850  CD  GLU A 246       4.964  -7.191 -35.358  1.00154.99           C  
ANISOU 1850  CD  GLU A 246    19889  22620  16379  -1139  -1092  -3614
ATOM   1851  OE1 GLU A 246       5.543  -8.283 -35.535  1.00159.88           O  
ANISOU 1851  OE1 GLU A 246    20719  23074  16955  -1007  -1209  -4029
ATOM   1852  OE2 GLU A 246       3.766  -7.003 -35.661  1.00153.63           O1-
ANISOU 1852  OE2 GLU A 246    19786  22345  16243  -1317  -1049  -3483
ATOM   1853  N   GLU A 247       8.080  -3.613 -36.720  1.00161.53           N  
ANISOU 1853  N   GLU A 247    19506  24627  17241   -247   -497  -3140
ATOM   1854  CA  GLU A 247       7.731  -2.297 -37.245  1.00158.12           C  
ANISOU 1854  CA  GLU A 247    18857  24279  16941   -306   -357  -2853
ATOM   1855  C   GLU A 247       7.738  -2.294 -38.771  1.00159.79           C  
ANISOU 1855  C   GLU A 247    19030  24560  17121   -152   -241  -3059
ATOM   1856  O   GLU A 247       6.813  -1.766 -39.402  1.00158.56           O  
ANISOU 1856  O   GLU A 247    18886  24308  17052   -290   -194  -2959
ATOM   1857  CB  GLU A 247       8.680  -1.233 -36.695  1.00156.07           C  
ANISOU 1857  CB  GLU A 247    18295  24268  16737   -227   -324  -2550
ATOM   1858  CG  GLU A 247       8.298   0.184 -37.095  1.00152.41           C  
ANISOU 1858  CG  GLU A 247    17647  23808  16453   -309   -217  -2275
ATOM   1859  CD  GLU A 247       9.173   1.235 -36.442  1.00149.98           C  
ANISOU 1859  CD  GLU A 247    17106  23659  16221   -279   -189  -1975
ATOM   1860  OE1 GLU A 247      10.095   0.860 -35.687  1.00151.01           O  
ANISOU 1860  OE1 GLU A 247    17190  23939  16246   -195   -251  -1939
ATOM   1861  OE2 GLU A 247       8.933   2.438 -36.683  1.00147.23           O1-
ANISOU 1861  OE2 GLU A 247    16549  23389  16004   -346   -103  -1811
ATOM   1862  N   ILE A 248       8.764  -2.895 -39.380  1.00157.09           N  
ANISOU 1862  N   ILE A 248    18644  24388  16655    157   -195  -3354
ATOM   1863  CA  ILE A 248       8.824  -2.972 -40.838  1.00159.20           C  
ANISOU 1863  CA  ILE A 248    18903  24707  16881    295    -79  -3554
ATOM   1864  C   ILE A 248       7.625  -3.739 -41.380  1.00160.78           C  
ANISOU 1864  C   ILE A 248    19446  24586  17058    120    -93  -3746
ATOM   1865  O   ILE A 248       7.065  -3.387 -42.427  1.00160.47           O  
ANISOU 1865  O   ILE A 248    19410  24537  17026     46    -32  -3726
ATOM   1866  CB  ILE A 248      10.155  -3.607 -41.285  1.00163.33           C  
ANISOU 1866  CB  ILE A 248    19339  25431  17288    715      2  -3862
ATOM   1867  CG1 ILE A 248      11.335  -2.732 -40.858  1.00162.24           C  
ANISOU 1867  CG1 ILE A 248    18820  25678  17146    882      8  -3608
ATOM   1868  CG2 ILE A 248      10.172  -3.821 -42.792  1.00166.34           C  
ANISOU 1868  CG2 ILE A 248    19767  25818  17615    831    133  -4086
ATOM   1869  CD1 ILE A 248      12.684  -3.394 -41.038  1.00167.01           C  
ANISOU 1869  CD1 ILE A 248    19307  26503  17648   1364     95  -3868
ATOM   1870  N   ARG A 249       7.203  -4.789 -40.672  1.00165.84           N  
ANISOU 1870  N   ARG A 249    20388  24961  17663     30   -201  -3925
ATOM   1871  CA  ARG A 249       6.023  -5.539 -41.094  1.00167.33           C  
ANISOU 1871  CA  ARG A 249    20924  24837  17819   -175   -250  -4074
ATOM   1872  C   ARG A 249       4.771  -4.670 -41.061  1.00163.32           C  
ANISOU 1872  C   ARG A 249    20355  24294  17405   -466   -271  -3724
ATOM   1873  O   ARG A 249       4.011  -4.613 -42.038  1.00163.89           O  
ANISOU 1873  O   ARG A 249    20501  24314  17457   -537   -232  -3753
ATOM   1874  CB  ARG A 249       5.846  -6.771 -40.209  1.00169.68           C  
ANISOU 1874  CB  ARG A 249    21556  24833  18083   -262   -420  -4302
ATOM   1875  CG  ARG A 249       4.662  -7.628 -40.591  1.00172.57           C  
ANISOU 1875  CG  ARG A 249    22308  24857  18403   -497   -510  -4450
ATOM   1876  CD  ARG A 249       4.640  -8.900 -39.777  1.00176.41           C  
ANISOU 1876  CD  ARG A 249    23149  24996  18884   -590   -720  -4712
ATOM   1877  NE  ARG A 249       5.816  -9.709 -40.073  1.00181.45           N  
ANISOU 1877  NE  ARG A 249    23872  25542  19530   -192   -678  -5165
ATOM   1878  CZ  ARG A 249       5.925 -10.495 -41.139  1.00185.97           C  
ANISOU 1878  CZ  ARG A 249    24688  25903  20069      7   -584  -5543
ATOM   1879  NH1 ARG A 249       4.927 -10.574 -42.008  1.00185.66           N  
ANISOU 1879  NH1 ARG A 249    24842  25766  19934   -216   -551  -5509
ATOM   1880  NH2 ARG A 249       7.031 -11.198 -41.337  1.00190.68           N1+
ANISOU 1880  NH2 ARG A 249    25332  26371  20746    478   -532  -5951
ATOM   1881  N   CYS A 250       4.538  -3.988 -39.935  1.00164.89           N  
ANISOU 1881  N   CYS A 250    20416  24519  17715   -609   -327  -3404
ATOM   1882  CA  CYS A 250       3.380  -3.109 -39.830  1.00161.44           C  
ANISOU 1882  CA  CYS A 250    19861  24076  17401   -808   -310  -3123
ATOM   1883  C   CYS A 250       3.399  -2.032 -40.904  1.00160.95           C  
ANISOU 1883  C   CYS A 250    19417  24358  17380   -754   -170  -3100
ATOM   1884  O   CYS A 250       2.339  -1.611 -41.381  1.00161.50           O  
ANISOU 1884  O   CYS A 250    19335  24552  17474   -911   -123  -3091
ATOM   1885  CB  CYS A 250       3.326  -2.474 -38.442  1.00158.80           C  
ANISOU 1885  CB  CYS A 250    19369  23790  17177   -925   -336  -2843
ATOM   1886  SG  CYS A 250       3.053  -3.654 -37.104  1.00162.20           S  
ANISOU 1886  SG  CYS A 250    20143  23929  17558  -1101   -537  -2869
ATOM   1887  N   ARG A 251       4.588  -1.580 -41.304  1.00167.75           N  
ANISOU 1887  N   ARG A 251    20114  25384  18239   -542   -118  -3088
ATOM   1888  CA  ARG A 251       4.682  -0.612 -42.387  1.00167.70           C  
ANISOU 1888  CA  ARG A 251    19768  25695  18256   -503    -34  -3075
ATOM   1889  C   ARG A 251       4.487  -1.250 -43.756  1.00171.16           C  
ANISOU 1889  C   ARG A 251    20356  26112  18563   -458     -1  -3344
ATOM   1890  O   ARG A 251       4.164  -0.539 -44.714  1.00171.09           O  
ANISOU 1890  O   ARG A 251    20106  26343  18558   -509     45  -3345
ATOM   1891  CB  ARG A 251       6.027   0.111 -42.323  1.00166.28           C  
ANISOU 1891  CB  ARG A 251    19347  25726  18106   -319    -14  -2950
ATOM   1892  CG  ARG A 251       6.193   0.930 -41.053  1.00163.74           C  
ANISOU 1892  CG  ARG A 251    18848  25453  17913   -387    -31  -2666
ATOM   1893  CD  ARG A 251       7.509   1.678 -41.018  1.00163.05           C  
ANISOU 1893  CD  ARG A 251    18518  25590  17845   -227    -23  -2526
ATOM   1894  NE  ARG A 251       7.729   2.318 -39.725  1.00160.76           N  
ANISOU 1894  NE  ARG A 251    18129  25297  17655   -296    -30  -2266
ATOM   1895  CZ  ARG A 251       7.281   3.526 -39.401  1.00158.84           C  
ANISOU 1895  CZ  ARG A 251    17635  25184  17532   -431     27  -2075
ATOM   1896  NH1 ARG A 251       6.578   4.232 -40.276  1.00159.11           N  
ANISOU 1896  NH1 ARG A 251    17483  25369  17604   -506     77  -2107
ATOM   1897  NH2 ARG A 251       7.530   4.026 -38.198  1.00156.85           N1+
ANISOU 1897  NH2 ARG A 251    17347  24899  17348   -493     45  -1858
ATOM   1898  N   LYS A 252       4.669  -2.569 -43.869  1.00166.01           N  
ANISOU 1898  N   LYS A 252    20119  25165  17790   -369    -22  -3577
ATOM   1899  CA  LYS A 252       4.381  -3.250 -45.127  1.00169.63           C  
ANISOU 1899  CA  LYS A 252    20778  25561  18113   -345     24  -3850
ATOM   1900  C   LYS A 252       2.889  -3.497 -45.307  1.00170.11           C  
ANISOU 1900  C   LYS A 252    20944  25533  18156   -606    -29  -3884
ATOM   1901  O   LYS A 252       2.369  -3.375 -46.422  1.00172.35           O  
ANISOU 1901  O   LYS A 252    21170  25944  18370   -674     14  -3992
ATOM   1902  CB  LYS A 252       5.133  -4.579 -45.209  1.00173.42           C  
ANISOU 1902  CB  LYS A 252    21616  25809  18466   -140     50  -4172
ATOM   1903  CG  LYS A 252       6.629  -4.468 -45.427  1.00175.03           C  
ANISOU 1903  CG  LYS A 252    21601  26262  18639    173    156  -4287
ATOM   1904  CD  LYS A 252       7.239  -5.852 -45.575  1.00180.85           C  
ANISOU 1904  CD  LYS A 252    22604  26835  19274    424    215  -4735
ATOM   1905  CE  LYS A 252       8.739  -5.787 -45.800  1.00183.91           C  
ANISOU 1905  CE  LYS A 252    22740  27493  19644    810    341  -4861
ATOM   1906  NZ  LYS A 252       9.326  -7.148 -45.949  1.00190.32           N1+
ANISOU 1906  NZ  LYS A 252    23806  28087  20421   1139    421  -5330
ATOM   1907  N   TYR A 253       2.184  -3.853 -44.235  1.00167.78           N  
ANISOU 1907  N   TYR A 253    20797  25041  17911   -766   -125  -3791
ATOM   1908  CA  TYR A 253       0.793  -4.275 -44.346  1.00169.22           C  
ANISOU 1908  CA  TYR A 253    21114  25126  18054  -1011   -185  -3837
ATOM   1909  C   TYR A 253      -0.206  -3.227 -43.881  1.00166.47           C  
ANISOU 1909  C   TYR A 253    20396  25026  17830  -1222   -148  -3593
ATOM   1910  O   TYR A 253      -1.125  -2.876 -44.628  1.00167.33           O  
ANISOU 1910  O   TYR A 253    20362  25300  17916  -1361   -101  -3610
ATOM   1911  CB  TYR A 253       0.578  -5.575 -43.556  1.00170.98           C  
ANISOU 1911  CB  TYR A 253    21808  24935  18219  -1070   -343  -3938
ATOM   1912  CG  TYR A 253       1.291  -6.772 -44.143  1.00175.44           C  
ANISOU 1912  CG  TYR A 253    22813  25204  18643   -889   -370  -4255
ATOM   1913  CD1 TYR A 253       0.760  -7.458 -45.226  1.00179.54           C  
ANISOU 1913  CD1 TYR A 253    23603  25587  19026   -925   -381  -4484
ATOM   1914  CD2 TYR A 253       2.495  -7.217 -43.613  1.00177.33           C  
ANISOU 1914  CD2 TYR A 253    23077  25427  18873   -703   -348  -4431
ATOM   1915  CE1 TYR A 253       1.407  -8.553 -45.767  1.00185.29           C  
ANISOU 1915  CE1 TYR A 253    24650  26129  19622   -775   -352  -4884
ATOM   1916  CE2 TYR A 253       3.151  -8.311 -44.147  1.00182.59           C  
ANISOU 1916  CE2 TYR A 253    24024  25921  19430   -521   -312  -4850
ATOM   1917  CZ  TYR A 253       2.602  -8.975 -45.224  1.00186.72           C  
ANISOU 1917  CZ  TYR A 253    24845  26270  19829   -560   -304  -5077
ATOM   1918  OH  TYR A 253       3.250 -10.064 -45.759  1.00193.41           O  
ANISOU 1918  OH  TYR A 253    26000  26897  20592   -355   -245  -5513
ATOM   1919  N   LEU A 254      -0.052  -2.712 -42.665  1.00166.58           N  
ANISOU 1919  N   LEU A 254    20262  25068  17963  -1246   -153  -3374
ATOM   1920  CA  LEU A 254      -1.118  -1.961 -42.020  1.00164.22           C  
ANISOU 1920  CA  LEU A 254    19711  24928  17759  -1453   -104  -3178
ATOM   1921  C   LEU A 254      -1.115  -0.498 -42.459  1.00162.09           C  
ANISOU 1921  C   LEU A 254    19001  24998  17589  -1421     19  -3040
ATOM   1922  O   LEU A 254      -0.250  -0.040 -43.212  1.00162.34           O  
ANISOU 1922  O   LEU A 254    18902  25156  17623  -1259     46  -3071
ATOM   1923  CB  LEU A 254      -0.982  -2.054 -40.504  1.00163.02           C  
ANISOU 1923  CB  LEU A 254    19617  24650  17673  -1506   -154  -3013
ATOM   1924  CG  LEU A 254      -1.075  -3.457 -39.910  1.00165.82           C  
ANISOU 1924  CG  LEU A 254    20410  24651  17942  -1575   -324  -3120
ATOM   1925  CD1 LEU A 254      -0.838  -3.403 -38.412  1.00164.73           C  
ANISOU 1925  CD1 LEU A 254    20285  24431  17874  -1634   -380  -2927
ATOM   1926  CD2 LEU A 254      -2.411  -4.093 -40.233  1.00168.51           C  
ANISOU 1926  CD2 LEU A 254    20887  24936  18204  -1803   -368  -3216
ATOM   1927  N   HIS A 255      -2.112   0.243 -41.973  1.00165.83           N  
ANISOU 1927  N   HIS A 255    19252  25621  18134  -1579     90  -2891
ATOM   1928  CA  HIS A 255      -2.181   1.685 -42.134  1.00164.14           C  
ANISOU 1928  CA  HIS A 255    18661  25682  18025  -1550    192  -2745
ATOM   1929  C   HIS A 255      -1.388   2.370 -41.022  1.00161.64           C  
ANISOU 1929  C   HIS A 255    18227  25370  17820  -1465    213  -2555
ATOM   1930  O   HIS A 255      -1.268   1.832 -39.917  1.00161.33           O  
ANISOU 1930  O   HIS A 255    18353  25163  17784  -1508    175  -2498
ATOM   1931  CB  HIS A 255      -3.633   2.156 -42.106  1.00163.23           C  
ANISOU 1931  CB  HIS A 255    18391  25716  17913  -1733    268  -2695
ATOM   1932  N   PRO A 256      -0.830   3.553 -41.289  1.00158.85           N  
ANISOU 1932  N   PRO A 256    17608  25202  17546  -1359    263  -2451
ATOM   1933  CA  PRO A 256      -0.005   4.217 -40.266  1.00156.34           C  
ANISOU 1933  CA  PRO A 256    17201  24881  17319  -1286    279  -2270
ATOM   1934  C   PRO A 256      -0.761   4.567 -38.997  1.00154.92           C  
ANISOU 1934  C   PRO A 256    16993  24679  17191  -1418    342  -2132
ATOM   1935  O   PRO A 256      -0.136   4.670 -37.933  1.00153.47           O  
ANISOU 1935  O   PRO A 256    16851  24415  17046  -1401    337  -2006
ATOM   1936  CB  PRO A 256       0.503   5.474 -40.986  1.00155.79           C  
ANISOU 1936  CB  PRO A 256    16884  25007  17301  -1181    314  -2194
ATOM   1937  CG  PRO A 256      -0.497   5.723 -42.063  1.00157.69           C  
ANISOU 1937  CG  PRO A 256    17059  25355  17501  -1246    339  -2280
ATOM   1938  CD  PRO A 256      -0.960   4.368 -42.509  1.00159.83           C  
ANISOU 1938  CD  PRO A 256    17519  25541  17667  -1325    299  -2481
ATOM   1939  N   SER A 257      -2.086   4.715 -39.066  1.00153.64           N  
ANISOU 1939  N   SER A 257    16765  24599  17011  -1556    403  -2156
ATOM   1940  CA  SER A 257      -2.881   5.097 -37.904  1.00152.65           C  
ANISOU 1940  CA  SER A 257    16715  24366  16920  -1636    425  -2013
ATOM   1941  C   SER A 257      -2.769   4.112 -36.747  1.00152.83           C  
ANISOU 1941  C   SER A 257    16843  24330  16896  -1783    431  -2008
ATOM   1942  O   SER A 257      -3.285   4.400 -35.662  1.00152.09           O  
ANISOU 1942  O   SER A 257    16789  24179  16818  -1865    457  -1885
ATOM   1943  CB  SER A 257      -4.348   5.249 -38.311  1.00153.77           C  
ANISOU 1943  CB  SER A 257    16819  24584  17021  -1734    459  -2061
ATOM   1944  OG  SER A 257      -4.893   4.008 -38.723  1.00155.95           O  
ANISOU 1944  OG  SER A 257    17098  24975  17182  -1921    486  -2241
ATOM   1945  N   SER A 258      -2.115   2.968 -36.944  1.00151.80           N  
ANISOU 1945  N   SER A 258    16966  24005  16708  -1745    314  -2101
ATOM   1946  CA  SER A 258      -1.943   1.980 -35.890  1.00152.93           C  
ANISOU 1946  CA  SER A 258    17374  23934  16800  -1837    231  -2070
ATOM   1947  C   SER A 258      -0.486   1.714 -35.541  1.00152.24           C  
ANISOU 1947  C   SER A 258    17420  23697  16727  -1682    137  -2028
ATOM   1948  O   SER A 258      -0.225   0.899 -34.646  1.00152.18           O  
ANISOU 1948  O   SER A 258    17651  23495  16678  -1744     36  -1994
ATOM   1949  CB  SER A 258      -2.619   0.659 -36.285  1.00155.96           C  
ANISOU 1949  CB  SER A 258    18022  24164  17072  -1953    133  -2234
ATOM   1950  OG  SER A 258      -4.021   0.822 -36.416  1.00157.03           O  
ANISOU 1950  OG  SER A 258    18042  24451  17172  -2134    219  -2248
ATOM   1951  N   TYR A 259       0.468   2.376 -36.208  1.00152.41           N  
ANISOU 1951  N   TYR A 259    17291  23820  16798  -1491    154  -2023
ATOM   1952  CA  TYR A 259       1.880   2.081 -35.968  1.00152.07           C  
ANISOU 1952  CA  TYR A 259    17361  23675  16746  -1331     68  -1993
ATOM   1953  C   TYR A 259       2.244   2.249 -34.498  1.00149.78           C  
ANISOU 1953  C   TYR A 259    17119  23309  16483  -1406     58  -1794
ATOM   1954  O   TYR A 259       2.943   1.407 -33.923  1.00149.69           O  
ANISOU 1954  O   TYR A 259    17344  23110  16419  -1374    -70  -1786
ATOM   1955  CB  TYR A 259       2.774   2.973 -36.833  1.00151.90           C  
ANISOU 1955  CB  TYR A 259    17103  23844  16769  -1150    112  -1978
ATOM   1956  CG  TYR A 259       2.728   2.677 -38.316  1.00153.40           C  
ANISOU 1956  CG  TYR A 259    17277  24102  16905  -1058     97  -2178
ATOM   1957  CD1 TYR A 259       2.103   1.536 -38.801  1.00155.58           C  
ANISOU 1957  CD1 TYR A 259    17800  24226  17086  -1110     39  -2374
ATOM   1958  CD2 TYR A 259       3.336   3.530 -39.230  1.00152.44           C  
ANISOU 1958  CD2 TYR A 259    16915  24194  16812   -937    133  -2168
ATOM   1959  CE1 TYR A 259       2.065   1.265 -40.155  1.00157.15           C  
ANISOU 1959  CE1 TYR A 259    18010  24484  17218  -1041     37  -2561
ATOM   1960  CE2 TYR A 259       3.307   3.264 -40.585  1.00154.10           C  
ANISOU 1960  CE2 TYR A 259    17115  24483  16954   -873    119  -2346
ATOM   1961  CZ  TYR A 259       2.669   2.131 -41.042  1.00156.63           C  
ANISOU 1961  CZ  TYR A 259    17687  24647  17177   -924     80  -2546
ATOM   1962  OH  TYR A 259       2.633   1.862 -42.390  1.00159.19           O  
ANISOU 1962  OH  TYR A 259    18025  25044  17415   -875     80  -2730
ATOM   1963  N   THR A 260       1.776   3.330 -33.873  1.00149.14           N  
ANISOU 1963  N   THR A 260    16831  23363  16471  -1506    181  -1639
ATOM   1964  CA  THR A 260       2.078   3.553 -32.464  1.00147.96           C  
ANISOU 1964  CA  THR A 260    16730  23154  16334  -1604    187  -1446
ATOM   1965  C   THR A 260       1.345   2.559 -31.572  1.00149.13           C  
ANISOU 1965  C   THR A 260    17105  23147  16413  -1803    122  -1443
ATOM   1966  O   THR A 260       1.848   2.200 -30.501  1.00149.06           O  
ANISOU 1966  O   THR A 260    17245  23011  16381  -1871     43  -1316
ATOM   1967  CB  THR A 260       1.722   4.991 -32.077  1.00146.37           C  
ANISOU 1967  CB  THR A 260    16337  23060  16217  -1630    306  -1303
ATOM   1968  OG1 THR A 260       2.449   5.903 -32.909  1.00146.23           O  
ANISOU 1968  OG1 THR A 260    16277  23014  16272  -1414    277  -1271
ATOM   1969  CG2 THR A 260       2.072   5.269 -30.620  1.00144.88           C  
ANISOU 1969  CG2 THR A 260    16263  22743  16041  -1715    288  -1101
ATOM   1970  N   LYS A 261       0.177   2.082 -32.003  1.00148.11           N  
ANISOU 1970  N   LYS A 261    17004  23029  16240  -1913    138  -1571
ATOM   1971  CA  LYS A 261      -0.628   1.217 -31.147  1.00150.03           C  
ANISOU 1971  CA  LYS A 261    17434  23162  16409  -2140     85  -1551
ATOM   1972  C   LYS A 261      -0.130  -0.224 -31.173  1.00151.96           C  
ANISOU 1972  C   LYS A 261    18023  23124  16591  -2120   -148  -1651
ATOM   1973  O   LYS A 261       0.105  -0.825 -30.118  1.00152.72           O  
ANISOU 1973  O   LYS A 261    18301  23063  16662  -2234   -272  -1550
ATOM   1974  CB  LYS A 261      -2.097   1.286 -31.568  1.00151.42           C  
ANISOU 1974  CB  LYS A 261    17497  23486  16548  -2284    190  -1636
ATOM   1975  CG  LYS A 261      -2.742   2.645 -31.347  1.00150.53           C  
ANISOU 1975  CG  LYS A 261    17069  23635  16490  -2316    385  -1550
ATOM   1976  CD  LYS A 261      -4.202   2.641 -31.771  1.00152.34           C  
ANISOU 1976  CD  LYS A 261    17186  24031  16666  -2447    472  -1642
ATOM   1977  CE  LYS A 261      -4.875   3.970 -31.465  1.00151.20           C  
ANISOU 1977  CE  LYS A 261    16956  23880  16614  -2325    503  -1547
ATOM   1978  NZ  LYS A 261      -4.325   5.080 -32.293  1.00149.80           N1+
ANISOU 1978  NZ  LYS A 261    16720  23637  16559  -2049    468  -1535
ATOM   1979  N   VAL A 262       0.045  -0.787 -32.373  1.00142.03           N  
ANISOU 1979  N   VAL A 262    16866  21791  15308  -1976   -226  -1857
ATOM   1980  CA  VAL A 262       0.377  -2.206 -32.509  1.00144.47           C  
ANISOU 1980  CA  VAL A 262    17539  21800  15553  -1948   -470  -2009
ATOM   1981  C   VAL A 262       1.649  -2.535 -31.737  1.00143.75           C  
ANISOU 1981  C   VAL A 262    17603  21536  15481  -1842   -642  -1922
ATOM   1982  O   VAL A 262       1.665  -3.426 -30.879  1.00144.19           O  
ANISOU 1982  O   VAL A 262    17888  21365  15531  -1960   -852  -1892
ATOM   1983  CB  VAL A 262       0.509  -2.587 -33.993  1.00146.12           C  
ANISOU 1983  CB  VAL A 262    17827  21976  15717  -1778   -489  -2255
ATOM   1984  CG1 VAL A 262       0.953  -4.036 -34.130  1.00148.36           C  
ANISOU 1984  CG1 VAL A 262    18535  21905  15931  -1717   -753  -2446
ATOM   1985  CG2 VAL A 262      -0.805  -2.353 -34.719  1.00147.31           C  
ANISOU 1985  CG2 VAL A 262    17836  22289  15847  -1914   -358  -2327
ATOM   1986  N   ILE A 263       2.734  -1.813 -32.031  1.00140.49           N  
ANISOU 1986  N   ILE A 263    17043  21240  15098  -1629   -575  -1870
ATOM   1987  CA  ILE A 263       3.994  -2.043 -31.331  1.00139.91           C  
ANISOU 1987  CA  ILE A 263    17047  21100  15014  -1546   -721  -1779
ATOM   1988  C   ILE A 263       3.819  -1.861 -29.830  1.00138.64           C  
ANISOU 1988  C   ILE A 263    16896  20868  14913  -1739   -764  -1518
ATOM   1989  O   ILE A 263       4.449  -2.570 -29.034  1.00140.63           O  
ANISOU 1989  O   ILE A 263    17239  21086  15106  -1852   -955  -1477
ATOM   1990  CB  ILE A 263       5.092  -1.117 -31.893  1.00137.94           C  
ANISOU 1990  CB  ILE A 263    16575  21051  14785  -1306   -599  -1724
ATOM   1991  CG1 ILE A 263       5.352  -1.439 -33.365  1.00139.78           C  
ANISOU 1991  CG1 ILE A 263    16786  21387  14935  -1117   -554  -2005
ATOM   1992  CG2 ILE A 263       6.377  -1.250 -31.092  1.00138.66           C  
ANISOU 1992  CG2 ILE A 263    16616  21254  14814  -1275   -711  -1612
ATOM   1993  CD1 ILE A 263       6.227  -0.424 -34.064  1.00138.89           C  
ANISOU 1993  CD1 ILE A 263    16412  21494  14867   -902   -416  -1937
ATOM   1994  N   HIS A 264       2.942  -0.940 -29.416  1.00140.22           N  
ANISOU 1994  N   HIS A 264    16878  21264  15136  -1913   -535  -1387
ATOM   1995  CA  HIS A 264       2.729  -0.722 -27.990  1.00140.03           C  
ANISOU 1995  CA  HIS A 264    16841  21244  15119  -2139   -513  -1156
ATOM   1996  C   HIS A 264       2.207  -1.976 -27.303  1.00141.95           C  
ANISOU 1996  C   HIS A 264    17337  21268  15330  -2344   -721  -1170
ATOM   1997  O   HIS A 264       2.457  -2.178 -26.109  1.00141.99           O  
ANISOU 1997  O   HIS A 264    17408  21198  15344  -2500   -809   -979
ATOM   1998  CB  HIS A 264       1.767   0.444 -27.766  1.00138.96           C  
ANISOU 1998  CB  HIS A 264    16445  21363  14990  -2281   -228  -1067
ATOM   1999  CG  HIS A 264       1.547   0.771 -26.322  1.00138.63           C  
ANISOU 1999  CG  HIS A 264    16390  21357  14926  -2517   -165   -839
ATOM   2000  ND1 HIS A 264       2.500   1.399 -25.549  1.00137.17           N  
ANISOU 2000  ND1 HIS A 264    16160  21185  14775  -2503   -154   -640
ATOM   2001  CD2 HIS A 264       0.487   0.552 -25.508  1.00139.87           C  
ANISOU 2001  CD2 HIS A 264    16575  21558  15012  -2792   -103   -772
ATOM   2002  CE1 HIS A 264       2.035   1.556 -24.322  1.00138.07           C  
ANISOU 2002  CE1 HIS A 264    16285  21332  14842  -2760    -87   -466
ATOM   2003  NE2 HIS A 264       0.816   1.050 -24.271  1.00139.64           N  
ANISOU 2003  NE2 HIS A 264    16524  21565  14970  -2935    -50   -544
ATOM   2004  N   GLU A 265       1.482  -2.827 -28.031  1.00134.84           N  
ANISOU 2004  N   GLU A 265    16575  20260  14396  -2368   -807  -1382
ATOM   2005  CA  GLU A 265       1.115  -4.128 -27.483  1.00137.54           C  
ANISOU 2005  CA  GLU A 265    17168  20361  14731  -2560  -1055  -1422
ATOM   2006  C   GLU A 265       2.329  -5.045 -27.410  1.00140.05           C  
ANISOU 2006  C   GLU A 265    17627  20587  15001  -2582  -1330  -1511
ATOM   2007  O   GLU A 265       2.577  -5.682 -26.378  1.00141.78           O  
ANISOU 2007  O   GLU A 265    17945  20700  15225  -2828  -1515  -1370
ATOM   2008  CB  GLU A 265       0.006  -4.761 -28.324  1.00140.03           C  
ANISOU 2008  CB  GLU A 265    17578  20629  14996  -2636  -1061  -1632
ATOM   2009  CG  GLU A 265      -0.444  -6.140 -27.847  1.00144.12           C  
ANISOU 2009  CG  GLU A 265    18332  20951  15474  -2934  -1297  -1694
ATOM   2010  CD  GLU A 265      -1.115  -6.114 -26.484  1.00143.94           C  
ANISOU 2010  CD  GLU A 265    18281  20961  15450  -3222  -1253  -1426
ATOM   2011  OE1 GLU A 265      -1.673  -5.061 -26.109  1.00142.49           O  
ANISOU 2011  OE1 GLU A 265    17877  21069  15195  -3310   -960  -1263
ATOM   2012  OE2 GLU A 265      -1.091  -7.152 -25.790  1.00146.40           O1-
ANISOU 2012  OE2 GLU A 265    18775  21112  15738  -3512  -1465  -1376
ATOM   2013  N   CYS A 266       3.106  -5.108 -28.494  1.00131.76           N  
ANISOU 2013  N   CYS A 266    16578  19588  13898  -2341  -1357  -1736
ATOM   2014  CA  CYS A 266       4.267  -5.992 -28.546  1.00135.37           C  
ANISOU 2014  CA  CYS A 266    17150  19999  14283  -2332  -1620  -1888
ATOM   2015  C   CYS A 266       5.214  -5.718 -27.386  1.00134.91           C  
ANISOU 2015  C   CYS A 266    16986  20011  14263  -2409  -1731  -1571
ATOM   2016  O   CYS A 266       5.478  -6.599 -26.558  1.00137.64           O  
ANISOU 2016  O   CYS A 266    17477  20185  14634  -2676  -2014  -1469
ATOM   2017  CB  CYS A 266       4.992  -5.822 -29.881  1.00135.73           C  
ANISOU 2017  CB  CYS A 266    17128  20209  14235  -1993  -1523  -2175
ATOM   2018  SG  CYS A 266       4.030  -6.312 -31.323  1.00139.00           S  
ANISOU 2018  SG  CYS A 266    17714  20500  14600  -1916  -1422  -2541
ATOM   2019  N   GLN A 267       5.716  -4.484 -27.296  1.00136.26           N  
ANISOU 2019  N   GLN A 267    16921  20386  14465  -2210  -1521  -1368
ATOM   2020  CA  GLN A 267       6.629  -4.123 -26.219  1.00135.56           C  
ANISOU 2020  CA  GLN A 267    16726  20361  14419  -2267  -1602  -1032
ATOM   2021  C   GLN A 267       5.996  -4.288 -24.846  1.00135.14           C  
ANISOU 2021  C   GLN A 267    16767  20141  14439  -2602  -1637   -763
ATOM   2022  O   GLN A 267       6.716  -4.293 -23.844  1.00135.33           O  
ANISOU 2022  O   GLN A 267    16767  20150  14502  -2728  -1762   -466
ATOM   2023  CB  GLN A 267       7.106  -2.678 -26.385  1.00131.81           C  
ANISOU 2023  CB  GLN A 267    16025  20070  13988  -2026  -1328   -876
ATOM   2024  CG  GLN A 267       6.013  -1.642 -26.171  1.00128.12           C  
ANISOU 2024  CG  GLN A 267    15517  19543  13619  -2057  -1037   -793
ATOM   2025  CD  GLN A 267       6.510  -0.220 -26.342  1.00124.74           C  
ANISOU 2025  CD  GLN A 267    14904  19218  13271  -1864   -813   -660
ATOM   2026  OE1 GLN A 267       7.694   0.012 -26.592  1.00124.69           O  
ANISOU 2026  OE1 GLN A 267    14791  19346  13238  -1713   -848   -601
ATOM   2027  NE2 GLN A 267       5.607   0.743 -26.195  1.00123.79           N  
ANISOU 2027  NE2 GLN A 267    14624  19262  13150  -2011   -542   -611
ATOM   2028  N   GLN A 268       4.671  -4.414 -24.776  1.00130.52           N  
ANISOU 2028  N   GLN A 268    16269  19460  13863  -2747  -1518   -834
ATOM   2029  CA  GLN A 268       3.999  -4.600 -23.500  1.00130.77           C  
ANISOU 2029  CA  GLN A 268    16374  19399  13913  -3067  -1511   -593
ATOM   2030  C   GLN A 268       3.941  -6.062 -23.079  1.00135.48           C  
ANISOU 2030  C   GLN A 268    17207  19763  14506  -3391  -1841   -584
ATOM   2031  O   GLN A 268       3.806  -6.345 -21.882  1.00137.55           O  
ANISOU 2031  O   GLN A 268    17549  19934  14778  -3687  -1909   -299
ATOM   2032  CB  GLN A 268       2.580  -4.021 -23.565  1.00128.85           C  
ANISOU 2032  CB  GLN A 268    16077  19221  13661  -3079  -1229   -638
ATOM   2033  CG  GLN A 268       1.869  -3.925 -22.225  1.00128.89           C  
ANISOU 2033  CG  GLN A 268    16106  19238  13630  -3372  -1136   -385
ATOM   2034  CD  GLN A 268       2.484  -2.877 -21.318  1.00127.21           C  
ANISOU 2034  CD  GLN A 268    15770  19173  13392  -3416   -977   -111
ATOM   2035  OE1 GLN A 268       2.822  -1.780 -21.760  1.00125.55           O  
ANISOU 2035  OE1 GLN A 268    15381  19129  13192  -3235   -785   -128
ATOM   2036  NE2 GLN A 268       2.636  -3.213 -20.042  1.00128.20           N  
ANISOU 2036  NE2 GLN A 268    15996  19228  13484  -3678  -1061    155
ATOM   2037  N   ARG A 269       4.063  -6.994 -24.024  1.00132.25           N  
ANISOU 2037  N   ARG A 269    16944  19221  14084  -3360  -2053   -882
ATOM   2038  CA  ARG A 269       3.984  -8.422 -23.730  1.00137.09           C  
ANISOU 2038  CA  ARG A 269    17852  19499  14738  -3689  -2400   -898
ATOM   2039  C   ARG A 269       5.331  -9.123 -23.756  1.00140.50           C  
ANISOU 2039  C   ARG A 269    18414  19733  15237  -3709  -2803   -866
ATOM   2040  O   ARG A 269       5.558 -10.039 -22.963  1.00144.48           O  
ANISOU 2040  O   ARG A 269    19152  19879  15867  -4022  -3145   -631
ATOM   2041  CB  ARG A 269       3.037  -9.111 -24.720  1.00138.64           C  
ANISOU 2041  CB  ARG A 269    18216  19565  14894  -3701  -2394  -1263
ATOM   2042  CG  ARG A 269       1.606  -8.626 -24.618  1.00136.56           C  
ANISOU 2042  CG  ARG A 269    17847  19457  14585  -3747  -2096  -1221
ATOM   2043  CD  ARG A 269       0.977  -9.064 -23.308  1.00138.59           C  
ANISOU 2043  CD  ARG A 269    18198  19623  14835  -4140  -2145   -907
ATOM   2044  NE  ARG A 269      -0.423  -8.660 -23.217  1.00138.39           N  
ANISOU 2044  NE  ARG A 269    18073  19783  14726  -4202  -1878   -882
ATOM   2045  CZ  ARG A 269      -0.837  -7.525 -22.665  1.00135.40           C  
ANISOU 2045  CZ  ARG A 269    17479  19664  14303  -4130  -1582   -708
ATOM   2046  NH1 ARG A 269       0.042  -6.680 -22.144  1.00133.16           N  
ANISOU 2046  NH1 ARG A 269    17070  19471  14054  -3996  -1503   -540
ATOM   2047  NH2 ARG A 269      -2.131  -7.236 -22.627  1.00134.89           N1+
ANISOU 2047  NH2 ARG A 269    17335  19761  14157  -4206  -1374   -705
ATOM   2048  N   MET A 270       6.233  -8.723 -24.654  1.00124.09           N  
ANISOU 2048  N   MET A 270    16199  17863  13088  -3377  -2797  -1064
ATOM   2049  CA  MET A 270       7.577  -9.286 -24.651  1.00127.27           C  
ANISOU 2049  CA  MET A 270    16622  17936  13801  -3008  -2942   -907
ATOM   2050  C   MET A 270       8.444  -8.644 -23.578  1.00125.60           C  
ANISOU 2050  C   MET A 270    16181  17888  13652  -3045  -3008   -411
ATOM   2051  O   MET A 270       9.291  -9.319 -22.981  1.00128.48           O  
ANISOU 2051  O   MET A 270    16618  17862  14337  -2934  -3209    -99
ATOM   2052  CB  MET A 270       8.216  -9.113 -26.028  1.00127.65           C  
ANISOU 2052  CB  MET A 270    16535  18071  13895  -2388  -2699  -1255
ATOM   2053  CG  MET A 270       7.454  -9.815 -27.136  1.00129.63           C  
ANISOU 2053  CG  MET A 270    17039  18123  14090  -2331  -2641  -1754
ATOM   2054  SD  MET A 270       8.137  -9.520 -28.776  1.00131.13           S  
ANISOU 2054  SD  MET A 270    17058  18506  14261  -1654  -2328  -2185
ATOM   2055  CE  MET A 270       9.592 -10.557 -28.744  1.00139.08           C  
ANISOU 2055  CE  MET A 270    18135  18952  15756  -1087  -2433  -2063
ATOM   2056  N   VAL A 271       8.245  -7.351 -23.326  1.00129.86           N  
ANISOU 2056  N   VAL A 271    16461  18974  13907  -3183  -2841   -328
ATOM   2057  CA  VAL A 271       8.891  -6.628 -22.241  1.00127.98           C  
ANISOU 2057  CA  VAL A 271    16046  18832  13750  -3199  -2785    134
ATOM   2058  C   VAL A 271       7.778  -6.065 -21.362  1.00125.37           C  
ANISOU 2058  C   VAL A 271    15765  18471  13398  -3408  -2452    240
ATOM   2059  O   VAL A 271       6.622  -5.974 -21.779  1.00124.31           O  
ANISOU 2059  O   VAL A 271    15688  18346  13198  -3415  -2232    -17
ATOM   2060  CB  VAL A 271       9.823  -5.510 -22.766  1.00125.29           C  
ANISOU 2060  CB  VAL A 271    15384  18866  13354  -2791  -2576    162
ATOM   2061  CG1 VAL A 271      10.578  -4.826 -21.633  1.00123.84           C  
ANISOU 2061  CG1 VAL A 271    15072  18709  13271  -2830  -2528    633
ATOM   2062  CG2 VAL A 271      10.793  -6.065 -23.797  1.00128.14           C  
ANISOU 2062  CG2 VAL A 271    15665  19161  13860  -2312  -2637      2
ATOM   2063  N   ALA A 272       8.125  -5.759 -20.108  1.00132.16           N  
ANISOU 2063  N   ALA A 272    16608  19295  14313  -3587  -2445    648
ATOM   2064  CA  ALA A 272       7.220  -5.138 -19.142  1.00130.09           C  
ANISOU 2064  CA  ALA A 272    16381  19062  13985  -3778  -2138    787
ATOM   2065  C   ALA A 272       6.148  -6.116 -18.677  1.00132.63           C  
ANISOU 2065  C   ALA A 272    16935  19188  14269  -4123  -2236    787
ATOM   2066  O   ALA A 272       5.379  -5.816 -17.757  1.00132.10           O  
ANISOU 2066  O   ALA A 272    16916  19168  14107  -4324  -2039    945
ATOM   2067  CB  ALA A 272       6.567  -3.879 -19.721  1.00125.62           C  
ANISOU 2067  CB  ALA A 272    15661  18715  13356  -3513  -1715    556
ATOM   2068  N   ASP A 273       6.096  -7.288 -19.303  1.00130.71           N  
ANISOU 2068  N   ASP A 273    16854  18724  14086  -4200  -2546    611
ATOM   2069  CA  ASP A 273       5.230  -8.374 -18.878  1.00134.24           C  
ANISOU 2069  CA  ASP A 273    17563  18913  14528  -4554  -2705    645
ATOM   2070  C   ASP A 273       5.992  -9.401 -18.053  1.00138.42           C  
ANISOU 2070  C   ASP A 273    18301  19076  15215  -4846  -3161   1006
ATOM   2071  O   ASP A 273       5.374 -10.293 -17.463  1.00142.30           O  
ANISOU 2071  O   ASP A 273    19038  19321  15708  -5179  -3316   1139
ATOM   2072  CB  ASP A 273       4.598  -9.044 -20.107  1.00135.93           C  
ANISOU 2072  CB  ASP A 273    17889  19019  14737  -4482  -2763    212
ATOM   2073  CG  ASP A 273       3.368  -9.864 -19.770  1.00139.03           C  
ANISOU 2073  CG  ASP A 273    18497  19253  15077  -4803  -2778    209
ATOM   2074  OD1 ASP A 273       2.971  -9.905 -18.588  1.00140.71           O  
ANISOU 2074  OD1 ASP A 273    18764  19477  15222  -5075  -2738    535
ATOM   2075  OD2 ASP A 273       2.793 -10.468 -20.701  1.00140.40           O1-
ANISOU 2075  OD2 ASP A 273    18791  19308  15247  -4783  -2825   -118
ATOM   2076  N   HIS A 274       7.321  -9.279 -17.997  1.00128.82           N  
ANISOU 2076  N   HIS A 274    16981  17818  14146  -4714  -3397   1207
ATOM   2077  CA  HIS A 274       8.183 -10.171 -17.233  1.00133.46           C  
ANISOU 2077  CA  HIS A 274    17723  18015  14969  -4934  -3889   1617
ATOM   2078  C   HIS A 274       9.192  -9.376 -16.413  1.00131.52           C  
ANISOU 2078  C   HIS A 274    17257  17954  14760  -4861  -3841   2033
ATOM   2079  O   HIS A 274      10.197  -9.936 -15.964  1.00135.39           O  
ANISOU 2079  O   HIS A 274    17764  18177  15502  -4913  -4271   2400
ATOM   2080  CB  HIS A 274       8.924 -11.130 -18.168  1.00138.03           C  
ANISOU 2080  CB  HIS A 274    18423  18189  15834  -4712  -4324   1455
ATOM   2081  CG  HIS A 274       8.029 -11.881 -19.103  1.00139.32           C  
ANISOU 2081  CG  HIS A 274    18849  18109  15977  -4698  -4297    991
ATOM   2082  ND1 HIS A 274       7.244 -12.939 -18.701  1.00142.85           N  
ANISOU 2082  ND1 HIS A 274    19663  18157  16455  -5162  -4572   1022
ATOM   2083  CD2 HIS A 274       7.798 -11.722 -20.428  1.00138.33           C  
ANISOU 2083  CD2 HIS A 274    18683  18093  15784  -4306  -4040    496
ATOM   2084  CE1 HIS A 274       6.567 -13.400 -19.738  1.00144.52           C  
ANISOU 2084  CE1 HIS A 274    20055  18234  16622  -5055  -4487    563
ATOM   2085  NE2 HIS A 274       6.885 -12.679 -20.798  1.00141.46           N  
ANISOU 2085  NE2 HIS A 274    19424  18150  16173  -4535  -4162    233
ATOM   2086  N   LEU A 275       8.936  -8.080 -16.208  1.00132.83           N  
ANISOU 2086  N   LEU A 275    17229  18522  14717  -4730  -3344   1991
ATOM   2087  CA  LEU A 275       9.989  -7.146 -15.820  1.00130.65           C  
ANISOU 2087  CA  LEU A 275    16725  18441  14476  -4561  -3236   2255
ATOM   2088  C   LEU A 275      10.669  -7.506 -14.503  1.00132.96           C  
ANISOU 2088  C   LEU A 275    17104  18524  14890  -4847  -3484   2806
ATOM   2089  O   LEU A 275      11.773  -7.013 -14.245  1.00133.00           O  
ANISOU 2089  O   LEU A 275    16918  18605  15011  -4713  -3511   3068
ATOM   2090  CB  LEU A 275       9.428  -5.719 -15.774  1.00125.74           C  
ANISOU 2090  CB  LEU A 275    15971  18159  13646  -4426  -2678   2087
ATOM   2091  CG  LEU A 275       8.223  -5.363 -14.897  1.00124.87           C  
ANISOU 2091  CG  LEU A 275    15998  18113  13332  -4675  -2374   2117
ATOM   2092  CD1 LEU A 275       8.629  -5.038 -13.466  1.00125.17           C  
ANISOU 2092  CD1 LEU A 275    16107  18139  13313  -4930  -2348   2569
ATOM   2093  CD2 LEU A 275       7.462  -4.197 -15.514  1.00120.38           C  
ANISOU 2093  CD2 LEU A 275    15280  17802  12657  -4422  -1930   1771
ATOM   2094  N   GLN A 276      10.056  -8.352 -13.668  1.00124.48           N  
ANISOU 2094  N   GLN A 276    16312  17198  13786  -5227  -3660   3003
ATOM   2095  CA  GLN A 276      10.777  -8.849 -12.499  1.00127.81           C  
ANISOU 2095  CA  GLN A 276    16843  17378  14342  -5491  -3981   3555
ATOM   2096  C   GLN A 276      12.062  -9.555 -12.909  1.00131.08           C  
ANISOU 2096  C   GLN A 276    17134  17498  15173  -5331  -4506   3753
ATOM   2097  O   GLN A 276      13.104  -9.390 -12.263  1.00132.10           O  
ANISOU 2097  O   GLN A 276    17128  17586  15478  -5327  -4638   4169
ATOM   2098  CB  GLN A 276       9.903  -9.796 -11.675  1.00131.61           C  
ANISOU 2098  CB  GLN A 276    17673  17639  14694  -5867  -4160   3718
ATOM   2099  CG  GLN A 276       8.792  -9.136 -10.883  1.00129.47           C  
ANISOU 2099  CG  GLN A 276    17502  17710  13979  -6005  -3736   3688
ATOM   2100  CD  GLN A 276       8.060 -10.130  -9.996  1.00133.33           C  
ANISOU 2100  CD  GLN A 276    18302  18061  14298  -6340  -3979   3889
ATOM   2101  OE1 GLN A 276       8.331 -11.332 -10.036  1.00137.57           O  
ANISOU 2101  OE1 GLN A 276    19003  18190  15079  -6480  -4448   4026
ATOM   2102  NE2 GLN A 276       7.140  -9.630  -9.179  1.00131.77           N  
ANISOU 2102  NE2 GLN A 276    18062  18157  13849  -6331  -3631   3701
ATOM   2103  N   PHE A 277      12.005 -10.343 -13.985  1.00115.98           N  
ANISOU 2103  N   PHE A 277    15263  15373  13433  -5157  -4821   3457
ATOM   2104  CA  PHE A 277      13.180 -11.080 -14.440  1.00120.13           C  
ANISOU 2104  CA  PHE A 277    15727  15515  14400  -4693  -5143   3595
ATOM   2105  C   PHE A 277      14.296 -10.131 -14.862  1.00118.29           C  
ANISOU 2105  C   PHE A 277    15097  15651  14198  -4176  -4923   3663
ATOM   2106  O   PHE A 277      15.427 -10.220 -14.364  1.00120.86           O  
ANISOU 2106  O   PHE A 277    15276  15867  14779  -4000  -5093   4098
ATOM   2107  CB  PHE A 277      12.783 -12.017 -15.583  1.00122.72           C  
ANISOU 2107  CB  PHE A 277    16279  15427  14921  -4327  -5101   3113
ATOM   2108  CG  PHE A 277      13.917 -12.839 -16.120  1.00127.83           C  
ANISOU 2108  CG  PHE A 277    16919  15586  16066  -3653  -5210   3145
ATOM   2109  CD1 PHE A 277      14.462 -13.868 -15.368  1.00133.42           C  
ANISOU 2109  CD1 PHE A 277    17818  15721  17155  -3705  -5613   3554
ATOM   2110  CD2 PHE A 277      14.420 -12.604 -17.389  1.00127.24           C  
ANISOU 2110  CD2 PHE A 277    16647  15625  16074  -2963  -4916   2758
ATOM   2111  CE1 PHE A 277      15.503 -14.632 -15.862  1.00139.26           C  
ANISOU 2111  CE1 PHE A 277    18540  16002  18372  -3036  -5715   3568
ATOM   2112  CE2 PHE A 277      15.459 -13.367 -17.891  1.00136.00           C  
ANISOU 2112  CE2 PHE A 277    17727  16314  17632  -2312  -4994   2757
ATOM   2113  CZ  PHE A 277      16.001 -14.383 -17.125  1.00142.70           C  
ANISOU 2113  CZ  PHE A 277    18758  16582  18880  -2326  -5392   3155
ATOM   2114  N   LEU A 278      13.993  -9.207 -15.778  1.00110.64           N  
ANISOU 2114  N   LEU A 278    18900  14206   8932  -4744    142     12
ATOM   2115  CA  LEU A 278      14.997  -8.247 -16.224  1.00110.35           C  
ANISOU 2115  CA  LEU A 278    18655  14258   9015  -4231    116    211
ATOM   2116  C   LEU A 278      15.566  -7.468 -15.046  1.00109.44           C  
ANISOU 2116  C   LEU A 278    18550  14044   8990  -4409    107    277
ATOM   2117  O   LEU A 278      16.789  -7.397 -14.868  1.00107.82           O  
ANISOU 2117  O   LEU A 278    18486  13628   8854  -4155    -67    507
ATOM   2118  CB  LEU A 278      14.392  -7.302 -17.262  1.00112.02           C  
ANISOU 2118  CB  LEU A 278    18411  14893   9259  -3946    310    138
ATOM   2119  CG  LEU A 278      14.015  -7.950 -18.594  1.00112.87           C  
ANISOU 2119  CG  LEU A 278    18470  15151   9262  -3658    294     99
ATOM   2120  CD1 LEU A 278      13.290  -6.961 -19.490  1.00115.09           C  
ANISOU 2120  CD1 LEU A 278    18330  15854   9544  -3462    453     20
ATOM   2121  CD2 LEU A 278      15.254  -8.496 -19.287  1.00111.88           C  
ANISOU 2121  CD2 LEU A 278    18516  14881   9111  -3212    111    344
ATOM   2122  N   HIS A 279      14.688  -6.896 -14.213  1.00115.67           N  
ANISOU 2122  N   HIS A 279    19176  15004   9769  -4863    294     41
ATOM   2123  CA  HIS A 279      15.143  -6.183 -13.022  1.00114.19           C  
ANISOU 2123  CA  HIS A 279    18997  14765   9627  -5094    297     46
ATOM   2124  C   HIS A 279      16.033  -7.055 -12.146  1.00111.10           C  
ANISOU 2124  C   HIS A 279    19084  13951   9178  -5254     23    222
ATOM   2125  O   HIS A 279      16.932  -6.542 -11.469  1.00109.73           O  
ANISOU 2125  O   HIS A 279    18966  13663   9061  -5198    -82    342
ATOM   2126  CB  HIS A 279      13.946  -5.677 -12.212  1.00113.94           C  
ANISOU 2126  CB  HIS A 279    18726  15013   9552  -5651    557   -312
ATOM   2127  CG  HIS A 279      13.191  -4.563 -12.869  1.00117.69           C  
ANISOU 2127  CG  HIS A 279    18708  15906  10103  -5509    785   -549
ATOM   2128  ND1 HIS A 279      12.160  -4.782 -13.757  1.00120.09           N  
ANISOU 2128  ND1 HIS A 279    18809  16435  10386  -5464    897   -744
ATOM   2129  CD2 HIS A 279      13.309  -3.219 -12.757  1.00119.83           C  
ANISOU 2129  CD2 HIS A 279    18664  16408  10459  -5424    897   -649
ATOM   2130  CE1 HIS A 279      11.682  -3.621 -14.169  1.00123.13           C  
ANISOU 2130  CE1 HIS A 279    18777  17166  10841  -5344   1039   -967
ATOM   2131  NE2 HIS A 279      12.361  -2.657 -13.575  1.00123.07           N  
ANISOU 2131  NE2 HIS A 279    18699  17166  10895  -5333   1048   -918
ATOM   2132  N   ALA A 280      15.809  -8.372 -12.154  1.00107.58           N  
ANISOU 2132  N   ALA A 280    19009  13255   8612  -5466   -120    245
ATOM   2133  CA  ALA A 280      16.632  -9.265 -11.345  1.00106.35           C  
ANISOU 2133  CA  ALA A 280    19375  12652   8381  -5649   -446    416
ATOM   2134  C   ALA A 280      18.015  -9.455 -11.956  1.00106.13           C  
ANISOU 2134  C   ALA A 280    19485  12384   8454  -5050   -728    653
ATOM   2135  O   ALA A 280      19.019  -9.467 -11.235  1.00105.04           O  
ANISOU 2135  O   ALA A 280    19580  11983   8347  -5019   -976    789
ATOM   2136  CB  ALA A 280      15.930 -10.611 -11.168  1.00106.95           C  
ANISOU 2136  CB  ALA A 280    19857  12499   8281  -6123   -535    386
ATOM   2137  N   GLU A 281      18.092  -9.608 -13.280  1.00109.54           N  
ANISOU 2137  N   GLU A 281    19763  12930   8926  -4583   -695    690
ATOM   2138  CA  GLU A 281      19.395  -9.732 -13.926  1.00109.14           C  
ANISOU 2138  CA  GLU A 281    19783  12727   8959  -4029   -919    886
ATOM   2139  C   GLU A 281      20.155  -8.412 -13.985  1.00107.98           C  
ANISOU 2139  C   GLU A 281    19265  12780   8983  -3682   -803   1014
ATOM   2140  O   GLU A 281      21.358  -8.420 -14.281  1.00108.00           O  
ANISOU 2140  O   GLU A 281    19324  12642   9069  -3289   -989   1188
ATOM   2141  CB  GLU A 281      19.232 -10.298 -15.337  1.00110.29           C  
ANISOU 2141  CB  GLU A 281    19869  12996   9042  -3677   -901    861
ATOM   2142  CG  GLU A 281      18.739 -11.739 -15.378  1.00111.52           C  
ANISOU 2142  CG  GLU A 281    20475  12862   9036  -3953  -1100    775
ATOM   2143  CD  GLU A 281      19.760 -12.730 -14.844  1.00112.15           C  
ANISOU 2143  CD  GLU A 281    21133  12387   9094  -3964  -1578    900
ATOM   2144  OE1 GLU A 281      20.974 -12.481 -15.008  1.00112.25           O  
ANISOU 2144  OE1 GLU A 281    21140  12303   9205  -3537  -1771   1018
ATOM   2145  OE2 GLU A 281      19.348 -13.759 -14.262  1.00112.88           O1-
ANISOU 2145  OE2 GLU A 281    21700  12117   9072  -4413  -1789    889
ATOM   2146  N   CYS A 282      19.487  -7.287 -13.710  1.00101.54           N  
ANISOU 2146  N   CYS A 282    18090  12271   8221  -3839   -518    926
ATOM   2147  CA  CYS A 282      20.161  -5.991 -13.745  1.00100.79           C  
ANISOU 2147  CA  CYS A 282    17674  12325   8296  -3565   -416   1078
ATOM   2148  C   CYS A 282      21.327  -5.938 -12.765  1.00 99.77           C  
ANISOU 2148  C   CYS A 282    17772  11900   8238  -3571   -658   1209
ATOM   2149  O   CYS A 282      22.422  -5.492 -13.122  1.00 99.78           O  
ANISOU 2149  O   CYS A 282    17666  11854   8392  -3174   -729   1425
ATOM   2150  CB  CYS A 282      19.164  -4.870 -13.458  1.00101.35           C  
ANISOU 2150  CB  CYS A 282    17407  12718   8384  -3829   -126    915
ATOM   2151  SG  CYS A 282      17.981  -4.581 -14.784  1.00103.68           S  
ANISOU 2151  SG  CYS A 282    17351  13399   8645  -3694    123    806
ATOM   2152  N   HIS A 283      21.109  -6.386 -11.521  1.00 97.34           N  
ANISOU 2152  N   HIS A 283    17774  11398   7813  -4042   -791   1087
ATOM   2153  CA  HIS A 283      22.178  -6.384 -10.521  1.00 96.68           C  
ANISOU 2153  CA  HIS A 283    17941  11029   7764  -4076  -1069   1196
ATOM   2154  C   HIS A 283      23.464  -6.992 -11.064  1.00 97.64           C  
ANISOU 2154  C   HIS A 283    18254  10855   7989  -3604  -1390   1394
ATOM   2155  O   HIS A 283      24.559  -6.475 -10.817  1.00 97.94           O  
ANISOU 2155  O   HIS A 283    18249  10787   8178  -3354  -1529   1541
ATOM   2156  CB  HIS A 283      21.739  -7.144  -9.270  1.00 96.22           C  
ANISOU 2156  CB  HIS A 283    18289  10762   7507  -4672  -1231   1070
ATOM   2157  CG  HIS A 283      22.779  -7.175  -8.192  1.00 95.87           C  
ANISOU 2157  CG  HIS A 283    18532  10430   7464  -4742  -1556   1174
ATOM   2158  ND1 HIS A 283      23.809  -8.092  -8.180  1.00 97.11           N  
ANISOU 2158  ND1 HIS A 283    19074  10162   7660  -4519  -1998   1319
ATOM   2159  CD2 HIS A 283      22.942  -6.414  -7.085  1.00 95.29           C  
ANISOU 2159  CD2 HIS A 283    18427  10431   7348  -5018  -1533   1135
ATOM   2160  CE1 HIS A 283      24.566  -7.888  -7.118  1.00 97.25           C  
ANISOU 2160  CE1 HIS A 283    19277   9999   7674  -4634  -2246   1376
ATOM   2161  NE2 HIS A 283      24.061  -6.877  -6.435  1.00 96.49           N  
ANISOU 2161  NE2 HIS A 283    18940  10210   7514  -4946  -1958   1277
ATOM   2162  N   ASN A 284      23.349  -8.099 -11.798  1.00105.93           N  
ANISOU 2162  N   ASN A 284    19526  11762   8961  -3490  -1530   1378
ATOM   2163  CA  ASN A 284      24.518  -8.695 -12.433  1.00108.01           C  
ANISOU 2163  CA  ASN A 284    19963  11773   9302  -3024  -1850   1505
ATOM   2164  C   ASN A 284      25.023  -7.824 -13.576  1.00109.70           C  
ANISOU 2164  C   ASN A 284    19735  12301   9645  -2523  -1623   1635
ATOM   2165  O   ASN A 284      26.224  -7.544 -13.674  1.00111.68           O  
ANISOU 2165  O   ASN A 284    19957  12435  10042  -2176  -1798   1778
ATOM   2166  CB  ASN A 284      24.179 -10.099 -12.938  1.00109.52           C  
ANISOU 2166  CB  ASN A 284    20535  11731   9346  -3064  -2075   1422
ATOM   2167  CG  ASN A 284      25.398 -10.856 -13.437  1.00112.34           C  
ANISOU 2167  CG  ASN A 284    21166  11749   9768  -2609  -2530   1483
ATOM   2168  OD1 ASN A 284      26.519 -10.352 -13.398  1.00113.45           O  
ANISOU 2168  OD1 ASN A 284    21197  11834  10075  -2261  -2674   1587
ATOM   2169  ND2 ASN A 284      25.178 -12.072 -13.923  1.00113.99           N  
ANISOU 2169  ND2 ASN A 284    21735  11717   9859  -2598  -2793   1393
ATOM   2170  N   ILE A 285      24.117  -7.377 -14.449  1.00102.65           N  
ANISOU 2170  N   ILE A 285    18496  11802   8703  -2497  -1251   1595
ATOM   2171  CA  ILE A 285      24.561  -6.778 -15.705  1.00103.92           C  
ANISOU 2171  CA  ILE A 285    18304  12258   8923  -2053  -1070   1743
ATOM   2172  C   ILE A 285      25.249  -5.433 -15.482  1.00103.75           C  
ANISOU 2172  C   ILE A 285    17938  12333   9151  -1917   -931   1946
ATOM   2173  O   ILE A 285      26.205  -5.099 -16.193  1.00106.49           O  
ANISOU 2173  O   ILE A 285    17930  12771   9762  -1488   -896   2026
ATOM   2174  CB  ILE A 285      23.378  -6.673 -16.683  1.00104.48           C  
ANISOU 2174  CB  ILE A 285    18107  12712   8879  -2073   -760   1652
ATOM   2175  CG1 ILE A 285      22.881  -8.074 -17.031  1.00105.52           C  
ANISOU 2175  CG1 ILE A 285    18576  12718   8799  -2151   -927   1459
ATOM   2176  CG2 ILE A 285      23.792  -5.967 -17.955  1.00106.59           C  
ANISOU 2176  CG2 ILE A 285    17979  13326   9193  -1671   -557   1830
ATOM   2177  CD1 ILE A 285      21.610  -8.093 -17.827  1.00106.23           C  
ANISOU 2177  CD1 ILE A 285    18444  13143   8776  -2228   -668   1321
ATOM   2178  N   ILE A 286      24.806  -4.644 -14.497  1.00 99.13           N  
ANISOU 2178  N   ILE A 286    17269  11752   8644  -2239   -822   1925
ATOM   2179  CA  ILE A 286      25.460  -3.358 -14.253  1.00 99.52           C  
ANISOU 2179  CA  ILE A 286    16927  11849   9037  -2099   -709   2072
ATOM   2180  C   ILE A 286      26.793  -3.507 -13.538  1.00100.21           C  
ANISOU 2180  C   ILE A 286    17153  11613   9307  -1950  -1011   2118
ATOM   2181  O   ILE A 286      27.571  -2.546 -13.500  1.00102.23           O  
ANISOU 2181  O   ILE A 286    17011  11896   9937  -1734   -936   2214
ATOM   2182  CB  ILE A 286      24.553  -2.384 -13.472  1.00 98.37           C  
ANISOU 2182  CB  ILE A 286    16616  11832   8930  -2476   -508   1984
ATOM   2183  CG1 ILE A 286      24.083  -2.982 -12.142  1.00 97.12           C  
ANISOU 2183  CG1 ILE A 286    16899  11513   8491  -2976   -660   1777
ATOM   2184  CG2 ILE A 286      23.363  -1.954 -14.319  1.00 99.40           C  
ANISOU 2184  CG2 ILE A 286    16439  12292   9035  -2505   -225   1925
ATOM   2185  CD1 ILE A 286      24.968  -2.666 -10.957  1.00 96.17           C  
ANISOU 2185  CD1 ILE A 286    16936  11157   8448  -3087   -867   1828
ATOM   2186  N   ARG A 287      27.083  -4.681 -12.972  1.00 93.65           N  
ANISOU 2186  N   ARG A 287    16879  10454   8251  -2060  -1387   2054
ATOM   2187  CA  ARG A 287      28.393  -4.968 -12.405  1.00 95.63           C  
ANISOU 2187  CA  ARG A 287    17278  10360   8699  -1849  -1767   2070
ATOM   2188  C   ARG A 287      29.271  -5.751 -13.374  1.00 98.26           C  
ANISOU 2188  C   ARG A 287    17546  10612   9177  -1359  -1956   2002
ATOM   2189  O   ARG A 287      30.269  -6.352 -12.965  1.00100.44           O  
ANISOU 2189  O   ARG A 287    18035  10537   9590  -1169  -2381   1934
ATOM   2190  CB  ARG A 287      28.243  -5.700 -11.072  1.00 95.80           C  
ANISOU 2190  CB  ARG A 287    17889  10040   8472  -2268  -2129   2007
ATOM   2191  CG  ARG A 287      27.567  -4.830 -10.027  1.00 94.38           C  
ANISOU 2191  CG  ARG A 287    17602  10022   8236  -2715  -1910   1944
ATOM   2192  CD  ARG A 287      27.450  -5.490  -8.670  1.00 95.14           C  
ANISOU 2192  CD  ARG A 287    18135   9873   8140  -3148  -2207   1810
ATOM   2193  NE  ARG A 287      26.624  -4.689  -7.767  1.00 94.38           N  
ANISOU 2193  NE  ARG A 287    17934  10024   7904  -3627  -1949   1693
ATOM   2194  CZ  ARG A 287      27.079  -3.698  -7.007  1.00 94.80           C  
ANISOU 2194  CZ  ARG A 287    17875  10116   8030  -3706  -1941   1739
ATOM   2195  NH1 ARG A 287      28.365  -3.371  -7.036  1.00 95.76           N  
ANISOU 2195  NH1 ARG A 287    17954  10021   8410  -3323  -2178   1923
ATOM   2196  NH2 ARG A 287      26.246  -3.029  -6.220  1.00 94.79           N1+
ANISOU 2196  NH2 ARG A 287    17795  10371   7850  -4182  -1703   1578
ATOM   2197  N   GLN A 288      28.895  -5.763 -14.649  1.00105.23           N  
ANISOU 2197  N   GLN A 288    18125  11828  10029  -1155  -1669   1979
ATOM   2198  CA  GLN A 288      29.763  -6.136 -15.758  1.00111.89           C  
ANISOU 2198  CA  GLN A 288    18676  12786  11050   -667  -1692   1871
ATOM   2199  C   GLN A 288      29.866  -4.949 -16.701  1.00113.54           C  
ANISOU 2199  C   GLN A 288    18236  13467  11439   -484  -1229   2010
ATOM   2200  O   GLN A 288      28.846  -4.436 -17.172  1.00109.89           O  
ANISOU 2200  O   GLN A 288    17635  13295  10823   -651   -915   2125
ATOM   2201  CB  GLN A 288      29.235  -7.369 -16.494  1.00114.71           C  
ANISOU 2201  CB  GLN A 288    19305  13140  11140   -620  -1811   1699
ATOM   2202  CG  GLN A 288      29.862  -7.594 -17.873  1.00121.62           C  
ANISOU 2202  CG  GLN A 288    19753  14330  12128   -157  -1689   1534
ATOM   2203  CD  GLN A 288      31.379  -7.629 -17.861  1.00127.79           C  
ANISOU 2203  CD  GLN A 288    20279  14992  13282    239  -1902   1377
ATOM   2204  OE1 GLN A 288      32.035  -6.673 -18.283  1.00131.10           O  
ANISOU 2204  OE1 GLN A 288    20168  15725  13919    411  -1611   1456
ATOM   2205  NE2 GLN A 288      31.946  -8.731 -17.383  1.00129.40           N  
ANISOU 2205  NE2 GLN A 288    20853  14728  13584    374  -2436   1144
ATOM   2206  N   GLU A 289      31.097  -4.517 -16.975  1.00114.01           N  
ANISOU 2206  N   GLU A 289    17900  13589  11829   -162  -1213   1999
ATOM   2207  CA  GLU A 289      31.315  -3.387 -17.867  1.00117.67           C  
ANISOU 2207  CA  GLU A 289    17774  14479  12457    -39   -801   2182
ATOM   2208  C   GLU A 289      30.831  -3.669 -19.284  1.00119.55           C  
ANISOU 2208  C   GLU A 289    17835  15150  12437     74   -554   2173
ATOM   2209  O   GLU A 289      30.726  -2.733 -20.086  1.00121.49           O  
ANISOU 2209  O   GLU A 289    17674  15773  12715     84   -217   2399
ATOM   2210  CB  GLU A 289      32.801  -3.017 -17.879  1.00125.39           C  
ANISOU 2210  CB  GLU A 289    18375  15452  13816    244   -840   2120
ATOM   2211  CG  GLU A 289      33.375  -2.641 -16.508  1.00122.87           C  
ANISOU 2211  CG  GLU A 289    18175  14731  13778    161  -1095   2122
ATOM   2212  CD  GLU A 289      32.803  -1.355 -15.941  1.00117.44           C  
ANISOU 2212  CD  GLU A 289    17345  14065  13212   -122   -872   2380
ATOM   2213  OE1 GLU A 289      32.475  -0.448 -16.733  1.00118.36           O  
ANISOU 2213  OE1 GLU A 289    17078  14505  13388   -144   -516   2596
ATOM   2214  OE2 GLU A 289      32.686  -1.250 -14.700  1.00111.96           O1-
ANISOU 2214  OE2 GLU A 289    16922  13061  12556   -330  -1083   2353
ATOM   2215  N   LYS A 290      30.533  -4.924 -19.608  1.00116.38           N  
ANISOU 2215  N   LYS A 290    17743  14693  11783    144   -742   1927
ATOM   2216  CA  LYS A 290      30.003  -5.293 -20.914  1.00117.42           C  
ANISOU 2216  CA  LYS A 290    17739  15245  11631    239   -536   1864
ATOM   2217  C   LYS A 290      28.481  -5.409 -20.873  1.00111.59           C  
ANISOU 2217  C   LYS A 290    17288  14525  10588    -64   -465   1945
ATOM   2218  O   LYS A 290      27.914  -5.932 -19.911  1.00107.31           O  
ANISOU 2218  O   LYS A 290    17201  13614   9960   -314   -691   1876
ATOM   2219  CB  LYS A 290      30.620  -6.610 -21.386  1.00120.90           C  
ANISOU 2219  CB  LYS A 290    18273  15635  12029    534   -792   1463
ATOM   2220  CG  LYS A 290      30.131  -7.075 -22.745  1.00120.87           C  
ANISOU 2220  CG  LYS A 290    18113  16098  11714    646   -594   1324
ATOM   2221  CD  LYS A 290      30.648  -6.179 -23.850  1.00123.68           C  
ANISOU 2221  CD  LYS A 290    17882  17060  12053    771   -190   1463
ATOM   2222  CE  LYS A 290      30.255  -6.716 -25.212  1.00125.11           C  
ANISOU 2222  CE  LYS A 290    17912  17753  11873    882    -20   1283
ATOM   2223  NZ  LYS A 290      30.704  -5.819 -26.310  1.00128.00           N1+
ANISOU 2223  NZ  LYS A 290    17748  18761  12126    915    381   1476
ATOM   2224  N   ASN A 292      27.256  -3.922 -23.481  1.00111.26           N  
ANISOU 2224  N   ASN A 292    16490  15600  10184    -29    252   2375
ATOM   2225  CA  ASN A 292      26.330  -4.128 -24.590  1.00109.68           C  
ANISOU 2225  CA  ASN A 292    16242  15796   9635    -31    387   2374
ATOM   2226  C   ASN A 292      24.995  -4.639 -24.060  1.00106.26           C  
ANISOU 2226  C   ASN A 292    16181  15146   9046   -271    270   2233
ATOM   2227  O   ASN A 292      23.931  -4.071 -24.344  1.00104.42           O  
ANISOU 2227  O   ASN A 292    15871  15079   8726   -415    381   2364
ATOM   2228  CB  ASN A 292      26.919  -5.111 -25.605  1.00113.64           C  
ANISOU 2228  CB  ASN A 292    16661  16609   9907    231    389   2086
ATOM   2229  CG  ASN A 292      26.132  -5.159 -26.903  1.00112.52           C  
ANISOU 2229  CG  ASN A 292    16385  16987   9381    246    561   2116
ATOM   2230  OD1 ASN A 292      25.122  -4.473 -27.060  1.00108.65           O  
ANISOU 2230  OD1 ASN A 292    15877  16592   8812     78    644   2366
ATOM   2231  ND2 ASN A 292      26.598  -5.970 -27.845  1.00116.17           N  
ANISOU 2231  ND2 ASN A 292    16729  17798   9614    459    590   1820
ATOM   2232  N   ASP A 293      25.071  -5.722 -23.283  1.00118.45           N  
ANISOU 2232  N   ASP A 293    18129  16308  10567   -329     19   1954
ATOM   2233  CA  ASP A 293      23.879  -6.270 -22.647  1.00115.50           C  
ANISOU 2233  CA  ASP A 293    18146  15711  10028   -645    -87   1811
ATOM   2234  C   ASP A 293      23.176  -5.208 -21.812  1.00112.59           C  
ANISOU 2234  C   ASP A 293    17723  15253   9804   -943     18   1984
ATOM   2235  O   ASP A 293      21.941  -5.164 -21.752  1.00111.07           O  
ANISOU 2235  O   ASP A 293    17596  15136   9469  -1188     85   1903
ATOM   2236  CB  ASP A 293      24.264  -7.464 -21.775  1.00116.28           C  
ANISOU 2236  CB  ASP A 293    18725  15334  10122   -718   -425   1580
ATOM   2237  CG  ASP A 293      24.936  -8.569 -22.566  1.00119.87           C  
ANISOU 2237  CG  ASP A 293    19210  15822  10514   -391   -593   1315
ATOM   2238  OD1 ASP A 293      24.679  -8.671 -23.785  1.00121.65           O  
ANISOU 2238  OD1 ASP A 293    19182  16482  10557   -215   -421   1234
ATOM   2239  OD2 ASP A 293      25.719  -9.338 -21.968  1.00121.40           O1-
ANISOU 2239  OD2 ASP A 293    19671  15607  10849   -307   -927   1160
ATOM   2240  N   MET A 294      23.955  -4.335 -21.171  1.00102.59           N  
ANISOU 2240  N   MET A 294    16292  13841   8848   -920     29   2169
ATOM   2241  CA  MET A 294      23.388  -3.273 -20.350  1.00100.19           C  
ANISOU 2241  CA  MET A 294    15877  13447   8743  -1173    111   2273
ATOM   2242  C   MET A 294      22.795  -2.163 -21.207  1.00100.49           C  
ANISOU 2242  C   MET A 294    15489  13808   8883  -1103    308   2476
ATOM   2243  O   MET A 294      21.795  -1.546 -20.816  1.00100.38           O  
ANISOU 2243  O   MET A 294    15391  13790   8958  -1318    354   2426
ATOM   2244  CB  MET A 294      24.470  -2.743 -19.408  1.00 99.27           C  
ANISOU 2244  CB  MET A 294    15717  13056   8945  -1150     25   2374
ATOM   2245  CG  MET A 294      24.020  -1.704 -18.410  1.00 97.43           C  
ANISOU 2245  CG  MET A 294    15370  12701   8949  -1411     77   2404
ATOM   2246  SD  MET A 294      25.336  -1.364 -17.227  1.00 96.46           S  
ANISOU 2246  SD  MET A 294    15282  12234   9135  -1392    -81   2452
ATOM   2247  CE  MET A 294      26.534  -0.543 -18.273  1.00 99.18           C  
ANISOU 2247  CE  MET A 294    15117  12764   9801   -983     49   2741
ATOM   2248  N   ALA A 295      23.384  -1.907 -22.378  1.00 94.86           N  
ANISOU 2248  N   ALA A 295    14502  13387   8154   -822    403   2687
ATOM   2249  CA  ALA A 295      22.791  -0.961 -23.318  1.00 95.11           C  
ANISOU 2249  CA  ALA A 295    14201  13720   8216   -771    522   2934
ATOM   2250  C   ALA A 295      21.415  -1.434 -23.769  1.00 95.36           C  
ANISOU 2250  C   ALA A 295    14342  13924   7967   -872    512   2738
ATOM   2251  O   ALA A 295      20.440  -0.672 -23.738  1.00 95.73           O  
ANISOU 2251  O   ALA A 295    14227  13996   8150   -983    510   2766
ATOM   2252  CB  ALA A 295      23.716  -0.764 -24.518  1.00 96.38           C  
ANISOU 2252  CB  ALA A 295    14110  14221   8290   -525    632   3194
ATOM   2253  N   ASN A 296      21.316  -2.699 -24.190  1.00 97.26           N  
ANISOU 2253  N   ASN A 296    14831  14269   7853   -824    481   2496
ATOM   2254  CA  ASN A 296      20.007  -3.252 -24.527  1.00 97.66           C  
ANISOU 2254  CA  ASN A 296    15003  14460   7645   -948    465   2255
ATOM   2255  C   ASN A 296      19.071  -3.238 -23.324  1.00 97.02           C  
ANISOU 2255  C   ASN A 296    15092  14109   7661  -1302    426   2014
ATOM   2256  O   ASN A 296      17.861  -3.027 -23.481  1.00 98.64           O  
ANISOU 2256  O   ASN A 296    15203  14447   7830  -1438    449   1865
ATOM   2257  CB  ASN A 296      20.159  -4.672 -25.074  1.00 98.40           C  
ANISOU 2257  CB  ASN A 296    15347  14645   7397   -845    410   1996
ATOM   2258  CG  ASN A 296      20.743  -4.700 -26.476  1.00 99.99           C  
ANISOU 2258  CG  ASN A 296    15311  15281   7399   -539    492   2128
ATOM   2259  OD1 ASN A 296      20.360  -3.907 -27.336  1.00100.12           O  
ANISOU 2259  OD1 ASN A 296    15049  15545   7448   -450    573   2316
ATOM   2260  ND2 ASN A 296      21.679  -5.612 -26.711  1.00101.26           N  
ANISOU 2260  ND2 ASN A 296    15568  15448   7458   -360    445   1956
ATOM   2261  N   MET A 297      19.613  -3.450 -22.121  1.00 95.12           N  
ANISOU 2261  N   MET A 297    15084  13522   7533  -1472    362   1947
ATOM   2262  CA  MET A 297      18.808  -3.360 -20.906  1.00 94.74           C  
ANISOU 2262  CA  MET A 297    15182  13282   7533  -1875    358   1717
ATOM   2263  C   MET A 297      18.145  -1.993 -20.781  1.00 96.44           C  
ANISOU 2263  C   MET A 297    14983  13591   8068  -1923    442   1752
ATOM   2264  O   MET A 297      16.934  -1.896 -20.541  1.00 98.92           O  
ANISOU 2264  O   MET A 297    15232  13996   8357  -2168    484   1466
ATOM   2265  CB  MET A 297      19.679  -3.653 -19.685  1.00 93.43           C  
ANISOU 2265  CB  MET A 297    15272  12749   7477  -2001    246   1699
ATOM   2266  CG  MET A 297      18.936  -3.590 -18.367  1.00 93.40           C  
ANISOU 2266  CG  MET A 297    15405  12592   7489  -2459    253   1443
ATOM   2267  SD  MET A 297      17.635  -4.820 -18.231  1.00 94.28           S  
ANISOU 2267  SD  MET A 297    15739  12708   7374  -2789    241   1036
ATOM   2268  CE  MET A 297      18.596  -6.299 -17.968  1.00 93.57           C  
ANISOU 2268  CE  MET A 297    16100  12242   7210  -2726    -24   1056
ATOM   2269  N   TYR A 298      18.928  -0.921 -20.933  1.00 93.52           N  
ANISOU 2269  N   TYR A 298    14307  13187   8038  -1698    446   2067
ATOM   2270  CA  TYR A 298      18.355   0.423 -20.950  1.00 98.16           C  
ANISOU 2270  CA  TYR A 298    14481  13808   9009  -1687    452   2127
ATOM   2271  C   TYR A 298      17.307   0.565 -22.047  1.00102.76           C  
ANISOU 2271  C   TYR A 298    14872  14667   9504  -1584    430   2104
ATOM   2272  O   TYR A 298      16.199   1.061 -21.802  1.00109.65           O  
ANISOU 2272  O   TYR A 298    15544  15566  10551  -1721    399   1843
ATOM   2273  CB  TYR A 298      19.459   1.465 -21.136  1.00 96.08           C  
ANISOU 2273  CB  TYR A 298    13950  13447   9108  -1454    433   2538
ATOM   2274  CG  TYR A 298      18.945   2.885 -21.275  1.00100.81           C  
ANISOU 2274  CG  TYR A 298    14126  14013  10166  -1405    364   2656
ATOM   2275  CD1 TYR A 298      18.534   3.612 -20.165  1.00105.33           C  
ANISOU 2275  CD1 TYR A 298    14528  14379  11114  -1594    330   2395
ATOM   2276  CD2 TYR A 298      18.862   3.493 -22.523  1.00101.13           C  
ANISOU 2276  CD2 TYR A 298    13938  14222  10264  -1181    298   3014
ATOM   2277  CE1 TYR A 298      18.063   4.910 -20.294  1.00111.07           C  
ANISOU 2277  CE1 TYR A 298    14841  15019  12341  -1515    204   2451
ATOM   2278  CE2 TYR A 298      18.389   4.788 -22.662  1.00105.72           C  
ANISOU 2278  CE2 TYR A 298    14162  14692  11313  -1128    144   3149
ATOM   2279  CZ  TYR A 298      17.993   5.492 -21.545  1.00110.85           C  
ANISOU 2279  CZ  TYR A 298    14622  15086  12411  -1273     83   2848
ATOM   2280  OH  TYR A 298      17.525   6.780 -21.680  1.00115.64           O  
ANISOU 2280  OH  TYR A 298    14848  15529  13561  -1188   -128   2932
ATOM   2281  N   VAL A 299      17.647   0.141 -23.270  1.00 94.48           N  
ANISOU 2281  N   VAL A 299    13858  13851   8187  -1339    432   2337
ATOM   2282  CA  VAL A 299      16.742   0.310 -24.407  1.00 97.84           C  
ANISOU 2282  CA  VAL A 299    14112  14566   8497  -1217    374   2368
ATOM   2283  C   VAL A 299      15.373  -0.284 -24.100  1.00102.51           C  
ANISOU 2283  C   VAL A 299    14786  15217   8946  -1448    369   1875
ATOM   2284  O   VAL A 299      14.334   0.345 -24.335  1.00108.76           O  
ANISOU 2284  O   VAL A 299    15311  16093   9921  -1452    278   1741
ATOM   2285  CB  VAL A 299      17.349  -0.312 -25.677  1.00 94.71           C  
ANISOU 2285  CB  VAL A 299    13798  14475   7713   -981    409   2600
ATOM   2286  CG1 VAL A 299      16.344  -0.278 -26.818  1.00 97.51           C  
ANISOU 2286  CG1 VAL A 299    14028  15156   7867   -885    326   2593
ATOM   2287  CG2 VAL A 299      18.619   0.421 -26.071  1.00 92.86           C  
ANISOU 2287  CG2 VAL A 299    13402  14261   7622   -803    443   3075
ATOM   2288  N   LEU A 300      15.351  -1.502 -23.557  1.00100.10           N  
ANISOU 2288  N   LEU A 300    14846  14852   8336  -1659    442   1583
ATOM   2289  CA  LEU A 300      14.072  -2.166 -23.327  1.00101.84           C  
ANISOU 2289  CA  LEU A 300    15163  15160   8371  -1937    466   1117
ATOM   2290  C   LEU A 300      13.360  -1.626 -22.092  1.00103.81           C  
ANISOU 2290  C   LEU A 300    15289  15277   8878  -2288    512    777
ATOM   2291  O   LEU A 300      12.150  -1.384 -22.133  1.00107.58           O  
ANISOU 2291  O   LEU A 300    15535  15904   9436  -2416    509    425
ATOM   2292  CB  LEU A 300      14.275  -3.675 -23.216  1.00 99.40           C  
ANISOU 2292  CB  LEU A 300    15313  14801   7651  -2082    491    949
ATOM   2293  CG  LEU A 300      14.706  -4.348 -24.521  1.00 99.04           C  
ANISOU 2293  CG  LEU A 300    15326  14967   7339  -1747    450   1098
ATOM   2294  CD1 LEU A 300      15.028  -5.812 -24.285  1.00 97.52           C  
ANISOU 2294  CD1 LEU A 300    15440  14536   7075  -1755    399    873
ATOM   2295  CD2 LEU A 300      13.628  -4.193 -25.586  1.00101.98           C  
ANISOU 2295  CD2 LEU A 300    15463  15689   7597  -1642    422    987
ATOM   2296  N   LEU A 301      14.083  -1.428 -20.987  1.00 98.17           N  
ANISOU 2296  N   LEU A 301    14693  14313   8293  -2451    551    826
ATOM   2297  CA  LEU A 301      13.435  -0.926 -19.780  1.00 98.56           C  
ANISOU 2297  CA  LEU A 301    14607  14301   8540  -2822    618    450
ATOM   2298  C   LEU A 301      12.893   0.487 -19.947  1.00 99.56           C  
ANISOU 2298  C   LEU A 301    14178  14474   9177  -2655    545    385
ATOM   2299  O   LEU A 301      12.009   0.890 -19.183  1.00100.73           O  
ANISOU 2299  O   LEU A 301    14093  14675   9506  -2936    596    -87
ATOM   2300  CB  LEU A 301      14.399  -0.955 -18.595  1.00 97.52           C  
ANISOU 2300  CB  LEU A 301    14715  13911   8425  -3011    643    542
ATOM   2301  CG  LEU A 301      14.819  -2.307 -18.027  1.00 97.34           C  
ANISOU 2301  CG  LEU A 301    15280  13748   7957  -3292    640    522
ATOM   2302  CD1 LEU A 301      15.867  -2.104 -16.950  1.00 96.65           C  
ANISOU 2302  CD1 LEU A 301    15367  13394   7961  -3390    592    673
ATOM   2303  CD2 LEU A 301      13.615  -3.040 -17.467  1.00 98.91           C  
ANISOU 2303  CD2 LEU A 301    15665  14077   7839  -3825    743     57
ATOM   2304  N   ARG A 302      13.399   1.249 -20.923  1.00107.34           N  
ANISOU 2304  N   ARG A 302    14937  15441  10405  -2228    408    826
ATOM   2305  CA  ARG A 302      13.000   2.650 -21.039  1.00114.43           C  
ANISOU 2305  CA  ARG A 302    15342  16275  11862  -2060    251    830
ATOM   2306  C   ARG A 302      11.566   2.790 -21.540  1.00119.62           C  
ANISOU 2306  C   ARG A 302    15718  17130  12603  -2057    146    440
ATOM   2307  O   ARG A 302      10.823   3.660 -21.070  1.00119.37           O  
ANISOU 2307  O   ARG A 302    15285  17046  13025  -2111     49     70
ATOM   2308  CB  ARG A 302      13.961   3.398 -21.960  1.00114.33           C  
ANISOU 2308  CB  ARG A 302    15222  16171  12045  -1672    110   1476
ATOM   2309  CG  ARG A 302      13.691   4.890 -22.034  1.00121.25           C  
ANISOU 2309  CG  ARG A 302    15638  16872  13560  -1507   -122   1564
ATOM   2310  CD  ARG A 302      14.683   5.588 -22.943  1.00116.90           C  
ANISOU 2310  CD  ARG A 302    15038  16234  13146  -1214   -252   2266
ATOM   2311  NE  ARG A 302      14.517   5.192 -24.337  1.00113.60           N  
ANISOU 2311  NE  ARG A 302    14722  16089  12350  -1031   -324   2574
ATOM   2312  CZ  ARG A 302      15.364   5.516 -25.308  1.00107.70           C  
ANISOU 2312  CZ  ARG A 302    14006  15409  11506   -847   -377   3187
ATOM   2313  NH1 ARG A 302      16.441   6.242 -25.034  1.00104.54           N  
ANISOU 2313  NH1 ARG A 302    13534  14792  11396   -820   -363   3561
ATOM   2314  NH2 ARG A 302      15.137   5.114 -26.552  1.00105.38           N1+
ANISOU 2314  NH2 ARG A 302    13803  15433  10803   -722   -431   3406
ATOM   2315  N   ALA A 303      11.153   1.943 -22.482  1.00112.75           N  
ANISOU 2315  N   ALA A 303    15019  16491  11330  -1985    145    458
ATOM   2316  CA  ALA A 303       9.809   2.004 -23.045  1.00116.12           C  
ANISOU 2316  CA  ALA A 303    15181  17123  11815  -1956     19     82
ATOM   2317  C   ALA A 303       8.768   1.328 -22.161  1.00112.80           C  
ANISOU 2317  C   ALA A 303    14770  16841  11249  -2404    205   -640
ATOM   2318  O   ALA A 303       7.679   0.989 -22.640  1.00113.23           O  
ANISOU 2318  O   ALA A 303    14691  17118  11212  -2440    162  -1014
ATOM   2319  CB  ALA A 303       9.794   1.381 -24.443  1.00115.36           C  
ANISOU 2319  CB  ALA A 303    15250  17255  11328  -1704    -63    375
ATOM   2320  N   VAL A 304       9.089   1.134 -20.887  1.00123.83           N  
ANISOU 2320  N   VAL A 304    16319  18130  12599  -2774    407   -841
ATOM   2321  CA  VAL A 304       8.233   0.451 -19.928  1.00119.14           C  
ANISOU 2321  CA  VAL A 304    15798  17693  11775  -3318    628  -1476
ATOM   2322  C   VAL A 304       7.676   1.478 -18.955  1.00117.30           C  
ANISOU 2322  C   VAL A 304    15089  17466  12012  -3505    647  -1985
ATOM   2323  O   VAL A 304       8.281   2.531 -18.725  1.00118.39           O  
ANISOU 2323  O   VAL A 304    14995  17391  12598  -3275    522  -1773
ATOM   2324  CB  VAL A 304       9.033  -0.651 -19.197  1.00115.37           C  
ANISOU 2324  CB  VAL A 304    15921  17110  10805  -3662    814  -1308
ATOM   2325  CG1 VAL A 304       8.228  -1.287 -18.070  1.00110.96           C  
ANISOU 2325  CG1 VAL A 304    15489  16703   9967  -4334   1043  -1897
ATOM   2326  CG2 VAL A 304       9.492  -1.704 -20.189  1.00114.85           C  
ANISOU 2326  CG2 VAL A 304    16260  17042  10335  -3456    764   -933
ATOM   2327  N   SER A 305       6.497   1.180 -18.404  1.00125.24           N  
ANISOU 2327  N   SER A 305    15911  18737  12937  -3934    805  -2708
ATOM   2328  CA  SER A 305       5.936   2.002 -17.338  1.00121.42           C  
ANISOU 2328  CA  SER A 305    14964  18341  12827  -4209    885  -3339
ATOM   2329  C   SER A 305       6.950   2.211 -16.217  1.00118.90           C  
ANISOU 2329  C   SER A 305    14860  17847  12468  -4422   1007  -3149
ATOM   2330  O   SER A 305       7.308   3.347 -15.888  1.00119.33           O  
ANISOU 2330  O   SER A 305    14556  17733  13049  -4205    879  -3146
ATOM   2331  CB  SER A 305       4.661   1.354 -16.796  1.00117.69           C  
ANISOU 2331  CB  SER A 305    14375  18256  12086  -4790   1138  -4145
ATOM   2332  OG  SER A 305       4.958   0.140 -16.129  1.00114.72           O  
ANISOU 2332  OG  SER A 305    14610  17943  11036  -5348   1412  -4060
ATOM   2333  N   THR A 306       7.426   1.116 -15.615  1.00117.07           N  
ANISOU 2333  N   THR A 306    15224  17626  11630  -4850   1215  -2990
ATOM   2334  CA  THR A 306       8.439   1.167 -14.556  1.00114.41           C  
ANISOU 2334  CA  THR A 306    15176  17119  11176  -5067   1291  -2771
ATOM   2335  C   THR A 306       9.547   0.172 -14.901  1.00115.99           C  
ANISOU 2335  C   THR A 306    16052  17074  10945  -4956   1233  -2081
ATOM   2336  O   THR A 306       9.538  -0.967 -14.430  1.00112.77           O  
ANISOU 2336  O   THR A 306    16160  16699   9988  -5412   1349  -2098
ATOM   2337  CB  THR A 306       7.821   0.866 -13.186  1.00110.16           C  
ANISOU 2337  CB  THR A 306    14669  16863  10322  -5828   1571  -3402
ATOM   2338  OG1 THR A 306       7.257  -0.451 -13.196  1.00109.04           O  
ANISOU 2338  OG1 THR A 306    14831  16768   9830  -6059   1747  -3255
ATOM   2339  CG2 THR A 306       6.734   1.875 -12.849  1.00109.41           C  
ANISOU 2339  CG2 THR A 306    13795  17013  10761  -5811   1646  -4099
ATOM   2340  N   GLY A 307      10.500   0.605 -15.725  1.00108.01           N  
ANISOU 2340  N   GLY A 307    15026  15815  10197  -4369   1036  -1495
ATOM   2341  CA  GLY A 307      11.633  -0.240 -16.054  1.00105.85           C  
ANISOU 2341  CA  GLY A 307    15294  15325   9598  -4213    967   -920
ATOM   2342  C   GLY A 307      12.964   0.242 -15.513  1.00104.29           C  
ANISOU 2342  C   GLY A 307    15193  14852   9582  -4055    891   -536
ATOM   2343  O   GLY A 307      13.786  -0.559 -15.057  1.00103.50           O  
ANISOU 2343  O   GLY A 307    15587  14582   9154  -4194    868   -303
ATOM   2344  N   LEU A 308      13.177   1.555 -15.546  1.00 98.89           N  
ANISOU 2344  N   LEU A 308    14029  14092   9452  -3764    815   -487
ATOM   2345  CA  LEU A 308      14.456   2.192 -15.233  1.00 97.09           C  
ANISOU 2345  CA  LEU A 308    13788  13599   9503  -3532    726   -102
ATOM   2346  C   LEU A 308      14.833   2.306 -13.752  1.00 94.58           C  
ANISOU 2346  C   LEU A 308    13587  13208   9142  -3917    793   -322
ATOM   2347  O   LEU A 308      16.029   2.219 -13.442  1.00 92.61           O  
ANISOU 2347  O   LEU A 308    13578  12733   8875  -3808    717     32
ATOM   2348  CB  LEU A 308      14.487   3.583 -15.871  1.00 99.59           C  
ANISOU 2348  CB  LEU A 308    13549  13829  10462  -3105    585     49
ATOM   2349  CG  LEU A 308      14.549   3.553 -17.401  1.00101.83           C  
ANISOU 2349  CG  LEU A 308    13793  14145  10753  -2677    467    478
ATOM   2350  CD1 LEU A 308      14.387   4.939 -17.985  1.00105.79           C  
ANISOU 2350  CD1 LEU A 308    13779  14543  11874  -2344    271    620
ATOM   2351  CD2 LEU A 308      15.859   2.939 -17.861  1.00 97.79           C  
ANISOU 2351  CD2 LEU A 308    13651  13527   9979  -2471    464   1019
ATOM   2352  N   PRO A 309      13.894   2.518 -12.812  1.00102.66           N  
ANISOU 2352  N   PRO A 309    14425  14442  10141  -4370    929   -921
ATOM   2353  CA  PRO A 309      14.328   2.866 -11.442  1.00 99.23           C  
ANISOU 2353  CA  PRO A 309    14014  13974   9715  -4698    978  -1124
ATOM   2354  C   PRO A 309      15.251   1.846 -10.790  1.00 96.63           C  
ANISOU 2354  C   PRO A 309    14355  13493   8866  -4945    940   -820
ATOM   2355  O   PRO A 309      16.246   2.240 -10.167  1.00 95.46           O  
ANISOU 2355  O   PRO A 309    14253  13152   8864  -4872    848   -639
ATOM   2356  CB  PRO A 309      13.002   3.002 -10.679  1.00 97.62           C  
ANISOU 2356  CB  PRO A 309    13533  14138   9422  -5224   1177  -1888
ATOM   2357  CG  PRO A 309      12.031   2.204 -11.452  1.00 99.11           C  
ANISOU 2357  CG  PRO A 309    13821  14519   9317  -5314   1250  -2012
ATOM   2358  CD  PRO A 309      12.427   2.377 -12.880  1.00103.00           C  
ANISOU 2358  CD  PRO A 309    14234  14806  10093  -4658   1061  -1493
ATOM   2359  N   HIS A 310      14.956   0.549 -10.906  1.00103.30           N  
ANISOU 2359  N   HIS A 310    15720  14387   9142  -5232    966   -768
ATOM   2360  CA  HIS A 310      15.829  -0.457 -10.307  1.00100.90           C  
ANISOU 2360  CA  HIS A 310    16087  13863   8387  -5450    834   -465
ATOM   2361  C   HIS A 310      17.222  -0.406 -10.924  1.00100.13           C  
ANISOU 2361  C   HIS A 310    16079  13425   8542  -4856    615     88
ATOM   2362  O   HIS A 310      18.232  -0.435 -10.212  1.00 98.24           O  
ANISOU 2362  O   HIS A 310    16074  12966   8286  -4866    467    277
ATOM   2363  CB  HIS A 310      15.213  -1.848 -10.466  1.00101.24           C  
ANISOU 2363  CB  HIS A 310    16465  13840   8163  -5676    797   -490
ATOM   2364  CG  HIS A 310      15.933  -2.927  -9.714  1.00 98.52           C  
ANISOU 2364  CG  HIS A 310    16592  13105   7736  -5812    553   -261
ATOM   2365  ND1 HIS A 310      16.991  -3.633 -10.249  1.00 96.64           N  
ANISOU 2365  ND1 HIS A 310    16658  12518   7541  -5384    275    116
ATOM   2366  CD2 HIS A 310      15.742  -3.424  -8.469  1.00 97.90           C  
ANISOU 2366  CD2 HIS A 310    16721  12946   7532  -6348    543   -364
ATOM   2367  CE1 HIS A 310      17.423  -4.513  -9.364  1.00 95.07           C  
ANISOU 2367  CE1 HIS A 310    16862  12017   7241  -5642     62    193
ATOM   2368  NE2 HIS A 310      16.681  -4.409  -8.276  1.00 95.70           N  
ANISOU 2368  NE2 HIS A 310    16918  12242   7202  -6243    214    -55
ATOM   2369  N   MET A 311      17.290  -0.315 -12.253  1.00 88.79           N  
ANISOU 2369  N   MET A 311    14432  11974   7328  -4353    592    326
ATOM   2370  CA  MET A 311      18.579  -0.257 -12.934  1.00 86.93           C  
ANISOU 2370  CA  MET A 311    14218  11503   7310  -3823    434    799
ATOM   2371  C   MET A 311      19.391   0.945 -12.467  1.00 86.84           C  
ANISOU 2371  C   MET A 311    13851  11365   7781  -3625    400    896
ATOM   2372  O   MET A 311      20.578   0.820 -12.137  1.00 85.42           O  
ANISOU 2372  O   MET A 311    13856  10955   7646  -3483    256   1140
ATOM   2373  CB  MET A 311      18.359  -0.210 -14.445  1.00 87.38           C  
ANISOU 2373  CB  MET A 311    14038  11675   7487  -3394    462    985
ATOM   2374  CG  MET A 311      19.624  -0.254 -15.273  1.00 85.63           C  
ANISOU 2374  CG  MET A 311    13818  11312   7406  -2903    351   1423
ATOM   2375  SD  MET A 311      19.235  -0.273 -17.030  1.00 86.52           S  
ANISOU 2375  SD  MET A 311    13690  11665   7516  -2510    404   1607
ATOM   2376  CE  MET A 311      20.872  -0.221 -17.747  1.00 84.90           C  
ANISOU 2376  CE  MET A 311    13442  11359   7457  -2044    327   2050
ATOM   2377  N   ILE A 312      18.757   2.120 -12.421  1.00 94.19           N  
ANISOU 2377  N   ILE A 312    14249  12422   9118  -3608    502    672
ATOM   2378  CA  ILE A 312      19.438   3.330 -11.961  1.00 94.99           C  
ANISOU 2378  CA  ILE A 312    13972  12380   9739  -3441    455    718
ATOM   2379  C   ILE A 312      19.947   3.141 -10.538  1.00 91.84           C  
ANISOU 2379  C   ILE A 312    13843  11896   9156  -3792    411    557
ATOM   2380  O   ILE A 312      21.102   3.462 -10.221  1.00 90.70           O  
ANISOU 2380  O   ILE A 312    13701  11534   9226  -3601    290    784
ATOM   2381  CB  ILE A 312      18.494   4.542 -12.065  1.00100.22           C  
ANISOU 2381  CB  ILE A 312    14030  13162  10887  -3410    516    403
ATOM   2382  CG1 ILE A 312      18.094   4.785 -13.521  1.00105.42           C  
ANISOU 2382  CG1 ILE A 312    14453  13867  11735  -3034    481    648
ATOM   2383  CG2 ILE A 312      19.144   5.780 -11.472  1.00100.97           C  
ANISOU 2383  CG2 ILE A 312    13737  13075  11553  -3283    443    388
