CNRS Nantes University US2B US2B
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***  fg  ***

elNémo ID: 23040422133762600

Job options:

ID        	=	 23040422133762600
JOBID     	=	 fg
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 3
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER fg

ATOM      1  N   GLN A   3     -39.670 -32.979 -26.019  1.00 50.86           N  
ANISOU    1  N   GLN A   3     6332   7544   5448   -508   -165   -738       N  
ATOM      2  CA  GLN A   3     -38.347 -32.436 -26.312  1.00 56.71           C  
ANISOU    2  CA  GLN A   3     7090   8280   6179   -513   -126   -735       C  
ATOM      3  C   GLN A   3     -38.259 -30.937 -25.994  1.00 50.48           C  
ANISOU    3  C   GLN A   3     6331   7485   5363   -463   -172   -586       C  
ATOM      4  O   GLN A   3     -37.364 -30.529 -25.249  1.00 46.50           O  
ANISOU    4  O   GLN A   3     5846   6887   4933   -411   -154   -556       O  
ATOM      5  CB  GLN A   3     -37.980 -32.689 -27.781  1.00 59.96           C  
ANISOU    5  CB  GLN A   3     7483   8825   6474   -615    -84   -820       C  
ATOM      6  CG  GLN A   3     -36.542 -32.326 -28.145  1.00 62.26           C  
ANISOU    6  CG  GLN A   3     7785   9112   6759   -633    -29   -846       C  
ATOM      7  CD  GLN A   3     -35.569 -33.477 -27.947  1.00 73.09           C  
ANISOU    7  CD  GLN A   3     9131  10398   8242   -641     49   -992       C  
ATOM      8  NE2 GLN A   3     -34.295 -33.148 -27.748  1.00 66.52           N  
ANISOU    8  NE2 GLN A   3     8309   9507   7458   -620     89   -998       N  
ATOM      9  OE1 GLN A   3     -35.956 -34.647 -27.977  1.00 72.17           O  
ANISOU    9  OE1 GLN A   3     8983  10264   8176   -665     75  -1098       O  
ATOM     10 HE21 GLN A   3     -34.061 -32.320 -27.737  1.00 80.64           H  
ATOM     11 HE22 GLN A   3     -33.705 -33.762 -27.632  1.00 80.64           H  
ATOM     12  N   PHE A   4     -39.177 -30.127 -26.542  1.00 54.20           N  
ANISOU   12  N   PHE A   4     6803   8052   5737   -480   -232   -493       N  
ATOM     13  CA  PHE A   4     -39.142 -28.684 -26.305  1.00 42.06           C  
ANISOU   13  CA  PHE A   4     5288   6505   4187   -435   -275   -350       C  
ATOM     14  C   PHE A   4     -40.455 -28.064 -25.828  1.00 35.89           C  
ANISOU   14  C   PHE A   4     4498   5719   3420   -390   -350   -246       C  
ATOM     15  O   PHE A   4     -40.422 -27.027 -25.154  1.00 36.45           O  
ANISOU   15  O   PHE A   4     4582   5726   3540   -330   -376   -146       O  
ATOM     16  CB  PHE A   4     -38.686 -27.960 -27.581  1.00 42.14           C  
ANISOU   16  CB  PHE A   4     5305   6636   4069   -502   -275   -311       C  
ATOM     17  CG  PHE A   4     -37.242 -28.165 -27.897  1.00 47.59           C  
ANISOU   17  CG  PHE A   4     6007   7316   4758   -533   -201   -388       C  
ATOM     18  CD1 PHE A   4     -36.271 -27.468 -27.205  1.00 58.99           C  
ANISOU   18  CD1 PHE A   4     7476   8667   6272   -477   -181   -343       C  
ATOM     19  CD2 PHE A   4     -36.849 -29.078 -28.859  1.00 51.62           C  
ANISOU   19  CD2 PHE A   4     6499   7910   5206   -620   -147   -516       C  
ATOM     20  CE1 PHE A   4     -34.931 -27.664 -27.476  1.00 57.30           C  
ANISOU   20  CE1 PHE A   4     7267   8440   6063   -503   -113   -418       C  
ATOM     21  CE2 PHE A   4     -35.508 -29.280 -29.134  1.00 47.43           C  
ANISOU   21  CE2 PHE A   4     5972   7364   4686   -650    -75   -598       C  
ATOM     22  CZ  PHE A   4     -34.550 -28.574 -28.442  1.00 43.27           C  
ANISOU   22  CZ  PHE A   4     5470   6742   4229   -589    -59   -546       C  
ATOM     23  H   PHE A   4     -39.820 -30.389 -27.048  1.00 65.85           H  
ATOM     24  N   ASP A   5     -41.600 -28.668 -26.155  1.00 40.35           N  
ANISOU   24  N   ASP A   5     5037   6346   3948   -420   -381   -275       N  
ATOM     25  CA  ASP A   5     -42.898 -28.173 -25.700  1.00 52.32           C  
ANISOU   25  CA  ASP A   5     6537   7856   5487   -379   -450   -190       C  
ATOM     26  C   ASP A   5     -43.326 -28.906 -24.434  1.00 38.90           C  
ANISOU   26  C   ASP A   5     4834   6046   3902   -329   -440   -240       C  
ATOM     27  O   ASP A   5     -43.501 -30.130 -24.449  1.00 44.12           O  
ANISOU   27  O   ASP A   5     5483   6706   4574   -359   -412   -346       O  
ATOM     28  CB  ASP A   5     -43.975 -28.348 -26.770  1.00 63.34           C  
ANISOU   28  CB  ASP A   5     7902   9391   6773   -443   -497   -183       C  
ATOM     29  CG  ASP A   5     -43.659 -27.611 -28.044  1.00 76.84           C  
ANISOU   29  CG  ASP A   5     9613  11226   8356   -504   -517   -118       C  