ATOM   2384  CD1 ILE A 312      16.964   5.771 -13.683  1.00111.71           C  
ANISOU 2384  CD1 ILE A 312    14714  14762  12970  -3015    463    287
ATOM   2385  N   GLN A 313      19.087   2.617  -9.660  1.00 89.31           N  
ANISOU 2385  N   GLN A 313    13751  11771   8410  -4342    507    154
ATOM   2386  CA  GLN A 313      19.484   2.326  -8.286  1.00 87.35           C  
ANISOU 2386  CA  GLN A 313    13842  11494   7855  -4769    450     15
ATOM   2387  C   GLN A 313      20.736   1.460  -8.250  1.00 85.62           C  
ANISOU 2387  C   GLN A 313    14157  10961   7412  -4612    201    460
ATOM   2388  O   GLN A 313      21.685   1.737  -7.504  1.00 85.08           O  
ANISOU 2388  O   GLN A 313    14153  10721   7452  -4583     51    544
ATOM   2389  CB  GLN A 313      18.329   1.634  -7.559  1.00 86.78           C  
ANISOU 2389  CB  GLN A 313    14040  11722   7212  -5453    603   -407
ATOM   2390  CG  GLN A 313      18.570   1.348  -6.087  1.00 86.35           C  
ANISOU 2390  CG  GLN A 313    14357  11718   6732  -6020    559   -574
ATOM   2391  CD  GLN A 313      18.677   2.605  -5.251  1.00 86.63           C  
ANISOU 2391  CD  GLN A 313    13884  11877   7154  -6065    630   -931
ATOM   2392  OE1 GLN A 313      19.766   2.995  -4.834  1.00 86.58           O  
ANISOU 2392  OE1 GLN A 313    13890  11643   7364  -5852    454   -728
ATOM   2393  NE2 GLN A 313      17.541   3.246  -4.997  1.00 87.07           N  
ANISOU 2393  NE2 GLN A 313    13456  12297   7330  -6335    875  -1521
ATOM   2394  N   GLU A 314      20.764   0.415  -9.081  1.00 93.73           N  
ANISOU 2394  N   GLU A 314    15539  11903   8169  -4479    125    708
ATOM   2395  CA  GLU A 314      21.901  -0.495  -9.075  1.00 92.28           C  
ANISOU 2395  CA  GLU A 314    15845  11404   7812  -4310   -161   1049
ATOM   2396  C   GLU A 314      23.164   0.161  -9.614  1.00 92.49           C  
ANISOU 2396  C   GLU A 314    15549  11241   8351  -3720   -258   1339
ATOM   2397  O   GLU A 314      24.263  -0.157  -9.148  1.00 92.19           O  
ANISOU 2397  O   GLU A 314    15763  10947   8317  -3614   -508   1494
ATOM   2398  CB  GLU A 314      21.574  -1.761  -9.863  1.00 91.78           C  
ANISOU 2398  CB  GLU A 314    16114  11289   7470  -4250   -238   1125
ATOM   2399  CG  GLU A 314      20.567  -2.649  -9.162  1.00 91.50           C  
ANISOU 2399  CG  GLU A 314    16320  11293   7153  -4757   -242    800
ATOM   2400  CD  GLU A 314      21.087  -3.165  -7.830  1.00 90.64           C  
ANISOU 2400  CD  GLU A 314    16594  10944   6902  -5090   -494    776
ATOM   2401  OE1 GLU A 314      22.315  -3.361  -7.702  1.00 90.34           O  
ANISOU 2401  OE1 GLU A 314    16752  10615   6957  -4801   -779   1014
ATOM   2402  OE2 GLU A 314      20.268  -3.369  -6.908  1.00 91.49           O1-
ANISOU 2402  OE2 GLU A 314    16790  11156   6817  -5659   -405    526
ATOM   2403  N   LEU A 315      23.044   1.074 -10.581  1.00 85.13           N  
ANISOU 2403  N   LEU A 315    14068  10426   7850  -3354    -88   1416
ATOM   2404  CA  LEU A 315      24.237   1.797 -11.010  1.00 85.14           C  
ANISOU 2404  CA  LEU A 315    13741  10280   8328  -2892   -146   1688
ATOM   2405  C   LEU A 315      24.751   2.701  -9.897  1.00 86.01           C  
ANISOU 2405  C   LEU A 315    13654  10283   8741  -2994   -198   1567
ATOM   2406  O   LEU A 315      25.967   2.810  -9.689  1.00 86.28           O  
ANISOU 2406  O   LEU A 315    13688  10115   8981  -2769   -355   1732
ATOM   2407  CB  LEU A 315      23.961   2.603 -12.280  1.00 85.43           C  
ANISOU 2407  CB  LEU A 315    13280  10461   8718  -2557     20   1852
ATOM   2408  CG  LEU A 315      25.212   3.294 -12.838  1.00 85.69           C  
ANISOU 2408  CG  LEU A 315    12991  10376   9190  -2143    -12   2177
ATOM   2409  CD1 LEU A 315      26.277   2.271 -13.193  1.00 85.35           C  
ANISOU 2409  CD1 LEU A 315    13254  10233   8940  -1921   -150   2345
ATOM   2410  CD2 LEU A 315      24.892   4.152 -14.047  1.00 86.24           C  
ANISOU 2410  CD2 LEU A 315    12614  10587   9565  -1901    123   2397
ATOM   2411  N   GLN A 316      23.841   3.345  -9.160  1.00 84.19           N  
ANISOU 2411  N   GLN A 316    13226  10208   8554  -3333    -73   1223
ATOM   2412  CA  GLN A 316      24.258   4.137  -8.007  1.00 84.76           C  
ANISOU 2412  CA  GLN A 316    13124  10217   8864  -3478   -126   1025
ATOM   2413  C   GLN A 316      25.024   3.283  -7.004  1.00 83.91           C  
ANISOU 2413  C   GLN A 316    13567   9956   8360  -3692   -364   1057
ATOM   2414  O   GLN A 316      26.096   3.675  -6.527  1.00 84.63           O  
ANISOU 2414  O   GLN A 316    13584   9860   8714  -3525   -524   1139
ATOM   2415  CB  GLN A 316      23.046   4.791  -7.338  1.00 85.60           C  
ANISOU 2415  CB  GLN A 316    12946  10580   8999  -3864     51    534
ATOM   2416  CG  GLN A 316      23.402   5.613  -6.100  1.00 86.00           C  
ANISOU 2416  CG  GLN A 316    12783  10621   9273  -4046      9    239
ATOM   2417  CD  GLN A 316      22.196   6.264  -5.450  1.00 86.44           C  
ANISOU 2417  CD  GLN A 316    12483  10980   9379  -4425    195   -355
ATOM   2418  OE1 GLN A 316      21.072   6.146  -5.938  1.00 86.82           O  
ANISOU 2418  OE1 GLN A 316    12414  11235   9337  -4537    351   -555
ATOM   2419  NE2 GLN A 316      22.421   6.931  -4.324  1.00 86.44           N  
ANISOU 2419  NE2 GLN A 316    12288  11035   9521  -4630    173   -698
ATOM   2420  N   ASN A 317      24.492   2.104  -6.676  1.00 85.66           N  
ANISOU 2420  N   ASN A 317    14359  10230   7959  -4072   -426   1004
ATOM   2421  CA  ASN A 317      25.160   1.261  -5.689  1.00 85.58           C  
ANISOU 2421  CA  ASN A 317    14941  10029   7547  -4320   -732   1072
ATOM   2422  C   ASN A 317      26.502   0.751  -6.209  1.00 85.73           C  
ANISOU 2422  C   ASN A 317    15126   9705   7745  -3827  -1029   1420
ATOM   2423  O   ASN A 317      27.488   0.700  -5.460  1.00 86.95           O  
ANISOU 2423  O   ASN A 317    15454   9642   7942  -3785  -1314   1473
ATOM   2424  CB  ASN A 317      24.246   0.103  -5.293  1.00 85.64           C  
ANISOU 2424  CB  ASN A 317    15549  10137   6854  -4884   -757    983
ATOM   2425  CG  ASN A 317      22.971   0.576  -4.615  1.00 86.34           C  
ANISOU 2425  CG  ASN A 317    15457  10626   6723  -5452   -453    544
ATOM   2426  OD1 ASN A 317      21.869   0.383  -5.130  1.00 85.86           O  
ANISOU 2426  OD1 ASN A 317    15311  10794   6517  -5621   -219    381
ATOM   2427  ND2 ASN A 317      23.118   1.209  -3.456  1.00 87.69           N  
ANISOU 2427  ND2 ASN A 317    15527  10911   6878  -5747   -456    297
ATOM   2428  N   HIS A 318      26.557   0.372  -7.489  1.00 81.61           N  
ANISOU 2428  N   HIS A 318    14522   9157   7328  -3450   -973   1614
ATOM   2429  CA  HIS A 318      27.817  -0.020  -8.115  1.00 81.98           C  
ANISOU 2429  CA  HIS A 318    14590   8958   7602  -2951  -1197   1852
ATOM   2430  C   HIS A 318      28.872   1.068  -7.963  1.00 83.17           C  
ANISOU 2430  C   HIS A 318    14261   9033   8306  -2638  -1202   1894
ATOM   2431  O   HIS A 318      29.988   0.812  -7.494  1.00 84.71           O  
ANISOU 2431  O   HIS A 318    14603   8984   8600  -2478  -1506   1938
ATOM   2432  CB  HIS A 318      27.583  -0.332  -9.596  1.00 80.97           C  
ANISOU 2432  CB  HIS A 318    14295   8949   7523  -2624  -1033   1983
ATOM   2433  CG  HIS A 318      28.821  -0.729 -10.342  1.00 82.59           C  
ANISOU 2433  CG  HIS A 318    14436   8996   7950  -2128  -1206   2141
ATOM   2434  ND1 HIS A 318      28.884  -0.742 -11.719  1.00 83.61           N  
ANISOU 2434  ND1 HIS A 318    14271   9300   8198  -1782  -1023   2253
ATOM   2435  CD2 HIS A 318      30.041  -1.125  -9.907  1.00 84.90           C  
ANISOU 2435  CD2 HIS A 318    14889   9005   8364  -1927  -1548   2156
ATOM   2436  CE1 HIS A 318      30.089  -1.125 -12.100  1.00 86.87           C  
ANISOU 2436  CE1 HIS A 318    14636   9582   8790  -1409  -1205   2295
ATOM   2437  NE2 HIS A 318      30.811  -1.364 -11.020  1.00 87.76           N  
ANISOU 2437  NE2 HIS A 318    15009   9396   8941  -1467  -1540   2226
ATOM   2438  N   ILE A 319      28.532   2.295  -8.361  1.00 77.07           N  
ANISOU 2438  N   ILE A 319    12908   8443   7933  -2546   -900   1873
ATOM   2439  CA  ILE A 319      29.513   3.373  -8.334  1.00 76.93           C  
ANISOU 2439  CA  ILE A 319    12406   8336   8488  -2261   -890   1940
ATOM   2440  C   ILE A 319      29.905   3.715  -6.905  1.00 78.28           C  
ANISOU 2440  C   ILE A 319    12659   8389   8694  -2490  -1073   1739
ATOM   2441  O   ILE A 319      31.064   4.056  -6.639  1.00 78.88           O  
ANISOU 2441  O   ILE A 319    12575   8291   9105  -2257  -1234   1784
ATOM   2442  CB  ILE A 319      28.965   4.592  -9.088  1.00 75.88           C  
ANISOU 2442  CB  ILE A 319    11682   8367   8782  -2152   -588   1994
ATOM   2443  CG1 ILE A 319      28.694   4.210 -10.541  1.00 75.03           C  
ANISOU 2443  CG1 ILE A 319    11525   8398   8586  -1920   -445   2229
ATOM   2444  CG2 ILE A 319      29.955   5.722  -9.025  1.00 76.21           C  
ANISOU 2444  CG2 ILE A 319    11242   8282   9433  -1918   -590   2080
ATOM   2445  CD1 ILE A 319      27.902   5.225 -11.307  1.00 74.56           C  
ANISOU 2445  CD1 ILE A 319    11012   8492   8826  -1876   -218   2306
ATOM   2446  N   HIS A 320      28.964   3.624  -5.963  1.00 74.21           N  
ANISOU 2446  N   HIS A 320    12378   8004   7816  -2971  -1048   1485
ATOM   2447  CA  HIS A 320      29.319   3.753  -4.553  1.00 76.14           C  
ANISOU 2447  CA  HIS A 320    12803   8187   7940  -3257  -1251   1284
ATOM   2448  C   HIS A 320      30.371   2.727  -4.157  1.00 77.65           C  
ANISOU 2448  C   HIS A 320    13521   8091   7893  -3165  -1679   1443
ATOM   2449  O   HIS A 320      31.354   3.056  -3.481  1.00 78.82           O  
ANISOU 2449  O   HIS A 320    13606   8078   8264  -3052  -1911   1407
ATOM   2450  CB  HIS A 320      28.077   3.600  -3.676  1.00 77.56           C  
ANISOU 2450  CB  HIS A 320    13220   8631   7619  -3872  -1134    975
ATOM   2451  CG  HIS A 320      28.361   3.715  -2.211  1.00 80.15           C  
ANISOU 2451  CG  HIS A 320    13756   8979   7717  -4244  -1324    753
ATOM   2452  ND1 HIS A 320      28.773   2.643  -1.448  1.00 82.48           N  
ANISOU 2452  ND1 HIS A 320    14751   9123   7464  -4505  -1690    868
ATOM   2453  CD2 HIS A 320      28.296   4.772  -1.367  1.00 81.23           C  
ANISOU 2453  CD2 HIS A 320    13503   9271   8090  -4408  -1230    415
ATOM   2454  CE1 HIS A 320      28.949   3.034  -0.199  1.00 84.89           C  
ANISOU 2454  CE1 HIS A 320    15107   9523   7623  -4835  -1803    637
ATOM   2455  NE2 HIS A 320      28.665   4.321  -0.122  1.00 84.10           N  
ANISOU 2455  NE2 HIS A 320    14331   9628   7994  -4779  -1508    329
ATOM   2456  N   ASP A 321      30.181   1.472  -4.576  1.00 87.83           N  
ANISOU 2456  N   ASP A 321    15319   9286   8767  -3195  -1830   1596
ATOM   2457  CA  ASP A 321      31.096   0.404  -4.183  1.00 89.38           C  
ANISOU 2457  CA  ASP A 321    16059   9146   8755  -3112  -2327   1720
ATOM   2458  C   ASP A 321      32.481   0.600  -4.792  1.00 90.55           C  
ANISOU 2458  C   ASP A 321    15865   9087   9455  -2499  -2479   1817
ATOM   2459  O   ASP A 321      33.482   0.671  -4.072  1.00 92.86           O  
ANISOU 2459  O   ASP A 321    16207   9167   9908  -2387  -2814   1776
ATOM   2460  CB  ASP A 321      30.517  -0.956  -4.579  1.00 88.31           C  
ANISOU 2460  CB  ASP A 321    16507   8922   8126  -3270  -2467   1835
ATOM   2461  CG  ASP A 321      29.374  -1.383  -3.683  1.00 88.16           C  
ANISOU 2461  CG  ASP A 321    16981   9050   7466  -3979  -2442   1740
ATOM   2462  OD1 ASP A 321      29.401  -1.040  -2.482  1.00 89.86           O  
ANISOU 2462  OD1 ASP A 321    17333   9321   7490  -4356  -2542   1620
ATOM   2463  OD2 ASP A 321      28.444  -2.051  -4.182  1.00 86.73           O1-
ANISOU 2463  OD2 ASP A 321    17032   8964   6957  -4188  -2307   1763
ATOM   2464  N   GLU A 322      32.560   0.679  -6.124  1.00 91.72           N  
ANISOU 2464  N   GLU A 322    15650   9325   9875  -2120  -2237   1923
ATOM   2465  CA  GLU A 322      33.863   0.818  -6.769  1.00 94.91           C  
ANISOU 2465  CA  GLU A 322    15696   9609  10758  -1592  -2331   1972
ATOM   2466  C   GLU A 322      34.556   2.106  -6.342  1.00 97.25           C  
ANISOU 2466  C   GLU A 322    15462   9922  11566  -1487  -2235   1910
ATOM   2467  O   GLU A 322      35.767   2.114  -6.088  1.00 99.55           O  
ANISOU 2467  O   GLU A 322    15644  10023  12157  -1215  -2502   1854
ATOM   2468  CB  GLU A 322      33.710   0.761  -8.290  1.00 96.22           C  
ANISOU 2468  CB  GLU A 322    15543   9973  11043  -1298  -2020   2090
ATOM   2469  CG  GLU A 322      35.028   0.878  -9.048  1.00102.21           C  
ANISOU 2469  CG  GLU A 322    15887  10704  12243   -809  -2051   2097
ATOM   2470  CD  GLU A 322      34.867   0.717 -10.551  1.00105.36           C  
ANISOU 2470  CD  GLU A 322    16020  11366  12646   -579  -1749   2198
ATOM   2471  OE1 GLU A 322      33.733   0.462 -11.009  1.00102.65           O  
ANISOU 2471  OE1 GLU A 322    15842  11185  11975   -761  -1559   2272
ATOM   2472  OE2 GLU A 322      35.874   0.860 -11.277  1.00111.39           O1-
ANISOU 2472  OE2 GLU A 322    16387  12211  13726   -236  -1691   2181
ATOM   2473  N   GLY A 323      33.803   3.199  -6.243  1.00 89.24           N  
ANISOU 2473  N   GLY A 323    14097   9115  10696  -1693  -1887   1879
ATOM   2474  CA  GLY A 323      34.358   4.466  -5.813  1.00 90.83           C  
ANISOU 2474  CA  GLY A 323    13788   9304  11419  -1626  -1806   1799
ATOM   2475  C   GLY A 323      34.940   4.396  -4.418  1.00 92.00           C  
ANISOU 2475  C   GLY A 323    14181   9277  11498  -1774  -2171   1611
ATOM   2476  O   GLY A 323      36.122   4.700  -4.215  1.00 94.60           O  
ANISOU 2476  O   GLY A 323    14277   9446  12219  -1506  -2356   1571
ATOM   2477  N   LEU A 324      34.115   3.986  -3.449  1.00 78.59           N  
ANISOU 2477  N   LEU A 324    12951   7634   9274  -2232  -2278   1483
ATOM   2478  CA  LEU A 324      34.595   3.835  -2.079  1.00 81.16           C  
ANISOU 2478  CA  LEU A 324    13599   7833   9407  -2447  -2657   1328
ATOM   2479  C   LEU A 324      35.811   2.922  -2.040  1.00 83.11           C  
ANISOU 2479  C   LEU A 324    14162   7747   9669  -2129  -3156   1426
ATOM   2480  O   LEU A 324      36.758   3.152  -1.275  1.00 85.07           O  
ANISOU 2480  O   LEU A 324    14370   7833  10119  -2026  -3474   1316
ATOM   2481  CB  LEU A 324      33.471   3.288  -1.198  1.00 82.49           C  
ANISOU 2481  CB  LEU A 324    14322   8160   8862  -3058  -2690   1227
ATOM   2482  CG  LEU A 324      33.611   3.345   0.325  1.00 85.59           C  
ANISOU 2482  CG  LEU A 324    15023   8571   8926  -3465  -2976   1032
ATOM   2483  CD1 LEU A 324      32.230   3.377   0.959  1.00 86.43           C  
ANISOU 2483  CD1 LEU A 324    15327   9038   8476  -4118  -2721    829
ATOM   2484  CD2 LEU A 324      34.422   2.185   0.879  1.00 88.62           C  
ANISOU 2484  CD2 LEU A 324    16091   8620   8962  -3457  -3594   1196
ATOM   2485  N   ARG A 325      35.806   1.893  -2.889  1.00100.16           N  
ANISOU 2485  N   ARG A 325    16596   9799  11661  -1942  -3249   1587
ATOM   2486  CA  ARG A 325      36.925   0.964  -2.964  1.00101.85           C  
ANISOU 2486  CA  ARG A 325    17067   9677  11957  -1588  -3756   1613
ATOM   2487  C   ARG A 325      38.196   1.671  -3.414  1.00104.64           C  
ANISOU 2487  C   ARG A 325    16770   9985  13004  -1087  -3725   1523
ATOM   2488  O   ARG A 325      39.284   1.406  -2.889  1.00106.29           O  
ANISOU 2488  O   ARG A 325    17047   9934  13405   -862  -4187   1408
ATOM   2489  CB  ARG A 325      36.566  -0.179  -3.915  1.00100.76           C  
ANISOU 2489  CB  ARG A 325    17242   9473  11569  -1473  -3798   1737
ATOM   2490  CG  ARG A 325      37.555  -1.322  -3.946  1.00102.12           C  
ANISOU 2490  CG  ARG A 325    17757   9252  11791  -1138  -4403   1705
ATOM   2491  CD  ARG A 325      37.020  -2.481  -4.767  1.00101.00           C  
ANISOU 2491  CD  ARG A 325    17976   9038  11361  -1101  -4462   1786
ATOM   2492  NE  ARG A 325      37.933  -3.616  -4.744  1.00103.12           N  
ANISOU 2492  NE  ARG A 325    18584   8872  11725   -773  -5120   1703
ATOM   2493  CZ  ARG A 325      37.945  -4.528  -3.778  1.00104.29           C  
ANISOU 2493  CZ  ARG A 325    19478   8620  11526  -1012  -5760   1773
ATOM   2494  NH1 ARG A 325      37.095  -4.427  -2.764  1.00103.59           N  
ANISOU 2494  NH1 ARG A 325    19862   8587  10910  -1629  -5758   1926
ATOM   2495  NH2 ARG A 325      38.805  -5.537  -3.821  1.00106.58           N1+
ANISOU 2495  NH2 ARG A 325    20039   8459  11998   -654  -6423   1673
ATOM   2496  N   ALA A 326      38.077   2.582  -4.381  1.00 93.01           N  
ANISOU 2496  N   ALA A 326    14665   8760  11912   -930  -3204   1575
ATOM   2497  CA  ALA A 326      39.243   3.337  -4.822  1.00 96.00           C  
ANISOU 2497  CA  ALA A 326    14402   9139  12934   -546  -3113   1508
ATOM   2498  C   ALA A 326      39.736   4.273  -3.726  1.00 96.93           C  
ANISOU 2498  C   ALA A 326    14297   9184  13349   -639  -3229   1349
ATOM   2499  O   ALA A 326      40.932   4.305  -3.416  1.00 98.60           O  
ANISOU 2499  O   ALA A 326    14334   9222  13907   -369  -3528   1197
ATOM   2500  CB  ALA A 326      38.913   4.118  -6.094  1.00 97.57           C  
ANISOU 2500  CB  ALA A 326    14045   9621  13405   -454  -2546   1670
ATOM   2501  N   THR A 327      38.826   5.029  -3.111  1.00 91.70           N  
ANISOU 2501  N   THR A 327    13609   8661  12571  -1014  -3012   1323
ATOM   2502  CA  THR A 327      39.213   6.015  -2.108  1.00 92.85           C  
ANISOU 2502  CA  THR A 327    13476   8777  13027  -1113  -3080   1122
ATOM   2503  C   THR A 327      39.470   5.403  -0.736  1.00 93.15           C  
ANISOU 2503  C   THR A 327    14063   8658  12672  -1312  -3606    964
ATOM   2504  O   THR A 327      39.637   6.151   0.233  1.00 94.23           O  
ANISOU 2504  O   THR A 327    14042   8819  12942  -1469  -3677    759
ATOM   2505  CB  THR A 327      38.143   7.102  -1.984  1.00 91.95           C  
ANISOU 2505  CB  THR A 327    13056   8883  12998  -1419  -2666   1070
ATOM   2506  OG1 THR A 327      36.941   6.536  -1.449  1.00 89.64           O  
ANISOU 2506  OG1 THR A 327    13282   8729  12049  -1849  -2667   1027
ATOM   2507  CG2 THR A 327      37.842   7.696  -3.347  1.00 91.44           C  
ANISOU 2507  CG2 THR A 327    12513   8936  13292  -1246  -2221   1285
ATOM   2508  N   SER A 328      39.497   4.076  -0.627  1.00102.17           N  
ANISOU 2508  N   SER A 328    15855   9630  13334  -1326  -4003   1058
ATOM   2509  CA  SER A 328      39.818   3.414   0.632  1.00105.59           C  
ANISOU 2509  CA  SER A 328    16886   9863  13371  -1522  -4597    981
ATOM   2510  C   SER A 328      41.236   2.862   0.685  1.00108.45           C  
ANISOU 2510  C   SER A 328    17279   9878  14047  -1064  -5157    911
ATOM   2511  O   SER A 328      41.801   2.739   1.777  1.00111.62           O  
ANISOU 2511  O   SER A 328    17952  10108  14352  -1132  -5661    795
ATOM   2512  CB  SER A 328      38.834   2.269   0.888  1.00106.41           C  
ANISOU 2512  CB  SER A 328    17790   9948  12693  -1934  -4768   1150
ATOM   2513  OG  SER A 328      38.997   1.232  -0.063  1.00106.29           O  
ANISOU 2513  OG  SER A 328    17993   9736  12655  -1641  -4913   1308
ATOM   2514  N   ASN A 329      41.822   2.537  -0.467  1.00126.39           N  
ANISOU 2514  N   ASN A 329    19257  12072  16694   -604  -5091    937
ATOM   2515  CA  ASN A 329      43.114   1.869  -0.649  1.00126.98           C  
ANISOU 2515  CA  ASN A 329    19299  11841  17105   -116  -5600    795
ATOM   2516  C   ASN A 329      44.318   2.794  -0.342  1.00129.02           C  
ANISOU 2516  C   ASN A 329    18929  12076  18015    172  -5661    536
ATOM   2517  O   ASN A 329      45.473   2.441  -0.622  1.00129.14           O  
ANISOU 2517  O   ASN A 329    18715  11904  18447    622  -5989    335
ATOM   2518  CB  ASN A 329      43.183   1.333  -2.086  1.00126.52           C  
ANISOU 2518  CB  ASN A 329    19024  11840  17208    219  -5366    839
ATOM   2519  CG  ASN A 329      44.255   0.263  -2.282  1.00125.44           C  
ANISOU 2519  CG  ASN A 329    19017  11366  17280    680  -5977    641
ATOM   2520  OD1 ASN A 329      44.988  -0.088  -1.361  1.00125.18           O  
ANISOU 2520  OD1 ASN A 329    19248  11008  17306    782  -6627    497
ATOM   2521  ND2 ASN A 329      44.334  -0.268  -3.497  1.00125.64           N  
ANISOU 2521  ND2 ASN A 329    18845  11471  17422    966  -5797    603
ATOM   2522  N   LEU A 330      44.087   3.973   0.240  1.00125.91           N  
ANISOU 2522  N   LEU A 330    18217  11866  17756    -74  -5367    484
ATOM   2523  CA  LEU A 330      45.124   4.989   0.384  1.00126.52           C  
ANISOU 2523  CA  LEU A 330    17611  11952  18510    167  -5313    249
ATOM   2524  C   LEU A 330      45.440   5.295   1.845  1.00127.07           C  
ANISOU 2524  C   LEU A 330    17868  11911  18500     -8  -5746     56
ATOM   2525  O   LEU A 330      46.038   6.335   2.140  1.00127.91           O  
ANISOU 2525  O   LEU A 330    17411  12068  19121     72  -5632   -149
ATOM   2526  CB  LEU A 330      44.699   6.266  -0.341  1.00127.88           C  
ANISOU 2526  CB  LEU A 330    17113  12411  19066     80  -4583    329
ATOM   2527  CG  LEU A 330      44.386   6.085  -1.829  1.00127.95           C  
ANISOU 2527  CG  LEU A 330    16902  12583  19131    220  -4129    545
ATOM   2528  CD1 LEU A 330      43.876   7.383  -2.434  1.00129.43           C  
ANISOU 2528  CD1 LEU A 330    16517  13003  19657     73  -3499    684
ATOM   2529  CD2 LEU A 330      45.588   5.554  -2.594  1.00128.70           C  
ANISOU 2529  CD2 LEU A 330    16712  12603  19586    681  -4285    406
ATOM   2530  N   THR A 331      45.063   4.409   2.763  1.00149.25           N  
ANISOU 2530  N   THR A 331    21469  14577  20662   -272  -6255    124
ATOM   2531  CA  THR A 331      45.220   4.683   4.186  1.00151.61           C  
ANISOU 2531  CA  THR A 331    22018  14846  20741   -534  -6651    -33
ATOM   2532  C   THR A 331      46.691   4.712   4.582  1.00152.13           C  
ANISOU 2532  C   THR A 331    21835  14649  21319   -103  -7198   -304
ATOM   2533  O   THR A 331      47.507   3.939   4.070  1.00150.60           O  
ANISOU 2533  O   THR A 331    21660  14187  21374    332  -7570   -347
ATOM   2534  CB  THR A 331      44.480   3.632   5.014  1.00150.71           C  
ANISOU 2534  CB  THR A 331    22876  14651  19737   -981  -7093    163
ATOM   2535  OG1 THR A 331      45.026   2.333   4.744  1.00148.98           O  
ANISOU 2535  OG1 THR A 331    23139  14038  19429   -687  -7702    280
ATOM   2536  CG2 THR A 331      42.996   3.637   4.676  1.00149.73           C  
ANISOU 2536  CG2 THR A 331    22949  14828  19113  -1444  -6531    364
ATOM   2537  N   GLN A 332      47.028   5.630   5.492  1.00158.84           N  
ANISOU 2537  N   GLN A 332    22403  15590  22361   -212  -7248   -545
ATOM   2538  CA  GLN A 332      48.362   5.848   6.048  1.00158.49           C  
ANISOU 2538  CA  GLN A 332    22072  15343  22805    136  -7751   -859
ATOM   2539  C   GLN A 332      49.342   6.346   4.988  1.00157.60           C  
ANISOU 2539  C   GLN A 332    21105  15201  23575    649  -7460  -1038
ATOM   2540  O   GLN A 332      50.493   6.665   5.318  1.00158.61           O  
ANISOU 2540  O   GLN A 332    20834  15199  24231    959  -7778  -1357
ATOM   2541  CB  GLN A 332      48.914   4.581   6.729  1.00156.98           C  
ANISOU 2541  CB  GLN A 332    22623  14778  22244    254  -8693   -837
ATOM   2542  CG  GLN A 332      50.176   4.767   7.572  1.00157.15           C  
ANISOU 2542  CG  GLN A 332    22471  14591  22647    544  -9340  -1181
ATOM   2543  CD  GLN A 332      50.610   3.488   8.262  1.00157.00           C  
ANISOU 2543  CD  GLN A 332    23271  14156  22226    632 -10354  -1109
ATOM   2544  OE1 GLN A 332      49.995   2.438   8.087  1.00156.85           O  
ANISOU 2544  OE1 GLN A 332    23954  13974  21666    472 -10576   -790
ATOM   2545  NE2 GLN A 332      51.675   3.572   9.053  1.00158.09           N  
ANISOU 2545  NE2 GLN A 332    23329  14089  22648    883 -11015  -1403
ATOM   2546  N   GLU A 333      48.911   6.474   3.734  1.00142.05           N  
ANISOU 2546  N   GLU A 333    18819  13386  21767    707  -6845   -855
ATOM   2547  CA  GLU A 333      49.799   6.805   2.629  1.00140.38           C  
ANISOU 2547  CA  GLU A 333    17861  13203  22273   1120  -6550   -986
ATOM   2548  C   GLU A 333      50.018   8.309   2.486  1.00141.56           C  
ANISOU 2548  C   GLU A 333    17207  13541  23037   1055  -6011  -1097
ATOM   2549  O   GLU A 333      50.683   8.727   1.535  1.00141.17           O  
ANISOU 2549  O   GLU A 333    16508  13571  23561   1292  -5671  -1161
ATOM   2550  CB  GLU A 333      49.230   6.209   1.335  1.00138.81           C  
ANISOU 2550  CB  GLU A 333    17734  13112  21894   1174  -6165   -720
ATOM   2551  CG  GLU A 333      50.188   6.162   0.153  1.00137.93           C  
ANISOU 2551  CG  GLU A 333    16992  13059  22355   1595  -5966   -880
ATOM   2552  CD  GLU A 333      49.573   5.498  -1.056  1.00139.37           C  
ANISOU 2552  CD  GLU A 333    17306  13383  22266   1620  -5629   -642
ATOM   2553  OE1 GLU A 333      48.382   5.133  -0.985  1.00140.63           O  
ANISOU 2553  OE1 GLU A 333    18024  13573  21834   1316  -5535   -341
ATOM   2554  OE2 GLU A 333      50.282   5.328  -2.070  1.00139.89           O1-
ANISOU 2554  OE2 GLU A 333    16898  13560  22692   1928  -5456   -794
ATOM   2555  N   ASN A 334      49.456   9.106   3.395  1.00136.62           N  
ANISOU 2555  N   ASN A 334    16618  12998  22295    710  -5932  -1133
ATOM   2556  CA  ASN A 334      49.618  10.564   3.494  1.00137.69           C  
ANISOU 2556  CA  ASN A 334    16045  13238  23033    619  -5538  -1283
ATOM   2557  C   ASN A 334      49.728  11.244   2.125  1.00136.64           C  
ANISOU 2557  C   ASN A 334    15252  13217  23447    718  -4903  -1113
ATOM   2558  O   ASN A 334      50.683  11.956   1.816  1.00134.50           O  
ANISOU 2558  O   ASN A 334    14315  12923  23864    895  -4774  -1282
ATOM   2559  CB  ASN A 334      50.786  10.938   4.426  1.00138.20           C  
ANISOU 2559  CB  ASN A 334    15823  13160  23526    803  -5996  -1697
ATOM   2560  CG  ASN A 334      52.166  10.500   3.922  1.00136.38           C  
ANISOU 2560  CG  ASN A 334    15247  12781  23789   1280  -6265  -1906
ATOM   2561  OD1 ASN A 334      52.349  10.085   2.784  1.00133.59           O  
ANISOU 2561  OD1 ASN A 334    14728  12473  23557   1475  -6022  -1779
ATOM   2562  ND2 ASN A 334      53.154  10.606   4.802  1.00137.42           N  
ANISOU 2562  ND2 ASN A 334    15236  12765  24210   1466  -6782  -2287
ATOM   2563  N   MET A 335      48.696  11.029   1.306  1.00120.42           N  
ANISOU 2563  N   MET A 335    13404  11302  21049    557  -4504   -762
ATOM   2564  CA  MET A 335      48.632  11.654  -0.011  1.00120.32           C  
ANISOU 2564  CA  MET A 335    12863  11423  21431    577  -3913   -523
ATOM   2565  C   MET A 335      47.227  12.145  -0.333  1.00120.59           C  
ANISOU 2565  C   MET A 335    13006  11586  21225    247  -3485   -225
ATOM   2566  O   MET A 335      46.298  11.336  -0.467  1.00120.20           O  
ANISOU 2566  O   MET A 335    13507  11612  20551    129  -3488    -44
ATOM   2567  CB  MET A 335      49.095  10.685  -1.100  1.00119.83           C  
ANISOU 2567  CB  MET A 335    12837  11424  21269    852  -3884   -425
ATOM   2568  CG  MET A 335      50.574  10.365  -1.067  1.00118.52           C  
ANISOU 2568  CG  MET A 335    12343  11166  21522   1221  -4214   -780
ATOM   2569  SD  MET A 335      51.587  11.827  -1.342  1.00117.47           S  
ANISOU 2569  SD  MET A 335    11239  11087  22306   1227  -3859   -937
ATOM   2570  CE  MET A 335      53.213  11.176  -0.971  1.00117.97           C  
ANISOU 2570  CE  MET A 335    11064  11030  22731   1671  -4414  -1482
ATOM   2571  N   PRO A 336      47.029  13.459  -0.461  1.00102.74           N  
ANISOU 2571  N   PRO A 336    10225   9330  19484     94  -3146   -188
ATOM   2572  CA  PRO A 336      45.752  13.965  -0.978  1.00100.12           C  
ANISOU 2572  CA  PRO A 336     9907   9093  19042   -158  -2754     90
ATOM   2573  C   PRO A 336      45.694  13.899  -2.496  1.00 99.10           C  
ANISOU 2573  C   PRO A 336     9597   9077  18978    -88  -2362    486
ATOM   2574  O   PRO A 336      44.609  13.811  -3.083  1.00 96.83           O  
ANISOU 2574  O   PRO A 336     9512   8897  18383   -232  -2122    756
ATOM   2575  CB  PRO A 336      45.719  15.410  -0.470  1.00101.16           C  
ANISOU 2575  CB  PRO A 336     9517   9110  19809   -305  -2653    -76
ATOM   2576  CG  PRO A 336      47.151  15.786  -0.361  1.00104.05           C  
ANISOU 2576  CG  PRO A 336     9416   9355  20763   -103  -2781   -266
ATOM   2577  CD  PRO A 336      47.887  14.542   0.049  1.00105.16           C  
ANISOU 2577  CD  PRO A 336     9947   9508  20501    128  -3193   -452
ATOM   2578  N   THR A 337      46.865  13.936  -3.140  1.00 96.41           N  
ANISOU 2578  N   THR A 337     8859   8751  19021    115  -2296    492
ATOM   2579  CA  THR A 337      46.915  13.867  -4.598  1.00 96.25           C  
ANISOU 2579  CA  THR A 337     8641   8914  19015    141  -1908    841
ATOM   2580  C   THR A 337      46.329  12.558  -5.111  1.00 94.38           C  
ANISOU 2580  C   THR A 337     8950   8836  18073    222  -1937    967
ATOM   2581  O   THR A 337      45.616  12.541  -6.121  1.00 92.90           O  
ANISOU 2581  O   THR A 337     8807   8813  17675    124  -1612   1308
ATOM   2582  CB  THR A 337      48.356  14.029  -5.083  1.00 99.59           C  
ANISOU 2582  CB  THR A 337     8530   9394  19916    311  -1842    716
ATOM   2583  OG1 THR A 337      49.164  12.972  -4.551  1.00101.04           O  
ANISOU 2583  OG1 THR A 337     8915   9547  19928    603  -2257    335
ATOM   2584  CG2 THR A 337      48.922  15.365  -4.632  1.00101.71           C  
ANISOU 2584  CG2 THR A 337     8238   9487  20920    196  -1796    611
ATOM   2585  N   LEU A 338      46.618  11.451  -4.425  1.00102.55           N  
ANISOU 2585  N   LEU A 338    10418   9799  18749    397  -2365    699
ATOM   2586  CA  LEU A 338      46.067  10.163  -4.830  1.00102.88           C  
ANISOU 2586  CA  LEU A 338    11009   9927  18154    468  -2458    793
ATOM   2587  C   LEU A 338      44.562  10.103  -4.609  1.00101.58           C  
ANISOU 2587  C   LEU A 338    11300   9791  17504    182  -2364    993
ATOM   2588  O   LEU A 338      43.851   9.422  -5.358  1.00101.72           O  
ANISOU 2588  O   LEU A 338    11610   9944  17093    160  -2220   1199
ATOM   2589  CB  LEU A 338      46.768   9.035  -4.073  1.00101.62           C  
ANISOU 2589  CB  LEU A 338    11223   9595  17792    709  -3032    469
ATOM   2590  CG  LEU A 338      48.116   8.556  -4.621  1.00103.52           C  
ANISOU 2590  CG  LEU A 338    11115   9864  18355   1075  -3159    220
ATOM   2591  CD1 LEU A 338      49.213   9.595  -4.454  1.00104.32           C  
ANISOU 2591  CD1 LEU A 338    10524   9952  19160   1137  -3075     15
ATOM   2592  CD2 LEU A 338      48.517   7.260  -3.942  1.00104.39           C  
ANISOU 2592  CD2 LEU A 338    11738   9741  18184   1320  -3816    -53
ATOM   2593  N   PHE A 339      44.061  10.813  -3.597  1.00 93.98           N  
ANISOU 2593  N   PHE A 339    10363   8730  16614    -43  -2436    884
ATOM   2594  CA  PHE A 339      42.626  10.835  -3.334  1.00 91.99           C  
ANISOU 2594  CA  PHE A 339    10459   8551  15943   -341  -2325    978
ATOM   2595  C   PHE A 339      41.882  11.654  -4.384  1.00 90.39           C  
ANISOU 2595  C   PHE A 339     9919   8464  15959   -444  -1865   1282
ATOM   2596  O   PHE A 339      40.853  11.208  -4.916  1.00 88.48           O  
ANISOU 2596  O   PHE A 339     9968   8355  15294   -552  -1710   1466
ATOM   2597  CB  PHE A 339      42.388  11.356  -1.914  1.00 92.09           C  
ANISOU 2597  CB  PHE A 339    10533   8479  15977   -557  -2541    675
ATOM   2598  CG  PHE A 339      40.947  11.566  -1.563  1.00 90.19           C  
ANISOU 2598  CG  PHE A 339    10509   8364  15393   -899  -2389    655
ATOM   2599  CD1 PHE A 339      40.049  10.515  -1.579  1.00 88.04           C  
ANISOU 2599  CD1 PHE A 339    10833   8209  14407  -1062  -2427    739
ATOM   2600  CD2 PHE A 339      40.511  12.799  -1.123  1.00 90.67           C  
ANISOU 2600  CD2 PHE A 339    10162   8419  15869  -1069  -2243    481
ATOM   2601  CE1 PHE A 339      38.725  10.712  -1.233  1.00 86.51           C  
ANISOU 2601  CE1 PHE A 339    10788   8175  13905  -1404  -2266    652
ATOM   2602  CE2 PHE A 339      39.193  12.998  -0.765  1.00 89.60           C  
ANISOU 2602  CE2 PHE A 339    10158   8429  15457  -1374  -2114    356
ATOM   2603  CZ  PHE A 339      38.299  11.953  -0.821  1.00 87.55           C  
ANISOU 2603  CZ  PHE A 339    10466   8334  14464  -1552  -2108    434
ATOM   2604  N   VAL A 340      42.408  12.833  -4.727  1.00 93.28           N  
ANISOU 2604  N   VAL A 340     9686   8766  16992   -419  -1675   1354
ATOM   2605  CA  VAL A 340      41.803  13.637  -5.787  1.00 91.89           C  
ANISOU 2605  CA  VAL A 340     9206   8648  17058   -518  -1311   1706
ATOM   2606  C   VAL A 340      41.865  12.894  -7.116  1.00 92.65           C  
ANISOU 2606  C   VAL A 340     9405   8962  16836   -406  -1104   2019
ATOM   2607  O   VAL A 340      40.854  12.746  -7.816  1.00 90.45           O  
ANISOU 2607  O   VAL A 340     9301   8810  16255   -500   -925   2263
ATOM   2608  CB  VAL A 340      42.490  15.009  -5.885  1.00 92.02           C  
ANISOU 2608  CB  VAL A 340     8588   8502  17873   -543  -1204   1757
ATOM   2609  CG1 VAL A 340      41.880  15.825  -7.013  1.00 89.52           C  
ANISOU 2609  CG1 VAL A 340     8017   8198  17800   -670   -902   2191
ATOM   2610  CG2 VAL A 340      42.399  15.742  -4.569  1.00 91.44           C  
ANISOU 2610  CG2 VAL A 340     8384   8230  18129   -642  -1416   1384
ATOM   2611  N   GLU A 341      43.059  12.422  -7.488  1.00 91.97           N  
ANISOU 2611  N   GLU A 341     9176   8945  16824   -199  -1133   1962
ATOM   2612  CA  GLU A 341      43.208  11.711  -8.752  1.00 94.89           C  
ANISOU 2612  CA  GLU A 341     9578   9577  16898    -91   -927   2171
ATOM   2613  C   GLU A 341      42.357  10.452  -8.791  1.00 94.32           C  
ANISOU 2613  C   GLU A 341    10110   9591  16138    -55  -1047   2146
ATOM   2614  O   GLU A 341      41.915  10.036  -9.868  1.00 96.03           O  
ANISOU 2614  O   GLU A 341    10407  10034  16047    -50   -826   2375
ATOM   2615  CB  GLU A 341      44.677  11.371  -8.997  1.00 97.61           C  
ANISOU 2615  CB  GLU A 341     9617  10002  17469    135   -973   1965
ATOM   2616  CG  GLU A 341      45.537  12.579  -9.313  1.00 96.24           C  
ANISOU 2616  CG  GLU A 341     8796   9829  17941     45   -746   2059
ATOM   2617  CD  GLU A 341      46.997  12.227  -9.508  1.00 97.97           C  
ANISOU 2617  CD  GLU A 341     8659  10171  18394    251   -779   1763
ATOM   2618  OE1 GLU A 341      47.373  11.064  -9.248  1.00 98.99           O  
ANISOU 2618  OE1 GLU A 341     9047  10315  18248    515  -1065   1435
ATOM   2619  OE2 GLU A 341      47.770  13.115  -9.928  1.00 98.86           O1-
ANISOU 2619  OE2 GLU A 341     8219  10354  18989    139   -539   1841
ATOM   2620  N   SER A 342      42.101   9.840  -7.632  1.00 95.18           N  
ANISOU 2620  N   SER A 342    10657   9529  15979    -66  -1402   1881
ATOM   2621  CA  SER A 342      41.273   8.639  -7.599  1.00 94.10           C  
ANISOU 2621  CA  SER A 342    11129   9436  15190    -93  -1541   1873
ATOM   2622  C   SER A 342      39.808   8.976  -7.852  1.00 90.12           C  
ANISOU 2622  C   SER A 342    10765   9031  14444   -353  -1302   2078
ATOM   2623  O   SER A 342      39.148   8.336  -8.683  1.00 89.58           O  
ANISOU 2623  O   SER A 342    10919   9130  13987   -354  -1165   2242
ATOM   2624  CB  SER A 342      41.445   7.918  -6.262  1.00 92.35           C  
ANISOU 2624  CB  SER A 342    11369   8996  14722   -105  -2017   1578
ATOM   2625  OG  SER A 342      40.936   8.696  -5.194  1.00 90.52           O  
ANISOU 2625  OG  SER A 342    11140   8676  14577   -361  -2064   1468
ATOM   2626  N   VAL A 343      39.280   9.983  -7.146  1.00 84.23           N  
ANISOU 2626  N   VAL A 343     9858   8191  13953   -561  -1267   2019
ATOM   2627  CA  VAL A 343      37.886  10.370  -7.362  1.00 82.54           C  
ANISOU 2627  CA  VAL A 343     9701   8065  13594   -784  -1072   2131
ATOM   2628  C   VAL A 343      37.675  10.822  -8.803  1.00 82.44           C  
ANISOU 2628  C   VAL A 343     9391   8193  13740   -724   -757   2511
ATOM   2629  O   VAL A 343      36.687  10.450  -9.453  1.00 81.11           O  
ANISOU 2629  O   VAL A 343     9427   8177  13215   -791   -628   2659
ATOM   2630  CB  VAL A 343      37.469  11.462  -6.360  1.00 82.89           C  
ANISOU 2630  CB  VAL A 343     9515   7983  13997   -982  -1111   1909
ATOM   2631  CG1 VAL A 343      36.042  11.903  -6.627  1.00 81.74           C  
ANISOU 2631  CG1 VAL A 343     9345   7925  13787  -1177   -934   1948
ATOM   2632  CG2 VAL A 343      37.616  10.965  -4.935  1.00 83.45           C  
ANISOU 2632  CG2 VAL A 343     9927   7989  13790  -1101  -1418   1541
ATOM   2633  N   LEU A 344      38.607  11.625  -9.328  1.00 91.21           N  
ANISOU 2633  N   LEU A 344    10023   9269  15363   -629   -638   2680
ATOM   2634  CA  LEU A 344      38.524  12.051 -10.722  1.00 91.02           C  
ANISOU 2634  CA  LEU A 344     9742   9405  15434   -628   -355   3093
ATOM   2635  C   LEU A 344      38.600  10.858 -11.668  1.00 94.50           C  
ANISOU 2635  C   LEU A 344    10442  10132  15333   -498   -261   3187
ATOM   2636  O   LEU A 344      37.941  10.840 -12.717  1.00 92.01           O  
ANISOU 2636  O   LEU A 344    10148  10013  14797   -547    -65   3479
ATOM   2637  CB  LEU A 344      39.642  13.047 -11.023  1.00 93.93           C  
ANISOU 2637  CB  LEU A 344     9578   9702  16410   -616   -252   3243
ATOM   2638  CG  LEU A 344      39.562  14.363 -10.250  1.00 90.67           C  
ANISOU 2638  CG  LEU A 344     8840   8978  16633   -743   -342   3177
ATOM   2639  CD1 LEU A 344      40.813  15.194 -10.473  1.00 93.64           C  
ANISOU 2639  CD1 LEU A 344     8717   9268  17592   -745   -262   3288
ATOM   2640  CD2 LEU A 344      38.320  15.137 -10.655  1.00 87.67           C  
ANISOU 2640  CD2 LEU A 344     8410   8518  16382   -897   -281   3417
ATOM   2641  N   GLU A 345      39.404   9.853 -11.308  1.00 91.64           N  
ANISOU 2641  N   GLU A 345    10267   9780  14774   -319   -437   2916
ATOM   2642  CA  GLU A 345      39.520   8.638 -12.110  1.00 96.82           C  
ANISOU 2642  CA  GLU A 345    11156  10669  14963   -162   -409   2900
ATOM   2643  C   GLU A 345      38.183   7.913 -12.201  1.00 91.36           C  
ANISOU 2643  C   GLU A 345    10945  10035  13734   -258   -433   2934
ATOM   2644  O   GLU A 345      37.751   7.506 -13.289  1.00 91.23           O  
ANISOU 2644  O   GLU A 345    10980  10272  13409   -234   -247   3111
ATOM   2645  CB  GLU A 345      40.593   7.735 -11.502  1.00102.97           C  
ANISOU 2645  CB  GLU A 345    12054  11339  15731     69   -714   2533
ATOM   2646  CG  GLU A 345      40.893   6.466 -12.263  1.00108.20           C  
ANISOU 2646  CG  GLU A 345    12890  12191  16029    286   -755   2410
ATOM   2647  CD  GLU A 345      41.998   5.662 -11.602  1.00108.48           C  
ANISOU 2647  CD  GLU A 345    13004  12041  16175    548  -1149   2011
ATOM   2648  OE1 GLU A 345      42.508   6.110 -10.551  1.00106.31           O  
ANISOU 2648  OE1 GLU A 345    12666  11512  16216    542  -1378   1863
ATOM   2649  OE2 GLU A 345      42.355   4.584 -12.125  1.00110.54           O1-
ANISOU 2649  OE2 GLU A 345    13376  12396  16227    774  -1267   1815
ATOM   2650  N   VAL A 346      37.507   7.751 -11.060  1.00 95.18           N  
ANISOU 2650  N   VAL A 346    11770  10315  14078   -400   -649   2746
ATOM   2651  CA  VAL A 346      36.189   7.119 -11.052  1.00 90.21           C  
ANISOU 2651  CA  VAL A 346    11573   9750  12954   -558   -653   2742
ATOM   2652  C   VAL A 346      35.209   7.921 -11.899  1.00 86.31           C  
ANISOU 2652  C   VAL A 346    10852   9411  12530   -676   -371   3013
ATOM   2653  O   VAL A 346      34.492   7.370 -12.749  1.00 85.29           O  
ANISOU 2653  O   VAL A 346    10895   9480  12031   -677   -255   3135
ATOM   2654  CB  VAL A 346      35.679   6.961  -9.608  1.00 86.87           C  
ANISOU 2654  CB  VAL A 346    11495   9136  12376   -778   -896   2474
ATOM   2655  CG1 VAL A 346      34.270   6.391  -9.601  1.00 82.53           C  
ANISOU 2655  CG1 VAL A 346    11339   8694  11327  -1010   -850   2445
ATOM   2656  CG2 VAL A 346      36.622   6.085  -8.802  1.00 89.74           C  
ANISOU 2656  CG2 VAL A 346    12161   9316  12621   -666  -1261   2256
ATOM   2657  N   HIS A 347      35.166   9.239 -11.678  1.00 93.11           N  
ANISOU 2657  N   HIS A 347    11323  10156  13897   -767   -301   3098
ATOM   2658  CA  HIS A 347      34.226  10.080 -12.413  1.00 89.38           C  
ANISOU 2658  CA  HIS A 347    10637   9749  13574   -867   -132   3353
ATOM   2659  C   HIS A 347      34.427   9.945 -13.918  1.00 90.04           C  
ANISOU 2659  C   HIS A 347    10609  10089  13512   -765     71   3727
ATOM   2660  O   HIS A 347      33.456   9.798 -14.671  1.00 87.40           O  
ANISOU 2660  O   HIS A 347    10385   9915  12909   -809    157   3884
ATOM   2661  CB  HIS A 347      34.375  11.536 -11.975  1.00 88.12           C  
ANISOU 2661  CB  HIS A 347    10039   9354  14090   -943   -155   3387
ATOM   2662  CG  HIS A 347      33.285  12.430 -12.477  1.00 85.72           C  
ANISOU 2662  CG  HIS A 347     9544   9010  14015  -1043   -106   3567
ATOM   2663  ND1 HIS A 347      33.325  13.032 -13.716  1.00 85.43           N  
ANISOU 2663  ND1 HIS A 347     9277   9031  14151  -1021      8   4032
ATOM   2664  CD2 HIS A 347      32.124  12.825 -11.905  1.00 85.09           C  
ANISOU 2664  CD2 HIS A 347     9458   8841  14030  -1173   -189   3321
ATOM   2665  CE1 HIS A 347      32.235  13.758 -13.886  1.00 85.38           C  
ANISOU 2665  CE1 HIS A 347     9156   8915  14369  -1099    -61   4091
ATOM   2666  NE2 HIS A 347      31.489  13.649 -12.802  1.00 84.67           N  
ANISOU 2666  NE2 HIS A 347     9167   8743  14262  -1176   -170   3624
ATOM   2667  N   GLY A 348      35.682   9.974 -14.373  1.00101.32           N  
ANISOU 2667  N   GLY A 348    11806  11599  15090   -645    153   3838
ATOM   2668  CA  GLY A 348      35.945   9.771 -15.790  1.00103.78           C  
ANISOU 2668  CA  GLY A 348    12005  12245  15180   -595    375   4141
ATOM   2669  C   GLY A 348      35.485   8.409 -16.276  1.00105.22           C  
ANISOU 2669  C   GLY A 348    12570  12671  14738   -494    381   4009
ATOM   2670  O   GLY A 348      34.829   8.296 -17.317  1.00103.36           O  
ANISOU 2670  O   GLY A 348    12374  12691  14206   -528    525   4241
ATOM   2671  N   LYS A 349      35.830   7.357 -15.526  1.00103.09           N  
ANISOU 2671  N   LYS A 349    12596  12302  14271   -373    186   3639
ATOM   2672  CA  LYS A 349      35.360   6.009 -15.838  1.00104.13           C  
ANISOU 2672  CA  LYS A 349    13133  12572  13859   -288    121   3476
ATOM   2673  C   LYS A 349      33.865   5.992 -16.142  1.00 96.59           C  
ANISOU 2673  C   LYS A 349    12396  11693  12610   -445    183   3595
ATOM   2674  O   LYS A 349      33.440   5.607 -17.240  1.00 95.93           O  
ANISOU 2674  O   LYS A 349    12343  11900  12204   -409    327   3731
ATOM   2675  CB  LYS A 349      35.682   5.071 -14.670  1.00107.33           C  
ANISOU 2675  CB  LYS A 349    13911  12705  14164   -221   -211   3105
ATOM   2676  CG  LYS A 349      35.174   3.638 -14.822  1.00108.30           C  
ANISOU 2676  CG  LYS A 349    14515  12861  13771   -167   -360   2928
ATOM   2677  CD  LYS A 349      35.937   2.849 -15.874  1.00117.57           C  
ANISOU 2677  CD  LYS A 349    15574  14283  14813     96   -308   2839
ATOM   2678  CE  LYS A 349      35.384   1.429 -15.999  1.00116.43           C  
ANISOU 2678  CE  LYS A 349    15912  14111  14215    152   -502   2639
ATOM   2679  NZ  LYS A 349      35.579   0.618 -14.760  1.00112.01           N1+
ANISOU 2679  NZ  LYS A 349    15809  13134  13615    148   -944   2390
ATOM   2680  N   PHE A 350      33.049   6.436 -15.183  1.00 96.11           N  
ANISOU 2680  N   PHE A 350    12449  11406  12662   -627     79   3502
ATOM   2681  CA  PHE A 350      31.609   6.267 -15.336  1.00 91.86           C  
ANISOU 2681  CA  PHE A 350    12121  10943  11836   -778    109   3491
ATOM   2682  C   PHE A 350      30.960   7.309 -16.237  1.00 90.14           C  
ANISOU 2682  C   PHE A 350    11587  10845  11818   -822    263   3813
ATOM   2683  O   PHE A 350      29.841   7.078 -16.705  1.00 88.74           O  
ANISOU 2683  O   PHE A 350    11541  10802  11375   -886    295   3825
ATOM   2684  CB  PHE A 350      30.925   6.262 -13.972  1.00 89.53           C  
ANISOU 2684  CB  PHE A 350    12052  10432  11532   -997    -45   3187
ATOM   2685  CG  PHE A 350      31.191   5.023 -13.185  1.00 90.24           C  
ANISOU 2685  CG  PHE A 350    12615  10418  11255  -1030   -249   2925
ATOM   2686  CD1 PHE A 350      30.533   3.847 -13.494  1.00 88.93           C  
ANISOU 2686  CD1 PHE A 350    12857  10353  10580  -1078   -284   2843
ATOM   2687  CD2 PHE A 350      32.099   5.027 -12.143  1.00 92.24           C  
ANISOU 2687  CD2 PHE A 350    12920  10445  11682  -1020   -449   2772
ATOM   2688  CE1 PHE A 350      30.776   2.699 -12.781  1.00 89.41           C  
ANISOU 2688  CE1 PHE A 350    13394  10252  10326  -1133   -537   2646
ATOM   2689  CE2 PHE A 350      32.345   3.883 -11.422  1.00 92.65           C  
ANISOU 2689  CE2 PHE A 350    13453  10353  11396  -1061   -718   2577
ATOM   2690  CZ  PHE A 350      31.682   2.716 -11.741  1.00 91.13           C  
ANISOU 2690  CZ  PHE A 350    13692  10224  10711  -1127   -773   2531
ATOM   2691  N   VAL A 351      31.611   8.444 -16.492  1.00 96.58           N  
ANISOU 2691  N   VAL A 351    12001  11592  13104   -804    322   4078
ATOM   2692  CA  VAL A 351      31.102   9.331 -17.534  1.00 97.59           C  
ANISOU 2692  CA  VAL A 351    11883  11820  13376   -846    410   4473
ATOM   2693  C   VAL A 351      31.326   8.709 -18.908  1.00 98.91           C  
ANISOU 2693  C   VAL A 351    12098  12382  13100   -764    576   4717
ATOM   2694  O   VAL A 351      30.442   8.752 -19.777  1.00 99.43           O  
ANISOU 2694  O   VAL A 351    12208  12629  12942   -795    606   4916
ATOM   2695  CB  VAL A 351      31.739  10.726 -17.420  1.00 99.66           C  
ANISOU 2695  CB  VAL A 351    11732  11855  14278   -900    393   4726
ATOM   2696  CG1 VAL A 351      31.392  11.559 -18.632  1.00102.25           C  
ANISOU 2696  CG1 VAL A 351    11863  12277  14711   -964    437   5231
ATOM   2697  CG2 VAL A 351      31.237  11.417 -16.168  1.00 98.71           C  
ANISOU 2697  CG2 VAL A 351    11527  11380  14596   -985    217   4437
ATOM   2698  N   GLN A 352      32.503   8.106 -19.118  1.00105.99           N  
ANISOU 2698  N   GLN A 352    12964  13441  13865   -652    671   4654
ATOM   2699  CA  GLN A 352      32.722   7.290 -20.309  1.00109.02           C  
ANISOU 2699  CA  GLN A 352    13400  14255  13766   -564    832   4722
ATOM   2700  C   GLN A 352      31.648   6.218 -20.437  1.00107.05           C  
ANISOU 2700  C   GLN A 352    13534  14106  13034   -523    765   4503
ATOM   2701  O   GLN A 352      31.070   6.021 -21.513  1.00106.31           O  
ANISOU 2701  O   GLN A 352    13470  14327  12596   -530    864   4673
ATOM   2702  CB  GLN A 352      34.107   6.640 -20.264  1.00116.44           C  
ANISOU 2702  CB  GLN A 352    14243  15311  14687   -414    887   4489
ATOM   2703  CG  GLN A 352      35.276   7.593 -20.414  1.00121.35           C  
ANISOU 2703  CG  GLN A 352    14432  15961  15716   -476   1021   4696
ATOM   2704  CD  GLN A 352      36.613   6.878 -20.320  1.00131.33           C  
ANISOU 2704  CD  GLN A 352    15559  17352  16987   -301   1051   4350
ATOM   2705  OE1 GLN A 352      36.669   5.672 -20.073  1.00136.21           O  
ANISOU 2705  OE1 GLN A 352    16435  17970  17350   -108    911   3960
ATOM   2706  NE2 GLN A 352      37.698   7.621 -20.516  1.00134.32           N  
ANISOU 2706  NE2 GLN A 352    15522  17822  17693   -373   1206   4473
ATOM   2707  N   LEU A 353      31.364   5.516 -19.336  1.00102.62           N  
ANISOU 2707  N   LEU A 353    13281  13287  12423   -514    588   4130
ATOM   2708  CA  LEU A 353      30.363   4.454 -19.366  1.00100.96           C  
ANISOU 2708  CA  LEU A 353    13455  13139  11765   -529    518   3907
ATOM   2709  C   LEU A 353      28.992   4.993 -19.760  1.00 97.22           C  
ANISOU 2709  C   LEU A 353    12967  12734  11240   -662    548   4057
ATOM   2710  O   LEU A 353      28.396   4.549 -20.748  1.00 97.49           O  
ANISOU 2710  O   LEU A 353    13073  13054  10915   -628    619   4127
ATOM   2711  CB  LEU A 353      30.296   3.756 -18.007  1.00100.31           C  
ANISOU 2711  CB  LEU A 353    13726  12736  11652   -593    303   3544
ATOM   2712  CG  LEU A 353      29.274   2.622 -17.916  1.00 98.00           C  
ANISOU 2712  CG  LEU A 353    13869  12465  10901   -683    217   3312
ATOM   2713  CD1 LEU A 353      29.613   1.515 -18.897  1.00100.96           C  
ANISOU 2713  CD1 LEU A 353    14359  13077  10924   -486    236   3244
ATOM   2714  CD2 LEU A 353      29.195   2.084 -16.499  1.00 96.87           C  
ANISOU 2714  CD2 LEU A 353    14096  12000  10711   -849     -7   3030
ATOM   2715  N   ILE A 354      28.477   5.958 -18.994  1.00 93.98           N  
ANISOU 2715  N   ILE A 354    12431  12065  11211   -799    472   4060
ATOM   2716  CA  ILE A 354      27.097   6.396 -19.182  1.00 93.45           C  
ANISOU 2716  CA  ILE A 354    12338  12013  11155   -907    436   4068
ATOM   2717  C   ILE A 354      26.916   7.052 -20.545  1.00 94.52           C  
ANISOU 2717  C   ILE A 354    12244  12367  11301   -846    494   4503
ATOM   2718  O   ILE A 354      25.906   6.828 -21.224  1.00 94.77           O  
ANISOU 2718  O   ILE A 354    12354  12579  11074   -851    475   4520
ATOM   2719  CB  ILE A 354      26.669   7.330 -18.036  1.00 93.60           C  
ANISOU 2719  CB  ILE A 354    12201  11716  11647  -1050    324   3889
ATOM   2720  CG1 ILE A 354      26.696   6.581 -16.705  1.00 92.87           C  
ANISOU 2720  CG1 ILE A 354    12403  11482  11400  -1184    263   3460
ATOM   2721  CG2 ILE A 354      25.274   7.871 -18.280  1.00 94.81           C  
ANISOU 2721  CG2 ILE A 354    12236  11883  11904  -1127    256   3834
ATOM   2722  CD1 ILE A 354      26.535   7.475 -15.500  1.00 93.47           C  
ANISOU 2722  CD1 ILE A 354    12295  11307  11913  -1335    179   3233
ATOM   2723  N   ASN A 355      27.886   7.861 -20.979  1.00104.81           N  
ANISOU 2723  N   ASN A 355    13273  13669  12879   -817    551   4871
ATOM   2724  CA  ASN A 355      27.750   8.471 -22.298  1.00105.32           C  
ANISOU 2724  CA  ASN A 355    13174  13962  12882   -828    587   5351
ATOM   2725  C   ASN A 355      27.928   7.453 -23.416  1.00105.77           C  
ANISOU 2725  C   ASN A 355    13377  14497  12313   -753    749   5395
ATOM   2726  O   ASN A 355      27.356   7.620 -24.499  1.00106.89           O  
ANISOU 2726  O   ASN A 355    13512  14858  12244   -756    726   5523
ATOM   2727  CB  ASN A 355      28.746   9.618 -22.468  1.00106.18           C  
ANISOU 2727  CB  ASN A 355    12966  13952  13427   -897    615   5760
ATOM   2728  CG  ASN A 355      28.333  10.863 -21.710  1.00106.63           C  
ANISOU 2728  CG  ASN A 355    12817  13545  14152   -969    400   5805
ATOM   2729  OD1 ASN A 355      27.157  11.229 -21.685  1.00108.21           O  
ANISOU 2729  OD1 ASN A 355    13020  13608  14487   -978    212   5752
ATOM   2730  ND2 ASN A 355      29.303  11.528 -21.098  1.00106.36           N  
ANISOU 2730  ND2 ASN A 355    12569  13268  14575  -1009    410   5854
ATOM   2731  N   THR A 356      28.699   6.392 -23.177  1.00102.72           N  
ANISOU 2731  N   THR A 356    13125  14228  11678   -655    853   5090
ATOM   2732  CA  THR A 356      29.030   5.468 -24.256  1.00105.42           C  
ANISOU 2732  CA  THR A 356    13527  15039  11490   -564   1009   5067
ATOM   2733  C   THR A 356      27.854   4.564 -24.616  1.00104.63           C  
ANISOU 2733  C   THR A 356    13705  15092  10957   -525    950   4850
ATOM   2734  O   THR A 356      27.491   4.447 -25.792  1.00105.59           O  
ANISOU 2734  O   THR A 356    13808  15551  10760   -512   1004   4929
ATOM   2735  CB  THR A 356      30.248   4.623 -23.872  1.00109.73           C  
ANISOU 2735  CB  THR A 356    14083  15611  11998   -432   1074   4739
ATOM   2736  OG1 THR A 356      31.371   5.480 -23.629  1.00112.31           O  
ANISOU 2736  OG1 THR A 356    14102  15844  12726   -476   1148   4923
ATOM   2737  CG2 THR A 356      30.597   3.653 -24.991  1.00113.62           C  
ANISOU 2737  CG2 THR A 356    14577  16607  11986   -318   1225   4612
ATOM   2738  N   VAL A 357      27.239   3.928 -23.620  1.00106.34           N  
ANISOU 2738  N   VAL A 357    14188  15026  11188   -531    818   4464
ATOM   2739  CA  VAL A 357      26.361   2.797 -23.868  1.00106.32           C  
ANISOU 2739  CA  VAL A 357    14477  15164  10755   -506    781   4170
ATOM   2740  C   VAL A 357      24.890   3.102 -23.602  1.00105.13           C  
ANISOU 2740  C   VAL A 357    14405  14893  10649   -637    672   4102
ATOM   2741  O   VAL A 357      24.023   2.468 -24.215  1.00105.92           O  
ANISOU 2741  O   VAL A 357    14641  15209  10393   -628    664   3980
ATOM   2742  CB  VAL A 357      26.817   1.578 -23.041  1.00107.56           C  
ANISOU 2742  CB  VAL A 357    14933  15132  10803   -453    700   3749
ATOM   2743  CG1 VAL A 357      28.228   1.170 -23.433  1.00111.85           C  
ANISOU 2743  CG1 VAL A 357    15350  15833  11316   -270    774   3714
ATOM   2744  CG2 VAL A 357      26.734   1.883 -21.552  1.00105.32           C  
ANISOU 2744  CG2 VAL A 357    14765  14401  10850   -597    567   3604
ATOM   2745  N   LEU A 358      24.574   4.045 -22.718  1.00105.28           N  
ANISOU 2745  N   LEU A 358    14303  14590  11108   -753    583   4119
ATOM   2746  CA  LEU A 358      23.215   4.191 -22.217  1.00105.84           C  
ANISOU 2746  CA  LEU A 358    14423  14537  11253   -891    480   3875
ATOM   2747  C   LEU A 358      22.403   5.254 -22.949  1.00108.43           C  
ANISOU 2747  C   LEU A 358    14482  14922  11795   -872    381   4137
ATOM   2748  O   LEU A 358      21.324   5.617 -22.470  1.00112.29           O  
ANISOU 2748  O   LEU A 358    14900  15275  12489   -967    268   3894
ATOM   2749  CB  LEU A 358      23.245   4.511 -20.721  1.00105.44           C  
ANISOU 2749  CB  LEU A 358    14386  14132  11544  -1048    421   3609
ATOM   2750  CG  LEU A 358      23.856   3.444 -19.813  1.00103.70           C  
ANISOU 2750  CG  LEU A 358    14505  13789  11108  -1116    425   3332
ATOM   2751  CD1 LEU A 358      23.889   3.924 -18.368  1.00103.96           C  
ANISOU 2751  CD1 LEU A 358    14526  13522  11453  -1306    358   3112
ATOM   2752  CD2 LEU A 358      23.100   2.136 -19.937  1.00104.54           C  
ANISOU 2752  CD2 LEU A 358    14974  14025  10722  -1203    421   3047
ATOM   2753  N   ASN A 359      22.884   5.758 -24.093  1.00116.50           N  
ANISOU 2753  N   ASN A 359    15348  16144  12771   -773    399   4608
ATOM   2754  CA  ASN A 359      22.259   6.908 -24.769  1.00118.47           C  
ANISOU 2754  CA  ASN A 359    15365  16363  13286   -766    218   4961
ATOM   2755  C   ASN A 359      22.024   8.047 -23.782  1.00119.80           C  
ANISOU 2755  C   ASN A 359    15301  16084  14134   -829     46   4894
ATOM   2756  O   ASN A 359      21.105   8.856 -23.931  1.00125.08           O  
ANISOU 2756  O   ASN A 359    15791  16604  15130   -819   -191   4928
ATOM   2757  CB  ASN A 359      20.942   6.514 -25.450  1.00122.30           C  
ANISOU 2757  CB  ASN A 359    15929  17061  13478   -735    106   4818
ATOM   2758  CG  ASN A 359      20.381   7.619 -26.347  1.00125.08           C  
ANISOU 2758  CG  ASN A 359    16079  17400  14048   -696   -153   5247
ATOM   2759  OD1 ASN A 359      21.018   8.653 -26.559  1.00124.33           O  
ANISOU 2759  OD1 ASN A 359    15815  17145  14281   -718   -241   5713
ATOM   2760  ND2 ASN A 359      19.162   7.419 -26.836  1.00129.07           N  
ANISOU 2760  ND2 ASN A 359    16606  18035  14402   -651   -316   5082
ATOM   2761  N   GLY A 360      22.839   8.111 -22.738  1.00111.52           N  
ANISOU 2761  N   GLY A 360    14235  14809  13329   -879    133   4746
ATOM   2762  CA  GLY A 360      22.430   8.812 -21.546  1.00112.89           C  
ANISOU 2762  CA  GLY A 360    14240  14620  14032   -962      8   4434
ATOM   2763  C   GLY A 360      23.557   9.545 -20.858  1.00114.04           C  
ANISOU 2763  C   GLY A 360    14217  14491  14623   -981     22   4570
ATOM   2764  O   GLY A 360      24.715   9.515 -21.282  1.00113.16           O  
ANISOU 2764  O   GLY A 360    14106  14463  14427   -939    142   4907
ATOM   2765  N   ASP A 361      23.177  10.243 -19.792  1.00113.56           N  
ANISOU 2765  N   ASP A 361    13965  14124  15060  -1055   -100   4253
ATOM   2766  CA  ASP A 361      21.762  10.363 -19.419  1.00119.43           C  
ANISOU 2766  CA  ASP A 361    14621  14830  15925  -1116   -232   3811
ATOM   2767  C   ASP A 361      21.625  11.639 -18.626  1.00123.22           C  
ANISOU 2767  C   ASP A 361    14721  14939  17156  -1138   -426   3640
ATOM   2768  O   ASP A 361      22.495  12.507 -18.679  1.00121.69           O  
ANISOU 2768  O   ASP A 361    14342  14507  17390  -1085   -501   3993
ATOM   2769  CB  ASP A 361      21.261   9.177 -18.577  1.00120.48           C  
ANISOU 2769  CB  ASP A 361    15042  15134  15601  -1283    -75   3255
ATOM   2770  CG  ASP A 361      19.746   9.040 -18.617  1.00129.93           C  
ANISOU 2770  CG  ASP A 361    16177  16453  16739  -1360   -148   2843
ATOM   2771  OD1 ASP A 361      19.100   9.856 -19.306  1.00133.71           O  
ANISOU 2771  OD1 ASP A 361    16383  16862  17559  -1232   -359   2974
ATOM   2772  OD2 ASP A 361      19.198   8.128 -17.967  1.00132.08           O1-
ANISOU 2772  OD2 ASP A 361    16669  16879  16637  -1564    -19   2389
ATOM   2773  N   GLN A 362      20.520  11.771 -17.919  1.00127.39           N  
ANISOU 2773  N   GLN A 362    15101  15434  17868  -1228   -508   3066
ATOM   2774  CA  GLN A 362      20.499  12.680 -16.789  1.00128.80           C  
ANISOU 2774  CA  GLN A 362    14949  15329  18661  -1297   -614   2680
ATOM   2775  C   GLN A 362      20.209  11.946 -15.493  1.00128.30           C  
ANISOU 2775  C   GLN A 362    15024  15433  18292  -1552   -417   2029
ATOM   2776  O   GLN A 362      20.798  12.269 -14.457  1.00124.97           O  
ANISOU 2776  O   GLN A 362    14514  14875  18095  -1652   -385   1820
ATOM   2777  CB  GLN A 362      19.467  13.799 -17.000  1.00134.83           C  
ANISOU 2777  CB  GLN A 362    15278  15864  20087  -1191   -949   2494
ATOM   2778  CG  GLN A 362      19.842  15.090 -16.280  1.00134.28           C  
ANISOU 2778  CG  GLN A 362    14797  15380  20845  -1157  -1155   2374
ATOM   2779  CD  GLN A 362      19.550  15.065 -14.795  1.00133.64           C  
ANISOU 2779  CD  GLN A 362    14551  15348  20880  -1353  -1040   1581
ATOM   2780  OE1 GLN A 362      18.598  14.430 -14.343  1.00133.22           O  
ANISOU 2780  OE1 GLN A 362    14536  15585  20497  -1519   -915   1004
ATOM   2781  NE2 GLN A 362      20.393  15.743 -14.021  1.00131.49           N  
ANISOU 2781  NE2 GLN A 362    14094  14824  21041  -1372  -1068   1542
ATOM   2782  N   HIS A 363      19.338  10.936 -15.535  1.00119.33           N  
ANISOU 2782  N   HIS A 363    14126  14603  16610  -1694   -288   1724
ATOM   2783  CA  HIS A 363      19.070  10.130 -14.350  1.00115.75           C  
ANISOU 2783  CA  HIS A 363    13887  14337  15754  -2024    -95   1178
ATOM   2784  C   HIS A 363      20.337   9.436 -13.868  1.00110.11           C  
ANISOU 2784  C   HIS A 363    13558  13597  14683  -2087     30   1419
ATOM   2785  O   HIS A 363      20.753   9.599 -12.715  1.00107.55           O  
ANISOU 2785  O   HIS A 363    13221  13197  14446  -2260     56   1151
ATOM   2786  CB  HIS A 363      17.980   9.101 -14.649  1.00116.90           C  
ANISOU 2786  CB  HIS A 363    14263  14803  15350  -2187     17    905
ATOM   2787  CG  HIS A 363      16.655   9.701 -14.999  1.00120.67           C  
ANISOU 2787  CG  HIS A 363    14340  15337  16173  -2142   -120    540
ATOM   2788  ND1 HIS A 363      16.292   9.995 -16.295  1.00125.44           N  
ANISOU 2788  ND1 HIS A 363    14831  15909  16924  -1853   -307    891
ATOM   2789  CD2 HIS A 363      15.604  10.058 -14.223  1.00118.61           C  
ANISOU 2789  CD2 HIS A 363    13744  15179  16144  -2351   -121   -186
ATOM   2790  CE1 HIS A 363      15.075  10.508 -16.304  1.00125.94           C  
ANISOU 2790  CE1 HIS A 363    14514  16003  17334  -1849   -459    409
ATOM   2791  NE2 HIS A 363      14.635  10.557 -15.059  1.00121.76           N  
ANISOU 2791  NE2 HIS A 363    13815  15568  16880  -2145   -334   -282
ATOM   2792  N   PHE A 364      20.967   8.649 -14.748  1.00112.05           N  
ANISOU 2792  N   PHE A 364    14129  13913  14530  -1938     84   1886
ATOM   2793  CA  PHE A 364      22.166   7.914 -14.355  1.00105.79           C  
ANISOU 2793  CA  PHE A 364    13684  13079  13432  -1953    149   2064
ATOM   2794  C   PHE A 364      23.279   8.861 -13.932  1.00104.08           C  
ANISOU 2794  C   PHE A 364    13214  12602  13728  -1836     77   2242
ATOM   2795  O   PHE A 364      24.016   8.576 -12.981  1.00101.55           O  
ANISOU 2795  O   PHE A 364    13059  12202  13324  -1942     79   2117
ATOM   2796  CB  PHE A 364      22.645   7.010 -15.494  1.00101.86           C  
ANISOU 2796  CB  PHE A 364    13472  12717  12514  -1764    201   2468
ATOM   2797  CG  PHE A 364      21.721   5.860 -15.798  1.00102.26           C  
ANISOU 2797  CG  PHE A 364    13847  13002  12006  -1895    267   2270
ATOM   2798  CD1 PHE A 364      21.670   4.758 -14.966  1.00 99.11           C  
ANISOU 2798  CD1 PHE A 364    13873  12630  11153  -2156    300   1996
ATOM   2799  CD2 PHE A 364      20.935   5.868 -16.934  1.00105.64           C  
ANISOU 2799  CD2 PHE A 364    14175  13607  12358  -1772    266   2383
ATOM   2800  CE1 PHE A 364      20.837   3.699 -15.248  1.00 98.85           C  
ANISOU 2800  CE1 PHE A 364    14143  12780  10633  -2308    350   1826
ATOM   2801  CE2 PHE A 364      20.097   4.812 -17.221  1.00106.17           C  
ANISOU 2801  CE2 PHE A 364    14518  13887  11936  -1893    324   2176
ATOM   2802  CZ  PHE A 364      20.048   3.727 -16.377  1.00102.63           C  
ANISOU 2802  CZ  PHE A 364    14478  13448  11070  -2168    377   1893
ATOM   2803  N   MET A 365      23.421   9.990 -14.631  1.00101.71           N  
ANISOU 2803  N   MET A 365    12527  12152  13966  -1634    -18   2548
ATOM   2804  CA  MET A 365      24.406  10.987 -14.223  1.00100.44           C  
ANISOU 2804  CA  MET A 365    12082  11716  14363  -1555    -95   2695
ATOM   2805  C   MET A 365      24.138  11.468 -12.803  1.00102.58           C  
ANISOU 2805  C   MET A 365    12181  11872  14922  -1748   -145   2146
ATOM   2806  O   MET A 365      25.068  11.609 -11.998  1.00100.39           O  
ANISOU 2806  O   MET A 365    11902  11468  14774  -1780   -153   2093
ATOM   2807  CB  MET A 365      24.395  12.164 -15.197  1.00102.30           C  
ANISOU 2807  CB  MET A 365    11949  11773  15145  -1375   -235   3111
ATOM   2808  CG  MET A 365      24.864  11.825 -16.600  1.00 99.07           C  
ANISOU 2808  CG  MET A 365    11679  11523  14439  -1230   -169   3701
ATOM   2809  SD  MET A 365      26.578  11.282 -16.646  1.00 92.91           S  
ANISOU 2809  SD  MET A 365    11059  10802  13441  -1167     -3   3990
ATOM   2810  CE  MET A 365      27.418  12.802 -16.214  1.00 94.24           C  
ANISOU 2810  CE  MET A 365    10785  10583  14439  -1158   -126   4165
ATOM   2811  N   SER A 366      22.868  11.714 -12.473  1.00108.09           N  
ANISOU 2811  N   SER A 366    12707  12648  15713  -1885   -178   1684
ATOM   2812  CA  SER A 366      22.529  12.133 -11.119  1.00108.16           C  
ANISOU 2812  CA  SER A 366    12517  12642  15935  -2114   -190   1067
ATOM   2813  C   SER A 366      22.804  11.029 -10.106  1.00104.61           C  
ANISOU 2813  C   SER A 366    12520  12392  14835  -2409    -52    818
ATOM   2814  O   SER A 366      23.194  11.318  -8.969  1.00102.97           O  
ANISOU 2814  O   SER A 366    12243  12141  14739  -2570    -69    509
ATOM   2815  CB  SER A 366      21.066  12.569 -11.053  1.00110.99           C  
ANISOU 2815  CB  SER A 366    12551  13105  16514  -2208   -240    547
ATOM   2816  OG  SER A 366      20.717  12.990  -9.746  1.00107.81           O  
ANISOU 2816  OG  SER A 366    11899  12760  16302  -2456   -222   -134
ATOM   2817  N   ALA A 367      22.610   9.765 -10.493  1.00102.09           N  
ANISOU 2817  N   ALA A 367    12675  12274  13840  -2495     51    951
ATOM   2818  CA  ALA A 367      22.956   8.657  -9.606  1.00 98.07           C  
ANISOU 2818  CA  ALA A 367    12671  11875  12715  -2775    102    818
ATOM   2819  C   ALA A 367      24.455   8.629  -9.330  1.00 95.77           C  
ANISOU 2819  C   ALA A 367    12508  11367  12514  -2612      3   1128
ATOM   2820  O   ALA A 367      24.887   8.445  -8.186  1.00 94.21           O  
ANISOU 2820  O   ALA A 367    12483  11149  12165  -2825    -52    906
ATOM   2821  CB  ALA A 367      22.491   7.334 -10.215  1.00 95.77           C  
ANISOU 2821  CB  ALA A 367    12850  11766  11773  -2858    177    941
ATOM   2822  N   LEU A 368      25.263   8.797 -10.380  1.00 84.61           N  
ANISOU 2822  N   LEU A 368    11005   9819  11322  -2254    -25   1624
ATOM   2823  CA  LEU A 368      26.704   8.963 -10.218  1.00 84.32           C  
ANISOU 2823  CA  LEU A 368    10952   9587  11500  -2069   -108   1874
ATOM   2824  C   LEU A 368      27.021  10.079  -9.231  1.00 85.32           C  
ANISOU 2824  C   LEU A 368    10710   9545  12164  -2129   -185   1622
ATOM   2825  O   LEU A 368      27.839   9.909  -8.317  1.00 85.66           O  
ANISOU 2825  O   LEU A 368    10886   9505  12155  -2194   -275   1510
ATOM   2826  CB  LEU A 368      27.335   9.247 -11.584  1.00 83.82           C  
ANISOU 2826  CB  LEU A 368    10704   9478  11666  -1738    -73   2388
ATOM   2827  CG  LEU A 368      28.821   9.581 -11.701  1.00 83.78           C  
ANISOU 2827  CG  LEU A 368    10550   9312  11971  -1530   -112   2668
ATOM   2828  CD1 LEU A 368      29.682   8.463 -11.187  1.00 83.89           C  
ANISOU 2828  CD1 LEU A 368    10964   9324  11588  -1518   -192   2596
ATOM   2829  CD2 LEU A 368      29.157   9.874 -13.151  1.00 83.66           C  
ANISOU 2829  CD2 LEU A 368    10341   9362  12083  -1313    -20   3149
ATOM   2830  N   ASP A 369      26.360  11.229  -9.397  1.00 88.06           N  
ANISOU 2830  N   ASP A 369    10583   9824  13052  -2100   -190   1501
ATOM   2831  CA  ASP A 369      26.628  12.377  -8.537  1.00 89.40           C  
ANISOU 2831  CA  ASP A 369    10335   9807  13827  -2128   -284   1223
ATOM   2832  C   ASP A 369      26.276  12.082  -7.085  1.00 89.37           C  
ANISOU 2832  C   ASP A 369    10470   9965  13523  -2476   -278    636
ATOM   2833  O   ASP A 369      27.006  12.479  -6.170  1.00 89.13           O  
ANISOU 2833  O   ASP A 369    10336   9830  13698  -2520   -362    461
ATOM   2834  CB  ASP A 369      25.858  13.597  -9.043  1.00 92.26           C  
ANISOU 2834  CB  ASP A 369    10176  10026  14852  -2020   -356   1167
ATOM   2835  CG  ASP A 369      26.405  14.126 -10.356  1.00 92.23           C  
ANISOU 2835  CG  ASP A 369    10012   9819  15213  -1732   -410   1808
ATOM   2836  OD1 ASP A 369      27.627  14.003 -10.588  1.00 89.15           O  
ANISOU 2836  OD1 ASP A 369     9706   9344  14822  -1617   -385   2184
ATOM   2837  OD2 ASP A 369      25.612  14.656 -11.161  1.00 95.44           O1-
ANISOU 2837  OD2 ASP A 369    10208  10167  15889  -1643   -487   1928
ATOM   2838  N   LYS A 370      25.160  11.391  -6.850  1.00 86.74           N  
ANISOU 2838  N   LYS A 370    10366   9914  12676  -2760   -175    316
ATOM   2839  CA  LYS A 370      24.787  11.040  -5.484  1.00 85.31           C  
ANISOU 2839  CA  LYS A 370    10361   9963  12091  -3189   -139   -225
ATOM   2840  C   LYS A 370      25.790  10.065  -4.882  1.00 84.25           C  
ANISOU 2840  C   LYS A 370    10781   9802  11429  -3292   -230    -28
ATOM   2841  O   LYS A 370      26.230  10.231  -3.736  1.00 84.93           O  
ANISOU 2841  O   LYS A 370    10894   9906  11468  -3488   -313   -299
ATOM   2842  CB  LYS A 370      23.382  10.441  -5.471  1.00 84.09           C  
ANISOU 2842  CB  LYS A 370    10346  10143  11461  -3518     18   -574
ATOM   2843  CG  LYS A 370      22.278  11.395  -5.895  1.00 85.93           C  
ANISOU 2843  CG  LYS A 370     9999  10419  12232  -3439     55   -916
ATOM   2844  CD  LYS A 370      20.940  10.674  -5.922  1.00 84.70           C  
ANISOU 2844  CD  LYS A 370     9993  10627  11564  -3771    223  -1277
ATOM   2845  CE  LYS A 370      19.819  11.563  -6.427  1.00 86.85           C  
ANISOU 2845  CE  LYS A 370     9672  10927  12398  -3642    207  -1645
ATOM   2846  NZ  LYS A 370      18.527  10.819  -6.492  1.00 85.62           N1+
ANISOU 2846  NZ  LYS A 370     9637  11150  11746  -3967    382  -2028
ATOM   2847  N   ALA A 371      26.166   9.039  -5.650  1.00 87.30           N  
ANISOU 2847  N   ALA A 371    11601  10139  11429  -3150   -253    420
ATOM   2848  CA  ALA A 371      27.099   8.031  -5.158  1.00 86.11           C  
ANISOU 2848  CA  ALA A 371    11991   9905  10821  -3202   -419    599
ATOM   2849  C   ALA A 371      28.425   8.666  -4.760  1.00 87.76           C  
ANISOU 2849  C   ALA A 371    11987   9873  11486  -2964   -582    693
ATOM   2850  O   ALA A 371      28.857   8.567  -3.604  1.00 87.44           O  
ANISOU 2850  O   ALA A 371    12121   9827  11276  -3172   -731    475
ATOM   2851  CB  ALA A 371      27.308   6.951  -6.222  1.00 84.42           C  
ANISOU 2851  CB  ALA A 371    12155   9643  10277  -2997   -439   1016
ATOM   2852  N   LEU A 372      29.081   9.342  -5.708  1.00 80.35           N  
ANISOU 2852  N   LEU A 372    10664   8750  11116  -2558   -560   1014
ATOM   2853  CA  LEU A 372      30.327  10.022  -5.381  1.00 81.62           C  
ANISOU 2853  CA  LEU A 372    10554   8688  11770  -2348   -689   1080
ATOM   2854  C   LEU A 372      30.126  11.109  -4.334  1.00 82.74           C  
ANISOU 2854  C   LEU A 372    10309   8820  12310  -2520   -713    644
ATOM   2855  O   LEU A 372      31.090  11.495  -3.666  1.00 83.89           O  
ANISOU 2855  O   LEU A 372    10332   8821  12721  -2455   -858    568
ATOM   2856  CB  LEU A 372      30.953  10.604  -6.646  1.00 80.79           C  
ANISOU 2856  CB  LEU A 372    10083   8435  12178  -1971   -615   1506
ATOM   2857  CG  LEU A 372      31.448   9.546  -7.630  1.00 80.35           C  
ANISOU 2857  CG  LEU A 372    10347   8420  11762  -1768   -602   1876
ATOM   2858  CD1 LEU A 372      31.937  10.188  -8.914  1.00 79.81           C  
ANISOU 2858  CD1 LEU A 372     9891   8305  12126  -1489   -474   2278
ATOM   2859  CD2 LEU A 372      32.547   8.722  -6.987  1.00 81.86           C  
ANISOU 2859  CD2 LEU A 372    10873   8510  11720  -1710   -825   1837
ATOM   2860  N   THR A 373      28.895  11.604  -4.174  1.00 86.55           N  
ANISOU 2860  N   THR A 373    10562   9463  12859  -2729   -586    300
ATOM   2861  CA  THR A 373      28.602  12.503  -3.063  1.00 87.08           C  
ANISOU 2861  CA  THR A 373    10272   9587  13227  -2939   -611   -251
ATOM   2862  C   THR A 373      28.764  11.784  -1.732  1.00 87.92           C  
ANISOU 2862  C   THR A 373    10809   9892  12703  -3313   -700   -558
ATOM   2863  O   THR A 373      29.295  12.353  -0.770  1.00 89.20           O  
ANISOU 2863  O   THR A 373    10783  10026  13083  -3382   -813   -851
ATOM   2864  CB  THR A 373      27.187  13.069  -3.191  1.00 86.23           C  
ANISOU 2864  CB  THR A 373     9814   9649  13300  -3085   -470   -643
ATOM   2865  OG1 THR A 373      27.073  13.816  -4.407  1.00 85.39           O  
ANISOU 2865  OG1 THR A 373     9324   9307  13815  -2736   -470   -316
ATOM   2866  CG2 THR A 373      26.858  13.969  -2.009  1.00 86.69           C  
ANISOU 2866  CG2 THR A 373     9454   9814  13671  -3309   -492  -1327
ATOM   2867  N   SER A 374      28.320  10.526  -1.661  1.00 84.78           N  
ANISOU 2867  N   SER A 374    11014   9687  11512  -3579   -678   -479
ATOM   2868  CA  SER A 374      28.464   9.758  -0.429  1.00 85.66           C  
ANISOU 2868  CA  SER A 374    11636   9967  10946  -3995   -812   -680
ATOM   2869  C   SER A 374      29.863   9.178  -0.252  1.00 86.92           C  
ANISOU 2869  C   SER A 374    12162   9855  11007  -3781  -1116   -324
ATOM   2870  O   SER A 374      30.242   8.848   0.877  1.00 88.47           O  
ANISOU 2870  O   SER A 374    12682  10113  10821  -4057  -1321   -489
ATOM   2871  CB  SER A 374      27.433   8.630  -0.385  1.00 84.45           C  
ANISOU 2871  CB  SER A 374    12014  10086   9987  -4422   -707   -718
ATOM   2872  OG  SER A 374      27.560   7.878   0.809  1.00 85.69           O  
ANISOU 2872  OG  SER A 374    12724  10395   9440  -4896   -868   -850
ATOM   2873  N   VAL A 375      30.634   9.053  -1.335  1.00 79.96           N  
ANISOU 2873  N   VAL A 375    11222   8703  10456  -3310  -1164    129
ATOM   2874  CA  VAL A 375      31.979   8.490  -1.234  1.00 80.19           C  
ANISOU 2874  CA  VAL A 375    11528   8482  10459  -3064  -1465    393
ATOM   2875  C   VAL A 375      32.915   9.435  -0.491  1.00 81.65           C  
ANISOU 2875  C   VAL A 375    11328   8539  11156  -2945  -1607    198
ATOM   2876  O   VAL A 375      33.740   9.002   0.323  1.00 83.30           O  
ANISOU 2876  O   VAL A 375    11841   8653  11156  -2979  -1920    162
ATOM   2877  CB  VAL A 375      32.521   8.161  -2.637  1.00 78.17           C  
ANISOU 2877  CB  VAL A 375    11214   8052  10436  -2615  -1424    835
ATOM   2878  CG1 VAL A 375      33.980   7.731  -2.561  1.00 78.94           C  
ANISOU 2878  CG1 VAL A 375    11443   7901  10648  -2311  -1730   1000
ATOM   2879  CG2 VAL A 375      31.682   7.084  -3.288  1.00 77.08           C  
ANISOU 2879  CG2 VAL A 375    11514   8030   9741  -2731  -1341    997
ATOM   2880  N   VAL A 376      32.792  10.738  -0.742  1.00 80.26           N  
ANISOU 2880  N   VAL A 376    10487   8334  11675  -2808  -1423     60
ATOM   2881  CA  VAL A 376      33.832  11.702  -0.395  1.00 81.38           C  
ANISOU 2881  CA  VAL A 376    10172   8275  12472  -2587  -1540    -33
ATOM   2882  C   VAL A 376      33.690  12.142   1.059  1.00 83.93           C  
ANISOU 2882  C   VAL A 376    10439   8749  12703  -2913  -1650   -556
ATOM   2883  O   VAL A 376      34.383  13.059   1.515  1.00 85.29           O  
ANISOU 2883  O   VAL A 376    10181   8790  13435  -2788  -1741   -753
ATOM   2884  CB  VAL A 376      33.781  12.904  -1.356  1.00 80.67           C  
ANISOU 2884  CB  VAL A 376     9419   8031  13199  -2319  -1337     98
ATOM   2885  CG1 VAL A 376      32.565  13.773  -1.060  1.00 81.54           C  
ANISOU 2885  CG1 VAL A 376     9169   8281  13533  -2542  -1181   -303
ATOM   2886  CG2 VAL A 376      35.088  13.696  -1.337  1.00 81.69           C  
ANISOU 2886  CG2 VAL A 376     9131   7894  14014  -2038  -1455    168
ATOM   2887  N   ASN A 377      32.808  11.485   1.806  1.00 96.09           N  
ANISOU 2887  N   ASN A 377    12407  10589  13513  -3367  -1638   -802
ATOM   2888  CA  ASN A 377      32.577  11.817   3.209  1.00 97.56           C  
ANISOU 2888  CA  ASN A 377    12577  11028  13464  -3768  -1711  -1335
ATOM   2889  C   ASN A 377      32.737  10.554   4.047  1.00 97.80           C  
ANISOU 2889  C   ASN A 377    13406  11185  12568  -4125  -1974  -1259
ATOM   2890  O   ASN A 377      31.890   9.656   3.997  1.00 96.02           O  
ANISOU 2890  O   ASN A 377    13665  11155  11664  -4466  -1892  -1181
ATOM   2891  CB  ASN A 377      31.197  12.447   3.399  1.00 95.26           C  
ANISOU 2891  CB  ASN A 377    11928  11064  13204  -4087  -1407  -1825
ATOM   2892  CG  ASN A 377      31.075  13.794   2.707  1.00 94.98           C  
ANISOU 2892  CG  ASN A 377    11100  10828  14162  -3737  -1261  -1933
ATOM   2893  OD1 ASN A 377      30.316  13.952   1.749  1.00 94.05           O  
ANISOU 2893  OD1 ASN A 377    10797  10682  14256  -3623  -1073  -1805
ATOM   2894  ND2 ASN A 377      31.827  14.773   3.192  1.00 96.00           N  
ANISOU 2894  ND2 ASN A 377    10769  10791  14917  -3573  -1388  -2159
ATOM   2895  N   TYR A 378      33.825  10.489   4.810  1.00108.34           N  
ANISOU 2895  N   TYR A 378    14887  12384  13892  -4058  -2323  -1270
ATOM   2896  CA  TYR A 378      34.130   9.333   5.641  1.00110.77           C  
ANISOU 2896  CA  TYR A 378    15982  12728  13378  -4366  -2693  -1147
ATOM   2897  C   TYR A 378      33.552   9.512   7.038  1.00114.67           C  
ANISOU 2897  C   TYR A 378    16609  13652  13310  -4991  -2698  -1635
ATOM   2898  O   TYR A 378      33.586  10.608   7.602  1.00116.04           O  
ANISOU 2898  O   TYR A 378    16215  13978  13896  -5014  -2597  -2103
ATOM   2899  CB  TYR A 378      35.642   9.122   5.729  1.00111.38           C  
ANISOU 2899  CB  TYR A 378    16159  12426  13734  -3947  -3136   -918
ATOM   2900  N   ARG A 379      33.022   8.421   7.597  1.00133.15           N  
ANISOU 2900  N   ARG A 379    19701  16197  14691  -5530  -2823  -1535
ATOM   2901  CA  ARG A 379      32.493   8.415   8.962  1.00133.56           C  
ANISOU 2901  CA  ARG A 379    19997  16727  14021  -6237  -2840  -1954
ATOM   2902  C   ARG A 379      33.147   7.225   9.663  1.00132.39           C  
ANISOU 2902  C   ARG A 379    20694  16432  13176  -6353  -3320  -1528
ATOM   2903  O   ARG A 379      32.531   6.166   9.808  1.00130.86           O  
ANISOU 2903  O   ARG A 379    21067  16343  12310  -6630  -3250  -1204
ATOM   2904  CB  ARG A 379      30.963   8.287   8.939  1.00132.47           C  
ANISOU 2904  CB  ARG A 379    19776  17061  13495  -6584  -2295  -2138
ATOM   2905  CG  ARG A 379      30.234   9.339   8.106  1.00132.48           C  
ANISOU 2905  CG  ARG A 379    18986  17140  14212  -6424  -1883  -2517
ATOM   2906  CD  ARG A 379      28.736   9.043   8.053  1.00129.97           C  
ANISOU 2906  CD  ARG A 379    18644  17255  13483  -6697  -1407  -2658
ATOM   2907  NE  ARG A 379      28.007   9.948   7.166  1.00127.30           N  
ANISOU 2907  NE  ARG A 379    17592  16933  13842  -6480  -1083  -2972
ATOM   2908  CZ  ARG A 379      27.769   9.702   5.879  1.00122.69           C  
ANISOU 2908  CZ  ARG A 379    17020  16094  13501  -6324  -1030  -2693
ATOM   2909  NH1 ARG A 379      28.203   8.578   5.326  1.00119.63           N  
ANISOU 2909  NH1 ARG A 379    17284  15418  12750  -6226  -1240  -2075
ATOM   2910  NH2 ARG A 379      27.097  10.579   5.144  1.00120.46           N1+
ANISOU 2910  NH2 ARG A 379    16060  15820  13888  -6093   -761  -2961
ATOM   2911  N   GLU A 380      34.395   7.394  10.101  1.00110.37           N  
ANISOU 2911  N   GLU A 380    17952  13363  10619  -6115  -3812  -1506
ATOM   2912  CA  GLU A 380      35.092   6.223  10.621  1.00113.53           C  
ANISOU 2912  CA  GLU A 380    19131  13513  10494  -6104  -4332  -1046
ATOM   2913  C   GLU A 380      34.835   5.960  12.105  1.00119.58           C  
ANISOU 2913  C   GLU A 380    20196  14673  10566  -6545  -4313  -1112
ATOM   2914  O   GLU A 380      34.474   4.833  12.466  1.00122.65           O  
ANISOU 2914  O   GLU A 380    21243  15047  10310  -6848  -4378   -699
ATOM   2915  CB  GLU A 380      36.591   6.328  10.328  1.00112.63           C  
ANISOU 2915  CB  GLU A 380    18965  12856  10972  -5550  -4922   -927
ATOM   2916  CG  GLU A 380      36.913   6.210   8.850  1.00107.78           C  
ANISOU 2916  CG  GLU A 380    18046  11847  11060  -4883  -4776   -618
ATOM   2917  CD  GLU A 380      38.398   6.242   8.572  1.00107.62           C  
ANISOU 2917  CD  GLU A 380    17838  11364  11688  -4215  -5200   -491