ATOM     30  OD1 ASP A   5     -42.994 -26.557 -27.974  1.00 80.05           O  
ANISOU   30  OD1 ASP A   5    10040  11602   8772   -476   -522    -28       O  
ATOM     31  OD2 ASP A   5     -44.082 -28.086 -29.118  1.00 82.17           O1-
ANISOU   31  OD2 ASP A   5    10267  12034   8920   -587   -528   -157       O1-
ATOM     32  H   ASP A   5     -41.649 -29.373 -26.644  1.00 49.24           H  
ATOM     33  N   PHE A   6     -43.543 -28.154 -23.359  1.00 26.36           N  
ANISOU   33  N   PHE A   6     3251   4367   2396   -259   -463   -164       N  
ATOM     34  CA  PHE A   6     -43.899 -28.721 -22.070  1.00 31.22           C  
ANISOU   34  CA  PHE A   6     3866   4882   3116   -217   -455   -200       C  
ATOM     35  C   PHE A   6     -45.129 -28.034 -21.498  1.00 28.84           C  
ANISOU   35  C   PHE A   6     3542   4567   2849   -179   -511   -126       C  
ATOM     36  O   PHE A   6     -45.499 -26.931 -21.901  1.00 32.22           O  
ANISOU   36  O   PHE A   6     3958   5034   3250   -167   -553    -32       O  
ATOM     37  CB  PHE A   6     -42.725 -28.601 -21.102  1.00 25.85           C  
ANISOU   37  CB  PHE A   6     3212   4091   2517   -177   -412   -204       C  
ATOM     38  CG  PHE A   6     -41.587 -29.493 -21.454  1.00 25.44           C  
ANISOU   38  CG  PHE A   6     3172   4030   2465   -208   -355   -295       C  
ATOM     39  CD1 PHE A   6     -40.633 -29.097 -22.378  1.00 34.97           C  
ANISOU   39  CD1 PHE A   6     4390   5289   3608   -237   -329   -294       C  
ATOM     40  CD2 PHE A   6     -41.492 -30.749 -20.890  1.00 19.75           C  
ANISOU   40  CD2 PHE A   6     2446   3247   1810   -213   -325   -382       C  
ATOM     41  CE1 PHE A   6     -39.589 -29.935 -22.714  1.00 28.94           C  
ANISOU   41  CE1 PHE A   6     3629   4514   2854   -269   -272   -389       C  
ATOM     42  CE2 PHE A   6     -40.454 -31.592 -21.220  1.00 36.99           C  
ANISOU   42  CE2 PHE A   6     4631   5412   4012   -240   -272   -470       C  
ATOM     43  CZ  PHE A   6     -39.500 -31.187 -22.135  1.00 28.10           C  
ANISOU   43  CZ  PHE A   6     3512   4337   2828   -267   -243   -479       C  
ATOM     44  H   PHE A   6     -43.488 -27.295 -23.354  1.00 32.45           H  
ATOM     45  N   ASP A   7     -45.779 -28.733 -20.566  1.00 22.95           N  
ANISOU   45  N   ASP A   7     2787   3764   2169   -164   -509   -171       N  
ATOM     46  CA  ASP A   7     -46.814 -28.098 -19.762  1.00 19.77           C  
ANISOU   46  CA  ASP A   7     2363   3327   1822   -125   -548   -116       C  
ATOM     47  C   ASP A   7     -46.196 -27.062 -18.837  1.00 28.86           C  
ANISOU   47  C   ASP A   7     3528   4394   3044    -75   -536    -54       C  
ATOM     48  O   ASP A   7     -46.682 -25.929 -18.733  1.00 27.83           O  
ANISOU   48  O   ASP A   7     3376   4260   2937    -45   -569     25       O  
ATOM     49  CB  ASP A   7     -47.570 -29.147 -18.946  1.00 38.37           C  
ANISOU   49  CB  ASP A   7     4709   5644   4226   -132   -542   -187       C  
ATOM     50  CG  ASP A   7     -48.498 -29.989 -19.792  1.00 23.26           C  
ANISOU   50  CG  ASP A   7     2771   3817   2251   -178   -561   -241       C  
ATOM     51  OD1 ASP A   7     -49.174 -29.431 -20.681  1.00 27.37           O  
ANISOU   51  OD1 ASP A   7     3266   4426   2709   -191   -607   -194       O  
ATOM     52  OD2 ASP A   7     -48.554 -31.215 -19.558  1.00 37.11           O1-
ANISOU   52  OD2 ASP A   7     4528   5550   4022   -204   -533   -328       O1-
ATOM     53  H   ASP A   7     -45.641 -29.562 -20.386  1.00 28.36           H  
ATOM     54  N   VAL A   8     -45.099 -27.436 -18.176  1.00 29.60           N  
ANISOU   54  N   VAL A   8     3651   4419   3178    -67   -489    -90       N  
ATOM     55  CA  VAL A   8     -44.432 -26.612 -17.176  1.00 18.04           C  
ANISOU   55  CA  VAL A   8     2200   2874   1781    -27   -469    -48       C  
ATOM     56  C   VAL A   8     -42.954 -26.526 -17.512  1.00 26.73           C  
ANISOU   56  C   VAL A   8     3331   3963   2864    -30   -431    -52       C  
ATOM     57  O   VAL A   8     -42.289 -27.557 -17.681  1.00 17.95           O  
ANISOU   57  O   VAL A   8     2233   2845   1744    -54   -400   -121       O  
ATOM     58  CB  VAL A   8     -44.603 -27.189 -15.757  1.00 30.48           C  
ANISOU   58  CB  VAL A   8     3777   4372   3432    -18   -453    -86       C  
ATOM     59  CG1 VAL A   8     -43.986 -26.246 -14.729  1.00 34.59           C  
ANISOU   59  CG1 VAL A   8     4304   4824   4013     14   -434    -43       C  
ATOM     60  CG2 VAL A   8     -46.061 -27.474 -15.465  1.00 19.14           C  