ATOM   2918  OE1 GLU A 380      39.177   6.495   9.516  1.00110.89           O  
ANISOU 2918  OE1 GLU A 380    18274  11746  12112  -4218  -5593   -675
ATOM   2919  OE2 GLU A 380      38.786   6.000   7.409  1.00104.58           O1-
ANISOU 2919  OE2 GLU A 380    17269  10679  11788  -3701  -5140   -240
ATOM   2920  N   PRO A 381      34.999   6.947  13.004  1.00119.09           N  
ANISOU 2920  N   PRO A 381    19669  14940  10639  -6627  -4229  -1611
ATOM   2921  CA  PRO A 381      34.783   6.504  14.382  1.00125.51           C  
ANISOU 2921  CA  PRO A 381    20882  16097  10710  -7078  -4260  -1578
ATOM   2922  C   PRO A 381      33.493   7.043  14.984  1.00127.82           C  
ANISOU 2922  C   PRO A 381    20800  17058  10708  -7542  -3622  -2022
ATOM   2923  O   PRO A 381      33.593   7.792  15.956  1.00131.32           O  
ANISOU 2923  O   PRO A 381    20908  17850  11138  -7657  -3569  -2473
ATOM   2924  CB  PRO A 381      35.992   7.082  15.114  1.00127.83           C  
ANISOU 2924  CB  PRO A 381    21005  16289  11275  -6836  -4712  -1809
ATOM   2925  CG  PRO A 381      36.212   8.377  14.414  1.00123.24           C  
ANISOU 2925  CG  PRO A 381    19576  15651  11599  -6475  -4543  -2297
ATOM   2926  CD  PRO A 381      35.821   8.171  12.963  1.00117.53           C  
ANISOU 2926  CD  PRO A 381    18795  14636  11225  -6280  -4359  -2052
ATOM   2927  N   SER A 383      38.285  11.442  10.142  1.00126.49           N  
ANISOU 2927  N   SER A 383    17396  14597  16066  -4223  -4147  -2351
ATOM   2928  CA  SER A 383      37.677  11.589  11.460  1.00130.29           C  
ANISOU 2928  CA  SER A 383    18048  15568  15888  -4847  -4164  -2816
ATOM   2929  C   SER A 383      37.746  13.027  11.975  1.00132.82           C  
ANISOU 2929  C   SER A 383    17538  16059  16868  -4803  -3983  -3450
ATOM   2930  O   SER A 383      38.634  13.354  12.763  1.00135.56           O  
ANISOU 2930  O   SER A 383    17788  16370  17349  -4724  -4319  -3673
ATOM   2931  CB  SER A 383      38.352  10.655  12.467  1.00131.38           C  
ANISOU 2931  CB  SER A 383    18964  15694  15261  -5086  -4773  -2663
ATOM   2932  OG  SER A 383      37.836  10.863  13.770  1.00131.37           O  
ANISOU 2932  OG  SER A 383    19090  16227  14599  -5702  -4765  -3117
ATOM   2933  N   VAL A 384      36.825  13.891  11.549  1.00126.12           N  
ANISOU 2933  N   VAL A 384    16079  15373  16467  -4838  -3497  -3771
ATOM   2934  CA  VAL A 384      35.761  13.583  10.597  1.00123.86           C  
ANISOU 2934  CA  VAL A 384    15846  15131  16085  -4902  -3115  -3551
ATOM   2935  C   VAL A 384      35.434  14.909   9.896  1.00123.58           C  
ANISOU 2935  C   VAL A 384    14892  14966  17096  -4576  -2767  -3828
ATOM   2936  O   VAL A 384      35.305  15.938  10.560  1.00123.99           O  
ANISOU 2936  O   VAL A 384    14375  15192  17542  -4666  -2701  -4442
ATOM   2937  CB  VAL A 384      34.518  12.936  11.306  1.00123.69           C  
ANISOU 2937  CB  VAL A 384    16308  15682  15007  -5649  -2949  -3792
ATOM   2938  CG1 VAL A 384      33.894  13.883  12.324  1.00126.46           C  
ANISOU 2938  CG1 VAL A 384    16145  16501  15403  -5861  -2708  -4498
ATOM   2939  CG2 VAL A 384      33.478  12.450  10.300  1.00119.67           C  
ANISOU 2939  CG2 VAL A 384    15929  15195  14348  -5706  -2605  -3525
ATOM   2940  N   CYS A 385      35.334  14.916   8.566  1.00115.44           N  
ANISOU 2940  N   CYS A 385    12940  11671  19251   -177  -4213   2669
ATOM   2941  CA  CYS A 385      35.444  13.723   7.735  1.00113.90           C  
ANISOU 2941  CA  CYS A 385    12515  11205  19557    -74  -4471   2597
ATOM   2942  C   CYS A 385      36.689  13.721   6.853  1.00113.14           C  
ANISOU 2942  C   CYS A 385    12308  10901  19779     63  -4465   2228
ATOM   2943  O   CYS A 385      36.671  13.136   5.772  1.00112.05           O  
ANISOU 2943  O   CYS A 385    12041  10586  19946    208  -4490   2011
ATOM   2944  CB  CYS A 385      34.203  13.585   6.851  1.00112.77           C  
ANISOU 2944  CB  CYS A 385    12388  11091  19367     57  -4320   2564
ATOM   2945  SG  CYS A 385      34.024  14.883   5.605  1.00111.83           S  
ANISOU 2945  SG  CYS A 385    12437  11079  18973    256  -3834   2182
ATOM   2946  N   LYS A 386      37.729  14.444   7.281  1.00108.87           N  
ANISOU 2946  N   LYS A 386    11830  10402  19133      9  -4401   2141
ATOM   2947  CA  LYS A 386      39.089  14.391   6.737  1.00108.56           C  
ANISOU 2947  CA  LYS A 386    11651  10174  19422     89  -4447   1852
ATOM   2948  C   LYS A 386      39.163  14.720   5.247  1.00107.37           C  
ANISOU 2948  C   LYS A 386    11492   9987  19316    299  -4164   1435
ATOM   2949  O   LYS A 386      40.248  14.679   4.660  1.00107.34           O  
ANISOU 2949  O   LYS A 386    11358   9847  19579    373  -4156   1152
ATOM   2950  CB  LYS A 386      39.746  13.022   6.997  1.00108.66           C  
ANISOU 2950  CB  LYS A 386    11371   9887  20026     37  -4902   1963
ATOM   2951  CG  LYS A 386      39.266  11.863   6.124  1.00107.66           C  
ANISOU 2951  CG  LYS A 386    11052   9538  20317    162  -5054   1870
ATOM   2952  CD  LYS A 386      39.943  10.550   6.464  1.00110.26           C  
ANISOU 2952  CD  LYS A 386    11081   9541  21273    108  -5526   1988
ATOM   2953  CE  LYS A 386      39.334   9.407   5.662  1.00111.10           C  
ANISOU 2953  CE  LYS A 386    11021   9425  21765    220  -5683   1908
ATOM   2954  NZ  LYS A 386      39.570   9.546   4.198  1.00110.19           N1+
ANISOU 2954  NZ  LYS A 386    10872   9234  21762    435  -5397   1409
ATOM   2955  N   ALA A 387      38.031  15.044   4.625  1.00104.80           N  
ANISOU 2955  N   ALA A 387    11294   9789  18738    375  -3935   1401
ATOM   2956  CA  ALA A 387      37.997  15.399   3.209  1.00103.92           C  
ANISOU 2956  CA  ALA A 387    11199   9674  18611    525  -3674   1041
ATOM   2957  C   ALA A 387      38.377  16.858   2.953  1.00104.24           C  
ANISOU 2957  C   ALA A 387    11430   9904  18272    546  -3331    855
ATOM   2958  O   ALA A 387      39.233  17.125   2.094  1.00104.21           O  
ANISOU 2958  O   ALA A 387    11373   9857  18365    612  -3211    531
ATOM   2959  CB  ALA A 387      36.616  15.104   2.619  1.00103.03           C  
ANISOU 2959  CB  ALA A 387    11133   9600  18413    572  -3615   1117
ATOM   2960  N   PRO A 388      37.784  17.832   3.661  1.00 96.84           N  
ANISOU 2960  N   PRO A 388    10709   9176  16911    487  -3163   1037
ATOM   2961  CA  PRO A 388      38.064  19.233   3.304  1.00 97.21           C  
ANISOU 2961  CA  PRO A 388    10936   9376  16625    517  -2845    850
ATOM   2962  C   PRO A 388      39.511  19.643   3.520  1.00 97.83           C  
ANISOU 2962  C   PRO A 388    10988   9422  16760    480  -2864    699
ATOM   2963  O   PRO A 388      40.077  20.339   2.670  1.00 97.46           O  
ANISOU 2963  O   PRO A 388    10972   9412  16649    535  -2672    427
ATOM   2964  CB  PRO A 388      37.104  20.019   4.207  1.00 98.13           C  
ANISOU 2964  CB  PRO A 388    11257   9683  16346    455  -2704   1095
ATOM   2965  CG  PRO A 388      36.856  19.130   5.360  1.00 98.67           C  
ANISOU 2965  CG  PRO A 388    11255   9723  16511    336  -2974   1408
ATOM   2966  CD  PRO A 388      36.854  17.747   4.804  1.00 97.54           C  
ANISOU 2966  CD  PRO A 388    10882   9376  16803    381  -3238   1401
ATOM   2967  N   GLU A 389      40.128  19.236   4.632  1.00 99.21           N  
ANISOU 2967  N   GLU A 389    11104   9537  17054    367  -3106    889
ATOM   2968  CA  GLU A 389      41.516  19.616   4.874  1.00 99.94           C  
ANISOU 2968  CA  GLU A 389    11161   9590  17223    319  -3148    778
ATOM   2969  C   GLU A 389      42.435  19.072   3.789  1.00 99.22           C  
ANISOU 2969  C   GLU A 389    10837   9329  17532    424  -3181    464
ATOM   2970  O   GLU A 389      43.312  19.789   3.293  1.00 99.48           O  
ANISOU 2970  O   GLU A 389    10882   9403  17514    448  -3025    231
ATOM   2971  CB  GLU A 389      41.976  19.130   6.247  1.00101.09           C  
ANISOU 2971  CB  GLU A 389    11261   9679  17468    147  -3456   1076
ATOM   2972  CG  GLU A 389      43.394  19.570   6.583  1.00101.75           C  
ANISOU 2972  CG  GLU A 389    11316   9722  17622     74  -3521   1007
ATOM   2973  CD  GLU A 389      43.835  19.146   7.968  1.00103.14           C  
ANISOU 2973  CD  GLU A 389    11466   9851  17870   -139  -3848   1338
ATOM   2974  OE1 GLU A 389      43.039  18.487   8.671  1.00103.77           O  
ANISOU 2974  OE1 GLU A 389    11548   9944  17938   -240  -4025   1620
ATOM   2975  OE2 GLU A 389      44.978  19.473   8.353  1.00103.67           O1-
ANISOU 2975  OE2 GLU A 389    11511   9879  18001   -228  -3940   1334
ATOM   2976  N   LEU A 390      42.254  17.804   3.411  1.00105.14           N  
ANISOU 2976  N   LEU A 390    11369   9891  18690    480  -3380    444
ATOM   2977  CA  LEU A 390      43.041  17.247   2.316  1.00104.91           C  
ANISOU 2977  CA  LEU A 390    11111   9701  19051    585  -3374     95
ATOM   2978  C   LEU A 390      42.799  18.014   1.026  1.00104.59           C  
ANISOU 2978  C   LEU A 390    11179   9804  18754    663  -3025   -215
ATOM   2979  O   LEU A 390      43.736  18.271   0.259  1.00105.00           O  
ANISOU 2979  O   LEU A 390    11139   9851  18904    699  -2895   -527
ATOM   2980  CB  LEU A 390      42.714  15.767   2.127  1.00104.56           C  
ANISOU 2980  CB  LEU A 390    10838   9418  19471    632  -3640    122
ATOM   2981  CG  LEU A 390      43.152  14.868   3.279  1.00105.17           C  
ANISOU 2981  CG  LEU A 390    10742   9304  19913    539  -4045    413
ATOM   2982  CD1 LEU A 390      42.704  13.432   3.039  1.00106.30           C  
ANISOU 2982  CD1 LEU A 390    10670   9201  20518    586  -4318    448
ATOM   2983  CD2 LEU A 390      44.660  14.953   3.467  1.00106.20           C  
ANISOU 2983  CD2 LEU A 390    10701   9317  20332    522  -4129    289
ATOM   2984  N   LEU A 391      41.551  18.407   0.775  1.00 96.78           N  
ANISOU 2984  N   LEU A 391    10379   8954  17439    673  -2877   -120
ATOM   2985  CA  LEU A 391      41.278  19.197  -0.415  1.00 95.40           C  
ANISOU 2985  CA  LEU A 391    10319   8921  17008    709  -2578   -364
ATOM   2986  C   LEU A 391      41.759  20.638  -0.285  1.00 94.17           C  
ANISOU 2986  C   LEU A 391    10344   8946  16490    665  -2364   -404
ATOM   2987  O   LEU A 391      41.699  21.383  -1.269  1.00 93.23           O  
ANISOU 2987  O   LEU A 391    10310   8947  16164    668  -2136   -600
ATOM   2988  CB  LEU A 391      39.785  19.129  -0.730  1.00 94.35           C  
ANISOU 2988  CB  LEU A 391    10305   8851  16693    725  -2520   -219
ATOM   2989  CG  LEU A 391      39.462  17.677  -1.096  1.00 95.77           C  
ANISOU 2989  CG  LEU A 391    10292   8835  17262    765  -2733   -246
ATOM   2990  CD1 LEU A 391      37.985  17.415  -1.275  1.00 95.06           C  
ANISOU 2990  CD1 LEU A 391    10289   8778  17050    768  -2741    -47
ATOM   2991  CD2 LEU A 391      40.217  17.295  -2.346  1.00 96.80           C  
ANISOU 2991  CD2 LEU A 391    10273   8884  17623    802  -2656   -658
ATOM   2992  N   ALA A 392      42.248  21.039   0.889  1.00 94.35           N  
ANISOU 2992  N   ALA A 392    10429   8989  16432    603  -2450   -218
ATOM   2993  CA  ALA A 392      42.929  22.319   1.046  1.00 93.59           C  
ANISOU 2993  CA  ALA A 392    10481   9025  16054    554  -2288   -279
ATOM   2994  C   ALA A 392      44.433  22.186   0.846  1.00 94.84           C  
ANISOU 2994  C   ALA A 392    10460   9106  16470    542  -2346   -482
ATOM   2995  O   ALA A 392      45.053  23.055   0.222  1.00 94.34           O  
ANISOU 2995  O   ALA A 392    10442   9147  16253    528  -2163   -681
ATOM   2996  CB  ALA A 392      42.636  22.915   2.425  1.00 93.32           C  
ANISOU 2996  CB  ALA A 392    10638   9067  15751    469  -2329     16
ATOM   2997  N   LYS A 393      45.034  21.110   1.366  1.00 96.68           N  
ANISOU 2997  N   LYS A 393    10470   9150  17112    538  -2611   -421
ATOM   2998  CA  LYS A 393      46.449  20.851   1.129  1.00 98.27           C  
ANISOU 2998  CA  LYS A 393    10443   9245  17650    542  -2677   -621
ATOM   2999  C   LYS A 393      46.732  20.386  -0.290  1.00 98.95           C  
ANISOU 2999  C   LYS A 393    10339   9290  17969    632  -2539  -1007
ATOM   3000  O   LYS A 393      47.897  20.381  -0.697  1.00100.24           O  
ANISOU 3000  O   LYS A 393    10318   9413  18353    640  -2502  -1240
ATOM   3001  CB  LYS A 393      46.987  19.817   2.119  1.00100.38           C  
ANISOU 3001  CB  LYS A 393    10504   9292  18342    503  -3032   -420
ATOM   3002  CG  LYS A 393      47.042  20.297   3.558  1.00100.33           C  
ANISOU 3002  CG  LYS A 393    10669   9341  18113    358  -3184    -62
ATOM   3003  CD  LYS A 393      47.940  21.524   3.688  1.00 99.79           C  
ANISOU 3003  CD  LYS A 393    10728   9403  17786    290  -3043   -126
ATOM   3004  CE  LYS A 393      49.398  21.211   3.377  1.00101.62           C  
ANISOU 3004  CE  LYS A 393    10678   9497  18436    304  -3133   -305
ATOM   3005  NZ  LYS A 393      50.007  20.292   4.375  1.00103.96           N1+
ANISOU 3005  NZ  LYS A 393    10771   9577  19152    221  -3514    -63
ATOM   3006  N   TYR A 394      45.711  19.982  -1.045  1.00 98.38           N  
ANISOU 3006  N   TYR A 394    10298   9229  17853    684  -2459  -1084
ATOM   3007  CA  TYR A 394      45.926  19.732  -2.465  1.00 99.04           C  
ANISOU 3007  CA  TYR A 394    10259   9327  18045    726  -2279  -1474
ATOM   3008  C   TYR A 394      46.132  21.039  -3.218  1.00 97.71           C  
ANISOU 3008  C   TYR A 394    10258   9407  17463    663  -1986  -1636
ATOM   3009  O   TYR A 394      47.014  21.136  -4.079  1.00 98.78           O  
ANISOU 3009  O   TYR A 394    10259   9589  17685    648  -1843  -1958
ATOM   3010  CB  TYR A 394      44.753  18.950  -3.049  1.00 98.93           C  
ANISOU 3010  CB  TYR A 394    10255   9257  18077    767  -2299  -1488
ATOM   3011  CG  TYR A 394      44.924  18.605  -4.510  1.00 99.97           C  
ANISOU 3011  CG  TYR A 394    10275   9405  18306    777  -2123  -1901
ATOM   3012  CD1 TYR A 394      45.803  17.608  -4.909  1.00102.57           C  
ANISOU 3012  CD1 TYR A 394    10305   9546  19123    834  -2185  -2201
ATOM   3013  CD2 TYR A 394      44.204  19.273  -5.489  1.00 98.67           C  
ANISOU 3013  CD2 TYR A 394    10297   9439  17753    714  -1896  -1995
ATOM   3014  CE1 TYR A 394      45.963  17.288  -6.243  1.00103.89           C  
ANISOU 3014  CE1 TYR A 394    10376   9744  19355    823  -1996  -2617
ATOM   3015  CE2 TYR A 394      44.356  18.959  -6.826  1.00 99.90           C  
ANISOU 3015  CE2 TYR A 394    10370   9636  17953    677  -1735  -2372
ATOM   3016  CZ  TYR A 394      45.236  17.966  -7.197  1.00102.54           C  
ANISOU 3016  CZ  TYR A 394    10419   9801  18740    730  -1770  -2698
ATOM   3017  OH  TYR A 394      45.390  17.651  -8.527  1.00104.11           O  
ANISOU 3017  OH  TYR A 394    10542  10057  18959    674  -1581  -3111
ATOM   3018  N   CYS A 395      45.330  22.058  -2.899  1.00 95.63           N  
ANISOU 3018  N   CYS A 395    10275   9301  16761    619  -1897  -1415
ATOM   3019  CA  CYS A 395      45.497  23.373  -3.510  1.00 94.46           C  
ANISOU 3019  CA  CYS A 395    10293   9367  16231    546  -1662  -1516
ATOM   3020  C   CYS A 395      46.785  24.030  -3.033  1.00 94.91           C  
ANISOU 3020  C   CYS A 395    10319   9459  16285    500  -1663  -1544
ATOM   3021  O   CYS A 395      47.645  24.407  -3.840  1.00 95.56           O  
ANISOU 3021  O   CYS A 395    10317   9637  16355    454  -1522  -1800
ATOM   3022  CB  CYS A 395      44.295  24.254  -3.174  1.00 92.47           C  
ANISOU 3022  CB  CYS A 395    10323   9224  15587    526  -1594  -1259
ATOM   3023  SG  CYS A 395      42.723  23.620  -3.770  1.00 91.92           S  
ANISOU 3023  SG  CYS A 395    10297   9131  15497    562  -1590  -1186
ATOM   3024  N   ASP A 396      46.925  24.181  -1.713  1.00 94.75           N  
ANISOU 3024  N   ASP A 396    10369   9374  16258    491  -1824  -1271
ATOM   3025  CA  ASP A 396      48.140  24.752  -1.143  1.00 95.34           C  
ANISOU 3025  CA  ASP A 396    10421   9462  16343    431  -1867  -1254
ATOM   3026  C   ASP A 396      49.381  24.019  -1.635  1.00 97.47           C  
ANISOU 3026  C   ASP A 396    10366   9630  17037    454  -1909  -1509
ATOM   3027  O   ASP A 396      50.398  24.645  -1.948  1.00 97.96           O  
ANISOU 3027  O   ASP A 396    10376   9779  17064    402  -1815  -1652
ATOM   3028  CB  ASP A 396      48.064  24.708   0.383  1.00 95.42           C  
ANISOU 3028  CB  ASP A 396    10526   9388  16340    391  -2082   -917
ATOM   3029  CG  ASP A 396      49.237  25.400   1.045  1.00 95.99           C  
ANISOU 3029  CG  ASP A 396    10621   9481  16371    299  -2143   -857
ATOM   3030  OD1 ASP A 396      49.258  26.650   1.075  1.00 94.83           O  
ANISOU 3030  OD1 ASP A 396    10701   9482  15848    238  -2002   -838
ATOM   3031  OD2 ASP A 396      50.144  24.691   1.529  1.00 97.78           O1-
ANISOU 3031  OD2 ASP A 396    10631   9557  16963    281  -2350   -819
ATOM   3032  N   ASN A 397      49.310  22.690  -1.719  1.00 98.97           N  
ANISOU 3032  N   ASN A 397    10321   9629  17653    533  -2050  -1575
ATOM   3033  CA  ASN A 397      50.445  21.916  -2.210  1.00101.42           C  
ANISOU 3033  CA  ASN A 397    10288   9810  18437    576  -2079  -1851
ATOM   3034  C   ASN A 397      50.697  22.186  -3.689  1.00101.77           C  
ANISOU 3034  C   ASN A 397    10269  10013  18386    565  -1785  -2251
ATOM   3035  O   ASN A 397      51.852  22.268  -4.125  1.00103.37           O  
ANISOU 3035  O   ASN A 397    10270  10241  18767    548  -1696  -2491
ATOM   3036  CB  ASN A 397      50.199  20.426  -1.968  1.00103.11           C  
ANISOU 3036  CB  ASN A 397    10273   9756  19150    665  -2311  -1831
ATOM   3037  CG  ASN A 397      51.444  19.583  -2.175  1.00106.11           C  
ANISOU 3037  CG  ASN A 397    10263   9936  20119    721  -2399  -2066
ATOM   3038  OD1 ASN A 397      52.521  20.101  -2.473  1.00106.95           O  
ANISOU 3038  OD1 ASN A 397    10260  10118  20259    691  -2277  -2240
ATOM   3039  ND2 ASN A 397      51.297  18.271  -2.025  1.00107.95           N  
ANISOU 3039  ND2 ASN A 397    10268   9901  20846    803  -2616  -2073
ATOM   3040  N   LEU A 398      49.630  22.333  -4.474  1.00100.49           N  
ANISOU 3040  N   LEU A 398    10273   9971  17938    553  -1634  -2318
ATOM   3041  CA  LEU A 398      49.750  22.528  -5.913  1.00101.05           C  
ANISOU 3041  CA  LEU A 398    10305  10210  17880    497  -1370  -2681
ATOM   3042  C   LEU A 398      50.039  23.971  -6.300  1.00 99.81           C  
ANISOU 3042  C   LEU A 398    10335  10321  17268    368  -1179  -2687
ATOM   3043  O   LEU A 398      50.196  24.251  -7.494  1.00100.41           O  
ANISOU 3043  O   LEU A 398    10390  10576  17186    274   -964  -2964
ATOM   3044  CB  LEU A 398      48.474  22.057  -6.615  1.00100.45           C  
ANISOU 3044  CB  LEU A 398    10330  10143  17693    503  -1323  -2721
ATOM   3045  N   LEU A 399      50.110  24.891  -5.336  1.00 98.33           N  
ANISOU 3045  N   LEU A 399    10333  10168  16860    341  -1259  -2392
ATOM   3046  CA  LEU A 399      50.424  26.282  -5.632  1.00 97.32           C  
ANISOU 3046  CA  LEU A 399    10381  10264  16333    220  -1113  -2379
ATOM   3047  C   LEU A 399      51.816  26.714  -5.195  1.00 98.34           C  
ANISOU 3047  C   LEU A 399    10393  10405  16565    179  -1147  -2397
ATOM   3048  O   LEU A 399      52.284  27.763  -5.647  1.00 98.04           O  
ANISOU 3048  O   LEU A 399    10441  10560  16249     64  -1017  -2451
ATOM   3049  CB  LEU A 399      49.392  27.213  -4.980  1.00 94.96           C  
ANISOU 3049  CB  LEU A 399    10415  10010  15655    203  -1146  -2055
ATOM   3050  CG  LEU A 399      47.969  27.130  -5.531  1.00 93.80           C  
ANISOU 3050  CG  LEU A 399    10412   9898  15328    212  -1084  -2007
ATOM   3051  CD1 LEU A 399      47.037  28.029  -4.734  1.00 91.89           C  
ANISOU 3051  CD1 LEU A 399    10455   9670  14787    217  -1116  -1691
ATOM   3052  CD2 LEU A 399      47.942  27.489  -7.006  1.00 94.16           C  
ANISOU 3052  CD2 LEU A 399    10455  10136  15186     90   -887  -2253
ATOM   3053  N   LYS A 400      52.488  25.942  -4.342  1.00103.68           N  
ANISOU 3053  N   LYS A 400    10872  10879  17644    254  -1337  -2331
ATOM   3054  CA  LYS A 400      53.807  26.325  -3.862  1.00104.40           C  
ANISOU 3054  CA  LYS A 400    10843  10962  17863    206  -1400  -2307
ATOM   3055  C   LYS A 400      54.830  26.289  -5.000  1.00105.53           C  
ANISOU 3055  C   LYS A 400    10727  11226  18144    163  -1202  -2680
ATOM   3056  O   LYS A 400      54.560  25.818  -6.109  1.00105.88           O  
ANISOU 3056  O   LYS A 400    10667  11341  18223    168  -1026  -2979
ATOM   3057  CB  LYS A 400      54.253  25.412  -2.720  1.00104.21           C  
ANISOU 3057  CB  LYS A 400    10640  10672  18283    276  -1684  -2128
ATOM   3058  CG  LYS A 400      53.359  25.467  -1.492  1.00103.38           C  
ANISOU 3058  CG  LYS A 400    10784  10478  18018    276  -1883  -1748
ATOM   3059  CD  LYS A 400      53.438  26.818  -0.800  1.00103.77           C  
ANISOU 3059  CD  LYS A 400    11136  10658  17633    164  -1881  -1521
ATOM   3060  CE  LYS A 400      52.529  26.872   0.420  1.00103.32           C  
ANISOU 3060  CE  LYS A 400    11326  10536  17395    148  -2040  -1183
ATOM   3061  NZ  LYS A 400      53.003  25.983   1.517  1.00103.37           N1+
ANISOU 3061  NZ  LYS A 400    11176  10335  17763    130  -2341   -975
ATOM   3062  N   LYS A 401      56.029  26.794  -4.702  1.00129.82           N  
ANISOU 3062  N   LYS A 401    13698  14337  21291    101  -1229  -2660
ATOM   3063  CA  LYS A 401      57.065  26.913  -5.722  1.00130.76           C  
ANISOU 3063  CA  LYS A 401    13571  14610  21501     36  -1023  -2996
ATOM   3064  C   LYS A 401      57.606  25.544  -6.122  1.00130.24           C  
ANISOU 3064  C   LYS A 401    13095  14372  22020    149  -1003  -3304
ATOM   3065  O   LYS A 401      57.567  25.168  -7.300  1.00130.80           O  
ANISOU 3065  O   LYS A 401    13028  14553  22115    135   -769  -3674
ATOM   3066  CB  LYS A 401      58.188  27.821  -5.217  1.00131.29           C  
ANISOU 3066  CB  LYS A 401    13631  14748  21505    -62  -1081  -2854
ATOM   3067  CG  LYS A 401      59.238  28.153  -6.263  1.00132.24           C  
ANISOU 3067  CG  LYS A 401    13527  15083  21635   -163   -851  -3165
ATOM   3068  CD  LYS A 401      60.308  29.076  -5.695  1.00133.41           C  
ANISOU 3068  CD  LYS A 401    13681  15292  21716   -267   -942  -2978
ATOM   3069  CE  LYS A 401      60.017  30.538  -6.020  1.00135.22           C  
ANISOU 3069  CE  LYS A 401    14248  15787  21342   -434   -850  -2862
ATOM   3070  NZ  LYS A 401      58.948  31.121  -5.158  1.00135.89           N1+
ANISOU 3070  NZ  LYS A 401    14735  15797  21099   -421  -1003  -2527
ATOM   3071  N   SER A 402      58.117  24.784  -5.148  1.00144.74           N  
ANISOU 3071  N   SER A 402    14726  15928  24342    248  -1255  -3158
ATOM   3072  CA  SER A 402      58.643  23.430  -5.357  1.00143.50           C  
ANISOU 3072  CA  SER A 402    14151  15533  24841    376  -1294  -3414
ATOM   3073  C   SER A 402      59.760  23.421  -6.406  1.00145.32           C  
ANISOU 3073  C   SER A 402    14055  15897  25262    345  -1025  -3841
ATOM   3074  O   SER A 402      59.646  22.821  -7.477  1.00145.81           O  
ANISOU 3074  O   SER A 402    13954  16007  25439    374   -797  -4249
ATOM   3075  CB  SER A 402      57.524  22.449  -5.732  1.00141.56           C  
ANISOU 3075  CB  SER A 402    13926  15166  24693    477  -1292  -3534
ATOM   3076  OG  SER A 402      56.993  22.725  -7.018  1.00143.00           O  
ANISOU 3076  OG  SER A 402    14218  15597  24518    410   -985  -3838
ATOM   3077  N   ALA A 403      60.851  24.104  -6.075  1.00145.96           N  
ANISOU 3077  N   ALA A 403    14045  16048  25366    269  -1049  -3744
ATOM   3078  CA  ALA A 403      62.010  24.169  -6.958  1.00146.72           C  
ANISOU 3078  CA  ALA A 403    13809  16288  25649    224   -799  -4113
ATOM   3079  C   ALA A 403      62.971  23.014  -6.688  1.00144.83           C  
ANISOU 3079  C   ALA A 403    13071  15735  26221    368   -910  -4266
ATOM   3080  O   ALA A 403      64.189  23.171  -6.783  1.00143.59           O  
ANISOU 3080  O   ALA A 403    12615  15607  26337    340   -848  -4373
ATOM   3081  CB  ALA A 403      62.726  25.502  -6.797  1.00148.07           C  
ANISOU 3081  CB  ALA A 403    14110  16698  25451     60   -770  -3930
ATOM   3082  N   GLY A 405      60.570  20.488 -10.192  1.00175.12           N  
ANISOU 3082  N   GLY A 405    16801  19655  30081    505   -176  -5621
ATOM   3083  CA  GLY A 405      59.180  20.587  -9.788  1.00170.86           C  
ANISOU 3083  CA  GLY A 405    16663  19083  29174    505   -355  -5288
ATOM   3084  C   GLY A 405      58.205  20.390 -10.932  1.00171.92           C  
ANISOU 3084  C   GLY A 405    16967  19387  28968    428   -126  -5574
ATOM   3085  O   GLY A 405      58.507  19.701 -11.906  1.00172.10           O  
ANISOU 3085  O   GLY A 405    16747  19426  29219    429    111  -6068
ATOM   3086  N   MET A 406      57.028  20.999 -10.814  1.00170.10           N  
ANISOU 3086  N   MET A 406    17152  19279  28199    351   -195  -5268
ATOM   3087  CA  MET A 406      56.005  20.899 -11.842  1.00170.66           C  
ANISOU 3087  CA  MET A 406    17422  19512  27910    249    -23  -5458
ATOM   3088  C   MET A 406      56.157  22.037 -12.849  1.00172.15           C  
ANISOU 3088  C   MET A 406    17770  20130  27509     -2    266  -5593
ATOM   3089  O   MET A 406      57.166  22.747 -12.880  1.00172.04           O  
ANISOU 3089  O   MET A 406    17651  20283  27432    -84    369  -5629
ATOM   3090  CB  MET A 406      54.610  20.896 -11.223  1.00169.48           C  
ANISOU 3090  CB  MET A 406    17602  19254  27540    295   -257  -5050
ATOM   3091  CG  MET A 406      54.264  19.642 -10.450  1.00167.33           C  
ANISOU 3091  CG  MET A 406    17186  18587  27804    499   -532  -4949
ATOM   3092  SD  MET A 406      52.591  19.737  -9.794  1.00167.89           S  
ANISOU 3092  SD  MET A 406    17647  18597  27547    519   -766  -4471
ATOM   3093  CE  MET A 406      51.638  19.617 -11.308  1.00167.51           C  
ANISOU 3093  CE  MET A 406    17754  18753  27138    379   -516  -4781
ATOM   3094  N   THR A 407      55.140  22.215 -13.688  1.00164.01           N  
ANISOU 3094  N   THR A 407    16991  19281  26045   -148    377  -5646
ATOM   3095  CA  THR A 407      55.156  23.210 -14.750  1.00166.80           C  
ANISOU 3095  CA  THR A 407    17503  20042  25831   -429    624  -5765
ATOM   3096  C   THR A 407      53.801  23.898 -14.796  1.00167.21           C  
ANISOU 3096  C   THR A 407    17965  20193  25375   -535    520  -5411
ATOM   3097  O   THR A 407      52.767  23.226 -14.752  1.00167.38           O  
ANISOU 3097  O   THR A 407    18091  20049  25457   -459    410  -5343
ATOM   3098  CB  THR A 407      55.463  22.557 -16.104  1.00168.70           C  
ANISOU 3098  CB  THR A 407    17550  20441  26107   -567    936  -6342
ATOM   3099  OG1 THR A 407      56.723  21.878 -16.035  1.00169.57           O  
ANISOU 3099  OG1 THR A 407    17239  20429  26761   -442   1044  -6693
ATOM   3100  CG2 THR A 407      55.518  23.600 -17.207  1.00171.61           C  
ANISOU 3100  CG2 THR A 407    18080  21264  25861   -910   1176  -6443
ATOM   3101  N   GLU A 408      53.802  25.228 -14.874  1.00159.55           N  
ANISOU 3101  N   GLU A 408    17212  19475  23936   -710    540  -5176
ATOM   3102  CA  GLU A 408      52.553  25.948 -15.069  1.00160.30           C  
ANISOU 3102  CA  GLU A 408    17665  19674  23569   -835    464  -4872
ATOM   3103  C   GLU A 408      52.081  25.786 -16.513  1.00161.55           C  
ANISOU 3103  C   GLU A 408    17878  20072  23432  -1090    663  -5159
ATOM   3104  O   GLU A 408      52.704  25.097 -17.326  1.00162.81           O  
ANISOU 3104  O   GLU A 408    17812  20319  23730  -1166    875  -5616
ATOM   3105  CB  GLU A 408      52.700  27.418 -14.681  1.00161.24           C  
ANISOU 3105  CB  GLU A 408    17987  19949  23328   -938    400  -4532
ATOM   3106  CG  GLU A 408      52.802  27.640 -13.179  1.00160.94           C  
ANISOU 3106  CG  GLU A 408    17996  19664  23491   -712    168  -4176
ATOM   3107  CD  GLU A 408      52.827  29.107 -12.801  1.00161.98           C  
ANISOU 3107  CD  GLU A 408    18361  19926  23257   -816     99  -3851
ATOM   3108  OE1 GLU A 408      52.897  29.958 -13.713  1.00162.66           O  
ANISOU 3108  OE1 GLU A 408    18540  20293  22972  -1063    220  -3898
ATOM   3109  OE2 GLU A 408      52.766  29.410 -11.590  1.00161.57           O1-
ANISOU 3109  OE2 GLU A 408    18407  19694  23287   -668    -84  -3546
ATOM   3110  N   ASN A 409      50.947  26.418 -16.824  1.00159.81           N  
ANISOU 3110  N   ASN A 409    17958  19950  22811  -1236    589  -4888
ATOM   3111  CA  ASN A 409      50.087  26.108 -17.967  1.00160.45           C  
ANISOU 3111  CA  ASN A 409    18155  20167  22643  -1453    674  -5031
ATOM   3112  C   ASN A 409      49.471  24.722 -17.787  1.00159.65           C  
ANISOU 3112  C   ASN A 409    17975  19779  22907  -1255    600  -5153
ATOM   3113  O   ASN A 409      48.688  24.277 -18.633  1.00160.57           O  
ANISOU 3113  O   ASN A 409    18184  19949  22875  -1404    640  -5268
ATOM   3114  CB  ASN A 409      50.829  26.193 -19.311  1.00161.35           C  
ANISOU 3114  CB  ASN A 409    18157  20630  22517  -1773    958  -5461
ATOM   3115  CG  ASN A 409      49.891  26.284 -20.504  1.00161.33           C  
ANISOU 3115  CG  ASN A 409    18358  20842  22100  -2098   1011  -5496
ATOM   3116  OD1 ASN A 409      48.671  26.323 -20.355  1.00161.13           O  
ANISOU 3116  OD1 ASN A 409    18548  20695  21978  -2078    829  -5182
ATOM   3117  ND2 ASN A 409      50.466  26.316 -21.702  1.00162.55           N  
ANISOU 3117  ND2 ASN A 409    18434  21325  22003  -2419   1262  -5877
ATOM   3118  N   GLU A 410      49.803  24.035 -16.696  1.00150.53           N  
ANISOU 3118  N   GLU A 410    16654  18314  22226   -942    469  -5107
ATOM   3119  CA  GLU A 410      49.279  22.739 -16.303  1.00149.18           C  
ANISOU 3119  CA  GLU A 410    16392  17827  22464   -726    339  -5155
ATOM   3120  C   GLU A 410      48.603  22.770 -14.945  1.00147.12           C  
ANISOU 3120  C   GLU A 410    16243  17305  22350   -492     56  -4681
ATOM   3121  O   GLU A 410      47.620  22.053 -14.739  1.00146.85           O  
ANISOU 3121  O   GLU A 410    16274  17083  22437   -398    -89  -4555
ATOM   3122  CB  GLU A 410      50.422  21.707 -16.267  1.00150.05           C  
ANISOU 3122  CB  GLU A 410    16133  17782  23096   -582    433  -5581
ATOM   3123  CG  GLU A 410      50.023  20.294 -15.890  1.00149.26           C  
ANISOU 3123  CG  GLU A 410    15894  17326  23492   -363    281  -5666
ATOM   3124  CD  GLU A 410      51.224  19.369 -15.815  1.00148.50           C  
ANISOU 3124  CD  GLU A 410    15404  17050  23969   -214    358  -6073
ATOM   3125  OE1 GLU A 410      52.360  19.852 -16.019  1.00148.66           O  
ANISOU 3125  OE1 GLU A 410    15259  17236  23991   -276    539  -6273
ATOM   3126  OE2 GLU A 410      51.034  18.163 -15.550  1.00147.06           O1-
ANISOU 3126  OE2 GLU A 410    15063  16551  24260    -38    227  -6183
ATOM   3127  N   VAL A 411      49.100  23.596 -14.019  1.00129.81           N  
ANISOU 3127  N   VAL A 411    14082  15110  20130   -417    -23  -4417
ATOM   3128  CA  VAL A 411      48.495  23.709 -12.696  1.00127.43           C  
ANISOU 3128  CA  VAL A 411    13901  14597  19917   -229   -268  -3979
ATOM   3129  C   VAL A 411      47.053  24.185 -12.810  1.00126.65           C  
ANISOU 3129  C   VAL A 411    14096  14547  19479   -297   -337  -3669
ATOM   3130  O   VAL A 411      46.172  23.729 -12.070  1.00125.18           O  
ANISOU 3130  O   VAL A 411    13978  14164  19421   -153   -514  -3411
ATOM   3131  CB  VAL A 411      49.335  24.646 -11.807  1.00126.64           C  
ANISOU 3131  CB  VAL A 411    13811  14529  19775   -192   -312  -3785
ATOM   3132  CG1 VAL A 411      48.675  24.835 -10.449  1.00124.60           C  
ANISOU 3132  CG1 VAL A 411    13709  14088  19545    -39   -541  -3348
ATOM   3133  CG2 VAL A 411      50.745  24.103 -11.649  1.00127.45           C  
ANISOU 3133  CG2 VAL A 411    13593  14555  20275   -117   -270  -4060
ATOM   3134  N   GLU A 412      46.784  25.097 -13.747  1.00122.79           N  
ANISOU 3134  N   GLU A 412    13768  14319  18567   -531   -209  -3677
ATOM   3135  CA  GLU A 412      45.417  25.565 -13.934  1.00123.08           C  
ANISOU 3135  CA  GLU A 412    14055  14388  18321   -609   -283  -3378
ATOM   3136  C   GLU A 412      44.535  24.466 -14.513  1.00123.40           C  
ANISOU 3136  C   GLU A 412    14082  14333  18470   -618   -317  -3479
ATOM   3137  O   GLU A 412      43.332  24.423 -14.228  1.00123.87           O  
ANISOU 3137  O   GLU A 412    14287  14295  18484   -571   -449  -3180
ATOM   3138  CB  GLU A 412      45.405  26.806 -14.829  1.00124.01           C  
ANISOU 3138  CB  GLU A 412    14328  14795  17995   -885   -174  -3345
ATOM   3139  CG  GLU A 412      44.118  27.620 -14.770  1.00124.40           C  
ANISOU 3139  CG  GLU A 412    14626  14850  17788   -944   -282  -2951
ATOM   3140  CD  GLU A 412      43.045  27.105 -15.705  1.00125.47           C  
ANISOU 3140  CD  GLU A 412    14835  15011  17826  -1088   -297  -2958
ATOM   3141  OE1 GLU A 412      43.396  26.505 -16.743  1.00126.15           O  
ANISOU 3141  OE1 GLU A 412    14834  15221  17876  -1259   -178  -3301
ATOM   3142  OE2 GLU A 412      41.849  27.306 -15.404  1.00125.57           O1-
ANISOU 3142  OE2 GLU A 412    14991  14923  17798  -1040   -424  -2626
ATOM   3143  N   ASP A 413      45.108  23.566 -15.316  1.00134.19           N  
ANISOU 3143  N   ASP A 413    15270  15722  19994   -681   -195  -3905
ATOM   3144  CA  ASP A 413      44.361  22.394 -15.762  1.00134.40           C  
ANISOU 3144  CA  ASP A 413    15270  15613  20184   -668   -247  -4029
ATOM   3145  C   ASP A 413      44.028  21.485 -14.586  1.00132.66           C  
ANISOU 3145  C   ASP A 413    14960  15062  20381   -378   -464  -3844
ATOM   3146  O   ASP A 413      42.884  21.036 -14.437  1.00132.61           O  
ANISOU 3146  O   ASP A 413    15055  14931  20398   -335   -610  -3624
ATOM   3147  CB  ASP A 413      45.157  21.629 -16.822  1.00135.71           C  
ANISOU 3147  CB  ASP A 413    15247  15859  20456   -789    -49  -4578
ATOM   3148  CG  ASP A 413      45.236  22.367 -18.145  1.00137.24           C  
ANISOU 3148  CG  ASP A 413    15556  16407  20183  -1145    154  -4754
ATOM   3149  OD1 ASP A 413      44.295  23.124 -18.464  1.00138.10           O  
ANISOU 3149  OD1 ASP A 413    15906  16641  19927  -1315     89  -4449
ATOM   3150  OD2 ASP A 413      46.239  22.184 -18.868  1.00137.93           O1-
ANISOU 3150  OD2 ASP A 413    15481  16648  20277  -1268    374  -5194
ATOM   3151  N   ARG A 414      45.021  21.205 -13.736  1.00131.84           N  
ANISOU 3151  N   ARG A 414    14661  14819  20613   -197   -504  -3909
ATOM   3152  CA  ARG A 414      44.794  20.331 -12.589  1.00129.87           C  
ANISOU 3152  CA  ARG A 414    14312  14263  20767     42   -738  -3717
ATOM   3153  C   ARG A 414      43.747  20.918 -11.651  1.00128.51           C  
ANISOU 3153  C   ARG A 414    14359  14059  20410    106   -899  -3209
ATOM   3154  O   ARG A 414      42.940  20.183 -11.069  1.00127.12           O  
ANISOU 3154  O   ARG A 414    14188  13692  20420    220  -1087  -2999
ATOM   3155  CB  ARG A 414      46.111  20.085 -11.849  1.00128.87           C  
ANISOU 3155  CB  ARG A 414    13941  14013  21012    182   -769  -3836
ATOM   3156  CG  ARG A 414      47.206  19.459 -12.709  1.00129.89           C  
ANISOU 3156  CG  ARG A 414    13802  14151  21398    146   -591  -4364
ATOM   3157  CD  ARG A 414      46.866  18.029 -13.105  1.00130.03           C  
ANISOU 3157  CD  ARG A 414    13671  13942  21792    216   -658  -4611
ATOM   3158  NE  ARG A 414      47.883  17.438 -13.972  1.00130.86           N  
ANISOU 3158  NE  ARG A 414    13513  14054  22153    181   -452  -5166
ATOM   3159  CZ  ARG A 414      48.939  16.758 -13.534  1.00129.50           C  
ANISOU 3159  CZ  ARG A 414    13018  13667  22518    340   -493  -5370
ATOM   3160  NH1 ARG A 414      49.124  16.579 -12.233  1.00126.88           N  
ANISOU 3160  NH1 ARG A 414    12602  13102  22503    520   -759  -5037
ATOM   3161  NH2 ARG A 414      49.812  16.256 -14.398  1.00130.52           N1+
ANISOU 3161  NH2 ARG A 414    12899  13815  22877    305   -267  -5909
ATOM   3162  N   LEU A 415      43.742  22.245 -11.494  1.00112.38           N  
ANISOU 3162  N   LEU A 415    12489  12199  18010     28   -826  -3013
ATOM   3163  CA  LEU A 415      42.695  22.890 -10.708  1.00109.93           C  
ANISOU 3163  CA  LEU A 415    12387  11871  17510     76   -935  -2574
ATOM   3164  C   LEU A 415      41.343  22.778 -11.404  1.00109.47           C  
ANISOU 3164  C   LEU A 415    12470  11845  17279    -15   -952  -2452
ATOM   3165  O   LEU A 415      40.319  22.523 -10.754  1.00108.33           O  
ANISOU 3165  O   LEU A 415    12396  11580  17184     82  -1091  -2149
ATOM   3166  CB  LEU A 415      43.058  24.353 -10.456  1.00108.56           C  
ANISOU 3166  CB  LEU A 415    12355  11866  17026      9   -848  -2437
ATOM   3167  CG  LEU A 415      44.293  24.611  -9.588  1.00108.73           C  
ANISOU 3167  CG  LEU A 415    12275  11853  17186     91   -864  -2468
ATOM   3168  CD1 LEU A 415      44.650  26.085  -9.586  1.00107.68           C  
ANISOU 3168  CD1 LEU A 415    12294  11902  16716    -13   -768  -2376
ATOM   3169  CD2 LEU A 415      44.071  24.116  -8.169  1.00108.03           C  
ANISOU 3169  CD2 LEU A 415    12164  11554  17328    268  -1060  -2205
ATOM   3170  N   THR A 416      41.324  22.961 -12.729  1.00114.84           N  
ANISOU 3170  N   THR A 416    13189  12695  17749   -222   -815  -2675
ATOM   3171  CA  THR A 416      40.097  22.768 -13.495  1.00116.61           C  
ANISOU 3171  CA  THR A 416    13536  12945  17825   -344   -851  -2570
ATOM   3172  C   THR A 416      39.513  21.381 -13.263  1.00115.50           C  
ANISOU 3172  C   THR A 416    13303  12578  18003   -220  -1003  -2569
ATOM   3173  O   THR A 416      38.287  21.219 -13.220  1.00115.37           O  
ANISOU 3173  O   THR A 416    13391  12502  17942   -221  -1117  -2295
ATOM   3174  CB  THR A 416      40.367  23.001 -14.984  1.00118.99           C  
ANISOU 3174  CB  THR A 416    13869  13471  17871   -627   -689  -2867
ATOM   3175  OG1 THR A 416      40.839  24.339 -15.180  1.00119.79           O  
ANISOU 3175  OG1 THR A 416    14061  13784  17668   -762   -581  -2815
ATOM   3176  CG2 THR A 416      39.102  22.792 -15.808  1.00120.43           C  
ANISOU 3176  CG2 THR A 416    14187  13678  17892   -792   -751  -2740
ATOM   3177  N   SER A 417      40.370  20.371 -13.095  1.00110.20           N  
ANISOU 3177  N   SER A 417    12423  11765  17684   -112  -1023  -2857
ATOM   3178  CA  SER A 417      39.882  19.066 -12.663  1.00108.68           C  
ANISOU 3178  CA  SER A 417    12127  11317  17852     29  -1215  -2812
ATOM   3179  C   SER A 417      39.400  19.116 -11.218  1.00106.16           C  
ANISOU 3179  C   SER A 417    11830  10860  17646    211  -1403  -2387
ATOM   3180  O   SER A 417      38.344  18.561 -10.890  1.00105.40           O  
ANISOU 3180  O   SER A 417    11773  10645  17627    262  -1565  -2133
ATOM   3181  CB  SER A 417      40.977  18.011 -12.829  1.00109.17           C  
ANISOU 3181  CB  SER A 417    11932  11232  18316    102  -1201  -3232
ATOM   3182  OG  SER A 417      41.323  17.833 -14.192  1.00111.91           O  
ANISOU 3182  OG  SER A 417    12254  11708  18557    -79  -1010  -3661
ATOM   3183  N   PHE A 418      40.157  19.790 -10.345  1.00 97.13           N  
ANISOU 3183  N   PHE A 418    10667   9745  16493    289  -1381  -2301
ATOM   3184  CA  PHE A 418      39.818  19.867  -8.927  1.00 95.71           C  
ANISOU 3184  CA  PHE A 418    10514   9461  16389    427  -1541  -1928
ATOM   3185  C   PHE A 418      38.431  20.442  -8.679  1.00 93.86           C  
ANISOU 3185  C   PHE A 418    10480   9290  15893    408  -1564  -1552
ATOM   3186  O   PHE A 418      37.832  20.149  -7.636  1.00 93.19           O  
ANISOU 3186  O   PHE A 418    10402   9104  15901    507  -1713  -1250
ATOM   3187  CB  PHE A 418      40.861  20.705  -8.190  1.00 95.15           C  
ANISOU 3187  CB  PHE A 418    10436   9454  16263    458  -1483  -1916
ATOM   3188  CG  PHE A 418      40.539  20.940  -6.746  1.00 93.87           C  
ANISOU 3188  CG  PHE A 418    10339   9227  16099    553  -1619  -1546
ATOM   3189  CD1 PHE A 418      40.722  19.943  -5.808  1.00 94.73           C  
ANISOU 3189  CD1 PHE A 418    10302   9140  16552    650  -1837  -1439
ATOM   3190  CD2 PHE A 418      40.044  22.164  -6.328  1.00 92.08           C  
ANISOU 3190  CD2 PHE A 418    10318   9137  15531    526  -1531  -1308
ATOM   3191  CE1 PHE A 418      40.422  20.162  -4.479  1.00 93.85           C  
ANISOU 3191  CE1 PHE A 418    10262   9001  16394    691  -1957  -1097
ATOM   3192  CE2 PHE A 418      39.741  22.389  -5.003  1.00 91.24           C  
ANISOU 3192  CE2 PHE A 418    10281   8991  15396    591  -1626  -1003
ATOM   3193  CZ  PHE A 418      39.931  21.386  -4.076  1.00 92.13           C  
ANISOU 3193  CZ  PHE A 418    10260   8941  15804    660  -1834   -896
ATOM   3194  N   ILE A 419      37.911  21.247  -9.611  1.00100.53           N  
ANISOU 3194  N   ILE A 419    11472  10301  16425    271  -1427  -1555
ATOM   3195  CA  ILE A 419      36.601  21.878  -9.434  1.00 99.86           C  
ANISOU 3195  CA  ILE A 419    11551  10263  16129    254  -1442  -1200
ATOM   3196  C   ILE A 419      35.523  20.853  -9.102  1.00 98.86           C  
ANISOU 3196  C   ILE A 419    11388   9987  16189    324  -1619   -984
ATOM   3197  O   ILE A 419      34.595  21.140  -8.336  1.00 97.61           O  
ANISOU 3197  O   ILE A 419    11299   9815  15974    388  -1670   -642
ATOM   3198  CB  ILE A 419      36.232  22.694 -10.693  1.00102.86           C  
ANISOU 3198  CB  ILE A 419    12057  10814  16213     59  -1314  -1254
ATOM   3199  CG1 ILE A 419      37.248  23.812 -10.925  1.00105.27           C  
ANISOU 3199  CG1 ILE A 419    12405  11279  16315    -23  -1158  -1412
ATOM   3200  CG2 ILE A 419      34.837  23.288 -10.568  1.00103.05           C  
ANISOU 3200  CG2 ILE A 419    12214  10850  16090     46  -1347   -879
ATOM   3201  CD1 ILE A 419      37.102  24.496 -12.268  1.00109.22           C  
ANISOU 3201  CD1 ILE A 419    13001  11960  16538   -264  -1054  -1507
ATOM   3202  N   THR A 420      35.629  19.643  -9.654  1.00 93.52           N  
ANISOU 3202  N   THR A 420    10593   9195  15744    310  -1713  -1185
ATOM   3203  CA  THR A 420      34.600  18.632  -9.430  1.00 93.84           C  
ANISOU 3203  CA  THR A 420    10600   9089  15967    356  -1906   -978
ATOM   3204  C   THR A 420      34.681  18.065  -8.015  1.00 93.69           C  
ANISOU 3204  C   THR A 420    10481   8929  16189    511  -2078   -767
ATOM   3205  O   THR A 420      33.697  18.086  -7.262  1.00 92.84           O  
ANISOU 3205  O   THR A 420    10420   8808  16045    556  -2167   -407
ATOM   3206  CB  THR A 420      34.738  17.521 -10.472  1.00 95.85           C  
ANISOU 3206  CB  THR A 420    10767   9247  16407    283  -1961  -1286
ATOM   3207  OG1 THR A 420      34.606  18.080 -11.784  1.00 96.20           O  
ANISOU 3207  OG1 THR A 420    10925   9455  16173     88  -1804  -1459
ATOM   3208  CG2 THR A 420      33.666  16.474 -10.276  1.00 96.29           C  
ANISOU 3208  CG2 THR A 420    10792   9140  16652    317  -2184  -1060
ATOM   3209  N   VAL A 421      35.853  17.547  -7.637  1.00 94.77           N  
ANISOU 3209  N   VAL A 421    10466   8963  16581    576  -2133   -979
ATOM   3210  CA  VAL A 421      36.035  17.016  -6.288  1.00 94.94           C  
ANISOU 3210  CA  VAL A 421    10387   8852  16833    680  -2328   -764
ATOM   3211  C   VAL A 421      35.662  18.063  -5.250  1.00 93.21           C  
ANISOU 3211  C   VAL A 421    10308   8766  16343    698  -2263   -443
ATOM   3212  O   VAL A 421      35.113  17.735  -4.190  1.00 93.08           O  
ANISOU 3212  O   VAL A 421    10281   8703  16382    736  -2411   -133
ATOM   3213  CB  VAL A 421      37.482  16.510  -6.102  1.00 96.49           C  
ANISOU 3213  CB  VAL A 421    10393   8924  17344    729  -2383  -1043
ATOM   3214  CG1 VAL A 421      37.703  16.021  -4.680  1.00 96.84           C  
ANISOU 3214  CG1 VAL A 421    10339   8839  17616    795  -2617   -780
ATOM   3215  CG2 VAL A 421      37.788  15.405  -7.095  1.00 98.63           C  
ANISOU 3215  CG2 VAL A 421    10507   9040  17926    724  -2436  -1390
ATOM   3216  N   PHE A 422      35.926  19.339  -5.540  1.00 92.09           N  
ANISOU 3216  N   PHE A 422    10298   8795  15898    657  -2041   -514
ATOM   3217  CA  PHE A 422      35.395  20.395  -4.685  1.00 90.66           C  
ANISOU 3217  CA  PHE A 422    10265   8729  15450    672  -1954   -234
ATOM   3218  C   PHE A 422      33.873  20.422  -4.740  1.00 90.05           C  
ANISOU 3218  C   PHE A 422    10266   8679  15270    667  -1963     49
ATOM   3219  O   PHE A 422      33.208  20.604  -3.713  1.00 89.62           O  
ANISOU 3219  O   PHE A 422    10254   8647  15151    708  -1987    338
ATOM   3220  CB  PHE A 422      35.971  21.752  -5.094  1.00 89.80           C  
ANISOU 3220  CB  PHE A 422    10277   8773  15072    622  -1736   -379
ATOM   3221  N   LYS A 423      33.306  20.230  -5.933  1.00 90.24           N  
ANISOU 3221  N   LYS A 423    10305   8707  15276    602  -1942    -29
ATOM   3222  CA  LYS A 423      31.858  20.290  -6.095  1.00 89.81           C  
ANISOU 3222  CA  LYS A 423    10312   8671  15141    584  -1959    252
ATOM   3223  C   LYS A 423      31.154  19.299  -5.181  1.00 90.28           C  
ANISOU 3223  C   LYS A 423    10286   8630  15386    648  -2153    523
ATOM   3224  O   LYS A 423      30.104  19.612  -4.608  1.00 89.80           O  
ANISOU 3224  O   LYS A 423    10267   8618  15233    672  -2135    832
ATOM   3225  CB  LYS A 423      31.493  20.031  -7.556  1.00 90.36           C  
ANISOU 3225  CB  LYS A 423    10399   8742  15193    468  -1957    113
ATOM   3226  CG  LYS A 423      30.015  19.975  -7.860  1.00 90.20           C  
ANISOU 3226  CG  LYS A 423    10422   8719  15130    427  -2010    409
ATOM   3227  CD  LYS A 423      29.808  19.736  -9.347  1.00 91.00           C  
ANISOU 3227  CD  LYS A 423    10559   8831  15186    267  -2020    247
ATOM   3228  CE  LYS A 423      30.215  18.316  -9.727  1.00 92.51           C  
ANISOU 3228  CE  LYS A 423    10644   8884  15621    255  -2175     20
ATOM   3229  NZ  LYS A 423      29.949  18.006 -11.159  1.00 93.64           N1+
ANISOU 3229  NZ  LYS A 423    10838   9042  15699     71  -2183   -151
ATOM   3230  N   TYR A 424      31.723  18.104  -5.013  1.00 91.45           N  
ANISOU 3230  N   TYR A 424    10298   8636  15814    670  -2345    418
ATOM   3231  CA  TYR A 424      31.029  17.078  -4.240  1.00 92.15           C  
ANISOU 3231  CA  TYR A 424    10296   8622  16094    699  -2573    694
ATOM   3232  C   TYR A 424      31.175  17.227  -2.729  1.00 92.06           C  
ANISOU 3232  C   TYR A 424    10273   8649  16058    735  -2620    923
ATOM   3233  O   TYR A 424      30.489  16.505  -1.998  1.00 92.68           O  
ANISOU 3233  O   TYR A 424    10289   8686  16240    730  -2797   1205
ATOM   3234  CB  TYR A 424      31.502  15.676  -4.638  1.00 93.79           C  
ANISOU 3234  CB  TYR A 424    10349   8628  16658    699  -2802    516
ATOM   3235  CG  TYR A 424      31.043  15.228  -6.004  1.00 94.37           C  
ANISOU 3235  CG  TYR A 424    10436   8650  16771    635  -2810    354
ATOM   3236  CD1 TYR A 424      29.726  14.856  -6.222  1.00 94.38           C  
ANISOU 3236  CD1 TYR A 424    10468   8637  16755    597  -2909    622
ATOM   3237  CD2 TYR A 424      31.932  15.138  -7.063  1.00 95.19           C  
ANISOU 3237  CD2 TYR A 424    10517   8724  16926    595  -2722    -66
ATOM   3238  CE1 TYR A 424      29.300  14.440  -7.464  1.00 95.10           C  
ANISOU 3238  CE1 TYR A 424    10588   8681  16865    508  -2935    488
ATOM   3239  CE2 TYR A 424      31.514  14.717  -8.307  1.00 96.04           C  
ANISOU 3239  CE2 TYR A 424    10655   8801  17035    499  -2725   -228
ATOM   3240  CZ  TYR A 424      30.199  14.370  -8.503  1.00 95.97           C  
ANISOU 3240  CZ  TYR A 424    10696   8771  16996    451  -2841     55
ATOM   3241  OH  TYR A 424      29.780  13.951  -9.743  1.00 96.98           O  
ANISOU 3241  OH  TYR A 424    10872   8869  17108    327  -2860    -95
ATOM   3242  N   ILE A 425      32.036  18.124  -2.238  1.00 91.50           N  
ANISOU 3242  N   ILE A 425    10266   8663  15838    746  -2478    821
ATOM   3243  CA  ILE A 425      32.285  18.187  -0.801  1.00 91.79           C  
ANISOU 3243  CA  ILE A 425    10300   8734  15843    741  -2543   1016
ATOM   3244  C   ILE A 425      31.001  18.534  -0.058  1.00 91.48           C  
ANISOU 3244  C   ILE A 425    10333   8813  15611    732  -2481   1357
ATOM   3245  O   ILE A 425      30.239  19.421  -0.464  1.00 90.57           O  
ANISOU 3245  O   ILE A 425    10318   8798  15294    752  -2274   1395
ATOM   3246  CB  ILE A 425      33.386  19.207  -0.474  1.00 91.27           C  
ANISOU 3246  CB  ILE A 425    10316   8746  15616    739  -2387    845
ATOM   3247  CG1 ILE A 425      34.678  18.861  -1.201  1.00 91.83           C  
ANISOU 3247  CG1 ILE A 425    10286   8711  15895    746  -2432    506
ATOM   3248  CG2 ILE A 425      33.657  19.231   1.023  1.00 91.86           C  
ANISOU 3248  CG2 ILE A 425    10404   8859  15638    694  -2474   1052
ATOM   3249  CD1 ILE A 425      35.698  19.967  -1.124  1.00 91.22           C  
ANISOU 3249  CD1 ILE A 425    10295   8726  15639    736  -2258    329
ATOM   3250  N   ASP A 426      30.755  17.819   1.041  1.00102.87           N  
ANISOU 3250  N   ASP A 426    11707  10246  17134    688  -2667   1613
ATOM   3251  CA  ASP A 426      29.588  18.104   1.870  1.00103.71           C  
ANISOU 3251  CA  ASP A 426    11862  10492  17051    662  -2592   1929
ATOM   3252  C   ASP A 426      29.794  19.383   2.674  1.00106.86           C  
ANISOU 3252  C   ASP A 426    12408  11053  17142    652  -2343   1918
ATOM   3253  O   ASP A 426      28.932  20.270   2.684  1.00108.62           O  
ANISOU 3253  O   ASP A 426    12716  11388  17165    687  -2108   1989
ATOM   3254  CB  ASP A 426      29.307  16.916   2.795  1.00103.82           C  
ANISOU 3254  CB  ASP A 426    11756  10466  17227    579  -2883   2212
ATOM   3255  CG  ASP A 426      27.945  16.996   3.466  1.00104.52           C  
ANISOU 3255  CG  ASP A 426    11856  10704  17152    540  -2818   2545
ATOM   3256  OD1 ASP A 426      27.199  17.967   3.208  1.00105.54           O  
ANISOU 3256  OD1 ASP A 426    12074  10947  17081    597  -2541   2548
ATOM   3257  OD2 ASP A 426      27.626  16.083   4.257  1.00105.01           O1-
ANISOU 3257  OD2 ASP A 426    11824  10770  17306    444  -3050   2811
ATOM   3258  N   ASP A 427      30.937  19.494   3.352  1.00 98.10           N  
ANISOU 3258  N   ASP A 427    11322   9940  16013    600  -2397   1827
ATOM   3259  CA  ASP A 427      31.274  20.664   4.163  1.00 99.81           C  
ANISOU 3259  CA  ASP A 427    11692  10294  15936    569  -2187   1796
ATOM   3260  C   ASP A 427      32.243  21.534   3.373  1.00 99.23           C  
ANISOU 3260  C   ASP A 427    11694  10188  15820    625  -2045   1482
ATOM   3261  O   ASP A 427      33.459  21.360   3.446  1.00 98.97           O  
ANISOU 3261  O   ASP A 427    11631  10088  15886    594  -2156   1338
ATOM   3262  CB  ASP A 427      31.874  20.251   5.501  1.00101.39           C  
ANISOU 3262  CB  ASP A 427    11885  10528  16109    431  -2361   1943
ATOM   3263  CG  ASP A 427      30.847  19.674   6.448  1.00102.65           C  
ANISOU 3263  CG  ASP A 427    12006  10790  16205    333  -2445   2274
ATOM   3264  OD1 ASP A 427      29.669  20.084   6.365  1.00103.14           O  
ANISOU 3264  OD1 ASP A 427    12102  10956  16130    381  -2248   2371
ATOM   3265  OD2 ASP A 427      31.217  18.814   7.275  1.00103.29           O1-
ANISOU 3265  OD2 ASP A 427    12011  10850  16385    196  -2717   2451
ATOM   3266  N   LYS A 428      31.694  22.481   2.607  1.00 90.23           N  
ANISOU 3266  N   LYS A 428    10640   9095  14547    697  -1811   1392
ATOM   3267  CA  LYS A 428      32.523  23.519   2.006  1.00 89.31           C  
ANISOU 3267  CA  LYS A 428    10621   8988  14326    722  -1656   1135
ATOM   3268  C   LYS A 428      32.989  24.524   3.047  1.00 89.52           C  
ANISOU 3268  C   LYS A 428    10795   9108  14112    682  -1521   1126
ATOM   3269  O   LYS A 428      33.965  25.244   2.811  1.00 89.06           O  
ANISOU 3269  O   LYS A 428    10809   9048  13982    674  -1456    930
ATOM   3270  CB  LYS A 428      31.751  24.228   0.896  1.00 88.39           C  
ANISOU 3270  CB  LYS A 428    10547   8886  14153    779  -1486   1085
ATOM   3271  CG  LYS A 428      31.366  23.318  -0.251  1.00 88.30           C  
ANISOU 3271  CG  LYS A 428    10419   8789  14344    786  -1613   1064
ATOM   3272  CD  LYS A 428      30.581  24.066  -1.310  1.00 87.63           C  
ANISOU 3272  CD  LYS A 428    10384   8726  14186    799  -1469   1056
ATOM   3273  CE  LYS A 428      30.216  23.158  -2.473  1.00 87.76           C  
ANISOU 3273  CE  LYS A 428    10308   8667  14370    769  -1603   1029
ATOM   3274  NZ  LYS A 428      29.231  22.112  -2.077  1.00 88.42           N1+
ANISOU 3274  NZ  LYS A 428    10295   8705  14594    782  -1753   1281
ATOM   3275  N   ASP A 429      32.303  24.569   4.190  1.00 91.74           N  
ANISOU 3275  N   ASP A 429    11123   9479  14257    640  -1477   1331
ATOM   3276  CA  ASP A 429      32.661  25.444   5.300  1.00 94.09           C  
ANISOU 3276  CA  ASP A 429    11575   9875  14300    572  -1349   1324
ATOM   3277  C   ASP A 429      34.129  25.292   5.693  1.00 94.44           C  
ANISOU 3277  C   ASP A 429    11636   9880  14367    482  -1508   1225
ATOM   3278  O   ASP A 429      34.927  26.234   5.582  1.00 95.08           O  
ANISOU 3278  O   ASP A 429    11829   9967  14330    480  -1404   1050
ATOM   3279  CB  ASP A 429      31.747  25.112   6.481  1.00 95.78           C  
ANISOU 3279  CB  ASP A 429    11793  10202  14395    497  -1332   1570
ATOM   3280  CG  ASP A 429      31.880  26.085   7.626  1.00 98.80           C  
ANISOU 3280  CG  ASP A 429    12356  10711  14473    412  -1147   1549
ATOM   3281  OD1 ASP A 429      32.653  27.059   7.511  1.00 99.46           O  
ANISOU 3281  OD1 ASP A 429    12569  10776  14446    424  -1040   1354
ATOM   3282  OD2 ASP A 429      31.213  25.857   8.655  1.00100.73           O1-
ANISOU 3282  OD2 ASP A 429    12615  11081  14579    316  -1110   1726
ATOM   3283  N   VAL A 430      34.501  24.095   6.154  1.00 92.32           N  
ANISOU 3283  N   VAL A 430    11242   9560  14276    399  -1781   1354
ATOM   3284  CA  VAL A 430      35.843  23.890   6.683  1.00 93.04           C  
ANISOU 3284  CA  VAL A 430    11324   9603  14424    294  -1963   1314
ATOM   3285  C   VAL A 430      36.873  23.965   5.568  1.00 92.12           C  
ANISOU 3285  C   VAL A 430    11132   9371  14497    374  -1988   1054
ATOM   3286  O   VAL A 430      38.035  24.318   5.806  1.00 92.37           O  
ANISOU 3286  O   VAL A 430    11196   9384  14518    317  -2033    954
ATOM   3287  CB  VAL A 430      35.908  22.553   7.442  1.00 94.61           C  
ANISOU 3287  CB  VAL A 430    11380   9752  14816    175  -2283   1552
ATOM   3288  CG1 VAL A 430      37.293  22.326   8.019  1.00 95.65           C  
ANISOU 3288  CG1 VAL A 430    11480   9813  15049     51  -2503   1546
ATOM   3289  CG2 VAL A 430      34.859  22.524   8.538  1.00 95.74           C  
ANISOU 3289  CG2 VAL A 430    11600  10053  14725     64  -2235   1811
ATOM   3290  N   PHE A 431      36.471  23.653   4.335  1.00 91.23           N  
ANISOU 3290  N   PHE A 431    10920   9195  14547    489  -1955    941
ATOM   3291  CA  PHE A 431      37.358  23.883   3.203  1.00 90.52           C  
ANISOU 3291  CA  PHE A 431    10779   9043  14571    543  -1916    664
ATOM   3292  C   PHE A 431      37.688  25.359   3.049  1.00 89.64           C  
ANISOU 3292  C   PHE A 431    10847   9026  14186    545  -1683    528
ATOM   3293  O   PHE A 431      38.843  25.720   2.787  1.00 89.60           O  
ANISOU 3293  O   PHE A 431    10836   9005  14203    520  -1688    355
ATOM   3294  CB  PHE A 431      36.737  23.342   1.923  1.00 89.98           C  
ANISOU 3294  CB  PHE A 431    10604   8918  14665    626  -1903    574
ATOM   3295  CG  PHE A 431      37.501  23.707   0.696  1.00 89.43           C  
ANISOU 3295  CG  PHE A 431    10506   8835  14640    650  -1812    280
ATOM   3296  CD1 PHE A 431      38.775  23.211   0.488  1.00 90.22           C  
ANISOU 3296  CD1 PHE A 431    10468   8850  14960    635  -1928     96
ATOM   3297  CD2 PHE A 431      36.942  24.530  -0.261  1.00 88.41           C  
ANISOU 3297  CD2 PHE A 431    10468   8779  14344    673  -1618    195
ATOM   3298  CE1 PHE A 431      39.486  23.549  -0.644  1.00 89.99           C  
ANISOU 3298  CE1 PHE A 431    10402   8840  14952    638  -1820   -189
ATOM   3299  CE2 PHE A 431      37.645  24.865  -1.398  1.00 88.16           C  
ANISOU 3299  CE2 PHE A 431    10412   8766  14318    653  -1539    -65
ATOM   3300  CZ  PHE A 431      38.920  24.374  -1.590  1.00 88.96           C  
ANISOU 3300  CZ  PHE A 431    10382   8811  14608    635  -1625   -268
ATOM   3301  N   GLN A 432      36.688  26.231   3.201  1.00 89.11           N  
ANISOU 3301  N   GLN A 432    10926   9047  13886    573  -1485    605
ATOM   3302  CA  GLN A 432      36.952  27.666   3.169  1.00 88.56           C  
ANISOU 3302  CA  GLN A 432    11031   9042  13577    570  -1285    493
ATOM   3303  C   GLN A 432      37.886  28.072   4.301  1.00 89.34           C  
ANISOU 3303  C   GLN A 432    11237   9170  13539    471  -1327    504
ATOM   3304  O   GLN A 432      38.965  28.628   4.066  1.00 89.14           O  
ANISOU 3304  O   GLN A 432    11249   9137  13485    438  -1326    355
ATOM   3305  CB  GLN A 432      35.644  28.453   3.252  1.00 88.33           C  
ANISOU 3305  CB  GLN A 432    11108   9067  13384    626  -1079    586
ATOM   3306  CG  GLN A 432      35.846  29.954   3.151  1.00 87.97           C  
ANISOU 3306  CG  GLN A 432    11231   9052  13140    633   -888    467
ATOM   3307  CD  GLN A 432      34.548  30.732   3.228  1.00 88.64           C  
ANISOU 3307  CD  GLN A 432    11390   9156  13134    703   -688    548
ATOM   3308  OE1 GLN A 432      33.473  30.156   3.405  1.00 88.46           O  
ANISOU 3308  OE1 GLN A 432    11292   9144  13176    743   -676    704
ATOM   3309  NE2 GLN A 432      34.642  32.052   3.100  1.00 89.76           N  
ANISOU 3309  NE2 GLN A 432    11665   9291  13149    717   -536    447
ATOM   3310  N   LYS A 433      37.489  27.784   5.546  1.00 90.43           N  
ANISOU 3310  N   LYS A 433    11426   9354  13580    396  -1372    693
ATOM   3311  CA  LYS A 433      38.291  28.217   6.689  1.00 91.45           C  
ANISOU 3311  CA  LYS A 433    11688   9525  13532    261  -1412    724
ATOM   3312  C   LYS A 433      39.721  27.694   6.631  1.00 91.80           C  
ANISOU 3312  C   LYS A 433    11626   9489  13767    192  -1640    669
ATOM   3313  O   LYS A 433      40.638  28.358   7.129  1.00 92.23           O  
ANISOU 3313  O   LYS A 433    11794   9560  13689     99  -1651    624
ATOM   3314  CB  LYS A 433      37.624  27.796   7.997  1.00 92.92           C  
ANISOU 3314  CB  LYS A 433    11925   9795  13585    148  -1452    950
ATOM   3315  CG  LYS A 433      36.397  28.612   8.351  1.00 93.13           C  
ANISOU 3315  CG  LYS A 433    12092   9925  13370    188  -1174    973
ATOM   3316  CD  LYS A 433      36.802  30.047   8.639  1.00 93.23           C  
ANISOU 3316  CD  LYS A 433    12325   9970  13129    167   -978    814
ATOM   3317  CE  LYS A 433      37.626  30.133   9.919  1.00 94.80           C  
ANISOU 3317  CE  LYS A 433    12661  10231  13128    -43  -1079    873
ATOM   3318  NZ  LYS A 433      38.022  31.530  10.266  1.00 95.14           N1+
ANISOU 3318  NZ  LYS A 433    12939  10296  12912    -80   -898    714
ATOM   3319  N   PHE A 434      39.943  26.524   6.031  1.00 91.85           N  
ANISOU 3319  N   PHE A 434    11405   9393  14100    236  -1825    666
ATOM   3320  CA  PHE A 434      41.316  26.043   5.897  1.00 92.46           C  
ANISOU 3320  CA  PHE A 434    11340   9371  14419    192  -2023    585
ATOM   3321  C   PHE A 434      42.050  26.734   4.755  1.00 91.47           C  
ANISOU 3321  C   PHE A 434    11198   9240  14315    264  -1893    317
ATOM   3322  O   PHE A 434      43.203  27.150   4.923  1.00 91.86           O  
ANISOU 3322  O   PHE A 434    11261   9280  14363    198  -1939    245
ATOM   3323  CB  PHE A 434      41.344  24.525   5.714  1.00 93.32           C  
ANISOU 3323  CB  PHE A 434    11194   9347  14917    213  -2274    656
ATOM   3324  CG  PHE A 434      41.166  23.758   6.995  1.00 94.91           C  
ANISOU 3324  CG  PHE A 434    11374   9534  15153     73  -2510    947
ATOM   3325  CD1 PHE A 434      41.318  24.387   8.220  1.00 95.72           C  
ANISOU 3325  CD1 PHE A 434    11668   9743  14959    -91  -2508   1096
ATOM   3326  CD2 PHE A 434      40.865  22.407   6.977  1.00 95.82           C  
ANISOU 3326  CD2 PHE A 434    11283   9533  15591     80  -2748   1074
ATOM   3327  CE1 PHE A 434      41.163  23.687   9.401  1.00 97.46           C  
ANISOU 3327  CE1 PHE A 434    11876   9979  15177   -269  -2735   1380
ATOM   3328  CE2 PHE A 434      40.712  21.702   8.156  1.00 97.49           C  
ANISOU 3328  CE2 PHE A 434    11469   9741  15832    -82  -2995   1372
ATOM   3329  CZ  PHE A 434      40.860  22.344   9.368  1.00 98.34           C  
ANISOU 3329  CZ  PHE A 434    11769   9979  15614   -269  -2988   1532
ATOM   3330  N   TYR A 435      41.405  26.876   3.594  1.00 90.34           N  
ANISOU 3330  N   TYR A 435    11029   9114  14181    373  -1740    186
ATOM   3331  CA  TYR A 435      42.068  27.541   2.478  1.00 89.63           C  
ANISOU 3331  CA  TYR A 435    10927   9050  14078    401  -1618    -56
ATOM   3332  C   TYR A 435      42.387  28.991   2.797  1.00 89.19           C  
ANISOU 3332  C   TYR A 435    11090   9080  13718    349  -1477    -82
ATOM   3333  O   TYR A 435      43.270  29.576   2.159  1.00 88.98           O  
ANISOU 3333  O   TYR A 435    11055   9080  13673    325  -1430   -248
ATOM   3334  CB  TYR A 435      41.207  27.435   1.221  1.00 88.75           C  
ANISOU 3334  CB  TYR A 435    10770   8956  13996    482  -1499   -154
ATOM   3335  CG  TYR A 435      41.849  27.982  -0.033  1.00 88.33           C  
ANISOU 3335  CG  TYR A 435    10685   8953  13924    470  -1389   -398
ATOM   3336  CD1 TYR A 435      42.988  27.397  -0.560  1.00 89.15           C  
ANISOU 3336  CD1 TYR A 435    10602   9017  14253    452  -1464   -590
ATOM   3337  CD2 TYR A 435      41.275  29.028  -0.731  1.00 87.40           C  
ANISOU 3337  CD2 TYR A 435    10701   8920  13586    465  -1216   -432
ATOM   3338  CE1 TYR A 435      43.568  27.875  -1.717  1.00 89.05           C  
ANISOU 3338  CE1 TYR A 435    10552   9084  14197    414  -1345   -821
ATOM   3339  CE2 TYR A 435      41.844  29.508  -1.895  1.00 87.24           C  
ANISOU 3339  CE2 TYR A 435    10652   8970  13526    413  -1133   -633
ATOM   3340  CZ  TYR A 435      42.989  28.927  -2.383  1.00 88.07           C  
ANISOU 3340  CZ  TYR A 435    10583   9068  13811    381  -1187   -832
ATOM   3341  OH  TYR A 435      43.561  29.399  -3.539  1.00 88.19           O  
ANISOU 3341  OH  TYR A 435    10563   9186  13758    303  -1086  -1040
ATOM   3342  N   ALA A 436      41.706  29.570   3.790  1.00 92.49           N  
ANISOU 3342  N   ALA A 436    11698   9543  13902    320  -1409     70
ATOM   3343  CA  ALA A 436      42.043  30.913   4.248  1.00 94.25           C  
ANISOU 3343  CA  ALA A 436    12139   9820  13851    262  -1293     38
ATOM   3344  C   ALA A 436      43.450  30.957   4.833  1.00 95.13           C  
ANISOU 3344  C   ALA A 436    12251   9913  13983    146  -1442     27
ATOM   3345  O   ALA A 436      44.252  31.827   4.479  1.00 95.72           O  
ANISOU 3345  O   ALA A 436    12389  10008  13971    111  -1396    -92
ATOM   3346  CB  ALA A 436      41.017  31.390   5.277  1.00 95.61           C  
ANISOU 3346  CB  ALA A 436    12498  10038  13794    248  -1180    176
ATOM   3347  N   ARG A 437      43.769  30.025   5.735  1.00107.02           N  
ANISOU 3347  N   ARG A 437    13677  11374  15611     67  -1644    175
ATOM   3348  CA  ARG A 437      45.117  29.990   6.297  1.00107.67           C  
ANISOU 3348  CA  ARG A 437    13733  11419  15757    -58  -1823    200
ATOM   3349  C   ARG A 437      46.136  29.477   5.288  1.00105.54           C  
ANISOU 3349  C   ARG A 437    13213  11081  15806     -9  -1906     40
ATOM   3350  O   ARG A 437      47.291  29.925   5.299  1.00106.53           O  
ANISOU 3350  O   ARG A 437    13329  11202  15946    -80  -1958    -20
ATOM   3351  CB  ARG A 437      45.146  29.140   7.567  1.00107.20           C  
ANISOU 3351  CB  ARG A 437    13653  11326  15751   -190  -2047    439
ATOM   3352  CG  ARG A 437      44.438  29.778   8.751  1.00110.09           C  
ANISOU 3352  CG  ARG A 437    14291  11793  15747   -304  -1958    577
ATOM   3353  CD  ARG A 437      44.512  28.883   9.972  1.00109.90           C  
ANISOU 3353  CD  ARG A 437    14238  11762  15757   -486  -2205    833
ATOM   3354  NE  ARG A 437      45.894  28.656  10.385  1.00110.12           N  
ANISOU 3354  NE  ARG A 437    14192  11713  15935   -633  -2462    904
ATOM   3355  CZ  ARG A 437      46.574  29.442  11.214  1.00112.53           C  
ANISOU 3355  CZ  ARG A 437    14699  12063  15994   -815  -2498    955
ATOM   3356  NH1 ARG A 437      46.001  30.520  11.731  1.00115.78           N  
ANISOU 3356  NH1 ARG A 437    15408  12593  15990   -867  -2276    913
ATOM   3357  NH2 ARG A 437      47.829  29.146  11.527  1.00110.99           N1+
ANISOU 3357  NH2 ARG A 437    14401  11782  15987   -950  -2760   1046
ATOM   3358  N   MET A 438      45.734  28.539   4.424  1.00 97.00           N  
ANISOU 3358  N   MET A 438    11925   9949  14983    104  -1915    -40
ATOM   3359  CA  MET A 438      46.592  28.128   3.316  1.00 95.97           C  
ANISOU 3359  CA  MET A 438    11560   9773  15130    157  -1927   -258
ATOM   3360  C   MET A 438      47.071  29.345   2.532  1.00 96.58           C  
ANISOU 3360  C   MET A 438    11736   9957  15002    143  -1742   -437
ATOM   3361  O   MET A 438      48.269  29.508   2.269  1.00 96.82           O  
ANISOU 3361  O   MET A 438    11662   9988  15139     97  -1780   -547
ATOM   3362  CB  MET A 438      45.834  27.173   2.387  1.00 94.41           C  
ANISOU 3362  CB  MET A 438    11196   9531  15145    272  -1899   -352
ATOM   3363  CG  MET A 438      45.317  25.871   3.014  1.00 93.69           C  
ANISOU 3363  CG  MET A 438    10978   9320  15299    289  -2104   -177
ATOM   3364  SD  MET A 438      46.548  24.716   3.645  1.00 95.28           S  
ANISOU 3364  SD  MET A 438    10908   9338  15957    232  -2430   -112
ATOM   3365  CE  MET A 438      46.373  24.958   5.412  1.00 95.97           C  
ANISOU 3365  CE  MET A 438    11195   9453  15815     63  -2598    250
ATOM   3366  N   LEU A 439      46.132  30.225   2.167  1.00 92.92           N  
ANISOU 3366  N   LEU A 439    11464   9583  14259    174  -1553   -449
ATOM   3367  CA  LEU A 439      46.470  31.431   1.416  1.00 92.25           C  
ANISOU 3367  CA  LEU A 439    11483   9595  13973    142  -1403   -584
ATOM   3368  C   LEU A 439      47.213  32.448   2.273  1.00 92.60           C  
ANISOU 3368  C   LEU A 439    11708   9659  13816     40  -1433   -515
ATOM   3369  O   LEU A 439      48.088  33.160   1.766  1.00 92.64           O  
ANISOU 3369  O   LEU A 439    11715   9720  13765    -20  -1402   -624
ATOM   3370  CB  LEU A 439      45.193  32.037   0.830  1.00 91.11           C  
ANISOU 3370  CB  LEU A 439    11472   9504  13640    197  -1233   -580
ATOM   3371  CG  LEU A 439      45.264  33.250  -0.094  1.00 90.48           C  
ANISOU 3371  CG  LEU A 439    11493   9515  13371    154  -1097   -686
ATOM   3372  CD1 LEU A 439      44.165  33.176  -1.133  1.00 89.79           C  
ANISOU 3372  CD1 LEU A 439    11380   9457  13278    201   -995   -714
ATOM   3373  CD2 LEU A 439      45.104  34.510   0.722  1.00 90.35           C  
ANISOU 3373  CD2 LEU A 439    11731   9497  13100    119  -1048   -589
ATOM   3374  N   ALA A 440      46.882  32.534   3.562  1.00 96.71           N  
ANISOU 3374  N   ALA A 440    12387  10146  14211     -3  -1496   -336
ATOM   3375  CA  ALA A 440      47.556  33.478   4.448  1.00 97.29           C  
ANISOU 3375  CA  ALA A 440    12659  10233  14072   -124  -1533   -272
ATOM   3376  C   ALA A 440      49.047  33.178   4.528  1.00 98.31           C  
ANISOU 3376  C   ALA A 440    12636  10331  14385   -214  -1706   -287
ATOM   3377  O   ALA A 440      49.888  34.020   4.189  1.00 98.33           O  
ANISOU 3377  O   ALA A 440    12681  10376  14303   -275  -1683   -367
ATOM   3378  CB  ALA A 440      46.920  33.436   5.838  1.00 97.99           C  
ANISOU 3378  CB  ALA A 440    12930  10309  13995   -185  -1570    -89
ATOM   3379  N   LYS A 441      49.392  31.967   4.971  1.00103.03           N  
ANISOU 3379  N   LYS A 441    13039  10844  15263   -228  -1895   -197
ATOM   3380  CA  LYS A 441      50.795  31.571   4.974  1.00102.62           C  
ANISOU 3380  CA  LYS A 441    12783  10734  15474   -296  -2068   -211
ATOM   3381  C   LYS A 441      51.377  31.587   3.567  1.00101.73           C  
ANISOU 3381  C   LYS A 441    12461  10664  15527   -222  -1956   -459
ATOM   3382  O   LYS A 441      52.576  31.829   3.393  1.00101.99           O  
ANISOU 3382  O   LYS A 441    12387  10704  15662   -288  -2012   -515
ATOM   3383  CB  LYS A 441      50.948  30.183   5.601  1.00102.03           C  
ANISOU 3383  CB  LYS A 441    12497  10529  15741   -312  -2308    -68
ATOM   3384  CG  LYS A 441      50.607  30.123   7.085  1.00103.25           C  
ANISOU 3384  CG  LYS A 441    12840  10664  15724   -455  -2462    206
ATOM   3385  CD  LYS A 441      50.766  28.710   7.638  1.00103.03           C  
ANISOU 3385  CD  LYS A 441    12580  10500  16066   -494  -2741    377
ATOM   3386  CE  LYS A 441      50.374  28.640   9.109  1.00104.18           C  
ANISOU 3386  CE  LYS A 441    12923  10663  15998   -684  -2899    667
ATOM   3387  NZ  LYS A 441      50.504  27.263   9.664  1.00105.86           N1+
ANISOU 3387  NZ  LYS A 441    12905  10740  16578   -753  -3212    876
ATOM   3388  N   ARG A 442      50.543  31.349   2.549  1.00 99.21           N  
ANISOU 3388  N   ARG A 442    12085  10388  15223   -106  -1796   -604
ATOM   3389  CA  ARG A 442      51.038  31.324   1.178  1.00 99.23           C  
ANISOU 3389  CA  ARG A 442    11898  10460  15344    -73  -1675   -854
ATOM   3390  C   ARG A 442      51.365  32.712   0.641  1.00 98.57           C  
ANISOU 3390  C   ARG A 442    11974  10517  14963   -151  -1539   -929
ATOM   3391  O   ARG A 442      52.046  32.814  -0.384  1.00 98.99           O  
ANISOU 3391  O   ARG A 442    11871  10658  15083   -178  -1457  -1118
ATOM   3392  CB  ARG A 442      50.022  30.638   0.261  1.00 98.59           C  
ANISOU 3392  CB  ARG A 442    11729  10388  15344     36  -1564   -973
ATOM   3393  N   LEU A 443      50.900  33.779   1.293  1.00 95.71           N  
ANISOU 3393  N   LEU A 443    11910  10176  14279   -197  -1513   -793
ATOM   3394  CA  LEU A 443      51.210  35.140   0.864  1.00 96.31           C  
ANISOU 3394  CA  LEU A 443    12146  10354  14093   -280  -1423   -838
ATOM   3395  C   LEU A 443      52.165  35.866   1.799  1.00 97.11           C  
ANISOU 3395  C   LEU A 443    12380  10434  14085   -400  -1544   -726
ATOM   3396  O   LEU A 443      53.177  36.408   1.343  1.00 97.17           O  
ANISOU 3396  O   LEU A 443    12329  10511  14080   -488  -1555   -792
ATOM   3397  CB  LEU A 443      49.928  35.975   0.710  1.00 96.81           C  
ANISOU 3397  CB  LEU A 443    12447  10441  13894   -241  -1289   -800
ATOM   3398  CG  LEU A 443      48.992  35.669  -0.457  1.00 96.20           C  
ANISOU 3398  CG  LEU A 443    12285  10416  13851   -169  -1161   -900
ATOM   3399  CD1 LEU A 443      47.788  36.590  -0.397  1.00 96.91           C  
ANISOU 3399  CD1 LEU A 443    12607  10493  13721   -139  -1063   -815
ATOM   3400  CD2 LEU A 443      49.719  35.816  -1.783  1.00 95.78           C  
ANISOU 3400  CD2 LEU A 443    12074  10493  13827   -248  -1100  -1080
ATOM   3401  N   ILE A 444      51.878  35.886   3.103  1.00106.50           N  
ANISOU 3401  N   ILE A 444    13747  11539  15179   -429  -1640   -552
ATOM   3402  CA  ILE A 444      52.648  36.695   4.039  1.00107.33           C  
ANISOU 3402  CA  ILE A 444    14038  11624  15117   -572  -1752   -438
ATOM   3403  C   ILE A 444      54.109  36.260   4.120  1.00106.89           C  
ANISOU 3403  C   ILE A 444    13766  11548  15298   -661  -1925   -416
ATOM   3404  O   ILE A 444      54.925  36.948   4.739  1.00107.65           O  
ANISOU 3404  O   ILE A 444    13988  11637  15277   -800  -2036   -320
ATOM   3405  CB  ILE A 444      51.956  36.664   5.424  1.00108.89           C  
ANISOU 3405  CB  ILE A 444    14466  11755  15151   -611  -1806   -271
ATOM   3406  CG1 ILE A 444      50.497  37.095   5.283  1.00110.65           C  
ANISOU 3406  CG1 ILE A 444    14862  11996  15185   -504  -1609   -311
ATOM   3407  CG2 ILE A 444      52.618  37.612   6.415  1.00109.61           C  
ANISOU 3407  CG2 ILE A 444    14808  11831  15006   -782  -1904   -168
ATOM   3408  CD1 ILE A 444      50.326  38.508   4.761  1.00111.17           C  
ANISOU 3408  CD1 ILE A 444    15116  12098  15026   -510  -1477   -399
ATOM   3409  N   HIS A 445      54.477  35.154   3.471  1.00119.26           N  
ANISOU 3409  N   HIS A 445    14999  13098  17216   -587  -1947   -511
ATOM   3410  CA  HIS A 445      55.865  34.711   3.455  1.00117.43           C  
ANISOU 3410  CA  HIS A 445    14508  12832  17278   -652  -2093   -512
ATOM   3411  C   HIS A 445      56.344  34.413   2.039  1.00116.15           C  
ANISOU 3411  C   HIS A 445    14051  12758  17323   -587  -1955   -763
ATOM   3412  O   HIS A 445      57.264  33.611   1.848  1.00114.51           O  
ANISOU 3412  O   HIS A 445    13525  12498  17484   -578  -2035   -825
ATOM   3413  CB  HIS A 445      56.055  33.495   4.360  1.00116.06           C  
ANISOU 3413  CB  HIS A 445    14174  12503  17420   -656  -2314   -359
ATOM   3414  CG  HIS A 445      55.779  33.780   5.801  1.00117.97           C  
ANISOU 3414  CG  HIS A 445    14697  12689  17439   -784  -2468   -103
ATOM   3415  ND1 HIS A 445      56.637  34.517   6.590  1.00119.17           N  
ANISOU 3415  ND1 HIS A 445    15000  12834  17444   -965  -2613     46
ATOM   3416  CD2 HIS A 445      54.736  33.441   6.594  1.00119.40           C  
ANISOU 3416  CD2 HIS A 445    15040  12835  17493   -781  -2491     24
ATOM   3417  CE1 HIS A 445      56.135  34.614   7.808  1.00120.82           C  
ANISOU 3417  CE1 HIS A 445    15465  13009  17433  -1078  -2713    240
ATOM   3418  NE2 HIS A 445      54.983  33.969   7.837  1.00120.96           N  
ANISOU 3418  NE2 HIS A 445    15487  13018  17456   -969  -2634    228
ATOM   3419  N   GLY A 446      55.735  35.056   1.047  1.00114.42           N  
ANISOU 3419  N   GLY A 446    13926  12673  16877   -559  -1751   -907
ATOM   3420  CA  GLY A 446      56.213  34.951  -0.331  1.00114.18           C  
ANISOU 3420  CA  GLY A 446    13656  12775  16953   -556  -1603  -1150
ATOM   3421  C   GLY A 446      56.366  33.532  -0.828  1.00112.98           C  
ANISOU 3421  C   GLY A 446    13155  12562  17209   -451  -1585  -1318
ATOM   3422  O   GLY A 446      57.364  33.205  -1.485  1.00112.36           O  
ANISOU 3422  O   GLY A 446    12791  12536  17364   -473  -1542  -1492
ATOM   3423  N   LEU A 447      55.395  32.673  -0.527  1.00108.79           N  
ANISOU 3423  N   LEU A 447    12633  11918  16785   -337  -1615  -1279
ATOM   3424  CA  LEU A 447      55.483  31.267  -0.892  1.00108.25           C  
ANISOU 3424  CA  LEU A 447    12244  11748  17139   -232  -1632  -1426
ATOM   3425  C   LEU A 447      54.794  30.943  -2.209  1.00107.84           C  
ANISOU 3425  C   LEU A 447    12116  11799  17059   -174  -1421  -1679
ATOM   3426  O   LEU A 447      55.086  29.898  -2.802  1.00107.70           O  
ANISOU 3426  O   LEU A 447    11804  11730  17387   -107  -1387  -1890
ATOM   3427  CB  LEU A 447      54.885  30.399   0.219  1.00107.80           C  
ANISOU 3427  CB  LEU A 447    12214  11497  17250   -165  -1828  -1216
ATOM   3428  CG  LEU A 447      55.661  30.399   1.536  1.00108.15           C  
ANISOU 3428  CG  LEU A 447    12270  11418  17403   -253  -2081   -964
ATOM   3429  CD1 LEU A 447      54.896  29.650   2.611  1.00108.08           C  
ANISOU 3429  CD1 LEU A 447    12336  11263  17468   -233  -2267   -733
ATOM   3430  CD2 LEU A 447      57.035  29.785   1.329  1.00108.27           C  
ANISOU 3430  CD2 LEU A 447    11916  11352  17868   -262  -2177  -1063
ATOM   3431  N   SER A 448      53.900  31.809  -2.682  1.00103.49           N  
ANISOU 3431  N   SER A 448    11817  11380  16125   -210  -1288  -1664
ATOM   3432  CA  SER A 448      53.138  31.517  -3.885  1.00103.17           C  
ANISOU 3432  CA  SER A 448    11736  11435  16028   -189  -1118  -1858
ATOM   3433  C   SER A 448      54.049  31.493  -5.112  1.00103.82           C  
ANISOU 3433  C   SER A 448    11589  11682  16176   -276   -964  -2155
ATOM   3434  O   SER A 448      55.230  31.850  -5.061  1.00104.45           O  
ANISOU 3434  O   SER A 448    11553  11817  16315   -350   -975  -2196
ATOM   3435  CB  SER A 448      52.020  32.541  -4.074  1.00103.19           C  
ANISOU 3435  CB  SER A 448    12050  11528  15632   -230  -1042  -1734
ATOM   3436  OG  SER A 448      51.283  32.272  -5.255  1.00102.99           O  
ANISOU 3436  OG  SER A 448    11989  11596  15547   -243   -904  -1890
ATOM   3437  N   MET A 449      53.478  31.053  -6.233  1.00107.71           N  
ANISOU 3437  N   MET A 449    12015  12264  16648   -285   -814  -2364
ATOM   3438  CA  MET A 449      54.208  30.958  -7.486  1.00108.67           C  
ANISOU 3438  CA  MET A 449    11925  12572  16791   -396   -632  -2683
ATOM   3439  C   MET A 449      53.708  31.913  -8.556  1.00109.14           C  
ANISOU 3439  C   MET A 449    12160  12878  16430   -574   -487  -2721
ATOM   3440  O   MET A 449      54.477  32.256  -9.459  1.00110.17           O  
ANISOU 3440  O   MET A 449    12173  13223  16464   -732   -350  -2920
ATOM   3441  CB  MET A 449      54.143  29.525  -8.034  1.00108.77           C  
ANISOU 3441  CB  MET A 449    11670  12496  17161   -302   -569  -2960
ATOM   3442  N   SER A 450      52.450  32.346  -8.482  1.00117.20           N  
ANISOU 3442  N   SER A 450    13442  13875  17213   -566   -522  -2527
ATOM   3443  CA  SER A 450      51.889  33.247  -9.486  1.00118.54           C  
ANISOU 3443  CA  SER A 450    13773  14249  17017   -750   -428  -2518
ATOM   3444  C   SER A 450      50.698  33.972  -8.882  1.00118.43           C  
ANISOU 3444  C   SER A 450    14052  14133  16812   -698   -527  -2209
ATOM   3445  O   SER A 450      49.698  33.333  -8.536  1.00118.40           O  
ANISOU 3445  O   SER A 450    14096  13983  16909   -564   -570  -2125
ATOM   3446  CB  SER A 450      51.469  32.475 -10.740  1.00118.86           C  
ANISOU 3446  CB  SER A 450    13696  14402  17064   -830   -288  -2772
ATOM   3447  OG  SER A 450      52.585  31.887 -11.384  1.00120.92           O  
ANISOU 3447  OG  SER A 450    13677  14778  17488   -895   -155  -3105
ATOM   3448  N   MET A 451      50.805  35.297  -8.750  1.00109.61           N  
ANISOU 3448  N   MET A 451    13121  13086  15442   -803   -564  -2046
ATOM   3449  CA  MET A 451      49.660  36.098  -8.327  1.00109.32           C  
ANISOU 3449  CA  MET A 451    13345  12956  15236   -768   -631  -1790
ATOM   3450  C   MET A 451      48.537  36.022  -9.352  1.00109.24           C  
ANISOU 3450  C   MET A 451    13378  13012  15116   -847   -576  -1789
ATOM   3451  O   MET A 451      47.363  35.848  -8.994  1.00108.88           O  