ANISOU   60  CG2 VAL A   8     2310   2952   2009    -26   -485   -100       C  
ATOM     61  H   VAL A   8     -44.710 -28.193 -18.297  1.00 36.34           H  
ATOM     62  N   VAL A   9     -42.429 -25.303 -17.568  1.00 25.22           N  
ANISOU   62  N   VAL A   9     3145   3760   2677     -5   -429     18       N  
ATOM     63  CA  VAL A   9     -40.996 -25.056 -17.674  1.00 17.77           C  
ANISOU   63  CA  VAL A   9     2228   2793   1730     -3   -389     18       C  
ATOM     64  C   VAL A   9     -40.534 -24.407 -16.383  1.00 17.35           C  
ANISOU   64  C   VAL A   9     2180   2654   1757     34   -369     43       C  
ATOM     65  O   VAL A   9     -41.036 -23.341 -16.000  1.00 26.75           O  
ANISOU   65  O   VAL A   9     3354   3827   2983     60   -386    103       O  
ATOM     66  CB  VAL A   9     -40.647 -24.161 -18.872  1.00 19.76           C  
ANISOU   66  CB  VAL A   9     2485   3110   1913    -15   -398     77       C  
ATOM     67  CG1 VAL A   9     -39.146 -23.874 -18.876  1.00 21.32           C  
ANISOU   67  CG1 VAL A   9     2709   3277   2113    -12   -351     71       C  
ATOM     68  CG2 VAL A   9     -41.095 -24.802 -20.169  1.00 19.09           C  
ANISOU   68  CG2 VAL A   9     2393   3126   1734    -65   -417     49       C  
ATOM     69  H   VAL A   9     -42.898 -24.583 -17.546  1.00 31.08           H  
ATOM     70  N   ILE A  10     -39.562 -25.032 -15.726  1.00 32.87           N  
ANISOU   70  N   ILE A  10     4164   4569   3758     34   -333     -3       N  
ATOM     71  CA  ILE A  10     -38.992 -24.531 -14.483  1.00 24.71           C  
ANISOU   71  CA  ILE A  10     3134   3464   2790     58   -312     15       C  
ATOM     72  C   ILE A  10     -37.564 -24.107 -14.767  1.00 23.96           C  
ANISOU   72  C   ILE A  10     3059   3357   2688     63   -277     22       C  
ATOM     73  O   ILE A  10     -36.743 -24.918 -15.220  1.00 20.96           O  
ANISOU   73  O   ILE A  10     2691   2982   2291     46   -256    -27       O  
ATOM     74  CB  ILE A  10     -39.031 -25.584 -13.369  1.00 20.50           C  
ANISOU   74  CB  ILE A  10     2600   2882   2306     49   -307    -32       C  
ATOM     75  CG1 ILE A  10     -40.470 -25.994 -13.073  1.00 15.82           C  
ANISOU   75  CG1 ILE A  10     1987   2303   1719     39   -338    -44       C  
ATOM     76  CG2 ILE A  10     -38.375 -25.030 -12.119  1.00 21.29           C  
ANISOU   76  CG2 ILE A  10     2703   2925   2461     63   -286    -12       C  
ATOM     77  CD1 ILE A  10     -40.589 -27.338 -12.380  1.00 21.85           C  
ANISOU   77  CD1 ILE A  10     2754   3036   2513     17   -337    -95       C  
ATOM     78  H   ILE A  10     -39.207 -25.770 -15.990  1.00 40.27           H  
ATOM     79  N   VAL A  11     -37.265 -22.844 -14.490  1.00 19.08           N  
ANISOU   79  N   VAL A  11     2440   2719   2090     85   -268     77       N  
ATOM     80  CA  VAL A  11     -35.937 -22.275 -14.678  1.00 20.79           C  
ANISOU   80  CA  VAL A  11     2675   2922   2304     91   -232     89       C  
ATOM     81  C   VAL A  11     -35.221 -22.325 -13.337  1.00 19.88           C  
ANISOU   81  C   VAL A  11     2560   2742   2252    101   -207     72       C  
ATOM     82  O   VAL A  11     -35.504 -21.521 -12.441  1.00 21.45           O  
ANISOU   82  O   VAL A  11     2746   2910   2494    115   -204    101       O  
ATOM     83  CB  VAL A  11     -36.000 -20.838 -15.206  1.00 27.62           C  
ANISOU   83  CB  VAL A  11     3536   3801   3156    104   -236    162       C  
ATOM     84  CG1 VAL A  11     -34.585 -20.320 -15.442  1.00 30.35           C  
ANISOU   84  CG1 VAL A  11     3902   4136   3494    104   -195    168       C  
ATOM     85  CG2 VAL A  11     -36.831 -20.759 -16.468  1.00 19.08           C  
ANISOU   85  CG2 VAL A  11     2448   2791   2009     88   -273    195       C  
ATOM     86  H   VAL A  11     -37.834 -22.279 -14.181  1.00 23.71           H  
ATOM     87  N   GLY A  12     -34.279 -23.257 -13.211  1.00 22.80           N  
ANISOU   87  N   GLY A  12     2940   3094   2630     91   -188     24       N  
ATOM     88  CA  GLY A  12     -33.501 -23.414 -12.001  1.00 14.81           C  
ANISOU   88  CA  GLY A  12     1926   2028   1672     96   -171     14       C  
ATOM     89  C   GLY A  12     -33.810 -24.712 -11.289  1.00 30.39           C  
ANISOU   89  C   GLY A  12     3892   3977   3678     82   -189    -22       C  
ATOM     90  O   GLY A  12     -34.977 -25.012 -11.020  1.00 28.28           O  
ANISOU   90  O   GLY A  12     3616   3718   3410     74   -215    -21       O  
ATOM     91  H   GLY A  12     -34.073 -23.820 -13.828  1.00 28.19           H  