ANISOU 3451  O   MET A 451    13437  12831  15103   -731   -611  -1640
ATOM   3452  CB  MET A 451      50.092  37.549  -8.114  1.00109.70           C  
ANISOU 3452  CB  MET A 451    13561  13057  15065   -883   -686  -1650
ATOM   3453  CG  MET A 451      51.070  37.741  -6.971  1.00109.96           C  
ANISOU 3453  CG  MET A 451    13602  13000  15176   -818   -769  -1597
ATOM   3454  SD  MET A 451      50.342  37.406  -5.359  1.00109.82           S  
ANISOU 3454  SD  MET A 451    13733  12721  15274   -595   -863  -1407
ATOM   3455  CE  MET A 451      49.337  38.870  -5.139  1.00110.80           C  
ANISOU 3455  CE  MET A 451    14166  12790  15142   -621   -881  -1203
ATOM   3456  N   ASP A 452      48.886  36.140 -10.637  1.00118.57           N  
ANISOU 3456  N   ASP A 452    14475  14416  16162  -1065   -492  -1949
ATOM   3457  CA  ASP A 452      47.900  36.065 -11.709  1.00118.02           C  
ANISOU 3457  CA  ASP A 452    14445  14433  15965  -1199   -457  -1944
ATOM   3458  C   ASP A 452      47.119  34.756 -11.660  1.00117.96           C  
ANISOU 3458  C   ASP A 452    14361  14300  16161  -1046   -438  -2012
ATOM   3459  O   ASP A 452      45.929  34.729 -11.996  1.00117.55           O  
ANISOU 3459  O   ASP A 452    14404  14205  16055  -1062   -469  -1881
ATOM   3460  CB  ASP A 452      48.606  36.222 -13.059  1.00117.69           C  
ANISOU 3460  CB  ASP A 452    14297  14681  15738  -1492   -357  -2151
ATOM   3461  CG  ASP A 452      47.645  36.492 -14.206  1.00117.93           C  
ANISOU 3461  CG  ASP A 452    14416  14835  15556  -1718   -361  -2082
ATOM   3462  OD1 ASP A 452      46.424  36.591 -13.967  1.00118.77           O  
ANISOU 3462  OD1 ASP A 452    14654  14785  15687  -1632   -448  -1863
ATOM   3463  OD2 ASP A 452      48.120  36.601 -15.357  1.00117.81           O1-
ANISOU 3463  OD2 ASP A 452    14331  15083  15347  -2002   -279  -2243
ATOM   3464  N   SER A 453      47.760  33.668 -11.229  1.00115.78           N  
ANISOU 3464  N   SER A 453    13903  13946  16143   -901   -409  -2197
ATOM   3465  CA  SER A 453      47.086  32.376 -11.171  1.00114.89           C  
ANISOU 3465  CA  SER A 453    13704  13697  16252   -761   -416  -2264
ATOM   3466  C   SER A 453      46.299  32.213  -9.875  1.00114.24           C  
ANISOU 3466  C   SER A 453    13725  13379  16302   -533   -537  -2005
ATOM   3467  O   SER A 453      45.132  31.800  -9.897  1.00113.96           O  
ANISOU 3467  O   SER A 453    13749  13256  16297   -471   -572  -1889
ATOM   3468  CB  SER A 453      48.107  31.246 -11.325  1.00114.70           C  
ANISOU 3468  CB  SER A 453    13415  13671  16496   -713   -348  -2582
ATOM   3469  OG  SER A 453      47.480  29.978 -11.247  1.00114.51           O  
ANISOU 3469  OG  SER A 453    13302  13490  16718   -578   -381  -2646
ATOM   3470  N   GLU A 454      46.921  32.532  -8.735  1.00101.06           N  
ANISOU 3470  N   GLU A 454    12080  11618  14701   -427   -603  -1908
ATOM   3471  CA  GLU A 454      46.230  32.402  -7.457  1.00100.45           C  
ANISOU 3471  CA  GLU A 454    12107  11348  14710   -248   -704  -1674
ATOM   3472  C   GLU A 454      44.997  33.292  -7.383  1.00100.83           C  
ANISOU 3472  C   GLU A 454    12374  11376  14560   -253   -706  -1441
ATOM   3473  O   GLU A 454      44.072  32.995  -6.617  1.00100.31           O  
ANISOU 3473  O   GLU A 454    12374  11176  14562   -119   -752  -1271
ATOM   3474  CB  GLU A 454      47.183  32.712  -6.303  1.00100.48           C  
ANISOU 3474  CB  GLU A 454    12123  11286  14770   -193   -776  -1612
ATOM   3475  CG  GLU A 454      46.566  32.497  -4.932  1.00100.18           C  
ANISOU 3475  CG  GLU A 454    12189  11077  14799    -47   -877  -1389
ATOM   3476  CD  GLU A 454      47.555  32.679  -3.806  1.00100.35           C  
ANISOU 3476  CD  GLU A 454    12218  11037  14874    -33   -970  -1327
ATOM   3477  OE1 GLU A 454      48.736  32.969  -4.091  1.00100.45           O  
ANISOU 3477  OE1 GLU A 454    12142  11126  14899   -117   -963  -1450
ATOM   3478  OE2 GLU A 454      47.149  32.530  -2.635  1.00100.85           O1-
ANISOU 3478  OE2 GLU A 454    12375  10985  14958     44  -1055  -1148
ATOM   3479  N   GLU A 455      44.951  34.370  -8.167  1.00106.55           N  
ANISOU 3479  N   GLU A 455    13195  12227  15061   -413   -664  -1420
ATOM   3480  CA  GLU A 455      43.692  35.088  -8.322  1.00107.63           C  
ANISOU 3480  CA  GLU A 455    13490  12324  15080   -426   -676  -1212
ATOM   3481  C   GLU A 455      42.670  34.228  -9.055  1.00107.28           C  
ANISOU 3481  C   GLU A 455    13385  12272  15105   -432   -669  -1210
ATOM   3482  O   GLU A 455      41.524  34.092  -8.611  1.00106.84           O  
ANISOU 3482  O   GLU A 455    13390  12092  15110   -318   -698  -1027
ATOM   3483  CB  GLU A 455      43.913  36.405  -9.065  1.00108.02           C  
ANISOU 3483  CB  GLU A 455    13635  12497  14909   -625   -673  -1173
ATOM   3484  CG  GLU A 455      42.652  37.245  -9.185  1.00109.35           C  
ANISOU 3484  CG  GLU A 455    13948  12588  15013   -636   -709   -939
ATOM   3485  CD  GLU A 455      42.886  38.552  -9.909  1.00109.25           C  
ANISOU 3485  CD  GLU A 455    14019  12675  14818   -849   -750   -873
ATOM   3486  OE1 GLU A 455      44.028  38.784 -10.360  1.00108.40           O  
ANISOU 3486  OE1 GLU A 455    13862  12726  14600  -1002   -738  -1013
ATOM   3487  OE2 GLU A 455      41.929  39.347 -10.024  1.00110.15           O1-
ANISOU 3487  OE2 GLU A 455    14233  12701  14919   -868   -802   -673
ATOM   3488  N   ALA A 456      43.077  33.626 -10.178  1.00107.66           N  
ANISOU 3488  N   ALA A 456    13308  12456  15142   -576   -624  -1422
ATOM   3489  CA  ALA A 456      42.155  32.831 -10.984  1.00107.60           C  
ANISOU 3489  CA  ALA A 456    13259  12452  15173   -623   -625  -1436
ATOM   3490  C   ALA A 456      41.603  31.642 -10.209  1.00106.02           C  
ANISOU 3490  C   ALA A 456    12990  12075  15217   -408   -673  -1398
ATOM   3491  O   ALA A 456      40.499  31.170 -10.504  1.00105.44           O  
ANISOU 3491  O   ALA A 456    12933  11945  15185   -396   -709  -1290
ATOM   3492  CB  ALA A 456      42.849  32.359 -12.262  1.00107.72           C  
ANISOU 3492  CB  ALA A 456    13153  12656  15120   -831   -545  -1728
ATOM   3493  N   MET A 457      42.353  31.137  -9.228  1.00108.43           N  
ANISOU 3493  N   MET A 457    13215  12291  15693   -257   -696  -1463
ATOM   3494  CA  MET A 457      41.802  30.122  -8.336  1.00106.93           C  
ANISOU 3494  CA  MET A 457    12973  11929  15727    -71   -778  -1365
ATOM   3495  C   MET A 457      40.601  30.662  -7.570  1.00106.59           C  
ANISOU 3495  C   MET A 457    13083  11796  15620     23   -810  -1059
ATOM   3496  O   MET A 457      39.543  30.020  -7.506  1.00105.46           O  
ANISOU 3496  O   MET A 457    12929  11573  15569     89   -854   -933
ATOM   3497  CB  MET A 457      42.876  29.626  -7.369  1.00106.51           C  
ANISOU 3497  CB  MET A 457    12812  11797  15861     35   -830  -1445
ATOM   3498  CG  MET A 457      42.359  28.585  -6.404  1.00104.52           C  
ANISOU 3498  CG  MET A 457    12503  11374  15837    193   -947  -1315
ATOM   3499  SD  MET A 457      41.738  27.145  -7.283  1.00103.59           S  
ANISOU 3499  SD  MET A 457    12235  11196  15931    201   -987  -1441
ATOM   3500  CE  MET A 457      40.555  26.519  -6.095  1.00102.04           C  
ANISOU 3500  CE  MET A 457    12078  10837  15857    352  -1126  -1122
ATOM   3501  N   ILE A 458      40.750  31.850  -6.978  1.00 93.70           N  
ANISOU 3501  N   ILE A 458    11587  10173  13842     26   -783   -946
ATOM   3502  CA  ILE A 458      39.641  32.460  -6.256  1.00 92.96           C  
ANISOU 3502  CA  ILE A 458    11628   9994  13698    115   -778   -696
ATOM   3503  C   ILE A 458      38.509  32.794  -7.218  1.00 92.92           C  
ANISOU 3503  C   ILE A 458    11658  10008  13638     38   -764   -583
ATOM   3504  O   ILE A 458      37.336  32.820  -6.829  1.00 92.60           O  
ANISOU 3504  O   ILE A 458    11656   9879  13647    127   -767   -383
ATOM   3505  CB  ILE A 458      40.142  33.695  -5.482  1.00 92.72           C  
ANISOU 3505  CB  ILE A 458    11738   9960  13531    121   -745   -648
ATOM   3506  CG1 ILE A 458      41.259  33.285  -4.524  1.00 92.95           C  
ANISOU 3506  CG1 ILE A 458    11728   9967  13621    170   -788   -731
ATOM   3507  CG2 ILE A 458      39.018  34.327  -4.685  1.00 92.36           C  
ANISOU 3507  CG2 ILE A 458    11818   9817  13455    223   -708   -436
ATOM   3508  CD1 ILE A 458      41.990  34.444  -3.904  1.00 92.94           C  
ANISOU 3508  CD1 ILE A 458    11863   9979  13473    135   -772   -721
ATOM   3509  N   ASN A 459      38.837  33.032  -8.491  1.00102.92           N  
ANISOU 3509  N   ASN A 459    12903  11397  14805   -147   -754   -700
ATOM   3510  CA  ASN A 459      37.806  33.155  -9.516  1.00104.28           C  
ANISOU 3510  CA  ASN A 459    13093  11594  14937   -267   -777   -586
ATOM   3511  C   ASN A 459      37.048  31.842  -9.683  1.00102.62           C  
ANISOU 3511  C   ASN A 459    12791  11323  14876   -210   -821   -568
ATOM   3512  O   ASN A 459      35.823  31.840  -9.857  1.00102.44           O  
ANISOU 3512  O   ASN A 459    12792  11238  14894   -202   -860   -359
ATOM   3513  CB  ASN A 459      38.440  33.590 -10.840  1.00106.59           C  
ANISOU 3513  CB  ASN A 459    13380  12063  15058   -528   -766   -730
ATOM   3514  CG  ASN A 459      37.413  33.967 -11.895  1.00108.21           C  
ANISOU 3514  CG  ASN A 459    13630  12301  15186   -708   -822   -563
ATOM   3515  OD1 ASN A 459      36.206  33.911 -11.660  1.00109.21           O  
ANISOU 3515  OD1 ASN A 459    13776  12303  15416   -621   -867   -337
ATOM   3516  ND2 ASN A 459      37.894  34.350 -13.072  1.00108.28           N  
ANISOU 3516  ND2 ASN A 459    13643  12486  15012   -982   -825   -663
ATOM   3517  N   LYS A 460      37.761  30.714  -9.631  1.00105.89           N  
ANISOU 3517  N   LYS A 460    13089  11742  15404   -170   -829   -778
ATOM   3518  CA  LYS A 460      37.103  29.413  -9.718  1.00104.10           C  
ANISOU 3518  CA  LYS A 460    12772  11433  15347   -109   -894   -768
ATOM   3519  C   LYS A 460      36.157  29.199  -8.543  1.00101.92           C  
ANISOU 3519  C   LYS A 460    12518  11016  15191     81   -942   -508
ATOM   3520  O   LYS A 460      34.967  28.913  -8.732  1.00101.91           O  
ANISOU 3520  O   LYS A 460    12521  10962  15239     92   -988   -321
ATOM   3521  CB  LYS A 460      38.149  28.298  -9.776  1.00103.03           C  
ANISOU 3521  CB  LYS A 460    12489  11292  15365    -85   -902  -1057
ATOM   3522  CG  LYS A 460      39.001  28.300 -11.033  1.00104.60           C  
ANISOU 3522  CG  LYS A 460    12635  11647  15460   -285   -825  -1357
ATOM   3523  CD  LYS A 460      40.011  27.163 -11.011  1.00103.11           C  
ANISOU 3523  CD  LYS A 460    12266  11418  15492   -228   -819  -1660
ATOM   3524  CE  LYS A 460      40.789  27.087 -12.315  1.00103.89           C  
ANISOU 3524  CE  LYS A 460    12295  11689  15488   -437   -704  -1997
ATOM   3525  NZ  LYS A 460      41.671  28.269 -12.512  1.00105.68           N1+
ANISOU 3525  NZ  LYS A 460    12569  12085  15498   -559   -610  -2053
ATOM   3526  N   LEU A 461      36.671  29.337  -7.316  1.00 87.72           N  
ANISOU 3526  N   LEU A 461    10731   9168  13430    212   -934   -485
ATOM   3527  CA  LEU A 461      35.818  29.186  -6.140  1.00 87.27           C  
ANISOU 3527  CA  LEU A 461    10700   9014  13445    361   -959   -249
ATOM   3528  C   LEU A 461      34.639  30.149  -6.183  1.00 86.93           C  
ANISOU 3528  C   LEU A 461    10756   8959  13317    366   -899    -24
ATOM   3529  O   LEU A 461      33.536  29.812  -5.737  1.00 86.91           O  
ANISOU 3529  O   LEU A 461    10734   8890  13396    451   -917    179
ATOM   3530  CB  LEU A 461      36.628  29.403  -4.863  1.00 87.14           C  
ANISOU 3530  CB  LEU A 461    10715   8977  13418    442   -952   -264
ATOM   3531  CG  LEU A 461      37.698  28.372  -4.520  1.00 87.71           C  
ANISOU 3531  CG  LEU A 461    10661   9015  13650    462  -1047   -419
ATOM   3532  CD1 LEU A 461      38.477  28.801  -3.291  1.00 87.70           C  
ANISOU 3532  CD1 LEU A 461    10718   9003  13601    498  -1053   -391
ATOM   3533  CD2 LEU A 461      37.052  27.028  -4.295  1.00 88.10           C  
ANISOU 3533  CD2 LEU A 461    10596   8971  13907    527  -1169   -328
ATOM   3534  N   LYS A 462      34.851  31.352  -6.723  1.00 99.82           N  
ANISOU 3534  N   LYS A 462    12475  10646  14807    272   -838    -48
ATOM   3535  CA  LYS A 462      33.775  32.336  -6.788  1.00100.91           C  
ANISOU 3535  CA  LYS A 462    12682  10737  14920    279   -797    163
ATOM   3536  C   LYS A 462      32.697  31.913  -7.777  1.00100.91           C  
ANISOU 3536  C   LYS A 462    12626  10723  14991    199   -865    301
ATOM   3537  O   LYS A 462      31.501  32.008  -7.477  1.00 99.52           O  
ANISOU 3537  O   LYS A 462    12436  10465  14912    278   -860    529
ATOM   3538  CB  LYS A 462      34.338  33.707  -7.161  1.00103.41           C  
ANISOU 3538  CB  LYS A 462    13096  11097  15099    178   -757    112
ATOM   3539  N   GLN A 463      33.097  31.445  -8.961  1.00105.72           N  
ANISOU 3539  N   GLN A 463    13201  11417  15553     29   -923    163
ATOM   3540  CA  GLN A 463      32.124  30.972  -9.936  1.00106.07           C  
ANISOU 3540  CA  GLN A 463    13207  11454  15641    -85  -1006    287
ATOM   3541  C   GLN A 463      31.507  29.638  -9.528  1.00103.24           C  
ANISOU 3541  C   GLN A 463    12763  11019  15445     29  -1068    352
ATOM   3542  O   GLN A 463      30.525  29.208 -10.144  1.00103.45           O  
ANISOU 3542  O   GLN A 463    12760  11014  15532    -39  -1149    506
ATOM   3543  CB  GLN A 463      32.783  30.869 -11.318  1.00108.83           C  
ANISOU 3543  CB  GLN A 463    13561  11939  15850   -337  -1035     89
ATOM   3544  CG  GLN A 463      31.816  30.648 -12.479  1.00111.03           C  
ANISOU 3544  CG  GLN A 463    13840  12234  16113   -532  -1133    232
ATOM   3545  CD  GLN A 463      32.509  30.638 -13.830  1.00114.32           C  
ANISOU 3545  CD  GLN A 463    14279  12820  16336   -827  -1143     20
ATOM   3546  OE1 GLN A 463      33.734  30.734 -13.914  1.00114.87           O  
ANISOU 3546  OE1 GLN A 463    14344  13000  16302   -870  -1062   -251
ATOM   3547  NE2 GLN A 463      31.724  30.531 -14.898  1.00115.52           N  
ANISOU 3547  NE2 GLN A 463    14455  13007  16431  -1053  -1240    148
ATOM   3548  N   ALA A 464      32.042  28.988  -8.494  1.00 95.52           N  
ANISOU 3548  N   ALA A 464    11742  10005  14545    183  -1056    264
ATOM   3549  CA  ALA A 464      31.446  27.761  -7.984  1.00 94.13           C  
ANISOU 3549  CA  ALA A 464    11479   9748  14536    287  -1142    362
ATOM   3550  C   ALA A 464      30.465  28.001  -6.845  1.00 93.16           C  
ANISOU 3550  C   ALA A 464    11360   9561  14475    439  -1108    634
ATOM   3551  O   ALA A 464      29.482  27.261  -6.725  1.00 92.37           O  
ANISOU 3551  O   ALA A 464    11195   9408  14495    478  -1182    821
ATOM   3552  CB  ALA A 464      32.539  26.798  -7.513  1.00 93.43           C  
ANISOU 3552  CB  ALA A 464    11317   9646  14537    343  -1187    142
ATOM   3553  N   CYS A 465      30.703  29.006  -6.000  1.00 88.47           N  
ANISOU 3553  N   CYS A 465    10839   8977  13799    515   -992    652
ATOM   3554  CA  CYS A 465      29.842  29.253  -4.847  1.00 88.58           C  
ANISOU 3554  CA  CYS A 465    10856   8951  13852    649   -920    861
ATOM   3555  C   CYS A 465      29.113  30.586  -4.933  1.00 88.82           C  
ANISOU 3555  C   CYS A 465    10940   8951  13856    664   -805    989
ATOM   3556  O   CYS A 465      27.879  30.605  -4.885  1.00 89.29           O  
ANISOU 3556  O   CYS A 465    10942   8960  14025    712   -789   1212
ATOM   3557  CB  CYS A 465      30.664  29.177  -3.555  1.00 88.51           C  
ANISOU 3557  CB  CYS A 465    10881   8962  13786    726   -880    773
ATOM   3558  SG  CYS A 465      31.318  27.543  -3.194  1.00 88.68           S  
ANISOU 3558  SG  CYS A 465    10797   8969  13928    728  -1051    700
ATOM   3559  N   GLY A 466      29.825  31.696  -5.059  1.00102.53           N  
ANISOU 3559  N   GLY A 466    12770  10704  15481    626   -735    862
ATOM   3560  CA  GLY A 466      29.198  33.000  -5.113  1.00104.66           C  
ANISOU 3560  CA  GLY A 466    13083  10913  15770    644   -645    972
ATOM   3561  C   GLY A 466      30.067  34.053  -4.451  1.00106.07           C  
ANISOU 3561  C   GLY A 466    13380  11096  15827    675   -542    824
ATOM   3562  O   GLY A 466      31.228  33.817  -4.127  1.00106.38           O  
ANISOU 3562  O   GLY A 466    13470  11200  15751    652   -556    643
ATOM   3563  N   TYR A 467      29.467  35.232  -4.253  1.00113.65           N  
ANISOU 3563  N   TYR A 467    14373  11967  16842    726   -448    909
ATOM   3564  CA  TYR A 467      30.217  36.365  -3.714  1.00115.55           C  
ANISOU 3564  CA  TYR A 467    14739  12186  16979    742   -362    772
ATOM   3565  C   TYR A 467      30.504  36.205  -2.226  1.00115.08           C  
ANISOU 3565  C   TYR A 467    14745  12149  16830    855   -241    690
ATOM   3566  O   TYR A 467      31.602  36.542  -1.768  1.00116.57           O  
ANISOU 3566  O   TYR A 467    15044  12377  16870    823   -231    529
ATOM   3567  CB  TYR A 467      29.467  37.673  -3.972  1.00118.37           C  
ANISOU 3567  CB  TYR A 467    15101  12408  17466    763   -313    878
ATOM   3568  CG  TYR A 467      29.590  38.204  -5.386  1.00121.70           C  
ANISOU 3568  CG  TYR A 467    15510  12819  17912    587   -461    934
ATOM   3569  CD1 TYR A 467      30.563  37.718  -6.251  1.00122.82           C  
ANISOU 3569  CD1 TYR A 467    15673  13096  17899    416   -579    822
ATOM   3570  CD2 TYR A 467      28.748  39.210  -5.847  1.00123.15           C  
ANISOU 3570  CD2 TYR A 467    15652  12859  18282    574   -484   1099
ATOM   3571  CE1 TYR A 467      30.684  38.209  -7.542  1.00124.38           C  
ANISOU 3571  CE1 TYR A 467    15866  13319  18075    211   -709    873
ATOM   3572  CE2 TYR A 467      28.861  39.707  -7.136  1.00124.33           C  
ANISOU 3572  CE2 TYR A 467    15793  13008  18440    369   -650   1183
ATOM   3573  CZ  TYR A 467      29.830  39.203  -7.978  1.00125.08           C  
ANISOU 3573  CZ  TYR A 467    15927  13272  18327    174   -758   1070
ATOM   3574  OH  TYR A 467      29.946  39.694  -9.259  1.00126.53           O  
ANISOU 3574  OH  TYR A 467    16108  13491  18476    -72   -919   1155
ATOM   3575  N   GLU A 468      29.532  35.714  -1.451  1.00 99.44           N  
ANISOU 3575  N   GLU A 468    12699  10156  14927    962   -154    811
ATOM   3576  CA  GLU A 468      29.736  35.603  -0.008  1.00101.19           C  
ANISOU 3576  CA  GLU A 468    12992  10423  15032   1026    -35    747
ATOM   3577  C   GLU A 468      30.882  34.663   0.332  1.00100.79           C  
ANISOU 3577  C   GLU A 468    12972  10473  14852    955   -153    650
ATOM   3578  O   GLU A 468      31.573  34.861   1.339  1.00102.89           O  
ANISOU 3578  O   GLU A 468    13347  10777  14969    941   -104    553
ATOM   3579  CB  GLU A 468      28.464  35.117   0.685  1.00101.62           C  
ANISOU 3579  CB  GLU A 468    12948  10481  15182   1121     72    910
ATOM   3580  CG  GLU A 468      28.624  35.012   2.199  1.00104.80           C  
ANISOU 3580  CG  GLU A 468    13433  10964  15425   1143    202    852
ATOM   3581  CD  GLU A 468      27.388  34.493   2.899  1.00106.32           C  
ANISOU 3581  CD  GLU A 468    13515  11197  15684   1210    318   1013
ATOM   3582  OE1 GLU A 468      26.394  34.182   2.208  1.00104.09           O  
ANISOU 3582  OE1 GLU A 468    13086  10868  15598   1255    286   1183
ATOM   3583  OE2 GLU A 468      27.415  34.393   4.145  1.00109.95           O1-
ANISOU 3583  OE2 GLU A 468    14039  11749  15990   1195    436    979
ATOM   3584  N   PHE A 469      31.102  33.643  -0.492  1.00 93.43           N  
ANISOU 3584  N   PHE A 469    11940   9571  13989    900   -314    671
ATOM   3585  CA  PHE A 469      32.045  32.593  -0.135  1.00 92.79           C  
ANISOU 3585  CA  PHE A 469    11837   9551  13866    853   -437    598
ATOM   3586  C   PHE A 469      33.493  33.025  -0.339  1.00 93.08           C  
ANISOU 3586  C   PHE A 469    11954   9613  13800    774   -484    401
ATOM   3587  O   PHE A 469      34.378  32.581   0.400  1.00 93.53           O  
ANISOU 3587  O   PHE A 469    12032   9703  13802    745   -544    338
ATOM   3588  CB  PHE A 469      31.735  31.336  -0.952  1.00 90.95           C  
ANISOU 3588  CB  PHE A 469    11458   9316  13781    831   -585    663
ATOM   3589  CG  PHE A 469      32.511  30.126  -0.529  1.00 90.28           C  
ANISOU 3589  CG  PHE A 469    11311   9255  13737    803   -729    615
ATOM   3590  CD1 PHE A 469      32.160  29.434   0.614  1.00 90.77           C  
ANISOU 3590  CD1 PHE A 469    11345   9334  13809    830   -758    748
ATOM   3591  CD2 PHE A 469      33.585  29.678  -1.277  1.00 89.46           C  
ANISOU 3591  CD2 PHE A 469    11160   9154  13678    738   -841    441
ATOM   3592  CE1 PHE A 469      32.869  28.322   1.005  1.00 90.26           C  
ANISOU 3592  CE1 PHE A 469    11207   9265  13823    790   -930    734
ATOM   3593  CE2 PHE A 469      34.299  28.568  -0.889  1.00 88.94           C  
ANISOU 3593  CE2 PHE A 469    11006   9073  13713    723   -985    396
ATOM   3594  CZ  PHE A 469      33.940  27.889   0.253  1.00 89.23           C  
ANISOU 3594  CZ  PHE A 469    11016   9103  13785    749  -1048    555
ATOM   3595  N   THR A 470      33.753  33.899  -1.311  1.00 93.44           N  
ANISOU 3595  N   THR A 470    12035   9645  13821    723   -471    325
ATOM   3596  CA  THR A 470      35.111  34.260  -1.698  1.00 94.66           C  
ANISOU 3596  CA  THR A 470    12239   9844  13885    630   -523    148
ATOM   3597  C   THR A 470      35.389  35.751  -1.516  1.00 97.12           C  
ANISOU 3597  C   THR A 470    12696  10125  14079    612   -437    101
ATOM   3598  O   THR A 470      36.176  36.333  -2.264  1.00 98.77           O  
ANISOU 3598  O   THR A 470    12933  10366  14228    514   -479      1
ATOM   3599  CB  THR A 470      35.375  33.847  -3.144  1.00 94.07           C  
ANISOU 3599  CB  THR A 470    12066   9812  13865    532   -611     77
ATOM   3600  OG1 THR A 470      34.449  34.517  -4.008  1.00 94.32           O  
ANISOU 3600  OG1 THR A 470    12102   9813  13924    500   -585    183
ATOM   3601  CG2 THR A 470      35.203  32.351  -3.306  1.00 91.99           C  
ANISOU 3601  CG2 THR A 470    11663   9554  13734    550   -705     88
ATOM   3602  N   SER A 471      34.756  36.386  -0.528  1.00 95.89           N  
ANISOU 3602  N   SER A 471    12630   9910  13891    695   -316    161
ATOM   3603  CA  SER A 471      34.965  37.815  -0.312  1.00 97.48           C  
ANISOU 3603  CA  SER A 471    12974  10051  14012    688   -237    101
ATOM   3604  C   SER A 471      36.240  38.070   0.483  1.00 98.52           C  
ANISOU 3604  C   SER A 471    13232  10223  13978    628   -259    -28
ATOM   3605  O   SER A 471      37.150  38.777   0.021  1.00 98.74           O  
ANISOU 3605  O   SER A 471    13321  10259  13935    542   -314   -118
ATOM   3606  CB  SER A 471      33.758  38.419   0.408  1.00 98.74           C  
ANISOU 3606  CB  SER A 471    13169  10117  14229    804    -74    179
ATOM   3607  OG  SER A 471      33.664  37.924   1.732  1.00 99.87           O  
ANISOU 3607  OG  SER A 471    13358  10305  14283    846      9    177
ATOM   3608  N   LYS A 472      36.311  37.506   1.693  1.00 98.86           N  
ANISOU 3608  N   LYS A 472    13314  10297  13951    651   -230    -16
ATOM   3609  CA  LYS A 472      37.517  37.622   2.503  1.00 99.94           C  
ANISOU 3609  CA  LYS A 472    13565  10472  13935    568   -282   -104
ATOM   3610  C   LYS A 472      38.740  37.128   1.749  1.00 98.68           C  
ANISOU 3610  C   LYS A 472    13318  10368  13809    480   -442   -175
ATOM   3611  O   LYS A 472      39.836  37.670   1.920  1.00 99.43           O  
ANISOU 3611  O   LYS A 472    13499  10477  13802    397   -492   -259
ATOM   3612  CB  LYS A 472      37.351  36.854   3.814  1.00101.01           C  
ANISOU 3612  CB  LYS A 472    13725  10651  14002    563   -270    -37
ATOM   3613  CG  LYS A 472      36.362  37.488   4.775  1.00103.37           C  
ANISOU 3613  CG  LYS A 472    14140  10925  14211    617    -75    -18
ATOM   3614  CD  LYS A 472      36.321  36.747   6.101  1.00104.88           C  
ANISOU 3614  CD  LYS A 472    14372  11200  14279    553    -74     50
ATOM   3615  CE  LYS A 472      35.356  37.412   7.071  1.00107.58           C  
ANISOU 3615  CE  LYS A 472    14830  11545  14501    586    161     31
ATOM   3616  NZ  LYS A 472      35.317  36.712   8.386  1.00109.50           N1+
ANISOU 3616  NZ  LYS A 472    15125  11906  14575    474    163    105
ATOM   3617  N   LEU A 473      38.572  36.108   0.908  1.00 97.99           N  
ANISOU 3617  N   LEU A 473    13053  10311  13868    493   -515   -154
ATOM   3618  CA  LEU A 473      39.661  35.690   0.035  1.00 97.43           C  
ANISOU 3618  CA  LEU A 473    12875  10294  13849    413   -627   -264
ATOM   3619  C   LEU A 473      39.997  36.774  -0.980  1.00 98.14           C  
ANISOU 3619  C   LEU A 473    13009  10407  13871    338   -605   -339
ATOM   3620  O   LEU A 473      41.173  37.008  -1.279  1.00 99.01           O  
ANISOU 3620  O   LEU A 473    13114  10573  13933    244   -662   -445
ATOM   3621  CB  LEU A 473      39.296  34.386  -0.677  1.00 95.06           C  
ANISOU 3621  CB  LEU A 473    12384  10010  13725    439   -691   -253
ATOM   3622  CG  LEU A 473      39.450  33.050   0.056  1.00 93.29           C  
ANISOU 3622  CG  LEU A 473    12054   9768  13625    470   -795   -207
ATOM   3623  CD1 LEU A 473      38.410  32.870   1.151  1.00 93.10           C  
ANISOU 3623  CD1 LEU A 473    12090   9714  13568    535   -750    -37
ATOM   3624  CD2 LEU A 473      39.352  31.928  -0.951  1.00 91.34           C  
ANISOU 3624  CD2 LEU A 473    11617   9522  13566    477   -869   -261
ATOM   3625  N   HIS A 474      38.978  37.454  -1.512  1.00103.87           N  
ANISOU 3625  N   HIS A 474    13768  11089  14609    364   -537   -266
ATOM   3626  CA  HIS A 474      39.212  38.411  -2.589  1.00104.32           C  
ANISOU 3626  CA  HIS A 474    13848  11169  14620    260   -556   -299
ATOM   3627  C   HIS A 474      39.974  39.631  -2.092  1.00105.55           C  
ANISOU 3627  C   HIS A 474    14163  11297  14646    210   -554   -348
ATOM   3628  O   HIS A 474      41.061  39.941  -2.592  1.00105.90           O  
ANISOU 3628  O   HIS A 474    14203  11419  14614     88   -621   -434
ATOM   3629  CB  HIS A 474      37.894  38.840  -3.231  1.00104.17           C  
ANISOU 3629  CB  HIS A 474    13812  11081  14687    286   -520   -170
ATOM   3630  CG  HIS A 474      38.075  39.799  -4.365  1.00104.91           C  
ANISOU 3630  CG  HIS A 474    13922  11198  14743    142   -578   -162
ATOM   3631  ND1 HIS A 474      38.555  39.410  -5.597  1.00104.92           N  
ANISOU 3631  ND1 HIS A 474    13827  11330  14710    -15   -652   -218
ATOM   3632  CD2 HIS A 474      37.864  41.134  -4.447  1.00105.90           C  
ANISOU 3632  CD2 HIS A 474    14145  11233  14861    111   -583   -104
ATOM   3633  CE1 HIS A 474      38.620  40.461  -6.394  1.00105.97           C  
ANISOU 3633  CE1 HIS A 474    14001  11473  14789   -159   -708   -171
ATOM   3634  NE2 HIS A 474      38.206  41.520  -5.720  1.00106.47           N  
ANISOU 3634  NE2 HIS A 474    14178  11389  14888    -79   -683    -92
ATOM   3635  N   ARG A 475      39.416  40.356  -1.121  1.00119.59           N  
ANISOU 3635  N   ARG A 475    16079  12965  16396    295   -471   -304
ATOM   3636  CA  ARG A 475      40.156  41.512  -0.622  1.00121.51           C  
ANISOU 3636  CA  ARG A 475    16489  13165  16514    239   -480   -363
ATOM   3637  C   ARG A 475      41.349  41.096   0.227  1.00121.87           C  
ANISOU 3637  C   ARG A 475    16584  13273  16449    190   -533   -436
ATOM   3638  O   ARG A 475      42.286  41.886   0.394  1.00123.40           O  
ANISOU 3638  O   ARG A 475    16886  13467  16532     99   -586   -489
ATOM   3639  CB  ARG A 475      39.229  42.455   0.145  1.00122.14           C  
ANISOU 3639  CB  ARG A 475    16705  13096  16608    338   -361   -335
ATOM   3640  CG  ARG A 475      38.200  43.134  -0.756  1.00121.79           C  
ANISOU 3640  CG  ARG A 475    16605  12954  16717    366   -346   -247
ATOM   3641  CD  ARG A 475      38.859  44.145  -1.705  1.00120.86           C  
ANISOU 3641  CD  ARG A 475    16518  12831  16572    221   -471   -250
ATOM   3642  NE  ARG A 475      37.890  44.796  -2.586  1.00120.02           N  
ANISOU 3642  NE  ARG A 475    16349  12619  16634    215   -500   -130
ATOM   3643  CZ  ARG A 475      38.201  45.668  -3.542  1.00119.60           C  
ANISOU 3643  CZ  ARG A 475    16299  12555  16590     66   -633    -78
ATOM   3644  NH1 ARG A 475      39.463  46.011  -3.751  1.00119.35           N  
ANISOU 3644  NH1 ARG A 475    16329  12623  16395    -82   -730   -150
ATOM   3645  NH2 ARG A 475      37.245  46.202  -4.292  1.00119.47           N1+
ANISOU 3645  NH2 ARG A 475    16212  12426  16755     47   -686     67
ATOM   3646  N   MET A 476      41.341  39.866   0.743  1.00104.71           N  
ANISOU 3646  N   MET A 476    14322  11143  14321    233   -544   -417
ATOM   3647  CA  MET A 476      42.552  39.276   1.300  1.00105.27           C  
ANISOU 3647  CA  MET A 476    14373  11270  14353    161   -645   -459
ATOM   3648  C   MET A 476      43.642  39.171   0.240  1.00104.48           C  
ANISOU 3648  C   MET A 476    14148  11259  14292     62   -737   -544
ATOM   3649  O   MET A 476      44.834  39.233   0.559  1.00105.11           O  
ANISOU 3649  O   MET A 476    14238  11371  14327    -23   -821   -588
ATOM   3650  CB  MET A 476      42.208  37.907   1.886  1.00104.61           C  
ANISOU 3650  CB  MET A 476    14180  11199  14369    220   -671   -396
ATOM   3651  CG  MET A 476      43.298  37.194   2.643  1.00105.13           C  
ANISOU 3651  CG  MET A 476    14210  11289  14446    147   -802   -393
ATOM   3652  SD  MET A 476      42.598  35.718   3.404  1.00104.30           S  
ANISOU 3652  SD  MET A 476    13994  11173  14463    205   -849   -270
ATOM   3653  CE  MET A 476      44.043  34.978   4.150  1.00104.79           C  
ANISOU 3653  CE  MET A 476    13986  11236  14592     89  -1057   -246
ATOM   3654  N   TYR A 477      43.246  39.022  -1.025  1.00 99.85           N  
ANISOU 3654  N   TYR A 477    13439  10719  13779     53   -720   -567
ATOM   3655  CA  TYR A 477      44.174  39.074  -2.148  1.00 99.82           C  
ANISOU 3655  CA  TYR A 477    13326  10829  13773    -71   -771   -667
ATOM   3656  C   TYR A 477      44.451  40.501  -2.602  1.00100.12           C  
ANISOU 3656  C   TYR A 477    13486  10878  13675   -180   -783   -661
ATOM   3657  O   TYR A 477      45.511  40.767  -3.180  1.00100.40           O  
ANISOU 3657  O   TYR A 477    13471  11019  13655   -312   -835   -735
ATOM   3658  CB  TYR A 477      43.611  38.249  -3.305  1.00 99.50           C  
ANISOU 3658  CB  TYR A 477    13115  10852  13840    -74   -749   -701
ATOM   3659  CG  TYR A 477      44.319  38.422  -4.626  1.00 99.79           C  
ANISOU 3659  CG  TYR A 477    13051  11033  13833   -234   -764   -814
ATOM   3660  CD1 TYR A 477      45.559  37.852  -4.859  1.00100.27           C  
ANISOU 3660  CD1 TYR A 477    12970  11191  13935   -301   -789   -964
ATOM   3661  CD2 TYR A 477      43.728  39.148  -5.652  1.00 99.88           C  
ANISOU 3661  CD2 TYR A 477    13094  11087  13767   -337   -754   -764
ATOM   3662  CE1 TYR A 477      46.194  38.007  -6.076  1.00100.85           C  
ANISOU 3662  CE1 TYR A 477    12943  11427  13947   -466   -772  -1087
ATOM   3663  CE2 TYR A 477      44.355  39.310  -6.866  1.00100.42           C  
ANISOU 3663  CE2 TYR A 477    13079  11320  13755   -528   -767   -859
ATOM   3664  CZ  TYR A 477      45.589  38.739  -7.074  1.00100.92           C  
ANISOU 3664  CZ  TYR A 477    13007  11505  13833   -592   -759  -1034
ATOM   3665  OH  TYR A 477      46.218  38.898  -8.287  1.00101.76           O  
ANISOU 3665  OH  TYR A 477    13021  11806  13839   -800   -742  -1150
ATOM   3666  N   THR A 478      43.524  41.426  -2.350  1.00110.31           N  
ANISOU 3666  N   THR A 478    14922  12058  14934   -131   -740   -572
ATOM   3667  CA  THR A 478      43.708  42.809  -2.777  1.00110.18           C  
ANISOU 3667  CA  THR A 478    15017  12016  14831   -234   -781   -547
ATOM   3668  C   THR A 478      44.667  43.566  -1.868  1.00110.66           C  
ANISOU 3668  C   THR A 478    15236  12038  14772   -278   -828   -578
ATOM   3669  O   THR A 478      45.399  44.444  -2.342  1.00110.36           O  
ANISOU 3669  O   THR A 478    15241  12039  14652   -415   -909   -584
ATOM   3670  CB  THR A 478      42.354  43.522  -2.834  1.00110.15           C  
ANISOU 3670  CB  THR A 478    15084  11868  14900   -156   -730   -444
ATOM   3671  OG1 THR A 478      41.505  42.854  -3.776  1.00109.75           O  
ANISOU 3671  OG1 THR A 478    14886  11860  14954   -150   -716   -388
ATOM   3672  CG2 THR A 478      42.520  44.973  -3.258  1.00110.08           C  
ANISOU 3672  CG2 THR A 478    15180  11796  14849   -265   -806   -402
ATOM   3673  N   ASP A 479      44.702  43.230  -0.574  1.00110.59           N  
ANISOU 3673  N   ASP A 479    15316  11963  14739   -191   -792   -586
ATOM   3674  CA  ASP A 479      45.600  43.917   0.348  1.00111.05           C  
ANISOU 3674  CA  ASP A 479    15545  11982  14666   -257   -848   -607
ATOM   3675  C   ASP A 479      47.069  43.806  -0.047  1.00110.80           C  
ANISOU 3675  C   ASP A 479    15430  12074  14594   -401   -967   -645
ATOM   3676  O   ASP A 479      47.898  44.523   0.522  1.00111.44           O  
ANISOU 3676  O   ASP A 479    15649  12129  14564   -489  -1043   -643
ATOM   3677  CB  ASP A 479      45.414  43.391   1.774  1.00112.82           C  
ANISOU 3677  CB  ASP A 479    15866  12151  14850   -186   -803   -598
ATOM   3678  CG  ASP A 479      44.114  43.855   2.404  1.00113.67           C  
ANISOU 3678  CG  ASP A 479    16106  12134  14952    -69   -662   -585
ATOM   3679  OD1 ASP A 479      43.601  44.921   2.000  1.00113.27           O  
ANISOU 3679  OD1 ASP A 479    16129  11987  14922    -51   -627   -592
ATOM   3680  OD2 ASP A 479      43.616  43.167   3.318  1.00115.09           O1-
ANISOU 3680  OD2 ASP A 479    16304  12308  15118     -5   -592   -566
ATOM   3681  N   MET A 480      47.415  42.941  -1.001  1.00102.20           N  
ANISOU 3681  N   MET A 480    14115  11118  13597   -434   -979   -689
ATOM   3682  CA  MET A 480      48.787  42.919  -1.491  1.00101.96           C  
ANISOU 3682  CA  MET A 480    13976  11218  13548   -574  -1063   -745
ATOM   3683  C   MET A 480      49.032  44.038  -2.497  1.00101.78           C  
ANISOU 3683  C   MET A 480    13983  11264  13424   -721  -1103   -735
ATOM   3684  O   MET A 480      50.101  44.660  -2.490  1.00101.92           O  
ANISOU 3684  O   MET A 480    14034  11336  13356   -852  -1191   -734
ATOM   3685  CB  MET A 480      49.102  41.557  -2.104  1.00101.42           C  
ANISOU 3685  CB  MET A 480    13641  11260  13634   -556  -1040   -834
ATOM   3686  CG  MET A 480      49.004  40.408  -1.110  1.00101.64           C  
ANISOU 3686  CG  MET A 480    13615  11210  13793   -437  -1051   -819
ATOM   3687  SD  MET A 480      50.097  40.599   0.314  1.00102.60           S  
ANISOU 3687  SD  MET A 480    13850  11265  13866   -495  -1178   -751
ATOM   3688  CE  MET A 480      48.935  41.097   1.587  1.00103.68           C  
ANISOU 3688  CE  MET A 480    14272  11258  13864   -412  -1127   -649
ATOM   3689  N   SER A 481      48.051  44.313  -3.359  1.00106.15           N  
ANISOU 3689  N   SER A 481    14523  11818  13993   -721  -1061   -703
ATOM   3690  CA  SER A 481      48.148  45.460  -4.257  1.00105.66           C  
ANISOU 3690  CA  SER A 481    14506  11800  13840   -885  -1133   -650
ATOM   3691  C   SER A 481      48.021  46.770  -3.485  1.00104.70           C  
ANISOU 3691  C   SER A 481    14623  11500  13658   -876  -1198   -573
ATOM   3692  O   SER A 481      48.832  47.691  -3.659  1.00103.65           O  
ANISOU 3692  O   SER A 481    14558  11397  13428  -1027  -1310   -543
ATOM   3693  CB  SER A 481      47.075  45.362  -5.343  1.00105.50           C  
ANISOU 3693  CB  SER A 481    14405  11809  13872   -908  -1099   -604
ATOM   3694  OG  SER A 481      47.102  46.491  -6.199  1.00105.53           O  
ANISOU 3694  OG  SER A 481    14452  11846  13799  -1094  -1202   -515
ATOM   3695  N   VAL A 482      47.002  46.868  -2.626  1.00100.69           N  
ANISOU 3695  N   VAL A 482    14240  10806  13213   -705  -1124   -550
ATOM   3696  CA  VAL A 482      46.851  48.039  -1.767  1.00101.59           C  
ANISOU 3696  CA  VAL A 482    14585  10728  13285   -678  -1154   -526
ATOM   3697  C   VAL A 482      48.096  48.236  -0.913  1.00102.02           C  
ANISOU 3697  C   VAL A 482    14752  10802  13210   -754  -1228   -563
ATOM   3698  O   VAL A 482      48.526  49.370  -0.667  1.00102.95           O  
ANISOU 3698  O   VAL A 482    15032  10832  13250   -841  -1324   -542
ATOM   3699  CB  VAL A 482      45.583  47.906  -0.903  1.00101.71           C  
ANISOU 3699  CB  VAL A 482    14685  10571  13388   -478  -1014   -537
ATOM   3700  CG1 VAL A 482      45.501  49.030   0.115  1.00102.99           C  
ANISOU 3700  CG1 VAL A 482    15092  10539  13501   -449  -1010   -569
ATOM   3701  CG2 VAL A 482      44.348  47.902  -1.785  1.00101.54           C  
ANISOU 3701  CG2 VAL A 482    14554  10505  13522   -420   -971   -467
ATOM   3702  N   SER A 483      48.705  47.139  -0.461  1.00100.34           N  
ANISOU 3702  N   SER A 483    14446  10688  12989   -734  -1207   -604
ATOM   3703  CA  SER A 483      49.924  47.257   0.330  1.00100.91           C  
ANISOU 3703  CA  SER A 483    14602  10778  12960   -828  -1304   -607
ATOM   3704  C   SER A 483      51.109  47.701  -0.518  1.00101.22           C  
ANISOU 3704  C   SER A 483    14552  10956  12950  -1014  -1430   -588
ATOM   3705  O   SER A 483      51.985  48.418  -0.023  1.00102.02           O  
ANISOU 3705  O   SER A 483    14784  11029  12949  -1124  -1545   -555
ATOM   3706  CB  SER A 483      50.240  45.934   1.020  1.00100.57           C  
ANISOU 3706  CB  SER A 483    14455  10785  12973   -769  -1280   -625
ATOM   3707  OG  SER A 483      51.450  46.035   1.744  1.00101.31           O  
ANISOU 3707  OG  SER A 483    14610  10890  12992   -883  -1402   -597
ATOM   3708  N   ALA A 484      51.162  47.288  -1.786  1.00108.19           N  
ANISOU 3708  N   ALA A 484    15215  12002  13889  -1070  -1408   -609
ATOM   3709  CA  ALA A 484      52.238  47.740  -2.664  1.00107.74           C  
ANISOU 3709  CA  ALA A 484    15059  12112  13763  -1272  -1505   -597
ATOM   3710  C   ALA A 484      52.139  49.240  -2.918  1.00106.20           C  
ANISOU 3710  C   ALA A 484    15041  11840  13471  -1391  -1620   -505
ATOM   3711  O   ALA A 484      53.092  49.993  -2.669  1.00105.67           O  
ANISOU 3711  O   ALA A 484    15063  11779  13309  -1524  -1750   -457
ATOM   3712  CB  ALA A 484      52.204  46.964  -3.982  1.00107.85           C  
ANISOU 3712  CB  ALA A 484    14812  12334  13833  -1328  -1429   -666
ATOM   3713  N   ASP A 485      50.982  49.693  -3.412  1.00106.33           N  
ANISOU 3713  N   ASP A 485    15101  11765  13533  -1350  -1595   -463
ATOM   3714  CA  ASP A 485      50.788  51.120  -3.658  1.00105.19           C  
ANISOU 3714  CA  ASP A 485    15108  11503  13355  -1455  -1729   -363
ATOM   3715  C   ASP A 485      50.986  51.932  -2.384  1.00104.74           C  
ANISOU 3715  C   ASP A 485    15309  11229  13257  -1401  -1787   -365
ATOM   3716  O   ASP A 485      51.591  53.012  -2.413  1.00103.92           O  
ANISOU 3716  O   ASP A 485    15322  11080  13084  -1546  -1947   -300
ATOM   3717  CB  ASP A 485      49.396  51.362  -4.242  1.00105.29           C  
ANISOU 3717  CB  ASP A 485    15108  11406  13490  -1388  -1693   -308
ATOM   3718  CG  ASP A 485      49.179  52.801  -4.660  1.00104.19           C  
ANISOU 3718  CG  ASP A 485    15079  11133  13374  -1515  -1865   -183
ATOM   3719  OD1 ASP A 485      49.747  53.217  -5.693  1.00103.03           O  
ANISOU 3719  OD1 ASP A 485    14846  11152  13149  -1755  -2002    -92
ATOM   3720  OD2 ASP A 485      48.430  53.513  -3.959  1.00104.25           O1-
ANISOU 3720  OD2 ASP A 485    15250  10870  13491  -1384  -1864   -178
ATOM   3721  N   LEU A 486      50.496  51.419  -1.253  1.00 97.80           N  
ANISOU 3721  N   LEU A 486    14528  10224  12407  -1216  -1663   -441
ATOM   3722  CA  LEU A 486      50.678  52.108   0.019  1.00 98.77           C  
ANISOU 3722  CA  LEU A 486    14912  10161  12455  -1189  -1695   -472
ATOM   3723  C   LEU A 486      52.158  52.230   0.369  1.00 99.21           C  
ANISOU 3723  C   LEU A 486    15008  10312  12375  -1354  -1835   -442
ATOM   3724  O   LEU A 486      52.612  53.284   0.837  1.00100.38           O  
ANISOU 3724  O   LEU A 486    15361  10341  12438  -1448  -1962   -416
ATOM   3725  CB  LEU A 486      49.916  51.368   1.119  1.00 98.51           C  
ANISOU 3725  CB  LEU A 486    14951  10037  12443  -1002  -1522   -556
ATOM   3726  CG  LEU A 486      49.807  52.024   2.496  1.00 99.84           C  
ANISOU 3726  CG  LEU A 486    15408  10011  12516   -970  -1499   -623
ATOM   3727  CD1 LEU A 486      49.005  53.308   2.399  1.00101.09           C  
ANISOU 3727  CD1 LEU A 486    15710   9943  12758   -926  -1499   -651
ATOM   3728  CD2 LEU A 486      49.172  51.077   3.496  1.00 99.65           C  
ANISOU 3728  CD2 LEU A 486    15410   9976  12475   -835  -1328   -690
ATOM   3729  N   ASN A 487      52.931  51.164   0.134  1.00108.87           N  
ANISOU 3729  N   ASN A 487    16027  11739  13601  -1392  -1824   -444
ATOM   3730  CA  ASN A 487      54.373  51.241   0.353  1.00109.48           C  
ANISOU 3730  CA  ASN A 487    16090  11915  13593  -1555  -1964   -396
ATOM   3731  C   ASN A 487      55.012  52.296  -0.540  1.00108.00           C  
ANISOU 3731  C   ASN A 487    15892  11800  13342  -1752  -2120   -313
ATOM   3732  O   ASN A 487      55.919  53.013  -0.103  1.00107.91           O  
ANISOU 3732  O   ASN A 487    16010  11756  13233  -1889  -2275   -248
ATOM   3733  CB  ASN A 487      55.028  49.876   0.128  1.00111.10           C  
ANISOU 3733  CB  ASN A 487    16022  12309  13884  -1545  -1914   -426
ATOM   3734  CG  ASN A 487      54.814  48.923   1.294  1.00112.42           C  
ANISOU 3734  CG  ASN A 487    16226  12395  14095  -1419  -1851   -454
ATOM   3735  OD1 ASN A 487      54.912  49.315   2.457  1.00112.72           O  
ANISOU 3735  OD1 ASN A 487    16499  12297  14032  -1437  -1907   -425
ATOM   3736  ND2 ASN A 487      54.531  47.662   0.985  1.00113.65           N  
ANISOU 3736  ND2 ASN A 487    16153  12636  14393  -1312  -1745   -508
ATOM   3737  N   ASN A 488      54.555  52.414  -1.791  1.00108.58           N  
ANISOU 3737  N   ASN A 488    15819  11977  13460  -1796  -2098   -297
ATOM   3738  CA  ASN A 488      55.057  53.487  -2.649  1.00107.42           C  
ANISOU 3738  CA  ASN A 488    15673  11901  13242  -2014  -2266   -190
ATOM   3739  C   ASN A 488      54.764  54.857  -2.045  1.00106.39           C  
ANISOU 3739  C   ASN A 488    15833  11505  13086  -2031  -2406   -131
ATOM   3740  O   ASN A 488      55.647  55.726  -1.979  1.00105.99           O  
ANISOU 3740  O   ASN A 488    15877  11450  12945  -2205  -2593    -43
ATOM   3741  CB  ASN A 488      54.447  53.381  -4.047  1.00106.75           C  
ANISOU 3741  CB  ASN A 488    15404  11961  13195  -2083  -2228   -167
ATOM   3742  CG  ASN A 488      54.905  52.150  -4.792  1.00107.81           C  
ANISOU 3742  CG  ASN A 488    15249  12378  13334  -2117  -2100   -251
ATOM   3743  OD1 ASN A 488      54.106  51.272  -5.111  1.00108.03           O  
ANISOU 3743  OD1 ASN A 488    15164  12434  13446  -1993  -1949   -329
ATOM   3744  ND2 ASN A 488      56.200  52.080  -5.079  1.00109.13           N  
ANISOU 3744  ND2 ASN A 488    15286  12751  13427  -2288  -2157   -245
ATOM   3745  N   LYS A 489      53.521  55.068  -1.599  1.00100.85           N  
ANISOU 3745  N   LYS A 489    15265  10571  12482  -1850  -2316   -185
ATOM   3746  CA  LYS A 489      53.157  56.357  -1.018  1.00102.23           C  
ANISOU 3746  CA  LYS A 489    15703  10461  12679  -1842  -2422   -172
ATOM   3747  C   LYS A 489      54.025  56.686   0.187  1.00103.06           C  
ANISOU 3747  C   LYS A 489    16030  10477  12650  -1887  -2497   -202
ATOM   3748  O   LYS A 489      54.455  57.835   0.354  1.00104.46           O  
ANISOU 3748  O   LYS A 489    16383  10523  12785  -2012  -2683   -146
ATOM   3749  CB  LYS A 489      51.676  56.374  -0.645  1.00102.26           C  
ANISOU 3749  CB  LYS A 489    15779  10237  12837  -1615  -2264   -260
ATOM   3750  CG  LYS A 489      50.754  56.432  -1.847  1.00102.01           C  
ANISOU 3750  CG  LYS A 489    15573  10223  12963  -1610  -2262   -182
ATOM   3751  CD  LYS A 489      49.301  56.515  -1.426  1.00102.32           C  
ANISOU 3751  CD  LYS A 489    15670  10015  13192  -1381  -2113   -255
ATOM   3752  CE  LYS A 489      48.389  56.568  -2.638  1.00102.23           C  
ANISOU 3752  CE  LYS A 489    15476  10011  13356  -1399  -2143   -141
ATOM   3753  NZ  LYS A 489      46.955  56.632  -2.247  1.00102.70           N1+
ANISOU 3753  NZ  LYS A 489    15557   9822  13641  -1169  -1997   -198
ATOM   3754  N   PHE A 490      54.315  55.694   1.032  1.00102.80           N  
ANISOU 3754  N   PHE A 490    15995  10510  12554  -1809  -2381   -273
ATOM   3755  CA  PHE A 490      55.252  55.972   2.114  1.00103.76           C  
ANISOU 3755  CA  PHE A 490    16318  10575  12531  -1907  -2488   -266
ATOM   3756  C   PHE A 490      56.661  56.236   1.597  1.00104.13           C  
ANISOU 3756  C   PHE A 490    16270  10794  12500  -2138  -2693   -130
ATOM   3757  O   PHE A 490      57.404  57.006   2.215  1.00105.39           O  
ANISOU 3757  O   PHE A 490    16631  10861  12551  -2272  -2863    -77
ATOM   3758  CB  PHE A 490      55.292  54.841   3.132  1.00103.24           C  
ANISOU 3758  CB  PHE A 490    16260  10545  12421  -1815  -2358   -331
ATOM   3759  CG  PHE A 490      56.348  55.040   4.167  1.00104.35           C  
ANISOU 3759  CG  PHE A 490    16584  10656  12408  -1962  -2500   -285
ATOM   3760  CD1 PHE A 490      56.209  56.023   5.128  1.00105.97           C  
ANISOU 3760  CD1 PHE A 490    17129  10640  12495  -2004  -2554   -338
ATOM   3761  CD2 PHE A 490      57.504  54.282   4.151  1.00104.05           C  
ANISOU 3761  CD2 PHE A 490    16372  10801  12360  -2073  -2590   -188
ATOM   3762  CE1 PHE A 490      57.189  56.232   6.063  1.00107.17           C  
ANISOU 3762  CE1 PHE A 490    17468  10766  12485  -2173  -2704   -281
ATOM   3763  CE2 PHE A 490      58.486  54.483   5.089  1.00105.24           C  
ANISOU 3763  CE2 PHE A 490    16684  10915  12385  -2231  -2750   -110
ATOM   3764  CZ  PHE A 490      58.331  55.462   6.044  1.00106.76           C  
ANISOU 3764  CZ  PHE A 490    17240  10900  12424  -2293  -2814   -149
ATOM   3765  N   ASN A 491      57.059  55.607   0.488  1.00125.13           N  
ANISOU 3765  N   ASN A 491    18625  13709  15208  -2198  -2676    -80
ATOM   3766  CA  ASN A 491      58.367  55.918  -0.080  1.00125.43           C  
ANISOU 3766  CA  ASN A 491    18548  13933  15178  -2429  -2851     43
ATOM   3767  C   ASN A 491      58.445  57.368  -0.529  1.00124.23           C  
ANISOU 3767  C   ASN A 491    18537  13688  14977  -2591  -3058    151
ATOM   3768  O   ASN A 491      59.527  57.966  -0.504  1.00124.38           O  
ANISOU 3768  O   ASN A 491    18595  13760  14905  -2790  -3254    267
ATOM   3769  CB  ASN A 491      58.701  54.987  -1.248  1.00126.76           C  
ANISOU 3769  CB  ASN A 491    18354  14406  15403  -2471  -2755     35
ATOM   3770  CG  ASN A 491      59.008  53.570  -0.799  1.00129.58           C  
ANISOU 3770  CG  ASN A 491    18537  14856  15841  -2354  -2613    -49
ATOM   3771  OD1 ASN A 491      58.330  52.618  -1.188  1.00130.93           O  
ANISOU 3771  OD1 ASN A 491    18543  15093  16112  -2213  -2435   -148
ATOM   3772  ND2 ASN A 491      60.038  53.426   0.029  1.00130.36           N  
ANISOU 3772  ND2 ASN A 491    18670  14946  15913  -2423  -2716      8
ATOM   3773  N   ASN A 492      57.318  57.954  -0.939  1.00119.50           N  
ANISOU 3773  N   ASN A 492    18006  12937  14462  -2517  -3038    132
ATOM   3774  CA  ASN A 492      57.321  59.378  -1.263  1.00118.37           C  
ANISOU 3774  CA  ASN A 492    18009  12647  14321  -2665  -3267    243
ATOM   3775  C   ASN A 492      57.316  60.235   0.000  1.00118.03           C  
ANISOU 3775  C   ASN A 492    18310  12289  14246  -2626  -3358    193
ATOM   3776  O   ASN A 492      58.111  61.174   0.126  1.00117.66           O  
ANISOU 3776  O   ASN A 492    18398  12182  14124  -2811  -3594    298
ATOM   3777  CB  ASN A 492      56.123  59.723  -2.144  1.00117.95           C  
ANISOU 3777  CB  ASN A 492    17888  12512  14417  -2612  -3245    262
ATOM   3778  CG  ASN A 492      56.224  61.104  -2.755  1.00117.26           C  
ANISOU 3778  CG  ASN A 492    17873  12316  14363  -2814  -3526    425
ATOM   3779  OD1 ASN A 492      57.189  61.830  -2.522  1.00116.98           O  
ANISOU 3779  OD1 ASN A 492    17949  12269  14228  -2990  -3735    518
ATOM   3780  ND2 ASN A 492      55.225  61.473  -3.546  1.00117.15           N  
ANISOU 3780  ND2 ASN A 492    17790  12215  14506  -2804  -3556    483
ATOM   3781  N   PHE A 493      56.425  59.926   0.946  1.00114.94           N  
ANISOU 3781  N   PHE A 493    18068  11703  13902  -2403  -3170     26
ATOM   3782  CA  PHE A 493      56.350  60.685   2.191  1.00115.30           C  
ANISOU 3782  CA  PHE A 493    18454  11461  13895  -2374  -3213    -69
ATOM   3783  C   PHE A 493      57.617  60.570   3.034  1.00115.69           C  
ANISOU 3783  C   PHE A 493    18628  11580  13747  -2526  -3327    -21
ATOM   3784  O   PHE A 493      57.789  61.359   3.970  1.00116.02           O  
ANISOU 3784  O   PHE A 493    18973  11405  13705  -2579  -3423    -72
ATOM   3785  CB  PHE A 493      55.132  60.222   3.000  1.00115.95           C  
ANISOU 3785  CB  PHE A 493    18632  11381  14043  -2121  -2944   -270
ATOM   3786  CG  PHE A 493      54.921  60.982   4.281  1.00116.85           C  
ANISOU 3786  CG  PHE A 493    19099  11208  14092  -2092  -2935   -419
ATOM   3787  CD1 PHE A 493      54.391  62.261   4.265  1.00118.11           C  
ANISOU 3787  CD1 PHE A 493    19425  11068  14384  -2076  -3026   -476
ATOM   3788  CD2 PHE A 493      55.251  60.416   5.501  1.00117.15           C  
ANISOU 3788  CD2 PHE A 493    19299  11269  13942  -2098  -2842   -506
ATOM   3789  CE1 PHE A 493      54.197  62.962   5.443  1.00119.68           C  
ANISOU 3789  CE1 PHE A 493    19951  10999  14525  -2053  -2994   -657
ATOM   3790  CE2 PHE A 493      55.060  61.111   6.681  1.00118.53           C  
ANISOU 3790  CE2 PHE A 493    19816  11203  14018  -2105  -2818   -665
ATOM   3791  CZ  PHE A 493      54.533  62.385   6.652  1.00119.84           C  
ANISOU 3791  CZ  PHE A 493    20149  11073  14311  -2076  -2878   -761
ATOM   3792  N   ILE A 494      58.510  59.627   2.719  1.00121.84           N  
ANISOU 3792  N   ILE A 494    19178  12646  14470  -2606  -3327     72
ATOM   3793  CA  ILE A 494      59.702  59.410   3.538  1.00122.14           C  
ANISOU 3793  CA  ILE A 494    19299  12746  14363  -2750  -3444    143
ATOM   3794  C   ILE A 494      60.590  60.649   3.523  1.00121.78           C  
ANISOU 3794  C   ILE A 494    19417  12622  14230  -2981  -3737    278
ATOM   3795  O   ILE A 494      60.857  61.259   4.566  1.00121.87           O  
ANISOU 3795  O   ILE A 494    19739  12440  14127  -3054  -3846    257
ATOM   3796  CB  ILE A 494      60.468  58.166   3.056  1.00123.45           C  
ANISOU 3796  CB  ILE A 494    19124  13218  14563  -2778  -3389    216
ATOM   3797  N   LYS A 495      61.075  61.029   2.341  1.00135.63           N  
ANISOU 3797  N   LYS A 495    20971  14538  16023  -3123  -3876    424
ATOM   3798  CA  LYS A 495      61.863  62.250   2.180  1.00134.90           C  
ANISOU 3798  CA  LYS A 495    21009  14383  15863  -3358  -4178    582
ATOM   3799  C   LYS A 495      60.963  63.317   1.568  1.00133.29           C  
ANISOU 3799  C   LYS A 495    20889  13983  15773  -3338  -4257    574
ATOM   3800  O   LYS A 495      60.986  63.573   0.366  1.00132.63           O  
ANISOU 3800  O   LYS A 495    20599  14048  15746  -3446  -4344    699
ATOM   3801  CB  LYS A 495      63.094  61.997   1.314  1.00135.75           C  
ANISOU 3801  CB  LYS A 495    20829  14820  15931  -3572  -4301    774
ATOM   3802  CG  LYS A 495      64.107  61.040   1.910  1.00137.62           C  
ANISOU 3802  CG  LYS A 495    20956  15217  16117  -3611  -4271    811
ATOM   3803  CD  LYS A 495      65.339  60.929   1.025  1.00138.57           C  
ANISOU 3803  CD  LYS A 495    20774  15648  16226  -3828  -4389    990
ATOM   3804  CE  LYS A 495      66.331  59.912   1.565  1.00140.03           C  
ANISOU 3804  CE  LYS A 495    20794  15975  16436  -3849  -4356   1030
ATOM   3805  NZ  LYS A 495      67.525  59.784   0.683  1.00140.33           N1+
ANISOU 3805  NZ  LYS A 495    20501  16322  16496  -4049  -4437   1180
ATOM   3806  N   ASN A 496      60.150  63.951   2.418  1.00127.20           N  
ANISOU 3806  N   ASN A 496    20417  12868  15046  -3211  -4228    422
ATOM   3807  CA  ASN A 496      59.299  65.027   1.923  1.00126.96           C  
ANISOU 3807  CA  ASN A 496    20462  12592  15187  -3183  -4328    414
ATOM   3808  C   ASN A 496      59.216  66.188   2.914  1.00128.25           C  
ANISOU 3808  C   ASN A 496    21003  12375  15350  -3200  -4469    320
ATOM   3809  O   ASN A 496      58.338  67.048   2.777  1.00130.32           O  
ANISOU 3809  O   ASN A 496    21360  12347  15810  -3117  -4511    248
ATOM   3810  CB  ASN A 496      57.897  64.492   1.592  1.00127.37           C  
ANISOU 3810  CB  ASN A 496    20386  12592  15419  -2929  -4063    273
ATOM   3811  CG  ASN A 496      57.133  65.395   0.634  1.00127.53           C  
ANISOU 3811  CG  ASN A 496    20339  12454  15663  -2946  -4200    354
ATOM   3812  OD1 ASN A 496      57.639  66.430   0.200  1.00126.74           O  
ANISOU 3812  OD1 ASN A 496    20288  12283  15585  -3152  -4501    517
ATOM   3813  ND2 ASN A 496      55.913  64.997   0.292  1.00129.47           N  
ANISOU 3813  ND2 ASN A 496    20461  12641  16089  -2744  -4001    264
ATOM   3814  N   GLN A 497      60.150  66.212   3.865  1.00129.04           N  
ANISOU 3814  N   GLN A 497    21319  12458  15251  -3313  -4550    314
ATOM   3815  CA  GLN A 497      60.245  67.260   4.879  1.00129.55           C  
ANISOU 3815  CA  GLN A 497    21762  12180  15281  -3382  -4714    227
ATOM   3816  C   GLN A 497      61.714  67.648   5.089  1.00129.29           C  
ANISOU 3816  C   GLN A 497    21891  12234  15000  -3615  -4903    346
ATOM   3817  O   GLN A 497      62.513  67.589   4.155  1.00131.21           O  
ANISOU 3817  O   GLN A 497    22454  12227  15172  -3735  -5090    313
ATOM   3818  CB  GLN A 497      59.626  66.793   6.197  1.00129.83           C  
ANISOU 3818  CB  GLN A 497    22027  11940  15361  -3148  -4444    -92
ATOM   3819  CG  GLN A 497      59.820  65.313   6.483  1.00129.63           C  
ANISOU 3819  CG  GLN A 497    22079  12048  15126  -3089  -4205   -216
ATOM   3820  CD  GLN A 497      58.525  64.529   6.397  1.00129.31           C  
ANISOU 3820  CD  GLN A 497    21742  12228  15160  -2887  -3913   -254
ATOM   3821  OE1 GLN A 497      57.917  64.426   5.332  1.00128.69           O  
ANISOU 3821  OE1 GLN A 497    21369  12281  15245  -2833  -3907   -148
ATOM   3822  NE2 GLN A 497      58.097  63.969   7.523  1.00129.55           N  
ANISOU 3822  NE2 GLN A 497    21859  12302  15062  -2797  -3681   -400
ATOM   3823  N   ASP A 498      62.066  68.041   6.312  1.00 30.00           N  
ATOM   3824  CA  ASP A 498      63.442  68.428   6.637  1.00 30.00           C  
ATOM   3825  C   ASP A 498      64.248  67.203   7.064  1.00 30.00           C  
ATOM   3826  O   ASP A 498      63.751  66.366   7.817  1.00 30.00           O  
ATOM   3827  CB  ASP A 498      63.457  69.484   7.743  1.00 20.00           C  
ATOM   3828  CG  ASP A 498      63.580  70.894   7.201  1.00 20.00           C  
ATOM   3829  OD1 ASP A 498      63.958  71.048   6.020  1.00 20.00           O  
ATOM   3830  OD2 ASP A 498      63.298  71.849   7.955  1.00 20.00           O1-
ATOM   3831  N   THR A 499      65.487  67.087   6.580  1.00120.63           N  
ANISOU 3831  N   THR A 499    21105  11559  13169  -4434  -5532    925
ATOM   3832  CA  THR A 499      66.328  65.931   6.905  1.00118.75           C  
ANISOU 3832  CA  THR A 499    20419  11680  13022  -4448  -5501   1113
ATOM   3833  C   THR A 499      65.511  64.707   6.522  1.00116.52           C  
ANISOU 3833  C   THR A 499    19872  11523  12878  -4171  -5156    950
ATOM   3834  O   THR A 499      64.538  64.845   5.780  1.00115.89           O  
ANISOU 3834  O   THR A 499    19680  11422  12931  -4051  -5076    883
ATOM   3835  CB  THR A 499      66.673  65.876   8.402  1.00118.94           C  
ANISOU 3835  CB  THR A 499    20372  11872  12948  -4614  -5600   1293
ATOM   3836  OG1 THR A 499      65.474  65.691   9.165  1.00118.79           O  
ANISOU 3836  OG1 THR A 499    20505  11781  12848  -4515  -5414   1140
ATOM   3837  CG2 THR A 499      67.353  67.165   8.839  1.00121.20           C  
ANISOU 3837  CG2 THR A 499    20903  12052  13097  -4914  -5966   1493
ATOM   3838  N   VAL A 500      65.848  63.512   6.997  1.00123.42           N  
ANISOU 3838  N   VAL A 500    20644  12519  13731  -4089  -4979    907
ATOM   3839  CA  VAL A 500      64.959  62.423   6.591  1.00121.36           C  
ANISOU 3839  CA  VAL A 500    20131  12381  13598  -3837  -4662    764
ATOM   3840  C   VAL A 500      64.367  61.739   7.822  1.00121.40           C  
ANISOU 3840  C   VAL A 500    20330  12278  13519  -3725  -4479    600
ATOM   3841  O   VAL A 500      63.208  61.321   7.822  1.00120.44           O  
ANISOU 3841  O   VAL A 500    20190  12109  13462  -3500  -4220    409
ATOM   3842  CB  VAL A 500      65.698  61.396   5.710  1.00119.94           C  
ANISOU 3842  CB  VAL A 500    19498  12537  13535  -3854  -4624    904
ATOM   3843  CG1 VAL A 500      64.774  60.247   5.337  1.00117.97           C  
ANISOU 3843  CG1 VAL A 500    19010  12395  13417  -3600  -4310    747
ATOM   3844  CG2 VAL A 500      66.272  62.065   4.469  1.00120.17           C  
ANISOU 3844  CG2 VAL A 500    19329  12718  13610  -3999  -4785   1060
ATOM   3845  N   SER A 506      65.301  50.856   6.831  1.00145.23           N  
ANISOU 3845  N   SER A 506    20803  16471  17908  -2953  -3584    690
ATOM   3846  CA  SER A 506      65.053  50.493   5.440  1.00143.97           C  
ANISOU 3846  CA  SER A 506    20315  16477  17912  -2805  -3393    553
ATOM   3847  C   SER A 506      64.264  49.188   5.381  1.00142.94           C  
ANISOU 3847  C   SER A 506    19989  16355  17968  -2595  -3206    432
ATOM   3848  O   SER A 506      64.777  48.135   5.757  1.00143.43           O  
ANISOU 3848  O   SER A 506    19830  16416  18252  -2590  -3264    498
ATOM   3849  CB  SER A 506      66.374  50.372   4.685  1.00144.88           C  
ANISOU 3849  CB  SER A 506    20084  16760  18203  -2922  -3483    642
ATOM   3850  OG  SER A 506      67.150  49.296   5.181  1.00145.82           O  
ANISOU 3850  OG  SER A 506    19952  16871  18581  -2940  -3572    740
ATOM   3851  N   PHE A 507      63.024  49.252   4.898  1.00129.76           N  
ANISOU 3851  N   PHE A 507    18386  14681  16234  -2428  -3001    269
ATOM   3852  CA  PHE A 507      62.068  48.189   5.184  1.00130.30           C  
ANISOU 3852  CA  PHE A 507    18395  14705  16407  -2245  -2852    179
ATOM   3853  C   PHE A 507      60.837  48.372   4.306  1.00130.39           C  
ANISOU 3853  C   PHE A 507    18415  14747  16378  -2079  -2633     14
ATOM   3854  O   PHE A 507      60.654  49.411   3.667  1.00130.12           O  
ANISOU 3854  O   PHE A 507    18489  14735  16216  -2119  -2620    -15
ATOM   3855  CB  PHE A 507      61.687  48.221   6.662  1.00130.80           C  
ANISOU 3855  CB  PHE A 507    18780  14604  16312  -2293  -2929    251
ATOM   3856  CG  PHE A 507      60.758  49.342   7.010  1.00130.99           C  
ANISOU 3856  CG  PHE A 507    19190  14517  16064  -2280  -2858    172
ATOM   3857  CD1 PHE A 507      61.184  50.654   6.956  1.00132.26           C  
ANISOU 3857  CD1 PHE A 507    19566  14634  16053  -2417  -2970    206
ATOM   3858  CD2 PHE A 507      59.482  49.081   7.463  1.00129.91           C  
ANISOU 3858  CD2 PHE A 507    19195  14304  15861  -2139  -2689     67
ATOM   3859  CE1 PHE A 507      60.331  51.687   7.280  1.00132.04           C  
ANISOU 3859  CE1 PHE A 507    19875  14469  15827  -2394  -2907    112
ATOM   3860  CE2 PHE A 507      58.640  50.111   7.807  1.00129.72           C  
ANISOU 3860  CE2 PHE A 507    19497  14159  15630  -2117  -2607    -28
ATOM   3861  CZ  PHE A 507      59.061  51.413   7.715  1.00130.51           C  
ANISOU 3861  CZ  PHE A 507    19801  14196  15592  -2238  -2715    -15
ATOM   3862  N   GLN A 508      59.982  47.345   4.299  1.00140.01           N  
ANISOU 3862  N   GLN A 508    19519  15958  17722  -1906  -2485    -73
ATOM   3863  CA  GLN A 508      58.730  47.341   3.551  1.00141.19           C  
ANISOU 3863  CA  GLN A 508    19660  16124  17862  -1744  -2285   -208
ATOM   3864  C   GLN A 508      57.679  46.568   4.341  1.00141.54           C  
ANISOU 3864  C   GLN A 508    19784  16068  17928  -1600  -2187   -238
ATOM   3865  O   GLN A 508      58.003  45.582   5.011  1.00141.79           O  
ANISOU 3865  O   GLN A 508    19712  16080  18081  -1601  -2251   -178
ATOM   3866  CB  GLN A 508      58.916  46.729   2.150  1.00142.62           C  
ANISOU 3866  CB  GLN A 508    19483  16484  18221  -1698  -2182   -303
ATOM   3867  CG  GLN A 508      59.788  47.569   1.213  1.00143.48           C  
ANISOU 3867  CG  GLN A 508    19511  16736  18270  -1858  -2244   -285
ATOM   3868  CD  GLN A 508      59.998  46.927  -0.147  1.00144.51           C  
ANISOU 3868  CD  GLN A 508    19289  17075  18542  -1848  -2118   -405
ATOM   3869  OE1 GLN A 508      59.552  45.805  -0.396  1.00145.66           O  
ANISOU 3869  OE1 GLN A 508    19243  17242  18858  -1711  -1991   -512
ATOM   3870  NE2 GLN A 508      60.683  47.639  -1.037  1.00143.84           N  
ANISOU 3870  NE2 GLN A 508    19123  17153  18379  -2012  -2153   -393
ATOM   3871  N   ILE A 509      56.420  47.011   4.255  1.00119.62           N  
ANISOU 3871  N   ILE A 509    17173  13224  15052  -1487  -2045   -316
ATOM   3872  CA  ILE A 509      55.350  46.517   5.116  1.00119.98           C  
ANISOU 3872  CA  ILE A 509    17344  13175  15068  -1372  -1942   -339
ATOM   3873  C   ILE A 509      54.177  46.014   4.283  1.00120.21           C  
ANISOU 3873  C   ILE A 509    17227  13235  15211  -1188  -1758   -433
ATOM   3874  O   ILE A 509      53.866  46.554   3.217  1.00119.29           O  
ANISOU 3874  O   ILE A 509    17057  13160  15107  -1162  -1698   -485
ATOM   3875  CB  ILE A 509      54.864  47.610   6.101  1.00119.82           C  
ANISOU 3875  CB  ILE A 509    17707  13012  14809  -1419  -1933   -349
ATOM   3876  CG1 ILE A 509      55.952  47.972   7.100  1.00120.36           C  
ANISOU 3876  CG1 ILE A 509    17951  13041  14739  -1624  -2126   -246
ATOM   3877  CG2 ILE A 509      53.620  47.180   6.864  1.00120.97           C  
ANISOU 3877  CG2 ILE A 509    17965  13088  14910  -1299  -1777   -401
ATOM   3878  CD1 ILE A 509      55.537  49.105   7.983  1.00120.17           C  
ANISOU 3878  CD1 ILE A 509    18311  12878  14471  -1688  -2109   -294
ATOM   3879  N   TYR A 510      53.527  44.961   4.786  1.00108.38           N  
ANISOU 3879  N   TYR A 510    15665  11719  13796  -1084  -1690   -431
ATOM   3880  CA  TYR A 510      52.220  44.519   4.318  1.00108.05           C  
ANISOU 3880  CA  TYR A 510    15552  11672  13830   -912  -1519   -497
ATOM   3881  C   TYR A 510      51.141  44.986   5.292  1.00109.36           C  
ANISOU 3881  C   TYR A 510    15985  11722  13846   -856  -1414   -508
ATOM   3882  O   TYR A 510      51.314  44.897   6.511  1.00110.62           O  
ANISOU 3882  O   TYR A 510    16307  11839  13885   -934  -1461   -461
ATOM   3883  CB  TYR A 510      52.174  42.996   4.187  1.00107.97           C  
ANISOU 3883  CB  TYR A 510    15274  11718  14032   -834  -1515   -488
ATOM   3884  CG  TYR A 510      53.062  42.432   3.100  1.00107.13           C  
ANISOU 3884  CG  TYR A 510    14866  11725  14115   -857  -1561   -535
ATOM   3885  CD1 TYR A 510      52.655  42.438   1.774  1.00106.95           C  
ANISOU 3885  CD1 TYR A 510    14696  11788  14152   -802  -1453   -631
ATOM   3886  CD2 TYR A 510      54.303  41.884   3.402  1.00106.53           C  
ANISOU 3886  CD2 TYR A 510    14641  11672  14164   -949  -1707   -486
ATOM   3887  CE1 TYR A 510      53.458  41.920   0.776  1.00106.16           C  
ANISOU 3887  CE1 TYR A 510    14322  11813  14200   -843  -1462   -710
ATOM   3888  CE2 TYR A 510      55.115  41.364   2.410  1.00105.69           C  
ANISOU 3888  CE2 TYR A 510    14233  11669  14254   -963  -1716   -563
ATOM   3889  CZ  TYR A 510      54.686  41.385   1.098  1.00105.78           C  
ANISOU 3889  CZ  TYR A 510    14116  11785  14291   -912  -1578   -692
ATOM   3890  OH  TYR A 510      55.486  40.871   0.103  1.00105.16           O  
ANISOU 3890  OH  TYR A 510    13741  11832  14382   -946  -1555   -804
ATOM   3891  N   VAL A 511      50.025  45.477   4.751  1.00111.23           N  
ANISOU 3891  N   VAL A 511    16255  11911  14095   -737  -1270   -571
ATOM   3892  CA  VAL A 511      48.910  45.975   5.551  1.00112.01           C  
ANISOU 3892  CA  VAL A 511    16570  11895  14095   -661  -1130   -614
ATOM   3893  C   VAL A 511      47.637  45.259   5.115  1.00112.58           C  
ANISOU 3893  C   VAL A 511    16490  11976  14308   -489   -979   -625
ATOM   3894  O   VAL A 511      47.411  45.051   3.918  1.00111.92           O  
ANISOU 3894  O   VAL A 511    16217  11941  14367   -432   -969   -625
ATOM   3895  CB  VAL A 511      48.760  47.505   5.429  1.00110.46           C  
ANISOU 3895  CB  VAL A 511    16579  11576  13814   -685  -1115   -675
ATOM   3896  CG1 VAL A 511      47.540  47.984   6.188  1.00110.92           C  
ANISOU 3896  CG1 VAL A 511    16819  11503  13823   -581   -935   -758
ATOM   3897  CG2 VAL A 511      50.005  48.191   5.957  1.00109.84           C  
ANISOU 3897  CG2 VAL A 511    16670  11482  13581   -868  -1279   -652
ATOM   3898  N   LEU A 512      46.803  44.888   6.091  1.00116.52           N  
ANISOU 3898  N   LEU A 512    17079  12441  14753   -429   -864   -629
ATOM   3899  CA  LEU A 512      45.768  43.880   5.908  1.00116.60           C  
ANISOU 3899  CA  LEU A 512    16922  12486  14894   -294   -758   -599
ATOM   3900  C   LEU A 512      44.448  44.398   6.468  1.00117.30           C  
ANISOU 3900  C   LEU A 512    17146  12484  14938   -189   -557   -653
ATOM   3901  O   LEU A 512      44.427  45.111   7.474  1.00118.32           O  
ANISOU 3901  O   LEU A 512    17509  12552  14895   -247   -494   -718
ATOM   3902  CB  LEU A 512      46.158  42.574   6.621  1.00116.82           C  
ANISOU 3902  CB  LEU A 512    16861  12596  14930   -349   -845   -513
ATOM   3903  CG  LEU A 512      47.414  41.806   6.188  1.00115.95           C  
ANISOU 3903  CG  LEU A 512    16560  12557  14938   -431  -1037   -462
ATOM   3904  CD1 LEU A 512      48.662  42.516   6.656  1.00116.58           C  
ANISOU 3904  CD1 LEU A 512    16784  12627  14884   -599  -1174   -452
ATOM   3905  CD2 LEU A 512      47.425  40.413   6.758  1.00116.46           C  
ANISOU 3905  CD2 LEU A 512    16487  12662  15102   -441  -1116   -366
ATOM   3906  N   GLN A 513      43.338  44.010   5.831  1.00112.71           N  
ANISOU 3906  N   GLN A 513    16410  11895  14519    -42   -448   -632
ATOM   3907  CA  GLN A 513      42.035  44.589   6.161  1.00113.47           C  
ANISOU 3907  CA  GLN A 513    16584  11889  14639     78   -247   -685
ATOM   3908  C   GLN A 513      41.496  44.127   7.521  1.00115.32           C  
ANISOU 3908  C   GLN A 513    16920  12161  14735     70   -116   -697
ATOM   3909  O   GLN A 513      40.424  44.586   7.937  1.00117.38           O  
ANISOU 3909  O   GLN A 513    17241  12352  15006    164     86   -765
ATOM   3910  CB  GLN A 513      41.041  44.285   5.031  1.00113.07           C  
ANISOU 3910  CB  GLN A 513    16322  11822  14819    215   -197   -625
ATOM   3911  CG  GLN A 513      39.711  45.041   5.096  1.00113.79           C  
ANISOU 3911  CG  GLN A 513    16442  11774  15020    350    -11   -664
ATOM   3912  CD  GLN A 513      38.856  44.848   3.854  1.00112.50           C  
ANISOU 3912  CD  GLN A 513    16070  11582  15095    447    -16   -569
ATOM   3913  OE1 GLN A 513      39.253  44.163   2.910  1.00110.68           O  
ANISOU 3913  OE1 GLN A 513    15690  11447  14918    401   -147   -495
ATOM   3914  NE2 GLN A 513      37.670  45.446   3.855  1.00113.09           N  
ANISOU 3914  NE2 GLN A 513    16127  11519  15323    569    129   -574
ATOM   3915  N   ALA A 514      42.205  43.241   8.221  1.00112.00           N  
ANISOU 3915  N   ALA A 514    16507  11852  14196    -54   -228   -627
ATOM   3916  CA  ALA A 514      42.019  42.900   9.633  1.00113.88           C  
ANISOU 3916  CA  ALA A 514    16888  12154  14229   -154   -160   -620
ATOM   3917  C   ALA A 514      40.709  42.185   9.944  1.00115.76           C  
ANISOU 3917  C   ALA A 514    17024  12444  14517    -54      7   -575
ATOM   3918  O   ALA A 514      40.473  41.849  11.112  1.00117.44           O  
ANISOU 3918  O   ALA A 514    17342  12740  14540   -160     74   -559
ATOM   3919  CB  ALA A 514      42.118  44.129  10.547  1.00114.41           C  
ANISOU 3919  CB  ALA A 514    17253  12150  14069   -241    -48   -769
ATOM   3920  N   GLY A 515      39.851  41.944   8.960  1.00115.19           N  
ANISOU 3920  N   GLY A 515    16753  12336  14677    120     68   -542
ATOM   3921  CA  GLY A 515      38.653  41.163   9.193  1.00116.00           C  
ANISOU 3921  CA  GLY A 515    16732  12496  14849    208    197   -466
ATOM   3922  C   GLY A 515      38.617  39.950   8.291  1.00113.80           C  
ANISOU 3922  C   GLY A 515    16197  12264  14777    264     46   -323
ATOM   3923  O   GLY A 515      37.966  38.945   8.590  1.00113.88           O  
ANISOU 3923  O   GLY A 515    16092  12348  14828    281     57   -210
ATOM   3924  N   ALA A 516      39.334  40.046   7.175  1.00111.05           N  
ANISOU 3924  N   ALA A 516    15761  11877  14555    277    -96   -334
ATOM   3925  CA  ALA A 516      39.425  38.986   6.187  1.00109.03           C  
ANISOU 3925  CA  ALA A 516    15272  11657  14497    318   -231   -248
ATOM   3926  C   ALA A 516      40.618  38.068   6.418  1.00108.30           C  
ANISOU 3926  C   ALA A 516    15117  11627  14404    200   -442   -203
ATOM   3927  O   ALA A 516      40.890  37.201   5.581  1.00106.57           O  
ANISOU 3927  O   ALA A 516    14701  11425  14365    226   -560   -174
ATOM   3928  CB  ALA A 516      39.500  39.592   4.784  1.00107.57           C  
ANISOU 3928  CB  ALA A 516    15014  11416  14444    373   -251   -300
ATOM   3929  N   TRP A 517      41.324  38.232   7.529  1.00115.01           N  
ANISOU 3929  N   TRP A 517    16123  12503  15072     62   -496   -198
ATOM   3930  CA  TRP A 517      42.565  37.503   7.787  1.00114.40           C  
ANISOU 3930  CA  TRP A 517    15984  12457  15024    -67   -722   -139
ATOM   3931  C   TRP A 517      42.459  36.708   9.078  1.00115.24           C  
ANISOU 3931  C   TRP A 517    16130  12623  15034   -188   -793     -4
ATOM   3932  O   TRP A 517      42.370  37.307  10.167  1.00117.43           O  
ANISOU 3932  O   TRP A 517    16631  12931  15058   -302   -716    -12
ATOM   3933  CB  TRP A 517      43.737  38.479   7.855  1.00114.48           C  
ANISOU 3933  CB  TRP A 517    16141  12443  14914   -175   -788   -218
ATOM   3934  CG  TRP A 517      44.092  39.055   6.526  1.00113.14           C  
ANISOU 3934  CG  TRP A 517    15890  12243  14854   -106   -784   -315
ATOM   3935  CD1 TRP A 517      43.585  40.188   5.962  1.00112.77           C  
ANISOU 3935  CD1 TRP A 517    15935  12144  14767    -37   -651   -401
ATOM   3936  CD2 TRP A 517      45.060  38.544   5.603  1.00112.02           C  
ANISOU 3936  CD2 TRP A 517    15552  12126  14883   -125   -926   -334
ATOM   3937  NE1 TRP A 517      44.165  40.406   4.736  1.00111.75           N  
ANISOU 3937  NE1 TRP A 517    15689  12026  14743    -36   -716   -450
ATOM   3938  CE2 TRP A 517      45.080  39.415   4.496  1.00111.34           C  
ANISOU 3938  CE2 TRP A 517    15462  12033  14807    -88   -865   -427
ATOM   3939  CE3 TRP A 517      45.922  37.443   5.611  1.00111.21           C  
ANISOU 3939  CE3 TRP A 517    15264  12047  14945   -176  -1100   -287
ATOM   3940  CZ2 TRP A 517      45.919  39.213   3.403  1.00110.61           C  
ANISOU 3940  CZ2 TRP A 517    15198  11992  14838   -118   -946   -486
ATOM   3941  CZ3 TRP A 517      46.750  37.241   4.523  1.00110.02           C  
ANISOU 3941  CZ3 TRP A 517    14927  11921  14956   -174  -1166   -369
ATOM   3942  CH2 TRP A 517      46.741  38.120   3.433  1.00109.76           C  
ANISOU 3942  CH2 TRP A 517    14905  11915  14883   -153  -1077   -473
ATOM   3943  N   PRO A 518      42.467  35.374   9.017  1.00125.42           N  
ANISOU 3943  N   PRO A 518    17214  13930  16511   -190   -947    121
ATOM   3944  CA  PRO A 518      42.343  34.579  10.248  1.00126.39           C  
ANISOU 3944  CA  PRO A 518    17362  14113  16547   -339  -1052    289
ATOM   3945  C   PRO A 518      43.593  34.582  11.111  1.00127.01           C  
ANISOU 3945  C   PRO A 518    17536  14197  16526   -561  -1258    363
ATOM   3946  O   PRO A 518      43.511  34.166  12.275  1.00128.18           O  
ANISOU 3946  O   PRO A 518    17766  14411  16524   -743  -1342    510
ATOM   3947  CB  PRO A 518      42.038  33.171   9.723  1.00124.96           C  
ANISOU 3947  CB  PRO A 518    16904  13911  16662   -261  -1191    400
ATOM   3948  CG  PRO A 518      42.669  33.142   8.367  1.00123.22           C  
ANISOU 3948  CG  PRO A 518    16520  13618  16681   -142  -1238    274
ATOM   3949  CD  PRO A 518      42.528  34.532   7.810  1.00123.51           C  
ANISOU 3949  CD  PRO A 518    16709  13650  16570    -70  -1033    110
ATOM   3950  N   LEU A 519      44.734  35.025  10.585  1.00140.12           N  
ANISOU 3950  N   LEU A 519    19181  15799  18258   -574  -1353    283
ATOM   3951  CA  LEU A 519      45.968  35.027  11.359  1.00141.11           C  
ANISOU 3951  CA  LEU A 519    19378  15917  18322   -790  -1572    376
ATOM   3952  C   LEU A 519      45.804  35.836  12.640  1.00143.91           C  
ANISOU 3952  C   LEU A 519    20055  16337  18287   -981  -1493    394
ATOM   3953  O   LEU A 519      45.184  36.903  12.650  1.00145.69           O  
ANISOU 3953  O   LEU A 519    20475  16575  18305   -918  -1247    242
ATOM   3954  CB  LEU A 519      47.122  35.588  10.526  1.00139.43           C  
ANISOU 3954  CB  LEU A 519    19111  15645  18222   -762  -1636    266
ATOM   3955  CG  LEU A 519      47.629  34.715   9.378  1.00137.35           C  
ANISOU 3955  CG  LEU A 519    18519  15329  18340   -638  -1745    233
ATOM   3956  CD1 LEU A 519      48.642  35.473   8.540  1.00137.54           C  
ANISOU 3956  CD1 LEU A 519    18515  15336  18407   -623  -1744    100
ATOM   3957  CD2 LEU A 519      48.240  33.435   9.924  1.00135.34           C  
ANISOU 3957  CD2 LEU A 519    18070  15027  18325   -746  -2025    414
ATOM   3958  N   THR A 520      46.361  35.312  13.726  1.00166.36           N  
ANISOU 3958  N   THR A 520    22949  19215  21045  -1231  -1710    580
ATOM   3959  CA  THR A 520      46.289  35.937  15.036  1.00166.62           C  
ANISOU 3959  CA  THR A 520    23295  19332  20680  -1475  -1664    611
ATOM   3960  C   THR A 520      47.667  36.426  15.461  1.00166.52           C  
ANISOU 3960  C   THR A 520    23410  19279  20581  -1688  -1873    661
ATOM   3961  O   THR A 520      48.682  36.163  14.810  1.00165.41           O  
ANISOU 3961  O   THR A 520    23081  19050  20716  -1650  -2067    699
ATOM   3962  CB  THR A 520      45.720  34.963  16.075  1.00166.51           C  
ANISOU 3962  CB  THR A 520    23273  19426  20568  -1663  -1756    820
ATOM   3963  OG1 THR A 520      46.568  33.812  16.174  1.00164.96           O  
ANISOU 3963  OG1 THR A 520    22855  19175  20646  -1783  -2122   1058
ATOM   3964  CG2 THR A 520      44.318  34.525  15.678  1.00166.70           C  
ANISOU 3964  CG2 THR A 520    23175  19497  20667  -1458  -1543    781
ATOM   3965  N   GLN A 521      47.686  37.148  16.581  1.00185.55           N  
ANISOU 3965  N   GLN A 521    26142  21759  22601  -1927  -1823    655
ATOM   3966  CA  GLN A 521      48.907  37.797  17.045  1.00184.95           C  
ANISOU 3966  CA  GLN A 521    26243  21645  22384  -2149  -2001    694
ATOM   3967  C   GLN A 521      49.862  36.826  17.731  1.00183.32           C  
ANISOU 3967  C   GLN A 521    25932  21438  22285  -2425  -2390    997
ATOM   3968  O   GLN A 521      51.082  37.012  17.649  1.00181.23           O  
ANISOU 3968  O   GLN A 521    25640  21093  22124  -2527  -2615   1075
ATOM   3969  CB  GLN A 521      48.543  38.953  17.981  1.00186.15           C  
ANISOU 3969  CB  GLN A 521    26795  21862  22070  -2315  -1797    550
ATOM   3970  CG  GLN A 521      47.931  38.520  19.305  1.00186.97           C  
ANISOU 3970  CG  GLN A 521    27064  22121  21856  -2590  -1778    662
ATOM   3971  CD  GLN A 521      46.446  38.208  19.203  1.00188.79           C  
ANISOU 3971  CD  GLN A 521    27222  22436  22074  -2408  -1486    567
ATOM   3972  OE1 GLN A 521      45.907  38.031  18.109  1.00188.50           O  
ANISOU 3972  OE1 GLN A 521    26959  22332  22332  -2081  -1366    481
ATOM   3973  NE2 GLN A 521      45.781  38.125  20.349  1.00190.41           N  
ANISOU 3973  NE2 GLN A 521    27615  22803  21930  -2641  -1375    592
ATOM   3974  N   ALA A 522      49.335  35.789  18.395  1.00192.29           N  
ANISOU 3974  N   ALA A 522    26990  22652  23420  -2556  -2492   1190
ATOM   3975  CA  ALA A 522      50.117  34.794  19.126  1.00190.91           C  
ANISOU 3975  CA  ALA A 522    26703  22466  23368  -2846  -2894   1520
ATOM   3976  C   ALA A 522      51.129  35.458  20.055  1.00191.39           C  
ANISOU 3976  C   ALA A 522    27032  22537  23150  -3199  -3080   1625
ATOM   3977  O   ALA A 522      52.341  35.349  19.830  1.00190.15           O  
ANISOU 3977  O   ALA A 522    26744  22262  23241  -3258  -3356   1748
ATOM   3978  CB  ALA A 522      50.828  33.849  18.155  1.00187.26           C  
ANISOU 3978  CB  ALA A 522    25829  21847  23474  -2661  -3130   1610
ATOM   3979  N   PRO A 523      50.676  36.149  21.114  1.00198.93           N  
ANISOU 3979  N   PRO A 523    28359  23631  23592  -3452  -2936   1577
ATOM   3980  CA  PRO A 523      51.581  36.918  21.974  1.00199.70           C  
ANISOU 3980  CA  PRO A 523    28762  23741  23372  -3798  -3084   1640
ATOM   3981  C   PRO A 523      52.367  36.040  22.944  1.00198.73           C  
ANISOU 3981  C   PRO A 523    28600  23638  23269  -4217  -3532   2040
ATOM   3982  O   PRO A 523      51.796  35.109  23.512  1.00196.62           O  
ANISOU 3982  O   PRO A 523    28258  23470  22979  -4368  -3627   2231
ATOM   3983  CB  PRO A 523      50.629  37.845  22.730  1.00200.45           C  
ANISOU 3983  CB  PRO A 523    29248  23987  22927  -3906  -2728   1408
ATOM   3984  CG  PRO A 523      49.365  37.062  22.823  1.00199.85           C  
ANISOU 3984  CG  PRO A 523    29048  24034  22853  -3814  -2558   1416
ATOM   3985  CD  PRO A 523      49.275  36.248  21.559  1.00199.30           C  
ANISOU 3985  CD  PRO A 523    28558  23838  23329  -3434  -2611   1444
ATOM   3986  N   PRO A 530      61.380  42.640  22.762  1.00236.71           N  
ANISOU 3986  N   PRO A 530    34395  27746  27800  -5207  -4801   2288
ATOM   3987  CA  PRO A 530      59.956  42.956  22.761  1.00235.81           C  
ANISOU 3987  CA  PRO A 530    34478  27725  27396  -5019  -4380   1958
ATOM   3988  C   PRO A 530      59.736  44.464  22.757  1.00235.93           C  
ANISOU 3988  C   PRO A 530    34886  27722  27033  -4994  -4136   1652
ATOM   3989  O   PRO A 530      58.680  44.945  22.346  1.00234.58           O  
ANISOU 3989  O   PRO A 530    34799  27572  26758  -4722  -3760   1327
ATOM   3990  CB  PRO A 530      59.270  42.322  23.955  1.00238.21           C  
ANISOU 3990  CB  PRO A 530    34957  28156  27394  -5318  -4407   2077
ATOM   3991  N   GLN A 531      60.733  45.204  23.229  1.00223.74           N  
ANISOU 3991  N   GLN A 531    33579  26124  25309  -5287  -4369   1769
ATOM   3992  CA  GLN A 531      60.715  46.654  23.147  1.00223.97           C  
ANISOU 3992  CA  GLN A 531    33954  26095  25048  -5267  -4201   1504
ATOM   3993  C   GLN A 531      61.330  47.106  21.826  1.00221.38           C  
ANISOU 3993  C   GLN A 531    33365  25666  25084  -4962  -4209   1449
ATOM   3994  O   GLN A 531      62.032  46.350  21.150  1.00220.07           O  
ANISOU 3994  O   GLN A 531    32789  25479  25350  -4855  -4396   1649
ATOM   3995  CB  GLN A 531      61.466  47.277  24.325  1.00227.44           C  
ANISOU 3995  CB  GLN A 531    34809  26526  25081  -5761  -4454   1651
ATOM   3996  N   GLU A 532      61.045  48.354  21.461  1.00213.56           N  
ANISOU 3996  N   GLU A 532    32608  24613  23922  -4831  -3999   1167
ATOM   3997  CA  GLU A 532      61.524  48.896  20.197  1.00211.30           C  
ANISOU 3997  CA  GLU A 532    32107  24252  23926  -4566  -3989   1101
ATOM   3998  C   GLU A 532      63.046  48.832  20.118  1.00211.97           C  
ANISOU 3998  C   GLU A 532    32047  24299  24194  -4771  -4378   1415
ATOM   3999  O   GLU A 532      63.752  48.966  21.122  1.00214.58           O  
ANISOU 3999  O   GLU A 532    32612  24612  24306  -5154  -4648   1623
ATOM   4000  CB  GLU A 532      61.049  50.339  20.023  1.00211.44           C  
ANISOU 4000  CB  GLU A 532    32454  24185  23700  -4477  -3771    791
ATOM   4001  N   LEU A 533      63.548  48.630  18.906  1.00201.82           N  
ANISOU 4001  N   LEU A 533    30366  23006  23309  -4526  -4400   1447
ATOM   4002  CA  LEU A 533      64.969  48.454  18.642  1.00202.30           C  
ANISOU 4002  CA  LEU A 533    30186  23042  23636  -4660  -4730   1730
ATOM   4003  C   LEU A 533      65.467  49.582  17.739  1.00201.36           C  
ANISOU 4003  C   LEU A 533    30078  22888  23542  -4559  -4707   1629
ATOM   4004  O   LEU A 533      64.763  50.564  17.487  1.00200.75           O  
ANISOU 4004  O   LEU A 533    30249  22778  23248  -4438  -4487   1367
ATOM   4005  CB  LEU A 533      65.231  47.077  18.027  1.00201.09           C  
ANISOU 4005  CB  LEU A 533    29501  22928  23976  -4491  -4790   1869
ATOM   4006  N   GLU A 534      66.685  49.449  17.229  1.00192.06           N  
ANISOU 4006  N   GLU A 534    28616  21710  22647  -4624  -4951   1850
ATOM   4007  CA  GLU A 534      67.200  50.490  16.353  1.00191.37           C  
ANISOU 4007  CA  GLU A 534    28487  21618  22608  -4565  -4968   1806
ATOM   4008  C   GLU A 534      66.081  51.500  16.101  1.00188.71           C  
ANISOU 4008  C   GLU A 534    27978  21336  22389  -4196  -4639   1519
ATOM   4009  O   GLU A 534      66.328  52.625  15.668  1.00188.19           O  
ANISOU 4009  O   GLU A 534    28007  21257  22241  -4145  -4590   1412
ATOM   4010  CB  GLU A 534      67.684  49.893  15.031  1.00192.04           C  
ANISOU 4010  CB  GLU A 534    28200  21725  23042  -4669  -5249   2092
ATOM   4011  N   LYS A 535      64.847  51.083  16.382  1.00171.51           N  
ANISOU 4011  N   LYS A 535    27164  18968  19034  -4340  -4097    890
ATOM   4012  CA  LYS A 535      63.671  51.931  16.205  1.00170.17           C  
ANISOU 4012  CA  LYS A 535    27034  18732  18891  -4088  -3882    632
ATOM   4013  C   LYS A 535      63.314  52.112  14.729  1.00167.29           C  
ANISOU 4013  C   LYS A 535    26202  18449  18911  -3775  -3776    623
ATOM   4014  O   LYS A 535      63.542  51.214  13.919  1.00166.18           O  
ANISOU 4014  O   LYS A 535    25760  18402  18979  -3666  -3728    691
ATOM   4015  CB  LYS A 535      63.889  53.288  16.882  1.00171.47           C  
ANISOU 4015  CB  LYS A 535    27442  18789  18918  -4262  -4075    661
ATOM   4016  N   SER A 536      62.750  53.276  14.405  1.00167.03           N  
ANISOU 4016  N   SER A 536    26122  18379  18962  -3655  -3751    540
ATOM   4017  CA  SER A 536      62.355  53.647  13.042  1.00165.80           C  
ANISOU 4017  CA  SER A 536    25573  18310  19114  -3404  -3650    510
ATOM   4018  C   SER A 536      60.909  53.336  12.640  1.00161.56           C  
ANISOU 4018  C   SER A 536    24959  17779  18648  -3112  -3330    284
ATOM   4019  O   SER A 536      60.545  53.520  11.478  1.00159.18           O  
ANISOU 4019  O   SER A 536    24367  17547  18568  -2913  -3227    237
ATOM   4020  CB  SER A 536      63.333  53.093  11.996  1.00168.26           C  
ANISOU 4020  CB  SER A 536    25460  18756  19716  -3416  -3786    719
ATOM   4021  OG  SER A 536      63.380  51.677  12.042  1.00167.90           O  
ANISOU 4021  OG  SER A 536    25295  18751  19749  -3373  -3725    751
ATOM   4022  N   VAL A 537      60.080  52.877  13.575  1.00163.10           N  
ANISOU 4022  N   VAL A 537    25401  17914  18656  -3096  -3167    147
ATOM   4023  CA  VAL A 537      58.696  52.594  13.223  1.00159.16           C  
ANISOU 4023  CA  VAL A 537    24830  17415  18230  -2828  -2864    -52
ATOM   4024  C   VAL A 537      57.833  53.848  13.265  1.00160.11           C  
ANISOU 4024  C   VAL A 537    25238  17378  18221  -2747  -2702   -287
ATOM   4025  O   VAL A 537      56.985  54.043  12.396  1.00160.16           O  
ANISOU 4025  O   VAL A 537    25111  17354  18387  -2511  -2525   -415
ATOM   4026  N   GLN A 538      58.038  54.709  14.266  1.00164.14           N  
ANISOU 4026  N   GLN A 538    26137  17770  18458  -2949  -2769   -348
ATOM   4027  CA  GLN A 538      57.207  55.903  14.401  1.00164.54           C  
ANISOU 4027  CA  GLN A 538    26464  17636  18417  -2869  -2608   -604
ATOM   4028  C   GLN A 538      57.521  56.954  13.344  1.00162.55           C  
ANISOU 4028  C   GLN A 538    26160  17279  18321  -2806  -2720   -602
ATOM   4029  O   GLN A 538      56.606  57.635  12.868  1.00162.74           O  
ANISOU 4029  O   GLN A 538    26206  17170  18459  -2619  -2561   -782
ATOM   4030  CB  GLN A 538      57.346  56.496  15.803  1.00166.43           C  
ANISOU 4030  CB  GLN A 538    27148  17781  18309  -3123  -2637   -700
ATOM   4031  CG  GLN A 538      56.707  57.875  15.956  1.00169.96           C  
ANISOU 4031  CG  GLN A 538    27893  17997  18689  -3067  -2510   -981
ATOM   4032  CD  GLN A 538      55.240  57.906  15.561  1.00167.53           C  
ANISOU 4032  CD  GLN A 538    27479  17619  18554  -2755  -2174  -1222
ATOM   4033  OE1 GLN A 538      54.479  56.987  15.861  1.00165.25           O  
ANISOU 4033  OE1 GLN A 538    27084  17446  18257  -2660  -1964  -1265
ATOM   4034  NE2 GLN A 538      54.841  58.971  14.872  1.00168.04           N  
ANISOU 4034  NE2 GLN A 538    27559  17488  18801  -2603  -2144  -1356
ATOM   4035  N   MET A 539      58.789  57.101  12.950  1.00177.70           N  
ANISOU 4035  N   MET A 539    27995  19257  20267  -2969  -3002   -385
ATOM   4036  CA  MET A 539      59.085  57.999  11.839  1.00177.64           C  
ANISOU 4036  CA  MET A 539    27892  19192  20412  -2926  -3117   -350
ATOM   4037  C   MET A 539      58.364  57.585  10.564  1.00177.74           C  
ANISOU 4037  C   MET A 539    27555  19287  20692  -2670  -2960   -378
ATOM   4038  O   MET A 539      58.341  58.360   9.601  1.00177.11           O  
ANISOU 4038  O   MET A 539    27400  19155  20738  -2626  -3023   -369
ATOM   4039  CB  MET A 539      60.586  58.059  11.569  1.00177.84           C  
ANISOU 4039  CB  MET A 539    27823  19317  20433  -3146  -3428    -92
ATOM   4040  CG  MET A 539      61.164  56.769  11.024  1.00173.88           C  
ANISOU 4040  CG  MET A 539    26919  19047  20102  -3119  -3456     86
ATOM   4041  SD  MET A 539      62.879  56.992  10.538  1.00172.42           S  
ANISOU 4041  SD  MET A 539    26573  18971  19968  -3354  -3792    366
ATOM   4042  CE  MET A 539      62.675  57.980   9.055  1.00170.12           C  
ANISOU 4042  CE  MET A 539    26151  18679  19808  -3257  -3791    327
ATOM   4043  N   PHE A 540      57.786  56.385  10.542  1.00149.45           N  
ANISOU 4043  N   PHE A 540    23763  15830  17191  -2525  -2777   -397
ATOM   4044  CA  PHE A 540      56.974  55.886   9.444  1.00150.15           C  
ANISOU 4044  CA  PHE A 540    23545  15993  17510  -2289  -2607   -439
ATOM   4045  C   PHE A 540      55.487  55.861   9.751  1.00151.50           C  
ANISOU 4045  C   PHE A 540    23801  16056  17708  -2085  -2330   -643
ATOM   4046  O   PHE A 540      54.676  55.959   8.828  1.00151.60           O  
ANISOU 4046  O   PHE A 540    23645  16046  17909  -1904  -2214   -697
ATOM   4047  CB  PHE A 540      57.413  54.465   9.070  1.00150.84           C  
ANISOU 4047  CB  PHE A 540    23292  16302  17720  -2263  -2610   -307
ATOM   4048  N   GLU A 541      55.115  55.742  11.028  1.00133.74           N  
ANISOU 4048  N   GLU A 541    21801  13746  15268  -2132  -2223   -751
ATOM   4049  CA  GLU A 541      53.733  55.469  11.399  1.00134.78           C  
ANISOU 4049  CA  GLU A 541    21962  13825  15421  -1946  -1932   -934
ATOM   4050  C   GLU A 541      52.854  56.710  11.305  1.00134.84           C  
ANISOU 4050  C   GLU A 541    22141  13597  15497  -1829  -1809  -1142
ATOM   4051  O   GLU A 541      51.638  56.588  11.118  1.00135.80           O  
ANISOU 4051  O   GLU A 541    22175  13663  15759  -1618  -1574  -1271
ATOM   4052  CB  GLU A 541      53.691  54.881  12.811  1.00136.22           C  
ANISOU 4052  CB  GLU A 541    22345  14062  15350  -2079  -1861   -969
ATOM   4053  CG  GLU A 541      52.327  54.386  13.258  1.00138.77           C  
ANISOU 4053  CG  GLU A 541    22663  14390  15674  -1914  -1554  -1131
ATOM   4054  CD  GLU A 541      52.375  53.718  14.617  1.00140.69           C  
ANISOU 4054  CD  GLU A 541    23084  14734  15639  -2099  -1513  -1126
ATOM   4055  OE1 GLU A 541      53.468  53.675  15.220  1.00139.80           O  
ANISOU 4055  OE1 GLU A 541    23110  14667  15342  -2360  -1740   -990
ATOM   4056  OE2 GLU A 541      51.323  53.229  15.080  1.00142.82           O1-
ANISOU 4056  OE2 GLU A 541    23348  15045  15873  -2004  -1268  -1238
ATOM   4057  N   LEU A 542      53.443  57.904  11.421  1.00133.73           N  
ANISOU 4057  N   LEU A 542    22225  13297  15287  -1961  -1976  -1169
ATOM   4058  CA  LEU A 542      52.676  59.133  11.255  1.00133.58           C  
ANISOU 4058  CA  LEU A 542    22342  13014  15398  -1848  -1898  -1359
ATOM   4059  C   LEU A 542      52.079  59.253   9.859  1.00132.88           C  
ANISOU 4059  C   LEU A 542    21954  12899  15635  -1657  -1890  -1296
ATOM   4060  O   LEU A 542      51.166  60.060   9.654  1.00133.89           O  
ANISOU 4060  O   LEU A 542    22118  12803  15953  -1514  -1790  -1443
ATOM   4061  CB  LEU A 542      53.555  60.350  11.552  1.00132.59           C  
ANISOU 4061  CB  LEU A 542    22497  12724  15159  -2048  -2135  -1365
ATOM   4062  N   PHE A 543      52.574  58.470   8.896  1.00119.46           N  
ANISOU 4062  N   PHE A 543    19957  11419  14015  -1666  -1996  -1085
ATOM   4063  CA  PHE A 543      52.003  58.489   7.554  1.00118.58           C  
ANISOU 4063  CA  PHE A 543    19564  11318  14172  -1526  -1989  -1014
ATOM   4064  C   PHE A 543      50.629  57.835   7.509  1.00119.06           C  
ANISOU 4064  C   PHE A 543    19487  11371  14381  -1291  -1710  -1119
ATOM   4065  O   PHE A 543      49.717  58.345   6.847  1.00119.56           O  
ANISOU 4065  O   PHE A 543    19457  11289  14682  -1151  -1652  -1156
ATOM   4066  CB  PHE A 543      52.945  57.803   6.568  1.00116.79           C  
ANISOU 4066  CB  PHE A 543    19066  11351  13959  -1626  -2153   -794
ATOM   4067  CG  PHE A 543      52.322  57.543   5.229  1.00115.93           C  
ANISOU 4067  CG  PHE A 543    18660  11315  14073  -1511  -2114   -725
ATOM   4068  CD1 PHE A 543      52.043  58.583   4.360  1.00116.05           C  
ANISOU 4068  CD1 PHE A 543    18651  11195  14247  -1524  -2232   -681
ATOM   4069  CD2 PHE A 543      52.013  56.251   4.840  1.00115.21           C  
ANISOU 4069  CD2 PHE A 543    18317  11422  14036  -1412  -1980   -692
ATOM   4070  CE1 PHE A 543      51.462  58.336   3.131  1.00115.41           C  
ANISOU 4070  CE1 PHE A 543    18308  11193  14350  -1462  -2216   -595
ATOM   4071  CE2 PHE A 543      51.438  55.998   3.612  1.00114.49           C  
ANISOU 4071  CE2 PHE A 543    17973  11405  14124  -1335  -1948   -631
ATOM   4072  CZ  PHE A 543      51.161  57.040   2.757  1.00114.56           C  
ANISOU 4072  CZ  PHE A 543    17967  11295  14264  -1371  -2066   -577
ATOM   4073  N   TYR A 544      50.457  56.699   8.186  1.00117.87           N  
ANISOU 4073  N   TYR A 544    19304  11371  14111  -1256  -1555  -1142
ATOM   4074  CA  TYR A 544      49.183  55.998   8.098  1.00119.97           C  
ANISOU 4074  CA  TYR A 544    19414  11653  14516  -1045  -1305  -1212
ATOM   4075  C   TYR A 544      48.100  56.683   8.921  1.00121.86           C  
ANISOU 4075  C   TYR A 544    19849  11668  14783   -927  -1082  -1445
ATOM   4076  O   TYR A 544      46.914  56.397   8.727  1.00123.34           O  
ANISOU 4076  O   TYR A 544    19899  11815  15149   -734   -876  -1509
ATOM   4077  CB  TYR A 544      49.338  54.542   8.547  1.00121.19           C  
ANISOU 4077  CB  TYR A 544    19458  12037  14551  -1058  -1233  -1145
ATOM   4078  CG  TYR A 544      48.218  53.634   8.076  1.00121.91           C  
ANISOU 4078  CG  TYR A 544    19305  12198  14818   -858  -1044  -1140
ATOM   4079  CD1 TYR A 544      48.221  53.123   6.784  1.00120.37           C  
ANISOU 4079  CD1 TYR A 544    18819  12113  14804   -801  -1112  -1009
ATOM   4080  CD2 TYR A 544      47.154  53.306   8.906  1.00123.83           C  
ANISOU 4080  CD2 TYR A 544    19610  12405  15035   -744   -797  -1268
ATOM   4081  CE1 TYR A 544      47.210  52.300   6.338  1.00120.42           C  
ANISOU 4081  CE1 TYR A 544    18613  12174  14965   -636   -960   -995
ATOM   4082  CE2 TYR A 544      46.135  52.481   8.465  1.00124.43           C  
ANISOU 4082  CE2 TYR A 544    19457  12543  15277   -571   -642  -1241
ATOM   4083  CZ  TYR A 544      46.170  51.984   7.180  1.00122.67           C  
ANISOU 4083  CZ  TYR A 544    18959  12411  15239   -516   -735  -1100
ATOM   4084  OH  TYR A 544      45.160  51.166   6.733  1.00124.26           O  
ANISOU 4084  OH  TYR A 544    18946  12666  15600   -359   -599  -1065
ATOM   4085  N   SER A 545      48.484  57.583   9.830  1.00130.97           N  
ANISOU 4085  N   SER A 545    21315  12673  15774  -1045  -1112  -1583
ATOM   4086  CA  SER A 545      47.504  58.349  10.591  1.00132.40           C  
ANISOU 4086  CA  SER A 545    21685  12622  16000   -939   -884  -1853
ATOM   4087  C   SER A 545      46.980  59.537   9.792  1.00131.94           C  
ANISOU 4087  C   SER A 545    21578  12283  16271   -818   -939  -1903
ATOM   4088  O   SER A 545      45.801  59.890   9.901  1.00133.44           O  
ANISOU 4088  O   SER A 545    21734  12288  16679   -629   -720  -2076
ATOM   4089  CB  SER A 545      48.120  58.829  11.906  1.00133.59           C  
ANISOU 4089  CB  SER A 545    22207  12722  15830  -1136   -889  -2006
ATOM   4090  OG  SER A 545      49.137  59.790  11.672  1.00132.13           O  
ANISOU 4090  OG  SER A 545    22169  12421  15612  -1295  -1172  -1944
ATOM   4091  N   GLN A 546      47.840  60.171   8.993  1.00122.73           N  
ANISOU 4091  N   GLN A 546    20393  11076  15163   -936  -1240  -1743
ATOM   4092  CA  GLN A 546      47.419  61.320   8.204  1.00123.12           C  
ANISOU 4092  CA  GLN A 546    20391  10854  15536   -862  -1353  -1746
ATOM   4093  C   GLN A 546      46.757  60.927   6.891  1.00122.66           C  
ANISOU 4093  C   GLN A 546    19986  10852  15767   -736  -1374  -1567
ATOM   4094  O   GLN A 546      45.973  61.716   6.352  1.00123.57           O  
ANISOU 4094  O   GLN A 546    20019  10719  16213   -625  -1393  -1587
ATOM   4095  CB  GLN A 546      48.613  62.233   7.913  1.00121.96           C  
ANISOU 4095  CB  GLN A 546    20380  10641  15317  -1076  -1691  -1631
ATOM   4096  CG  GLN A 546      49.160  62.946   9.137  1.00123.31           C  
ANISOU 4096  CG  GLN A 546    20925  10667  15259  -1207  -1707  -1821
ATOM   4097  CD  GLN A 546      50.304  63.884   8.801  1.00121.94           C  
ANISOU 4097  CD  GLN A 546    20876  10414  15040  -1420  -2064  -1685
ATOM   4098  OE1 GLN A 546      50.749  63.953   7.654  1.00120.02           O  
ANISOU 4098  OE1 GLN A 546    20429  10261  14911  -1485  -2296  -1438
ATOM   4099  NE2 GLN A 546      50.781  64.620   9.800  1.00122.46           N  
ANISOU 4099  NE2 GLN A 546    21283  10321  14924  -1550  -2112  -1845
ATOM   4100  N   HIS A 547      47.047  59.735   6.364  1.00123.50           N  
ANISOU 4100  N   HIS A 547    19886  11265  15773   -763  -1383  -1392
ATOM   4101  CA  HIS A 547      46.498  59.359   5.065  1.00122.79           C  
ANISOU 4101  CA  HIS A 547    19486  11248  15920   -688  -1422  -1219
ATOM   4102  C   HIS A 547      45.066  58.847   5.173  1.00124.42           C  
ANISOU 4102  C   HIS A 547    19555  11394  16323   -454  -1147  -1308
ATOM   4103  O   HIS A 547      44.255  59.082   4.271  1.00124.78           O  
ANISOU 4103  O   HIS A 547    19409  11335  16668   -362  -1171  -1220
ATOM   4104  CB  HIS A 547      47.383  58.309   4.398  1.00120.60           C  
ANISOU 4104  CB  HIS A 547    19034  11311  15477   -813  -1533  -1026
ATOM   4105  CG  HIS A 547      46.959  57.969   3.003  1.00120.06           C  
ANISOU 4105  CG  HIS A 547    18674  11342  15602   -792  -1596   -855
ATOM   4106  ND1 HIS A 547      46.017  57.002   2.727  1.00120.96           N  
ANISOU 4106  ND1 HIS A 547    18594  11544  15822   -640  -1413   -845
ATOM   4107  CD2 HIS A 547      47.341  58.475   1.807  1.00119.00           C  
ANISOU 4107  CD2 HIS A 547    18418  11242  15554   -932  -1829   -679
ATOM   4108  CE1 HIS A 547      45.842  56.920   1.420  1.00120.17           C  
ANISOU 4108  CE1 HIS A 547    18276  11523  15861   -690  -1529   -679
ATOM   4109  NE2 HIS A 547      46.633  57.804   0.839  1.00119.43           N  
ANISOU 4109  NE2 HIS A 547    18220  11408  15749   -875  -1778   -576
ATOM   4110  N   PHE A 548      44.737  58.141   6.250  1.00127.91           N  
ANISOU 4110  N   PHE A 548    20086  11912  16604   -378   -899  -1459
ATOM   4111  CA  PHE A 548      43.380  57.671   6.480  1.00130.33           C  
ANISOU 4111  CA  PHE A 548    20270  12170  17077   -165   -620  -1551
ATOM   4112  C   PHE A 548      42.764  58.403   7.665  1.00133.16           C  
ANISOU 4112  C   PHE A 548    20847  12299  17451    -77   -393  -1839
ATOM   4113  O   PHE A 548      43.468  58.874   8.562  1.00134.92           O  
ANISOU 4113  O   PHE A 548    21344  12483  17436   -203   -412  -1977
ATOM   4114  CB  PHE A 548      43.341  56.157   6.711  1.00130.27           C  
ANISOU 4114  CB  PHE A 548    20148  12458  16892   -150   -495  -1485
ATOM   4115  CG  PHE A 548      43.646  55.349   5.480  1.00128.45           C  
ANISOU 4115  CG  PHE A 548    19659  12430  16716   -189   -651  -1251
ATOM   4116  CD1 PHE A 548      42.701  55.219   4.475  1.00128.50           C  
ANISOU 4116  CD1 PHE A 548    19427  12395  17003    -72   -632  -1148
ATOM   4117  CD2 PHE A 548      44.864  54.706   5.334  1.00127.03           C  
ANISOU 4117  CD2 PHE A 548    19468  12480  16317   -353   -809  -1142
ATOM   4118  CE1 PHE A 548      42.971  54.480   3.338  1.00126.94           C  
ANISOU 4118  CE1 PHE A 548    19010  12393  16828   -133   -762   -959
ATOM   4119  CE2 PHE A 548      45.138  53.960   4.199  1.00125.67           C  
ANISOU 4119  CE2 PHE A 548    19053  12496  16199   -391   -920   -972
ATOM   4120  CZ  PHE A 548      44.190  53.847   3.202  1.00125.38           C  
ANISOU 4120  CZ  PHE A 548    18806  12429  16404   -289   -891   -890
ATOM   4121  N   SER A 549      41.432  58.493   7.651  1.00139.85           N  
ANISOU 4121  N   SER A 549    21560  12992  18584    133   -173  -1933
ATOM   4122  CA  SER A 549      40.721  59.338   8.606  1.00141.98           C  
ANISOU 4122  CA  SER A 549    21988  13000  18959    242     64  -2238
ATOM   4123  C   SER A 549      40.942  58.873  10.042  1.00142.94           C  
ANISOU 4123  C   SER A 549    22351  13275  18685    161    290  -2446
ATOM   4124  O   SER A 549      41.540  59.586  10.855  1.00144.08           O  
ANISOU 4124  O   SER A 549    22786  13324  18633     37    278  -2629
ATOM   4125  CB  SER A 549      39.229  59.358   8.266  1.00143.16           C  
ANISOU 4125  CB  SER A 549    21890  12987  19518    487    270  -2273
ATOM   4126  OG  SER A 549      38.651  58.074   8.434  1.00143.67           O  
ANISOU 4126  OG  SER A 549    21804  13304  19480    557    467  -2210
ATOM   4127  N   GLY A 550      40.464  57.678  10.373  1.00144.36           N  
ANISOU 4127  N   GLY A 550    22421  13696  18734    204    480  -2407
ATOM   4128  CA  GLY A 550      40.531  57.212  11.744  1.00145.42           C  
ANISOU 4128  CA  GLY A 550    22766  13986  18502    105    698  -2584
ATOM   4129  C   GLY A 550      40.904  55.752  11.888  1.00144.39           C  
ANISOU 4129  C   GLY A 550    22556  14202  18103      2    661  -2385
ATOM   4130  O   GLY A 550      40.470  55.087  12.834  1.00145.90           O  
ANISOU 4130  O   GLY A 550    22800  14547  18089    -26    887  -2475
ATOM   4131  N   ARG A 551      41.706  55.237  10.962  1.00132.99           N  
ANISOU 4131  N   ARG A 551    20977  12885  16669    -64    378  -2117
ATOM   4132  CA  ARG A 551      42.084  53.833  10.998  1.00132.39           C  
ANISOU 4132  CA  ARG A 551    20789  13102  16412   -145    318  -1927
ATOM   4133  C   ARG A 551      43.135  53.595  12.074  1.00132.27           C  
ANISOU 4133  C   ARG A 551    21030  13226  16002   -393    239  -1945
ATOM   4134  O   ARG A 551      44.165  54.275  12.113  1.00131.43           O  
ANISOU 4134  O   ARG A 551    21097  13056  15784   -543     39  -1942
ATOM   4135  CB  ARG A 551      42.603  53.379   9.635  1.00130.32           C  
ANISOU 4135  CB  ARG A 551    20287  12922  16309   -137     65  -1674
ATOM   4136  CG  ARG A 551      41.535  53.368   8.559  1.00130.41           C  
ANISOU 4136  CG  ARG A 551    20029  12844  16677     66    123  -1604
ATOM   4137  CD  ARG A 551      42.045  52.772   7.264  1.00128.58           C  
ANISOU 4137  CD  ARG A 551    19572  12743  16541     33   -104  -1370
ATOM   4138  NE  ARG A 551      41.007  52.765   6.239  1.00128.52           N  
ANISOU 4138  NE  ARG A 551    19325  12656  16852    189    -67  -1286
ATOM   4139  CZ  ARG A 551      41.158  52.245   5.026  1.00127.54           C  
ANISOU 4139  CZ  ARG A 551    18986  12639  16834    169   -220  -1101
ATOM   4140  NH1 ARG A 551      42.303  51.668   4.687  1.00126.37           N  
ANISOU 4140  NH1 ARG A 551    18813  12683  16519     22   -394  -1007
ATOM   4141  NH2 ARG A 551      40.158  52.287   4.156  1.00127.84           N1+
ANISOU 4141  NH2 ARG A 551    18829  12595  17151    284   -195  -1015
ATOM   4142  N   LYS A 552      42.864  52.634  12.952  1.00137.07           N  
ANISOU 4142  N   LYS A 552    21657  14022  16403   -457    375  -1943
ATOM   4143  CA  LYS A 552      43.784  52.238  14.010  1.00137.47           C  
ANISOU 4143  CA  LYS A 552    21926  14226  16081   -724    281  -1913
ATOM   4144  C   LYS A 552      44.509  50.974  13.567  1.00136.20           C  
ANISOU 4144  C   LYS A 552    21564  14269  15919   -796     50  -1629
ATOM   4145  O   LYS A 552      43.877  49.931  13.368  1.00136.77           O  
ANISOU 4145  O   LYS A 552    21417  14463  16087   -699    124  -1528
ATOM   4146  CB  LYS A 552      43.029  52.003  15.320  1.00140.45           C  
ANISOU 4146  CB  LYS A 552    22460  14691  16215   -794    565  -2083
ATOM   4147  CG  LYS A 552      43.892  51.716  16.550  1.00141.22           C  
ANISOU 4147  CG  LYS A 552    22828  14940  15889  -1122    473  -2062
ATOM   4148  CD  LYS A 552      44.241  50.238  16.694  1.00141.33           C  
ANISOU 4148  CD  LYS A 552    22685  15200  15815  -1240    320  -1785
ATOM   4149  CE  LYS A 552      42.998  49.379  16.877  1.00143.58           C  
ANISOU 4149  CE  LYS A 552    22790  15608  16155  -1118    564  -1784
ATOM   4150  NZ  LYS A 552      42.289  49.679  18.151  1.00146.19           N1+
ANISOU 4150  NZ  LYS A 552    23352  15999  16196  -1238    864  -2016
ATOM   4151  N   LEU A 553      45.826  51.065  13.417  1.00119.35           N  
ANISOU 4151  N   LEU A 553    19492  12159  13698   -964   -229  -1505
ATOM   4152  CA  LEU A 553      46.633  49.909  13.067  1.00117.21           C  
ANISOU 4152  CA  LEU A 553    19025  12057  13453  -1043   -450  -1261
ATOM   4153  C   LEU A 553      47.259  49.299  14.316  1.00118.61           C  
ANISOU 4153  C   LEU A 553    19366  12367  13331  -1306   -540  -1182
ATOM   4154  O   LEU A 553      47.592  50.001  15.274  1.00120.97           O  
ANISOU 4154  O   LEU A 553    19974  12624  13364  -1494   -534  -1286
ATOM   4155  CB  LEU A 553      47.724  50.273  12.051  1.00115.60           C  
ANISOU 4155  CB  LEU A 553    18728  11818  13378  -1070   -706  -1150
ATOM   4156  CG  LEU A 553      48.815  51.301  12.368  1.00116.88           C  
ANISOU 4156  CG  LEU A 553    19138  11892  13380  -1261   -884  -1171
ATOM   4157  CD1 LEU A 553      49.971  50.696  13.148  1.00117.34           C  
ANISOU 4157  CD1 LEU A 553    19277  12073  13234  -1519  -1095  -1017
ATOM   4158  CD2 LEU A 553      49.335  51.894  11.077  1.00115.40           C  
ANISOU 4158  CD2 LEU A 553    18810  11642  13395  -1202  -1040  -1109
ATOM   4159  N   THR A 554      47.410  47.977  14.293  1.00117.37           N  
ANISOU 4159  N   THR A 554    19001  12364  13230  -1334   -639   -991
ATOM   4160  CA  THR A 554      48.080  47.229  15.347  1.00117.62           C  
ANISOU 4160  CA  THR A 554    19126  12522  13041  -1601   -795   -843
ATOM   4161  C   THR A 554      49.225  46.439  14.733  1.00116.84           C  
ANISOU 4161  C   THR A 554    18793  12474  13127  -1652  -1097   -612
ATOM   4162  O   THR A 554      49.054  45.795  13.692  1.00116.68           O  
ANISOU 4162  O   THR A 554    18468  12473  13392  -1462  -1111   -552
ATOM   4163  CB  THR A 554      47.111  46.287  16.069  1.00119.00           C  
ANISOU 4163  CB  THR A 554    19257  12827  13131  -1614   -638   -817
ATOM   4164  OG1 THR A 554      46.542  45.369  15.127  1.00119.83           O  
ANISOU 4164  OG1 THR A 554    19021  12967  13541  -1385   -614   -727
ATOM   4165  CG2 THR A 554      45.998  47.073  16.748  1.00120.19           C  
ANISOU 4165  CG2 THR A 554    19628  12943  13095  -1577   -306  -1072
ATOM   4166  N   TRP A 555      50.388  46.491  15.377  1.00116.29           N  
ANISOU 4166  N   TRP A 555    18860  12422  12903  -1916  -1335   -491
ATOM   4167  CA  TRP A 555      51.590  45.865  14.842  1.00115.30           C  
ANISOU 4167  CA  TRP A 555    18508  12323  12979  -1975  -1624   -285
ATOM   4168  C   TRP A 555      51.651  44.392  15.226  1.00115.40           C  
ANISOU 4168  C   TRP A 555    18316  12438  13093  -2047  -1753    -83
ATOM   4169  O   TRP A 555      51.525  44.041  16.404  1.00116.39           O  
ANISOU 4169  O   TRP A 555    18604  12627  12992  -2263  -1789     -2
ATOM   4170  CB  TRP A 555      52.839  46.591  15.346  1.00115.55           C  
ANISOU 4170  CB  TRP A 555    18755  12310  12839  -2232  -1849   -216
ATOM   4171  CG  TRP A 555      53.056  47.932  14.714  1.00115.14           C  
ANISOU 4171  CG  TRP A 555    18827  12144  12777  -2160  -1810   -362
ATOM   4172  CD1 TRP A 555      52.644  49.139  15.193  1.00116.53           C  
ANISOU 4172  CD1 TRP A 555    19331  12219  12726  -2196  -1672   -556
ATOM   4173  CD2 TRP A 555      53.761  48.204  13.495  1.00114.04           C  
ANISOU 4173  CD2 TRP A 555    18480  11979  12871  -2060  -1924   -323
ATOM   4174  NE1 TRP A 555      53.034  50.144  14.341  1.00115.84           N  
ANISOU 4174  NE1 TRP A 555    19250  12027  12738  -2120  -1720   -618
ATOM   4175  CE2 TRP A 555      53.723  49.594  13.292  1.00113.97           C  
ANISOU 4175  CE2 TRP A 555    18690  11851  12762  -2049  -1873   -468
ATOM   4176  CE3 TRP A 555      54.414  47.404  12.553  1.00113.37           C  
ANISOU 4176  CE3 TRP A 555    18041  11963  13073  -1989  -2056   -193
ATOM   4177  CZ2 TRP A 555      54.312  50.202  12.190  1.00113.06           C  
ANISOU 4177  CZ2 TRP A 555    18453  11703  12802  -1991  -1971   -453
ATOM   4178  CZ3 TRP A 555      54.999  48.012  11.460  1.00112.80           C  
ANISOU 4178  CZ3 TRP A 555    17850  11874  13134  -1931  -2117   -208
ATOM   4179  CH2 TRP A 555      54.945  49.395  11.289  1.00112.52           C  
ANISOU 4179  CH2 TRP A 555    18041  11738  12972  -1943  -2085   -320
ATOM   4180  N   LEU A 556      51.843  43.536  14.226  1.00127.66           N  
ANISOU 4180  N   LEU A 556    19512  14004  14988  -1882  -1828     -4
ATOM   4181  CA  LEU A 556      52.082  42.114  14.435  1.00127.66           C  
ANISOU 4181  CA  LEU A 556    19269  14061  15176  -1936  -2002    196
ATOM   4182  C   LEU A 556      53.579  41.849  14.380  1.00127.03           C  
ANISOU 4182  C   LEU A 556    19061  13954  15253  -2093  -2315    370
ATOM   4183  O   LEU A 556      54.257  42.287  13.445  1.00127.02           O  
ANISOU 4183  O   LEU A 556    18939  13917  15405  -2006  -2349    318
ATOM   4184  CB  LEU A 556      51.363  41.270  13.382  1.00127.70           C  
ANISOU 4184  CB  LEU A 556    18949  14080  15491  -1660  -1892    156
ATOM   4185  CG  LEU A 556      49.836  41.273  13.420  1.00128.74           C  
ANISOU 4185  CG  LEU A 556    19136  14241  15538  -1501  -1610     36
ATOM   4186  CD1 LEU A 556      49.277  40.496  12.239  1.00128.21           C  
ANISOU 4186  CD1 LEU A 556    18747  14177  15792  -1246  -1541     10
ATOM   4187  CD2 LEU A 556      49.337  40.699  14.735  1.00129.94           C  
ANISOU 4187  CD2 LEU A 556    19420  14471  15481  -1683  -1619    145
ATOM   4188  N   HIS A 557      54.087  41.134  15.381  1.00139.19           N  
ANISOU 4188  N   HIS A 557    20614  15514  16760  -2340  -2549    591
ATOM   4189  CA  HIS A 557      55.502  40.808  15.460  1.00138.75           C  
ANISOU 4189  CA  HIS A 557    20416  15414  16889  -2510  -2873    793
ATOM   4190  C   HIS A 557      55.793  39.339  15.200  1.00138.37           C  
ANISOU 4190  C   HIS A 557    19974  15345  17254  -2461  -3060    961
ATOM   4191  O   HIS A 557      56.962  38.974  15.043  1.00137.01           O  
ANISOU 4191  O   HIS A 557    19592  15115  17349  -2542  -3311   1107
ATOM   4192  CB  HIS A 557      56.056  41.193  16.838  1.00139.15           C  
ANISOU 4192  CB  HIS A 557    20784  15472  16613  -2885  -3068    956
ATOM   4193  CG  HIS A 557      55.977  42.659  17.130  1.00139.65           C  
ANISOU 4193  CG  HIS A 557    21238  15525  16298  -2961  -2926    786
ATOM   4194  ND1 HIS A 557      54.873  43.242  17.714  1.00140.36           N  
ANISOU 4194  ND1 HIS A 557    21633  15657  16042  -2967  -2664    606
ATOM   4195  CD2 HIS A 557      56.862  43.661  16.917  1.00139.04           C  
ANISOU 4195  CD2 HIS A 557    21284  15389  16155  -3035  -3012    760
ATOM   4196  CE1 HIS A 557      55.082  44.539  17.850  1.00139.82           C  
ANISOU 4196  CE1 HIS A 557    21862  15536  15728  -3033  -2596    462
ATOM   4197  NE2 HIS A 557      56.282  44.819  17.374  1.00138.94           N  
ANISOU 4197  NE2 HIS A 557    21656  15365  15771  -3080  -2817    564
ATOM   4198  N   TYR A 558      54.762  38.495  15.144  1.00160.53           N  
ANISOU 4198  N   TYR A 558    22664  18186  20146  -2328  -2948    943
ATOM   4199  CA  TYR A 558      54.945  37.057  14.989  1.00160.14           C  
ANISOU 4199  CA  TYR A 558    22254  18094  20496  -2291  -3140   1103
ATOM   4200  C   TYR A 558      55.499  36.677  13.621  1.00158.37           C  
ANISOU 4200  C   TYR A 558    21658  17809  20708  -2049  -3135    996
ATOM   4201  O   TYR A 558      55.975  35.549  13.454  1.00154.82           O  
ANISOU 4201  O   TYR A 558    20880  17287  20658  -2031  -3334   1116
ATOM   4202  CB  TYR A 558      53.605  36.359  15.245  1.00161.10           C  
ANISOU 4202  CB  TYR A 558    22373  18274  20564  -2209  -3003   1098
ATOM   4203  CG  TYR A 558      53.627  34.846  15.212  1.00161.18           C  
ANISOU 4203  CG  TYR A 558    22044  18230  20969  -2188  -3216   1275
ATOM   4204  CD1 TYR A 558      54.176  34.114  16.258  1.00160.95           C  
ANISOU 4204  CD1 TYR A 558    21984  18170  21001  -2478  -3555   1578
ATOM   4205  CD2 TYR A 558      53.064  34.149  14.150  1.00161.22           C  
ANISOU 4205  CD2 TYR A 558    21765  18204  21286  -1897  -3094   1149
ATOM   4206  CE1 TYR A 558      54.186  32.727  16.234  1.00160.12           C  
ANISOU 4206  CE1 TYR A 558    21554  17986  21299  -2461  -3779   1752
ATOM   4207  CE2 TYR A 558      53.068  32.765  14.117  1.00160.42           C  
ANISOU 4207  CE2 TYR A 558    21356  18029  21568  -1873  -3298   1297
ATOM   4208  CZ  TYR A 558      53.629  32.059  15.161  1.00159.48           C  
ANISOU 4208  CZ  TYR A 558    21193  17860  21540  -2147  -3644   1598
ATOM   4209  OH  TYR A 558      53.632  30.682  15.128  1.00156.49           O  
ANISOU 4209  OH  TYR A 558    20494  17379  21585  -2125  -3875   1755
ATOM   4210  N   LEU A 559      55.465  37.586  12.648  1.00146.36           N  
ANISOU 4210  N   LEU A 559    20171  16314  19124  -1880  -2920    773
ATOM   4211  CA  LEU A 559      55.801  37.262  11.262  1.00144.63           C  
ANISOU 4211  CA  LEU A 559    19617  16080  19253  -1660  -2853    630
ATOM   4212  C   LEU A 559      56.718  38.329  10.664  1.00144.74           C  
ANISOU 4212  C   LEU A 559    19672  16113  19208  -1685  -2836    542
ATOM   4213  O   LEU A 559      56.506  38.814   9.552  1.00145.27           O  
ANISOU 4213  O   LEU A 559    19681  16230  19286  -1522  -2643    350
ATOM   4214  CB  LEU A 559      54.528  37.112  10.430  1.00145.23           C  
ANISOU 4214  CB  LEU A 559    19648  16201  19332  -1409  -2579    441
ATOM   4215  CG  LEU A 559      53.532  36.038  10.880  1.00146.52           C  
ANISOU 4215  CG  LEU A 559    19747  16356  19568  -1362  -2581    522
ATOM   4216  CD1 LEU A 559      52.274  36.082  10.027  1.00148.26           C  
ANISOU 4216  CD1 LEU A 559    19951  16619  19762  -1127  -2305    343
ATOM   4217  CD2 LEU A 559      54.161  34.656  10.859  1.00144.30           C  
ANISOU 4217  CD2 LEU A 559    19115  15990  19723  -1373  -2826    654
ATOM   4218  N   CYS A 560      57.764  38.704  11.400  1.00141.98           N  
ANISOU 4218  N   CYS A 560    19422  15731  18793  -1916  -3058    705
ATOM   4219  CA  CYS A 560      58.667  39.772  10.992  1.00141.31           C  
ANISOU 4219  CA  CYS A 560    19407  15665  18620  -1982  -3075    662
ATOM   4220  C   CYS A 560      60.071  39.224  10.780  1.00139.51           C  
ANISOU 4220  C   CYS A 560    18853  15394  18760  -2060  -3311    788
ATOM   4221  O   CYS A 560      60.559  38.417  11.578  1.00140.03           O  
ANISOU 4221  O   CYS A 560    18813  15382  19011  -2201  -3561   1004
ATOM   4222  CB  CYS A 560      58.689  40.888  12.036  1.00142.20           C  
ANISOU 4222  CB  CYS A 560    19955  15770  18303  -2202  -3124    732
ATOM   4223  SG  CYS A 560      57.095  41.709  12.237  1.00144.67           S  
ANISOU 4223  SG  CYS A 560    20633  16115  18219  -2096  -2811    537
ATOM   4224  N   THR A 561      60.724  39.670   9.709  1.00133.64           N  
ANISOU 4224  N   THR A 561    17940  14702  18134  -1982  -3237    663
ATOM   4225  CA  THR A 561      62.020  39.142   9.320  1.00132.51           C  
ANISOU 4225  CA  THR A 561    17429  14533  18385  -2018  -3402    732
ATOM   4226  C   THR A 561      63.140  40.113   9.697  1.00132.80           C  
ANISOU 4226  C   THR A 561    17603  14571  18283  -2240  -3577    875
ATOM   4227  O   THR A 561      62.918  41.138  10.349  1.00133.60           O  
ANISOU 4227  O   THR A 561    18103  14677  17981  -2379  -3593    925
ATOM   4228  CB  THR A 561      62.042  38.838   7.820  1.00131.81           C  
ANISOU 4228  CB  THR A 561    17007  14529  18547  -1800  -3189    485
ATOM   4229  OG1 THR A 561      61.931  40.060   7.082  1.00132.56           O  
ANISOU 4229  OG1 THR A 561    17274  14741  18351  -1788  -3016    345
ATOM   4230  CG2 THR A 561      60.885  37.924   7.447  1.00131.79           C  
ANISOU 4230  CG2 THR A 561    16900  14518  18656  -1594  -3026    349
ATOM   4231  N   GLY A 562      64.362  39.778   9.286  1.00135.38           N  
ANISOU 4231  N   GLY A 562    17587  14887  18964  -2275  -3708    934
ATOM   4232  CA  GLY A 562      65.532  40.618   9.475  1.00135.85           C  
ANISOU 4232  CA  GLY A 562    17702  14956  18958  -2475  -3880   1076
ATOM   4233  C   GLY A 562      66.417  40.562   8.247  1.00136.10           C  
ANISOU 4233  C   GLY A 562    17340  15077  19295  -2386  -3794    948
ATOM   4234  O   GLY A 562      65.904  40.405   7.135  1.00137.22           O  
ANISOU 4234  O   GLY A 562    17327  15322  19488  -2187  -3530    691
ATOM   4235  N   GLU A 563      67.736  40.679   8.408  1.00145.70           N  
ANISOU 4235  N   GLU A 563    18380  16268  20711  -2544  -4006   1121
ATOM   4236  CA  GLU A 563      68.648  40.541   7.275  1.00145.29           C  
ANISOU 4236  CA  GLU A 563    17906  16314  20982  -2472  -3914    994
ATOM   4237  C   GLU A 563      69.695  39.474   7.574  1.00145.10           C  
ANISOU 4237  C   GLU A 563    17448  16158  21525  -2507  -4135   1150
ATOM   4238  O   GLU A 563      70.593  39.679   8.399  1.00145.85           O  
ANISOU 4238  O   GLU A 563    17570  16162  21686  -2723  -4432   1439
ATOM   4239  CB  GLU A 563      69.306  41.868   6.906  1.00145.12           C  
ANISOU 4239  CB  GLU A 563    18031  16422  20686  -2615  -3915   1021
ATOM   4240  CG  GLU A 563      70.129  41.767   5.627  1.00145.31           C  
ANISOU 4240  CG  GLU A 563    17624  16602  20986  -2550  -3764    856
ATOM   4241  CD  GLU A 563      69.290  41.360   4.419  1.00145.71           C  
ANISOU 4241  CD  GLU A 563    17518  16784  21059  -2323  -3422    515
ATOM   4242  OE1 GLU A 563      68.068  41.619   4.411  1.00146.66           O  
ANISOU 4242  OE1 GLU A 563    17942  16912  20868  -2238  -3290    417
ATOM   4243  OE2 GLU A 563      69.854  40.772   3.473  1.00145.10           O1-
ANISOU 4243  OE2 GLU A 563    17008  16804  21319  -2240  -3281    340
ATOM   4244  N   VAL A 564      69.562  38.347   6.877  1.00167.84           N  
ANISOU 4244  N   VAL A 564    19925  19017  24829  -2297  -3995    954
ATOM   4245  CA  VAL A 564      70.415  37.161   6.888  1.00164.80           C  
ANISOU 4245  CA  VAL A 564    19033  18487  25094  -2253  -4139   1009
ATOM   4246  C   VAL A 564      71.753  37.441   6.209  1.00165.19           C  
ANISOU 4246  C   VAL A 564    18728  18621  25414  -2303  -4125    979
ATOM   4247  O   VAL A 564      72.053  38.589   5.862  1.00166.34           O  
ANISOU 4247  O   VAL A 564    19058  18938  25205  -2410  -4053    972
ATOM   4248  CB  VAL A 564      69.689  35.983   6.218  1.00162.63           C  
ANISOU 4248  CB  VAL A 564    18482  18175  25134  -1992  -3937    736
ATOM   4249  CG1 VAL A 564      68.373  35.712   6.933  1.00162.01           C  
ANISOU 4249  CG1 VAL A 564    18745  18022  24788  -1959  -3965    798
ATOM   4250  CG2 VAL A 564      69.450  36.270   4.746  1.00164.00           C  
ANISOU 4250  CG2 VAL A 564    18537  18572  25202  -1835  -3551    355
ATOM   4251  N   LYS A 565      72.586  36.399   6.079  1.00187.63           N  
ANISOU 4251  N   LYS A 565    21052  21332  28907  -2239  -4216    983
ATOM   4252  CA  LYS A 565      73.837  36.464   5.321  1.00187.84           C  
ANISOU 4252  CA  LYS A 565    20643  21442  29287  -2248  -4150    899
ATOM   4253  C   LYS A 565      74.942  37.247   6.031  1.00188.38           C  
ANISOU 4253  C   LYS A 565    20782  21482  29312  -2514  -4451   1258
ATOM   4254  O   LYS A 565      75.259  38.386   5.676  1.00190.38           O  
ANISOU 4254  O   LYS A 565    21218  21931  29187  -2632  -4375   1259
ATOM   4255  CB  LYS A 565      73.544  37.025   3.915  1.00188.44           C  
ANISOU 4255  CB  LYS A 565    20704  21814  29081  -2140  -3734    518
ATOM   4256  CG  LYS A 565      74.699  37.106   2.915  1.00188.70           C  
ANISOU 4256  CG  LYS A 565    20281  22008  29408  -2145  -3570    349
ATOM   4257  CD  LYS A 565      75.142  38.554   2.699  1.00190.70           C  
ANISOU 4257  CD  LYS A 565    20787  22488  29180  -2350  -3563    455
ATOM   4258  CE  LYS A 565      76.187  38.677   1.604  1.00191.44           C  
ANISOU 4258  CE  LYS A 565    20439  22801  29499  -2370  -3356    264
ATOM   4259  NZ  LYS A 565      75.618  38.344   0.268  1.00193.13           N1+
ANISOU 4259  NZ  LYS A 565    20487  23230  29664  -2210  -2937   -187
ATOM   4260  N   MET A 566      75.474  36.644   7.100  1.00196.75           N  
ANISOU 4260  N   MET A 566    21725  22289  30742  -2634  -4828   1594
ATOM   4261  CA  MET A 566      76.728  37.050   7.732  1.00195.34           C  
ANISOU 4261  CA  MET A 566    21455  22034  30732  -2880  -5155   1953
ATOM   4262  C   MET A 566      77.828  37.362   6.722  1.00196.84           C  
ANISOU 4262  C   MET A 566    21233  22382  31174  -2855  -4986   1809
ATOM   4263  O   MET A 566      77.873  36.773   5.637  1.00197.36           O  
ANISOU 4263  O   MET A 566    20891  22533  31562  -2634  -4673   1448
ATOM   4264  CB  MET A 566      77.229  35.941   8.666  1.00192.34           C  
ANISOU 4264  CB  MET A 566    20780  21338  30963  -2947  -5539   2259
ATOM   4265  CG  MET A 566      76.481  35.788   9.974  1.00190.68           C  
ANISOU 4265  CG  MET A 566    20995  20973  30482  -3111  -5837   2557
ATOM   4266  SD  MET A 566      76.789  37.177  11.077  1.00190.31           S  
ANISOU 4266  SD  MET A 566    21536  20977  29796  -3509  -6136   2954
ATOM   4267  CE  MET A 566      78.513  36.899  11.486  1.00189.59           C  
ANISOU 4267  CE  MET A 566    20974  20703  30357  -3719  -6546   3348
ATOM   4268  N   ASN A 567      78.718  38.287   7.075  1.00195.92           N  
ANISOU 4268  N   ASN A 567    21222  22316  30903  -3099  -5189   2086
ATOM   4269  CA  ASN A 567      79.891  38.593   6.259  1.00197.79           C  
ANISOU 4269  CA  ASN A 567    21047  22700  31405  -3122  -5083   2021
ATOM   4270  C   ASN A 567      81.138  37.940   6.856  1.00196.59           C  
ANISOU 4270  C   ASN A 567    20435  22310  31950  -3225  -5424   2337
ATOM   4271  O   ASN A 567      82.003  38.618   7.413  1.00196.91           O  
ANISOU 4271  O   ASN A 567    20549  22331  31937  -3479  -5710   2689
ATOM   4272  CB  ASN A 567      80.087  40.107   6.142  1.00198.89           C  
ANISOU 4272  CB  ASN A 567    21580  23066  30924  -3329  -5079   2121
ATOM   4273  CG  ASN A 567      81.170  40.487   5.146  1.00200.64           C  
ANISOU 4273  CG  ASN A 567    21393  23505  31335  -3356  -4913   2016
ATOM   4274  OD1 ASN A 567      81.800  39.627   4.530  1.00201.34           O  
ANISOU 4274  OD1 ASN A 567    20891  23584  32025  -3214  -4770   1841
ATOM   4275  ND2 ASN A 567      81.394  41.787   4.990  1.00201.10           N  
ANISOU 4275  ND2 ASN A 567    21759  23761  30890  -3546  -4930   2117
ATOM   4276  N   VAL A 594      77.021  34.292  25.687  1.00229.53           N  
ANISOU 4276  N   VAL A 594    29047  24774  33390  -7776 -10846   7689
ATOM   4277  CA  VAL A 594      76.659  33.903  27.043  1.00232.34           C  
ANISOU 4277  CA  VAL A 594    29739  25229  33313  -8125 -11132   8043
ATOM   4278  C   VAL A 594      75.680  32.731  26.962  1.00231.66           C  
ANISOU 4278  C   VAL A 594    29441  25092  33490  -7967 -11077   7968
ATOM   4279  O   VAL A 594      74.977  32.575  25.964  1.00228.25           O  
ANISOU 4279  O   VAL A 594    28821  24616  33288  -7671 -10744   7556
ATOM   4280  CB  VAL A 594      76.059  35.094  27.825  1.00231.79           C  
ANISOU 4280  CB  VAL A 594    30432  25398  32241  -8539 -11030   7964
ATOM   4281  CG1 VAL A 594      75.778  34.717  29.276  1.00235.30           C  
ANISOU 4281  CG1 VAL A 594    31212  25991  32202  -8949 -11343   8334
ATOM   4282  CG2 VAL A 594      76.972  36.306  27.742  1.00232.04           C  
ANISOU 4282  CG2 VAL A 594    30665  25462  32035  -8648 -11046   7977
ATOM   4283  N   SER A 595      75.639  31.910  28.009  1.00242.32           N  
ANISOU 4283  N   SER A 595    30819  26455  34798  -8173 -11424   8376
ATOM   4284  CA  SER A 595      74.771  30.742  28.037  1.00242.95           C  
ANISOU 4284  CA  SER A 595    30699  26483  35129  -8049 -11430   8373
ATOM   4285  C   SER A 595      73.302  31.168  28.114  1.00241.47           C  
ANISOU 4285  C   SER A 595    30970  26502  34274  -8195 -11099   8038
ATOM   4286  O   SER A 595      72.965  32.356  28.140  1.00239.94           O  
ANISOU 4286  O   SER A 595    31254  26463  33449  -8380 -10855   7798
ATOM   4287  CB  SER A 595      75.146  29.839  29.209  1.00247.05           C  
ANISOU 4287  CB  SER A 595    31174  26978  35716  -8280 -11920   8938
ATOM   4288  OG  SER A 595      76.458  29.326  29.058  1.00249.68           O  
ANISOU 4288  OG  SER A 595    31036  27061  36769  -8098 -12217   9244
ATOM   4289  N   TYR A 596      72.410  30.173  28.154  1.00244.28           N  
ANISOU 4289  N   TYR A 596    31183  26842  34788  -8107 -11089   8026
ATOM   4290  CA  TYR A 596      70.980  30.465  28.108  1.00241.99           C  
ANISOU 4290  CA  TYR A 596    31256  26722  33967  -8198 -10755   7695
ATOM   4291  C   TYR A 596      70.433  30.829  29.484  1.00243.96           C  
ANISOU 4291  C   TYR A 596    32106  27236  33352  -8732 -10864   7914
ATOM   4292  O   TYR A 596      69.663  31.787  29.613  1.00242.02           O  
ANISOU 4292  O   TYR A 596    32370  27211  32374  -8824 -10493   7600
ATOM   4293  CB  TYR A 596      70.211  29.276  27.520  1.00240.95           C  
ANISOU 4293  CB  TYR A 596    30720  26488  34343  -7853 -10667   7562
ATOM   4294  CG  TYR A 596      70.123  28.052  28.414  1.00243.93           C  
ANISOU 4294  CG  TYR A 596    30955  26835  34893  -8005 -11060   8013
ATOM   4295  CD1 TYR A 596      71.124  27.090  28.418  1.00245.53           C  
ANISOU 4295  CD1 TYR A 596    30671  26791  35827  -7816 -11409   8350
ATOM   4296  CD2 TYR A 596      69.018  27.848  29.234  1.00244.77           C  
ANISOU 4296  CD2 TYR A 596    31415  27155  34430  -8315 -11058   8095
ATOM   4297  CE1 TYR A 596      71.037  25.972  29.229  1.00248.22           C  
ANISOU 4297  CE1 TYR A 596    30905  27083  36323  -7932 -11770   8777
ATOM   4298  CE2 TYR A 596      68.923  26.735  30.047  1.00246.56           C  
ANISOU 4298  CE2 TYR A 596    31522  27377  34782  -8448 -11416   8519
ATOM   4299  CZ  TYR A 596      69.934  25.800  30.040  1.00248.76           C  
ANISOU 4299  CZ  TYR A 596    31336  27390  35790  -8252 -11781   8867
ATOM   4300  OH  TYR A 596      69.840  24.690  30.847  1.00252.84           O  
ANISOU 4300  OH  TYR A 596    31755  27870  36445  -8385 -12154   9313
ATOM   4301  N   LYS A 597      70.817  30.083  30.519  1.00237.88           N  
ANISOU 4301  N   LYS A 597    31292  26502  32589  -8968 -11292   8405
ATOM   4302  CA  LYS A 597      70.324  30.317  31.869  1.00240.23           C  
ANISOU 4302  CA  LYS A 597    32122  27083  32072  -9507 -11429   8631
ATOM   4303  C   LYS A 597      71.195  31.311  32.631  1.00243.57           C  
ANISOU 4303  C   LYS A 597    32923  27630  31993  -9865 -11606   8814
ATOM   4304  O   LYS A 597      70.909  31.611  33.795  1.00247.10           O  
ANISOU 4304  O   LYS A 597    33839  28333  31716 -10355 -11733   8986
ATOM   4305  CB  LYS A 597      70.230  28.981  32.622  1.00241.21           C  
ANISOU 4305  CB  LYS A 597    32021  27207  32419  -9609 -11827   9082
ATOM   4306  CG  LYS A 597      69.432  29.018  33.921  1.00243.16           C  
ANISOU 4306  CG  LYS A 597    32768  27784  31836 -10157 -11922   9267
ATOM   4307  CD  LYS A 597      67.961  29.288  33.638  1.00239.87           C  
ANISOU 4307  CD  LYS A 597    32621  27517  31001 -10184 -11456   8840
ATOM   4308  CE  LYS A 597      67.140  29.330  34.915  1.00242.86           C  
ANISOU 4308  CE  LYS A 597    33489  28244  30544 -10750 -11508   8994
ATOM   4309  NZ  LYS A 597      67.066  28.000  35.577  1.00246.44           N1+
ANISOU 4309  NZ  LYS A 597    33686  28723  31225 -10848 -11924   9462
ATOM   4310  N   GLU A 598      72.239  31.840  31.993  1.00244.48           N  
ANISOU 4310  N   GLU A 598    32847  27583  32460  -9646 -11613   8766
ATOM   4311  CA  GLU A 598      73.086  32.864  32.588  1.00246.12           C  
ANISOU 4311  CA  GLU A 598    33401  27895  32219  -9949 -11764   8903
ATOM   4312  C   GLU A 598      72.677  34.277  32.192  1.00243.23           C  
ANISOU 4312  C   GLU A 598    33502  27610  31305 -10005 -11331   8446
ATOM   4313  O   GLU A 598      73.171  35.238  32.789  1.00244.91           O  
ANISOU 4313  O   GLU A 598    34118  27941  30998 -10314 -11415   8509
ATOM   4314  CB  GLU A 598      74.552  32.619  32.208  1.00246.78           C  
ANISOU 4314  CB  GLU A 598    33004  27756  33005  -9708 -12067   9176
ATOM   4315  CG  GLU A 598      75.129  31.346  32.812  1.00249.67           C  
ANISOU 4315  CG  GLU A 598    32991  28019  33853  -9723 -12565   9705
ATOM   4316  CD  GLU A 598      76.564  31.093  32.397  1.00250.35           C  
ANISOU 4316  CD  GLU A 598    32589  27848  34684  -9468 -12833   9962
ATOM   4317  OE1 GLU A 598      77.077  31.838  31.535  1.00247.97           O  
ANISOU 4317  OE1 GLU A 598    32189  27458  34568  -9251 -12606   9704
ATOM   4318  OE2 GLU A 598      77.179  30.147  32.932  1.00253.48           O1-
ANISOU 4318  OE2 GLU A 598    32699  28124  35487  -9492 -13271  10432
ATOM   4319  N   LEU A 599      71.796  34.425  31.204  1.00241.74           N  
ANISOU 4319  N   LEU A 599    33275  27351  31226  -9715 -10890   7993
ATOM   4320  CA  LEU A 599      71.141  35.692  30.889  1.00238.86           C  
ANISOU 4320  CA  LEU A 599    33395  27113  30247  -9665 -10399   7508
ATOM   4321  C   LEU A 599      69.631  35.513  30.878  1.00236.89           C  
ANISOU 4321  C   LEU A 599    33343  27074  29590  -9470  -9950   7144
ATOM   4322  O   LEU A 599      68.930  35.935  29.956  1.00234.72           O  
ANISOU 4322  O   LEU A 599    33070  26866  29246  -8949  -9416   6635
ATOM   4323  CB  LEU A 599      71.609  36.284  29.563  1.00235.41           C  
ANISOU 4323  CB  LEU A 599    32703  26575  30168  -9103 -10085   7153
ATOM   4324  CG  LEU A 599      73.002  36.911  29.537  1.00236.93           C  
ANISOU 4324  CG  LEU A 599    32844  26629  30549  -9279 -10388   7394
ATOM   4325  CD1 LEU A 599      73.334  37.401  28.137  1.00233.42           C  
ANISOU 4325  CD1 LEU A 599    32107  26122  30459  -8699 -10033   7014
ATOM   4326  CD2 LEU A 599      73.095  38.048  30.543  1.00239.00           C  
ANISOU 4326  CD2 LEU A 599    33777  27037  29995  -9792 -10457   7458
ATOM   4327  N   GLN A 600      69.112  34.860  31.920  1.00236.21           N  
ANISOU 4327  N   GLN A 600    33414  27099  29235  -9914 -10184   7429
ATOM   4328  CA  GLN A 600      67.671  34.835  32.141  1.00238.49           C  
ANISOU 4328  CA  GLN A 600    33985  27636  28995  -9846  -9768   7114
ATOM   4329  C   GLN A 600      67.116  36.237  32.359  1.00241.53           C  
ANISOU 4329  C   GLN A 600    34978  28239  28553  -9878  -9302   6679
ATOM   4330  O   GLN A 600      65.915  36.459  32.167  1.00244.33           O  
ANISOU 4330  O   GLN A 600    35515  28769  28552  -9625  -8809   6265
ATOM   4331  CB  GLN A 600      67.350  33.942  33.344  1.00238.98           C  
ANISOU 4331  CB  GLN A 600    34131  27801  28867 -10423 -10162   7561
ATOM   4332  CG  GLN A 600      65.869  33.707  33.599  1.00239.93           C  
ANISOU 4332  CG  GLN A 600    34460  28181  28520 -10376  -9779   7300
ATOM   4333  CD  GLN A 600      65.622  32.821  34.805  1.00241.63           C  
ANISOU 4333  CD  GLN A 600    34751  28519  28539 -11002 -10206   7783
ATOM   4334  OE1 GLN A 600      66.558  32.420  35.497  1.00242.83           O  
ANISOU 4334  OE1 GLN A 600    34813  28601  28849 -11409 -10772   8295
ATOM   4335  NE2 GLN A 600      64.357  32.511  35.063  1.00241.91           N  
ANISOU 4335  NE2 GLN A 600    34925  28790  28199 -10994  -9909   7605
ATOM   4336  N   ASP A 601      67.971  37.188  32.735  1.00244.68           N  
ANISOU 4336  N   ASP A 601    35678  28612  28676 -10173  -9454   6762
ATOM   4337  CA  ASP A 601      67.558  38.560  33.032  1.00245.24           C  
ANISOU 4337  CA  ASP A 601    36344  28854  27980 -10258  -9071   6372
ATOM   4338  C   ASP A 601      67.604  39.434  31.776  1.00245.27           C  
ANISOU 4338  C   ASP A 601    36262  28768  28162  -9648  -8650   5906
ATOM   4339  O   ASP A 601      68.298  40.448  31.704  1.00244.41           O  
ANISOU 4339  O   ASP A 601    36369  28603  27894  -9711  -8669   5844
ATOM   4340  CB  ASP A 601      68.431  39.134  34.144  1.00244.30           C  
ANISOU 4340  CB  ASP A 601    36630  28756  27438 -10940  -9480   6714
ATOM   4341  CG  ASP A 601      69.913  39.125  33.792  1.00243.06           C  
ANISOU 4341  CG  ASP A 601    36157  28341  27852 -10972  -9931   7077
ATOM   4342  OD1 ASP A 601      70.275  38.610  32.713  1.00240.61           O  
ANISOU 4342  OD1 ASP A 601    35294  27847  28282 -10476  -9926   7061
ATOM   4343  OD2 ASP A 601      70.718  39.639  34.597  1.00244.93           O1-
ANISOU 4343  OD2 ASP A 601    36699  28567  27795 -11504 -10286   7372
ATOM   4344  N   SER A 602      66.830  39.027  30.774  1.00244.08           N  
ANISOU 4344  N   SER A 602    35795  28609  28336  -9070  -8279   5589
ATOM   4345  CA  SER A 602      66.722  39.806  29.550  1.00240.18           C  
ANISOU 4345  CA  SER A 602    35217  28058  27983  -8503  -7860   5141
ATOM   4346  C   SER A 602      65.909  41.075  29.810  1.00239.83           C  
ANISOU 4346  C   SER A 602    35736  28171  27219  -8507  -7413   4698
ATOM   4347  O   SER A 602      65.477  41.356  30.932  1.00242.71           O  
ANISOU 4347  O   SER A 602    36553  28692  26975  -8946  -7409   4714
ATOM   4348  CB  SER A 602      66.099  38.964  28.439  1.00236.75           C  
ANISOU 4348  CB  SER A 602    34297  27576  28081  -7933  -7612   4947
ATOM   4349  OG  SER A 602      64.757  38.630  28.744  1.00236.38           O  
ANISOU 4349  OG  SER A 602    34397  27700  27718  -7887  -7317   4756
ATOM   4350  N   THR A 603      65.688  41.851  28.751  1.00244.01           N  
ANISOU 4350  N   THR A 603    36229  28655  27828  -8021  -7030   4290
ATOM   4351  CA  THR A 603      64.938  43.096  28.862  1.00245.18           C  
ANISOU 4351  CA  THR A 603    36857  28900  27400  -7961  -6605   3846
ATOM   4352  C   THR A 603      63.448  42.774  28.992  1.00246.35           C  
ANISOU 4352  C   THR A 603    37087  29209  27306  -7798  -6200   3560
ATOM   4353  O   THR A 603      63.052  41.618  29.162  1.00245.76           O  
ANISOU 4353  O   THR A 603    36761  29189  27428  -7821  -6297   3749
ATOM   4354  CB  THR A 603      65.239  44.008  27.675  1.00245.34           C  
ANISOU 4354  CB  THR A 603    36783  28806  27630  -7524  -6386   3558
ATOM   4355  OG1 THR A 603      64.866  43.354  26.457  1.00245.97           O  
ANISOU 4355  OG1 THR A 603    36377  28842  28236  -6992  -6188   3422
ATOM   4356  CG2 THR A 603      66.723  44.350  27.629  1.00243.83           C  
ANISOU 4356  CG2 THR A 603    36523  28478  27643  -7728  -6793   3861
ATOM   4357  N   GLN A 604      62.599  43.798  28.917  1.00242.66           N  
ANISOU 4357  N   GLN A 604    36962  28808  26431  -7635  -5751   3106
ATOM   4358  CA  GLN A 604      61.179  43.629  29.224  1.00243.96           C  
ANISOU 4358  CA  GLN A 604    37265  29139  26291  -7552  -5357   2831
ATOM   4359  C   GLN A 604      60.523  42.764  28.149  1.00244.55           C  
ANISOU 4359  C   GLN A 604    36857  29188  26874  -7032  -5171   2748
ATOM   4360  O   GLN A 604      60.256  43.211  27.032  1.00244.81           O  
ANISOU 4360  O   GLN A 604    36733  29135  27147  -6553  -4892   2457
ATOM   4361  CB  GLN A 604      60.499  44.989  29.379  1.00244.12           C  
ANISOU 4361  CB  GLN A 604    37740  29197  25819  -7490  -4931   2355
ATOM   4362  CG  GLN A 604      60.493  45.900  28.157  1.00243.29           C  
ANISOU 4362  CG  GLN A 604    37542  28937  25960  -6989  -4675   2028
ATOM   4363  CD  GLN A 604      59.862  47.248  28.445  1.00244.13           C  
ANISOU 4363  CD  GLN A 604    38110  29046  25602  -6981  -4307   1586
ATOM   4364  OE1 GLN A 604      59.448  47.524  29.571  1.00245.28           O  
ANISOU 4364  OE1 GLN A 604    38657  29317  25220  -7351  -4214   1490
ATOM   4365  NE2 GLN A 604      59.765  48.087  27.421  1.00243.82           N  
ANISOU 4365  NE2 GLN A 604    38008  28868  25764  -6568  -4092   1305
ATOM   4366  N   MET A 605      60.282  41.500  28.493  1.00244.34           N  
ANISOU 4366  N   MET A 605    36592  29231  27014  -7154  -5354   3025
ATOM   4367  CA  MET A 605      59.645  40.532  27.611  1.00244.72           C  
ANISOU 4367  CA  MET A 605    36194  29259  27530  -6726  -5225   2986
ATOM   4368  C   MET A 605      59.280  39.302  28.428  1.00245.12           C  
ANISOU 4368  C   MET A 605    36144  29425  27566  -7028  -5448   3306
ATOM   4369  O   MET A 605      60.023  38.909  29.331  1.00245.45           O  
ANISOU 4369  O   MET A 605    36251  29477  27533  -7514  -5878   3700
ATOM   4370  CB  MET A 605      60.558  40.152  26.436  1.00243.75           C  
ANISOU 4370  CB  MET A 605    35599  28937  28079  -6392  -5414   3096
ATOM   4371  CG  MET A 605      61.883  39.529  26.828  1.00242.52           C  
ANISOU 4371  CG  MET A 605    35249  28669  28229  -6721  -5968   3570
ATOM   4372  SD  MET A 605      62.928  39.211  25.393  1.00241.94           S  
ANISOU 4372  SD  MET A 605    34616  28376  28935  -6301  -6103   3613
ATOM   4373  CE  MET A 605      63.424  40.873  24.954  1.00241.73           C  
ANISOU 4373  CE  MET A 605    34895  28319  28633  -6213  -5908   3333
ATOM   4374  N   ASN A 606      58.134  38.708  28.111  1.00239.78           N  
ANISOU 4374  N   ASN A 606    35306  28834  26963  -6760  -5176   3157
ATOM   4375  CA  ASN A 606      57.609  37.592  28.882  1.00240.03           C  
ANISOU 4375  CA  ASN A 606    35263  29001  26936  -7039  -5344   3431
ATOM   4376  C   ASN A 606      58.152  36.271  28.352  1.00238.47           C  
ANISOU 4376  C   ASN A 606    34535  28642  27431  -6915  -5727   3776
ATOM   4377  O   ASN A 606      58.402  36.113  27.154  1.00238.09           O  
ANISOU 4377  O   ASN A 606    34136  28425  27904  -6454  -5665   3655
ATOM   4378  CB  ASN A 606      56.080  37.588  28.844  1.00242.05           C  
ANISOU 4378  CB  ASN A 606    35602  29433  26932  -6828  -4869   3116
ATOM   4379  CG  ASN A 606      55.471  36.630  29.851  1.00242.61           C  
ANISOU 4379  CG  ASN A 606    35698  29703  26780  -7214  -5012   3386
ATOM   4380  OD1 ASN A 606      56.180  35.921  30.565  1.00241.39           O  
ANISOU 4380  OD1 ASN A 606    35488  29545  26684  -7645  -5492   3828
ATOM   4381  ND2 ASN A 606      54.146  36.616  29.922  1.00244.19           N  
ANISOU 4381  ND2 ASN A 606    35974  30080  26727  -7079  -4606   3136
ATOM   4382  N   GLU A 607      58.325  35.314  29.265  1.00238.48           N  
ANISOU 4382  N   GLU A 607    34479  28697  27437  -7350  -6129   4203
ATOM   4383  CA  GLU A 607      58.894  34.009  28.953  1.00237.00           C  
ANISOU 4383  CA  GLU A 607    33796  28331  27924  -7310  -6563   4577
ATOM   4384  C   GLU A 607      57.869  33.021  28.404  1.00236.95           C  
ANISOU 4384  C   GLU A 607    33474  28341  28214  -6978  -6408   4507
ATOM   4385  O   GLU A 607      58.109  31.810  28.465  1.00235.26           O  
ANISOU 4385  O   GLU A 607    32908  28019  28460  -7058  -6791   4854
ATOM   4386  CB  GLU A 607      59.572  33.419  30.194  1.00236.90           C  
ANISOU 4386  CB  GLU A 607    33849  28341  27822  -7960  -7125   5114
ATOM   4387  CG  GLU A 607      60.820  34.169  30.641  1.00237.04           C  
ANISOU 4387  CG  GLU A 607    34073  28278  27714  -8296  -7408   5286
ATOM   4388  CD  GLU A 607      61.455  33.564  31.880  1.00235.49           C  
ANISOU 4388  CD  GLU A 607    33943  28105  27427  -8977  -7992   5852
ATOM   4389  OE1 GLU A 607      60.856  32.639  32.467  1.00235.13           O  
ANISOU 4389  OE1 GLU A 607    33829  28170  27337  -9219  -8152   6094
ATOM   4390  OE2 GLU A 607      62.554  34.015  32.268  1.00233.98           O1-
ANISOU 4390  OE2 GLU A 607    33868  27823  27210  -9289  -8310   6077
ATOM   4391  N   LYS A 608      56.734  33.498  27.886  1.00239.21           N  
ANISOU 4391  N   LYS A 608    33872  28745  28272  -6619  -5879   4083
ATOM   4392  CA  LYS A 608      55.756  32.593  27.289  1.00240.14           C  
ANISOU 4392  CA  LYS A 608    33689  28870  28684  -6287  -5728   4013
ATOM   4393  C   LYS A 608      56.324  31.920  26.044  1.00239.03           C  
ANISOU 4393  C   LYS A 608    33045  28465  29310  -5856  -5860   4016
ATOM   4394  O   LYS A 608      56.454  30.692  25.990  1.00237.61           O  
ANISOU 4394  O   LYS A 608    32508  28173  29601  -5871  -6186   4296
ATOM   4395  CB  LYS A 608      54.467  33.350  26.958  1.00241.80           C  
ANISOU 4395  CB  LYS A 608    34122  29244  28508  -5992  -5133   3559
ATOM   4396  CG  LYS A 608      53.664  33.778  28.177  1.00242.13           C  
ANISOU 4396  CG  LYS A 608    34594  29568  27834  -6390  -4950   3525
ATOM   4397  CD  LYS A 608      52.377  34.483  27.772  1.00242.66           C  
ANISOU 4397  CD  LYS A 608    34815  29762  27623  -6050  -4354   3067
ATOM   4398  CE  LYS A 608      51.563  34.899  28.989  1.00243.34           C  
ANISOU 4398  CE  LYS A 608    35308  30138  27012  -6441  -4131   2993
ATOM   4399  NZ  LYS A 608      50.311  35.609  28.609  1.00245.09           N1+
ANISOU 4399  NZ  LYS A 608    35649  30460  27015  -6099  -3544   2540
ATOM   4400  N   GLU A 609      56.672  32.712  25.031  1.00227.15           N  
ANISOU 4400  N   GLU A 609    31503  26859  27946  -5481  -5612   3699
ATOM   4401  CA  GLU A 609      57.362  32.206  23.852  1.00225.60           C  
ANISOU 4401  CA  GLU A 609    30853  26433  28434  -5113  -5718   3670
ATOM   4402  C   GLU A 609      58.833  32.589  23.816  1.00224.40           C  
ANISOU 4402  C   GLU A 609    30638  26130  28495  -5243  -6004   3814
ATOM   4403  O   GLU A 609      59.549  32.150  22.911  1.00222.70           O  
ANISOU 4403  O   GLU A 609    30023  25725  28868  -4982  -6115   3807
ATOM   4404  CB  GLU A 609      56.675  32.686  22.569  1.00226.17           C  
ANISOU 4404  CB  GLU A 609    30856  26508  28573  -4583  -5239   3221
ATOM   4405  CG  GLU A 609      55.321  32.049  22.306  1.00226.51           C  
ANISOU 4405  CG  GLU A 609    30810  26636  28617  -4367  -5005   3106
ATOM   4406  CD  GLU A 609      54.712  32.501  20.992  1.00226.92           C  
ANISOU 4406  CD  GLU A 609    30775  26673  28773  -3869  -4579   2701
ATOM   4407  OE1 GLU A 609      55.283  33.408  20.352  1.00226.10           O  
ANISOU 4407  OE1 GLU A 609    30721  26518  28669  -3717  -4443   2498
ATOM   4408  OE2 GLU A 609      53.668  31.943  20.595  1.00227.68           O1-
ANISOU 4408  OE2 GLU A 609    30748  26810  28950  -3651  -4399   2606
ATOM   4409  N   LEU A 610      59.302  33.402  24.766  1.00233.89           N  
ANISOU 4409  N   LEU A 610    32219  27414  29236  -5645  -6116   3933
ATOM   4410  CA  LEU A 610      60.727  33.706  24.840  1.00232.27           C  
ANISOU 4410  CA  LEU A 610    31950  27063  29237  -5822  -6443   4135
ATOM   4411  C   LEU A 610      61.539  32.452  25.133  1.00229.57           C  
ANISOU 4411  C   LEU A 610    31212  26542  29473  -6019  -6983   4585
ATOM   4412  O   LEU A 610      62.569  32.200  24.496  1.00226.62           O  
ANISOU 4412  O   LEU A 610    30478  25965  29662  -5872  -7179   4660
ATOM   4413  CB  LEU A 610      60.987  34.767  25.906  1.00232.38           C  
ANISOU 4413  CB  LEU A 610    32483  27206  28606  -6264  -6482   4197
ATOM   4414  CG  LEU A 610      62.463  35.127  26.080  1.00230.74           C  
ANISOU 4414  CG  LEU A 610    32243  26856  28572  -6499  -6851   4445
ATOM   4415  CD1 LEU A 610      63.018  35.737  24.802  1.00230.39           C  
ANISOU 4415  CD1 LEU A 610    32001  26695  28842  -6065  -6646   4166
ATOM   4416  CD2 LEU A 610      62.665  36.051  27.270  1.00230.37           C  
ANISOU 4416  CD2 LEU A 610    32734  26940  27857  -7007  -6937   4546
ATOM   4417  N   THR A 611      61.087  31.649  26.100  1.00232.71           N  
ANISOU 4417  N   THR A 611    31653  27009  29756  -6364  -7234   4892
ATOM   4418  CA  THR A 611      61.808  30.434  26.462  1.00230.37           C  
ANISOU 4418  CA  THR A 611    30980  26523  30027  -6589  -7793   5359
ATOM   4419  C   THR A 611      61.860  29.432  25.315  1.00228.89           C  
ANISOU 4419  C   THR A 611    30227  26116  30624  -6118  -7801   5267
ATOM   4420  O   THR A 611      62.773  28.599  25.277  1.00226.82           O  
ANISOU 4420  O   THR A 611    29562  25613  31004  -6181  -8232   5569
ATOM   4421  CB  THR A 611      61.171  29.791  27.698  1.00231.23           C  
ANISOU 4421  CB  THR A 611    31266  26781  29810  -7065  -8041   5699
ATOM   4422  OG1 THR A 611      61.985  28.702  28.150  1.00228.65           O  
ANISOU 4422  OG1 THR A 611    30595  26248  30034  -7354  -8657   6211
ATOM   4423  CG2 THR A 611      59.772  29.277  27.383  1.00232.94           C  
ANISOU 4423  CG2 THR A 611    31442  27124  29941  -6797  -7716   5482
ATOM   4424  N   LYS A 612      60.914  29.498  24.380  1.00226.83           N  
ANISOU 4424  N   LYS A 612    29922  25922  30343  -5656  -7338   4854
ATOM   4425  CA  LYS A 612      60.909  28.620  23.218  1.00224.09           C  
ANISOU 4425  CA  LYS A 612    29074  25383  30688  -5203  -7292   4705
ATOM   4426  C   LYS A 612      61.804  29.123  22.093  1.00222.58           C  
ANISOU 4426  C   LYS A 612    28661  25062  30849  -4864  -7142   4447
ATOM   4427  O   LYS A 612      61.899  28.460  21.055  1.00219.85           O  
ANISOU 4427  O   LYS A 612    27897  24563  31074  -4490  -7074   4278
ATOM   4428  CB  LYS A 612      59.480  28.450  22.692  1.00225.43           C  
ANISOU 4428  CB  LYS A 612    29296  25687  30668  -4885  -6877   4394
ATOM   4429  CG  LYS A 612      58.533  27.749  23.653  1.00226.22           C  
ANISOU 4429  CG  LYS A 612    29520  25914  30519  -5170  -7017   4643
ATOM   4430  CD  LYS A 612      57.142  27.617  23.050  1.00228.06           C  
ANISOU 4430  CD  LYS A 612    29779  26272  30602  -4828  -6593   4331
ATOM   4431  CE  LYS A 612      56.206  26.853  23.971  1.00228.58           C  
ANISOU 4431  CE  LYS A 612    29928  26472  30451  -5112  -6740   4594
ATOM   4432  NZ  LYS A 612      55.916  27.608  25.222  1.00231.05           N1+
ANISOU 4432  NZ  LYS A 612    30728  27047  30015  -5570  -6703   4710
ATOM   4433  N   THR A 613      62.458  30.275  22.271  1.00219.47           N  
ANISOU 4433  N   THR A 613    28537  24732  30120  -5002  -7086   4407
ATOM   4434  CA  THR A 613      63.236  30.897  21.208  1.00217.46           C  
ANISOU 4434  CA  THR A 613    28117  24403  30104  -4704  -6905   4150
ATOM   4435  C   THR A 613      64.656  31.252  21.637  1.00214.53           C  
ANISOU 4435  C   THR A 613    27705  23920  29886  -4990  -7262   4431
ATOM   4436  O   THR A 613      65.368  31.918  20.877  1.00211.13           O  
ANISOU 4436  O   THR A 613    27187  23461  29574  -4808  -7123   4248
ATOM   4437  CB  THR A 613      62.529  32.159  20.696  1.00219.21           C  
ANISOU 4437  CB  THR A 613    28708  24823  29759  -4494  -6390   3733
ATOM   4438  OG1 THR A 613      62.410  33.107  21.764  1.00219.32           O  
ANISOU 4438  OG1 THR A 613    29237  24987  29109  -4863  -6402   3829
ATOM   4439  CG2 THR A 613      61.141  31.822  20.168  1.00221.39           C  
ANISOU 4439  CG2 THR A 613    28986  25195  29937  -4187  -6033   3457
ATOM   4440  N   ILE A 614      65.086  30.831  22.822  1.00225.95           N  
ANISOU 4440  N   ILE A 614    29208  25311  31333  -5452  -7728   4888
ATOM   4441  CA  ILE A 614      66.419  31.165  23.309  1.00224.50           C  
ANISOU 4441  CA  ILE A 614    29000  25016  31284  -5768  -8105   5203
ATOM   4442  C   ILE A 614      67.484  30.383  22.550  1.00221.63           C  
ANISOU 4442  C   ILE A 614    28017  24380  31811  -5554  -8332   5287
ATOM   4443  O   ILE A 614      68.318  30.964  21.856  1.00219.92           O  
ANISOU 4443  O   ILE A 614    27664  24118  31778  -5390  -8232   5145
ATOM   4444  CB  ILE A 614      66.539  30.910  24.820  1.00225.43           C  
ANISOU 4444  CB  ILE A 614    29363  25158  31131  -6370  -8566   5696
ATOM   4445  CG1 ILE A 614      65.520  31.755  25.585  1.00229.17           C  
ANISOU 4445  CG1 ILE A 614    30461  25921  30694  -6598  -8298   5564
ATOM   4446  CG2 ILE A 614      67.951  31.213  25.299  1.00224.15           C  
ANISOU 4446  CG2 ILE A 614    29152  24861  31155  -6710  -8993   6056
ATOM   4447  CD1 ILE A 614      65.696  33.243  25.392  1.00228.39           C  
ANISOU 4447  CD1 ILE A 614    30750  25944  30082  -6559  -7984   5279
ATOM   4448  N   THR A 661      51.786  24.070  13.630  1.00178.55           N  
ANISOU 4448  N   THR A 661    21751  19573  26517  -1582  -4630   2092
ATOM   4449  CA  THR A 661      50.864  23.823  12.523  1.00176.84           C  
ANISOU 4449  CA  THR A 661    21450  19370  26371  -1279  -4358   1828
ATOM   4450  C   THR A 661      49.807  22.725  12.775  1.00174.13           C  
ANISOU 4450  C   THR A 661    21015  18996  26150  -1280  -4490   1997
ATOM   4451  O   THR A 661      48.703  22.824  12.242  1.00173.61           O  
ANISOU 4451  O   THR A 661    21034  19030  25901  -1114  -4226   1856
ATOM   4452  CB  THR A 661      51.635  23.489  11.218  1.00174.64           C  
ANISOU 4452  CB  THR A 661    20844  18927  26584  -1027  -4306   1537
ATOM   4453  OG1 THR A 661      52.462  22.335  11.408  1.00172.56           O  
ANISOU 4453  OG1 THR A 661    20224  18415  26924  -1078  -4689   1687
ATOM   4454  CG2 THR A 661      52.500  24.669  10.795  1.00176.09           C  
ANISOU 4454  CG2 THR A 661    21131  19187  26589  -1003  -4110   1339
ATOM   4455  N   PRO A 662      50.118  21.667  13.566  1.00172.47           N  
ANISOU 4455  N   PRO A 662    20623  18642  26267  -1475  -4917   2320
ATOM   4456  CA  PRO A 662      49.033  20.765  13.981  1.00170.41           C  
ANISOU 4456  CA  PRO A 662    20333  18397  26018  -1534  -5050   2531
ATOM   4457  C   PRO A 662      48.127  21.419  15.013  1.00174.26           C  
ANISOU 4457  C   PRO A 662    21190  19161  25861  -1760  -4921   2707
ATOM   4458  O   PRO A 662      46.896  21.384  14.894  1.00176.15           O  
ANISOU 4458  O   PRO A 662    21529  19532  25869  -1677  -4717   2676
ATOM   4459  CB  PRO A 662      49.777  19.554  14.560  1.00167.63           C  
ANISOU 4459  CB  PRO A 662    19678  17801  26213  -1712  -5576   2843
ATOM   4460  CG  PRO A 662      51.082  20.088  14.997  1.00169.32           C  
ANISOU 4460  CG  PRO A 662    19902  17964  26467  -1878  -5722   2914
ATOM   4461  CD  PRO A 662      51.432  21.157  14.008  1.00171.26           C  
ANISOU 4461  CD  PRO A 662    20235  18281  26553  -1635  -5315   2511
ATOM   4462  N   GLN A 663      48.741  22.046  16.020  1.00167.84           N  
ANISOU 4462  N   GLN A 663    20579  18439  24753  -2053  -5026   2879
ATOM   4463  CA  GLN A 663      47.971  22.726  17.055  1.00172.33           C  
ANISOU 4463  CA  GLN A 663    21512  19281  24687  -2297  -4881   3009
ATOM   4464  C   GLN A 663      47.256  23.947  16.487  1.00176.50           C  
ANISOU 4464  C   GLN A 663    22298  19984  24781  -2081  -4363   2669
ATOM   4465  O   GLN A 663      46.132  24.266  16.899  1.00178.23           O  
ANISOU 4465  O   GLN A 663    22724  20403  24593  -2125  -4137   2678
ATOM   4466  CB  GLN A 663      48.897  23.111  18.209  1.00173.55           C  
ANISOU 4466  CB  GLN A 663    21826  19476  24640  -2681  -5130   3252
ATOM   4467  CG  GLN A 663      48.198  23.677  19.427  1.00177.74           C  
ANISOU 4467  CG  GLN A 663    22724  20290  24521  -3008  -5029   3407
ATOM   4468  CD  GLN A 663      49.156  23.949  20.570  1.00179.31           C  
ANISOU 4468  CD  GLN A 663    23076  20520  24534  -3434  -5324   3672
ATOM   4469  OE1 GLN A 663      50.365  23.750  20.443  1.00177.43           O  
ANISOU 4469  OE1 GLN A 663    22660  20080  24676  -3471  -5611   3757
ATOM   4470  NE2 GLN A 663      48.620  24.404  21.696  1.00182.20           N  
ANISOU 4470  NE2 GLN A 663    23770  21144  24315  -3772  -5251   3804
ATOM   4471  N   GLU A 664      47.893  24.630  15.530  1.00171.58           N  
ANISOU 4471  N   GLU A 664    21646  19284  24263  -1852  -4176   2374
ATOM   4472  CA  GLU A 664      47.245  25.728  14.818  1.00174.53           C  
ANISOU 4472  CA  GLU A 664    22214  19781  24319  -1626  -3723   2057
ATOM   4473  C   GLU A 664      45.890  25.301  14.270  1.00173.58           C  
ANISOU 4473  C   GLU A 664    22036  19709  24209  -1425  -3532   1989
ATOM   4474  O   GLU A 664      44.888  26.007  14.430  1.00175.90           O  
ANISOU 4474  O   GLU A 664    22553  20170  24110  -1395  -3230   1911
ATOM   4475  CB  GLU A 664      48.148  26.216  13.682  1.00173.83           C  
ANISOU 4475  CB  GLU A 664    22011  19578  24459  -1409  -3619   1781
ATOM   4476  CG  GLU A 664      49.451  26.849  14.138  1.00174.78           C  
ANISOU 4476  CG  GLU A 664    22212  19669  24528  -1588  -3756   1825
ATOM   4477  CD  GLU A 664      49.239  28.171  14.844  1.00179.62           C  
ANISOU 4477  CD  GLU A 664    23225  20461  24563  -1738  -3544   1789
ATOM   4478  OE1 GLU A 664      48.276  28.885  14.492  1.00182.83           O  
ANISOU 4478  OE1 GLU A 664    23804  20981  24681  -1589  -3197   1597
ATOM   4479  OE2 GLU A 664      50.036  28.497  15.749  1.00180.39           O1-
ANISOU 4479  OE2 GLU A 664    23457  20570  24512  -2012  -3731   1951
ATOM   4480  N   MET A 665      45.841  24.134  13.623  1.00171.23           N  
ANISOU 4480  N   MET A 665    21428  19252  24381  -1288  -3711   2016
ATOM   4481  CA  MET A 665      44.570  23.619  13.126  1.00169.44           C  
ANISOU 4481  CA  MET A 665    21134  19056  24188  -1122  -3579   1989
ATOM   4482  C   MET A 665      43.669  23.190  14.278  1.00169.55           C  
ANISOU 4482  C   MET A 665    21249  19213  23961  -1350  -3678   2290
ATOM   4483  O   MET A 665      42.444  23.374  14.221  1.00170.77           O  
ANISOU 4483  O   MET A 665    21501  19505  23880  -1274  -3436   2264
ATOM   4484  CB  MET A 665      44.813  22.450  12.170  1.00165.53           C  
ANISOU 4484  CB  MET A 665    20289  18339  24266   -940  -3768   1931
ATOM   4485  CG  MET A 665      45.700  22.774  10.967  1.00164.38           C  
ANISOU 4485  CG  MET A 665    20012  18073  24370   -729  -3655   1611
ATOM   4486  SD  MET A 665      45.117  24.123   9.918  1.00166.39           S  
ANISOU 4486  SD  MET A 665    20475  18478  24269   -512  -3165   1272
ATOM   4487  CE  MET A 665      46.252  25.423  10.394  1.00169.19           C  
ANISOU 4487  CE  MET A 665    21037  18900  24348   -648  -3103   1214
ATOM   4488  N   GLU A 666      44.265  22.623  15.335  1.00170.10           N  
ANISOU 4488  N   GLU A 666    21286  19258  24088  -1650  -4039   2590
ATOM   4489  CA  GLU A 666      43.496  22.184  16.497  1.00171.31           C  
ANISOU 4489  CA  GLU A 666    21532  19573  23986  -1931  -4164   2905
ATOM   4490  C   GLU A 666      42.617  23.303  17.043  1.00175.94           C  
ANISOU 4490  C   GLU A 666    22455  20437  23958  -1999  -3771   2814
ATOM   4491  O   GLU A 666      41.403  23.131  17.204  1.00176.30           O  
ANISOU 4491  O   GLU A 666    22536  20626  23825  -1985  -3615   2869
ATOM   4492  CB  GLU A 666      44.440  21.668  17.584  1.00170.52           C  
ANISOU 4492  CB  GLU A 666    21395  19422  23973  -2298  -4607   3236
ATOM   4493  CG  GLU A 666      45.138  20.367  17.239  1.00165.95           C  
ANISOU 4493  CG  GLU A 666    20443  18553  24058  -2267  -5049   3391
ATOM   4494  CD  GLU A 666      46.144  19.954  18.292  1.00165.74           C  
ANISOU 4494  CD  GLU A 666    20370  18453  24151  -2640  -5507   3736
ATOM   4495  OE1 GLU A 666      46.384  20.748  19.227  1.00169.03           O  
ANISOU 4495  OE1 GLU A 666    21067  19053  24102  -2925  -5465   3829
ATOM   4496  OE2 GLU A 666      46.699  18.841  18.183  1.00162.44           O1-
ANISOU 4496  OE2 GLU A 666    19632  17781  24307  -2658  -5919   3914
ATOM   4497  N   GLN A 667      43.210  24.462  17.334  1.00172.87           N  
ANISOU 4497  N   GLN A 667    22307  20117  23259  -2072  -3604   2669
ATOM   4498  CA  GLN A 667      42.395  25.590  17.773  1.00176.08           C  
ANISOU 4498  CA  GLN A 667    23022  20751  23128  -2103  -3203   2525
ATOM   4499  C   GLN A 667      41.767  26.365  16.621  1.00176.64           C  
ANISOU 4499  C   GLN A 667    23113  20801  23201  -1729  -2802   2188
ATOM   4500  O   GLN A 667      40.930  27.240  16.871  1.00179.21           O  
ANISOU 4500  O   GLN A 667    23647  21283  23161  -1705  -2455   2057
ATOM   4501  CB  GLN A 667      43.209  26.539  18.659  1.00178.16           C  
ANISOU 4501  CB  GLN A 667    23565  21099  23027  -2369  -3196   2513
ATOM   4502  CG  GLN A 667      43.386  26.051  20.095  1.00178.31           C  
ANISOU 4502  CG  GLN A 667    23682  21254  22815  -2829  -3484   2856
ATOM   4503  CD  GLN A 667      44.506  25.045  20.252  1.00175.51           C  
ANISOU 4503  CD  GLN A 667    23098  20710  22878  -2995  -4006   3140
ATOM   4504  OE1 GLN A 667      45.374  24.933  19.392  1.00173.89           O  
ANISOU 4504  OE1 GLN A 667    22703  20279  23087  -2787  -4120   3036
ATOM   4505  NE2 GLN A 667      44.491  24.306  21.356  1.00174.25           N  
ANISOU 4505  NE2 GLN A 667    22939  20642  22624  -3386  -4329   3506
ATOM   4506  N   THR A 668      42.141  26.073  15.372  1.00163.79           N  
ANISOU 4506  N   THR A 668    21269  18983  21982  -1454  -2842   2045
ATOM   4507  CA  THR A 668      41.425  26.642  14.237  1.00163.12           C  
ANISOU 4507  CA  THR A 668    21175  18883  21918  -1135  -2509   1780
ATOM   4508  C   THR A 668      40.058  25.991  14.053  1.00161.62           C  
ANISOU 4508  C   THR A 668    20882  18752  21773  -1036  -2424   1867
ATOM   4509  O   THR A 668      39.161  26.604  13.464  1.00161.84           O  
ANISOU 4509  O   THR A 668    20965  18827  21699   -841  -2111   1705
ATOM   4510  CB  THR A 668      42.270  26.505  12.962  1.00160.83           C  
ANISOU 4510  CB  THR A 668    20692  18402  22015   -919  -2578   1598
ATOM   4511  OG1 THR A 668      43.527  27.166  13.151  1.00163.13           O  
ANISOU 4511  OG1 THR A 668    21074  18654  22256  -1017  -2646   1530
ATOM   4512  CG2 THR A 668      41.575  27.134  11.760  1.00159.53           C  
ANISOU 4512  CG2 THR A 668    20532  18234  21849   -637  -2259   1345
ATOM   4513  N   ARG A 669      39.866  24.781  14.585  1.00165.76           N  
ANISOU 4513  N   ARG A 669    21258  19273  22451  -1185  -2714   2144
ATOM   4514  CA  ARG A 669      38.599  24.066  14.450  1.00165.31           C  
ANISOU 4514  CA  ARG A 669    21087  19270  22454  -1115  -2679   2266
ATOM   4515  C   ARG A 669      37.424  24.741  15.160  1.00168.74           C  
ANISOU 4515  C   ARG A 669    21718  19944  22452  -1186  -2358   2281
ATOM   4516  O   ARG A 669      36.312  24.204  15.092  1.00167.96           O  
ANISOU 4516  O   ARG A 669    21523  19911  22382  -1137  -2308   2396
ATOM   4517  CB  ARG A 669      38.748  22.639  14.981  1.00163.33           C  
ANISOU 4517  CB  ARG A 669    20638  18959  22461  -1302  -3106   2590
ATOM   4518  CG  ARG A 669      39.666  21.747  14.163  1.00159.18           C  
ANISOU 4518  CG  ARG A 669    19846  18161  22473  -1184  -3416   2565
ATOM   4519  CD  ARG A 669      39.753  20.360  14.780  1.00156.85           C  
ANISOU 4519  CD  ARG A 669    19353  17785  22458  -1384  -3863   2908
ATOM   4520  NE  ARG A 669      40.661  19.482  14.049  1.00152.90           N  
ANISOU 4520  NE  ARG A 669    18574  16994  22525  -1269  -4164   2865
ATOM   4521  CZ  ARG A 669      40.954  18.241  14.421  1.00149.93           C  
ANISOU 4521  CZ  ARG A 669    17975  16465  22526  -1408  -4601   3132
ATOM   4522  NH1 ARG A 669      40.409  17.730  15.517  1.00150.95           N  
ANISOU 4522  NH1 ARG A 669    18139  16725  22490  -1693  -4806   3490