ATOM     92  N   GLY A  13     -32.764 -25.479 -10.972  1.00 29.18           N  
ANISOU   92  N   GLY A  13     3738   3789   3559     77   -177    -49       N  
ATOM     93  CA  GLY A  13     -32.905 -26.778 -10.339  1.00 14.63           C  
ANISOU   93  CA  GLY A  13     1886   1913   1759     63   -196    -75       C  
ATOM     94  C   GLY A  13     -32.318 -26.843  -8.943  1.00 20.00           C  
ANISOU   94  C   GLY A  13     2558   2551   2489     57   -200    -51       C  
ATOM     95  O   GLY A  13     -31.612 -27.799  -8.602  1.00 24.40           O  
ANISOU   95  O   GLY A  13     3106   3070   3095     51   -207    -64       O  
ATOM     96  H   GLY A  13     -31.946 -25.259 -11.118  1.00 35.83           H  
ATOM     97  N   GLY A  14     -32.590 -25.822  -8.134  1.00 20.88           N  
ANISOU   97  N   GLY A  14     2669   2672   2593     55   -197    -15       N  
ATOM     98  CA  GLY A  14     -32.321 -25.870  -6.718  1.00 25.35           C  
ANISOU   98  CA  GLY A  14     3225   3216   3190     34   -206      8       C  
ATOM     99  C   GLY A  14     -33.467 -26.573  -6.016  1.00 13.88           C  
ANISOU   99  C   GLY A  14     1765   1765   1742      5   -236     10       C  
ATOM    100  O   GLY A  14     -34.334 -27.161  -6.665  1.00 29.30           O  
ANISOU  100  O   GLY A  14     3722   3728   3684      7   -250    -11       O  
ATOM    101  H   GLY A  14     -32.936 -25.079  -8.396  1.00 25.88           H  
ATOM    102  N   PRO A  15     -33.505 -26.516  -4.682  1.00 20.17           N  
ANISOU  102  N   PRO A  15     2553   2560   2552    -28   -245     34       N  
ATOM    103  CA  PRO A  15     -34.600 -27.198  -3.961  1.00 18.13           C  
ANISOU  103  CA  PRO A  15     2289   2307   2293    -65   -272     35       C  
ATOM    104  C   PRO A  15     -35.986 -26.665  -4.297  1.00 17.64           C  
ANISOU  104  C   PRO A  15     2224   2275   2204    -63   -269     17       C  
ATOM    105  O   PRO A  15     -36.960 -27.428  -4.241  1.00 18.92           O  
ANISOU  105  O   PRO A  15     2384   2441   2363    -82   -291      4       O  
ATOM    106  CB  PRO A  15     -34.243 -26.974  -2.484  1.00 13.76           C  
ANISOU  106  CB  PRO A  15     1724   1761   1745   -110   -276     65       C  
ATOM    107  CG  PRO A  15     -33.336 -25.785  -2.479  1.00 24.08           C  
ANISOU  107  CG  PRO A  15     3028   3076   3047    -92   -241     70       C  
ATOM    108  CD  PRO A  15     -32.571 -25.835  -3.772  1.00 17.20           C  
ANISOU  108  CD  PRO A  15     2169   2184   2184    -41   -230     57       C  
ATOM    109  N   ALA A  16     -36.106 -25.380  -4.646  1.00 34.26           N  
ANISOU  109  N   ALA A  16     4324   4397   4295    -41   -243     18       N  
ATOM    110  CA  ALA A  16     -37.400 -24.828  -5.036  1.00 31.01           C  
ANISOU  110  CA  ALA A  16     3901   4008   3872    -33   -244      6       C  
ATOM    111  C   ALA A  16     -37.879 -25.443  -6.343  1.00 33.06           C  
ANISOU  111  C   ALA A  16     4171   4279   4112     -9   -263     -8       C  
ATOM    112  O   ALA A  16     -38.999 -25.962  -6.430  1.00 33.50           O  
ANISOU  112  O   ALA A  16     4219   4348   4160    -22   -284    -25       O  
ATOM    113  CB  ALA A  16     -37.304 -23.308  -5.171  1.00 39.29           C  
ANISOU  113  CB  ALA A  16     4938   5063   4929    -11   -214     18       C  
ATOM    114  H   ALA A  16     -35.459 -24.814  -4.665  1.00 41.92           H  
ATOM    115  N   GLY A  17     -37.029 -25.395  -7.371  1.00 35.24           N  
ANISOU  115  N   GLY A  17     4462   4554   4375     19   -254     -6       N  
ATOM    116  CA  GLY A  17     -37.403 -25.936  -8.664  1.00 32.60           C  
ANISOU  116  CA  GLY A  17     4134   4243   4011     31   -267    -26       C  
ATOM    117  C   GLY A  17     -37.587 -27.441  -8.655  1.00 23.42           C  
ANISOU  117  C   GLY A  17     2973   3066   2859     11   -285    -59       C  
ATOM    118  O   GLY A  17     -38.521 -27.961  -9.269  1.00 20.33           O  
ANISOU  118  O   GLY A  17     2578   2700   2448      4   -301    -83       O  
ATOM    119  H   GLY A  17     -36.239 -25.056  -7.341  1.00 43.11           H  
ATOM    120  N   CYS A  18     -36.695 -28.168  -7.973  1.00 17.69           N  
ANISOU  120  N   CYS A  18     2250   2300   2171     -1   -283    -60       N  
ATOM    121  CA  CYS A  18     -36.817 -29.622  -7.939  1.00 22.16           C  
ANISOU  121  CA  CYS A  18     2814   2840   2767    -20   -300    -87       C  
ATOM    122  C   CYS A  18     -38.103 -30.044  -7.241  1.00 19.65           C  
ANISOU  122  C   CYS A  18     2489   2529   2448    -50   -323    -88       C  
ATOM    123  O   CYS A  18     -38.744 -31.027  -7.638  1.00 21.79           O  