ATOM   4523  NH2 ARG A 669      41.792  17.509  13.699  1.00145.90           N1+
ANISOU 4523  NH2 ARG A 669    17198  15669  22567  -1273  -4836   3038
ATOM   4524  N   SER A 670      37.618  25.876  15.834  1.00138.31           N  
ANISOU 4524  N   SER A 670    18124  16217  18210  -1301  -2137   2163
ATOM   4525  CA  SER A 670      36.542  26.545  16.563  1.00141.65           C  
ANISOU 4525  CA  SER A 670    18726  16863  18230  -1376  -1805   2136
ATOM   4526  C   SER A 670      35.958  27.733  15.812  1.00143.27           C  
ANISOU 4526  C   SER A 670    19023  17049  18365  -1098  -1393   1833
ATOM   4527  O   SER A 670      34.745  27.984  15.891  1.00145.67           O  
ANISOU 4527  O   SER A 670    19335  17466  18548  -1020  -1117   1808
ATOM   4528  CB  SER A 670      37.043  27.014  17.932  1.00143.98           C  
ANISOU 4528  CB  SER A 670    19267  17324  18116  -1728  -1819   2197
ATOM   4529  OG  SER A 670      38.013  28.037  17.793  1.00145.57           O  
ANISOU 4529  OG  SER A 670    19639  17443  18229  -1702  -1747   1979
ATOM   4530  N   ALA A 671      36.800  28.481  15.093  1.00130.99           N  
ANISOU 4530  N   ALA A 671    17523  15350  16898   -957  -1356   1615
ATOM   4531  CA  ALA A 671      36.299  29.578  14.274  1.00132.55           C  
ANISOU 4531  CA  ALA A 671    17783  15498  17081   -702  -1022   1355
ATOM   4532  C   ALA A 671      35.262  29.091  13.274  1.00131.23           C  
ANISOU 4532  C   ALA A 671    17409  15276  17176   -464   -953   1379
ATOM   4533  O   ALA A 671      34.368  29.852  12.888  1.00133.52           O  
ANISOU 4533  O   ALA A 671    17732  15576  17422   -299   -656   1251
ATOM   4534  CB  ALA A 671      37.456  30.269  13.554  1.00131.29           C  
ANISOU 4534  CB  ALA A 671    17674  15191  17017   -614  -1066   1164
ATOM   4535  N   VAL A 672      35.357  27.828  12.851  1.00123.00           N  
ANISOU 4535  N   VAL A 672    16148  14160  16426   -450  -1236   1547
ATOM   4536  CA  VAL A 672      34.303  27.241  12.030  1.00120.81           C  
ANISOU 4536  CA  VAL A 672    15687  13845  16372   -270  -1202   1608
ATOM   4537  C   VAL A 672      33.005  27.157  12.820  1.00123.15           C  
ANISOU 4537  C   VAL A 672    15999  14318  16476   -338  -1027   1753
ATOM   4538  O   VAL A 672      31.920  27.432  12.294  1.00123.44           O  
ANISOU 4538  O   VAL A 672    15978  14361  16563   -168   -809   1721
ATOM   4539  CB  VAL A 672      34.735  25.856  11.513  1.00116.16           C  
ANISOU 4539  CB  VAL A 672    14871  13127  16138   -267  -1562   1747
ATOM   4540  CG1 VAL A 672      33.615  25.216  10.707  1.00112.84           C  
ANISOU 4540  CG1 VAL A 672    14277  12669  15927   -107  -1543   1823
ATOM   4541  CG2 VAL A 672      36.004  25.968  10.692  1.00114.52           C  
ANISOU 4541  CG2 VAL A 672    14623  12756  16133   -192  -1689   1569
ATOM   4542  N   ASP A 673      33.097  26.784  14.098  1.00120.44           N  
ANISOU 4542  N   ASP A 673    15725  14129  15909   -606  -1123   1923
ATOM   4543  CA  ASP A 673      31.902  26.673  14.927  1.00123.53           C  
ANISOU 4543  CA  ASP A 673    16124  14728  16084   -710   -947   2060
ATOM   4544  C   ASP A 673      31.220  28.026  15.089  1.00128.10           C  
ANISOU 4544  C   ASP A 673    16857  15388  16426   -611   -497   1829
ATOM   4545  O   ASP A 673      30.015  28.165  14.832  1.00130.20           O  
ANISOU 4545  O   ASP A 673    17035  15699  16737   -470   -266   1833
ATOM   4546  CB  ASP A 673      32.270  26.080  16.289  1.00124.48           C  
ANISOU 4546  CB  ASP A 673    16312  15018  15966  -1072  -1150   2283
ATOM   4547  CG  ASP A 673      31.054  25.755  17.135  1.00126.86           C  
ANISOU 4547  CG  ASP A 673    16588  15565  16050  -1221  -1009   2461
ATOM   4548  OD1 ASP A 673      30.379  24.743  16.846  1.00124.77           O  
ANISOU 4548  OD1 ASP A 673    16115  15295  15995  -1187  -1168   2683
ATOM   4549  OD2 ASP A 673      30.778  26.511  18.090  1.00130.54           O1-
ANISOU 4549  OD2 ASP A 673    17237  16232  16130  -1381   -735   2371
ATOM   4550  N   GLU A 674      31.979  29.049  15.494  1.00128.54           N  
ANISOU 4550  N   GLU A 674    17135  15446  16260   -678   -377   1624
ATOM   4551  CA  GLU A 674      31.342  30.346  15.707  1.00132.85           C  
ANISOU 4551  CA  GLU A 674    17825  16044  16608   -588     45   1385
ATOM   4552  C   GLU A 674      30.905  30.984  14.393  1.00132.21           C  
ANISOU 4552  C   GLU A 674    17653  15776  16806   -256    201   1225
ATOM   4553  O   GLU A 674      29.885  31.682  14.358  1.00135.89           O  
ANISOU 4553  O   GLU A 674    18110  16264  17258   -125    524   1120
ATOM   4554  CB  GLU A 674      32.265  31.284  16.487  1.00135.30           C  
ANISOU 4554  CB  GLU A 674    18409  16389  16609   -759    118   1204
ATOM   4555  CG  GLU A 674      31.597  32.604  16.866  1.00140.63           C  
ANISOU 4555  CG  GLU A 674    19243  17115  17076   -692    558    936
ATOM   4556  CD  GLU A 674      32.444  33.457  17.790  1.00142.32           C  
ANISOU 4556  CD  GLU A 674    19751  17384  16940   -908    626    764
ATOM   4557  OE1 GLU A 674      33.557  33.024  18.151  1.00139.16           O  
ANISOU 4557  OE1 GLU A 674    19430  16992  16453  -1123    318    882
ATOM   4558  OE2 GLU A 674      31.992  34.563  18.157  1.00145.67           O1-
ANISOU 4558  OE2 GLU A 674    20323  17831  17194   -867    981    511
ATOM   4559  N   ASP A 675      31.643  30.750  13.303  1.00129.44           N  
ANISOU 4559  N   ASP A 675    17220  15243  16718   -132    -23   1209
ATOM   4560  CA  ASP A 675      31.181  31.213  11.998  1.00128.46           C  
ANISOU 4560  CA  ASP A 675    16995  14962  16852    136     81   1106
ATOM   4561  C   ASP A 675      29.876  30.537  11.596  1.00126.92           C  
ANISOU 4561  C   ASP A 675    16593  14789  16840    246    123   1276
ATOM   4562  O   ASP A 675      29.032  31.160  10.941  1.00126.97           O  
ANISOU 4562  O   ASP A 675    16541  14726  16977    429    327   1209
ATOM   4563  CB  ASP A 675      32.252  30.978  10.931  1.00124.71           C  
ANISOU 4563  CB  ASP A 675    16467  14327  16591    201   -170   1057
ATOM   4564  CG  ASP A 675      33.409  31.956  11.039  1.00126.74           C  
ANISOU 4564  CG  ASP A 675    16914  14531  16709    152   -155    860
ATOM   4565  OD1 ASP A 675      33.189  33.093  11.508  1.00131.53           O  
ANISOU 4565  OD1 ASP A 675    17688  15162  17126    156     97    708
ATOM   4566  OD2 ASP A 675      34.538  31.591  10.647  1.00124.26           O1-
ANISOU 4566  OD2 ASP A 675    16574  14146  16494    110   -394    851
ATOM   4567  N   ARG A 676      29.689  29.271  11.977  1.00121.85           N  
ANISOU 4567  N   ARG A 676    15831  14235  16232    125    -90   1515
ATOM   4568  CA  ARG A 676      28.400  28.627  11.749  1.00121.10           C  
ANISOU 4568  CA  ARG A 676    15550  14184  16279    200    -50   1702
ATOM   4569  C   ARG A 676      27.308  29.265  12.595  1.00127.12           C  
ANISOU 4569  C   ARG A 676    16348  15106  16844    183    306   1681
ATOM   4570  O   ARG A 676      26.173  29.427  12.131  1.00127.99           O  
ANISOU 4570  O   ARG A 676    16327  15196  17108    339    479   1721
ATOM   4571  CB  ARG A 676      28.485  27.130  12.040  1.00117.60           C  
ANISOU 4571  CB  ARG A 676    14975  13793  15916     52   -383   1974
ATOM   4572  CG  ARG A 676      29.263  26.340  11.012  1.00111.60           C  
ANISOU 4572  CG  ARG A 676    14106  12846  15451    119   -711   1992
ATOM   4573  CD  ARG A 676      29.241  24.861  11.337  1.00110.67           C  
ANISOU 4573  CD  ARG A 676    13840  12750  15459    -19  -1046   2264
ATOM   4574  NE  ARG A 676      29.950  24.068  10.340  1.00106.89           N  
ANISOU 4574  NE  ARG A 676    13239  12073  15301     57  -1342   2246
ATOM   4575  CZ  ARG A 676      30.104  22.751  10.414  1.00105.57           C  
ANISOU 4575  CZ  ARG A 676    12924  11852  15336    -32  -1680   2445
ATOM   4576  NH1 ARG A 676      29.598  22.082  11.442  1.00107.63           N  
ANISOU 4576  NH1 ARG A 676    13145  12256  15494   -218  -1789   2711
ATOM   4577  NH2 ARG A 676      30.761  22.103   9.463  1.00102.40           N1+
ANISOU 4577  NH2 ARG A 676    12408  11254  15246     54  -1911   2371
ATOM   4578  N   LYS A 677      27.624  29.625  13.843  1.00126.26           N  
ANISOU 4578  N   LYS A 677    16410  15161  16403    -18    423   1617
ATOM   4579  CA  LYS A 677      26.635  30.310  14.672  1.00131.10           C  
ANISOU 4579  CA  LYS A 677    17064  15935  16813    -42    809   1535
ATOM   4580  C   LYS A 677      26.222  31.641  14.054  1.00132.28           C  
ANISOU 4580  C   LYS A 677    17241  15933  17087    205   1122   1278
ATOM   4581  O   LYS A 677      25.032  31.982  14.032  1.00134.25           O  
ANISOU 4581  O   LYS A 677    17373  16209  17429    329   1397   1268
ATOM   4582  CB  LYS A 677      27.180  30.505  16.088  1.00133.73           C  
ANISOU 4582  CB  LYS A 677    17609  16471  16730   -338    871   1477
ATOM   4583  CG  LYS A 677      27.284  29.201  16.866  1.00132.46           C  
ANISOU 4583  CG  LYS A 677    17394  16498  16438   -622    590   1783
ATOM   4584  CD  LYS A 677      27.685  29.401  18.322  1.00134.34           C  
ANISOU 4584  CD  LYS A 677    17845  16974  16225   -968    662   1755
ATOM   4585  CE  LYS A 677      29.175  29.669  18.460  1.00132.90           C  
ANISOU 4585  CE  LYS A 677    17860  16692  15945  -1093    437   1667
ATOM   4586  NZ  LYS A 677      29.615  29.711  19.883  1.00134.14           N1+
ANISOU 4586  NZ  LYS A 677    18227  17085  15656  -1486    433   1698
ATOM   4587  N   MET A 678      27.189  32.396  13.528  1.00130.06           N  
ANISOU 4587  N   MET A 678    17095  15484  16840    276   1068   1084
ATOM   4588  CA  MET A 678      26.868  33.661  12.874  1.00131.00           C  
ANISOU 4588  CA  MET A 678    17233  15431  17111    495   1308    865
ATOM   4589  C   MET A 678      26.039  33.435  11.616  1.00128.43           C  
ANISOU 4589  C   MET A 678    16678  14961  17158    713   1262    991
ATOM   4590  O   MET A 678      25.056  34.147  11.374  1.00130.48           O  
ANISOU 4590  O   MET A 678    16849  15151  17576    872   1516    931
ATOM   4591  CB  MET A 678      28.153  34.415  12.534  1.00130.48           C  
ANISOU 4591  CB  MET A 678    17353  15226  16998    492   1202    674
ATOM   4592  CG  MET A 678      29.027  34.739  13.735  1.00133.32           C  
ANISOU 4592  CG  MET A 678    17959  15705  16991    263   1230    551
ATOM   4593  SD  MET A 678      28.268  35.848  14.935  1.00137.52           S  
ANISOU 4593  SD  MET A 678    18639  16348  17264    218   1696    307
ATOM   4594  CE  MET A 678      29.441  35.700  16.281  1.00138.59           C  
ANISOU 4594  CE  MET A 678    19054  16668  16936   -146   1580    275
ATOM   4595  N   TYR A 679      26.420  32.444  10.807  1.00122.14           N  
ANISOU 4595  N   TYR A 679    15779  14111  16519    712    936   1164
ATOM   4596  CA  TYR A 679      25.726  32.194   9.547  1.00117.19           C  
ANISOU 4596  CA  TYR A 679    14961  13349  16219    881    858   1284
ATOM   4597  C   TYR A 679      24.279  31.782   9.796  1.00118.67           C  
ANISOU 4597  C   TYR A 679    14962  13624  16503    927   1004   1469
ATOM   4598  O   TYR A 679      23.348  32.307   9.168  1.00117.93           O  
ANISOU 4598  O   TYR A 679    14745  13424  16638   1088   1151   1486
ATOM   4599  CB  TYR A 679      26.471  31.114   8.762  1.00111.44           C  
ANISOU 4599  CB  TYR A 679    14172  12565  15604    838    490   1401
ATOM   4600  CG  TYR A 679      26.018  30.942   7.333  1.00107.60           C  
ANISOU 4600  CG  TYR A 679    13539  11931  15414    974    384   1477
ATOM   4601  CD1 TYR A 679      26.440  31.822   6.347  1.00105.74           C  
ANISOU 4601  CD1 TYR A 679    13354  11546  15275   1059    391   1326
ATOM   4602  CD2 TYR A 679      25.176  29.903   6.966  1.00106.01           C  
ANISOU 4602  CD2 TYR A 679    13156  11745  15378    989    259   1712
ATOM   4603  CE1 TYR A 679      26.040  31.673   5.037  1.00102.59           C  
ANISOU 4603  CE1 TYR A 679    12837  11032  15112   1136    282   1405
ATOM   4604  CE2 TYR A 679      24.767  29.746   5.656  1.00102.70           C  
ANISOU 4604  CE2 TYR A 679    12622  11195  15204   1080    151   1784
ATOM   4605  CZ  TYR A 679      25.203  30.635   4.696  1.00101.12           C  
ANISOU 4605  CZ  TYR A 679    12483  10863  15076   1144    166   1629
ATOM   4606  OH  TYR A 679      24.803  30.491   3.388  1.00 98.37           O  
ANISOU 4606  OH  TYR A 679    12035  10403  14939   1189     49   1709
ATOM   4607  N   LEU A 680      24.071  30.845  10.724  1.00114.03           N  
ANISOU 4607  N   LEU A 680    14341  13231  15754    770    952   1630
ATOM   4608  CA  LEU A 680      22.717  30.421  11.058  1.00115.77           C  
ANISOU 4608  CA  LEU A 680    14380  13569  16039    787   1095   1820
ATOM   4609  C   LEU A 680      21.917  31.549  11.696  1.00118.40           C  
ANISOU 4609  C   LEU A 680    14722  13953  16313    859   1528   1649
ATOM   4610  O   LEU A 680      20.706  31.639  11.476  1.00119.49           O  
ANISOU 4610  O   LEU A 680    14669  14081  16653    980   1698   1747
ATOM   4611  CB  LEU A 680      22.759  29.203  11.979  1.00116.85           C  
ANISOU 4611  CB  LEU A 680    14490  13920  15985    562    925   2036
ATOM   4612  CG  LEU A 680      23.337  27.933  11.350  1.00114.73           C  
ANISOU 4612  CG  LEU A 680    14154  13579  15860    507    489   2233
ATOM   4613  CD1 LEU A 680      23.437  26.813  12.377  1.00116.21           C  
ANISOU 4613  CD1 LEU A 680    14322  13964  15868    260    299   2454
ATOM   4614  CD2 LEU A 680      22.513  27.497  10.147  1.00113.35           C  
ANISOU 4614  CD2 LEU A 680    13780  13265  16021    671    386   2392
ATOM   4615  N   GLN A 681      22.568  32.411  12.484  1.00122.98           N  
ANISOU 4615  N   GLN A 681    15513  14577  16638    785   1710   1389
ATOM   4616  CA  GLN A 681      21.905  33.614  12.986  1.00126.38           C  
ANISOU 4616  CA  GLN A 681    15963  15004  17052    878   2134   1156
ATOM   4617  C   GLN A 681      21.374  34.468  11.840  1.00124.32           C  
ANISOU 4617  C   GLN A 681    15580  14474  17182   1142   2214   1097
ATOM   4618  O   GLN A 681      20.199  34.871  11.829  1.00124.22           O  
ANISOU 4618  O   GLN A 681    15389  14431  17378   1277   2474   1105
ATOM   4619  CB  GLN A 681      22.885  34.414  13.847  1.00128.31           C  
ANISOU 4619  CB  GLN A 681    16489  15293  16970    748   2253    869
ATOM   4620  CG  GLN A 681      22.324  35.689  14.442  1.00130.51           C  
ANISOU 4620  CG  GLN A 681    16817  15553  17217    829   2697    571
ATOM   4621  CD  GLN A 681      23.313  36.378  15.364  1.00132.57           C  
ANISOU 4621  CD  GLN A 681    17381  15876  17112    659   2792    297
ATOM   4622  OE1 GLN A 681      24.454  35.938  15.508  1.00132.16           O  
ANISOU 4622  OE1 GLN A 681    17495  15869  16850    486   2507    350
ATOM   4623  NE2 GLN A 681      22.876  37.454  16.004  1.00134.58           N  
ANISOU 4623  NE2 GLN A 681    17705  16125  17305    702   3190     -1
ATOM   4624  N   ALA A 682      22.237  34.753  10.861  1.00116.11           N  
ANISOU 4624  N   ALA A 682    14622  13238  16256   1202   1982   1048
ATOM   4625  CA  ALA A 682      21.814  35.497   9.682  1.00115.22           C  
ANISOU 4625  CA  ALA A 682    14398  12873  16505   1405   1988   1038
ATOM   4626  C   ALA A 682      20.632  34.824   8.997  1.00115.02           C  
ANISOU 4626  C   ALA A 682    14102  12822  16777   1496   1927   1323
ATOM   4627  O   ALA A 682      19.697  35.499   8.550  1.00116.15           O  
ANISOU 4627  O   ALA A 682    14088  12820  17223   1654   2086   1338
ATOM   4628  CB  ALA A 682      22.985  35.645   8.712  1.00112.32           C  
ANISOU 4628  CB  ALA A 682    14154  12361  16163   1395   1698    991
ATOM   4629  N   ALA A 683      20.652  33.492   8.907  1.00113.42           N  
ANISOU 4629  N   ALA A 683    13834  12743  16517   1392   1680   1562
ATOM   4630  CA  ALA A 683      19.513  32.784   8.330  1.00111.48           C  
ANISOU 4630  CA  ALA A 683    13342  12485  16531   1454   1608   1850
ATOM   4631  C   ALA A 683      18.244  33.012   9.146  1.00115.13           C  
ANISOU 4631  C   ALA A 683    13641  13057  17047   1505   1950   1888
ATOM   4632  O   ALA A 683      17.160  33.210   8.581  1.00114.67           O  
ANISOU 4632  O   ALA A 683    13367  12891  17312   1640   2026   2027
ATOM   4633  CB  ALA A 683      19.823  31.292   8.226  1.00109.30           C  
ANISOU 4633  CB  ALA A 683    13042  12320  16168   1318   1278   2077
ATOM   4634  N   ILE A 684      18.363  32.996  10.478  1.00111.46           N  
ANISOU 4634  N   ILE A 684    13269  12813  16266   1383   2159   1768
ATOM   4635  CA  ILE A 684      17.200  33.192  11.342  1.00114.92           C  
ANISOU 4635  CA  ILE A 684    13553  13399  16713   1404   2523   1769
ATOM   4636  C   ILE A 684      16.563  34.549  11.081  1.00116.70           C  
ANISOU 4636  C   ILE A 684    13687  13420  17234   1619   2839   1570
ATOM   4637  O   ILE A 684      15.344  34.657  10.900  1.00118.45           O  
ANISOU 4637  O   ILE A 684    13650  13600  17756   1746   3007   1693
ATOM   4638  CB  ILE A 684      17.591  33.041  12.823  1.00117.14           C  
ANISOU 4638  CB  ILE A 684    13996  13969  16545   1187   2698   1630
ATOM   4639  CG1 ILE A 684      18.157  31.650  13.099  1.00115.74           C  
ANISOU 4639  CG1 ILE A 684    13873  13974  16129    960   2346   1874
ATOM   4640  CG2 ILE A 684      16.393  33.324  13.713  1.00121.14           C  
ANISOU 4640  CG2 ILE A 684    14340  14649  17041   1198   3125   1584
ATOM   4641  CD1 ILE A 684      17.207  30.538  12.787  1.00115.64           C  
ANISOU 4641  CD1 ILE A 684    13612  14035  16289    952   2192   2238
ATOM   4642  N   VAL A 685      17.375  35.610  11.069  1.00116.00           N  
ANISOU 4642  N   VAL A 685    13796  13186  17092   1662   2913   1270
ATOM   4643  CA  VAL A 685      16.817  36.944  10.854  1.00117.98           C  
ANISOU 4643  CA  VAL A 685    13960  13210  17658   1865   3193   1069
ATOM   4644  C   VAL A 685      16.253  37.068   9.443  1.00116.45           C  
ANISOU 4644  C   VAL A 685    13562  12750  17936   2027   2992   1292
ATOM   4645  O   VAL A 685      15.115  37.518   9.246  1.00118.60           O  
ANISOU 4645  O   VAL A 685    13583  12901  18580   2182   3183   1352
ATOM   4646  CB  VAL A 685      17.877  38.023  11.139  1.00118.07           C  
ANISOU 4646  CB  VAL A 685    14245  13115  17502   1854   3270    714
ATOM   4647  CG1 VAL A 685      17.345  39.396  10.771  1.00120.00           C  
ANISOU 4647  CG1 VAL A 685    14388  13068  18139   2070   3492    526
ATOM   4648  CG2 VAL A 685      18.272  37.988  12.603  1.00120.31           C  
ANISOU 4648  CG2 VAL A 685    14722  13664  17326   1673   3506    492
ATOM   4649  N   ARG A 686      17.040  36.659   8.444  1.00118.61           N  
ANISOU 4649  N   ARG A 686    13931  12934  18203   1976   2604   1422
ATOM   4650  CA  ARG A 686      16.613  36.745   7.050  1.00117.15           C  
ANISOU 4650  CA  ARG A 686    13588  12518  18406   2072   2377   1640
ATOM   4651  C   ARG A 686      15.269  36.066   6.825  1.00118.21           C  
ANISOU 4651  C   ARG A 686    13427  12684  18805   2122   2388   1955
ATOM   4652  O   ARG A 686      14.442  36.550   6.044  1.00118.98           O  
ANISOU 4652  O   ARG A 686    13321  12571  19315   2244   2381   2093
ATOM   4653  CB  ARG A 686      17.673  36.114   6.150  1.00113.50           C  
ANISOU 4653  CB  ARG A 686    13278  12041  17807   1956   1974   1728
ATOM   4654  CG  ARG A 686      17.393  36.225   4.664  1.00112.02           C  
ANISOU 4654  CG  ARG A 686    12976  11639  17947   1998   1720   1928
ATOM   4655  CD  ARG A 686      18.465  35.491   3.885  1.00108.81           C  
ANISOU 4655  CD  ARG A 686    12721  11266  17357   1862   1367   1971
ATOM   4656  NE  ARG A 686      18.419  34.060   4.169  1.00107.95           N  
ANISOU 4656  NE  ARG A 686    12581  11348  17086   1764   1227   2139
ATOM   4657  CZ  ARG A 686      19.354  33.395   4.840  1.00107.03           C  
ANISOU 4657  CZ  ARG A 686    12623  11397  16648   1652   1157   2040
ATOM   4658  NH1 ARG A 686      20.423  34.026   5.304  1.00106.78           N  
ANISOU 4658  NH1 ARG A 686    12798  11375  16398   1619   1221   1774
ATOM   4659  NH2 ARG A 686      19.217  32.096   5.052  1.00106.54           N1+
ANISOU 4659  NH2 ARG A 686    12503  11476  16502   1564   1001   2224
ATOM   4660  N   ILE A 687      15.033  34.938   7.497  1.00114.49           N  
ANISOU 4660  N   ILE A 687    12920  12469  18112   2012   2381   2097
ATOM   4661  CA  ILE A 687      13.772  34.228   7.308  1.00114.39           C  
ANISOU 4661  CA  ILE A 687    12626  12503  18333   2042   2371   2420
ATOM   4662  C   ILE A 687      12.657  34.868   8.127  1.00118.27           C  
ANISOU 4662  C   ILE A 687    12909  13031  18998   2159   2806   2340
ATOM   4663  O   ILE A 687      11.533  35.032   7.641  1.00119.23           O  
ANISOU 4663  O   ILE A 687    12753  13024  19524   2279   2860   2536
ATOM   4664  CB  ILE A 687      13.945  32.736   7.647  1.00113.87           C  
ANISOU 4664  CB  ILE A 687    12590  12685  17991   1867   2153   2632
ATOM   4665  CG1 ILE A 687      14.916  32.072   6.667  1.00109.51           C  
ANISOU 4665  CG1 ILE A 687    12188  12052  17369   1779   1723   2714
ATOM   4666  CG2 ILE A 687      12.601  32.026   7.628  1.00114.36           C  
ANISOU 4666  CG2 ILE A 687    12362  12823  18265   1884   2173   2963
ATOM   4667  CD1 ILE A 687      15.351  30.693   7.088  1.00109.10           C  
ANISOU 4667  CD1 ILE A 687    12200  12205  17047   1606   1493   2853
ATOM   4668  N   MET A 688      12.944  35.247   9.375  1.00119.93           N  
ANISOU 4668  N   MET A 688    13241  13415  18914   2114   3128   2046
ATOM   4669  CA  MET A 688      11.902  35.784  10.242  1.00124.17           C  
ANISOU 4669  CA  MET A 688    13576  14024  19578   2205   3584   1926
ATOM   4670  C   MET A 688      11.427  37.171   9.826  1.00126.13           C  
ANISOU 4670  C   MET A 688    13690  13952  20281   2433   3800   1748
ATOM   4671  O   MET A 688      10.349  37.592  10.260  1.00129.77           O  
ANISOU 4671  O   MET A 688    13893  14404  21009   2554   4150   1704
ATOM   4672  CB  MET A 688      12.384  35.817  11.692  1.00126.19           C  
ANISOU 4672  CB  MET A 688    14026  14569  19352   2054   3871   1637
ATOM   4673  CG  MET A 688      12.442  34.454  12.342  1.00125.78           C  
ANISOU 4673  CG  MET A 688    14005  14864  18922   1820   3738   1859
ATOM   4674  SD  MET A 688      10.802  33.709  12.423  1.00128.20           S  
ANISOU 4674  SD  MET A 688    13910  15316  19485   1852   3862   2212
ATOM   4675  CE  MET A 688      10.018  34.737  13.661  1.00133.81           C  
ANISOU 4675  CE  MET A 688    14496  16156  20188   1916   4528   1848
ATOM   4676  N   LYS A 689      12.190  37.896   9.006  1.00124.10           N  
ANISOU 4676  N   LYS A 689    13582  13429  20141   2490   3600   1648
ATOM   4677  CA  LYS A 689      11.712  39.211   8.589  1.00126.20           C  
ANISOU 4677  CA  LYS A 689    13701  13364  20886   2695   3762   1512
ATOM   4678  C   LYS A 689      10.726  39.113   7.429  1.00126.02           C  
ANISOU 4678  C   LYS A 689    13370  13118  21392   2798   3560   1885
ATOM   4679  O   LYS A 689       9.636  39.691   7.486  1.00129.32           O  
ANISOU 4679  O   LYS A 689    13489  13387  22258   2961   3803   1904
ATOM   4680  CB  LYS A 689      12.885  40.121   8.220  1.00124.58           C  
ANISOU 4680  CB  LYS A 689    13767  12960  20606   2695   3630   1264
ATOM   4681  CG  LYS A 689      13.671  40.628   9.417  1.00125.98           C  
ANISOU 4681  CG  LYS A 689    14210  13273  20383   2634   3909    843
ATOM   4682  CD  LYS A 689      14.858  41.473   8.984  1.00124.18           C  
ANISOU 4682  CD  LYS A 689    14249  12850  20085   2621   3732    641
ATOM   4683  CE  LYS A 689      14.410  42.812   8.422  1.00126.21           C  
ANISOU 4683  CE  LYS A 689    14358  12722  20873   2819   3813    538
ATOM   4684  NZ  LYS A 689      15.567  43.692   8.103  1.00124.85           N1+
ANISOU 4684  NZ  LYS A 689    14450  12372  20614   2790   3656    330
ATOM   4685  N   ALA A 690      11.089  38.385   6.372  1.00122.44           N  
ANISOU 4685  N   ALA A 690    12979  12637  20907   2695   3118   2181
ATOM   4686  CA  ALA A 690      10.259  38.356   5.171  1.00122.20           C  
ANISOU 4686  CA  ALA A 690    12699  12381  21353   2751   2878   2542
ATOM   4687  C   ALA A 690       8.889  37.752   5.453  1.00124.56           C  
ANISOU 4687  C   ALA A 690    12663  12775  21887   2802   3024   2808
ATOM   4688  O   ALA A 690       7.855  38.370   5.172  1.00127.26           O  
ANISOU 4688  O   ALA A 690    12702  12902  22748   2949   3144   2919
ATOM   4689  CB  ALA A 690      10.970  37.581   4.069  1.00118.13           C  
ANISOU 4689  CB  ALA A 690    12347  11868  20670   2589   2400   2769
ATOM   4690  N   ARG A 691       8.860  36.537   5.990  1.00123.71           N  
ANISOU 4690  N   ARG A 691    12592  12981  21432   2674   2996   2933
ATOM   4691  CA  ARG A 691       7.619  35.921   6.436  1.00126.15           C  
ANISOU 4691  CA  ARG A 691    12599  13438  21895   2697   3162   3169
ATOM   4692  C   ARG A 691       7.431  36.217   7.919  1.00129.53           C  
ANISOU 4692  C   ARG A 691    13007  14093  22116   2728   3659   2852
ATOM   4693  O   ARG A 691       8.399  36.261   8.683  1.00128.92           O  
ANISOU 4693  O   ARG A 691    13215  14183  21585   2632   3756   2553
ATOM   4694  CB  ARG A 691       7.634  34.413   6.160  1.00123.64           C  
ANISOU 4694  CB  ARG A 691    12317  13326  21336   2520   2824   3512
ATOM   4695  CG  ARG A 691       8.680  33.636   6.942  1.00121.85           C  
ANISOU 4695  CG  ARG A 691    12385  13390  20522   2347   2773   3359
ATOM   4696  CD  ARG A 691       8.730  32.157   6.554  1.00119.43           C  
ANISOU 4696  CD  ARG A 691    12103  13226  20048   2181   2388   3700
ATOM   4697  NE  ARG A 691       9.270  31.917   5.217  1.00116.13           N  
ANISOU 4697  NE  ARG A 691    11799  12607  19718   2138   1961   3837
ATOM   4698  CZ  ARG A 691       8.564  31.448   4.193  1.00115.51           C  
ANISOU 4698  CZ  ARG A 691    11556  12400  19931   2125   1692   4192
ATOM   4699  NH1 ARG A 691       7.279  31.158   4.346  1.00117.83           N  
ANISOU 4699  NH1 ARG A 691    11551  12734  20486   2167   1789   4472
ATOM   4700  NH2 ARG A 691       9.145  31.258   3.016  1.00112.74           N1+
ANISOU 4700  NH2 ARG A 691    11343  11895  19600   2053   1328   4267
ATOM   4701  N   LYS A 692       6.181  36.445   8.318  1.00133.37           N  
ANISOU 4701  N   LYS A 692    13147  14585  22942   2848   3980   2915
ATOM   4702  CA  LYS A 692       5.923  37.107   9.593  1.00137.46           C  
ANISOU 4702  CA  LYS A 692    13612  15238  23377   2914   4523   2533
ATOM   4703  C   LYS A 692       6.106  36.169  10.784  1.00139.35           C  
ANISOU 4703  C   LYS A 692    13972  15932  23041   2708   4675   2485
ATOM   4704  O   LYS A 692       6.915  36.439  11.678  1.00140.87           O  
ANISOU 4704  O   LYS A 692    14431  16288  22805   2614   4867   2129
ATOM   4705  CB  LYS A 692       4.519  37.719   9.587  1.00141.78           C  
ANISOU 4705  CB  LYS A 692    13717  15622  24533   3122   4837   2593
ATOM   4706  CG  LYS A 692       4.382  38.905   8.638  1.00142.27           C  
ANISOU 4706  CG  LYS A 692    13659  15211  25187   3325   4754   2558
ATOM   4707  CD  LYS A 692       2.993  39.525   8.687  1.00147.01           C  
ANISOU 4707  CD  LYS A 692    13786  15623  26446   3538   5070   2611
ATOM   4708  CE  LYS A 692       2.887  40.700   7.725  1.00147.64           C  
ANISOU 4708  CE  LYS A 692    13741  15205  27150   3718   4932   2611
ATOM   4709  NZ  LYS A 692       1.534  41.321   7.744  1.00152.52           N1+
ANISOU 4709  NZ  LYS A 692    13865  15597  28490   3936   5217   2676
ATOM   4710  N   VAL A 693       5.358  35.068  10.821  1.00140.07           N  
ANISOU 4710  N   VAL A 693    13872  16234  23116   2613   4573   2858
ATOM   4711  CA  VAL A 693       5.339  34.176  11.975  1.00142.36           C  
ANISOU 4711  CA  VAL A 693    14214  16964  22914   2399   4721   2867
ATOM   4712  C   VAL A 693       5.521  32.740  11.500  1.00139.43           C  
ANISOU 4712  C   VAL A 693    13902  16723  22351   2217   4229   3300
ATOM   4713  O   VAL A 693       5.013  32.358  10.440  1.00136.79           O  
ANISOU 4713  O   VAL A 693    13403  16200  22371   2281   3920   3657
ATOM   4714  CB  VAL A 693       4.027  34.325  12.781  1.00146.47           C  
ANISOU 4714  CB  VAL A 693    14371  17663  23620   2457   5206   2852
ATOM   4715  CG1 VAL A 693       3.983  33.346  13.946  1.00148.78           C  
ANISOU 4715  CG1 VAL A 693    14712  18442  23373   2187   5327   2908
ATOM   4716  CG2 VAL A 693       3.866  35.753  13.281  1.00149.56           C  
ANISOU 4716  CG2 VAL A 693    14698  17903  24225   2646   5715   2372
ATOM   4717  N   LEU A 694       6.259  31.949  12.281  1.00139.17           N  
ANISOU 4717  N   LEU A 694    14108  17000  21769   1976   4141   3269
ATOM   4718  CA  LEU A 694       6.432  30.524  12.029  1.00136.58           C  
ANISOU 4718  CA  LEU A 694    13828  16818  21248   1785   3698   3654
ATOM   4719  C   LEU A 694       6.384  29.757  13.343  1.00138.77           C  
ANISOU 4719  C   LEU A 694    14134  17532  21058   1529   3840   3682
ATOM   4720  O   LEU A 694       6.787  30.270  14.387  1.00140.92           O  
ANISOU 4720  O   LEU A 694    14553  17993  20997   1441   4170   3342
ATOM   4721  CB  LEU A 694       7.762  30.216  11.332  1.00132.07           C  
ANISOU 4721  CB  LEU A 694    13580  16095  20504   1721   3252   3630
ATOM   4722  CG  LEU A 694       7.970  30.694   9.901  1.00129.30           C  
ANISOU 4722  CG  LEU A 694    13243  15354  20530   1892   2990   3673
ATOM   4723  CD1 LEU A 694       9.390  30.375   9.475  1.00125.46           C  
ANISOU 4723  CD1 LEU A 694    13090  14802  19779   1792   2630   3578
ATOM   4724  CD2 LEU A 694       6.963  30.043   8.972  1.00128.85           C  
ANISOU 4724  CD2 LEU A 694    12921  15189  20848   1933   2743   4111
ATOM   4725  N   ARG A 695       5.895  28.521  13.284  1.00147.19           N  
ANISOU 4725  N   ARG A 695    15069  18763  22093   1385   3569   4100
ATOM   4726  CA  ARG A 695       5.981  27.634  14.432  1.00150.58           C  
ANISOU 4726  CA  ARG A 695    15551  19603  22059   1089   3582   4196
ATOM   4727  C   ARG A 695       7.398  27.082  14.550  1.00150.26           C  
ANISOU 4727  C   ARG A 695    15868  19589  21634    900   3214   4140
ATOM   4728  O   ARG A 695       8.163  27.046  13.581  1.00147.40           O  
ANISOU 4728  O   ARG A 695    15660  18942  21404    991   2868   4137
ATOM   4729  CB  ARG A 695       4.956  26.504  14.319  1.00149.41           C  
ANISOU 4729  CB  ARG A 695    15125  19605  22037    993   3391   4686
ATOM   4730  CG  ARG A 695       5.145  25.537  13.154  1.00145.01           C  
ANISOU 4730  CG  ARG A 695    14590  18827  21681    997   2801   5053
ATOM   4731  CD  ARG A 695       3.981  24.538  13.086  1.00145.09           C  
ANISOU 4731  CD  ARG A 695    14299  18979  21851    913   2657   5533
ATOM   4732  NE  ARG A 695       3.972  23.585  14.196  1.00148.37           N  
ANISOU 4732  NE  ARG A 695    14723  19795  21856    604   2613   5702
ATOM   4733  CZ  ARG A 695       4.559  22.392  14.166  1.00145.91           C  
ANISOU 4733  CZ  ARG A 695    14549  19538  21351    393   2128   5950
ATOM   4734  NH1 ARG A 695       5.181  21.985  13.070  1.00139.95           N  
ANISOU 4734  NH1 ARG A 695    13929  18468  20777    471   1676   6032
ATOM   4735  NH2 ARG A 695       4.504  21.594  15.224  1.00147.57           N1+
ANISOU 4735  NH2 ARG A 695    14750  20117  21204     91   2090   6121
ATOM   4736  N   HIS A 696       7.752  26.669  15.769  1.00148.03           N  
ANISOU 4736  N   HIS A 696    15709  19660  20875    618   3297   4092
ATOM   4737  CA  HIS A 696       9.135  26.295  16.053  1.00148.16           C  
ANISOU 4737  CA  HIS A 696    16058  19706  20529    426   2999   4001
ATOM   4738  C   HIS A 696       9.678  25.245  15.080  1.00143.82           C  
ANISOU 4738  C   HIS A 696    15562  18956  20126    413   2396   4302
ATOM   4739  O   HIS A 696      10.852  25.335  14.682  1.00142.31           O  
ANISOU 4739  O   HIS A 696    15613  18581  19876    427   2156   4147
ATOM   4740  CB  HIS A 696       9.270  25.840  17.512  1.00151.79           C  
ANISOU 4740  CB  HIS A 696    16600  20603  20470     69   3123   4008
ATOM   4741  CG  HIS A 696      10.638  25.360  17.870  1.00151.62           C  
ANISOU 4741  CG  HIS A 696    16888  20620  20100   -164   2779   3978
ATOM   4742  ND1 HIS A 696      11.691  26.217  18.102  1.00152.48           N  
ANISOU 4742  ND1 HIS A 696    17279  20641  20015   -155   2891   3595
ATOM   4743  CD2 HIS A 696      11.130  24.108  18.006  1.00149.87           C  
ANISOU 4743  CD2 HIS A 696    16722  20489  19732   -410   2300   4298
ATOM   4744  CE1 HIS A 696      12.772  25.511  18.378  1.00151.47           C  
ANISOU 4744  CE1 HIS A 696    17360  20558  19632   -388   2504   3688
ATOM   4745  NE2 HIS A 696      12.459  24.229  18.325  1.00149.56           N  
ANISOU 4745  NE2 HIS A 696    16981  20416  19430   -542   2140   4109
ATOM   4746  N   ASN A 697       8.829  24.287  14.637  1.00149.12           N  
ANISOU 4746  N   ASN A 697    16002  19641  21015    396   2157   4713
ATOM   4747  CA  ASN A 697       9.267  23.271  13.700  1.00145.33           C  
ANISOU 4747  CA  ASN A 697    15562  18960  20695    383   1602   4977
ATOM   4748  C   ASN A 697       9.501  23.819  12.325  1.00140.36           C  
ANISOU 4748  C   ASN A 697    14968  17941  20422    650   1487   4867
ATOM   4749  O   ASN A 697      10.362  23.318  11.600  1.00135.95           O  
ANISOU 4749  O   ASN A 697    14558  17192  19906    643   1095   4886
ATOM   4750  CB  ASN A 697       8.212  22.153  13.474  1.00143.98           C  
ANISOU 4750  CB  ASN A 697    15132  18871  20705    309   1368   5451
ATOM   4751  CG  ASN A 697       8.888  20.825  13.218  1.00140.43           C  
ANISOU 4751  CG  ASN A 697    14779  18372  20207    136    799   5702
ATOM   4752  OD1 ASN A 697       8.314  19.898  12.620  1.00138.67           O  
ANISOU 4752  OD1 ASN A 697    14405  18076  20208    121    478   6055
ATOM   4753  ND2 ASN A 697      10.088  20.706  13.801  1.00139.76           N  
ANISOU 4753  ND2 ASN A 697    14936  18347  19818    -21    679   5528
ATOM   4754  N   ALA A 698       8.766  24.832  11.951  1.00127.15           N  
ANISOU 4754  N   ALA A 698    13154  16145  19013    869   1814   4753
ATOM   4755  CA  ALA A 698       8.680  25.186  10.550  1.00124.74           C  
ANISOU 4755  CA  ALA A 698    12813  15487  19096   1081   1651   4779
ATOM   4756  C   ALA A 698       9.794  26.133  10.140  1.00122.67           C  
ANISOU 4756  C   ALA A 698    12799  15014  18798   1189   1682   4403
ATOM   4757  O   ALA A 698      10.204  26.144   8.971  1.00119.90           O  
ANISOU 4757  O   ALA A 698    12515  14399  18641   1275   1410   4416
ATOM   4758  CB  ALA A 698       7.299  25.776  10.265  1.00127.04           C  
ANISOU 4758  CB  ALA A 698    12796  15714  19758   1253   1929   4900
ATOM   4759  N   LEU A 699      10.283  26.927  11.089  1.00120.63           N  
ANISOU 4759  N   LEU A 699    12679  14880  18275   1165   2011   4069
ATOM   4760  CA  LEU A 699      11.484  27.723  10.877  1.00118.77           C  
ANISOU 4760  CA  LEU A 699    12709  14485  17934   1220   2011   3721
ATOM   4761  C   LEU A 699      12.679  26.831  10.561  1.00115.70           C  
ANISOU 4761  C   LEU A 699    12527  14061  17372   1083   1567   3768
ATOM   4762  O   LEU A 699      13.407  27.058   9.585  1.00112.97           O  
ANISOU 4762  O   LEU A 699    12301  13477  17147   1169   1362   3668
ATOM   4763  CB  LEU A 699      11.741  28.569  12.124  1.00121.45           C  
ANISOU 4763  CB  LEU A 699    13164  15008  17972   1167   2430   3385
ATOM   4764  CG  LEU A 699      12.954  29.476  12.090  1.00120.07           C  
ANISOU 4764  CG  LEU A 699    13268  14695  17656   1206   2469   3014
ATOM   4765  CD1 LEU A 699      12.809  30.476  10.963  1.00118.90           C  
ANISOU 4765  CD1 LEU A 699    13070  14210  17895   1457   2507   2905
ATOM   4766  CD2 LEU A 699      13.083  30.170  13.427  1.00123.23           C  
ANISOU 4766  CD2 LEU A 699    13780  15313  17729   1111   2880   2712
ATOM   4767  N   ILE A 700      12.895  25.804  11.387  1.00126.41           N  
ANISOU 4767  N   ILE A 700    13915  15655  18460    857   1412   3924
ATOM   4768  CA  ILE A 700      13.806  24.743  11.003  1.00122.77           C  
ANISOU 4768  CA  ILE A 700    13570  15131  17948    738    944   4045
ATOM   4769  C   ILE A 700      13.227  24.042   9.770  1.00118.18           C  
ANISOU 4769  C   ILE A 700    12832  14359  17714    826    642   4322
ATOM   4770  O   ILE A 700      12.025  24.114   9.487  1.00118.59           O  
ANISOU 4770  O   ILE A 700    12666  14403  17988    913    759   4513
ATOM   4771  CB  ILE A 700      14.023  23.768  12.173  1.00125.59           C  
ANISOU 4771  CB  ILE A 700    13955  15771  17994    460    815   4207
ATOM   4772  CG1 ILE A 700      14.499  24.538  13.404  1.00131.28           C  
ANISOU 4772  CG1 ILE A 700    14838  16699  18343    341   1142   3933
ATOM   4773  CG2 ILE A 700      15.077  22.719  11.842  1.00122.28           C  
ANISOU 4773  CG2 ILE A 700    13647  15250  17564    343    326   4301
ATOM   4774  CD1 ILE A 700      14.477  23.732  14.679  1.00133.89           C  
ANISOU 4774  CD1 ILE A 700    15172  17362  18336     27   1087   4114
ATOM   4775  N   GLN A 701      14.110  23.374   9.023  1.00127.20           N  
ANISOU 4775  N   GLN A 701    14084  15338  18908    797    254   4331
ATOM   4776  CA  GLN A 701      13.898  22.796   7.694  1.00119.44           C  
ANISOU 4776  CA  GLN A 701    13030  14133  18219    866    -58   4495
ATOM   4777  C   GLN A 701      13.894  23.902   6.644  1.00116.96           C  
ANISOU 4777  C   GLN A 701    12746  13595  18098   1053     75   4311
ATOM   4778  O   GLN A 701      14.165  23.647   5.463  1.00112.12           O  
ANISOU 4778  O   GLN A 701    12164  12784  17653   1086   -177   4326
ATOM   4779  CB  GLN A 701      12.581  22.009   7.612  1.00118.67           C  
ANISOU 4779  CB  GLN A 701    12692  14101  18296    833   -148   4885
ATOM   4780  CG  GLN A 701      12.373  20.964   8.696  1.00121.51           C  
ANISOU 4780  CG  GLN A 701    12984  14708  18475    628   -265   5123
ATOM   4781  CD  GLN A 701      13.390  19.855   8.645  1.00118.36           C  
ANISOU 4781  CD  GLN A 701    12701  14254  18018    487   -695   5159
ATOM   4782  OE1 GLN A 701      13.792  19.417   7.568  1.00114.00           O  
ANISOU 4782  OE1 GLN A 701    12189  13470  17658    540   -984   5145
ATOM   4783  NE2 GLN A 701      13.814  19.386   9.814  1.00122.14           N  
ANISOU 4783  NE2 GLN A 701    13227  14941  18241    291   -743   5203
ATOM   4784  N   GLU A 702      13.726  25.149   7.082  1.00109.15           N  
ANISOU 4784  N   GLU A 702    11771  12635  17067   1153    458   4105
ATOM   4785  CA  GLU A 702      13.923  26.294   6.207  1.00107.52           C  
ANISOU 4785  CA  GLU A 702    11620  12211  17022   1306    567   3904
ATOM   4786  C   GLU A 702      15.259  26.961   6.454  1.00107.75           C  
ANISOU 4786  C   GLU A 702    11895  12216  16830   1298    625   3550
ATOM   4787  O   GLU A 702      15.907  27.392   5.503  1.00104.81           O  
ANISOU 4787  O   GLU A 702    11625  11660  16538   1350    511   3412
ATOM   4788  CB  GLU A 702      12.806  27.331   6.359  1.00110.15           C  
ANISOU 4788  CB  GLU A 702    11779  12521  17553   1449    929   3910
ATOM   4789  CG  GLU A 702      12.964  28.484   5.359  1.00108.20           C  
ANISOU 4789  CG  GLU A 702    11569  12016  17527   1589    977   3753
ATOM   4790  CD  GLU A 702      11.865  29.529   5.437  1.00110.50           C  
ANISOU 4790  CD  GLU A 702    11657  12227  18099   1744   1304   3765
ATOM   4791  OE1 GLU A 702      10.965  29.399   6.292  1.00113.72           O  
ANISOU 4791  OE1 GLU A 702    11890  12796  18523   1755   1541   3864
ATOM   4792  OE2 GLU A 702      11.907  30.488   4.635  1.00109.46           O1-
ANISOU 4792  OE2 GLU A 702    11530  11869  18189   1847   1320   3676
ATOM   4793  N   VAL A 703      15.694  27.054   7.712  1.00106.14           N  
ANISOU 4793  N   VAL A 703    11790  12205  16333   1209    794   3412
ATOM   4794  CA  VAL A 703      17.108  27.320   7.962  1.00104.86           C  
ANISOU 4794  CA  VAL A 703    11870  12032  15938   1147    735   3142
ATOM   4795  C   VAL A 703      17.950  26.273   7.248  1.00102.43           C  
ANISOU 4795  C   VAL A 703    11621  11637  15660   1069    316   3216
ATOM   4796  O   VAL A 703      18.970  26.584   6.611  1.00100.54           O  
ANISOU 4796  O   VAL A 703    11520  11263  15417   1093    203   3020
ATOM   4797  CB  VAL A 703      17.390  27.337   9.475  1.00106.93           C  
ANISOU 4797  CB  VAL A 703    12226  12542  15860   1002    918   3051
ATOM   4798  CG1 VAL A 703      18.862  27.612   9.740  1.00105.73           C  
ANISOU 4798  CG1 VAL A 703    12322  12370  15481    923    834   2800
ATOM   4799  CG2 VAL A 703      16.501  28.350  10.160  1.00109.75           C  
ANISOU 4799  CG2 VAL A 703    12512  12987  16201   1080   1368   2940
ATOM   4800  N   ILE A 704      17.509  25.014   7.322  1.00102.67           N  
ANISOU 4800  N   ILE A 704    11531  11738  15741    974     82   3496
ATOM   4801  CA  ILE A 704      18.184  23.919   6.633  1.00100.81           C  
ANISOU 4801  CA  ILE A 704    11317  11397  15590    908   -319   3568
ATOM   4802  C   ILE A 704      18.126  24.134   5.127  1.00 99.00           C  
ANISOU 4802  C   ILE A 704    11071  10945  15599   1018   -429   3532
ATOM   4803  O   ILE A 704      19.140  24.024   4.427  1.00 97.23           O  
ANISOU 4803  O   ILE A 704    10956  10600  15388   1010   -605   3362
ATOM   4804  CB  ILE A 704      17.548  22.575   7.026  1.00101.85           C  
ANISOU 4804  CB  ILE A 704    11302  11632  15762    786   -545   3899
ATOM   4805  CG1 ILE A 704      17.399  22.473   8.545  1.00104.19           C  
ANISOU 4805  CG1 ILE A 704    11598  12190  15797    641   -399   3970
ATOM   4806  CG2 ILE A 704      18.379  21.423   6.490  1.00100.35           C  
ANISOU 4806  CG2 ILE A 704    11142  11319  15667    710   -961   3930
ATOM   4807  CD1 ILE A 704      18.682  22.561   9.298  1.00104.07           C  
ANISOU 4807  CD1 ILE A 704    11769  12235  15539    523   -441   3775
ATOM   4808  N   SER A 705      16.931  24.434   4.604  1.00 99.65           N  
ANISOU 4808  N   SER A 705    11008  10979  15875   1102   -329   3701
ATOM   4809  CA  SER A 705      16.796  24.692   3.173  1.00 98.28           C  
ANISOU 4809  CA  SER A 705    10821  10607  15912   1166   -441   3700
ATOM   4810  C   SER A 705      17.734  25.803   2.710  1.00 97.09           C  
ANISOU 4810  C   SER A 705    10832  10356  15701   1221   -336   3387
ATOM   4811  O   SER A 705      18.302  25.728   1.615  1.00 95.51           O  
ANISOU 4811  O   SER A 705    10699  10029  15560   1198   -518   3300
ATOM   4812  CB  SER A 705      15.348  25.048   2.839  1.00 99.61           C  
ANISOU 4812  CB  SER A 705    10800  10740  16307   1240   -320   3941
ATOM   4813  OG  SER A 705      15.203  25.362   1.464  1.00 98.54           O  
ANISOU 4813  OG  SER A 705    10661  10417  16363   1264   -443   3965
ATOM   4814  N   GLN A 706      17.911  26.840   3.532  1.00102.74           N  
ANISOU 4814  N   GLN A 706    11613  11134  16289   1278    -42   3210
ATOM   4815  CA  GLN A 706      18.706  27.993   3.119  1.00102.43           C  
ANISOU 4815  CA  GLN A 706    11718  10992  16210   1331     61   2937
ATOM   4816  C   GLN A 706      20.195  27.672   3.142  1.00101.17           C  
ANISOU 4816  C   GLN A 706    11735  10844  15862   1249    -99   2722
ATOM   4817  O   GLN A 706      20.911  27.924   2.167  1.00 98.99           O  
ANISOU 4817  O   GLN A 706    11538  10457  15616   1240   -216   2586
ATOM   4818  CB  GLN A 706      18.413  29.195   4.022  1.00106.02           C  
ANISOU 4818  CB  GLN A 706    12189  11489  16603   1417    423   2800
ATOM   4819  CG  GLN A 706      16.980  29.728   3.999  1.00107.82           C  
ANISOU 4819  CG  GLN A 706    12217  11675  17073   1526    632   2964
ATOM   4820  CD  GLN A 706      16.590  30.349   2.683  1.00105.64           C  
ANISOU 4820  CD  GLN A 706    11874  11185  17079   1590    552   3033
ATOM   4821  OE1 GLN A 706      17.396  31.012   2.039  1.00104.16           O  
ANISOU 4821  OE1 GLN A 706    11818  10886  16871   1586    492   2856
ATOM   4822  NE2 GLN A 706      15.341  30.148   2.280  1.00105.73           N  
ANISOU 4822  NE2 GLN A 706    11673  11145  17356   1629    537   3311
ATOM   4823  N   SER A 707      20.679  27.100   4.247  1.00101.02           N  
ANISOU 4823  N   SER A 707    11765  10964  15652   1169   -115   2702
ATOM   4824  CA  SER A 707      22.103  26.835   4.412  1.00100.26           C  
ANISOU 4824  CA  SER A 707    11815  10874  15405   1090   -262   2513
ATOM   4825  C   SER A 707      22.513  25.474   3.853  1.00 97.49           C  
ANISOU 4825  C   SER A 707    11411  10474  15159   1015   -605   2602
ATOM   4826  O   SER A 707      23.459  24.853   4.358  1.00 97.47           O  
ANISOU 4826  O   SER A 707    11461  10504  15070    928   -760   2541
ATOM   4827  CB  SER A 707      22.490  26.969   5.885  1.00103.77           C  
ANISOU 4827  CB  SER A 707    12349  11479  15599   1011   -129   2451
ATOM   4828  OG  SER A 707      21.788  26.039   6.686  1.00105.56           O  
ANISOU 4828  OG  SER A 707    12466  11845  15795    927   -180   2691
ATOM   4829  N   ARG A 708      21.813  25.000   2.819  1.00113.82           N  
ANISOU 4829  N   ARG A 708    13369  12449  17427   1040   -737   2746
ATOM   4830  CA  ARG A 708      22.080  23.690   2.229  1.00110.08           C  
ANISOU 4830  CA  ARG A 708    12839  11908  17081    974  -1055   2817
ATOM   4831  C   ARG A 708      23.520  23.561   1.730  1.00108.84           C  
ANISOU 4831  C   ARG A 708    12781  11673  16901    940  -1190   2547
ATOM   4832  O   ARG A 708      24.243  22.641   2.126  1.00108.16           O  
ANISOU 4832  O   ARG A 708    12682  11582  16833    876  -1386   2526
ATOM   4833  CB  ARG A 708      21.058  23.423   1.111  1.00108.00           C  
ANISOU 4833  CB  ARG A 708    12470  11552  17013    993  -1142   2992
ATOM   4834  CG  ARG A 708      20.828  24.590   0.130  1.00107.94           C  
ANISOU 4834  CG  ARG A 708    12502  11464  17047   1047   -999   2906
ATOM   4835  CD  ARG A 708      21.674  24.540  -1.140  1.00107.36           C  
ANISOU 4835  CD  ARG A 708    12507  11288  16996    992  -1146   2708
ATOM   4836  NE  ARG A 708      21.368  23.403  -2.003  1.00106.00           N  
ANISOU 4836  NE  ARG A 708    12268  11045  16962    918  -1401   2816
ATOM   4837  CZ  ARG A 708      20.388  23.392  -2.902  1.00105.26           C  
ANISOU 4837  CZ  ARG A 708    12111  10889  16993    885  -1461   3002
ATOM   4838  NH1 ARG A 708      19.618  24.462  -3.063  1.00105.91           N  
ANISOU 4838  NH1 ARG A 708    12167  10961  17114    929  -1293   3113
ATOM   4839  NH2 ARG A 708      20.183  22.316  -3.649  1.00103.73           N1+
ANISOU 4839  NH2 ARG A 708    11879  10630  16904    799  -1702   3077
ATOM   4840  N   ALA A 709      23.961  24.482   0.871  1.00100.24           N  
ANISOU 4840  N   ALA A 709    11775  10522  15790    975  -1093   2348
ATOM   4841  CA  ALA A 709      25.227  24.315   0.164  1.00 99.01           C  
ANISOU 4841  CA  ALA A 709    11683  10298  15637    935  -1216   2096
ATOM   4842  C   ALA A 709      26.436  24.750   0.977  1.00100.12           C  
ANISOU 4842  C   ALA A 709    11928  10487  15626    922  -1153   1902
ATOM   4843  O   ALA A 709      27.568  24.505   0.548  1.00 99.45           O  
ANISOU 4843  O   ALA A 709    11869  10353  15563    887  -1262   1701
ATOM   4844  CB  ALA A 709      25.206  25.085  -1.158  1.00 98.19           C  
ANISOU 4844  CB  ALA A 709    11622  10131  15553    934  -1160   1984
ATOM   4845  N   ARG A 710      26.232  25.394   2.124  1.00 95.16           N  
ANISOU 4845  N   ARG A 710    11357   9954  14846    937   -976   1950
ATOM   4846  CA  ARG A 710      27.361  25.749   2.973  1.00 95.28           C  
ANISOU 4846  CA  ARG A 710    11484  10018  14701    893   -943   1794
ATOM   4847  C   ARG A 710      27.845  24.541   3.763  1.00 95.97           C  
ANISOU 4847  C   ARG A 710    11513  10129  14822    802  -1169   1886
ATOM   4848  O   ARG A 710      29.045  24.242   3.784  1.00 95.68           O  
ANISOU 4848  O   ARG A 710    11498  10047  14810    754  -1309   1746
ATOM   4849  CB  ARG A 710      26.973  26.889   3.913  1.00 96.20           C  
ANISOU 4849  CB  ARG A 710    11699  10227  14626    919   -668   1787
ATOM   4850  N   PHE A 711      26.918  23.833   4.404  1.00 98.43           N  
ANISOU 4850  N   PHE A 711    11736  10506  15158    768  -1222   2138
ATOM   4851  CA  PHE A 711      27.183  22.663   5.236  1.00 98.76           C  
ANISOU 4851  CA  PHE A 711    11707  10576  15243    653  -1464   2295
ATOM   4852  C   PHE A 711      25.837  22.136   5.719  1.00 99.75           C  
ANISOU 4852  C   PHE A 711    11729  10794  15377    626  -1460   2592
ATOM   4853  O   PHE A 711      24.804  22.798   5.572  1.00100.58           O  
ANISOU 4853  O   PHE A 711    11826  10952  15438    701  -1233   2651
ATOM   4854  CB  PHE A 711      28.098  23.001   6.417  1.00100.96           C  
ANISOU 4854  CB  PHE A 711    12098  10943  15319    544  -1443   2236
ATOM   4855  CG  PHE A 711      27.565  24.095   7.299  1.00104.14           C  
ANISOU 4855  CG  PHE A 711    12619  11503  15446    530  -1130   2236
ATOM   4856  CD1 PHE A 711      27.844  25.420   7.018  1.00104.80           C  
ANISOU 4856  CD1 PHE A 711    12836  11572  15413    614   -883   2010
ATOM   4857  CD2 PHE A 711      26.793  23.802   8.408  1.00106.78           C  
ANISOU 4857  CD2 PHE A 711    12929  12002  15642    423  -1081   2451
ATOM   4858  CE1 PHE A 711      27.357  26.429   7.818  1.00108.05           C  
ANISOU 4858  CE1 PHE A 711    13351  12100  15604    611   -589   1975
ATOM   4859  CE2 PHE A 711      26.306  24.811   9.213  1.00110.29           C  
ANISOU 4859  CE2 PHE A 711    13477  12594  15835    408   -761   2405
ATOM   4860  CZ  PHE A 711      26.586  26.124   8.916  1.00110.95           C  
ANISOU 4860  CZ  PHE A 711    13690  12631  15833    512   -512   2155
ATOM   4861  N   ASN A 712      25.853  20.933   6.292  1.00103.20           N  
ANISOU 4861  N   ASN A 712    12070  11243  15898    512  -1728   2793
ATOM   4862  CA  ASN A 712      24.684  20.416   6.989  1.00104.79           C  
ANISOU 4862  CA  ASN A 712    12177  11575  16063    441  -1737   3100
ATOM   4863  C   ASN A 712      24.708  20.935   8.423  1.00109.71           C  
ANISOU 4863  C   ASN A 712    12891  12411  16383    312  -1565   3149
ATOM   4864  O   ASN A 712      25.562  20.494   9.208  1.00111.04           O  
ANISOU 4864  O   ASN A 712    13095  12611  16486    158  -1749   3179
ATOM   4865  CB  ASN A 712      24.648  18.895   6.964  1.00103.34           C  
ANISOU 4865  CB  ASN A 712    11848  11309  16107    352  -2124   3316
ATOM   4866  CG  ASN A 712      24.167  18.344   5.632  1.00100.63           C  
ANISOU 4866  CG  ASN A 712    11408  10795  16031    459  -2252   3322
ATOM   4867  OD1 ASN A 712      23.208  18.849   5.046  1.00100.53           O  
ANISOU 4867  OD1 ASN A 712    11382  10801  16014    550  -2069   3360
ATOM   4868  ND2 ASN A 712      24.830  17.300   5.151  1.00 98.70           N  
ANISOU 4868  ND2 ASN A 712    11092  10375  16037    437  -2574   3283
ATOM   4869  N   PRO A 713      23.825  21.850   8.795  1.00 99.33           N  
ANISOU 4869  N   PRO A 713    11611  11237  14894    355  -1224   3152
ATOM   4870  CA  PRO A 713      23.910  22.464  10.124  1.00101.14           C  
ANISOU 4870  CA  PRO A 713    11953  11674  14802    222  -1013   3128
ATOM   4871  C   PRO A 713      23.407  21.545  11.221  1.00103.39           C  
ANISOU 4871  C   PRO A 713    12157  12152  14976      6  -1145   3432
ATOM   4872  O   PRO A 713      22.547  20.687  11.013  1.00103.81           O  
ANISOU 4872  O   PRO A 713    12047  12213  15183     -2  -1287   3684
ATOM   4873  CB  PRO A 713      23.016  23.702   9.993  1.00101.45           C  
ANISOU 4873  CB  PRO A 713    12017  11764  14765    369   -596   3011
ATOM   4874  CG  PRO A 713      22.031  23.325   8.951  1.00100.62           C  
ANISOU 4874  CG  PRO A 713    11746  11553  14933    506   -648   3155
ATOM   4875  CD  PRO A 713      22.748  22.436   7.981  1.00 98.80           C  
ANISOU 4875  CD  PRO A 713    11479  11128  14930    523  -1007   3153
ATOM   4876  N   SER A 714      23.960  21.749  12.411  1.00107.77           N  
ANISOU 4876  N   SER A 714    12833  12870  15244   -195  -1107   3416
ATOM   4877  CA  SER A 714      23.613  20.936  13.567  1.00110.28           C  
ANISOU 4877  CA  SER A 714    13097  13405  15398   -465  -1245   3709
ATOM   4878  C   SER A 714      22.332  21.467  14.195  1.00112.34           C  
ANISOU 4878  C   SER A 714    13325  13914  15444   -488   -867   3769
ATOM   4879  O   SER A 714      22.285  22.620  14.634  1.00113.16           O  
ANISOU 4879  O   SER A 714    13561  14122  15314   -463   -490   3539
ATOM   4880  CB  SER A 714      24.753  20.946  14.581  1.00111.48           C  
ANISOU 4880  CB  SER A 714    13400  13641  15315   -713  -1376   3681
ATOM   4881  OG  SER A 714      25.930  20.385  14.026  1.00109.90           O  
ANISOU 4881  OG  SER A 714    13190  13204  15365   -690  -1736   3640
ATOM   4882  N   ILE A 715      21.295  20.626  14.240  1.00112.63           N  
ANISOU 4882  N   ILE A 715    13177  14041  15576   -538   -963   4071
ATOM   4883  CA  ILE A 715      20.060  20.998  14.921  1.00115.06           C  
ANISOU 4883  CA  ILE A 715    13416  14612  15691   -589   -614   4158
ATOM   4884  C   ILE A 715      20.327  21.317  16.386  1.00117.95           C  
ANISOU 4884  C   ILE A 715    13921  15276  15619   -883   -453   4129
ATOM   4885  O   ILE A 715      19.559  22.054  17.015  1.00120.15           O  
ANISOU 4885  O   ILE A 715    14208  15774  15670   -907    -35   4039
ATOM   4886  CB  ILE A 715      19.013  19.873  14.763  1.00115.82           C  
ANISOU 4886  CB  ILE A 715    13279  14761  15964   -636   -821   4537
ATOM   4887  CG1 ILE A 715      18.794  19.559  13.282  1.00113.09           C  
ANISOU 4887  CG1 ILE A 715    12824  14114  16032   -373   -995   4551
ATOM   4888  CG2 ILE A 715      17.684  20.268  15.393  1.00118.46           C  
ANISOU 4888  CG2 ILE A 715    13506  15371  16134   -673   -436   4626
ATOM   4889  CD1 ILE A 715      18.262  20.726  12.487  1.00111.98           C  
ANISOU 4889  CD1 ILE A 715    12683  13868  15996    -93   -624   4319
ATOM   4890  N   SER A 716      21.421  20.793  16.942  1.00126.79           N  
ANISOU 4890  N   SER A 716    15148  16403  16622  -1118   -775   4195
ATOM   4891  CA  SER A 716      21.829  21.147  18.295  1.00129.36           C  
ANISOU 4891  CA  SER A 716    15645  16999  16508  -1434   -653   4157
ATOM   4892  C   SER A 716      22.233  22.613  18.415  1.00132.47           C  
ANISOU 4892  C   SER A 716    16251  17384  16699  -1321   -241   3743
ATOM   4893  O   SER A 716      22.267  23.143  19.530  1.00135.53           O  
ANISOU 4893  O   SER A 716    16785  18026  16683  -1556     -3   3652
ATOM   4894  CB  SER A 716      22.987  20.252  18.740  1.00128.13           C  
ANISOU 4894  CB  SER A 716    15544  16798  16343  -1705  -1149   4345
ATOM   4895  OG  SER A 716      22.599  18.888  18.779  1.00127.45           O  
ANISOU 4895  OG  SER A 716    15263  16728  16435  -1849  -1546   4744
ATOM   4896  N   MET A 717      22.536  23.276  17.299  1.00135.77           N  
ANISOU 4896  N   MET A 717    16691  17518  17376   -992   -162   3493
ATOM   4897  CA  MET A 717      22.996  24.660  17.301  1.00139.30           C  
ANISOU 4897  CA  MET A 717    17334  17910  17683   -872    174   3110
ATOM   4898  C   MET A 717      21.885  25.661  17.015  1.00141.69           C  
ANISOU 4898  C   MET A 717    17576  18226  18034   -635    650   2923
ATOM   4899  O   MET A 717      21.882  26.757  17.585  1.00144.69           O  
ANISOU 4899  O   MET A 717    18102  18693  18179   -644   1020   2648
ATOM   4900  CB  MET A 717      24.111  24.848  16.265  1.00137.03           C  
ANISOU 4900  CB  MET A 717    17113  17307  17645   -684    -43   2950
ATOM   4901  CG  MET A 717      25.332  23.976  16.500  1.00134.75           C  
ANISOU 4901  CG  MET A 717    16871  16959  17371   -887   -497   3089
ATOM   4902  SD  MET A 717      26.092  24.240  18.111  1.00138.83           S  
ANISOU 4902  SD  MET A 717    17621  17729  17399  -1293   -484   3082
ATOM   4903  CE  MET A 717      26.758  25.884  17.897  1.00140.83           C  
ANISOU 4903  CE  MET A 717    18116  17871  17523  -1124   -140   2633
ATOM   4904  N   ILE A 718      20.940  25.305  16.142  1.00122.24           N  
ANISOU 4904  N   ILE A 718    14891  15662  15891   -428    636   3067
ATOM   4905  CA  ILE A 718      19.927  26.260  15.705  1.00122.65           C  
ANISOU 4905  CA  ILE A 718    14852  15664  16086   -175   1041   2909
ATOM   4906  C   ILE A 718      19.007  26.644  16.857  1.00126.54           C  
ANISOU 4906  C   ILE A 718    15314  16461  16304   -309   1448   2876
ATOM   4907  O   ILE A 718      18.593  27.803  16.974  1.00127.87           O  
ANISOU 4907  O   ILE A 718    15512  16619  16455   -170   1869   2598
ATOM   4908  CB  ILE A 718      19.144  25.690  14.508  1.00120.78           C  
ANISOU 4908  CB  ILE A 718    14382  15252  16258     36    880   3120
ATOM   4909  CG1 ILE A 718      20.073  25.510  13.309  1.00117.25           C  
ANISOU 4909  CG1 ILE A 718    13985  14506  16058    174    555   3066
ATOM   4910  CG2 ILE A 718      17.982  26.594  14.138  1.00121.73           C  
ANISOU 4910  CG2 ILE A 718    14367  15328  16558    266   1272   3023
ATOM   4911  CD1 ILE A 718      19.448  24.749  12.169  1.00115.56           C  
ANISOU 4911  CD1 ILE A 718    13573  14133  16200    312    326   3290
ATOM   4912  N   LYS A 719      18.679  25.690  17.733  1.00134.57           N  
ANISOU 4912  N   LYS A 719    16265  17754  17110   -593   1331   3149
ATOM   4913  CA  LYS A 719      17.787  25.990  18.852  1.00137.85           C  
ANISOU 4913  CA  LYS A 719    16640  18504  17232   -759   1733   3118
ATOM   4914  C   LYS A 719      18.427  26.982  19.817  1.00140.24           C  
ANISOU 4914  C   LYS A 719    17208  18938  17139   -912   2030   2771
ATOM   4915  O   LYS A 719      17.803  27.980  20.207  1.00142.78           O  
ANISOU 4915  O   LYS A 719    17533  19346  17373   -833   2521   2496
ATOM   4916  CB  LYS A 719      17.402  24.700  19.577  1.00136.96           C  
ANISOU 4916  CB  LYS A 719    16413  18676  16951  -1081   1490   3516
ATOM   4917  CG  LYS A 719      16.510  23.776  18.763  1.00134.79           C  
ANISOU 4917  CG  LYS A 719    15858  18315  17042   -946   1269   3859
ATOM   4918  CD  LYS A 719      16.124  22.539  19.555  1.00135.60           C  
ANISOU 4918  CD  LYS A 719    15850  18709  16964  -1289   1023   4262
ATOM   4919  CE  LYS A 719      15.242  21.614  18.734  1.00134.22           C  
ANISOU 4919  CE  LYS A 719    15404  18432  17161  -1160    781   4610
ATOM   4920  NZ  LYS A 719      14.858  20.395  19.496  1.00135.16           N1+
ANISOU 4920  NZ  LYS A 719    15407  18828  17120  -1505    510   5028
ATOM   4921  N   LYS A 720      19.675  26.724  20.217  1.00135.89           N  
ANISOU 4921  N   LYS A 720    16877  18392  16365  -1137   1735   2776
ATOM   4922  CA  LYS A 720      20.382  27.666  21.076  1.00137.72           C  
ANISOU 4922  CA  LYS A 720    17387  18721  16218  -1298   1972   2454
ATOM   4923  C   LYS A 720      20.572  29.008  20.385  1.00137.69           C  
ANISOU 4923  C   LYS A 720    17472  18442  16404   -962   2250   2061
ATOM   4924  O   LYS A 720      20.551  30.054  21.045  1.00140.17           O  
ANISOU 4924  O   LYS A 720    17941  18841  16476  -1000   2644   1730
ATOM   4925  CB  LYS A 720      21.733  27.086  21.495  1.00136.18           C  
ANISOU 4925  CB  LYS A 720    17387  18536  15820  -1590   1535   2581
ATOM   4926  N   CYS A 721      20.748  29.000  19.062  1.00133.07           N  
ANISOU 4926  N   CYS A 721    16791  17525  16245   -650   2046   2089
ATOM   4927  CA  CYS A 721      20.836  30.251  18.317  1.00131.79           C  
ANISOU 4927  CA  CYS A 721    16681  17094  16299   -339   2278   1763
ATOM   4928  C   CYS A 721      19.538  31.043  18.437  1.00134.38           C  
ANISOU 4928  C   CYS A 721    16860  17466  16733   -166   2774   1601
ATOM   4929  O   CYS A 721      19.555  32.255  18.681  1.00135.91           O  
ANISOU 4929  O   CYS A 721    17169  17598  16874    -74   3125   1247
ATOM   4930  CB  CYS A 721      21.172  29.954  16.854  1.00127.64           C  
ANISOU 4930  CB  CYS A 721    16056  16248  16192    -88   1946   1874
ATOM   4931  SG  CYS A 721      21.491  31.399  15.824  1.00125.74           S  
ANISOU 4931  SG  CYS A 721    15893  15667  16218    241   2113   1534
ATOM   4932  N   ILE A 722      18.397  30.363  18.281  1.00132.49           N  
ANISOU 4932  N   ILE A 722    16350  17324  16666   -122   2802   1857
ATOM   4933  CA  ILE A 722      17.093  30.985  18.523  1.00135.55           C  
ANISOU 4933  CA  ILE A 722    16551  17791  17162     11   3278   1739
ATOM   4934  C   ILE A 722      17.053  31.610  19.911  1.00139.86           C  
ANISOU 4934  C   ILE A 722    17251  18619  17269   -214   3694   1453
ATOM   4935  O   ILE A 722      16.766  32.804  20.074  1.00141.89           O  
ANISOU 4935  O   ILE A 722    17540  18796  17575    -64   4114   1089
ATOM   4936  CB  ILE A 722      15.965  29.953  18.355  1.00136.08           C  
ANISOU 4936  CB  ILE A 722    16314  17990  17400      3   3196   2118
ATOM   4937  CG1 ILE A 722      15.908  29.445  16.917  1.00132.15           C  
ANISOU 4937  CG1 ILE A 722    15669  17192  17351    236   2824   2361
ATOM   4938  CG2 ILE A 722      14.636  30.548  18.780  1.00139.88           C  
ANISOU 4938  CG2 ILE A 722    16585  18601  17963    100   3713   1998
ATOM   4939  CD1 ILE A 722      15.622  30.528  15.928  1.00131.05           C  
ANISOU 4939  CD1 ILE A 722    15461  16729  17602    578   2997   2160
ATOM   4940  N   GLU A 723      17.345  30.800  20.934  1.00136.85           N  
ANISOU 4940  N   GLU A 723    16970  18570  16456   -597   3572   1615
ATOM   4941  CA  GLU A 723      17.290  31.287  22.307  1.00141.34           C  
ANISOU 4941  CA  GLU A 723    17699  19460  16542   -881   3956   1365
ATOM   4942  C   GLU A 723      18.279  32.418  22.563  1.00141.50           C  
ANISOU 4942  C   GLU A 723    18036  19347  16379   -883   4090    956
ATOM   4943  O   GLU A 723      18.140  33.130  23.564  1.00145.45           O  
ANISOU 4943  O   GLU A 723    18675  20047  16543  -1045   4502    641
ATOM   4944  CB  GLU A 723      17.536  30.134  23.280  1.00142.92           C  
ANISOU 4944  CB  GLU A 723    17962  20032  16309  -1340   3705   1675
ATOM   4945  CG  GLU A 723      16.455  29.065  23.243  1.00143.73           C  
ANISOU 4945  CG  GLU A 723    17756  20325  16530  -1392   3625   2068
ATOM   4946  CD  GLU A 723      15.110  29.572  23.731  1.00147.91           C  
ANISOU 4946  CD  GLU A 723    18085  21070  17043  -1339   4201   1906
ATOM   4947  OE1 GLU A 723      15.090  30.447  24.622  1.00151.55           O  
ANISOU 4947  OE1 GLU A 723    18696  21705  17183  -1463   4648   1531
ATOM   4948  OE2 GLU A 723      14.074  29.096  23.221  1.00147.73           O1-
ANISOU 4948  OE2 GLU A 723    17751  21039  17342  -1176   4211   2147
ATOM   4949  N   VAL A 724      19.272  32.600  21.691  1.00143.50           N  
ANISOU 4949  N   VAL A 724    18408  19278  16837   -723   3759    945
ATOM   4950  CA  VAL A 724      20.130  33.776  21.791  1.00143.88           C  
ANISOU 4950  CA  VAL A 724    18729  19158  16780   -677   3892    559
ATOM   4951  C   VAL A 724      19.476  34.980  21.124  1.00144.33           C  
ANISOU 4951  C   VAL A 724    18672  18937  17230   -286   4251    254
ATOM   4952  O   VAL A 724      19.516  36.095  21.656  1.00145.83           O  
ANISOU 4952  O   VAL A 724    19013  19105  17291   -274   4621   -143
ATOM   4953  CB  VAL A 724      21.519  33.482  21.194  1.00141.72           C  
ANISOU 4953  CB  VAL A 724    18625  18679  16544   -698   3390    677
ATOM   4954  CG1 VAL A 724      22.337  34.759  21.104  1.00142.34           C  
ANISOU 4954  CG1 VAL A 724    18952  18541  16591   -601   3513    298
ATOM   4955  CG2 VAL A 724      22.252  32.460  22.045  1.00141.27           C  
ANISOU 4955  CG2 VAL A 724    18704  18882  16090  -1119   3061    931
ATOM   4956  N   LEU A 725      18.853  34.779  19.959  1.00142.92           N  
ANISOU 4956  N   LEU A 725    18224  18532  17547     23   4137    439
ATOM   4957  CA  LEU A 725      18.256  35.903  19.246  1.00142.62           C  
ANISOU 4957  CA  LEU A 725    18058  18196  17937    383   4413    201
ATOM   4958  C   LEU A 725      16.986  36.421  19.906  1.00145.15           C  
ANISOU 4958  C   LEU A 725    18195  18652  18303    442   4958      3
ATOM   4959  O   LEU A 725      16.592  37.560  19.639  1.00145.35           O  
ANISOU 4959  O   LEU A 725    18160  18442  18625    694   5262   -293
ATOM   4960  CB  LEU A 725      17.967  35.529  17.792  1.00139.74           C  
ANISOU 4960  CB  LEU A 725    17464  17556  18076    655   4107    481
ATOM   4961  CG  LEU A 725      19.126  35.753  16.818  1.00137.72           C  
ANISOU 4961  CG  LEU A 725    17366  17013  17946    748   3734    478
ATOM   4962  CD1 LEU A 725      20.250  34.765  17.054  1.00137.88           C  
ANISOU 4962  CD1 LEU A 725    17566  17171  17650    485   3327    666
ATOM   4963  CD2 LEU A 725      18.637  35.679  15.383  1.00134.69           C  
ANISOU 4963  CD2 LEU A 725    16750  16353  18075   1025   3545    675
ATOM   4964  N   ILE A 726      16.334  35.627  20.763  1.00141.07           N  
ANISOU 4964  N   ILE A 726    17575  18505  17520    210   5091    157
ATOM   4965  CA  ILE A 726      15.194  36.157  21.510  1.00146.08           C  
ANISOU 4965  CA  ILE A 726    18044  19309  18148    234   5660    -82
ATOM   4966  C   ILE A 726      15.628  37.076  22.639  1.00149.88           C  
ANISOU 4966  C   ILE A 726    18808  19926  18215     49   6042   -552
ATOM   4967  O   ILE A 726      14.770  37.618  23.348  1.00154.60           O  
ANISOU 4967  O   ILE A 726    19298  20670  18772     50   6568   -836
ATOM   4968  CB  ILE A 726      14.297  35.024  22.053  1.00148.02           C  
ANISOU 4968  CB  ILE A 726    18070  19935  18237     28   5698    241
ATOM   4969  CG1 ILE A 726      15.071  34.084  22.984  1.00148.27           C  
ANISOU 4969  CG1 ILE A 726    18337  20328  17670   -432   5442    423
ATOM   4970  CG2 ILE A 726      13.678  34.240  20.906  1.00144.84           C  
ANISOU 4970  CG2 ILE A 726    17360  19367  18305    246   5380    671
ATOM   4971  CD1 ILE A 726      15.003  34.450  24.460  1.00153.55           C  
ANISOU 4971  CD1 ILE A 726    19176  21378  17786   -772   5874    119
ATOM   4972  N   ASP A 727      16.934  37.265  22.830  1.00152.61           N  
ANISOU 4972  N   ASP A 727    19506  20225  18253   -119   5799   -652
ATOM   4973  CA  ASP A 727      17.463  38.166  23.845  1.00154.22           C  
ANISOU 4973  CA  ASP A 727    20021  20527  18050   -313   6111  -1095
ATOM   4974  C   ASP A 727      17.839  39.534  23.297  1.00153.22           C  
ANISOU 4974  C   ASP A 727    20000  19988  18230    -16   6232  -1471
ATOM   4975  O   ASP A 727      17.788  40.520  24.040  1.00155.42           O  
ANISOU 4975  O   ASP A 727    20424  20282  18345    -57   6651  -1924
ATOM   4976  CB  ASP A 727      18.697  37.550  24.514  1.00154.56           C  
ANISOU 4976  CB  ASP A 727    20401  20790  17534   -732   5759   -958
ATOM   4977  CG  ASP A 727      18.358  36.353  25.379  1.00156.97           C  
ANISOU 4977  CG  ASP A 727    20654  21552  17435  -1120   5699   -653
ATOM   4978  OD1 ASP A 727      17.237  36.310  25.929  1.00160.12           O  
ANISOU 4978  OD1 ASP A 727    20858  22197  17782  -1161   6109   -724
ATOM   4979  OD2 ASP A 727      19.216  35.454  25.509  1.00156.09           O1-
ANISOU 4979  OD2 ASP A 727    20682  21550  17075  -1391   5233   -335
ATOM   4980  N   LYS A 728      18.219  39.613  22.025  1.00158.62           N  
ANISOU 4980  N   LYS A 728    20617  20308  19345    261   5870  -1299
ATOM   4981  CA  LYS A 728      18.657  40.864  21.418  1.00157.32           C  
ANISOU 4981  CA  LYS A 728    20552  19743  19480    518   5904  -1596
ATOM   4982  C   LYS A 728      17.546  41.909  21.437  1.00158.49           C  
ANISOU 4982  C   LYS A 728    20484  19718  20018    795   6413  -1934
ATOM   4983  O   LYS A 728      16.495  41.719  20.825  1.00158.23           O  
ANISOU 4983  O   LYS A 728    20095  19592  20434   1032   6486  -1764
ATOM   4984  CB  LYS A 728      19.115  40.625  19.981  1.00154.28           C  
ANISOU 4984  CB  LYS A 728    20082  19045  19493    739   5420  -1294
ATOM   4985  CG  LYS A 728      20.234  39.606  19.835  1.00153.79           C  
ANISOU 4985  CG  LYS A 728    20194  19100  19140    509   4909   -978
ATOM   4986  CD  LYS A 728      21.543  40.101  20.424  1.00154.24           C  
ANISOU 4986  CD  LYS A 728    20638  19169  18798    290   4818  -1198
ATOM   4987  CE  LYS A 728      22.662  39.098  20.171  1.00153.20           C  
ANISOU 4987  CE  LYS A 728    20628  19105  18475     96   4291   -869
ATOM   4988  NZ  LYS A 728      23.958  39.528  20.764  1.00153.41           N1+
ANISOU 4988  NZ  LYS A 728    21018  19149  18121   -139   4174  -1041
ATOM   4989  N   TYR A 730      15.401  40.037  18.866  1.00155.26           N  
ANISOU 4989  N   TYR A 730    19146  19089  20758   1314   5904   -878
ATOM   4990  CA  TYR A 730      14.671  40.369  17.650  1.00153.19           C  
ANISOU 4990  CA  TYR A 730    18579  18478  21148   1654   5830   -730
ATOM   4991  C   TYR A 730      13.394  39.540  17.551  1.00153.31           C  
ANISOU 4991  C   TYR A 730    18227  18647  21377   1700   5912   -418
ATOM   4992  O   TYR A 730      12.551  39.785  16.690  1.00151.95           O  
ANISOU 4992  O   TYR A 730    17754  18224  21757   1961   5914   -281
ATOM   4993  CB  TYR A 730      15.529  40.114  16.408  1.00150.50           C  
ANISOU 4993  CB  TYR A 730    18327  17895  20959   1717   5284   -470
ATOM   4994  CG  TYR A 730      16.837  40.872  16.355  1.00150.82           C  
ANISOU 4994  CG  TYR A 730    18709  17775  20822   1673   5142   -718
ATOM   4995  CD1 TYR A 730      16.876  42.217  16.015  1.00151.00           C  
ANISOU 4995  CD1 TYR A 730    18750  17459  21165   1880   5289  -1013
ATOM   4996  CD2 TYR A 730      18.039  40.227  16.610  1.00150.96           C  
ANISOU 4996  CD2 TYR A 730    19012  17961  20384   1421   4829   -632
ATOM   4997  CE1 TYR A 730      18.078  42.903  15.956  1.00150.92           C  
ANISOU 4997  CE1 TYR A 730    19050  17305  20988   1828   5138  -1217
ATOM   4998  CE2 TYR A 730      19.241  40.902  16.550  1.00150.65           C  
ANISOU 4998  CE2 TYR A 730    19270  17780  20191   1374   4687   -834
ATOM   4999  CZ  TYR A 730      19.256  42.238  16.225  1.00150.50           C  
ANISOU 4999  CZ  TYR A 730    19277  17444  20460   1573   4843  -1124
ATOM   5000  OH  TYR A 730      20.457  42.908  16.168  1.00149.68           O  
ANISOU 5000  OH  TYR A 730    19469  17205  20198   1513   4687  -1308
ATOM   5001  N   ILE A 731      13.264  38.548  18.431  1.00152.55           N  
ANISOU 5001  N   ILE A 731    18153  18964  20844   1425   5953   -278
ATOM   5002  CA  ILE A 731      12.230  37.525  18.327  1.00152.91           C  
ANISOU 5002  CA  ILE A 731    17887  19199  21013   1408   5921    100
ATOM   5003  C   ILE A 731      11.546  37.365  19.678  1.00157.95           C  
ANISOU 5003  C   ILE A 731    18460  20245  21310   1203   6386    -52
ATOM   5004  O   ILE A 731      12.201  37.410  20.725  1.00159.68           O  
ANISOU 5004  O   ILE A 731    18961  20721  20988    924   6514   -278
ATOM   5005  CB  ILE A 731      12.827  36.181  17.853  1.00148.50           C  
ANISOU 5005  CB  ILE A 731    17407  18743  20273   1238   5359    547
ATOM   5006  CG1 ILE A 731      13.430  36.328  16.455  1.00143.86           C  
ANISOU 5006  CG1 ILE A 731    16859  17771  20030   1433   4934    682
ATOM   5007  CG2 ILE A 731      11.779  35.079  17.858  1.00149.18           C  
ANISOU 5007  CG2 ILE A 731    17193  19047  20442   1181   5314    942
ATOM   5008  CD1 ILE A 731      14.271  35.149  16.032  1.00139.72           C  
ANISOU 5008  CD1 ILE A 731    16467  17316  19305   1264   4403   1010
ATOM   5009  N   GLU A 732      10.226  37.176  19.653  1.00162.53           N  
ANISOU 5009  N   GLU A 732    18662  20892  22198   1321   6636     80
ATOM   5010  CA  GLU A 732       9.434  36.957  20.854  1.00166.18           C  
ANISOU 5010  CA  GLU A 732    19000  21768  22372   1127   7094    -31
ATOM   5011  C   GLU A 732       8.541  35.737  20.666  1.00165.72           C  
ANISOU 5011  C   GLU A 732    18641  21925  22401   1059   6931    467
ATOM   5012  O   GLU A 732       8.106  35.432  19.552  1.00162.48           O  
ANISOU 5012  O   GLU A 732    18006  21261  22470   1280   6643    800
ATOM   5013  CB  GLU A 732       8.572  38.185  21.192  1.00168.95           C  
ANISOU 5013  CB  GLU A 732    19145  21994  23053   1356   7715   -478
ATOM   5014  CG  GLU A 732       7.795  38.065  22.493  1.00174.79           C  
ANISOU 5014  CG  GLU A 732    19767  23185  23461   1140   8261   -674
ATOM   5015  CD  GLU A 732       6.951  39.285  22.784  1.00180.08           C  
ANISOU 5015  CD  GLU A 732    20206  23699  24515   1392   8891  -1152
ATOM   5016  OE1 GLU A 732       6.952  40.219  21.955  1.00179.11           O  
ANISOU 5016  OE1 GLU A 732    20006  23094  24953   1739   8866  -1298
ATOM   5017  OE2 GLU A 732       6.283  39.308  23.839  1.00185.43           O1-
ANISOU 5017  OE2 GLU A 732    20770  24737  24949   1232   9408  -1384
ATOM   5018  N   ARG A 733       8.277  35.037  21.769  1.00173.97           N  
ANISOU 5018  N   ARG A 733    19691  23449  22962    725   7102    527
ATOM   5019  CA  ARG A 733       7.380  33.888  21.782  1.00174.41           C  
ANISOU 5019  CA  ARG A 733    19458  23765  23045    614   6990    985
ATOM   5020  C   ARG A 733       6.481  33.987  23.005  1.00179.32           C  
ANISOU 5020  C   ARG A 733    19914  24812  23408    430   7578    788
ATOM   5021  O   ARG A 733       6.964  34.238  24.112  1.00182.82           O  
ANISOU 5021  O   ARG A 733    20610  25547  23305    143   7839    472
ATOM   5022  CB  ARG A 733       8.168  32.572  21.787  1.00173.33           C  
ANISOU 5022  CB  ARG A 733    19522  23812  22523    307   6411   1402
ATOM   5023  CG  ARG A 733       8.894  32.305  20.476  1.00170.53           C  
ANISOU 5023  CG  ARG A 733    19260  23057  22478    496   5834   1640
ATOM   5024  CD  ARG A 733       9.708  31.021  20.503  1.00169.19           C  
ANISOU 5024  CD  ARG A 733    19272  23039  21973    206   5276   2009
ATOM   5025  NE  ARG A 733      10.351  30.781  19.214  1.00164.17           N  
ANISOU 5025  NE  ARG A 733    18699  22023  21656    397   4772   2195
ATOM   5026  CZ  ARG A 733      11.174  29.770  18.956  1.00162.04           C  
ANISOU 5026  CZ  ARG A 733    18578  21759  21230    230   4246   2477
ATOM   5027  NH1 ARG A 733      11.473  28.894  19.905  1.00164.02           N  
ANISOU 5027  NH1 ARG A 733    18930  22361  21029   -139   4112   2641
ATOM   5028  NH2 ARG A 733      11.699  29.639  17.746  1.00158.03           N1+
ANISOU 5028  NH2 ARG A 733    18109  20906  21031    418   3851   2592
ATOM   5029  N   SER A 734       5.176  33.791  22.802  1.00200.15           N  
ANISOU 5029  N   SER A 734    22124  27494  26429    576   7787    977
ATOM   5030  CA  SER A 734       4.190  34.077  23.842  1.00203.84           C  
ANISOU 5030  CA  SER A 734    22363  28318  26771    474   8432    729
ATOM   5031  C   SER A 734       3.835  32.847  24.677  1.00204.91           C  
ANISOU 5031  C   SER A 734    22440  29011  26406     51   8376   1076
ATOM   5032  O   SER A 734       4.052  32.833  25.893  1.00208.50           O  
ANISOU 5032  O   SER A 734    23071  29892  26256   -314   8669    845
ATOM   5033  CB  SER A 734       2.926  34.670  23.209  1.00203.65           C  
ANISOU 5033  CB  SER A 734    21865  28021  27490    879   8746    708
ATOM   5034  OG  SER A 734       3.197  35.923  22.605  1.00202.89           O  
ANISOU 5034  OG  SER A 734    21811  27435  27844   1235   8862    339
ATOM   5035  N   GLN A 735       3.289  31.811  24.043  1.00220.47           N  
ANISOU 5035  N   GLN A 735    24169  30988  28612     69   7989   1639
ATOM   5036  CA  GLN A 735       2.803  30.653  24.781  1.00222.02           C  
ANISOU 5036  CA  GLN A 735    24250  31696  28410   -315   7933   2007
ATOM   5037  C   GLN A 735       2.770  29.447  23.854  1.00219.21           C  
ANISOU 5037  C   GLN A 735    23801  31212  28276   -301   7258   2644
ATOM   5038  O   GLN A 735       2.387  29.566  22.687  1.00217.13           O  
ANISOU 5038  O   GLN A 735    23340  30542  28617     59   7066   2818
ATOM   5039  CB  GLN A 735       1.410  30.916  25.368  1.00224.84           C  
ANISOU 5039  CB  GLN A 735    24192  32334  28903   -292   8562   1894
ATOM   5040  CG  GLN A 735       0.891  29.804  26.263  1.00226.33           C  
ANISOU 5040  CG  GLN A 735    24263  33113  28618   -738   8567   2238
ATOM   5041  CD  GLN A 735       1.755  29.599  27.493  1.00227.92           C  
ANISOU 5041  CD  GLN A 735    24852  33754  27994  -1244   8611   2060
ATOM   5042  OE1 GLN A 735       2.516  28.636  27.578  1.00225.63           O  
ANISOU 5042  OE1 GLN A 735    24801  33586  27344  -1550   8055   2420
ATOM   5043  NE2 GLN A 735       1.643  30.511  28.453  1.00231.62           N  
ANISOU 5043  NE2 GLN A 735    25381  34450  28174  -1345   9267   1498
ATOM   5044  N   ALA A 736       3.173  28.290  24.382  1.00228.36           N  
ANISOU 5044  N   ALA A 736    25106  32713  28949   -712   6889   2991
ATOM   5045  CA  ALA A 736       3.275  27.066  23.589  1.00224.86           C  
ANISOU 5045  CA  ALA A 736    24618  32152  28666   -742   6211   3574
ATOM   5046  C   ALA A 736       2.101  26.141  23.903  1.00225.21           C  
ANISOU 5046  C   ALA A 736    24307  32549  28714   -921   6234   4008
ATOM   5047  O   ALA A 736       2.201  25.198  24.688  1.00225.26           O  
ANISOU 5047  O   ALA A 736    24373  32964  28253  -1346   6049   4280
ATOM   5048  CB  ALA A 736       4.616  26.381  23.839  1.00222.99           C  
ANISOU 5048  CB  ALA A 736    24777  31971  27978  -1051   5696   3692
ATOM   5049  N   SER A 737       0.966  26.426  23.267  1.00225.60           N  
ANISOU 5049  N   SER A 737    23971  32428  29319   -602   6445   4094
ATOM   5050  CA  SER A 737      -0.106  25.454  23.085  1.00224.13           C  
ANISOU 5050  CA  SER A 737    23428  32412  29321   -672   6283   4622
ATOM   5051  C   SER A 737      -0.118  24.907  21.667  1.00219.67           C  
ANISOU 5051  C   SER A 737    22794  31401  29271   -418   5694   5029
ATOM   5052  O   SER A 737      -0.245  23.694  21.467  1.00216.80           O  
ANISOU 5052  O   SER A 737    22380  31132  28864   -603   5211   5534
ATOM   5053  CB  SER A 737      -1.466  26.080  23.410  1.00226.29           C  
ANISOU 5053  CB  SER A 737    23272  32839  29867   -526   6935   4479
ATOM   5054  OG  SER A 737      -1.556  26.428  24.781  1.00230.32           O  
ANISOU 5054  OG  SER A 737    23823  33836  29853   -822   7490   4130
ATOM   5055  N   ALA A 738       0.007  25.793  20.685  1.00209.00           N  
ANISOU 5055  N   ALA A 738    21444  29566  28401    -15   5725   4812
ATOM   5056  CA  ALA A 738       0.476  25.464  19.349  1.00204.37           C  
ANISOU 5056  CA  ALA A 738    20956  28525  28172    187   5147   5053