ANISOU  123  O   CYS A  18     2757   2799   2724    -63   -335   -119       O  
ATOM    124  CB  CYS A  18     -35.606 -30.233  -7.239  1.00 28.35           C  
ANISOU  124  CB  CYS A  18     3595   3572   3606    -26   -300    -73       C  
ATOM    125  SG  CYS A  18     -34.128 -30.247  -8.260  1.00 28.28           S  
ANISOU  125  SG  CYS A  18     3586   3546   3614      4   -271    -99       S  
ATOM    126  H   CYS A  18     -36.028 -27.848  -7.535  1.00 22.05           H  
ATOM    127  N   THR A  19     -38.498 -29.306  -6.203  1.00 14.41           N  
ANISOU  127  N   THR A  19     1820   1875   1779    -66   -324    -60       N  
ATOM    128  CA  THR A  19     -39.716 -29.641  -5.476  1.00 18.91           C  
ANISOU  128  CA  THR A  19     2381   2457   2347   -102   -341    -65       C  
ATOM    129  C   THR A  19     -40.949 -29.318  -6.307  1.00 25.27           C  
ANISOU  129  C   THR A  19     3177   3301   3122    -89   -346    -91       C  
ATOM    130  O   THR A  19     -41.875 -30.132  -6.393  1.00 30.46           O  
ANISOU  130  O   THR A  19     3830   3966   3778   -110   -362   -117       O  
ATOM    131  CB  THR A  19     -39.745 -28.888  -4.144  1.00 14.25           C  
ANISOU  131  CB  THR A  19     1781   1874   1758   -132   -334    -40       C  
ATOM    132  CG2 THR A  19     -41.065 -29.130  -3.421  1.00 21.66           C  
ANISOU  132  CG2 THR A  19     2707   2832   2689   -176   -345    -55       C  
ATOM    133  OG1 THR A  19     -38.655 -29.325  -3.320  1.00 26.24           O  
ANISOU  133  OG1 THR A  19     3306   3365   3300   -153   -339     -9       O  
ATOM    134  H   THR A  19     -38.082 -28.616  -5.905  1.00 16.29           H  
ATOM    135  HG1 THR A  19     -37.924 -29.171  -3.705  1.00 32.31           H  
ATOM    136  N   CYS A  20     -40.964 -28.142  -6.942  1.00 24.01           N  
ANISOU  136  N   CYS A  20     3013   3166   2943    -57   -334    -81       N  
ATOM    137  CA  CYS A  20     -42.045 -27.790  -7.857  1.00 23.07           C  
ANISOU  137  CA  CYS A  20     2881   3087   2798    -42   -346    -92       C  
ATOM    138  C   CYS A  20     -42.245 -28.864  -8.914  1.00 15.05           C  
ANISOU  138  C   CYS A  20     1872   2087   1759    -44   -359   -126       C  
ATOM    139  O   CYS A  20     -43.384 -29.235  -9.232  1.00 15.27           O  
ANISOU  139  O   CYS A  20     1887   2143   1772    -56   -377   -149       O  
ATOM    140  CB  CYS A  20     -41.735 -26.455  -8.536  1.00 25.09           C  
ANISOU  140  CB  CYS A  20     3132   3359   3041     -6   -335    -62       C  
ATOM    141  SG  CYS A  20     -43.118 -25.809  -9.493  1.00 20.41           S  
ANISOU  141  SG  CYS A  20     2513   2814   2428     12   -360    -54       S  
ATOM    142  H   CYS A  20     -40.362 -27.535  -6.859  1.00 29.63           H  
ATOM    143  N   ALA A  21     -41.144 -29.362  -9.477  1.00 20.14           N  
ANISOU  143  N   ALA A  21     2532   2716   2404    -36   -347   -136       N  
ATOM    144  CA  ALA A  21     -41.217 -30.375 -10.523  1.00 20.66           C  
ANISOU  144  CA  ALA A  21     2599   2797   2452    -44   -349   -181       C  
ATOM    145  C   ALA A  21     -41.725 -31.697  -9.974  1.00 23.06           C  
ANISOU  145  C   ALA A  21     2899   3072   2791    -75   -360   -214       C  
ATOM    146  O   ALA A  21     -42.511 -32.390 -10.630  1.00 36.23           O  
ANISOU  146  O   ALA A  21     4558   4766   4441    -90   -367   -256       O  
ATOM    147  CB  ALA A  21     -39.837 -30.573 -11.146  1.00 21.51           C  
ANISOU  147  CB  ALA A  21     2718   2888   2566    -32   -325   -194       C  
ATOM    148  H   ALA A  21     -40.343 -29.129  -9.271  1.00 24.99           H  
ATOM    149  N   LEU A  22     -41.247 -32.080  -8.794  1.00 32.15           N  
ANISOU  149  N   LEU A  22     4054   4170   3990    -89   -360   -193       N  
ATOM    150  CA  LEU A  22     -41.766 -33.268  -8.134  1.00 30.40           C  
ANISOU  150  CA  LEU A  22     3829   3917   3805   -124   -374   -208       C  
ATOM    151  C   LEU A  22     -43.289 -33.263  -8.140  1.00 20.08           C  
ANISOU  151  C   LEU A  22     2511   2651   2468   -143   -389   -228       C  
ATOM    152  O   LEU A  22     -43.927 -34.249  -8.525  1.00 19.47           O  
ANISOU  152  O   LEU A  22     2428   2575   2396   -163   -395   -270       O  
ATOM    153  CB  LEU A  22     -41.221 -33.330  -6.711  1.00 15.33           C  
ANISOU  153  CB  LEU A  22     1925   1965   1935   -144   -382   -161       C  
ATOM    154  CG  LEU A  22     -41.793 -34.404  -5.792  1.00 18.64           C  
ANISOU  154  CG  LEU A  22     2341   2355   2388   -190   -401   -157       C  
ATOM    155  CD1 LEU A  22     -41.694 -35.759  -6.444  1.00 24.10           C  
ANISOU  155  CD1 LEU A  22     3027   3006   3124   -194   -402   -196       C  
ATOM    156  CD2 LEU A  22     -41.050 -34.375  -4.461  1.00 19.67           C  
ANISOU  156  CD2 LEU A  22     2475   2454   2546   -215   -412    -98       C  
ATOM    157  H   LEU A  22     -40.628 -31.671  -8.359  1.00 39.39           H  
ATOM    158  N   TYR A  23     -43.890 -32.135  -7.757  1.00 30.21           N  
ANISOU  158  N   TYR A  23     3787   3967   3726   -137   -392   -205       N  
ATOM    159  CA  TYR A  23     -45.339 -32.073  -7.593  1.00 20.26           C  
ANISOU  159  CA  TYR A  23     2508   2740   2449   -157   -406   -224       C  
ATOM    160  C   TYR A  23     -46.062 -31.956  -8.934  1.00 39.18           C  
ANISOU  160  C   TYR A  23     4892   5190   4806   -138   -416   -252       C  
ATOM    161  O   TYR A  23     -47.100 -32.604  -9.125  1.00 29.21           O  
ANISOU  161  O   TYR A  23     3616   3948   3535   -161   -428   -289       O  
ATOM    162  CB  TYR A  23     -45.690 -30.921  -6.639  1.00 21.89           C  
ANISOU  162  CB  TYR A  23     2702   2956   2659   -161   -401   -197       C  
ATOM    163  CG  TYR A  23     -45.649 -31.348  -5.176  1.00 15.58           C  
ANISOU  163  CG  TYR A  23     1907   2130   1884   -209   -399   -186       C  
ATOM    164  CD1 TYR A  23     -44.439 -31.516  -4.512  1.00 17.16           C  
ANISOU  164  CD1 TYR A  23     2124   2294   2103   -218   -393   -151       C  
ATOM    165  CD2 TYR A  23     -46.819 -31.615  -4.474  1.00 30.62           C  
ANISOU  165  CD2 TYR A  23     3797   4050   3788   -253   -404   -208       C  
ATOM    166  CE1 TYR A  23     -44.395 -31.923  -3.189  1.00 19.86           C  
ANISOU  166  CE1 TYR A  23     2468   2621   2457   -272   -397   -131       C  
ATOM    167  CE2 TYR A  23     -46.783 -32.028  -3.144  1.00 27.25           C  
ANISOU  167  CE2 TYR A  23     3374   3609   3371   -310   -403   -195       C  
ATOM    168  CZ  TYR A  23     -45.566 -32.177  -2.510  1.00 25.42           C  
ANISOU  168  CZ  TYR A  23     3160   3346   3152   -321   -402   -152       C  
ATOM    169  OH  TYR A  23     -45.509 -32.583  -1.196  1.00 33.89           O  
ANISOU  169  OH  TYR A  23     4235   4415   4227   -386   -407   -127       O  
ATOM    170  H   TYR A  23     -43.483 -31.397  -7.589  1.00 37.07           H  
ATOM    171  HH  TYR A  23     -46.285 -32.705  -0.899  1.00 41.49           H  
ATOM    172  N   THR A  24     -45.527 -31.169  -9.883  1.00 15.86           N  
ANISOU  172  N   THR A  24     1940   2262   1824   -104   -412   -234       N  
ATOM    173  CA  THR A  24     -46.169 -31.041 -11.195  1.00 16.27           C  
ANISOU  173  CA  THR A  24     1977   2376   1827    -96   -427   -251       C  
ATOM    174  C   THR A  24     -46.066 -32.335 -11.996  1.00 16.62           C  
ANISOU  174  C   THR A  24     2027   2431   1858   -119   -421   -308       C  
ATOM    175  O   THR A  24     -46.986 -32.686 -12.746  1.00 23.58           O  
ANISOU  175  O   THR A  24     2892   3365   2704   -135   -435   -342       O  
ATOM    176  CB  THR A  24     -45.555 -29.901 -12.022  1.00 16.32           C  
ANISOU  176  CB  THR A  24     1987   2412   1803    -63   -425   -209       C  
ATOM    177  CG2 THR A  24     -45.815 -28.535 -11.395  1.00 16.10           C  
ANISOU  177  CG2 THR A  24     1945   2375   1799    -39   -430   -158       C  
ATOM    178  OG1 THR A  24     -44.145 -30.113 -12.175  1.00 26.00           O  
ANISOU  178  OG1 THR A  24     3237   3608   3035    -57   -399   -210       O  
ATOM    179  H   THR A  24     -44.807 -30.709  -9.792  1.00 14.94           H  
ATOM    180  HG1 THR A  24     -44.006 -30.820 -12.608  1.00 32.02           H  
ATOM    181  N   ALA A  25     -44.939 -33.042 -11.889  1.00 19.33           N  
ANISOU  181  N   ALA A  25     2387   2725   2232   -123   -398   -324       N  
ATOM    182  CA  ALA A  25     -44.797 -34.313 -12.592  1.00 16.99           C  
ANISOU  182  CA  ALA A  25     2087   2426   1942   -148   -384   -390       C  
ATOM    183  C   ALA A  25     -45.758 -35.359 -12.039  1.00 25.02           C  
ANISOU  183  C   ALA A  25     3094   3422   2990   -180   -393   -425       C  
ATOM    184  O   ALA A  25     -46.290 -36.184 -12.794  1.00 17.57           O  
ANISOU  184  O   ALA A  25     2137   2506   2032   -205   -389   -486       O  
ATOM    185  CB  ALA A  25     -43.354 -34.805 -12.499  1.00 16.96           C  
ANISOU  185  CB  ALA A  25     2095   2360   1989   -141   -357   -398       C  
ATOM    186  H   ALA A  25     -44.254 -32.812 -11.422  1.00 24.01           H  