ATOM   5057  C   ALA A 738       1.766  26.240  19.132  1.00203.83           C  
ANISOU 5057  C   ALA A 738    21270  28185  27991    292   5096   4634
ATOM   5058  O   ALA A 738       1.832  27.430  19.456  1.00206.11           O  
ANISOU 5058  O   ALA A 738    21594  28412  28308    440   5573   4162
ATOM   5059  CB  ALA A 738      -0.562  25.820  18.282  1.00202.37           C  
ANISOU 5059  CB  ALA A 738    20347  27934  28609    540   5185   5225
ATOM   5060  N   ASP A 739       2.792  25.561  18.616  1.00184.96           N  
ANISOU 5060  N   ASP A 739    19159  25639  25478    208   4527   4797
ATOM   5061  CA  ASP A 739       4.105  26.179  18.464  1.00184.74           C  
ANISOU 5061  CA  ASP A 739    19501  25393  25298    263   4439   4434
ATOM   5062  C   ASP A 739       3.996  27.490  17.694  1.00183.89           C  
ANISOU 5062  C   ASP A 739    19343  24887  25638    650   4696   4109
ATOM   5063  O   ASP A 739       3.245  27.598  16.721  1.00181.49           O  
ANISOU 5063  O   ASP A 739    18790  24316  25852    897   4622   4303
ATOM   5064  CB  ASP A 739       5.064  25.220  17.756  1.00182.09           C  
ANISOU 5064  CB  ASP A 739    19386  24879  24921    181   3768   4701
ATOM   5065  CG  ASP A 739       5.452  24.036  18.626  1.00182.85           C  
ANISOU 5065  CG  ASP A 739    19592  25332  24549   -225   3484   4959
ATOM   5066  OD1 ASP A 739       5.469  24.190  19.867  1.00186.29           O  
ANISOU 5066  OD1 ASP A 739    20086  26145  24549   -481   3803   4801
ATOM   5067  OD2 ASP A 739       5.742  22.954  18.072  1.00179.81           O1-
ANISOU 5067  OD2 ASP A 739    19235  24848  24238   -304   2934   5318
ATOM   5068  N   GLU A 740       4.742  28.494  18.150  1.00175.23           N  
ANISOU 5068  N   GLU A 740    18485  23749  24343    681   4982   3627
ATOM   5069  CA  GLU A 740       4.570  29.852  17.656  1.00175.25           C  
ANISOU 5069  CA  GLU A 740    18424  23415  24748   1019   5303   3274
ATOM   5070  C   GLU A 740       5.837  30.653  17.920  1.00175.47           C  
ANISOU 5070  C   GLU A 740    18834  23337  24498   1005   5356   2833
ATOM   5071  O   GLU A 740       6.412  30.575  19.008  1.00178.34           O  
ANISOU 5071  O   GLU A 740    19421  24008  24330    735   5496   2639
ATOM   5072  CB  GLU A 740       3.357  30.519  18.321  1.00178.53           C  
ANISOU 5072  CB  GLU A 740    18511  23988  25335   1108   5929   3091
ATOM   5073  CG  GLU A 740       2.994  31.891  17.775  1.00178.31           C  
ANISOU 5073  CG  GLU A 740    18337  23572  25841   1478   6251   2770
ATOM   5074  CD  GLU A 740       3.734  33.012  18.480  1.00181.00           C  
ANISOU 5074  CD  GLU A 740    18940  23898  25936   1486   6626   2184
ATOM   5075  OE1 GLU A 740       4.073  32.845  19.671  1.00183.69           O  
ANISOU 5075  OE1 GLU A 740    19459  24626  25710   1200   6854   1985
ATOM   5076  OE2 GLU A 740       3.975  34.060  17.845  1.00180.45           O1-
ANISOU 5076  OE2 GLU A 740    18902  23428  26233   1757   6677   1933
ATOM   5077  N   TYR A 741       6.258  31.422  16.916  1.00162.19           N  
ANISOU 5077  N   TYR A 741    17224  21228  23174   1274   5230   2695
ATOM   5078  CA  TYR A 741       7.439  32.275  17.034  1.00162.52           C  
ANISOU 5078  CA  TYR A 741    17611  21122  23019   1292   5264   2288
ATOM   5079  C   TYR A 741       7.202  33.525  16.200  1.00160.80           C  
ANISOU 5079  C   TYR A 741    17286  20476  23334   1643   5420   2067
ATOM   5080  O   TYR A 741       7.215  33.459  14.966  1.00156.28           O  
ANISOU 5080  O   TYR A 741    16650  19586  23143   1808   5068   2293
ATOM   5081  CB  TYR A 741       8.698  31.542  16.578  1.00160.24           C  
ANISOU 5081  CB  TYR A 741    17625  20770  22488   1152   4706   2448
ATOM   5082  N   SER A 742       6.990  34.655  16.866  1.00160.68           N  
ANISOU 5082  N   SER A 742    17253  20448  23348   1736   5933   1629
ATOM   5083  CA  SER A 742       6.753  35.924  16.197  1.00159.17           C  
ANISOU 5083  CA  SER A 742    16950  19840  23689   2059   6102   1392
ATOM   5084  C   SER A 742       8.052  36.716  16.085  1.00158.27           C  
ANISOU 5084  C   SER A 742    17210  19523  23402   2071   5999   1056
ATOM   5085  O   SER A 742       9.100  36.324  16.603  1.00159.58           O  
ANISOU 5085  O   SER A 742    17712  19885  23038   1833   5843    983
ATOM   5086  CB  SER A 742       5.691  36.737  16.948  1.00162.66           C  
ANISOU 5086  CB  SER A 742    17110  20340  24353   2183   6736   1089
ATOM   5087  OG  SER A 742       5.473  37.989  16.321  1.00162.13           O  
ANISOU 5087  OG  SER A 742    16919  19833  24851   2498   6879    859
ATOM   5088  N   TYR A 743       7.970  37.851  15.394  1.00147.29           N  
ANISOU 5088  N   TYR A 743    15747  17727  22489   2342   6068    872
ATOM   5089  CA  TYR A 743       9.123  38.701  15.147  1.00145.38           C  
ANISOU 5089  CA  TYR A 743    15824  17247  22168   2381   5952    579
ATOM   5090  C   TYR A 743       8.921  40.066  15.790  1.00149.81           C  
ANISOU 5090  C   TYR A 743    16370  17673  22877   2522   6462     67
ATOM   5091  O   TYR A 743       7.799  40.571  15.878  1.00153.66           O  
ANISOU 5091  O   TYR A 743    16517  18061  23804   2711   6820    -14
ATOM   5092  CB  TYR A 743       9.379  38.865  13.644  1.00141.41           C  
ANISOU 5092  CB  TYR A 743    15292  16351  22088   2545   5500    824
ATOM   5093  CG  TYR A 743      10.584  39.718  13.316  1.00139.35           C  
ANISOU 5093  CG  TYR A 743    15346  15853  21749   2570   5348    559
ATOM   5094  CD1 TYR A 743      11.872  39.234  13.498  1.00136.22           C  
ANISOU 5094  CD1 TYR A 743    15313  15609  20836   2356   5076    536
ATOM   5095  CD2 TYR A 743      10.434  41.004  12.816  1.00140.71           C  
ANISOU 5095  CD2 TYR A 743    15436  15637  22391   2800   5457    352
ATOM   5096  CE1 TYR A 743      12.976  40.009  13.198  1.00134.45           C  
ANISOU 5096  CE1 TYR A 743    15364  15178  20542   2371   4935    310
ATOM   5097  CE2 TYR A 743      11.532  41.786  12.512  1.00138.94           C  
ANISOU 5097  CE2 TYR A 743    15495  15202  22092   2807   5300    131
ATOM   5098  CZ  TYR A 743      12.800  41.284  12.705  1.00135.77           C  
ANISOU 5098  CZ  TYR A 743    15456  14980  21151   2592   5048    110
ATOM   5099  OH  TYR A 743      13.896  42.059  12.403  1.00134.11           O  
ANISOU 5099  OH  TYR A 743    15516  14571  20868   2591   4891    -96
ATOM   5100  N   VAL A 744      10.026  40.653  16.245  1.00151.66           N  
ANISOU 5100  N   VAL A 744    16969  17895  22759   2427   6489   -283
ATOM   5101  CA  VAL A 744      10.047  41.991  16.822  1.00155.09           C  
ANISOU 5101  CA  VAL A 744    17462  18166  23299   2544   6921   -808
ATOM   5102  C   VAL A 744      11.036  42.830  16.025  1.00152.21           C  
ANISOU 5102  C   VAL A 744    17322  17419  23091   2651   6623   -919
ATOM   5103  O   VAL A 744      12.097  42.337  15.625  1.00149.04           O  
ANISOU 5103  O   VAL A 744    17192  17054  22384   2506   6195   -748
ATOM   5104  CB  VAL A 744      10.424  41.958  18.319  1.00158.26           C  
ANISOU 5104  CB  VAL A 744    18118  18960  23053   2273   7288  -1168
ATOM   5105  CG1 VAL A 744      10.510  43.367  18.890  1.00162.38           C  
ANISOU 5105  CG1 VAL A 744    18732  19291  23675   2386   7726  -1749
ATOM   5106  CG2 VAL A 744       9.424  41.120  19.103  1.00161.38           C  
ANISOU 5106  CG2 VAL A 744    18277  19765  23274   2135   7581  -1040
ATOM   5107  N   ALA A 745      10.683  44.091  15.788  1.00164.45           N  
ANISOU 5107  N   ALA A 745    18742  18598  25142   2900   6843  -1199
ATOM   5108  CA  ALA A 745      11.499  44.993  14.977  1.00162.78           C  
ANISOU 5108  CA  ALA A 745    18700  17994  25156   3012   6563  -1287
ATOM   5109  C   ALA A 745      12.935  45.112  15.490  1.00164.20           C  
ANISOU 5109  C   ALA A 745    19355  18298  24736   2793   6442  -1517
ATOM   5110  O   ALA A 745      13.831  45.540  14.760  1.00161.95           O  
ANISOU 5110  O   ALA A 745    19258  17775  24502   2813   6099  -1490
ATOM   5111  CB  ALA A 745      10.851  46.368  14.919  1.00163.08           C  
ANISOU 5111  CB  ALA A 745    18523  17637  25804   3288   6884  -1611
ATOM   5112  OXT ALA A 745      13.240  44.784  16.637  1.00167.83           O1-
ANISOU 5112  OXT ALA A 745    20019  19105  24645   2572   6671  -1719
TER    5113      ALA A 745
ATOM   5114  N   THR V 157     -19.116  33.590 -61.639  1.00270.15           N  
ANISOU 5114  N   THR V 157    30910  51470  20266  19718   1732   4570
ATOM   5115  CA  THR V 157     -19.720  32.437 -62.296  1.00270.46           C  
ANISOU 5115  CA  THR V 157    31017  51371  20373  19751   1637   4522
ATOM   5116  C   THR V 157     -20.557  32.868 -63.496  1.00270.98           C  
ANISOU 5116  C   THR V 157    31174  51313  20474  19766   1527   4517
ATOM   5117  O   THR V 157     -21.256  33.879 -63.446  1.00270.88           O  
ANISOU 5117  O   THR V 157    31186  51201  20533  19716   1478   4560
ATOM   5118  CB  THR V 157     -20.601  31.633 -61.325  1.00269.91           C  
ANISOU 5118  CB  THR V 157    30935  51153  20463  19683   1593   4534
ATOM   5119  OG1 THR V 157     -21.663  32.465 -60.842  1.00269.46           O  
ANISOU 5119  OG1 THR V 157    30873  51001  20508  19612   1556   4562
ATOM   5120  CG2 THR V 157     -19.778  31.136 -60.148  1.00269.66           C  
ANISOU 5120  CG2 THR V 157    30808  51247  20404  19659   1677   4565
ATOM   5121  N   LEU V 158     -20.477  32.091 -64.579  1.00271.67           N  
ANISOU 5121  N   LEU V 158    31303  51413  20508  19843   1472   4460
ATOM   5122  CA  LEU V 158     -21.217  32.432 -65.789  1.00272.38           C  
ANISOU 5122  CA  LEU V 158    31467  51416  20607  19858   1361   4463
ATOM   5123  C   LEU V 158     -22.711  32.193 -65.609  1.00271.95           C  
ANISOU 5123  C   LEU V 158    31475  51107  20745  19802   1253   4462
ATOM   5124  O   LEU V 158     -23.532  33.013 -66.036  1.00272.19           O  
ANISOU 5124  O   LEU V 158    31557  51022  20842  19768   1164   4500
ATOM   5125  CB  LEU V 158     -20.683  31.627 -66.973  1.00273.52           C  
ANISOU 5125  CB  LEU V 158    31610  51704  20612  19970   1334   4385
ATOM   5126  CG  LEU V 158     -21.283  31.932 -68.347  1.00274.57           C  
ANISOU 5126  CG  LEU V 158    31799  51819  20707  19990   1220   4394
ATOM   5127  CD1 LEU V 158     -20.963  33.357 -68.772  1.00275.17           C  
ANISOU 5127  CD1 LEU V 158    31870  51981  20703  19936   1211   4507
ATOM   5128  CD2 LEU V 158     -20.788  30.935 -69.382  1.00275.81           C  
ANISOU 5128  CD2 LEU V 158    31923  52159  20714  20120   1193   4282
ATOM   5129  N   LYS V 159     -23.080  31.077 -64.977  1.00276.59           N  
ANISOU 5129  N   LYS V 159    32053  51609  21431  19792   1242   4425
ATOM   5130  CA  LYS V 159     -24.490  30.747 -64.798  1.00276.35           C  
ANISOU 5130  CA  LYS V 159    32056  51374  21569  19742   1139   4421
ATOM   5131  C   LYS V 159     -25.213  31.811 -63.981  1.00275.79           C  
ANISOU 5131  C   LYS V 159    31957  51242  21589  19662   1134   4463
ATOM   5132  O   LYS V 159     -26.229  32.363 -64.418  1.00276.06           O  
ANISOU 5132  O   LYS V 159    32034  51151  21705  19649   1031   4459
ATOM   5133  CB  LYS V 159     -24.622  29.378 -64.129  1.00276.22           C  
ANISOU 5133  CB  LYS V 159    32012  51299  21641  19734   1122   4404
ATOM   5134  CG  LYS V 159     -26.055  28.918 -63.925  1.00276.15           C  
ANISOU 5134  CG  LYS V 159    32016  51115  21795  19684   1015   4404
ATOM   5135  CD  LYS V 159     -26.101  27.536 -63.296  1.00276.37           C  
ANISOU 5135  CD  LYS V 159    32008  51083  21916  19673    975   4418
ATOM   5136  CE  LYS V 159     -27.531  27.091 -63.046  1.00276.45           C  
ANISOU 5136  CE  LYS V 159    32009  50957  22074  19620    870   4432
ATOM   5137  NZ  LYS V 159     -27.595  25.738 -62.427  1.00276.97           N1+
ANISOU 5137  NZ  LYS V 159    32034  50954  22246  19602    805   4478
ATOM   5138  N   GLU V 160     -24.693  32.121 -62.792  1.00282.34           N  
ANISOU 5138  N   GLU V 160    32702  52173  22402  19620   1232   4494
ATOM   5139  CA  GLU V 160     -25.423  32.991 -61.877  1.00282.01           C  
ANISOU 5139  CA  GLU V 160    32601  52107  22442  19562   1218   4505
ATOM   5140  C   GLU V 160     -25.421  34.439 -62.355  1.00282.43           C  
ANISOU 5140  C   GLU V 160    32690  52136  22484  19577   1176   4519
ATOM   5141  O   GLU V 160     -26.415  35.154 -62.182  1.00282.68           O  
ANISOU 5141  O   GLU V 160    32716  52063  22628  19563   1077   4497
ATOM   5142  CB  GLU V 160     -24.835  32.881 -60.470  1.00281.46           C  
ANISOU 5142  CB  GLU V 160    32413  52192  22336  19518   1331   4533
ATOM   5143  CG  GLU V 160     -25.603  33.651 -59.411  1.00281.32           C  
ANISOU 5143  CG  GLU V 160    32296  52212  22382  19471   1315   4521
ATOM   5144  CD  GLU V 160     -25.047  33.433 -58.018  1.00280.96           C  
ANISOU 5144  CD  GLU V 160    32111  52363  22277  19424   1424   4557
ATOM   5145  OE1 GLU V 160     -24.049  32.693 -57.884  1.00280.80           O  
ANISOU 5145  OE1 GLU V 160    32085  52419  22188  19424   1503   4601
ATOM   5146  OE2 GLU V 160     -25.610  33.997 -57.057  1.00281.02           O1-
ANISOU 5146  OE2 GLU V 160    32003  52465  22306  19393   1418   4534
ATOM   5147  N   ARG V 161     -24.322  34.894 -62.962  1.00278.96           N  
ANISOU 5147  N   ARG V 161    32278  51796  21918  19612   1229   4557
ATOM   5148  CA  ARG V 161     -24.295  36.265 -63.460  1.00279.69           C  
ANISOU 5148  CA  ARG V 161    32408  51849  22013  19617   1157   4605
ATOM   5149  C   ARG V 161     -25.062  36.421 -64.766  1.00280.64           C  
ANISOU 5149  C   ARG V 161    32632  51812  22185  19632    999   4623
ATOM   5150  O   ARG V 161     -25.555  37.516 -65.055  1.00281.45           O  
ANISOU 5150  O   ARG V 161    32776  51792  22368  19622    868   4665
ATOM   5151  CB  ARG V 161     -22.856  36.756 -63.620  1.00279.95           C  
ANISOU 5151  CB  ARG V 161    32414  52073  21881  19635   1259   4662
ATOM   5152  CG  ARG V 161     -22.181  37.073 -62.293  1.00279.26           C  
ANISOU 5152  CG  ARG V 161    32220  52132  21755  19615   1387   4659
ATOM   5153  CD  ARG V 161     -20.807  37.691 -62.484  1.00279.67           C  
ANISOU 5153  CD  ARG V 161    32236  52378  21648  19635   1475   4716
ATOM   5154  NE  ARG V 161     -20.166  37.987 -61.205  1.00279.05           N  
ANISOU 5154  NE  ARG V 161    32048  52455  21525  19618   1598   4710
ATOM   5155  CZ  ARG V 161     -20.321  39.129 -60.541  1.00279.24           C  
ANISOU 5155  CZ  ARG V 161    32033  52468  21599  19601   1567   4726
ATOM   5156  NH1 ARG V 161     -21.097  40.085 -61.032  1.00280.12           N  
ANISOU 5156  NH1 ARG V 161    32216  52389  21827  19602   1399   4753
ATOM   5157  NH2 ARG V 161     -19.701  39.315 -59.383  1.00278.74           N1+
ANISOU 5157  NH2 ARG V 161    31855  52584  21471  19590   1685   4713
ATOM   5158  N   CYS V 162     -25.181  35.358 -65.566  1.00278.30           N  
ANISOU 5158  N   CYS V 162    32377  51514  21849  19661    988   4592
ATOM   5159  CA  CYS V 162     -26.128  35.408 -66.676  1.00279.17           C  
ANISOU 5159  CA  CYS V 162    32572  51479  22021  19670    830   4598
ATOM   5160  C   CYS V 162     -27.562  35.426 -66.163  1.00278.93           C  
ANISOU 5160  C   CYS V 162    32539  51261  22180  19646    728   4546
ATOM   5161  O   CYS V 162     -28.422  36.098 -66.741  1.00279.79           O  
ANISOU 5161  O   CYS V 162    32702  51220  22386  19643    569   4565
ATOM   5162  CB  CYS V 162     -25.903  34.239 -67.634  1.00279.50           C  
ANISOU 5162  CB  CYS V 162    32639  51596  21963  19723    840   4557
ATOM   5163  SG  CYS V 162     -24.415  34.378 -68.649  1.00280.53           S  
ANISOU 5163  SG  CYS V 162    32753  51989  21846  19773    902   4600
ATOM   5164  N   LEU V 163     -27.836  34.700 -65.075  1.00286.53           N  
ANISOU 5164  N   LEU V 163    33428  52246  23194  19626    802   4487
ATOM   5165  CA  LEU V 163     -29.124  34.840 -64.402  1.00286.46           C  
ANISOU 5165  CA  LEU V 163    33372  52129  23340  19602    716   4432
ATOM   5166  C   LEU V 163     -29.366  36.285 -63.980  1.00286.96           C  
ANISOU 5166  C   LEU V 163    33407  52144  23483  19604    643   4432
ATOM   5167  O   LEU V 163     -30.468  36.817 -64.156  1.00287.71           O  
ANISOU 5167  O   LEU V 163    33506  52095  23714  19619    488   4389
ATOM   5168  CB  LEU V 163     -29.189  33.916 -63.184  1.00285.61           C  
ANISOU 5168  CB  LEU V 163    33162  52116  23240  19566    813   4401
ATOM   5169  CG  LEU V 163     -29.279  32.399 -63.353  1.00285.39           C  
ANISOU 5169  CG  LEU V 163    33147  52084  23205  19564    830   4394
ATOM   5170  CD1 LEU V 163     -29.111  31.710 -62.009  1.00284.84           C  
ANISOU 5170  CD1 LEU V 163    32965  52124  23138  19515    915   4412
ATOM   5171  CD2 LEU V 163     -30.607  32.014 -63.975  1.00285.90           C  
ANISOU 5171  CD2 LEU V 163    33247  52007  23373  19575    692   4348
ATOM   5172  N   GLN V 164     -28.338  36.938 -63.431  1.00285.72           N  
ANISOU 5172  N   GLN V 164    33210  52102  23247  19599    737   4472
ATOM   5173  CA  GLN V 164     -28.495  38.307 -62.951  1.00286.38           C  
ANISOU 5173  CA  GLN V 164    33255  52139  23416  19613    656   4463
ATOM   5174  C   GLN V 164     -28.688  39.285 -64.104  1.00287.79           C  
ANISOU 5174  C   GLN V 164    33545  52141  23660  19636    473   4534
ATOM   5175  O   GLN V 164     -29.454  40.248 -63.985  1.00288.82           O  
ANISOU 5175  O   GLN V 164    33665  52120  23952  19664    304   4499
ATOM   5176  CB  GLN V 164     -27.286  38.701 -62.102  1.00285.87           C  
ANISOU 5176  CB  GLN V 164    33120  52260  23239  19603    805   4494
ATOM   5177  CG  GLN V 164     -27.179  37.930 -60.795  1.00284.81           C  
ANISOU 5177  CG  GLN V 164    32856  52303  23057  19570    950   4441
ATOM   5178  CD  GLN V 164     -25.940  38.289 -60.000  1.00284.39           C  
ANISOU 5178  CD  GLN V 164    32728  52449  22877  19560   1097   4476
ATOM   5179  OE1 GLN V 164     -25.104  39.073 -60.450  1.00284.82           O  
ANISOU 5179  OE1 GLN V 164    32827  52518  22872  19581   1103   4538
ATOM   5180  NE2 GLN V 164     -25.815  37.714 -58.809  1.00283.69           N  
ANISOU 5180  NE2 GLN V 164    32516  52535  22740  19524   1208   4450
ATOM   5181  N   VAL V 165     -28.001  39.060 -65.227  1.00290.39           N  
ANISOU 5181  N   VAL V 165    33970  52498  23867  19626    485   4633
ATOM   5182  CA  VAL V 165     -28.191  39.923 -66.389  1.00292.01           C  
ANISOU 5182  CA  VAL V 165    34282  52556  24110  19623    290   4739
ATOM   5183  C   VAL V 165     -29.572  39.708 -66.998  1.00292.66           C  
ANISOU 5183  C   VAL V 165    34412  52449  24337  19637    116   4694
ATOM   5184  O   VAL V 165     -30.199  40.659 -67.483  1.00294.17           O  
ANISOU 5184  O   VAL V 165    34659  52449  24664  19644   -105   4744
ATOM   5185  CB  VAL V 165     -27.067  39.690 -67.418  1.00292.41           C  
ANISOU 5185  CB  VAL V 165    34391  52758  23952  19599    352   4855
ATOM   5186  CG1 VAL V 165     -27.339  40.462 -68.700  1.00294.34           C  
ANISOU 5186  CG1 VAL V 165    34749  52877  24210  19565    128   4996
ATOM   5187  CG2 VAL V 165     -25.724  40.105 -66.836  1.00292.07           C  
ANISOU 5187  CG2 VAL V 165    34292  52903  23777  19589    497   4903
ATOM   5188  N   VAL V 166     -30.079  38.473 -66.970  1.00296.03           N  
ANISOU 5188  N   VAL V 166    34814  52916  24748  19642    193   4606
ATOM   5189  CA  VAL V 166     -31.395  38.202 -67.542  1.00296.65           C  
ANISOU 5189  CA  VAL V 166    34925  52839  24949  19657     36   4556
ATOM   5190  C   VAL V 166     -32.498  38.787 -66.666  1.00296.95           C  
ANISOU 5190  C   VAL V 166    34882  52757  25190  19685    -75   4447
ATOM   5191  O   VAL V 166     -33.489  39.325 -67.176  1.00298.24           O  
ANISOU 5191  O   VAL V 166    35075  52739  25503  19711   -284   4431
ATOM   5192  CB  VAL V 166     -31.582  36.689 -67.767  1.00295.74           C  
ANISOU 5192  CB  VAL V 166    34802  52808  24756  19659    139   4496
ATOM   5193  CG1 VAL V 166     -33.021  36.377 -68.134  1.00296.26           C  
ANISOU 5193  CG1 VAL V 166    34876  52736  24954  19675     -8   4426
ATOM   5194  CG2 VAL V 166     -30.660  36.208 -68.876  1.00296.03           C  
ANISOU 5194  CG2 VAL V 166    34908  52960  24611  19662    191   4572
ATOM   5195  N   ARG V 167     -32.345  38.711 -65.340  1.00297.14           N  
ANISOU 5195  N   ARG V 167    34786  52897  25218  19684     49   4363
ATOM   5196  CA  ARG V 167     -33.382  39.242 -64.458  1.00297.66           C  
ANISOU 5196  CA  ARG V 167    34733  52909  25455  19722    -53   4228
ATOM   5197  C   ARG V 167     -33.528  40.755 -64.552  1.00299.29           C  
ANISOU 5197  C   ARG V 167    34948  52945  25821  19773   -251   4231
ATOM   5198  O   ARG V 167     -34.499  41.298 -64.014  1.00300.21           O  
ANISOU 5198  O   ARG V 167    34962  52987  26119  19830   -387   4090
ATOM   5199  CB  ARG V 167     -33.116  38.850 -63.004  1.00296.54           C  
ANISOU 5199  CB  ARG V 167    34439  52982  25251  19702    119   4149
ATOM   5200  CG  ARG V 167     -33.274  37.370 -62.721  1.00295.39           C  
ANISOU 5200  CG  ARG V 167    34257  52967  25009  19655    253   4138
ATOM   5201  CD  ARG V 167     -33.148  37.077 -61.237  1.00294.71           C  
ANISOU 5201  CD  ARG V 167    34003  53103  24871  19626    381   4083
ATOM   5202  NE  ARG V 167     -33.240  35.647 -60.967  1.00293.90           N  
ANISOU 5202  NE  ARG V 167    33871  53107  24690  19576    480   4111
ATOM   5203  CZ  ARG V 167     -32.185  34.848 -60.864  1.00292.99           C  
ANISOU 5203  CZ  ARG V 167    33792  53080  24452  19536    628   4204
ATOM   5204  NH1 ARG V 167     -30.965  35.348 -60.988  1.00292.67           N  
ANISOU 5204  NH1 ARG V 167    33805  53071  24327  19539    713   4267
ATOM   5205  NH2 ARG V 167     -32.347  33.555 -60.622  1.00292.61           N1+
ANISOU 5205  NH2 ARG V 167    33714  53088  24375  19498    674   4233
ATOM   5206  N   SER V 168     -32.597  41.446 -65.209  1.00297.22           N  
ANISOU 5206  N   SER V 168    34796  52630  25506  19759   -286   4383
ATOM   5207  CA  SER V 168     -32.737  42.876 -65.445  1.00299.16           C  
ANISOU 5207  CA  SER V 168    35075  52669  25924  19803   -523   4425
ATOM   5208  C   SER V 168     -33.567  43.190 -66.683  1.00300.87           C  
ANISOU 5208  C   SER V 168    35405  52647  26267  19811   -783   4497
ATOM   5209  O   SER V 168     -33.861  44.364 -66.929  1.00302.88           O  
ANISOU 5209  O   SER V 168    35692  52680  26710  19852  -1038   4538
ATOM   5210  CB  SER V 168     -31.357  43.527 -65.574  1.00299.35           C  
ANISOU 5210  CB  SER V 168    35163  52754  25824  19769   -470   4586
ATOM   5211  OG  SER V 168     -30.684  43.069 -66.734  1.00299.31           O  
ANISOU 5211  OG  SER V 168    35285  52804  25634  19701   -427   4757
ATOM   5212  N   LEU V 169     -33.950  42.173 -67.462  1.00299.44           N  
ANISOU 5212  N   LEU V 169    35279  52499  25994  19777   -744   4516
ATOM   5213  CA  LEU V 169     -34.734  42.372 -68.676  1.00301.07           C  
ANISOU 5213  CA  LEU V 169    35587  52514  26291  19776   -982   4591
ATOM   5214  C   LEU V 169     -35.926  41.424 -68.746  1.00300.58           C  
ANISOU 5214  C   LEU V 169    35473  52456  26278  19801   -982   4449
ATOM   5215  O   LEU V 169     -36.507  41.248 -69.822  1.00301.56           O  
ANISOU 5215  O   LEU V 169    35677  52484  26417  19791  -1125   4509
ATOM   5216  CB  LEU V 169     -33.856  42.206 -69.919  1.00301.46           C  
ANISOU 5216  CB  LEU V 169    35778  52627  26137  19695   -971   4806
ATOM   5217  CG  LEU V 169     -32.754  43.248 -70.119  1.00302.55           C  
ANISOU 5217  CG  LEU V 169    35987  52754  26214  19649  -1032   4994
ATOM   5218  CD1 LEU V 169     -31.873  42.879 -71.302  1.00302.90           C  
ANISOU 5218  CD1 LEU V 169    36133  52953  26002  19555   -986   5181
ATOM   5219  CD2 LEU V 169     -33.356  44.632 -70.304  1.00305.05           C  
ANISOU 5219  CD2 LEU V 169    36353  52770  26784  19676  -1375   5065
ATOM   5220  N   VAL V 170     -36.301  40.809 -67.627  1.00302.08           N  
ANISOU 5220  N   VAL V 170    28935  41066  44774  12552  15810  -1173
ATOM   5221  CA  VAL V 170     -37.431  39.889 -67.563  1.00302.23           C  
ANISOU 5221  CA  VAL V 170    29088  41043  44702  12475  15957  -1195
ATOM   5222  C   VAL V 170     -38.265  40.239 -66.339  1.00302.46           C  
ANISOU 5222  C   VAL V 170    29148  41065  44708  12506  15958  -1256
ATOM   5223  O   VAL V 170     -37.722  40.401 -65.240  1.00302.85           O  
ANISOU 5223  O   VAL V 170    29228  41108  44731  12632  15907  -1269
ATOM   5224  CB  VAL V 170     -36.975  38.418 -67.502  1.00302.77           C  
ANISOU 5224  CB  VAL V 170    29349  41053  44637  12522  16083  -1159
ATOM   5225  CG1 VAL V 170     -38.166  37.504 -67.270  1.00303.06           C  
ANISOU 5225  CG1 VAL V 170    29536  41041  44572  12443  16248  -1193
ATOM   5226  CG2 VAL V 170     -36.250  38.031 -68.782  1.00302.55           C  
ANISOU 5226  CG2 VAL V 170    29297  41029  44629  12482  16095  -1098
ATOM   5227  N   LYS V 171     -39.577  40.359 -66.532  1.00307.34           N  
ANISOU 5227  N   LYS V 171    29751  41695  45330  12391  16016  -1293
ATOM   5228  CA  LYS V 171     -40.471  40.638 -65.421  1.00307.57           C  
ANISOU 5228  CA  LYS V 171    29812  41721  45330  12411  16028  -1351
ATOM   5229  C   LYS V 171     -40.434  39.493 -64.410  1.00308.23           C  
ANISOU 5229  C   LYS V 171    30098  41743  45275  12487  16135  -1362
ATOM   5230  O   LYS V 171     -40.174  38.340 -64.771  1.00308.51           O  
ANISOU 5230  O   LYS V 171    30264  41735  45223  12475  16247  -1332
ATOM   5231  CB  LYS V 171     -41.903  40.837 -65.917  1.00307.33           C  
ANISOU 5231  CB  LYS V 171    29731  41730  45310  12269  16085  -1383
ATOM   5232  CG  LYS V 171     -42.138  42.109 -66.710  1.00306.78           C  
ANISOU 5232  CG  LYS V 171    29466  41726  45370  12209  15975  -1378
ATOM   5233  CD  LYS V 171     -43.606  42.235 -67.088  1.00306.69           C  
ANISOU 5233  CD  LYS V 171    29411  41773  45345  12083  16039  -1409
ATOM   5234  CE  LYS V 171     -43.878  43.500 -67.883  1.00306.23           C  
ANISOU 5234  CE  LYS V 171    29167  41782  45404  12035  15934  -1399
ATOM   5235  NZ  LYS V 171     -45.317  43.620 -68.249  1.00306.25           N1+
ANISOU 5235  NZ  LYS V 171    29117  41863  45379  11922  15994  -1425
ATOM   5236  N   PRO V 172     -40.691  39.780 -63.129  1.00313.22           N  
ANISOU 5236  N   PRO V 172    30765  42364  45880  12567  16110  -1405
ATOM   5237  CA  PRO V 172     -40.804  38.696 -62.142  1.00313.88           C  
ANISOU 5237  CA  PRO V 172    31048  42387  45825  12633  16221  -1420
ATOM   5238  C   PRO V 172     -42.019  37.809 -62.352  1.00314.06           C  
ANISOU 5238  C   PRO V 172    31184  42384  45760  12511  16388  -1447
ATOM   5239  O   PRO V 172     -42.121  36.764 -61.696  1.00314.66           O  
ANISOU 5239  O   PRO V 172    31447  42398  45711  12549  16507  -1455
ATOM   5240  CB  PRO V 172     -40.888  39.445 -60.806  1.00314.07           C  
ANISOU 5240  CB  PRO V 172    31048  42421  45864  12732  16136  -1465
ATOM   5241  CG  PRO V 172     -41.443  40.783 -61.163  1.00313.52           C  
ANISOU 5241  CG  PRO V 172    30793  42408  45922  12665  16035  -1490
ATOM   5242  CD  PRO V 172     -40.889  41.108 -62.522  1.00313.03           C  
ANISOU 5242  CD  PRO V 172    30611  42377  45947  12604  15985  -1442
ATOM   5243  N   GLU V 173     -42.937  38.189 -63.238  1.00312.32           N  
ANISOU 5243  N   GLU V 173    30859  42215  45593  12366  16406  -1462
ATOM   5244  CA  GLU V 173     -44.103  37.382 -63.567  1.00312.53           C  
ANISOU 5244  CA  GLU V 173    30971  42242  45535  12230  16571  -1491
ATOM   5245  C   GLU V 173     -43.859  36.470 -64.762  1.00312.54           C  
ANISOU 5245  C   GLU V 173    31029  42224  45499  12139  16679  -1450
ATOM   5246  O   GLU V 173     -44.797  35.817 -65.232  1.00312.73           O  
ANISOU 5246  O   GLU V 173    31108  42260  45456  12003  16823  -1473
ATOM   5247  CB  GLU V 173     -45.307  38.285 -63.847  1.00312.18           C  
ANISOU 5247  CB  GLU V 173    30774  42287  45554  12122  16537  -1531
ATOM   5248  CG  GLU V 173     -45.766  39.107 -62.654  1.00312.26           C  
ANISOU 5248  CG  GLU V 173    30746  42312  45586  12197  16458  -1577
ATOM   5249  CD  GLU V 173     -44.981  40.397 -62.499  1.00311.87           C  
ANISOU 5249  CD  GLU V 173    30552  42280  45663  12295  16272  -1560
ATOM   5250  OE1 GLU V 173     -44.123  40.680 -63.362  1.00311.51           O  
ANISOU 5250  OE1 GLU V 173    30425  42244  45691  12298  16202  -1514
ATOM   5251  OE2 GLU V 173     -45.221  41.127 -61.516  1.00311.95           O1-
ANISOU 5251  OE2 GLU V 173    30534  42296  45697  12366  16201  -1596
ATOM   5252  N   ASN V 174     -42.627  36.413 -65.262  1.00308.86           N  
ANISOU 5252  N   ASN V 174    30549  41735  45070  12208  16617  -1391
ATOM   5253  CA  ASN V 174     -42.270  35.617 -66.429  1.00308.85           C  
ANISOU 5253  CA  ASN V 174    30595  41713  45041  12134  16706  -1346
ATOM   5254  C   ASN V 174     -41.038  34.771 -66.133  1.00309.32           C  
ANISOU 5254  C   ASN V 174    30807  41693  45028  12267  16734  -1296
ATOM   5255  O   ASN V 174     -40.133  34.638 -66.962  1.00309.15           O  
ANISOU 5255  O   ASN V 174    30758  41669  45036  12283  16704  -1240
ATOM   5256  CB  ASN V 174     -42.047  36.514 -67.646  1.00308.12           C  
ANISOU 5256  CB  ASN V 174    30297  41693  45081  12065  16593  -1317
ATOM   5257  CG  ASN V 174     -42.002  35.739 -68.951  1.00308.06           C  
ANISOU 5257  CG  ASN V 174    30323  41680  45047  11949  16700  -1282
ATOM   5258  OD1 ASN V 174     -42.114  34.513 -68.966  1.00308.61           O  
ANISOU 5258  OD1 ASN V 174    30576  41684  44998  11918  16867  -1280
ATOM   5259  ND2 ASN V 174     -41.842  36.456 -70.058  1.00307.44           N  
ANISOU 5259  ND2 ASN V 174    30072  41665  45078  11883  16611  -1256
ATOM   5260  N   TYR V 175     -40.982  34.196 -64.934  1.00309.87           N  
ANISOU 5260  N   TYR V 175    17661  41194  58880  -3980    967   1451
ATOM   5261  CA  TYR V 175     -39.894  33.310 -64.544  1.00309.97           C  
ANISOU 5261  CA  TYR V 175    17744  41315  58716  -4103    496   1456
ATOM   5262  C   TYR V 175     -40.203  31.842 -64.805  1.00309.43           C  
ANISOU 5262  C   TYR V 175    18010  41079  58478  -4366   -418   2612
ATOM   5263  O   TYR V 175     -39.365  30.986 -64.505  1.00309.59           O  
ANISOU 5263  O   TYR V 175    18122  41178  58331  -4478   -886   2733
ATOM   5264  CB  TYR V 175     -39.555  33.505 -63.062  1.00314.49           C  
ANISOU 5264  CB  TYR V 175    17567  43176  58749  -4185    630   1026
ATOM   5265  CG  TYR V 175     -38.856  34.810 -62.748  1.00315.07           C  
ANISOU 5265  CG  TYR V 175    17363  43351  58998  -3934   1438   -236
ATOM   5266  CD1 TYR V 175     -38.279  35.573 -63.754  1.00311.41           C  
ANISOU 5266  CD1 TYR V 175    17350  41803  59168  -3673   1941   -944
ATOM   5267  CD2 TYR V 175     -38.769  35.275 -61.442  1.00319.52           C  
ANISOU 5267  CD2 TYR V 175    17232  45082  59089  -3958   1696   -718
ATOM   5268  CE1 TYR V 175     -37.637  36.765 -63.469  1.00312.15           C  
ANISOU 5268  CE1 TYR V 175    17186  41968  59450  -3461   2677  -2095
ATOM   5269  CE2 TYR V 175     -38.129  36.464 -61.146  1.00320.30           C  
ANISOU 5269  CE2 TYR V 175    17085  45260  59355  -3739   2405  -1881
ATOM   5270  CZ  TYR V 175     -37.565  37.205 -62.163  1.00316.60           C  
ANISOU 5270  CZ  TYR V 175    17050  43696  59548  -3501   2892  -2564
ATOM   5271  OH  TYR V 175     -36.928  38.390 -61.874  1.00317.58           O  
ANISOU 5271  OH  TYR V 175    16925  43876  59865  -3300   3597  -3719
ATOM   5272  N   ARG V 176     -41.378  31.531 -65.351  1.00308.98           N  
ANISOU 5272  N   ARG V 176    18136  40788  58474  -4467   -696   3456
ATOM   5273  CA  ARG V 176     -41.753  30.151 -65.627  1.00308.70           C  
ANISOU 5273  CA  ARG V 176    18427  40564  58301  -4734  -1580   4583
ATOM   5274  C   ARG V 176     -42.190  29.998 -67.079  1.00304.83           C  
ANISOU 5274  C   ARG V 176    18698  38812  58313  -4641  -1766   5001
ATOM   5275  O   ARG V 176     -42.036  28.926 -67.673  1.00303.09           O  
ANISOU 5275  O   ARG V 176    19028  37971  58162  -4760  -2443   5668
ATOM   5276  CB  ARG V 176     -42.873  29.702 -64.683  1.00313.13           C  
ANISOU 5276  CB  ARG V 176    18383  42255  58337  -5027  -1893   5391
ATOM   5277  CG  ARG V 176     -43.254  28.235 -64.813  1.00313.55           C  
ANISOU 5277  CG  ARG V 176    18697  42233  58204  -5344  -2827   6573
ATOM   5278  CD  ARG V 176     -44.383  27.864 -63.862  1.00318.30           C  
ANISOU 5278  CD  ARG V 176    18660  43963  58316  -5633  -3060   7353
ATOM   5279  NE  ARG V 176     -43.983  27.927 -62.459  1.00322.31           N  
ANISOU 5279  NE  ARG V 176    18515  45685  58265  -5702  -2902   7029
ATOM   5280  CZ  ARG V 176     -44.829  27.816 -61.440  1.00327.06           C  
ANISOU 5280  CZ  ARG V 176    18471  47416  58380  -5897  -2920   7497
ATOM   5281  NH1 ARG V 176     -46.123  27.638 -61.668  1.00328.39           N  
ANISOU 5281  NH1 ARG V 176    18522  47661  58590  -6054  -3085   8314
ATOM   5282  NH2 ARG V 176     -44.385  27.885 -60.193  1.00330.71           N1+
ANISOU 5282  NH2 ARG V 176    18409  48928  58318  -5926  -2774   7152
ATOM   5283  N   ARG V 177     -42.730  31.072 -67.659  1.00303.63           N  
ANISOU 5283  N   ARG V 177    18604  38258  58502  -4414  -1173   4605
ATOM   5284  CA  ARG V 177     -43.271  31.014 -69.011  1.00300.42           C  
ANISOU 5284  CA  ARG V 177    18901  36700  58545  -4306  -1330   5004
ATOM   5285  C   ARG V 177     -42.197  31.076 -70.090  1.00296.05           C  
ANISOU 5285  C   ARG V 177    19149  34878  58460  -4048  -1209   4505
ATOM   5286  O   ARG V 177     -42.450  30.632 -71.216  1.00293.38           O  
ANISOU 5286  O   ARG V 177    19534  33518  58419  -3997  -1568   4992
ATOM   5287  CB  ARG V 177     -44.271  32.153 -69.227  1.00301.01           C  
ANISOU 5287  CB  ARG V 177    18746  36821  58803  -4138   -740   4773
ATOM   5288  CG  ARG V 177     -45.539  32.040 -68.399  1.00305.22           C  
ANISOU 5288  CG  ARG V 177    18582  38432  58955  -4377   -897   5430
ATOM   5289  CD  ARG V 177     -46.465  33.216 -68.663  1.00305.74           C  
ANISOU 5289  CD  ARG V 177    18443  38484  59242  -4169   -278   5143
ATOM   5290  NE  ARG V 177     -47.682  33.151 -67.860  1.00310.07           N  
ANISOU 5290  NE  ARG V 177    18288  40077  59448  -4377   -373   5755
ATOM   5291  CZ  ARG V 177     -48.625  34.088 -67.858  1.00311.60           C  
ANISOU 5291  CZ  ARG V 177    18144  40508  59741  -4237    122   5619
ATOM   5292  NH1 ARG V 177     -48.492  35.166 -68.619  1.00309.07           N  
ANISOU 5292  NH1 ARG V 177    18144  39447  59842  -3889    737   4888
ATOM   5293  NH2 ARG V 177     -49.701  33.948 -67.096  1.00315.83           N1+
ANISOU 5293  NH2 ARG V 177    18023  42017  59962  -4435     19   6222
ATOM   5294  N   LEU V 178     -41.015  31.618 -69.781  1.00295.97           N  
ANISOU 5294  N   LEU V 178    19031  34893  58529  -3880   -712   3549
ATOM   5295  CA  LEU V 178     -39.964  31.715 -70.789  1.00292.12           C  
ANISOU 5295  CA  LEU V 178    19273  33205  58513  -3625   -530   3051
ATOM   5296  C   LEU V 178     -39.501  30.344 -71.260  1.00290.53           C  
ANISOU 5296  C   LEU V 178    19663  32434  58292  -3754  -1337   3748
ATOM   5297  O   LEU V 178     -39.034  30.207 -72.397  1.00289.29           O  
ANISOU 5297  O   LEU V 178    20298  31083  58537  -3555  -1360   3698
ATOM   5298  CB  LEU V 178     -38.775  32.507 -70.246  1.00292.47           C  
ANISOU 5298  CB  LEU V 178    18991  33491  58645  -3459    123   1917
ATOM   5299  CG  LEU V 178     -38.974  34.002 -70.006  1.00293.36           C  
ANISOU 5299  CG  LEU V 178    18688  33871  58905  -3252   1033   1024
ATOM   5300  CD1 LEU V 178     -37.738  34.591 -69.351  1.00294.28           C  
ANISOU 5300  CD1 LEU V 178    18445  34303  59065  -3151   1534    -19
ATOM   5301  CD2 LEU V 178     -39.280  34.713 -71.313  1.00290.14           C  
ANISOU 5301  CD2 LEU V 178    18922  32289  59028  -2963   1454    832
ATOM   5302  N   ASP V 179     -39.618  29.325 -70.406  1.00292.61           N  
ANISOU 5302  N   ASP V 179    19578  33519  58083  -4070  -1988   4398
ATOM   5303  CA  ASP V 179     -39.216  27.960 -70.743  1.00291.58           C  
ANISOU 5303  CA  ASP V 179    19965  32942  57878  -4216  -2801   5109
ATOM   5304  C   ASP V 179     -37.747  27.903 -71.159  1.00289.14           C  
ANISOU 5304  C   ASP V 179    20094  31908  57858  -3998  -2633   4465
ATOM   5305  O   ASP V 179     -37.385  27.251 -72.140  1.00286.44           O  
ANISOU 5305  O   ASP V 179    20537  30530  57766  -3910  -2988   4783
ATOM   5306  CB  ASP V 179     -40.117  27.374 -71.834  1.00289.78           C  
ANISOU 5306  CB  ASP V 179    20414  31856  57834  -4259  -3324   5996
ATOM   5307  CG  ASP V 179     -41.532  27.127 -71.349  1.00292.74           C  
ANISOU 5307  CG  ASP V 179    20329  32997  57900  -4545  -3674   6812
ATOM   5308  OD1 ASP V 179     -41.710  26.863 -70.141  1.00296.27           O  
ANISOU 5308  OD1 ASP V 179    20058  34625  57885  -4791  -3812   7000
ATOM   5309  OD2 ASP V 179     -42.466  27.197 -72.175  1.00291.74           O1-
ANISOU 5309  OD2 ASP V 179    20560  32290  57999  -4516  -3809   7270
ATOM   5310  N   ILE V 180     -36.895  28.601 -70.408  1.00290.34           N  
ANISOU 5310  N   ILE V 180    19733  32599  57985  -3901  -2084   3547
ATOM   5311  CA  ILE V 180     -35.470  28.665 -70.712  1.00288.54           C  
ANISOU 5311  CA  ILE V 180    19801  31762  58069  -3691  -1844   2845
ATOM   5312  C   ILE V 180     -34.852  27.290 -70.500  1.00288.94           C  
ANISOU 5312  C   ILE V 180    20053  31850  57882  -3860  -2632   3418
ATOM   5313  O   ILE V 180     -34.400  26.645 -71.452  1.00286.29           O  
ANISOU 5313  O   ILE V 180    20475  30493  57811  -3755  -2939   3696
ATOM   5314  CB  ILE V 180     -34.770  29.724 -69.840  1.00290.40           C  
ANISOU 5314  CB  ILE V 180    19350  32678  58312  -3587  -1125   1750
ATOM   5315  CG1 ILE V 180     -35.350  31.113 -70.113  1.00289.94           C  
ANISOU 5315  CG1 ILE V 180    19148  32499  58516  -3396   -318   1155
ATOM   5316  CG2 ILE V 180     -33.272  29.716 -70.084  1.00289.04           C  
ANISOU 5316  CG2 ILE V 180    19414  31932  58476  -3400   -927   1061
ATOM   5317  CD1 ILE V 180     -34.920  32.158 -69.104  1.00292.54           C  
ANISOU 5317  CD1 ILE V 180    18717  33677  58759  -3344    335    174
ATOM   5318  N   VAL V 181     -34.851  26.828 -69.251  1.00292.44           N  
ANISOU 5318  N   VAL V 181    19842  33466  57807  -4110  -2967   3614
ATOM   5319  CA  VAL V 181     -34.420  25.483 -68.881  1.00293.52           C  
ANISOU 5319  CA  VAL V 181    20082  33819  57623  -4308  -3768   4250
ATOM   5320  C   VAL V 181     -35.331  25.008 -67.759  1.00297.42           C  
ANISOU 5320  C   VAL V 181    19953  35554  57497  -4645  -4197   4918
ATOM   5321  O   VAL V 181     -35.600  25.757 -66.814  1.00300.17           O  
ANISOU 5321  O   VAL V 181    19580  36876  57596  -4685  -3782   4489
ATOM   5322  CB  VAL V 181     -32.943  25.429 -68.434  1.00294.03           C  
ANISOU 5322  CB  VAL V 181    19993  33981  57745  -4192  -3652   3535
ATOM   5323  CG1 VAL V 181     -32.602  24.052 -67.880  1.00295.81           C  
ANISOU 5323  CG1 VAL V 181    20228  34609  57557  -4411  -4497   4222
ATOM   5324  CG2 VAL V 181     -32.011  25.766 -69.582  1.00290.39           C  
ANISOU 5324  CG2 VAL V 181    20182  32239  57913  -3866  -3263   2967
ATOM   5325  N   ARG V 182     -35.809  23.768 -67.860  1.00297.86           N  
ANISOU 5325  N   ARG V 182    20300  35568  57305  -4885  -5017   5971
ATOM   5326  CA  ARG V 182     -36.785  23.288 -66.892  1.00301.64           C  
ANISOU 5326  CA  ARG V 182    20234  37146  57230  -5217  -5420   6704
ATOM   5327  C   ARG V 182     -36.160  22.982 -65.537  1.00305.32           C  
ANISOU 5327  C   ARG V 182    20080  38734  57195  -5342  -5559   6509
ATOM   5328  O   ARG V 182     -36.884  22.903 -64.539  1.00309.05           O  
ANISOU 5328  O   ARG V 182    19954  40291  57182  -5565  -5663   6863
ATOM   5329  CB  ARG V 182     -37.503  22.057 -67.433  1.00301.22           C  
ANISOU 5329  CB  ARG V 182    20688  36670  57093  -5451  -6261   7901
ATOM   5330  CG  ARG V 182     -38.482  22.371 -68.547  1.00298.84           C  
ANISOU 5330  CG  ARG V 182    20843  35540  57163  -5393  -6193   8242
ATOM   5331  CD  ARG V 182     -37.818  22.298 -69.899  1.00294.48           C  
ANISOU 5331  CD  ARG V 182    21200  33559  57129  -5121  -6183   8037
ATOM   5332  NE  ARG V 182     -38.783  22.393 -70.988  1.00292.49           N  
ANISOU 5332  NE  ARG V 182    21475  32476  57180  -5084  -6280   8504
ATOM   5333  CZ  ARG V 182     -39.094  23.527 -71.605  1.00290.68           C  
ANISOU 5333  CZ  ARG V 182    21334  31790  57320  -4839  -5619   7959
ATOM   5334  NH1 ARG V 182     -38.510  24.658 -71.238  1.00290.57           N  
ANISOU 5334  NH1 ARG V 182    20917  32061  57426  -4622  -4803   6927
ATOM   5335  NH2 ARG V 182     -39.984  23.530 -72.588  1.00289.14           N1+
ANISOU 5335  NH2 ARG V 182    21643  30841  57377  -4808  -5788   8439
ATOM   5336  N   SER V 183     -34.842  22.805 -65.477  1.00304.60           N  
ANISOU 5336  N   SER V 183    20119  38408  57208  -5195  -5563   5964
ATOM   5337  CA  SER V 183     -34.128  22.691 -64.214  1.00308.12           C  
ANISOU 5337  CA  SER V 183    19969  39873  57228  -5255  -5614   5597
ATOM   5338  C   SER V 183     -33.502  24.014 -63.791  1.00308.68           C  
ANISOU 5338  C   SER V 183    19563  40255  57466  -5025  -4787   4371
ATOM   5339  O   SER V 183     -32.623  24.030 -62.922  1.00311.06           O  
ANISOU 5339  O   SER V 183    19467  41169  57551  -4998  -4771   3852
ATOM   5340  CB  SER V 183     -33.059  21.601 -64.306  1.00307.62           C  
ANISOU 5340  CB  SER V 183    20289  39445  57148  -5250  -6205   5794
ATOM   5341  OG  SER V 183     -32.045  21.957 -65.228  1.00304.13           O  
ANISOU 5341  OG  SER V 183    20319  37945  57291  -4951  -5873   5121
ATOM   5342  N   LEU V 184     -33.939  25.123 -64.388  1.00306.73           N  
ANISOU 5342  N   LEU V 184    19355  39586  57603  -4857  -4116   3897
ATOM   5343  CA  LEU V 184     -33.358  26.428 -64.098  1.00307.10           C  
ANISOU 5343  CA  LEU V 184    19007  39806  57870  -4631  -3303   2716
ATOM   5344  C   LEU V 184     -34.423  27.459 -63.746  1.00308.62           C  
ANISOU 5344  C   LEU V 184    18735  40583  57945  -4639  -2756   2532
ATOM   5345  O   LEU V 184     -34.148  28.396 -62.990  1.00310.84           O  
ANISOU 5345  O   LEU V 184    18461  41513  58133  -4547  -2213   1702
ATOM   5346  CB  LEU V 184     -32.523  26.914 -65.284  1.00302.94           C  
ANISOU 5346  CB  LEU V 184    19053  38000  58051  -4336  -2884   2084
ATOM   5347  CG  LEU V 184     -31.815  28.262 -65.146  1.00303.01           C  
ANISOU 5347  CG  LEU V 184    18737  37992  58401  -4093  -2024    831
ATOM   5348  CD1 LEU V 184     -30.823  28.234 -63.997  1.00306.39           C  
ANISOU 5348  CD1 LEU V 184    18597  39259  58558  -4120  -2073    248
ATOM   5349  CD2 LEU V 184     -31.120  28.624 -66.447  1.00298.84           C  
ANISOU 5349  CD2 LEU V 184    18864  36096  58585  -3818  -1644    380
ATOM   5350  N   TYR V 185     -35.640  27.310 -64.281  1.00300.69           N  
ANISOU 5350  N   TYR V 185    40475  52596  21177  25126  -2806  -3642
ATOM   5351  CA  TYR V 185     -36.682  28.268 -63.928  1.00299.97           C  
ANISOU 5351  CA  TYR V 185    40298  52570  21106  25054  -2760  -3576
ATOM   5352  C   TYR V 185     -37.102  28.120 -62.473  1.00294.45           C  
ANISOU 5352  C   TYR V 185    39332  51587  20959  24420  -2939  -3916
ATOM   5353  O   TYR V 185     -37.729  29.031 -61.923  1.00292.97           O  
ANISOU 5353  O   TYR V 185    39012  51334  20968  24235  -2800  -3811
ATOM   5354  CB  TYR V 185     -37.902  28.135 -64.848  1.00304.20           C  
ANISOU 5354  CB  TYR V 185    40831  53379  21369  25360  -3058  -3841
ATOM   5355  CG  TYR V 185     -38.789  26.931 -64.607  1.00303.48           C  
ANISOU 5355  CG  TYR V 185    40498  53271  21540  25115  -3665  -4591
ATOM   5356  CD1 TYR V 185     -38.559  25.729 -65.256  1.00306.02           C  
ANISOU 5356  CD1 TYR V 185    40807  53626  21842  25291  -3987  -4950
ATOM   5357  CD2 TYR V 185     -39.882  27.012 -63.751  1.00300.94           C  
ANISOU 5357  CD2 TYR V 185    39942  52919  21482  24781  -3906  -4944
ATOM   5358  CE1 TYR V 185     -39.379  24.634 -65.045  1.00306.24           C  
ANISOU 5358  CE1 TYR V 185    40586  53642  22128  25174  -4523  -5659
ATOM   5359  CE2 TYR V 185     -40.705  25.924 -63.533  1.00301.20           C  
ANISOU 5359  CE2 TYR V 185    39735  52959  21750  24657  -4425  -5617
ATOM   5360  CZ  TYR V 185     -40.448  24.737 -64.183  1.00303.99           C  
ANISOU 5360  CZ  TYR V 185    40071  53333  22098  24873  -4729  -5984
ATOM   5361  OH  TYR V 185     -41.263  23.649 -63.972  1.00305.05           O  
ANISOU 5361  OH  TYR V 185    39961  53490  22453  24827  -5231  -6714
ATOM   5362  N   GLU V 186     -36.772  26.990 -61.844  1.00310.01           N  
ANISOU 5362  N   GLU V 186    41237  53379  23175  24131  -3232  -4292
ATOM   5363  CA  GLU V 186     -36.890  26.864 -60.399  1.00304.59           C  
ANISOU 5363  CA  GLU V 186    40357  52367  23004  23585  -3284  -4495
ATOM   5364  C   GLU V 186     -35.809  27.646 -59.666  1.00301.11           C  
ANISOU 5364  C   GLU V 186    39810  51553  23045  23261  -2813  -4170
ATOM   5365  O   GLU V 186     -35.928  27.848 -58.453  1.00297.01           O  
ANISOU 5365  O   GLU V 186    39115  50798  22936  22867  -2827  -4270
ATOM   5366  CB  GLU V 186     -36.834  25.390 -59.994  1.00303.85           C  
ANISOU 5366  CB  GLU V 186    40280  52160  23008  23463  -3682  -4947
ATOM   5367  CG  GLU V 186     -38.005  24.563 -60.502  1.00305.96           C  
ANISOU 5367  CG  GLU V 186    40492  52678  23082  23699  -4176  -5407
ATOM   5368  CD  GLU V 186     -39.323  24.969 -59.872  1.00303.96           C  
ANISOU 5368  CD  GLU V 186    40032  52487  22971  23525  -4294  -5607
ATOM   5369  OE1 GLU V 186     -39.316  25.392 -58.697  1.00300.37           O  
ANISOU 5369  OE1 GLU V 186    39492  51781  22854  23135  -4091  -5497
ATOM   5370  OE2 GLU V 186     -40.366  24.867 -60.552  1.00306.48           O1-
ANISOU 5370  OE2 GLU V 186    40227  53047  23173  23731  -4547  -5914
ATOM   5371  N   ASP V 187     -34.764  28.084 -60.370  1.00299.81           N  
ANISOU 5371  N   ASP V 187    39710  51323  22881  23444  -2399  -3815
ATOM   5372  CA  ASP V 187     -33.740  28.954 -59.809  1.00298.88           C  
ANISOU 5372  CA  ASP V 187    39385  50821  23354  23172  -1911  -3557
ATOM   5373  C   ASP V 187     -33.933  30.416 -60.190  1.00301.13           C  
ANISOU 5373  C   ASP V 187    39574  51044  23798  23303  -1416  -3095
ATOM   5374  O   ASP V 187     -33.283  31.284 -59.599  1.00300.60           O  
ANISOU 5374  O   ASP V 187    39231  50601  24384  23036  -1023  -2943
ATOM   5375  CB  ASP V 187     -32.346  28.494 -60.253  1.00300.60           C  
ANISOU 5375  CB  ASP V 187    39652  50907  23654  23250  -1681  -3498
ATOM   5376  CG  ASP V 187     -31.937  27.179 -59.620  1.00298.16           C  
ANISOU 5376  CG  ASP V 187    39400  50532  23356  23053  -2107  -3934
ATOM   5377  OD1 ASP V 187     -32.391  26.894 -58.492  1.00294.83           O  
ANISOU 5377  OD1 ASP V 187    38899  49999  23122  22748  -2403  -4207
ATOM   5378  OD2 ASP V 187     -31.159  26.431 -60.250  1.00300.00           O1-
ANISOU 5378  OD2 ASP V 187    39773  50814  23397  23238  -2122  -3977
ATOM   5379  N   LEU V 188     -34.803  30.707 -61.160  1.00297.04           N  
ANISOU 5379  N   LEU V 188    39263  50870  22728  23739  -1435  -2899
ATOM   5380  CA  LEU V 188     -35.125  32.088 -61.499  1.00299.59           C  
ANISOU 5380  CA  LEU V 188    39551  51130  23151  23920   -975  -2432
ATOM   5381  C   LEU V 188     -35.895  32.800 -60.396  1.00296.21           C  
ANISOU 5381  C   LEU V 188    38853  50544  23148  23530  -1086  -2550
ATOM   5382  O   LEU V 188     -36.029  34.027 -60.453  1.00297.93           O  
ANISOU 5382  O   LEU V 188    38969  50586  23643  23587   -673  -2179
ATOM   5383  CB  LEU V 188     -35.931  32.139 -62.800  1.00304.27           C  
ANISOU 5383  CB  LEU V 188    40488  52200  22922  24568  -1055  -2242
ATOM   5384  CG  LEU V 188     -35.203  31.770 -64.093  1.00309.32           C  
ANISOU 5384  CG  LEU V 188    41432  53027  23070  25114   -824  -1960
ATOM   5385  CD1 LEU V 188     -36.179  31.705 -65.256  1.00314.09           C  
ANISOU 5385  CD1 LEU V 188    42374  54196  22769  25802  -1100  -1913
ATOM   5386  CD2 LEU V 188     -34.106  32.778 -64.380  1.00312.53           C  
ANISOU 5386  CD2 LEU V 188    41786  53021  23941  25189     55  -1343
ATOM   5387  N   GLU V 189     -36.398  32.070 -59.401  1.00309.57           N  
ANISOU 5387  N   GLU V 189    40435  52274  24912  23168  -1595  -3030
ATOM   5388  CA  GLU V 189     -37.199  32.638 -58.324  1.00306.55           C  
ANISOU 5388  CA  GLU V 189    39815  51797  24864  22823  -1742  -3170
ATOM   5389  C   GLU V 189     -36.528  32.450 -56.966  1.00302.82           C  
ANISOU 5389  C   GLU V 189    39094  50980  24983  22331  -1804  -3411
ATOM   5390  O   GLU V 189     -37.203  32.401 -55.936  1.00299.95           O  
ANISOU 5390  O   GLU V 189    38599  50612  24757  22054  -2081  -3658
ATOM   5391  CB  GLU V 189     -38.598  32.022 -58.319  1.00305.88           C  
ANISOU 5391  CB  GLU V 189    39813  52094  24315  22900  -2257  -3525
ATOM   5392  CG  GLU V 189     -39.428  32.354 -59.551  1.00310.06           C  
ANISOU 5392  CG  GLU V 189    40545  53016  24247  23413  -2281  -3392
ATOM   5393  CD  GLU V 189     -40.794  31.694 -59.533  1.00310.07           C  
ANISOU 5393  CD  GLU V 189    40530  53380  23902  23467  -2816  -3897
ATOM   5394  OE1 GLU V 189     -41.050  30.879 -58.622  1.00307.05           O  
ANISOU 5394  OE1 GLU V 189    39999  52909  23758  23124  -3112  -4291
ATOM   5395  OE2 GLU V 189     -41.611  31.989 -60.431  1.00313.72           O1-
ANISOU 5395  OE2 GLU V 189    41119  54205  23877  23883  -2914  -3921
ATOM   5396  N   ASP V 190     -35.195  32.349 -56.948  1.00310.67           N  
ANISOU 5396  N   ASP V 190    40020  51703  26318  22255  -1545  -3360
ATOM   5397  CA  ASP V 190     -34.461  32.081 -55.717  1.00308.33           C  
ANISOU 5397  CA  ASP V 190    39514  51129  26508  21869  -1664  -3659
ATOM   5398  C   ASP V 190     -33.226  32.959 -55.539  1.00309.16           C  
ANISOU 5398  C   ASP V 190    39291  50821  27356  21725  -1206  -3553
ATOM   5399  O   ASP V 190     -32.455  32.728 -54.600  1.00307.40           O  
ANISOU 5399  O   ASP V 190    38872  50386  27538  21460  -1325  -3866
ATOM   5400  CB  ASP V 190     -34.036  30.608 -55.651  1.00308.48           C  
ANISOU 5400  CB  ASP V 190    39759  51246  26202  21893  -1993  -3951
ATOM   5401  CG  ASP V 190     -35.200  29.668 -55.415  1.00308.01           C  
ANISOU 5401  CG  ASP V 190    39899  51452  25677  21930  -2452  -4196
ATOM   5402  OD1 ASP V 190     -36.190  30.089 -54.779  1.00306.15           O  
ANISOU 5402  OD1 ASP V 190    39556  51269  25499  21797  -2571  -4249
ATOM   5403  OD2 ASP V 190     -35.122  28.503 -55.856  1.00309.83           O1-
ANISOU 5403  OD2 ASP V 190    40362  51810  25551  22093  -2676  -4360
ATOM   5404  N   HIS V 191     -33.008  33.955 -56.403  1.00299.18           N  
ANISOU 5404  N   HIS V 191    37945  49417  26315  21925   -667  -3144
ATOM   5405  CA  HIS V 191     -31.775  34.743 -56.405  1.00301.32           C  
ANISOU 5405  CA  HIS V 191    37853  49229  27407  21827   -115  -3054
ATOM   5406  C   HIS V 191     -32.095  36.226 -56.241  1.00301.85           C  
ANISOU 5406  C   HIS V 191    37610  48994  28088  21769    282  -2816
ATOM   5407  O   HIS V 191     -32.189  36.965 -57.233  1.00305.88           O  
ANISOU 5407  O   HIS V 191    38204  49425  28592  22089    818  -2320
ATOM   5408  CB  HIS V 191     -30.975  34.497 -57.683  1.00306.26           C  
ANISOU 5408  CB  HIS V 191    38657  49856  27852  22172    339  -2740
ATOM   5409  CG  HIS V 191     -30.450  33.100 -57.808  1.00306.30           C  
ANISOU 5409  CG  HIS V 191    38896  50079  27407  22206    -17  -3016
ATOM   5410  ND1 HIS V 191     -31.182  32.078 -58.373  1.00306.24           N  
ANISOU 5410  ND1 HIS V 191    39327  50522  26511  22462   -438  -3036
ATOM   5411  CD2 HIS V 191     -29.266  32.556 -57.440  1.00306.35           C  
ANISOU 5411  CD2 HIS V 191    38734  49897  27768  22033    -29  -3325
ATOM   5412  CE1 HIS V 191     -30.473  30.964 -58.348  1.00306.25           C  
ANISOU 5412  CE1 HIS V 191    39438  50576  26348  22440   -675  -3309
ATOM   5413  NE2 HIS V 191     -29.306  31.227 -57.787  1.00306.26           N  
ANISOU 5413  NE2 HIS V 191    39099  50213  27054  22189   -439  -3471
ATOM   5414  N   PRO V 192     -32.271  36.698 -55.001  1.00301.73           N  
ANISOU 5414  N   PRO V 192    37253  48798  28594  21408     43  -3147
ATOM   5415  CA  PRO V 192     -32.382  38.146 -54.772  1.00303.62           C  
ANISOU 5415  CA  PRO V 192    37107  48653  29602  21322    440  -2998
ATOM   5416  C   PRO V 192     -31.029  38.839 -54.839  1.00307.98           C  
ANISOU 5416  C   PRO V 192    37177  48633  31210  21232   1053  -3040
ATOM   5417  O   PRO V 192     -30.016  38.208 -55.160  1.00309.32           O  
ANISOU 5417  O   PRO V 192    37336  48742  31451  21259   1193  -3146
ATOM   5418  CB  PRO V 192     -32.981  38.236 -53.361  1.00299.71           C  
ANISOU 5418  CB  PRO V 192    36419  48214  29244  20977   -111  -3433
ATOM   5419  CG  PRO V 192     -33.599  36.894 -53.114  1.00295.73           C  
ANISOU 5419  CG  PRO V 192    36332  48196  27835  20992   -715  -3620
ATOM   5420  CD  PRO V 192     -32.703  35.927 -53.824  1.00297.23           C  
ANISOU 5420  CD  PRO V 192    36730  48443  27761  21148   -628  -3606
ATOM   5421  N   ASN V 193     -30.999  40.133 -54.537  1.00298.40           N  
ANISOU 5421  N   ASN V 193    35522  46970  30887  21124   1437  -3000
ATOM   5422  CA  ASN V 193     -29.747  40.883 -54.505  1.00303.39           C  
ANISOU 5422  CA  ASN V 193    35564  46966  32746  21003   2062  -3143
ATOM   5423  C   ASN V 193     -29.032  40.665 -53.175  1.00301.72           C  
ANISOU 5423  C   ASN V 193    34872  46599  33169  20593   1604  -3925
ATOM   5424  O   ASN V 193     -28.137  39.828 -53.070  1.00301.52           O  
ANISOU 5424  O   ASN V 193    34819  46623  33120  20527   1457  -4243
ATOM   5425  CB  ASN V 193     -30.004  42.376 -54.733  1.00307.88           C  
ANISOU 5425  CB  ASN V 193    35820  47044  34117  21081   2702  -2812
ATOM   5426  CG  ASN V 193     -28.723  43.166 -54.948  1.00314.61           C  
ANISOU 5426  CG  ASN V 193    36050  47161  36325  21025   3541  -2886
ATOM   5427  OD1 ASN V 193     -27.623  42.613 -54.921  1.00315.86           O  
ANISOU 5427  OD1 ASN V 193    35982  47200  36833  20914   3623  -3221
ATOM   5428  ND2 ASN V 193     -28.863  44.469 -55.164  1.00319.47           N  
ANISOU 5428  ND2 ASN V 193    36364  47252  37768  21108   4196  -2595
TER    5429      ASN V 193
ATOM   5430  N   MET C  17      -1.532  18.988 -72.724  1.00242.13           N  
ANISOU 5430  N   MET C  17    26907  43356  21734  -7026   -747   2086
ATOM   5431  CA  MET C  17      -0.852  20.259 -72.943  1.00247.56           C  
ANISOU 5431  CA  MET C  17    27685  43807  22570  -7540   -584   2430
ATOM   5432  C   MET C  17      -1.703  21.185 -73.807  1.00250.95           C  
ANISOU 5432  C   MET C  17    28529  44006  22813  -7661   -604   3133
ATOM   5433  O   MET C  17      -1.678  22.404 -73.640  1.00254.23           O  
ANISOU 5433  O   MET C  17    29220  43905  23470  -7908   -627   3496
ATOM   5434  CB  MET C  17       0.515  20.028 -73.592  1.00251.44           C  
ANISOU 5434  CB  MET C  17    27777  44903  22857  -7997   -256   2241
ATOM   5435  CG  MET C  17       1.371  21.278 -73.708  1.00257.31           C  
ANISOU 5435  CG  MET C  17    28550  45421  23795  -8590    -68   2530
ATOM   5436  SD  MET C  17       1.871  21.940 -72.107  1.00256.05           S  
ANISOU 5436  SD  MET C  17    28397  44568  24324  -8588   -246   2219
ATOM   5437  CE  MET C  17       2.181  23.652 -72.532  1.00263.31           C  
ANISOU 5437  CE  MET C  17    29628  45025  25395  -9227   -128   2866
ATOM   5438  N   TYR C  18      -2.461  20.594 -74.729  1.00246.77           N  
ANISOU 5438  N   TYR C  18    28062  43849  21850  -7475   -620   3315
ATOM   5439  CA  TYR C  18      -3.345  21.348 -75.609  1.00249.64           C  
ANISOU 5439  CA  TYR C  18    28808  43947  22098  -7478   -679   3917
ATOM   5440  C   TYR C  18      -4.563  20.499 -75.938  1.00245.31           C  
ANISOU 5440  C   TYR C  18    28283  43254  21668  -6861   -872   3793
ATOM   5441  O   TYR C  18      -4.423  19.329 -76.307  1.00241.90           O  
ANISOU 5441  O   TYR C  18    27542  43096  21272  -6632   -809   3387
ATOM   5442  CB  TYR C  18      -2.630  21.766 -76.898  1.00254.24           C  
ANISOU 5442  CB  TYR C  18    29356  44802  22441  -7944   -399   4207
ATOM   5443  CG  TYR C  18      -1.548  22.804 -76.710  1.00259.42           C  
ANISOU 5443  CG  TYR C  18    30032  45452  23085  -8616   -166   4444
ATOM   5444  CD1 TYR C  18      -1.866  24.151 -76.596  1.00264.10           C  
ANISOU 5444  CD1 TYR C  18    31058  45386  23902  -8803   -264   4945
ATOM   5445  CD2 TYR C  18      -0.210  22.440 -76.656  1.00259.69           C  
ANISOU 5445  CD2 TYR C  18    29619  45918  23133  -8954    104   4057
ATOM   5446  CE1 TYR C  18      -0.881  25.106 -76.428  1.00269.10           C  
ANISOU 5446  CE1 TYR C  18    31697  45773  24777  -9346   -102   5071
ATOM   5447  CE2 TYR C  18       0.782  23.388 -76.487  1.00264.42           C  
ANISOU 5447  CE2 TYR C  18    30177  46312  23978  -9497    281   4171
ATOM   5448  CZ  TYR C  18       0.441  24.719 -76.373  1.00269.22           C  
ANISOU 5448  CZ  TYR C  18    31237  46240  24816  -9707    176   4685
ATOM   5449  OH  TYR C  18       1.424  25.667 -76.205  1.00274.12           O  
ANISOU 5449  OH  TYR C  18    31833  46629  25693 -10279    335   4805
ATOM   5450  N   VAL C  19      -5.751  21.092 -75.806  1.00249.18           N  
ANISOU 5450  N   VAL C  19    29143  43295  22241  -6599  -1099   4148
ATOM   5451  CA  VAL C  19      -7.005  20.412 -76.095  1.00246.22           C  
ANISOU 5451  CA  VAL C  19    28808  42742  22004  -6046  -1261   4072
ATOM   5452  C   VAL C  19      -7.826  21.255 -77.062  1.00250.27           C  
ANISOU 5452  C   VAL C  19    29690  43039  22361  -6040  -1336   4629
ATOM   5453  O   VAL C  19      -7.603  22.456 -77.229  1.00254.64           O  
ANISOU 5453  O   VAL C  19    30544  43430  22779  -6390  -1323   5100
ATOM   5454  CB  VAL C  19      -7.824  20.117 -74.820  1.00240.90           C  
ANISOU 5454  CB  VAL C  19    28168  41712  21649  -5592  -1490   3834
ATOM   5455  CG1 VAL C  19      -7.054  19.186 -73.899  1.00236.91           C  
ANISOU 5455  CG1 VAL C  19    27324  41370  21322  -5534  -1423   3246
ATOM   5456  CG2 VAL C  19      -8.187  21.412 -74.111  1.00242.29           C  
ANISOU 5456  CG2 VAL C  19    28714  41501  21845  -5667  -1680   4234
ATOM   5457  N   LYS C  20      -8.792  20.597 -77.698  1.00247.82           N  
ANISOU 5457  N   LYS C  20    29376  42697  22090  -5638  -1417   4568
ATOM   5458  CA  LYS C  20      -9.683  21.220 -78.663  1.00251.35           C  
ANISOU 5458  CA  LYS C  20    30152  42960  22391  -5538  -1514   5015
ATOM   5459  C   LYS C  20     -11.110  21.189 -78.131  1.00248.24           C  
ANISOU 5459  C   LYS C  20    29913  42186  22223  -5022  -1781   5024
ATOM   5460  O   LYS C  20     -11.505  20.257 -77.425  1.00243.26           O  
ANISOU 5460  O   LYS C  20    29061  41523  21842  -4692  -1836   4614
ATOM   5461  CB  LYS C  20      -9.607  20.506 -80.020  1.00253.35           C  
ANISOU 5461  CB  LYS C  20    30275  43543  22444  -5525  -1381   4944
ATOM   5462  CG  LYS C  20     -10.389  21.173 -81.139  1.00257.79           C  
ANISOU 5462  CG  LYS C  20    31192  43959  22796  -5459  -1462   5401
ATOM   5463  CD  LYS C  20     -10.312  20.357 -82.419  1.00259.45           C  
ANISOU 5463  CD  LYS C  20    31265  44510  22805  -5410  -1346   5276
ATOM   5464  CE  LYS C  20      -8.940  20.467 -83.062  1.00263.51           C  
ANISOU 5464  CE  LYS C  20    31643  45415  23063  -5892  -1066   5305
ATOM   5465  NZ  LYS C  20      -8.885  19.765 -84.374  1.00265.83           N1+
ANISOU 5465  NZ  LYS C  20    31848  46033  23122  -5826   -968   5224
ATOM   5466  N   LEU C  21     -11.882  22.220 -78.472  1.00253.62           N  
ANISOU 5466  N   LEU C  21    30982  42562  22822  -4952  -1941   5495
ATOM   5467  CA  LEU C  21     -13.268  22.357 -78.033  1.00251.66           C  
ANISOU 5467  CA  LEU C  21    30895  41965  22761  -4466  -2204   5547
ATOM   5468  C   LEU C  21     -14.117  22.725 -79.242  1.00255.58           C  
ANISOU 5468  C   LEU C  21    31655  42387  23066  -4318  -2296   5882
ATOM   5469  O   LEU C  21     -14.024  23.847 -79.751  1.00260.58           O  
ANISOU 5469  O   LEU C  21    32645  42854  23509  -4522  -2332   6354
ATOM   5470  CB  LEU C  21     -13.396  23.411 -76.932  1.00251.75           C  
ANISOU 5470  CB  LEU C  21    31155  41599  22900  -4461  -2383   5772
ATOM   5471  CG  LEU C  21     -12.700  23.092 -75.606  1.00247.75           C  
ANISOU 5471  CG  LEU C  21    30428  41119  22589  -4538  -2347   5426
ATOM   5472  CD1 LEU C  21     -12.785  24.275 -74.652  1.00248.87           C  
ANISOU 5472  CD1 LEU C  21    30882  40865  22813  -4566  -2553   5719
ATOM   5473  CD2 LEU C  21     -13.291  21.842 -74.972  1.00241.99           C  
ANISOU 5473  CD2 LEU C  21    29386  40434  22126  -4109  -2368   4906
ATOM   5474  N   ILE C  22     -14.947  21.789 -79.695  1.00256.52           N  
ANISOU 5474  N   ILE C  22    31625  42600  23240  -3971  -2342   5644
ATOM   5475  CA  ILE C  22     -15.730  21.945 -80.917  1.00258.69           C  
ANISOU 5475  CA  ILE C  22    32110  42869  23313  -3816  -2429   5885
ATOM   5476  C   ILE C  22     -17.175  22.250 -80.551  1.00258.05           C  
ANISOU 5476  C   ILE C  22    32196  42464  23388  -3353  -2711   5970
ATOM   5477  O   ILE C  22     -17.740  21.637 -79.636  1.00254.21           O  
ANISOU 5477  O   ILE C  22    31503  41900  23186  -3072  -2784   5653
ATOM   5478  CB  ILE C  22     -15.633  20.680 -81.792  1.00255.73           C  
ANISOU 5478  CB  ILE C  22    31464  42840  22860  -3776  -2298   5568
ATOM   5479  CG1 ILE C  22     -14.185  20.439 -82.223  1.00256.90           C  
ANISOU 5479  CG1 ILE C  22    31441  43341  22827  -4214  -2024   5489
ATOM   5480  CG2 ILE C  22     -16.535  20.793 -83.012  1.00258.02           C  
ANISOU 5480  CG2 ILE C  22    31978  43115  22940  -3576  -2420   5788
ATOM   5481  CD1 ILE C  22     -13.956  19.084 -82.858  1.00253.01           C  
ANISOU 5481  CD1 ILE C  22    30642  43184  22309  -4150  -1903   5101
ATOM   5482  N   SER C  23     -17.776  23.199 -81.264  1.00260.06           N  
ANISOU 5482  N   SER C  23    32829  42527  23454  -3268  -2867   6392
ATOM   5483  CA  SER C  23     -19.173  23.553 -81.072  1.00259.79           C  
ANISOU 5483  CA  SER C  23    32965  42217  23528  -2810  -3153   6488
ATOM   5484  C   SER C  23     -20.059  22.784 -82.051  1.00258.21           C  
ANISOU 5484  C   SER C  23    32693  42174  23242  -2552  -3219   6358
ATOM   5485  O   SER C  23     -19.584  22.132 -82.983  1.00258.42           O  
ANISOU 5485  O   SER C  23    32613  42485  23088  -2726  -3060   6265
ATOM   5486  CB  SER C  23     -19.374  25.059 -81.245  1.00264.90           C  
ANISOU 5486  CB  SER C  23    34103  42517  24031  -2816  -3331   7016
ATOM   5487  OG  SER C  23     -19.118  25.459 -82.580  1.00268.27           O  
ANISOU 5487  OG  SER C  23    34797  43017  24117  -3011  -3272   7333
ATOM   5488  N   SER C  24     -21.373  22.869 -81.828  1.00259.88           N  
ANISOU 5488  N   SER C  24    32959  42201  23582  -2127  -3469   6347
ATOM   5489  CA  SER C  24     -22.317  22.200 -82.715  1.00258.97           C  
ANISOU 5489  CA  SER C  24    32792  42209  23395  -1880  -3572   6236
ATOM   5490  C   SER C  24     -22.376  22.848 -84.091  1.00264.08           C  
ANISOU 5490  C   SER C  24    33804  42867  23667  -1928  -3639   6608
ATOM   5491  O   SER C  24     -22.781  22.191 -85.055  1.00263.70           O  
ANISOU 5491  O   SER C  24    33712  43003  23481  -1840  -3661   6511
ATOM   5492  CB  SER C  24     -23.714  22.181 -82.092  1.00257.27           C  
ANISOU 5492  CB  SER C  24    32525  41813  23412  -1436  -3827   6134
ATOM   5493  OG  SER C  24     -24.249  23.489 -81.995  1.00261.57           O  
ANISOU 5493  OG  SER C  24    33438  42057  23888  -1239  -4066   6505
ATOM   5494  N   ASP C  25     -21.986  24.118 -84.205  1.00256.48           N  
ANISOU 5494  N   ASP C  25    33227  41690  22535  -2066  -3676   7036
ATOM   5495  CA  ASP C  25     -21.958  24.791 -85.496  1.00262.64           C  
ANISOU 5495  CA  ASP C  25    34403  42448  22940  -2138  -3715   7419
ATOM   5496  C   ASP C  25     -20.713  24.459 -86.309  1.00264.25           C  
ANISOU 5496  C   ASP C  25    34555  42954  22896  -2586  -3405   7441
ATOM   5497  O   ASP C  25     -20.682  24.753 -87.509  1.00269.17           O  
ANISOU 5497  O   ASP C  25    35452  43636  23183  -2644  -3397   7691
ATOM   5498  CB  ASP C  25     -22.058  26.306 -85.304  1.00267.05           C  
ANISOU 5498  CB  ASP C  25    35442  42601  23423  -2111  -3885   7894
ATOM   5499  CG  ASP C  25     -23.421  26.741 -84.799  1.00267.05           C  
ANISOU 5499  CG  ASP C  25    35564  42315  23589  -1592  -4240   7915
ATOM   5500  OD1 ASP C  25     -24.417  26.051 -85.103  1.00265.89           O  
ANISOU 5500  OD1 ASP C  25    35252  42292  23483  -1266  -4382   7684
ATOM   5501  OD2 ASP C  25     -23.496  27.772 -84.099  1.00268.46           O1-
ANISOU 5501  OD2 ASP C  25    36000  42141  23862  -1513  -4388   8159
ATOM   5502  N   GLY C  26     -19.695  23.860 -85.693  1.00257.84           N  
ANISOU 5502  N   GLY C  26    33400  42340  22227  -2885  -3157   7179
ATOM   5503  CA  GLY C  26     -18.502  23.427 -86.393  1.00258.75           C  
ANISOU 5503  CA  GLY C  26    33388  42793  22131  -3285  -2859   7129
ATOM   5504  C   GLY C  26     -17.241  24.191 -86.050  1.00262.15           C  
ANISOU 5504  C   GLY C  26    33904  43197  22504  -3761  -2656   7354
ATOM   5505  O   GLY C  26     -16.152  23.754 -86.444  1.00261.86           O  
ANISOU 5505  O   GLY C  26    33674  43483  22335  -4114  -2385   7245
ATOM   5506  N   HIS C  27     -17.344  25.308 -85.335  1.00257.97           N  
ANISOU 5506  N   HIS C  27    33654  42292  22071  -3787  -2783   7657
ATOM   5507  CA  HIS C  27     -16.169  26.111 -85.015  1.00261.71           C  
ANISOU 5507  CA  HIS C  27    34249  42690  22499  -4283  -2608   7908
ATOM   5508  C   HIS C  27     -15.306  25.404 -83.976  1.00257.35           C  
ANISOU 5508  C   HIS C  27    33252  42346  22184  -4487  -2435   7512
ATOM   5509  O   HIS C  27     -15.780  25.073 -82.883  1.00253.52           O  
ANISOU 5509  O   HIS C  27    32586  41744  21998  -4220  -2568   7252
ATOM   5510  CB  HIS C  27     -16.590  27.490 -84.514  1.00265.83           C  
ANISOU 5510  CB  HIS C  27    35231  42688  23083  -4225  -2838   8342
ATOM   5511  CG  HIS C  27     -17.234  28.343 -85.562  1.00271.16           C  
ANISOU 5511  CG  HIS C  27    36410  43128  23492  -4087  -2994   8781
ATOM   5512  ND1 HIS C  27     -18.588  28.314 -85.819  1.00270.42           N  
ANISOU 5512  ND1 HIS C  27    36452  42896  23401  -3543  -3285   8772
ATOM   5513  CD2 HIS C  27     -16.710  29.256 -86.414  1.00277.03           C  
ANISOU 5513  CD2 HIS C  27    37565  43740  23954  -4421  -2901   9237
ATOM   5514  CE1 HIS C  27     -18.869  29.169 -86.786  1.00275.82           C  
ANISOU 5514  CE1 HIS C  27    37620  43378  23802  -3521  -3381   9197
ATOM   5515  NE2 HIS C  27     -17.747  29.754 -87.164  1.00280.17           N  
ANISOU 5515  NE2 HIS C  27    38358  43916  24177  -4050  -3146   9494
ATOM   5516  N   GLU C  28     -14.041  25.174 -84.317  1.00257.21           N  
ANISOU 5516  N   GLU C  28    33059  42644  22024  -4948  -2139   7456
ATOM   5517  CA  GLU C  28     -13.087  24.601 -83.382  1.00253.63           C  
ANISOU 5517  CA  GLU C  28    32212  42400  21756  -5180  -1971   7098
ATOM   5518  C   GLU C  28     -12.506  25.688 -82.482  1.00256.88           C  
ANISOU 5518  C   GLU C  28    32825  42513  22266  -5508  -1981   7369
ATOM   5519  O   GLU C  28     -12.472  26.871 -82.833  1.00262.54           O  
ANISOU 5519  O   GLU C  28    33974  42925  22853  -5716  -2026   7864
ATOM   5520  CB  GLU C  28     -11.961  23.884 -84.128  1.00252.98           C  
ANISOU 5520  CB  GLU C  28    31832  42811  21479  -5517  -1661   6893
ATOM   5521  CG  GLU C  28     -12.400  22.638 -84.881  1.00250.35           C  
ANISOU 5521  CG  GLU C  28    31253  42779  21088  -5205  -1653   6550
ATOM   5522  CD  GLU C  28     -11.254  21.973 -85.619  1.00251.97           C  
ANISOU 5522  CD  GLU C  28    31179  43468  21090  -5510  -1366   6351
ATOM   5523  OE1 GLU C  28     -10.148  22.552 -85.648  1.00255.21           O  
ANISOU 5523  OE1 GLU C  28    31594  43997  21378  -5982  -1155   6511
ATOM   5524  OE2 GLU C  28     -11.460  20.870 -86.170  1.00250.25           O1-
ANISOU 5524  OE2 GLU C  28    30738  43504  20841  -5282  -1354   6032
ATOM   5525  N   PHE C  29     -12.043  25.270 -81.302  1.00254.55           N  
ANISOU 5525  N   PHE C  29    32234  42277  22208  -5555  -1952   7037
ATOM   5526  CA  PHE C  29     -11.480  26.207 -80.327  1.00257.22           C  
ANISOU 5526  CA  PHE C  29    32742  42329  22661  -5860  -1983   7243
ATOM   5527  C   PHE C  29     -10.365  25.475 -79.577  1.00254.40           C  
ANISOU 5527  C   PHE C  29    31947  42313  22400  -6127  -1777   6811
ATOM   5528  O   PHE C  29     -10.611  24.807 -78.572  1.00249.53           O  
ANISOU 5528  O   PHE C  29    31087  41709  22013  -5841  -1872   6420
ATOM   5529  CB  PHE C  29     -12.548  26.726 -79.375  1.00257.32           C  
ANISOU 5529  CB  PHE C  29    32989  41875  22907  -5442  -2319   7342
ATOM   5530  CG  PHE C  29     -13.603  27.562 -80.042  1.00260.82           C  
ANISOU 5530  CG  PHE C  29    33885  41957  23257  -5173  -2547   7769
ATOM   5531  CD1 PHE C  29     -13.368  28.894 -80.340  1.00267.67           C  
ANISOU 5531  CD1 PHE C  29    35242  42444  24016  -5470  -2604   8313
ATOM   5532  CD2 PHE C  29     -14.833  27.014 -80.370  1.00257.48           C  
ANISOU 5532  CD2 PHE C  29    33410  41554  22866  -4627  -2711   7617
ATOM   5533  CE1 PHE C  29     -14.340  29.662 -80.954  1.00270.82           C  
ANISOU 5533  CE1 PHE C  29    36082  42493  24323  -5184  -2834   8687
ATOM   5534  CE2 PHE C  29     -15.807  27.777 -80.984  1.00260.38           C  
ANISOU 5534  CE2 PHE C  29    34187  41615  23131  -4355  -2935   7981
ATOM   5535  CZ  PHE C  29     -15.561  29.102 -81.276  1.00266.99           C  
ANISOU 5535  CZ  PHE C  29    35522  42078  23845  -4611  -3003   8512
ATOM   5536  N   ILE C  30      -9.141  25.627 -80.069  1.00252.42           N  
ANISOU 5536  N   ILE C  30    31602  42331  21974  -6668  -1494   6875
ATOM   5537  CA  ILE C  30      -7.979  24.976 -79.476  1.00249.96           C  
ANISOU 5537  CA  ILE C  30    30865  42391  21717  -6952  -1280   6460
ATOM   5538  C   ILE C  30      -7.388  25.892 -78.414  1.00250.69           C  
ANISOU 5538  C   ILE C  30    31113  42203  21934  -7317  -1303   6637
ATOM   5539  O   ILE C  30      -7.195  27.091 -78.650  1.00255.87           O  
ANISOU 5539  O   ILE C  30    32156  42528  22533  -7681  -1298   7145
ATOM   5540  CB  ILE C  30      -6.935  24.628 -80.549  1.00253.65           C  
ANISOU 5540  CB  ILE C  30    31100  43334  21940  -7336   -953   6393
ATOM   5541  CG1 ILE C  30      -7.507  23.615 -81.543  1.00252.60           C  
ANISOU 5541  CG1 ILE C  30    30812  43473  21692  -6951   -958   6177
ATOM   5542  CG2 ILE C  30      -5.668  24.090 -79.908  1.00251.86           C  
ANISOU 5542  CG2 ILE C  30    30440  43483  21772  -7651   -737   5972
ATOM   5543  CD1 ILE C  30      -6.645  23.410 -82.768  1.00257.24           C  
ANISOU 5543  CD1 ILE C  30    31265  44483  21993  -7269   -678   6197
ATOM   5544  N   VAL C  31      -7.104  25.330 -77.239  1.00256.05           N  
ANISOU 5544  N   VAL C  31    31519  42976  22791  -7221  -1340   6217
ATOM   5545  CA  VAL C  31      -6.510  26.085 -76.141  1.00256.31           C  
ANISOU 5545  CA  VAL C  31    31630  42584  23172  -7445  -1370   6180
ATOM   5546  C   VAL C  31      -5.857  25.077 -75.208  1.00251.27           C  
ANISOU 5546  C   VAL C  31    30515  42196  22759  -7335  -1295   5499
ATOM   5547  O   VAL C  31      -6.177  23.888 -75.239  1.00247.00           O  
ANISOU 5547  O   VAL C  31    29702  42105  22041  -7024  -1311   5165
ATOM   5548  CB  VAL C  31      -7.576  26.945 -75.412  1.00255.71           C  
ANISOU 5548  CB  VAL C  31    31968  41763  23425  -7050  -1723   6393
ATOM   5549  CG1 VAL C  31      -8.572  26.058 -74.675  1.00249.35           C  
ANISOU 5549  CG1 VAL C  31    31006  41007  22730  -6412  -1946   6032
ATOM   5550  CG2 VAL C  31      -6.926  27.965 -74.482  1.00257.64           C  
ANISOU 5550  CG2 VAL C  31    32367  41371  24152  -7277  -1760   6370
ATOM   5551  N   LYS C  32      -4.920  25.550 -74.384  1.00260.01           N  
ANISOU 5551  N   LYS C  32    31534  43002  24257  -7596  -1227   5286
ATOM   5552  CA  LYS C  32      -4.260  24.679 -73.420  1.00256.34           C  
ANISOU 5552  CA  LYS C  32    30650  42715  24032  -7477  -1185   4631
ATOM   5553  C   LYS C  32      -5.290  23.977 -72.544  1.00249.90           C  
ANISOU 5553  C   LYS C  32    29827  41759  23366  -6831  -1452   4332
ATOM   5554  O   LYS C  32      -6.396  24.480 -72.322  1.00249.41           O  
ANISOU 5554  O   LYS C  32    30096  41272  23399  -6499  -1693   4599
ATOM   5555  CB  LYS C  32      -3.287  25.474 -72.548  1.00260.56           C  
ANISOU 5555  CB  LYS C  32    31170  42810  25022  -7791  -1154   4486
ATOM   5556  CG  LYS C  32      -2.057  25.978 -73.282  1.00266.11           C  
ANISOU 5556  CG  LYS C  32    31750  43747  25611  -8486   -844   4659
ATOM   5557  CD  LYS C  32      -1.199  26.854 -72.386  1.00269.34           C  
ANISOU 5557  CD  LYS C  32    32178  43648  26511  -8797   -863   4542
ATOM   5558  CE  LYS C  32      -0.513  26.030 -71.308  1.00264.56           C  
ANISOU 5558  CE  LYS C  32    31143  43190  26187  -8620   -872   3831
ATOM   5559  NZ  LYS C  32       0.423  26.849 -70.490  1.00268.37           N1+
ANISOU 5559  NZ  LYS C  32    31601  43232  27134  -8957   -887   3685
ATOM   5560  N   ARG C  33      -4.917  22.797 -72.043  1.00260.35           N  
ANISOU 5560  N   ARG C  33    30768  43452  24702  -6653  -1409   3767
ATOM   5561  CA  ARG C  33      -5.880  21.971 -71.323  1.00253.75           C  
ANISOU 5561  CA  ARG C  33    29901  42574  23937  -6080  -1629   3486
ATOM   5562  C   ARG C  33      -6.314  22.627 -70.018  1.00253.37           C  
ANISOU 5562  C   ARG C  33    30069  41840  24362  -5792  -1854   3417
ATOM   5563  O   ARG C  33      -7.485  22.532 -69.633  1.00250.72           O  
ANISOU 5563  O   ARG C  33    29893  41293  24076  -5343  -2066   3481
ATOM   5564  CB  ARG C  33      -5.298  20.577 -71.075  1.00248.50           C  
ANISOU 5564  CB  ARG C  33    28820  42426  23172  -5981  -1541   2898
ATOM   5565  CG  ARG C  33      -4.068  20.529 -70.181  1.00249.36           C  
ANISOU 5565  CG  ARG C  33    28688  42463  23593  -6150  -1455   2433
ATOM   5566  CD  ARG C  33      -3.555  19.101 -70.049  1.00244.26           C  
ANISOU 5566  CD  ARG C  33    27661  42353  22792  -6010  -1396   1865
ATOM   5567  NE  ARG C  33      -4.495  18.238 -69.338  1.00237.97           N  
ANISOU 5567  NE  ARG C  33    26899  41356  22163  -5444  -1572   1606
ATOM   5568  CZ  ARG C  33      -4.437  16.910 -69.337  1.00233.20           C  
ANISOU 5568  CZ  ARG C  33    26072  40768  21767  -5104  -1438   1181
ATOM   5569  NH1 ARG C  33      -3.481  16.285 -70.010  1.00233.29           N  
ANISOU 5569  NH1 ARG C  33    25786  41203  21652  -5294  -1221    958
ATOM   5570  NH2 ARG C  33      -5.335  16.205 -68.663  1.00227.97           N1+
ANISOU 5570  NH2 ARG C  33    25505  39688  21426  -4582  -1516    999
ATOM   5571  N   GLU C  34      -5.398  23.322 -69.337  1.00251.60           N  
ANISOU 5571  N   GLU C  34    29849  41266  24481  -6042  -1816   3289
ATOM   5572  CA  GLU C  34      -5.746  23.936 -68.060  1.00251.40           C  
ANISOU 5572  CA  GLU C  34    30035  40589  24897  -5752  -2038   3183
ATOM   5573  C   GLU C  34      -6.729  25.087 -68.237  1.00254.56           C  
ANISOU 5573  C   GLU C  34    30891  40471  25358  -5628  -2222   3716
ATOM   5574  O   GLU C  34      -7.561  25.329 -67.355  1.00253.32           O  
ANISOU 5574  O   GLU C  34    30921  39894  25435  -5186  -2448   3671
ATOM   5575  CB  GLU C  34      -4.482  24.412 -67.343  1.00254.99           C  
ANISOU 5575  CB  GLU C  34    30385  40800  25698  -6071  -1972   2907
ATOM   5576  CG  GLU C  34      -4.734  24.976 -65.953  1.00254.88           C  
ANISOU 5576  CG  GLU C  34    30576  40131  26137  -5755  -2209   2725
ATOM   5577  CD  GLU C  34      -3.457  25.373 -65.243  1.00257.87           C  
ANISOU 5577  CD  GLU C  34    30826  40295  26856  -6066  -2167   2409
ATOM   5578  OE1 GLU C  34      -2.371  25.227 -65.843  1.00260.78           O  
ANISOU 5578  OE1 GLU C  34    30922  41043  27118  -6545  -1940   2339
ATOM   5579  OE2 GLU C  34      -3.538  25.829 -64.083  1.00257.80           O1-
ANISOU 5579  OE2 GLU C  34    30979  39755  27217  -5824  -2363   2219
ATOM   5580  N   HIS C  35      -6.656  25.801 -69.363  1.00251.92           N  
ANISOU 5580  N   HIS C  35    30751  40166  24802  -5993  -2133   4220
ATOM   5581  CA  HIS C  35      -7.650  26.832 -69.641  1.00255.66           C  
ANISOU 5581  CA  HIS C  35    31682  40177  25280  -5838  -2335   4738
ATOM   5582  C   HIS C  35      -9.036  26.232 -69.835  1.00251.00           C  
ANISOU 5582  C   HIS C  35    31123  39766  24480  -5313  -2494   4812
ATOM   5583  O   HIS C  35     -10.042  26.905 -69.584  1.00252.71           O  
ANISOU 5583  O   HIS C  35    31657  39555  24807  -4969  -2732   5060
ATOM   5584  CB  HIS C  35      -7.246  27.640 -70.873  1.00262.39           C  
ANISOU 5584  CB  HIS C  35    32749  41058  25887  -6359  -2198   5268
ATOM   5585  CG  HIS C  35      -6.011  28.464 -70.679  1.00269.09           C  
ANISOU 5585  CG  HIS C  35    33634  41627  26981  -6904  -2073   5287
ATOM   5586  ND1 HIS C  35      -4.745  27.975 -70.918  1.00269.60           N  
ANISOU 5586  ND1 HIS C  35    33311  42145  26978  -7363  -1782   5027
ATOM   5587  CD2 HIS C  35      -5.850  29.746 -70.274  1.00275.27           C  
ANISOU 5587  CD2 HIS C  35    34788  41723  28079  -7071  -2210   5526
ATOM   5588  CE1 HIS C  35      -3.856  28.919 -70.665  1.00275.54           C  
ANISOU 5588  CE1 HIS C  35    34168  42519  28005  -7812  -1735   5110
ATOM   5589  NE2 HIS C  35      -4.500  30.004 -70.273  1.00279.23           N  
ANISOU 5589  NE2 HIS C  35    35111  42274  28710  -7654  -1999   5416
ATOM   5590  N   ALA C  36      -9.109  24.978 -70.279  1.00258.19           N  
ANISOU 5590  N   ALA C  36    31702  41306  25092  -5240  -2380   4589
ATOM   5591  CA  ALA C  36     -10.383  24.289 -70.427  1.00253.83           C  
ANISOU 5591  CA  ALA C  36    31125  40963  24355  -4773  -2531   4608
ATOM   5592  C   ALA C  36     -10.825  23.577 -69.157  1.00248.89           C  
ANISOU 5592  C   ALA C  36    30332  40251  23984  -4319  -2651   4147
ATOM   5593  O   ALA C  36     -12.016  23.275 -69.017  1.00246.72           O  
ANISOU 5593  O   ALA C  36    30089  39987  23665  -3894  -2818   4192
ATOM   5594  CB  ALA C  36     -10.309  23.280 -71.577  1.00251.15           C  
ANISOU 5594  CB  ALA C  36    30547  41328  23550  -4914  -2379   4610
ATOM   5595  N   LEU C  37      -9.904  23.313 -68.225  1.00254.58           N  
ANISOU 5595  N   LEU C  37    30875  40890  24964  -4402  -2573   3708
ATOM   5596  CA  LEU C  37     -10.226  22.624 -66.973  1.00249.29           C  
ANISOU 5596  CA  LEU C  37    30070  40129  24519  -3991  -2674   3258
ATOM   5597  C   LEU C  37     -10.971  23.507 -65.976  1.00250.39           C  
ANISOU 5597  C   LEU C  37    30493  39650  24994  -3625  -2890   3340
ATOM   5598  O   LEU C  37     -11.126  23.087 -64.821  1.00247.02           O  
ANISOU 5598  O   LEU C  37    29989  39087  24782  -3307  -2960   2969
ATOM   5599  CB  LEU C  37      -8.950  22.090 -66.317  1.00247.91           C  
ANISOU 5599  CB  LEU C  37    29638  40060  24495  -4186  -2540   2756
ATOM   5600  CG  LEU C  37      -8.153  20.993 -67.028  1.00246.08           C  
ANISOU 5600  CG  LEU C  37    29064  40473  23962  -4447  -2341   2510
ATOM   5601  CD1 LEU C  37      -6.861  20.698 -66.279  1.00245.34           C  
ANISOU 5601  CD1 LEU C  37    28747  40392  24078  -4617  -2245   2020
ATOM   5602  CD2 LEU C  37      -8.971  19.727 -67.207  1.00240.70           C  
ANISOU 5602  CD2 LEU C  37    28228  40127  23098  -4107  -2362   2339
ATOM   5603  N   THR C  38     -11.431  24.697 -66.368  1.00246.05           N  
ANISOU 5603  N   THR C  38    30282  38724  24481  -3640  -3004   3802
ATOM   5604  CA  THR C  38     -12.103  25.583 -65.423  1.00246.52           C  
ANISOU 5604  CA  THR C  38    30625  38186  24854  -3265  -3225   3860
ATOM   5605  C   THR C  38     -13.468  25.033 -65.029  1.00243.36           C  
ANISOU 5605  C   THR C  38    30168  37891  24407  -2710  -3365   3803
ATOM   5606  O   THR C  38     -13.798  24.952 -63.840  1.00240.84           O  
ANISOU 5606  O   THR C  38    29845  37334  24331  -2344  -3457   3522
ATOM   5607  CB  THR C  38     -12.243  26.979 -66.024  1.00252.09           C  
ANISOU 5607  CB  THR C  38    31736  38463  25584  -3420  -3334   4376
ATOM   5608  OG1 THR C  38     -13.054  26.913 -67.204  1.00253.76           O  
ANISOU 5608  OG1 THR C  38    32013  38962  25444  -3387  -3363   4775
ATOM   5609  CG2 THR C  38     -10.880  27.522 -66.393  1.00255.60           C  
ANISOU 5609  CG2 THR C  38    32223  38810  26084  -4022  -3177   4443
ATOM   5610  N   SER C  39     -14.276  24.653 -66.014  1.00250.33           N  
ANISOU 5610  N   SER C  39    31001  39142  24972  -2644  -3383   4065
ATOM   5611  CA  SER C  39     -15.580  24.074 -65.738  1.00246.16           C  
ANISOU 5611  CA  SER C  39    30368  38778  24384  -2164  -3507   4018
ATOM   5612  C   SER C  39     -15.427  22.616 -65.328  1.00239.64           C  
ANISOU 5612  C   SER C  39    29178  38390  23483  -2119  -3390   3572
ATOM   5613  O   SER C  39     -14.620  21.876 -65.898  1.00237.79           O  
ANISOU 5613  O   SER C  39    28757  38449  23145  -2432  -3185   3397
ATOM   5614  CB  SER C  39     -16.484  24.184 -66.964  1.00247.48           C  
ANISOU 5614  CB  SER C  39    30606  39186  24240  -2118  -3594   4446
ATOM   5615  OG  SER C  39     -15.997  23.385 -68.025  1.00246.13           O  
ANISOU 5615  OG  SER C  39    30247  39403  23869  -2432  -3371   4388
ATOM   5616  N   GLY C  40     -16.210  22.207 -64.327  1.00246.29           N  
ANISOU 5616  N   GLY C  40    29948  39107  24525  -1683  -3443   3317
ATOM   5617  CA  GLY C  40     -16.104  20.848 -63.824  1.00240.95           C  
ANISOU 5617  CA  GLY C  40    29017  38509  24022  -1581  -3232   2809
ATOM   5618  C   GLY C  40     -16.455  19.796 -64.857  1.00237.94           C  
ANISOU 5618  C   GLY C  40    28464  38321  23623  -1631  -3025   2738
ATOM   5619  O   GLY C  40     -15.905  18.690 -64.837  1.00234.69           O  
ANISOU 5619  O   GLY C  40    27870  38013  23289  -1729  -2829   2388
ATOM   5620  N   THR C  41     -17.367  20.122 -65.775  1.00240.24           N  
ANISOU 5620  N   THR C  41    28826  38639  23816  -1547  -3086   3062
ATOM   5621  CA  THR C  41     -17.759  19.150 -66.788  1.00237.88           C  
ANISOU 5621  CA  THR C  41    28373  38514  23495  -1585  -2931   2996
ATOM   5622  C   THR C  41     -16.599  18.827 -67.727  1.00239.32           C  
ANISOU 5622  C   THR C  41    28472  38951  23507  -1995  -2768   2977
ATOM   5623  O   THR C  41     -16.386  17.660 -68.069  1.00236.23           O  
ANISOU 5623  O   THR C  41    27894  38691  23173  -2044  -2593   2699
ATOM   5624  CB  THR C  41     -18.984  19.655 -67.559  1.00238.88           C  
ANISOU 5624  CB  THR C  41    28605  38612  23545  -1392  -3066   3335
ATOM   5625  OG1 THR C  41     -19.443  18.638 -68.459  1.00236.45           O  
ANISOU 5625  OG1 THR C  41    28141  38465  23235  -1405  -2943   3231
ATOM   5626  CG2 THR C  41     -18.674  20.926 -68.337  1.00244.33           C  
ANISOU 5626  CG2 THR C  41    29542  39296  23996  -1582  -3199   3799
ATOM   5627  N   ILE C  42     -15.814  19.834 -68.121  1.00239.11           N  
ANISOU 5627  N   ILE C  42    28589  38994  23269  -2302  -2825   3271
ATOM   5628  CA  ILE C  42     -14.724  19.586 -69.060  1.00240.08           C  
ANISOU 5628  CA  ILE C  42    28614  39410  23195  -2717  -2653   3276
ATOM   5629  C   ILE C  42     -13.580  18.850 -68.375  1.00237.45           C  
ANISOU 5629  C   ILE C  42    28078  39181  22961  -2865  -2507   2836
ATOM   5630  O   ILE C  42     -12.985  17.932 -68.952  1.00235.42           O  
ANISOU 5630  O   ILE C  42    27621  39152  22674  -3007  -2316   2610
ATOM   5631  CB  ILE C  42     -14.250  20.901 -69.708  1.00246.06           C  
ANISOU 5631  CB  ILE C  42    29612  40203  23678  -3057  -2738   3766
ATOM   5632  CG1 ILE C  42     -15.369  21.513 -70.552  1.00248.27           C  
ANISOU 5632  CG1 ILE C  42    30108  40363  23861  -2880  -2870   4182
ATOM   5633  CG2 ILE C  42     -13.021  20.658 -70.571  1.00248.01           C  
ANISOU 5633  CG2 ILE C  42    29730  40797  23705  -3526  -2528   3749
ATOM   5634  CD1 ILE C  42     -15.070  22.915 -71.039  1.00253.53           C  
ANISOU 5634  CD1 ILE C  42    31112  40916  24300  -3155  -2989   4722
ATOM   5635  N   LYS C  43     -13.252  19.229 -67.135  1.00242.08           N  
ANISOU 5635  N   LYS C  43    28717  39589  23672  -2804  -2609   2691
ATOM   5636  CA  LYS C  43     -12.245  18.467 -66.406  1.00239.50           C  
ANISOU 5636  CA  LYS C  43    28207  39314  23477  -2875  -2486   2221
ATOM   5637  C   LYS C  43     -12.727  17.056 -66.105  1.00233.92           C  
ANISOU 5637  C   LYS C  43    27358  38510  23012  -2560  -2354   1839
ATOM   5638  O   LYS C  43     -11.902  16.171 -65.853  1.00231.22           O  
ANISOU 5638  O   LYS C  43    26864  38223  22767  -2609  -2209   1466
ATOM   5639  CB  LYS C  43     -11.844  19.176 -65.109  1.00240.58           C  
ANISOU 5639  CB  LYS C  43    28450  39248  23710  -2847  -2657   2119
ATOM   5640  CG  LYS C  43     -12.891  19.183 -64.011  1.00239.05           C  
ANISOU 5640  CG  LYS C  43    28363  38722  23744  -2378  -2794   2033
ATOM   5641  CD  LYS C  43     -12.367  19.920 -62.784  1.00240.60           C  
ANISOU 5641  CD  LYS C  43    28665  38735  24019  -2365  -2983   1915
ATOM   5642  CE  LYS C  43     -13.391  19.954 -61.661  1.00238.91           C  
ANISOU 5642  CE  LYS C  43    28552  38221  24004  -1876  -3109   1825
ATOM   5643  NZ  LYS C  43     -13.641  18.598 -61.098  1.00233.04           N1+
ANISOU 5643  NZ  LYS C  43    27674  37392  23478  -1618  -2921   1399
ATOM   5644  N   ALA C  44     -14.042  16.828 -66.127  1.00233.61           N  
ANISOU 5644  N   ALA C  44    27377  38316  23070  -2249  -2408   1938
ATOM   5645  CA  ALA C  44     -14.565  15.471 -66.111  1.00230.48           C  
ANISOU 5645  CA  ALA C  44    26867  37855  22852  -2045  -2283   1664
ATOM   5646  C   ALA C  44     -14.518  14.815 -67.486  1.00231.60           C  
ANISOU 5646  C   ALA C  44    26895  38233  22869  -2194  -2162   1718
ATOM   5647  O   ALA C  44     -14.591  13.584 -67.571  1.00229.27           O  
ANISOU 5647  O   ALA C  44    26499  37911  22699  -2105  -2048   1458
ATOM   5648  CB  ALA C  44     -16.000  15.465 -65.582  1.00229.37           C  
ANISOU 5648  CB  ALA C  44    26803  37497  22849  -1700  -2387   1737
ATOM   5649  N   MET C  45     -14.396  15.602 -68.560  1.00231.41           N  
ANISOU 5649  N   MET C  45    26912  38422  22593  -2416  -2196   2060
ATOM   5650  CA  MET C  45     -14.301  15.023 -69.897  1.00231.87           C  
ANISOU 5650  CA  MET C  45    26870  38723  22507  -2552  -2090   2106
ATOM   5651  C   MET C  45     -12.877  14.570 -70.199  1.00232.39           C  
ANISOU 5651  C   MET C  45    26771  39042  22486  -2830  -1922   1887
ATOM   5652  O   MET C  45     -12.661  13.448 -70.670  1.00230.51           O  
ANISOU 5652  O   MET C  45    26395  38898  22290  -2802  -1801   1652
ATOM   5653  CB  MET C  45     -14.783  16.024 -70.951  1.00235.45           C  
ANISOU 5653  CB  MET C  45    27462  39284  22713  -2657  -2191   2568
ATOM   5654  CG  MET C  45     -16.250  16.377 -70.806  1.00235.37           C  
ANISOU 5654  CG  MET C  45    27587  39057  22785  -2344  -2361   2764
ATOM   5655  SD  MET C  45     -16.931  17.570 -71.971  1.00240.17           S  
ANISOU 5655  SD  MET C  45    28418  39706  23129  -2381  -2515   3306
ATOM   5656  CE  MET C  45     -17.076  16.555 -73.433  1.00239.28           C  
ANISOU 5656  CE  MET C  45    28178  39842  22898  -2443  -2404   3240
ATOM   5657  N   LEU C  46     -11.892  15.433 -69.934  1.00231.41           N  
ANISOU 5657  N   LEU C  46    26659  39036  22232  -3103  -1923   1961
ATOM   5658  CA  LEU C  46     -10.498  15.039 -70.089  1.00231.83           C  
ANISOU 5658  CA  LEU C  46    26517  39360  22207  -3371  -1762   1713
ATOM   5659  C   LEU C  46     -10.098  13.954 -69.100  1.00227.75           C  
ANISOU 5659  C   LEU C  46    25893  38672  21969  -3158  -1687   1224
ATOM   5660  O   LEU C  46      -9.117  13.242 -69.341  1.00227.60           O  
ANISOU 5660  O   LEU C  46    25692  38851  21936  -3264  -1540    952
ATOM   5661  CB  LEU C  46      -9.584  16.254 -69.933  1.00234.97           C  
ANISOU 5661  CB  LEU C  46    26960  39917  22402  -3752  -1796   1905
ATOM   5662  CG  LEU C  46      -9.728  17.318 -71.021  1.00239.78           C  
ANISOU 5662  CG  LEU C  46    27718  40696  22692  -4044  -1832   2429
ATOM   5663  CD1 LEU C  46      -8.871  18.532 -70.706  1.00242.91           C  
ANISOU 5663  CD1 LEU C  46    28223  41170  22903  -4454  -1880   2652
ATOM   5664  CD2 LEU C  46      -9.375  16.740 -72.383  1.00241.87           C  
ANISOU 5664  CD2 LEU C  46    27825  41311  22763  -4208  -1662   2444
ATOM   5665  N   SER C  47     -10.833  13.814 -67.995  1.00233.48           N  
ANISOU 5665  N   SER C  47    26742  39029  22941  -2846  -1784   1114
ATOM   5666  CA  SER C  47     -10.627  12.697 -67.083  1.00229.19           C  
ANISOU 5666  CA  SER C  47    26166  38250  22668  -2607  -1719    695
ATOM   5667  C   SER C  47     -11.148  11.383 -67.646  1.00226.33           C  
ANISOU 5667  C   SER C  47    25761  37839  22395  -2438  -1637    574
ATOM   5668  O   SER C  47     -10.962  10.340 -67.009  1.00223.05           O  
ANISOU 5668  O   SER C  47    25350  37212  22185  -2256  -1583    260
ATOM   5669  CB  SER C  47     -11.300  12.984 -65.740  1.00227.44           C  
ANISOU 5669  CB  SER C  47    26107  37660  22650  -2344  -1848    645
ATOM   5670  OG  SER C  47     -11.145  11.893 -64.849  1.00224.00           O  
ANISOU 5670  OG  SER C  47    25684  36964  22462  -2118  -1788    277
ATOM   5671  N   GLY C  48     -11.797  11.410 -68.809  1.00226.83           N  
ANISOU 5671  N   GLY C  48    25810  38067  22308  -2492  -1647    825
ATOM   5672  CA  GLY C  48     -12.283  10.212 -69.447  1.00224.69           C  
ANISOU 5672  CA  GLY C  48    25505  37770  22095  -2363  -1598    722
ATOM   5673  C   GLY C  48     -11.164   9.235 -69.740  1.00223.91           C  
ANISOU 5673  C   GLY C  48    25272  37803  22001  -2421  -1462    419
ATOM   5674  O   GLY C  48     -10.128   9.592 -70.310  1.00226.47           O  
ANISOU 5674  O   GLY C  48    25454  38457  22137  -2661  -1381    420
ATOM   5675  N   PRO C  49     -11.352   7.979 -69.346  1.00225.97           N  
ANISOU 5675  N   PRO C  49    25579  37814  22467  -2205  -1443    161
ATOM   5676  CA  PRO C  49     -10.295   6.982 -69.530  1.00225.57           C  
ANISOU 5676  CA  PRO C  49    25431  37833  22441  -2200  -1339   -141
ATOM   5677  C   PRO C  49     -10.024   6.705 -71.001  1.00228.38           C  
ANISOU 5677  C   PRO C  49    25652  38548  22572  -2337  -1282    -73
ATOM   5678  O   PRO C  49     -10.830   7.003 -71.886  1.00230.11           O  
ANISOU 5678  O   PRO C  49    25893  38884  22654  -2385  -1334    184
ATOM   5679  CB  PRO C  49     -10.849   5.742 -68.821  1.00222.23           C  
ANISOU 5679  CB  PRO C  49    25163  36999  22273  -1931  -1380   -342
ATOM   5680  CG  PRO C  49     -12.327   5.917 -68.865  1.00221.80           C  
ANISOU 5680  CG  PRO C  49    25217  36806  22250  -1851  -1479   -112
ATOM   5681  CD  PRO C  49     -12.570   7.396 -68.757  1.00223.43           C  
ANISOU 5681  CD  PRO C  49    25407  37145  22343  -1967  -1523    154
ATOM   5682  N   GLY C  50      -8.855   6.121 -71.249  1.00231.51           N  
ANISOU 5682  N   GLY C  50    25909  39128  22928  -2382  -1180   -319
ATOM   5683  CA  GLY C  50      -8.412   5.833 -72.598  1.00234.06           C  
ANISOU 5683  CA  GLY C  50    26076  39836  23020  -2508  -1114   -300
ATOM   5684  C   GLY C  50      -6.919   6.018 -72.772  1.00236.07           C  
ANISOU 5684  C   GLY C  50    26090  40474  23134  -2698   -981   -473
ATOM   5685  O   GLY C  50      -6.326   5.475 -73.710  1.00237.29           O  
ANISOU 5685  O   GLY C  50    26089  40935  23134  -2745   -909   -574
ATOM   5686  N   GLN C  51      -6.301   6.778 -71.872  1.00226.22           N  
ANISOU 5686  N   GLN C  51    24798  39229  21928  -2807   -952   -523
ATOM   5687  CA  GLN C  51      -4.858   6.996 -71.902  1.00228.05           C  
ANISOU 5687  CA  GLN C  51    24775  39837  22036  -3010   -824   -719
ATOM   5688  C   GLN C  51      -4.365   7.552 -70.570  1.00227.92           C  
ANISOU 5688  C   GLN C  51    24792  39633  22173  -3017   -837   -857
ATOM   5689  O   GLN C  51      -3.527   6.943 -69.903  1.00225.52           O  
ANISOU 5689  O   GLN C  51    24431  39237  22019  -2880   -792  -1200
ATOM   5690  CB  GLN C  51      -4.475   7.944 -73.042  1.00232.49           C  
ANISOU 5690  CB  GLN C  51    25146  40954  22235  -3405   -754   -457
ATOM   5691  CG  GLN C  51      -2.976   8.147 -73.202  1.00233.77           C  
ANISOU 5691  CG  GLN C  51    24992  41603  22227  -3673   -603   -661
ATOM   5692  CD  GLN C  51      -2.628   9.033 -74.382  1.00237.24           C  
ANISOU 5692  CD  GLN C  51    25261  42599  22279  -4103   -535   -372
ATOM   5693  OE1 GLN C  51      -3.511   9.538 -75.076  1.00238.87           O  
ANISOU 5693  OE1 GLN C  51    25625  42785  22349  -4175   -611      1
ATOM   5694  NE2 GLN C  51      -1.335   9.225 -74.617  1.00237.88           N  
ANISOU 5694  NE2 GLN C  51    25030  43177  22175  -4392   -393   -541
ATOM   5695  N   ASN C  58      -5.343  15.389 -76.739  1.00243.49           N  
ANISOU 5695  N   ASN C  58    27126  43430  21960  -5422   -865   2201
ATOM   5696  CA  ASN C  58      -6.742  15.324 -76.334  1.00240.26           C  
ANISOU 5696  CA  ASN C  58    26962  42550  21776  -5017  -1059   2309
ATOM   5697  C   ASN C  58      -7.573  16.335 -77.117  1.00243.75           C  
ANISOU 5697  C   ASN C  58    27723  42868  22023  -5089  -1149   2860
ATOM   5698  O   ASN C  58      -7.166  17.482 -77.284  1.00247.63           O  
ANISOU 5698  O   ASN C  58    28370  43414  22305  -5457  -1114   3224
ATOM   5699  CB  ASN C  58      -6.879  15.578 -74.832  1.00236.70           C  
ANISOU 5699  CB  ASN C  58    26583  41768  21586  -4890  -1169   2170
ATOM   5700  CG  ASN C  58      -6.306  14.451 -73.996  1.00232.72           C  
ANISOU 5700  CG  ASN C  58    25836  41248  21340  -4688  -1104   1612
ATOM   5701  OD1 ASN C  58      -6.482  13.275 -74.313  1.00230.73           O  
ANISOU 5701  OD1 ASN C  58    25469  40988  21210  -4422  -1057   1350
ATOM   5702  ND2 ASN C  58      -5.615  14.806 -72.918  1.00231.76           N  
ANISOU 5702  ND2 ASN C  58    25669  41083  21305  -4804  -1109   1434
ATOM   5703  N   GLU C  59      -8.736  15.903 -77.602  1.00244.92           N  
ANISOU 5703  N   GLU C  59    27989  42825  22244  -4742  -1260   2925
ATOM   5704  CA  GLU C  59      -9.635  16.772 -78.349  1.00247.95           C  
ANISOU 5704  CA  GLU C  59    28684  43059  22465  -4726  -1369   3408
ATOM   5705  C   GLU C  59     -11.071  16.477 -77.945  1.00244.70           C  
ANISOU 5705  C   GLU C  59    28406  42271  22298  -4273  -1566   3390
ATOM   5706  O   GLU C  59     -11.445  15.318 -77.744  1.00240.47           O  
ANISOU 5706  O   GLU C  59    27716  41681  21971  -3989  -1572   3036
ATOM   5707  CB  GLU C  59      -9.454  16.600 -79.864  1.00250.53           C  
ANISOU 5707  CB  GLU C  59    29005  43689  22496  -4848  -1267   3549
ATOM   5708  CG  GLU C  59      -8.109  17.100 -80.379  1.00254.68           C  
ANISOU 5708  CG  GLU C  59    29437  44591  22737  -5336  -1057   3656
ATOM   5709  CD  GLU C  59      -7.940  16.910 -81.872  1.00257.27           C  
ANISOU 5709  CD  GLU C  59    29770  45220  22762  -5426   -949   3784
ATOM   5710  OE1 GLU C  59      -8.814  16.275 -82.497  1.00255.58           O  
ANISOU 5710  OE1 GLU C  59    29608  44939  22560  -5100  -1047   3740
ATOM   5711  OE2 GLU C  59      -6.930  17.399 -82.421  1.00261.18           O1-
ANISOU 5711  OE2 GLU C  59    30221  46015  23000  -5832   -760   3925
ATOM   5712  N   VAL C  60     -11.870  17.536 -77.830  1.00246.92           N  
ANISOU 5712  N   VAL C  60    28984  42283  22551  -4214  -1723   3780
ATOM   5713  CA  VAL C  60     -13.218  17.469 -77.279  1.00244.42           C  
ANISOU 5713  CA  VAL C  60    28787  41617  22463  -3804  -1919   3782
ATOM   5714  C   VAL C  60     -14.178  18.180 -78.224  1.00247.62           C  
ANISOU 5714  C   VAL C  60    29473  41921  22692  -3704  -2055   4202
ATOM   5715  O   VAL C  60     -13.840  19.221 -78.797  1.00252.42           O  
ANISOU 5715  O   VAL C  60    30302  42554  23051  -3959  -2047   4600
ATOM   5716  CB  VAL C  60     -13.271  18.097 -75.868  1.00243.79           C  
ANISOU 5716  CB  VAL C  60    28788  41262  22578  -3746  -2021   3784
ATOM   5717  CG1 VAL C  60     -14.691  18.169 -75.360  1.00241.95           C  
ANISOU 5717  CG1 VAL C  60    28684  40699  22547  -3328  -2220   3829
ATOM   5718  CG2 VAL C  60     -12.401  17.306 -74.901  1.00240.34           C  
ANISOU 5718  CG2 VAL C  60    28090  40897  22329  -3786  -1903   3324
ATOM   5719  N   ASN C  61     -15.373  17.616 -78.389  1.00251.49           N  
ANISOU 5719  N   ASN C  61    29968  42280  23309  -3343  -2178   4115
ATOM   5720  CA  ASN C  61     -16.418  18.203 -79.215  1.00253.97           C  
ANISOU 5720  CA  ASN C  61    30534  42483  23479  -3178  -2341   4458
ATOM   5721  C   ASN C  61     -17.699  18.386 -78.407  1.00252.18           C  
ANISOU 5721  C   ASN C  61    30385  41942  23489  -2803  -2549   4462
ATOM   5722  O   ASN C  61     -17.827  17.909 -77.276  1.00248.83           O  
ANISOU 5722  O   ASN C  61    29806  41397  23339  -2662  -2547   4178
ATOM   5723  CB  ASN C  61     -16.683  17.348 -80.466  1.00253.32           C  
ANISOU 5723  CB  ASN C  61    30381  42614  23254  -3119  -2305   4366
ATOM   5724  CG  ASN C  61     -17.166  15.940 -80.137  1.00248.38           C  
ANISOU 5724  CG  ASN C  61    29508  41981  22885  -2880  -2299   3929
ATOM   5725  OD1 ASN C  61     -17.407  15.598 -78.979  1.00245.03           O  
ANISOU 5725  OD1 ASN C  61    28975  41376  22748  -2737  -2318   3704
ATOM   5726  ND2 ASN C  61     -17.312  15.117 -81.169  1.00248.21           N  
ANISOU 5726  ND2 ASN C  61    29424  42135  22749  -2839  -2274   3821
ATOM   5727  N   PHE C  62     -18.653  19.095 -79.009  1.00250.57           N  
ANISOU 5727  N   PHE C  62    30430  41610  23164  -2630  -2731   4787
ATOM   5728  CA  PHE C  62     -19.964  19.327 -78.414  1.00249.10           C  
ANISOU 5728  CA  PHE C  62    30313  41170  23165  -2251  -2946   4814
ATOM   5729  C   PHE C  62     -21.003  19.339 -79.523  1.00250.58           C  
ANISOU 5729  C   PHE C  62    30629  41375  23203  -2051  -3097   4976
ATOM   5730  O   PHE C  62     -20.871  20.098 -80.488  1.00255.05           O  
ANISOU 5730  O   PHE C  62    31456  41964  23488  -2155  -3141   5320
ATOM   5731  CB  PHE C  62     -20.005  20.649 -77.637  1.00252.05           C  
ANISOU 5731  CB  PHE C  62    30933  41274  23561  -2214  -3085   5112
ATOM   5732  CG  PHE C  62     -19.127  20.667 -76.419  1.00251.43           C  
ANISOU 5732  CG  PHE C  62    30740  41146  23645  -2363  -2984   4938
ATOM   5733  CD1 PHE C  62     -19.549  20.086 -75.235  1.00247.81           C  
ANISOU 5733  CD1 PHE C  62    30093  40580  23485  -2126  -3003   4611
ATOM   5734  CD2 PHE C  62     -17.881  21.270 -76.457  1.00254.75           C  
ANISOU 5734  CD2 PHE C  62    31253  41632  23910  -2755  -2872   5103
ATOM   5735  CE1 PHE C  62     -18.743  20.104 -74.112  1.00247.41           C  
ANISOU 5735  CE1 PHE C  62    29960  40477  23569  -2239  -2928   4436
ATOM   5736  CE2 PHE C  62     -17.070  21.291 -75.339  1.00254.18           C  
ANISOU 5736  CE2 PHE C  62    31078  41525  23975  -2896  -2804   4928
ATOM   5737  CZ  PHE C  62     -17.502  20.707 -74.165  1.00250.59           C  
ANISOU 5737  CZ  PHE C  62    30449  40952  23812  -2618  -2841   4586
ATOM   5738  N   ARG C  63     -22.031  18.504 -79.386  1.00253.18           N  
ANISOU 5738  N   ARG C  63    30792  41690  23714  -1779  -3178   4737
ATOM   5739  CA  ARG C  63     -23.056  18.354 -80.409  1.00253.38           C  
ANISOU 5739  CA  ARG C  63    30897  41759  23615  -1587  -3334   4829
ATOM   5740  C   ARG C  63     -24.360  19.060 -80.055  1.00254.51           C  
ANISOU 5740  C   ARG C  63    31169  41690  23845  -1240  -3597   4993
ATOM   5741  O   ARG C  63     -25.369  18.851 -80.736  1.00255.02           O  
ANISOU 5741  O   ARG C  63    31252  41787  23855  -1039  -3756   5016
ATOM   5742  CB  ARG C  63     -23.323  16.870 -80.670  1.00249.22           C  
ANISOU 5742  CB  ARG C  63    30099  41390  23205  -1554  -3257   4459
ATOM   5743  N   GLU C  64     -24.367  19.886 -79.007  1.00257.00           N  
ANISOU 5743  N   GLU C  64    31566  41795  24288  -1153  -3662   5097
ATOM   5744  CA  GLU C  64     -25.581  20.567 -78.577  1.00258.16           C  
ANISOU 5744  CA  GLU C  64    31815  41743  24531   -789  -3919   5228
ATOM   5745  C   GLU C  64     -25.401  22.049 -78.282  1.00263.14           C  
ANISOU 5745  C   GLU C  64    32789  42123  25071   -733  -4064   5600
ATOM   5746  O   GLU C  64     -26.409  22.748 -78.131  1.00265.92           O  
ANISOU 5746  O   GLU C  64    33283  42299  25455   -398  -4316   5755
ATOM   5747  CB  GLU C  64     -26.168  19.886 -77.330  1.00253.23           C  
ANISOU 5747  CB  GLU C  64    30892  41080  24243   -606  -3896   4899
ATOM   5748  CG  GLU C  64     -26.747  18.500 -77.584  1.00250.08           C  
ANISOU 5748  CG  GLU C  64    30201  40859  23961   -584  -3826   4581
ATOM   5749  CD  GLU C  64     -25.693  17.411 -77.597  1.00247.25           C  
ANISOU 5749  CD  GLU C  64    29664  40642  23638   -879  -3560   4302
ATOM   5750  OE1 GLU C  64     -24.510  17.722 -77.345  1.00248.09           O  
ANISOU 5750  OE1 GLU C  64    29831  40739  23690  -1103  -3421   4332
ATOM   5751  OE2 GLU C  64     -26.049  16.243 -77.861  1.00244.91           O1-
ANISOU 5751  OE2 GLU C  64    29172  40460  23424   -883  -3502   4054
ATOM   5752  N   ILE C  65     -24.177  22.552 -78.202  1.00255.74           N  
ANISOU 5752  N   ILE C  65    31991  41153  24024  -1048  -3929   5751
ATOM   5753  CA  ILE C  65     -23.916  23.956 -77.892  1.00260.64           C  
ANISOU 5753  CA  ILE C  65    32971  41494  24568  -1045  -4066   6128
ATOM   5754  C   ILE C  65     -23.561  24.670 -79.187  1.00265.54           C  
ANISOU 5754  C   ILE C  65    33946  42102  24845  -1236  -4089   6525
ATOM   5755  O   ILE C  65     -22.615  24.250 -79.873  1.00265.77           O  
ANISOU 5755  O   ILE C  65    33918  42356  24707  -1604  -3864   6509
ATOM   5756  CB  ILE C  65     -22.794  24.107 -76.854  1.00260.29           C  
ANISOU 5756  CB  ILE C  65    32867  41392  24638  -1304  -3916   6059
ATOM   5757  CG1 ILE C  65     -23.201  23.463 -75.529  1.00256.32           C  
ANISOU 5757  CG1 ILE C  65    32061  40868  24461  -1074  -3905   5678
ATOM   5758  CG2 ILE C  65     -22.456  25.576 -76.652  1.00265.16           C  
ANISOU 5758  CG2 ILE C  65    33899  41688  25161  -1361  -4067   6494
ATOM   5759  CD1 ILE C  65     -22.066  23.343 -74.536  1.00254.75           C  
ANISOU 5759  CD1 ILE C  65    31753  40667  24373  -1325  -3743   5515
ATOM   5760  N   PRO C  66     -24.268  25.740 -79.561  1.00261.09           N  
ANISOU 5760  N   PRO C  66    33759  41282  24162   -993  -4352   6879
ATOM   5761  CA  PRO C  66     -23.922  26.461 -80.793  1.00266.68           C  
ANISOU 5761  CA  PRO C  66    34859  41941  24528  -1178  -4368   7281
ATOM   5762  C   PRO C  66     -22.622  27.238 -80.666  1.00268.62           C  
ANISOU 5762  C   PRO C  66    35335  42060  24668  -1624  -4220   7571
ATOM   5763  O   PRO C  66     -21.988  27.241 -79.606  1.00265.58           O  
ANISOU 5763  O   PRO C  66    34809  41623  24476  -1776  -4132   7455
ATOM   5764  CB  PRO C  66     -25.122  27.392 -81.000  1.00270.83           C  
ANISOU 5764  CB  PRO C  66    35728  42169  25005   -728  -4729   7540
ATOM   5765  CG  PRO C  66     -25.664  27.606 -79.629  1.00268.06           C  
ANISOU 5765  CG  PRO C  66    35256  41624  24973   -415  -4879   7391
ATOM   5766  CD  PRO C  66     -25.448  26.315 -78.893  1.00261.73           C  
ANISOU 5766  CD  PRO C  66    33929  41106  24410   -511  -4653   6913
ATOM   5767  N   SER C  67     -22.219  27.907 -81.747  1.00267.00           N  
ANISOU 5767  N   SER C  67    35496  41799  24155  -1852  -4194   7955
ATOM   5768  CA  SER C  67     -20.939  28.606 -81.757  1.00270.41           C  
ANISOU 5768  CA  SER C  67    36141  42129  24474  -2364  -4021   8250
ATOM   5769  C   SER C  67     -21.039  29.984 -81.113  1.00274.88           C  
ANISOU 5769  C   SER C  67    37142  42177  25123  -2296  -4255   8628
ATOM   5770  O   SER C  67     -20.143  30.386 -80.360  1.00275.58           O  
ANISOU 5770  O   SER C  67    37263  42120  25323  -2628  -4171   8707
ATOM   5771  CB  SER C  67     -20.423  28.723 -83.190  1.00273.97           C  
ANISOU 5771  CB  SER C  67    36803  42736  24559  -2673  -3863   8505
ATOM   5772  OG  SER C  67     -21.265  29.555 -83.969  1.00278.61           O  
ANISOU 5772  OG  SER C  67    37849  43059  24953  -2394  -4111   8858
ATOM   5773  N   HIS C  68     -22.123  30.717 -81.389  1.00277.33           N  
ANISOU 5773  N   HIS C  68    37799  42187  25387  -1857  -4570   8854
ATOM   5774  CA  HIS C  68     -22.306  32.047 -80.818  1.00282.63           C  
ANISOU 5774  CA  HIS C  68    38924  42312  26151  -1722  -4838   9208
ATOM   5775  C   HIS C  68     -22.445  32.025 -79.303  1.00280.07           C  
ANISOU 5775  C   HIS C  68    38392  41843  26180  -1518  -4947   8974
ATOM   5776  O   HIS C  68     -22.483  33.095 -78.685  1.00284.45           O  
ANISOU 5776  O   HIS C  68    39306  41919  26855  -1422  -5174   9233
ATOM   5777  CB  HIS C  68     -23.533  32.724 -81.435  1.00286.86           C  
ANISOU 5777  CB  HIS C  68    39835  42597  26563  -1204  -5174   9427
ATOM   5778  CG  HIS C  68     -24.826  32.037 -81.123  1.00283.37           C  
ANISOU 5778  CG  HIS C  68    39069  42330  26268   -622  -5358   9052
ATOM   5779  ND1 HIS C  68     -25.271  30.934 -81.820  1.00279.79           N  
ANISOU 5779  ND1 HIS C  68    38285  42299  25723   -545  -5261   8759
ATOM   5780  CD2 HIS C  68     -25.769  32.293 -80.185  1.00282.55           C  
ANISOU 5780  CD2 HIS C  68    38916  42028  26410   -110  -5635   8916
ATOM   5781  CE1 HIS C  68     -26.434  30.545 -81.329  1.00276.65           C  
ANISOU 5781  CE1 HIS C  68    37651  41946  25517    -55  -5467   8473
ATOM   5782  NE2 HIS C  68     -26.757  31.351 -80.334  1.00278.17           N  
ANISOU 5782  NE2 HIS C  68    37994  41789  25910    224  -5685   8555
ATOM   5783  N   VAL C  69     -22.525  30.846 -78.694  1.00279.32           N  
ANISOU 5783  N   VAL C  69    37756  42115  26260  -1438  -4803   8491
ATOM   5784  CA  VAL C  69     -22.574  30.698 -77.247  1.00275.96           C  
ANISOU 5784  CA  VAL C  69    37098  41605  26150  -1267  -4861   8230
ATOM   5785  C   VAL C  69     -21.251  30.171 -76.704  1.00273.64           C  
ANISOU 5785  C   VAL C  69    36543  41511  25919  -1781  -4568   8055
ATOM   5786  O   VAL C  69     -20.720  30.694 -75.723  1.00275.89           O  
ANISOU 5786  O   VAL C  69    36923  41542  26360  -1899  -4629   8115
ATOM   5787  CB  VAL C  69     -23.748  29.787 -76.827  1.00270.25           C  
ANISOU 5787  CB  VAL C  69    35973  41103  25606   -758  -4933   7798
ATOM   5788  CG1 VAL C  69     -23.746  29.583 -75.324  1.00266.80           C  
ANISOU 5788  CG1 VAL C  69    35288  40605  25479   -593  -4954   7513
ATOM   5789  CG2 VAL C  69     -25.062  30.375 -77.295  1.00273.51           C  
ANISOU 5789  CG2 VAL C  69    36637  41322  25961   -243  -5255   7959
ATOM   5790  N   LEU C  70     -20.701  29.133 -77.340  1.00270.36           N  
ANISOU 5790  N   LEU C  70    35805  41540  25379  -2077  -4269   7824
ATOM   5791  CA  LEU C  70     -19.421  28.588 -76.900  1.00267.33           C  
ANISOU 5791  CA  LEU C  70    35156  41388  25031  -2549  -3991   7625
ATOM   5792  C   LEU C  70     -18.305  29.616 -77.018  1.00271.53           C  
ANISOU 5792  C   LEU C  70    36045  41685  25440  -3078  -3942   8040
ATOM   5793  O   LEU C  70     -17.388  29.633 -76.188  1.00269.65           O  
ANISOU 5793  O   LEU C  70    35709  41436  25307  -3390  -3852   7954
ATOM   5794  CB  LEU C  70     -19.075  27.333 -77.702  1.00265.17           C  
ANISOU 5794  CB  LEU C  70    34509  41610  24634  -2727  -3707   7315
ATOM   5795  CG  LEU C  70     -17.784  26.621 -77.288  1.00261.94           C  
ANISOU 5795  CG  LEU C  70    33771  41496  24257  -3158  -3419   7031
ATOM   5796  CD1 LEU C  70     -17.888  26.121 -75.856  1.00256.50           C  
ANISOU 5796  CD1 LEU C  70    32808  40779  23873  -2943  -3460   6646
ATOM   5797  CD2 LEU C  70     -17.457  25.478 -78.234  1.00260.82           C  
ANISOU 5797  CD2 LEU C  70    33322  41801  23977  -3300  -3172   6766
ATOM   5798  N   SER C  71     -18.362  30.480 -78.036  1.00266.89           N  
ANISOU 5798  N   SER C  71    35886  40889  24630  -3203  -4002   8490
ATOM   5799  CA  SER C  71     -17.372  31.547 -78.148  1.00272.94           C  
ANISOU 5799  CA  SER C  71    37050  41343  25310  -3732  -3965   8923
ATOM   5800  C   SER C  71     -17.431  32.478 -76.943  1.00275.71           C  
ANISOU 5800  C   SER C  71    37683  41157  25917  -3635  -4245   9077
ATOM   5801  O   SER C  71     -16.392  32.861 -76.390  1.00277.62           O  
ANISOU 5801  O   SER C  71    38008  41248  26228  -4108  -4172   9176
ATOM   5802  CB  SER C  71     -17.587  32.329 -79.444  1.00278.18           C  
ANISOU 5802  CB  SER C  71    38173  41819  25706  -3808  -4007   9377
ATOM   5803  OG  SER C  71     -18.823  33.021 -79.425  1.00280.18           O  
ANISOU 5803  OG  SER C  71    38766  41679  26012  -3249  -4372   9557
ATOM   5804  N   LYS C  72     -18.642  32.844 -76.514  1.00274.80           N  
ANISOU 5804  N   LYS C  72    37713  40747  25950  -3015  -4578   9081
ATOM   5805  CA  LYS C  72     -18.783  33.704 -75.344  1.00277.21           C  
ANISOU 5805  CA  LYS C  72    38287  40519  26520  -2833  -4883   9188
ATOM   5806  C   LYS C  72     -18.347  32.989 -74.073  1.00272.52           C  
ANISOU 5806  C   LYS C  72    37251  40053  26243  -2809  -4748   8665
ATOM   5807  O   LYS C  72     -17.791  33.616 -73.164  1.00274.52           O  
ANISOU 5807  O   LYS C  72    37646  39798  26863  -2890  -4760   8538
ATOM   5808  CB  LYS C  72     -20.227  34.184 -75.214  1.00278.54           C  
ANISOU 5808  CB  LYS C  72    38650  40395  26786  -2104  -5242   9230
ATOM   5809  CG  LYS C  72     -20.661  35.139 -76.304  1.00284.21           C  
ANISOU 5809  CG  LYS C  72    39898  40782  27307  -2035  -5403   9675
ATOM   5810  CD  LYS C  72     -22.084  35.598 -76.071  1.00285.10           C  
ANISOU 5810  CD  LYS C  72    40168  40633  27524  -1270  -5774   9665
ATOM   5811  CE  LYS C  72     -22.540  36.543 -77.161  1.00289.91           C  
ANISOU 5811  CE  LYS C  72    41321  40913  27919  -1156  -5954  10087
ATOM   5812  NZ  LYS C  72     -23.934  36.980 -76.919  1.00290.68           N1+
ANISOU 5812  NZ  LYS C  72    41543  40794  28108   -374  -6324  10042
ATOM   5813  N   VAL C  73     -18.602  31.682 -73.983  1.00276.45           N  
ANISOU 5813  N   VAL C  73    37221  41166  26652  -2666  -4608   8297
ATOM   5814  CA  VAL C  73     -18.165  30.930 -72.812  1.00271.80           C  
ANISOU 5814  CA  VAL C  73    36218  40691  26364  -2633  -4453   7759
ATOM   5815  C   VAL C  73     -16.645  30.895 -72.738  1.00273.15           C  
ANISOU 5815  C   VAL C  73    36318  40857  26610  -3260  -4149   7641
ATOM   5816  O   VAL C  73     -16.058  31.046 -71.659  1.00273.40           O  
ANISOU 5816  O   VAL C  73    36287  40585  27009  -3298  -4103   7334
ATOM   5817  CB  VAL C  73     -18.761  29.511 -72.830  1.00264.29           C  
ANISOU 5817  CB  VAL C  73    34748  40328  25341  -2358  -4338   7354
ATOM   5818  CG1 VAL C  73     -18.210  28.701 -71.672  1.00260.02           C  
ANISOU 5818  CG1 VAL C  73    33828  39970  24996  -2395  -4208   6884
ATOM   5819  CG2 VAL C  73     -20.277  29.569 -72.764  1.00263.61           C  
ANISOU 5819  CG2 VAL C  73    34675  40122  25362  -1696  -4566   7303
ATOM   5820  N   CYS C  74     -15.982  30.703 -73.880  1.00270.20           N  
ANISOU 5820  N   CYS C  74    35943  40837  25883  -3752  -3940   7872
ATOM   5821  CA  CYS C  74     -14.524  30.668 -73.893  1.00271.45           C  
ANISOU 5821  CA  CYS C  74    35991  41057  26088  -4369  -3633   7767
ATOM   5822  C   CYS C  74     -13.940  32.040 -73.571  1.00278.03           C  
ANISOU 5822  C   CYS C  74    37267  41175  27194  -4640  -3705   8015
ATOM   5823  O   CYS C  74     -13.002  32.156 -72.768  1.00278.75           O  
ANISOU 5823  O   CYS C  74    37249  41060  27604  -4893  -3585   7738
ATOM   5824  CB  CYS C  74     -14.033  30.166 -75.250  1.00270.90           C  
ANISOU 5824  CB  CYS C  74    35821  41571  25536  -4801  -3390   7977
ATOM   5825  SG  CYS C  74     -14.466  28.450 -75.621  1.00262.27           S  
ANISOU 5825  SG  CYS C  74    34150  41195  24303  -4505  -3227   7480
ATOM   5826  N   MET C  75     -14.486  33.096 -74.186  1.00270.41           N  
ANISOU 5826  N   MET C  75    36825  39808  26111  -4586  -3926   8533
ATOM   5827  CA  MET C  75     -14.062  34.447 -73.833  1.00275.25           C  
ANISOU 5827  CA  MET C  75    37922  39661  27000  -4791  -4058   8780
ATOM   5828  C   MET C  75     -14.312  34.742 -72.360  1.00272.51           C  
ANISOU 5828  C   MET C  75    37577  38817  27150  -4373  -4261   8415
ATOM   5829  O   MET C  75     -13.608  35.565 -71.764  1.00274.93           O  
ANISOU 5829  O   MET C  75    38113  38572  27775  -4619  -4296   8408
ATOM   5830  CB  MET C  75     -14.774  35.480 -74.708  1.00281.40           C  
ANISOU 5830  CB  MET C  75    39300  40070  27551  -4698  -4319   9385
ATOM   5831  CG  MET C  75     -14.383  35.445 -76.177  1.00285.57           C  
ANISOU 5831  CG  MET C  75    39951  40969  27583  -5191  -4120   9822
ATOM   5832  SD  MET C  75     -15.161  36.763 -77.134  1.00293.43           S  
ANISOU 5832  SD  MET C  75    41738  41431  28320  -5085  -4460  10550
ATOM   5833  CE  MET C  75     -16.847  36.170 -77.241  1.00290.14           C  
ANISOU 5833  CE  MET C  75    41174  41294  27773  -4202  -4754  10417
ATOM   5834  N   TYR C  76     -15.305  34.085 -71.758  1.00277.95           N  
ANISOU 5834  N   TYR C  76    38010  39694  27902  -3749  -4396   8111
ATOM   5835  CA  TYR C  76     -15.510  34.218 -70.320  1.00277.60           C  
ANISOU 5835  CA  TYR C  76    37910  39270  28294  -3342  -4543   7716
ATOM   5836  C   TYR C  76     -14.438  33.469 -69.539  1.00274.71           C  
ANISOU 5836  C   TYR C  76    37118  39118  28141  -3625  -4274   7216
ATOM   5837  O   TYR C  76     -13.997  33.932 -68.481  1.00278.08           O  
ANISOU 5837  O   TYR C  76    37624  39083  28950  -3595  -4342   6975
ATOM   5838  CB  TYR C  76     -16.901  33.716 -69.934  1.00273.63           C  
ANISOU 5838  CB  TYR C  76    37241  38955  27772  -2616  -4739   7553
ATOM   5839  CG  TYR C  76     -17.186  33.829 -68.455  1.00272.99           C  
ANISOU 5839  CG  TYR C  76    37100  38526  28098  -2158  -4876   7151
ATOM   5840  CD1 TYR C  76     -17.482  35.056 -67.877  1.00279.72           C  
ANISOU 5840  CD1 TYR C  76    38412  38655  29214  -1884  -5170   7276
ATOM   5841  CD2 TYR C  76     -17.148  32.710 -67.634  1.00266.15           C  
ANISOU 5841  CD2 TYR C  76    35745  38045  27337  -1993  -4719   6643
ATOM   5842  CE1 TYR C  76     -17.739  35.164 -66.524  1.00279.71           C  
ANISOU 5842  CE1 TYR C  76    38366  38353  29559  -1444  -5292   6898
ATOM   5843  CE2 TYR C  76     -17.402  32.808 -66.281  1.00265.07           C  
ANISOU 5843  CE2 TYR C  76    35571  37604  27540  -1573  -4830   6284
ATOM   5844  CZ  TYR C  76     -17.697  34.037 -65.732  1.00272.38           C  
ANISOU 5844  CZ  TYR C  76    36940  37840  28713  -1293  -5110   6408
ATOM   5845  OH  TYR C  76     -17.951  34.140 -64.385  1.00272.08           O  
ANISOU 5845  OH  TYR C  76    36874  37516  28988   -852  -5219   6039
ATOM   5846  N   PHE C  77     -14.015  32.304 -70.038  1.00275.28           N  
ANISOU 5846  N   PHE C  77    36747  39882  27964  -3873  -3990   7036
ATOM   5847  CA  PHE C  77     -12.927  31.573 -69.396  1.00272.50           C  
ANISOU 5847  CA  PHE C  77    35997  39762  27780  -4156  -3741   6564
ATOM   5848  C   PHE C  77     -11.654  32.408 -69.360  1.00278.10           C  
ANISOU 5848  C   PHE C  77    36887  40101  28678  -4746  -3637   6658
ATOM   5849  O   PHE C  77     -11.029  32.561 -68.304  1.00279.62           O  
ANISOU 5849  O   PHE C  77    37014  39993  29238  -4778  -3645   6314
ATOM   5850  CB  PHE C  77     -12.671  30.248 -70.117  1.00267.88           C  
ANISOU 5850  CB  PHE C  77    34958  39979  26844  -4340  -3474   6404
ATOM   5851  CG  PHE C  77     -13.743  29.215 -69.906  1.00263.37           C  
ANISOU 5851  CG  PHE C  77    34111  39797  26161  -3809  -3552   6173
ATOM   5852  CD1 PHE C  77     -14.679  29.359 -68.896  1.00263.10           C  
ANISOU 5852  CD1 PHE C  77    34133  39452  26380  -3236  -3783   6012
ATOM   5853  CD2 PHE C  77     -13.799  28.088 -70.710  1.00259.68           C  
ANISOU 5853  CD2 PHE C  77    33320  40015  25330  -3894  -3391   6107
ATOM   5854  CE1 PHE C  77     -15.660  28.402 -68.699  1.00258.35           C  
ANISOU 5854  CE1 PHE C  77    33256  39226  25680  -2793  -3836   5810
ATOM   5855  CE2 PHE C  77     -14.775  27.129 -70.518  1.00255.15           C  
ANISOU 5855  CE2 PHE C  77    32496  39784  24667  -3448  -3473   5898
ATOM   5856  CZ  PHE C  77     -15.707  27.286 -69.512  1.00254.06           C  
ANISOU 5856  CZ  PHE C  77    32400  39340  24792  -2915  -3687   5758
ATOM   5857  N   THR C  78     -11.264  32.969 -70.510  1.00268.84           N  
ANISOU 5857  N   THR C  78    35952  38943  27251  -5226  -3544   7128
ATOM   5858  CA  THR C  78      -9.978  33.658 -70.608  1.00273.67           C  
ANISOU 5858  CA  THR C  78    36674  39305  28001  -5887  -3391   7233
ATOM   5859  C   THR C  78      -9.829  34.751 -69.553  1.00277.45           C  
ANISOU 5859  C   THR C  78    37499  38966  28952  -5808  -3636   7185
ATOM   5860  O   THR C  78      -8.745  34.931 -68.984  1.00279.05           O  
ANISOU 5860  O   THR C  78    37586  39004  29437  -6187  -3531   6946
ATOM   5861  CB  THR C  78      -9.802  34.248 -72.008  1.00278.46           C  
ANISOU 5861  CB  THR C  78    37589  39970  28243  -6357  -3296   7833
ATOM   5862  OG1 THR C  78     -10.842  35.201 -72.263  1.00281.77           O  
ANISOU 5862  OG1 THR C  78    38562  39877  28621  -6026  -3625   8276
ATOM   5863  CG2 THR C  78      -9.855  33.150 -73.060  1.00274.95           C  
ANISOU 5863  CG2 THR C  78    36797  40357  27315  -6449  -3046   7850
ATOM   5864  N   TYR C  79     -10.909  35.484 -69.270  1.00274.40           N  
ANISOU 5864  N   TYR C  79    37531  38069  28660  -5301  -3981   7386
ATOM   5865  CA  TYR C  79     -10.828  36.589 -68.319  1.00281.42           C  
ANISOU 5865  CA  TYR C  79    38809  38144  29973  -5188  -4252   7360
ATOM   5866  C   TYR C  79     -10.460  36.096 -66.924  1.00278.07           C  
ANISOU 5866  C   TYR C  79    38056  37676  29920  -4961  -4246   6737
ATOM   5867  O   TYR C  79      -9.395  36.430 -66.392  1.00281.81           O  
ANISOU 5867  O   TYR C  79    38505  37887  30683  -5351  -4188   6549
ATOM   5868  CB  TYR C  79     -12.151  37.355 -68.276  1.00284.18           C  
ANISOU 5868  CB  TYR C  79    39631  38026  30316  -4587  -4634   7644
ATOM   5869  CG  TYR C  79     -12.114  38.543 -67.340  1.00291.85           C  
ANISOU 5869  CG  TYR C  79    41058  38130  31702  -4431  -4948   7627
ATOM   5870  CD1 TYR C  79     -11.495  39.728 -67.716  1.00301.08           C  
ANISOU 5870  CD1 TYR C  79    42721  38714  32961  -4925  -5042   8018
ATOM   5871  CD2 TYR C  79     -12.667  38.470 -66.067  1.00290.18           C  
ANISOU 5871  CD2 TYR C  79    40787  37683  31785  -3805  -5148   7213
ATOM   5872  CE1 TYR C  79     -11.448  40.814 -66.862  1.00308.29           C  
ANISOU 5872  CE1 TYR C  79    44075  38803  34257  -4785  -5359   7989
ATOM   5873  CE2 TYR C  79     -12.621  39.551 -65.205  1.00297.16           C  
ANISOU 5873  CE2 TYR C  79    42097  37775  33035  -3637  -5450   7172
ATOM   5874  CZ  TYR C  79     -12.013  40.720 -65.608  1.00306.17           C  
ANISOU 5874  CZ  TYR C  79    43740  38319  34271  -4123  -5568   7554
ATOM   5875  OH  TYR C  79     -11.967  41.797 -64.752  1.00312.85           O  
ANISOU 5875  OH  TYR C  79    45037  38348  35485  -3952  -5899   7502
ATOM   5876  N   LYS C  80     -11.334  35.294 -66.313  1.00279.91           N  
ANISOU 5876  N   LYS C  80    38037  38170  30146  -4337  -4309   6412
ATOM   5877  CA  LYS C  80     -11.104  34.869 -64.938  1.00275.92           C  
ANISOU 5877  CA  LYS C  80    37286  37579  29972  -4053  -4333   5842
ATOM   5878  C   LYS C  80      -9.993  33.837 -64.811  1.00271.04           C  
ANISOU 5878  C   LYS C  80    36150  37484  29348  -4443  -4015   5438
ATOM   5879  O   LYS C  80      -9.579  33.539 -63.685  1.00269.18           O  
ANISOU 5879  O   LYS C  80    35733  37148  29395  -4298  -4028   4962
ATOM   5880  CB  LYS C  80     -12.400  34.338 -64.322  1.00269.72           C  
ANISOU 5880  CB  LYS C  80    36399  36919  29162  -3284  -4483   5641
ATOM   5881  CG  LYS C  80     -13.431  35.430 -64.073  1.00274.46           C  
ANISOU 5881  CG  LYS C  80    37493  36918  29872  -2793  -4843   5901
ATOM   5882  CD  LYS C  80     -14.686  34.896 -63.405  1.00269.28           C  
ANISOU 5882  CD  LYS C  80    36680  36432  29203  -2041  -4965   5672
ATOM   5883  CE  LYS C  80     -15.688  36.015 -63.166  1.00274.11           C  
ANISOU 5883  CE  LYS C  80    37767  36465  29916  -1524  -5330   5908
ATOM   5884  NZ  LYS C  80     -16.935  35.524 -62.518  1.00269.45           N1+
ANISOU 5884  NZ  LYS C  80    36990  36081  29309   -790  -5433   5686
ATOM   5885  N   VAL C  81      -9.500  33.285 -65.921  1.00273.97           N  
ANISOU 5885  N   VAL C  81    36288  38413  29395  -4904  -3743   5599
ATOM   5886  CA  VAL C  81      -8.234  32.564 -65.863  1.00271.35           C  
ANISOU 5886  CA  VAL C  81    35523  38491  29087  -5364  -3457   5250
ATOM   5887  C   VAL C  81      -7.072  33.545 -65.786  1.00279.89           C  
ANISOU 5887  C   VAL C  81    36779  39138  30427  -5950  -3433   5343
ATOM   5888  O   VAL C  81      -6.120  33.340 -65.024  1.00279.56           O  
ANISOU 5888  O   VAL C  81    36490  39076  30652  -6132  -3363   4921
ATOM   5889  CB  VAL C  81      -8.093  31.611 -67.063  1.00266.96           C  
ANISOU 5889  CB  VAL C  81    34642  38711  28079  -5628  -3172   5357
ATOM   5890  CG1 VAL C  81      -6.709  30.986 -67.082  1.00265.29           C  
ANISOU 5890  CG1 VAL C  81    34001  38914  27884  -6128  -2881   5017
ATOM   5891  CG2 VAL C  81      -9.141  30.524 -66.991  1.00258.90           C  
ANISOU 5891  CG2 VAL C  81    33395  38120  26853  -5072  -3204   5173
ATOM   5892  N   ARG C  82      -7.137  34.630 -66.559  1.00267.92           N  
ANISOU 5892  N   ARG C  82    35701  37256  28841  -6256  -3507   5894
ATOM   5893  CA  ARG C  82      -6.067  35.622 -66.545  1.00276.97           C  
ANISOU 5893  CA  ARG C  82    37047  37958  30230  -6867  -3493   6035
ATOM   5894  C   ARG C  82      -6.219  36.590 -65.375  1.00282.07           C  
ANISOU 5894  C   ARG C  82    38071  37771  31334  -6592  -3841   5915
ATOM   5895  O   ARG C  82      -5.343  36.677 -64.508  1.00283.44           O  
ANISOU 5895  O   ARG C  82    38097  37743  31853  -6767  -3848   5535
ATOM   5896  CB  ARG C  82      -6.041  36.377 -67.880  1.00282.71           C  
ANISOU 5896  CB  ARG C  82    38123  38625  30669  -7349  -3424   6698
ATOM   5897  CG  ARG C  82      -4.874  37.346 -68.052  1.00291.56           C  
ANISOU 5897  CG  ARG C  82    39426  39367  31988  -8104  -3353   6905
ATOM   5898  CD  ARG C  82      -5.242  38.763 -67.626  1.00299.76           C  
ANISOU 5898  CD  ARG C  82    41127  39449  33321  -8014  -3733   7199
ATOM   5899  NE  ARG C  82      -4.182  39.722 -67.924  1.00308.88           N  
ANISOU 5899  NE  ARG C  82    42500  40227  34633  -8795  -3671   7473
ATOM   5900  CZ  ARG C  82      -4.177  40.982 -67.501  1.00317.06           C  
ANISOU 5900  CZ  ARG C  82    44089  40396  35984  -8877  -3985   7681
ATOM   5901  NH1 ARG C  82      -5.177  41.439 -66.759  1.00317.82           N  
ANISOU 5901  NH1 ARG C  82    44571  39928  36260  -8184  -4383   7629
ATOM   5902  NH2 ARG C  82      -3.172  41.787 -67.820  1.00324.34           N1+
ANISOU 5902  NH2 ARG C  82    45177  41017  37038  -9654  -3905   7935
ATOM   5903  N   TYR C  83      -7.330  37.323 -65.334  1.00281.05           N  
ANISOU 5903  N   TYR C  83    38427  37154  31204  -6135  -4149   6215
ATOM   5904  CA  TYR C  83      -7.524  38.412 -64.377  1.00287.11           C  
ANISOU 5904  CA  TYR C  83    39650  37073  32367  -5879  -4511   6182
ATOM   5905  C   TYR C  83      -8.327  37.899 -63.186  1.00281.00           C  
ANISOU 5905  C   TYR C  83    38747  36272  31747  -5084  -4684   5719
ATOM   5906  O   TYR C  83      -9.558  37.840 -63.230  1.00278.91           O  
ANISOU 5906  O   TYR C  83    38625  36018  31331  -4496  -4840   5841
ATOM   5907  CB  TYR C  83      -8.216  39.596 -65.044  1.00294.25           C  
ANISOU 5907  CB  TYR C  83    41202  37425  33175  -5848  -4768   6786
ATOM   5908  N   THR C  84      -7.623  37.533 -62.117  1.00281.35           N  
ANISOU 5908  N   THR C  84    38518  36295  32087  -5070  -4654   5185
ATOM   5909  CA  THR C  84      -8.256  37.187 -60.853  1.00276.75           C  
ANISOU 5909  CA  THR C  84    37873  35592  31686  -4358  -4829   4737
ATOM   5910  C   THR C  84      -7.272  37.468 -59.726  1.00277.01           C  
ANISOU 5910  C   THR C  84    37877  35238  32135  -4493  -4916   4301
ATOM   5911  O   THR C  84      -6.083  37.153 -59.835  1.00277.30           O  
ANISOU 5911  O   THR C  84    37607  35512  32244  -5053  -4707   4121
ATOM   5912  CB  THR C  84      -8.728  35.722 -60.828  1.00270.07           C  
ANISOU 5912  CB  THR C  84    36522  35509  30582  -4023  -4612   4447
ATOM   5913  OG1 THR C  84      -9.457  35.471 -59.620  1.00266.24           O  
ANISOU 5913  OG1 THR C  84    36032  34877  30249  -3320  -4784   4075
ATOM   5914  CG2 THR C  84      -7.558  34.749 -60.939  1.00267.54           C  
ANISOU 5914  CG2 THR C  84    35684  35748  30220  -4497  -4294   4119
ATOM   5915  N   ASN C  85      -7.774  38.097 -58.660  1.00276.40           N  
ANISOU 5915  N   ASN C  85    38127  34567  32327  -3969  -5238   4128
ATOM   5916  CA  ASN C  85      -6.952  38.501 -57.515  1.00279.50           C  
ANISOU 5916  CA  ASN C  85    38576  34493  33129  -4017  -5394   3716
ATOM   5917  C   ASN C  85      -5.772  39.371 -57.947  1.00287.93           C  
ANISOU 5917  C   ASN C  85    39806  35196  34398  -4807  -5399   3919
ATOM   5918  O   ASN C  85      -4.715  39.369 -57.312  1.00288.92           O  
ANISOU 5918  O   ASN C  85    39759  35211  34806  -5107  -5391   3555
ATOM   5919  CB  ASN C  85      -6.464  37.282 -56.728  1.00271.06           C  
ANISOU 5919  CB  ASN C  85    36977  33919  32093  -3886  -5209   3117
ATOM   5920  CG  ASN C  85      -7.582  36.586 -55.979  1.00264.87           C  
ANISOU 5920  CG  ASN C  85    36110  33328  31200  -3081  -5263   2859
ATOM   5921  OD1 ASN C  85      -8.445  37.234 -55.387  1.00268.08           O  
ANISOU 5921  OD1 ASN C  85    36883  33271  31705  -2535  -5536   2895
ATOM   5922  ND2 ASN C  85      -7.573  35.258 -56.002  1.00256.01           N  
ANISOU 5922  ND2 ASN C  85    34508  32897  29866  -3006  -5004   2595
ATOM   5923  N   SER C  86      -5.947  40.123 -59.030  1.00279.96           N  
ANISOU 5923  N   SER C  86    39131  34000  33240  -5158  -5417   4505
ATOM   5924  CA  SER C  86      -4.901  40.965 -59.583  1.00286.32           C  
ANISOU 5924  CA  SER C  86    40115  34484  34190  -5965  -5394   4786
ATOM   5925  C   SER C  86      -5.053  42.394 -59.062  1.00291.90           C  
ANISOU 5925  C   SER C  86    41482  34204  35221  -5870  -5825   4943
ATOM   5926  O   SER C  86      -5.851  42.672 -58.161  1.00290.48           O  
ANISOU 5926  O   SER C  86    41567  33624  35177  -5162  -6129   4749
ATOM   5927  CB  SER C  86      -4.936  40.909 -61.112  1.00288.97           C  
ANISOU 5927  CB  SER C  86    40443  35216  34137  -6451  -5139   5348
ATOM   5928  OG  SER C  86      -6.127  41.485 -61.618  1.00290.99           O  
ANISOU 5928  OG  SER C  86    41182  35189  34194  -6062  -5349   5806
ATOM   5929  N   SER C  87      -4.278  43.314 -59.632  1.00290.55           N  
ANISOU 5929  N   SER C  87    41589  33635  35170  -6593  -5853   5297
ATOM   5930  CA  SER C  87      -4.263  44.718 -59.224  1.00299.05           C  
ANISOU 5930  CA  SER C  87    43324  33731  36569  -6630  -6270   5471
ATOM   5931  C   SER C  87      -4.782  45.563 -60.385  1.00304.87           C  
ANISOU 5931  C   SER C  87    44600  34169  37069  -6852  -6355   6190
ATOM   5932  O   SER C  87      -4.019  45.962 -61.268  1.00309.29           O  
ANISOU 5932  O   SER C  87    45229  34714  37574  -7658  -6193   6573
ATOM   5933  CB  SER C  87      -2.858  45.147 -58.802  1.00303.05           C  
ANISOU 5933  CB  SER C  87    43742  33937  37466  -7324  -6279   5254
ATOM   5934  OG  SER C  87      -1.965  45.119 -59.903  1.00304.34           O  
ANISOU 5934  OG  SER C  87    43700  34446  37489  -8227  -5944   5594
ATOM   5935  N   THR C  88      -6.085  45.832 -60.381  1.00305.27           N  
ANISOU 5935  N   THR C  88    45030  33994  36965  -6130  -6610   6369
ATOM   5936  CA ATHR C  88      -6.711  46.648 -61.413  0.50308.49           C  
ANISOU 5936  CA ATHR C  88    46003  34076  37135  -6209  -6755   7029
ATOM   5937  CA BTHR C  88      -6.711  46.648 -61.413  0.50308.49           C  
ANISOU 5937  CA BTHR C  88    46003  34076  37135  -6209  -6755   7029
ATOM   5938  C   THR C  88      -8.181  46.815 -61.057  1.00306.18           C  
ANISOU 5938  C   THR C  88    46023  33570  36743  -5229  -7077   7029
ATOM   5939  O   THR C  88      -8.737  46.044 -60.268  1.00301.00           O  
ANISOU 5939  O   THR C  88    45018  33254  36095  -4571  -7058   6577
ATOM   5940  N   GLU C  89      -8.803  47.833 -61.648  1.00308.60           N  
ANISOU 5940  N   GLU C  89    46992  33314  36947  -5141  -7376   7543
ATOM   5941  CA  GLU C  89     -10.222  48.100 -61.434  1.00307.07           C  
ANISOU 5941  CA  GLU C  89    47127  32906  36639  -4220  -7706   7592
ATOM   5942  C   GLU C  89     -11.033  47.141 -62.298  1.00302.09           C  
ANISOU 5942  C   GLU C  89    46129  33101  35550  -3972  -7439   7760
ATOM   5943  O   GLU C  89     -10.977  47.206 -63.530  1.00303.60           O  
ANISOU 5943  O   GLU C  89    46432  33491  35433  -4419  -7292   8261
ATOM   5944  CB  GLU C  89     -10.546  49.555 -61.758  1.00313.32           C  
ANISOU 5944  CB  GLU C  89    48789  32769  37491  -4211  -8156   8066
ATOM   5945  CG  GLU C  89      -9.909  50.556 -60.803  1.00318.50           C  
ANISOU 5945  CG  GLU C  89    49870  32529  38617  -4331  -8504   7867
ATOM   5946  CD  GLU C  89     -10.232  51.994 -61.160  1.00326.13           C  
ANISOU 5946  CD  GLU C  89    51744  32541  39631  -4332  -8975   8350
ATOM   5947  OE1 GLU C  89     -10.848  52.221 -62.222  1.00325.26           O  
ANISOU 5947  OE1 GLU C  89    51931  32478  39175  -4319  -9003   8872
ATOM   5948  OE2 GLU C  89      -9.867  52.897 -60.378  1.00332.37           O1-
ANISOU 5948  OE2 GLU C  89    52972  32515  40797  -4334  -9337   8202
ATOM   5949  N   ILE C  90     -11.785  46.253 -61.654  1.00311.92           N  
ANISOU 5949  N   ILE C  90    46948  34824  36743  -3272  -7381   7345
ATOM   5950  CA  ILE C  90     -12.509  45.183 -62.339  1.00307.25           C  
ANISOU 5950  CA  ILE C  90    45913  35075  35754  -3039  -7114   7407
ATOM   5951  C   ILE C  90     -13.651  45.764 -63.165  1.00311.05           C  
ANISOU 5951  C   ILE C  90    46850  35380  35954  -2654  -7370   7896
ATOM   5952  O   ILE C  90     -14.540  46.429 -62.613  1.00312.83           O  
ANISOU 5952  O   ILE C  90    47455  35119  36286  -1963  -7759   7857
ATOM   5953  CB  ILE C  90     -13.033  44.143 -61.336  1.00299.80           C  
ANISOU 5953  CB  ILE C  90    44434  34617  34858  -2393  -7016   6831
ATOM   5954  CG1 ILE C  90     -11.867  43.470 -60.609  1.00295.98           C  
ANISOU 5954  CG1 ILE C  90    43485  34368  34606  -2788  -6752   6352
ATOM   5955  CG2 ILE C  90     -13.893  43.107 -62.042  1.00295.57           C  
ANISOU 5955  CG2 ILE C  90    43491  34889  33924  -2124  -6796   6915
ATOM   5956  CD1 ILE C  90     -12.291  42.628 -59.426  1.00289.54           C  
ANISOU 5956  CD1 ILE C  90    42265  33855  33893  -2153  -6716   5768
ATOM   5957  N   PRO C  91     -13.670  45.545 -64.474  1.00315.03           N  
ANISOU 5957  N   PRO C  91    47339  36269  36089  -3048  -7178   8347
ATOM   5958  CA  PRO C  91     -14.768  46.038 -65.311  1.00314.93           C  
ANISOU 5958  CA  PRO C  91    47747  36134  35778  -2667  -7429   8807
ATOM   5959  C   PRO C  91     -15.965  45.092 -65.256  1.00306.51           C  
ANISOU 5959  C   PRO C  91    46246  35725  34490  -1938  -7384   8600
ATOM   5960  O   PRO C  91     -15.985  44.109 -64.516  1.00300.45           O  
ANISOU 5960  O   PRO C  91    44904  35447  33808  -1710  -7178   8112
ATOM   5961  CB  PRO C  91     -14.149  46.074 -66.709  1.00315.80           C  
ANISOU 5961  CB  PRO C  91    47959  36460  35572  -3460  -7188   9335
ATOM   5962  CG  PRO C  91     -13.116  45.000 -66.675  1.00312.34           C  
ANISOU 5962  CG  PRO C  91    46846  36691  35138  -4023  -6704   9035
ATOM   5963  CD  PRO C  91     -12.562  45.001 -65.278  1.00314.37           C  
ANISOU 5963  CD  PRO C  91    46929  36664  35853  -3924  -6751   8485
ATOM   5964  N   GLU C  92     -16.973  45.408 -66.065  1.00314.12           N  
ANISOU 5964  N   GLU C  92    47504  36686  35160  -1584  -7592   8986
ATOM   5965  CA  GLU C  92     -18.189  44.619 -66.170  1.00306.35           C  
ANISOU 5965  CA  GLU C  92    46151  36305  33945   -918  -7590   8862
ATOM   5966  C   GLU C  92     -18.075  43.644 -67.344  1.00301.84           C  
ANISOU 5966  C   GLU C  92    45184  36531  32969  -1332  -7232   9070
ATOM   5967  O   GLU C  92     -17.007  43.477 -67.942  1.00304.07           O  
ANISOU 5967  O   GLU C  92    45402  36963  33167  -2106  -6942   9233
ATOM   5968  CB  GLU C  92     -19.402  45.543 -66.301  1.00307.73           C  
ANISOU 5968  CB  GLU C  92    46857  36015  34052   -215  -8069   9110
ATOM   5969  CG  GLU C  92     -19.711  46.349 -65.044  1.00310.29           C  
ANISOU 5969  CG  GLU C  92    47491  35658  34748    368  -8432   8813
ATOM   5970  CD  GLU C  92     -18.869  47.606 -64.924  1.00318.95           C  
ANISOU 5970  CD  GLU C  92    49268  35831  36088    -51  -8669   9031
ATOM   5971  OE1 GLU C  92     -18.085  47.892 -65.853  1.00322.91           O  
ANISOU 5971  OE1 GLU C  92    50014  36217  36458   -806  -8548   9451
ATOM   5972  OE2 GLU C  92     -18.991  48.307 -63.897  1.00321.51           O1-
ANISOU 5972  OE2 GLU C  92    49887  35545  36728    368  -8977   8780
ATOM   5973  N   PHE C  93     -19.185  42.990 -67.683  1.00307.72           N  
ANISOU 5973  N   PHE C  93    45649  37813  33458   -811  -7253   9052
ATOM   5974  CA  PHE C  93     -19.194  41.941 -68.700  1.00302.36           C  
ANISOU 5974  CA  PHE C  93    44545  37941  32398  -1102  -6937   9170
ATOM   5975  C   PHE C  93     -20.349  42.174 -69.664  1.00302.67           C  
ANISOU 5975  C   PHE C  93    44825  38086  32091   -697  -7186   9558
ATOM   5976  O   PHE C  93     -21.521  42.165 -69.236  1.00301.18           O  
ANISOU 5976  O   PHE C  93    44571  37930  31934     62  -7437   9404
ATOM   5977  CB  PHE C  93     -19.304  40.563 -68.047  1.00294.77           C  
ANISOU 5977  CB  PHE C  93    42831  37685  31481   -914  -6651   8639
ATOM   5978  CG  PHE C  93     -18.118  40.198 -67.209  1.00294.76           C  
ANISOU 5978  CG  PHE C  93    42556  37671  31768  -1336  -6387   8252
ATOM   5979  CD1 PHE C  93     -16.963  39.708 -67.794  1.00293.99           C  
ANISOU 5979  CD1 PHE C  93    42244  37903  31557  -2097  -6032   8304
ATOM   5980  CD2 PHE C  93     -18.154  40.356 -65.834  1.00296.00           C  
ANISOU 5980  CD2 PHE C  93    42670  37499  32299   -952  -6503   7823
ATOM   5981  CE1 PHE C  93     -15.870  39.376 -67.021  1.00293.75           C  
ANISOU 5981  CE1 PHE C  93    41944  37873  31796  -2460  -5812   7925
ATOM   5982  CE2 PHE C  93     -17.065  40.026 -65.057  1.00295.99           C  
ANISOU 5982  CE2 PHE C  93    42427  37477  32558  -1317  -6288   7454
ATOM   5983  CZ  PHE C  93     -15.922  39.535 -65.650  1.00294.71           C  
ANISOU 5983  CZ  PHE C  93    42038  37645  32294  -2069  -5950   7500
ATOM   5984  N   PRO C  94     -20.083  42.379 -70.956  1.00305.44           N  
ANISOU 5984  N   PRO C  94    45444  38513  32097  -1159  -7129  10052
ATOM   5985  CA  PRO C  94     -21.178  42.563 -71.920  1.00305.81           C  
ANISOU 5985  CA  PRO C  94    45722  38686  31786   -766  -7381  10417
ATOM   5986  C   PRO C  94     -21.750  41.223 -72.367  1.00299.30           C  
ANISOU 5986  C   PRO C  94    44257  38782  30682   -602  -7165  10242
ATOM   5987  O   PRO C  94     -21.010  40.298 -72.712  1.00295.48           O  
ANISOU 5987  O   PRO C  94    43355  38850  30065  -1120  -6772  10140
ATOM   5988  CB  PRO C  94     -20.503  43.296 -73.085  1.00310.95           C  
ANISOU 5988  CB  PRO C  94    46933  39041  32174  -1410  -7368  11009
ATOM   5989  CG  PRO C  94     -19.078  42.851 -73.013  1.00310.43           C  
ANISOU 5989  CG  PRO C  94    46587  39168  32195  -2224  -6924  10889
ATOM   5990  CD  PRO C  94     -18.767  42.675 -71.548  1.00308.94           C  
ANISOU 5990  CD  PRO C  94    46093  38807  32481  -2047  -6886  10333
ATOM   5991  N   ILE C  95     -23.077  41.125 -72.358  1.00302.50           N  
ANISOU 5991  N   ILE C  95    44583  39352  31003    129  -7440  10194
ATOM   5992  CA  ILE C  95     -23.795  39.948 -72.835  1.00298.31           C  
ANISOU 5992  CA  ILE C  95    43496  39645  30203    342  -7315  10062
ATOM   5993  C   ILE C  95     -24.908  40.420 -73.760  1.00301.63           C  
ANISOU 5993  C   ILE C  95    44155  40035  30416    835  -7527  10269
ATOM   5994  O   ILE C  95     -25.684  41.310 -73.396  1.00304.42           O  
ANISOU 5994  O   ILE C  95    44832  39917  30918   1416  -7878  10297
ATOM   5995  CB  ILE C  95     -24.373  39.114 -71.674  1.00293.14           C  
ANISOU 5995  CB  ILE C  95    42237  39338  29805    837  -7250   9494
ATOM   5996  CG1 ILE C  95     -23.250  38.571 -70.789  1.00289.70           C  
ANISOU 5996  CG1 ILE C  95    41477  38954  29643    405  -6894   9107
ATOM   5997  CG2 ILE C  95     -25.217  37.969 -72.211  1.00289.17           C  
ANISOU 5997  CG2 ILE C  95    41192  39630  29050   1078  -7141   9352
ATOM   5998  CD1 ILE C  95     -23.738  37.961 -69.491  1.00285.46           C  
ANISOU 5998  CD1 ILE C  95    40474  38597  29391    894  -6859   8567
ATOM   5999  N   ALA C  96     -24.982  39.831 -74.951  1.00296.76           N  
ANISOU 5999  N   ALA C  96    43366  39914  29475    640  -7293  10356
ATOM   6000  CA  ALA C  96     -25.973  40.262 -75.927  1.00301.66           C  
ANISOU 6000  CA  ALA C  96    44219  40519  29880   1082  -7468  10536
ATOM   6001  C   ALA C  96     -27.380  39.931 -75.433  1.00299.69           C  
ANISOU 6001  C   ALA C  96    43607  40534  29729   1920  -7666  10195
ATOM   6002  O   ALA C  96     -27.594  38.880 -74.822  1.00293.64           O  
ANISOU 6002  O   ALA C  96    42260  40249  29060   2027  -7516   9790
ATOM   6003  CB  ALA C  96     -25.728  39.601 -77.281  1.00302.10           C  
ANISOU 6003  CB  ALA C  96    44153  41065  29567    704  -7175  10644
ATOM   6004  N   PRO C  97     -28.360  40.797 -75.693  1.00300.63           N  
ANISOU 6004  N   PRO C  97    44029  40371  29824   2511  -7988  10342
ATOM   6005  CA  PRO C  97     -29.702  40.610 -75.131  1.00297.92           C  
ANISOU 6005  CA  PRO C  97    43315  40281  29601   3321  -8183  10036
ATOM   6006  C   PRO C  97     -30.550  39.561 -75.834  1.00293.79           C  
ANISOU 6006  C   PRO C  97    42353  40435  28838   3571  -8083   9789
ATOM   6007  O   PRO C  97     -31.735  39.440 -75.511  1.00291.87           O  
ANISOU 6007  O   PRO C  97    41830  40416  28653   4244  -8260   9552
ATOM   6008  CB  PRO C  97     -30.329  42.004 -75.290  1.00303.09           C  
ANISOU 6008  CB  PRO C  97    44459  40382  30321   3763  -8551  10332
ATOM   6009  CG  PRO C  97     -29.634  42.588 -76.472  1.00308.03           C  
ANISOU 6009  CG  PRO C  97    45658  40696  30684   3266  -8512  10779
ATOM   6010  CD  PRO C  97     -28.230  42.069 -76.427  1.00306.78           C  
ANISOU 6010  CD  PRO C  97    45504  40558  30501   2441  -8188  10805
ATOM   6011  N   GLU C  98     -29.998  38.795 -76.773  1.00298.56           N  
ANISOU 6011  N   GLU C  98    42888  41352  29200   3041  -7819   9807
ATOM   6012  CA  GLU C  98     -30.739  37.742 -77.447  1.00294.22           C  
ANISOU 6012  CA  GLU C  98    41983  41319  28487   3172  -7768   9510
ATOM   6013  C   GLU C  98     -30.069  36.383 -77.315  1.00287.82           C  
ANISOU 6013  C   GLU C  98    40647  40978  27734   2624  -7384   9200
ATOM   6014  O   GLU C  98     -30.751  35.357 -77.375  1.00282.88           O  
ANISOU 6014  O   GLU C  98    39567  40758  27157   2737  -7344   8830
ATOM   6015  CB  GLU C  98     -30.909  38.089 -78.946  1.00298.66           C  
ANISOU 6015  CB  GLU C  98    42917  41881  28677   3140  -7820   9836
ATOM   6016  CG  GLU C  98     -31.812  37.145 -79.730  1.00295.20           C  
ANISOU 6016  CG  GLU C  98    42210  41865  28089   3313  -7879   9547
ATOM   6017  CD  GLU C  98     -32.009  37.606 -81.163  1.00300.15           C  
ANISOU 6017  CD  GLU C  98    43261  42452  28329   3367  -7969   9882
ATOM   6018  OE1 GLU C  98     -31.395  38.622 -81.546  1.00306.10           O  
ANISOU 6018  OE1 GLU C  98    44484  42875  28944   3211  -7942  10357
ATOM   6019  OE2 GLU C  98     -32.803  36.973 -81.893  1.00298.33           O1-
ANISOU 6019  OE2 GLU C  98    42898  42488  27968   3527  -8094   9683
ATOM   6020  N   ILE C  99     -28.748  36.355 -77.110  1.00293.51           N  
ANISOU 6020  N   ILE C  99    41399  41641  28479   2013  -7105   9338
ATOM   6021  CA  ILE C  99     -28.030  35.122 -76.801  1.00287.09           C  
ANISOU 6021  CA  ILE C  99    40063  41273  27746   1549  -6730   9024
ATOM   6022  C   ILE C  99     -27.977  34.873 -75.301  1.00282.35           C  
ANISOU 6022  C   ILE C  99    39141  40657  27482   1689  -6719   8721
ATOM   6023  O   ILE C  99     -27.679  33.745 -74.881  1.00276.66           O  
ANISOU 6023  O   ILE C  99    37915  40337  26865   1472  -6444   8365
ATOM   6024  CB  ILE C  99     -26.623  35.196 -77.434  1.00288.08           C  
ANISOU 6024  CB  ILE C  99    40381  41383  27692    810  -6443   9309
ATOM   6025  CG1 ILE C  99     -26.739  35.348 -78.950  1.00292.80           C  
ANISOU 6025  CG1 ILE C  99    41265  42052  27936    705  -6429   9577
ATOM   6026  CG2 ILE C  99     -25.787  33.954 -77.119  1.00281.80           C  
ANISOU 6026  CG2 ILE C  99    39053  41052  26964    347  -6054   8974
ATOM   6027  CD1 ILE C  99     -25.441  35.717 -79.631  1.00295.60           C  
ANISOU 6027  CD1 ILE C  99    41921  42297  28096     17  -6192   9936
ATOM   6028  N   ALA C 100     -28.301  35.882 -74.484  1.00288.73           N  
ANISOU 6028  N   ALA C 100    40233  41006  28465   2087  -7017   8835
ATOM   6029  CA  ALA C 100     -28.263  35.737 -73.031  1.00286.06           C  
ANISOU 6029  CA  ALA C 100    39633  40618  28439   2268  -7031   8559
ATOM   6030  C   ALA C 100     -29.107  34.565 -72.548  1.00279.33           C  
ANISOU 6030  C   ALA C 100    38163  40247  27724   2546  -6927   8054
ATOM   6031  O   ALA C 100     -28.784  33.949 -71.525  1.00276.00           O  
ANISOU 6031  O   ALA C 100    37377  39988  27504   2473  -6751   7758
ATOM   6032  CB  ALA C 100     -28.731  37.031 -72.366  1.00289.80           C  
ANISOU 6032  CB  ALA C 100    40525  40515  29071   2785  -7421   8734
ATOM   6033  N   LEU C 101     -30.193  34.250 -73.255  1.00287.56           N  
ANISOU 6033  N   LEU C 101    39090  41489  28679   2831  -7042   7952
ATOM   6034  CA  LEU C 101     -30.947  33.042 -72.943  1.00280.63           C  
ANISOU 6034  CA  LEU C 101    37604  41062  27959   2932  -6906   7503
ATOM   6035  C   LEU C 101     -30.109  31.800 -73.215  1.00275.48           C  
ANISOU 6035  C   LEU C 101    36590  40831  27248   2377  -6482   7311
ATOM   6036  O   LEU C 101     -29.913  30.962 -72.328  1.00269.56           O  
ANISOU 6036  O   LEU C 101    35423  40305  26693   2288  -6259   6974
ATOM   6037  CB  LEU C 101     -32.243  33.009 -73.754  1.00281.56           C  
ANISOU 6037  CB  LEU C 101    37690  41279  28012   3260  -7150   7483
ATOM   6038  CG  LEU C 101     -33.274  34.098 -73.455  1.00285.92           C  
ANISOU 6038  CG  LEU C 101    38497  41462  28678   3835  -7606   7597
ATOM   6039  CD1 LEU C 101     -34.442  34.012 -74.427  1.00286.21           C  
ANISOU 6039  CD1 LEU C 101    38483  41634  28629   4048  -7845   7609
ATOM   6040  CD2 LEU C 101     -33.759  34.004 -72.019  1.00283.38           C  
ANISOU 6040  CD2 LEU C 101    37795  41159  28717   4142  -7611   7305
ATOM   6041  N   GLU C 102     -29.591  31.678 -74.441  1.00281.83           N  
ANISOU 6041  N   GLU C 102    37568  41735  27780   2011  -6369   7517
ATOM   6042  CA  GLU C 102     -28.766  30.529 -74.798  1.00277.85           C  
ANISOU 6042  CA  GLU C 102    36745  41615  27212   1495  -5988   7333
ATOM   6043  C   GLU C 102     -27.488  30.482 -73.968  1.00277.01           C  
ANISOU 6043  C   GLU C 102    36592  41461  27197   1119  -5766   7305
ATOM   6044  O   GLU C 102     -27.064  29.406 -73.528  1.00272.17           O  
ANISOU 6044  O   GLU C 102    35569  41151  26694    893  -5491   6965
ATOM   6045  CB  GLU C 102     -28.436  30.576 -76.290  1.00280.31           C  
ANISOU 6045  CB  GLU C 102    37302  42004  27197   1207  -5933   7594
ATOM   6046  CG  GLU C 102     -29.635  30.402 -77.211  1.00280.72           C  
ANISOU 6046  CG  GLU C 102    37351  42172  27138   1523  -6133   7571
ATOM   6047  CD  GLU C 102     -30.215  29.004 -77.158  1.00274.32           C  
ANISOU 6047  CD  GLU C 102    35979  41780  26471   1527  -5981   7136
ATOM   6048  OE1 GLU C 102     -29.439  28.049 -76.955  1.00269.71           O  
ANISOU 6048  OE1 GLU C 102    35087  41447  25943   1160  -5656   6910
ATOM   6049  OE2 GLU C 102     -31.445  28.860 -77.319  1.00273.67           O1-
ANISOU 6049  OE2 GLU C 102    35766  41763  26453   1887  -6195   7024
ATOM   6050  N   LEU C 103     -26.857  31.640 -73.748  1.00277.57           N  
ANISOU 6050  N   LEU C 103    37101  41129  27236   1035  -5899   7661
ATOM   6051  CA  LEU C 103     -25.654  31.683 -72.922  1.00275.05           C  
ANISOU 6051  CA  LEU C 103    36760  40725  27020    658  -5742   7652
ATOM   6052  C   LEU C 103     -25.954  31.259 -71.491  1.00270.58           C  
ANISOU 6052  C   LEU C 103    35854  40209  26745    958  -5741   7274
ATOM   6053  O   LEU C 103     -25.133  30.599 -70.843  1.00266.31           O  
ANISOU 6053  O   LEU C 103    35051  39840  26293    663  -5512   7039
ATOM   6054  CB  LEU C 103     -25.048  33.086 -72.950  1.00280.03           C  
ANISOU 6054  CB  LEU C 103    37972  40821  27604    505  -5946   8133
ATOM   6055  CG  LEU C 103     -23.744  33.275 -72.172  1.00278.36           C  
ANISOU 6055  CG  LEU C 103    37818  40445  27502     34  -5842   8180
ATOM   6056  CD1 LEU C 103     -22.644  32.404 -72.755  1.00275.97           C  
ANISOU 6056  CD1 LEU C 103    37271  40551  27035   -605  -5461   8092
ATOM   6057  CD2 LEU C 103     -23.327  34.737 -72.164  1.00283.93           C  
ANISOU 6057  CD2 LEU C 103    39168  40487  28227    -94  -6115   8655
ATOM   6058  N   LEU C 104     -27.127  31.636 -70.979  1.00279.09           N  
ANISOU 6058  N   LEU C 104    36935  41142  27965   1556  -5996   7198
ATOM   6059  CA  LEU C 104     -27.551  31.164 -69.666  1.00275.00           C  
ANISOU 6059  CA  LEU C 104    36062  40714  27713   1873  -5965   6813
ATOM   6060  C   LEU C 104     -27.756  29.655 -69.665  1.00267.87           C  
ANISOU 6060  C   LEU C 104    34621  40293  26865   1729  -5660   6385
ATOM   6061  O   LEU C 104     -27.419  28.972 -68.689  1.00263.80           O  
ANISOU 6061  O   LEU C 104    33809  39913  26511   1671  -5475   6068
ATOM   6062  CB  LEU C 104     -28.834  31.879 -69.248  1.00277.42           C  
ANISOU 6062  CB  LEU C 104    36463  40794  28148   2535  -6293   6818
ATOM   6063  CG  LEU C 104     -29.398  31.495 -67.883  1.00273.60           C  
ANISOU 6063  CG  LEU C 104    35621  40393  27942   2908  -6258   6433
ATOM   6064  CD1 LEU C 104     -28.399  31.827 -66.797  1.00274.01           C  
ANISOU 6064  CD1 LEU C 104    35775  40235  28101   2824  -6220   6419
ATOM   6065  CD2 LEU C 104     -30.724  32.197 -67.637  1.00275.97           C  
ANISOU 6065  CD2 LEU C 104    35980  40511  28367   3530  -6570   6438
ATOM   6066  N   MET C 105     -28.302  29.118 -70.756  1.00273.85           N  
ANISOU 6066  N   MET C 105    35274  41285  27492   1671  -5619   6375
ATOM   6067  CA  MET C 105     -28.583  27.689 -70.827  1.00267.32           C  
ANISOU 6067  CA  MET C 105    33971  40861  26737   1540  -5363   5996
ATOM   6068  C   MET C 105     -27.296  26.874 -70.845  1.00264.30           C  
ANISOU 6068  C   MET C 105    33446  40667  26310   1020  -5039   5850
ATOM   6069  O   MET C 105     -27.109  25.971 -70.020  1.00259.37           O  
ANISOU 6069  O   MET C 105    32495  40200  25854    958  -4839   5498
ATOM   6070  CB  MET C 105     -29.425  27.397 -72.065  1.00267.86           C  
ANISOU 6070  CB  MET C 105    34010  41097  26668   1595  -5438   6056
ATOM   6071  CG  MET C 105     -30.804  28.015 -72.029  1.00270.60           C  
ANISOU 6071  CG  MET C 105    34407  41324  27085   2115  -5756   6123
ATOM   6072  SD  MET C 105     -31.704  27.722 -73.553  1.00271.72           S  
ANISOU 6072  SD  MET C 105    34550  41654  27038   2153  -5883   6211
ATOM   6073  CE  MET C 105     -31.969  25.965 -73.399  1.00264.20           C  
ANISOU 6073  CE  MET C 105    32998  41149  26238   1943  -5564   5764
ATOM   6074  N   ALA C 106     -26.396  27.175 -71.786  1.00264.57           N  
ANISOU 6074  N   ALA C 106    33723  40687  26114    640  -4981   6115
ATOM   6075  CA  ALA C 106     -25.118  26.474 -71.826  1.00262.05           C  
ANISOU 6075  CA  ALA C 106    33262  40559  25747    142  -4685   5978
ATOM   6076  C   ALA C 106     -24.283  26.766 -70.588  1.00261.72           C  
ANISOU 6076  C   ALA C 106    33234  40365  25841     56  -4655   5905
ATOM   6077  O   ALA C 106     -23.427  25.958 -70.211  1.00258.20           O  
ANISOU 6077  O   ALA C 106    32557  40104  25443   -239  -4418   5634
ATOM   6078  CB  ALA C 106     -24.346  26.851 -73.090  1.00265.50           C  
ANISOU 6078  CB  ALA C 106    33961  41020  25897   -252  -4629   6307
ATOM   6079  N   ALA C 107     -24.511  27.916 -69.949  1.00266.83           N  
ANISOU 6079  N   ALA C 107    34167  40662  26555    327  -4915   6134
ATOM   6080  CA  ALA C 107     -23.871  28.184 -68.666  1.00264.83           C  
ANISOU 6080  CA  ALA C 107    33919  40245  26458    324  -4934   6035
ATOM   6081  C   ALA C 107     -24.362  27.212 -67.602  1.00260.01           C  
ANISOU 6081  C   ALA C 107    32909  39811  26071    590  -4811   5554
ATOM   6082  O   ALA C 107     -23.576  26.730 -66.778  1.00256.51           O  
ANISOU 6082  O   ALA C 107    32314  39433  25717    417  -4664   5300
ATOM   6083  CB  ALA C 107     -24.133  29.628 -68.241  1.00269.02           C  
ANISOU 6083  CB  ALA C 107    34865  40313  27039    618  -5277   6386
ATOM   6084  N   ASN C 108     -25.664  26.913 -67.604  1.00269.61           N  
ANISOU 6084  N   ASN C 108    33960  41100  27378    989  -4871   5424
ATOM   6085  CA  ASN C 108     -26.188  25.874 -66.724  1.00264.36           C  
ANISOU 6085  CA  ASN C 108    32909  40621  26914   1161  -4712   4992
ATOM   6086  C   ASN C 108     -25.633  24.505 -67.100  1.00259.57           C  
ANISOU 6086  C   ASN C 108    32021  40317  26289    764  -4402   4711
ATOM   6087  O   ASN C 108     -25.413  23.661 -66.223  1.00255.91           O  
ANISOU 6087  O   ASN C 108    31322  39940  25970    733  -4225   4365
ATOM   6088  CB  ASN C 108     -27.718  25.873 -66.780  1.00264.00           C  
ANISOU 6088  CB  ASN C 108    32734  40616  26956   1597  -4843   4962
ATOM   6089  CG  ASN C 108     -28.351  25.009 -65.703  1.00259.30           C  
ANISOU 6089  CG  ASN C 108    31776  40170  26577   1797  -4697   4581
ATOM   6090  OD1 ASN C 108     -27.662  24.388 -64.895  1.00256.02           O  
ANISOU 6090  OD1 ASN C 108    31232  39798  26244   1640  -4506   4326
ATOM   6091  ND2 ASN C 108     -29.678  24.969 -65.688  1.00259.92           N  
ANISOU 6091  ND2 ASN C 108    31687  40334  26739   2138  -4787   4548
ATOM   6092  N   PHE C 109     -25.387  24.275 -68.392  1.00257.23           N  
ANISOU 6092  N   PHE C 109    31766  40159  25811    478  -4339   4851
ATOM   6093  CA  PHE C 109     -24.838  22.998 -68.838  1.00252.56           C  
ANISOU 6093  CA  PHE C 109    30927  39832  25201    133  -4063   4588
ATOM   6094  C   PHE C 109     -23.418  22.786 -68.326  1.00251.37           C  
ANISOU 6094  C   PHE C 109    30767  39693  25050   -204  -3898   4448
ATOM   6095  O   PHE C 109     -23.108  21.743 -67.738  1.00246.87           O  
ANISOU 6095  O   PHE C 109    29957  39229  24614   -284  -3705   4080
ATOM   6096  CB  PHE C 109     -24.869  22.922 -70.364  1.00253.46           C  
ANISOU 6096  CB  PHE C 109    31118  40084  25101    -60  -4056   4790
ATOM   6097  CG  PHE C 109     -24.259  21.667 -70.923  1.00249.89           C  
ANISOU 6097  CG  PHE C 109    30438  39888  24620   -390  -3795   4537
ATOM   6098  CD1 PHE C 109     -24.933  20.462 -70.862  1.00245.81           C  
ANISOU 6098  CD1 PHE C 109    29634  39518  24246   -308  -3687   4231
ATOM   6099  CD2 PHE C 109     -23.007  21.697 -71.512  1.00250.92           C  
ANISOU 6099  CD2 PHE C 109    30648  40110  24581   -786  -3662   4616
ATOM   6100  CE1 PHE C 109     -24.369  19.308 -71.377  1.00242.50           C  
ANISOU 6100  CE1 PHE C 109    29040  39287  23812   -577  -3474   4004
ATOM   6101  CE2 PHE C 109     -22.437  20.549 -72.028  1.00247.78           C  
ANISOU 6101  CE2 PHE C 109    30039  39945  24163  -1043  -3437   4367
ATOM   6102  CZ  PHE C 109     -23.119  19.353 -71.961  1.00243.63           C  
ANISOU 6102  CZ  PHE C 109    29257  39518  23792   -920  -3354   4059
ATOM   6103  N   LEU C 110     -22.541  23.763 -68.541  1.00251.08           N  
ANISOU 6103  N   LEU C 110    31000  39537  24864   -419  -3980   4745
ATOM   6104  CA  LEU C 110     -21.114  23.577 -68.314  1.00249.53           C  
ANISOU 6104  CA  LEU C 110    30779  39412  24619   -827  -3825   4643
ATOM   6105  C   LEU C 110     -20.712  23.657 -66.847  1.00246.93           C  
ANISOU 6105  C   LEU C 110    30413  38945  24463   -721  -3855   4418
ATOM   6106  O   LEU C 110     -19.520  23.532 -66.549  1.00245.71           O  
ANISOU 6106  O   LEU C 110    30234  38848  24279  -1047  -3757   4301
ATOM   6107  CB  LEU C 110     -20.324  24.605 -69.127  1.00253.89           C  
ANISOU 6107  CB  LEU C 110    31637  39895  24933  -1173  -3896   5082
ATOM   6108  CG  LEU C 110     -20.433  24.415 -70.641  1.00256.42           C  
ANISOU 6108  CG  LEU C 110    31989  40397  25041  -1357  -3813   5267
ATOM   6109  CD1 LEU C 110     -19.766  25.554 -71.378  1.00261.37           C  
ANISOU 6109  CD1 LEU C 110    32978  40898  25434  -1683  -3888   5751
ATOM   6110  CD2 LEU C 110     -19.819  23.089 -71.055  1.00253.29           C  
ANISOU 6110  CD2 LEU C 110    31272  40337  24629  -1618  -3526   4915
ATOM   6111  N   ASP C 111     -21.660  23.859 -65.931  1.00254.65           N  
ANISOU 6111  N   ASP C 111    31381  39762  25611   -272  -3990   4338
ATOM   6112  CA  ASP C 111     -21.401  23.889 -64.491  1.00253.35           C  
ANISOU 6112  CA  ASP C 111    31180  39469  25612   -101  -4021   4094
ATOM   6113  C   ASP C 111     -20.399  24.971 -64.098  1.00257.25           C  
ANISOU 6113  C   ASP C 111    31941  39742  26060   -280  -4180   4304
ATOM   6114  O   ASP C 111     -19.808  24.909 -63.016  1.00255.78           O  
ANISOU 6114  O   ASP C 111    31747  39331  26106   -254  -4109   3978
ATOM   6115  CB  ASP C 111     -20.916  22.524 -63.986  1.00248.08           C  
ANISOU 6115  CB  ASP C 111    30228  38972  25057   -240  -3757   3614
ATOM   6116  CG  ASP C 111     -21.992  21.461 -64.052  1.00244.34           C  
ANISOU 6116  CG  ASP C 111    29520  38615  24705    -42  -3625   3396
ATOM   6117  OD1 ASP C 111     -23.185  21.812 -63.938  1.00245.78           O  
ANISOU 6117  OD1 ASP C 111    29708  38736  24940    307  -3751   3512
ATOM   6118  OD2 ASP C 111     -21.644  20.274 -64.221  1.00240.39           O1-
ANISOU 6118  OD2 ASP C 111    28830  38260  24249   -241  -3404   3115
ATOM   6119  N   CYS C 112     -20.194  25.965 -64.956  1.00249.21           N  
ANISOU 6119  N   CYS C 112    31226  38489  24974   -460  -4270   4691
ATOM   6120  CA  CYS C 112     -19.218  27.016 -64.693  1.00254.74           C  
ANISOU 6120  CA  CYS C 112    32252  38654  25882   -688  -4278   4755
ATOM   6121  C   CYS C 112     -19.899  28.310 -64.262  1.00260.28           C  
ANISOU 6121  C   CYS C 112    33317  38796  26783   -289  -4535   4958
ATOM   6122  O   CYS C 112     -19.272  29.188 -63.669  1.00264.38           O  
ANISOU 6122  O   CYS C 112    34112  38786  27553   -344  -4591   4926
ATOM   6123  CB  CYS C 112     -18.354  27.263 -65.932  1.00257.89           C  
ANISOU 6123  CB  CYS C 112    32775  39142  26068  -1240  -4180   5051
ATOM   6124  SG  CYS C 112     -19.262  27.892 -67.364  1.00260.72           S  
ANISOU 6124  SG  CYS C 112    33378  39568  26115  -1182  -4361   5631
ATOM   6125  OXT CYS C 112     -21.091  28.507 -64.494  1.00261.35           O1-
ANISOU 6125  OXT CYS C 112    33475  38993  26833    111  -4708   5143
TER    6126      CYS C 112
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.