ATOM    187  N   ARG A  26     -45.974 -35.349 -10.715  1.00 22.20           N  
ANISOU  187  N   ARG A  26     2743   3020   2673   -188   -403   -390       N  
ATOM    188  CA  ARG A  26     -46.926 -36.253 -10.074  1.00 30.00           C  
ANISOU  188  CA  ARG A  26     3724   3989   3686   -225   -412   -414       C  
ATOM    189  C   ARG A  26     -48.362 -35.925 -10.457  1.00 27.23           C  
ANISOU  189  C   ARG A  26     3352   3707   3287   -234   -429   -437       C  
ATOM    190  O   ARG A  26     -49.215 -36.823 -10.497  1.00 31.39           O  
ANISOU  190  O   ARG A  26     3868   4239   3820   -266   -432   -483       O  
ATOM    191  CB  ARG A  26     -46.751 -36.189  -8.556  1.00 31.14           C  
ANISOU  191  CB  ARG A  26     3879   4083   3871   -240   -418   -365       C  
ATOM    192  CG  ARG A  26     -45.541 -36.961  -8.052  1.00 36.58           C  
ANISOU  192  CG  ARG A  26     4579   4695   4623   -245   -411   -344       C  
ATOM    193  CD  ARG A  26     -45.275 -36.736  -6.571  1.00 38.51           C  
ANISOU  193  CD  ARG A  26     4834   4907   4892   -266   -422   -283       C  
ATOM    194  NE  ARG A  26     -46.420 -37.100  -5.741  1.00 38.89           N  
ANISOU  194  NE  ARG A  26     4877   4963   4935   -314   -435   -285       N  
ATOM    195  CZ  ARG A  26     -46.687 -38.328  -5.299  1.00 43.45           C  
ANISOU  195  CZ  ARG A  26     5455   5499   5556   -355   -443   -291       C  
ATOM    196  NH1 ARG A  26     -45.896 -39.353  -5.590  1.00 44.66           N1+
ANISOU  196  NH1 ARG A  26     5608   5588   5772   -351   -440   -295       N1+
ATOM    197  NH2 ARG A  26     -47.762 -38.526  -4.553  1.00 48.36           N  
ANISOU  197  NH2 ARG A  26     6074   6138   6163   -402   -451   -294       N  
ATOM    198  H   ARG A  26     -45.575 -34.822 -10.163  1.00 27.46           H  
ATOM    199  HE  ARG A  26     -46.965 -36.473  -5.521  1.00 47.48           H  
ATOM    200 HH11 ARG A  26     -45.195 -39.231  -6.074  1.00 54.41           H  
ATOM    201 HH12 ARG A  26     -46.084 -40.139  -5.295  1.00 54.41           H  
ATOM    202 HH21 ARG A  26     -48.279 -37.866  -4.359  1.00 58.85           H  
ATOM    203 HH22 ARG A  26     -47.944 -39.314  -4.261  1.00 58.85           H  
ATOM    204  N   SER A  27     -48.633 -34.657 -10.781  1.00 40.67           N  
ANISOU  204  N   SER A  27     5046   5459   4949   -205   -441   -405       N  
ATOM    205  CA  SER A  27     -49.901 -34.219 -11.348  1.00 27.73           C  
ANISOU  205  CA  SER A  27     3379   3890   3269   -206   -464   -418       C  
ATOM    206  C   SER A  27     -50.023 -34.631 -12.809  1.00 24.73           C  
ANISOU  206  C   SER A  27     2988   3570   2837   -212   -467   -460       C  
ATOM    207  O   SER A  27     -51.031 -34.297 -13.450  1.00 26.50           O  
ANISOU  207  O   SER A  27     3186   3863   3020   -214   -492   -466       O  
ATOM    208  CB  SER A  27     -50.028 -32.698 -11.242  1.00 32.50           C  
ANISOU  208  CB  SER A  27     3971   4516   3863   -171   -478   -362       C  
ATOM    209  OG  SER A  27     -50.044 -32.266  -9.896  1.00 49.07           O  
ANISOU  209  OG  SER A  27     6070   6570   6004   -175   -470   -337       O  
ATOM    210  H   SER A  27     -48.074 -34.011 -10.677  1.00 49.62           H  
ATOM    211  HG  SER A  27     -50.115 -31.430  -9.863  1.00 59.70           H  
ATOM    212  N   GLU A  28     -49.028 -35.372 -13.308  1.00 36.77           N  
ANISOU  212  N   GLU A  28     4530   5073   4369   -220   -442   -490       N  
ATOM    213  CA  GLU A  28     -48.890 -35.824 -14.698  1.00 46.91           C  
ANISOU  213  CA  GLU A  28     5804   6416   5604   -237   -432   -542       C  
ATOM    214  C   GLU A  28     -48.881 -34.671 -15.703  1.00 29.58           C  
ANISOU  214  C   GLU A  28     3602   4303   3335   -219   -452   -502       C  
ATOM    215  O   GLU A  28     -49.269 -34.827 -16.862  1.00 29.45           O  
ANISOU  215  O   GLU A  28     3568   4369   3253   -243   -460   -534       O  
ATOM    216  CB  GLU A  28     -49.966 -36.856 -15.052  1.00 54.90           C  
ANISOU  216  CB  GLU A  28     6794   7461   6606   -279   -434   -614       C  
ATOM    217  CG  GLU A  28     -49.644 -38.285 -14.539  1.00 77.66           C  
ANISOU  217  CG  GLU A  28     9682  10262   9562   -307   -403   -671       C  
ATOM    218  CD  GLU A  28     -48.527 -38.996 -15.321  1.00 99.65           C  
ANISOU  218  CD  GLU A  28    12468  13028  12366   -318   -364   -726       C  
ATOM    219  OE1 GLU A  28     -48.388 -38.753 -16.539  1.00103.09           O  
ANISOU  219  OE1 GLU A  28    12893  13542  12734   -329   -357   -757       O  
ATOM    220  OE2 GLU A  28     -47.786 -39.806 -14.719  1.00104.25           O1-
ANISOU  220  OE2 GLU A  28    13059  13517  13034   -321   -342   -738       O1-
ATOM    221  H   GLU A  28     -48.371 -35.647 -12.825  1.00 44.95           H  
ATOM    222  N   LEU A  29     -48.315 -33.540 -15.280  1.00 25.82           N  
ANISOU  222  N   LEU A  29     3138   3803   2868   -181   -458   -430       N  
ATOM    223  CA  LEU A  29     -47.965 -32.447 -16.176  1.00 27.64           C  
ANISOU  223  CA  LEU A  29     3368   4092   3043   -162   -471   -380       C  
ATOM    224  C   LEU A  29     -46.571 -32.669 -16.745  1.00 18.53           C  
ANISOU  224  C   LEU A  29     2236   2928   1877   -167   -436   -399       C  
ATOM    225  O   LEU A  29     -45.631 -32.965 -16.003  1.00 27.72           O  
ANISOU  225  O   LEU A  29     3419   4013   3100   -155   -408   -404       O  
ATOM    226  CB  LEU A  29     -48.001 -31.117 -15.434  1.00 17.99           C  
ANISOU  226  CB  LEU A  29     2145   2841   1850   -121   -488   -300       C  
ATOM    227  CG  LEU A  29     -49.370 -30.696 -14.916  1.00 20.38           C  
ANISOU  227  CG  LEU A  29     2417   3155   2173   -114   -520   -282       C  
ATOM    228  CD1 LEU A  29     -49.179 -29.591 -13.898  1.00 17.57           C  
ANISOU  228  CD1 LEU A  29     2060   2744   1872    -80   -517   -226       C  
ATOM    229  CD2 LEU A  29     -50.261 -30.249 -16.057  1.00 22.48           C  
ANISOU  229  CD2 LEU A  29     2651   3512   2380   -118   -561   -261       C  
ATOM    230  H   LEU A  29     -48.121 -33.380 -14.457  1.00 31.80           H  
ATOM    231  N   LYS A  30     -46.442 -32.536 -18.063  1.00 30.36           N  
ANISOU  231  N   LYS A  30     3727   4510   3298   -189   -437   -411       N  
ATOM    232  CA  LYS A  30     -45.139 -32.666 -18.706  1.00 37.02           C  
ANISOU  232  CA  LYS A  30     4587   5356   4124   -201   -399   -437       C  
ATOM    233  C   LYS A  30     -44.247 -31.505 -18.270  1.00 39.23           C  
ANISOU  233  C   LYS A  30     4887   5595   4422   -158   -397   -359       C  
ATOM    234  O   LYS A  30     -44.541 -30.342 -18.556  1.00 38.74           O  
ANISOU  234  O   LYS A  30     4822   5575   4322   -141   -427   -285       O  
ATOM    235  CB  LYS A  30     -45.303 -32.706 -20.225  1.00 43.51           C  
ANISOU  235  CB  LYS A  30     5394   6295   4844   -248   -402   -466       C  
ATOM    236  CG  LYS A  30     -44.185 -33.454 -20.953  1.00 55.58           C  
ANISOU  236  CG  LYS A  30     6926   7831   6360   -285   -348   -549       C  
ATOM    237  CD  LYS A  30     -44.083 -33.055 -22.431  1.00 62.85           C  
ANISOU  237  CD  LYS A  30     7839   8879   7163   -335   -350   -553       C  
ATOM    238  CE  LYS A  30     -42.818 -33.627 -23.083  1.00 59.90           C  
ANISOU  238  CE  LYS A  30     7468   8508   6784   -372   -288   -638       C  
ATOM    239  NZ  LYS A  30     -42.246 -32.749 -24.148  1.00 66.52           N1+
ANISOU  239  NZ  LYS A  30     8314   9441   7520   -403   -287   -601       N1+
ATOM    240  H   LYS A  30     -47.089 -32.373 -18.605  1.00 37.25           H  
ATOM    241  HZ1 LYS A  30     -41.520 -33.126 -24.497  1.00 80.64           H  
ATOM    242  HZ2 LYS A  30     -42.846 -32.624 -24.794  1.00 80.64           H  
ATOM    243  HZ3 LYS A  30     -42.024 -31.959 -23.805  1.00 80.64           H  
ATOM    244  N   THR A  31     -43.163 -31.830 -17.559  1.00 43.28           N  
ANISOU  244  N   THR A  31     5418   6025   5001   -143   -363   -375       N  
ATOM    245  CA  THR A  31     -42.374 -30.840 -16.841  1.00 46.58           C  
ANISOU  245  CA  THR A  31     5854   6391   5453   -103   -358   -308       C  
ATOM    246  C   THR A  31     -40.902 -30.939 -17.205  1.00 32.95           C  
ANISOU  246  C   THR A  31     4142   4644   3732   -105   -317   -332       C  
ATOM    247  O   THR A  31     -40.350 -32.039 -17.319  1.00 29.42           O  
ANISOU  247  O   THR A  31     3691   4168   3320   -125   -287   -404       O  
ATOM    248  CB  THR A  31     -42.518 -31.022 -15.323  1.00 63.74           C  
ANISOU  248  CB  THR A  31     8031   8480   7707    -82   -362   -292       C  
ATOM    249  CG2 THR A  31     -41.830 -29.896 -14.585  1.00 74.72           C  
ANISOU  249  CG2 THR A  31     9434   9830   9125    -48   -357   -226       C  
ATOM    250  OG1 THR A  31     -43.904 -31.046 -14.968  1.00 65.01           O  
ANISOU  250  OG1 THR A  31     8174   8659   7866    -87   -393   -285       O  
ATOM    251  H   THR A  31     -42.865 -32.633 -17.480  1.00 52.75           H  
ATOM    252  HG1 THR A  31     -44.285 -31.696 -15.340  1.00 78.83           H  
ATOM    253  N   VAL A  32     -40.266 -29.780 -17.359  1.00 22.34           N  
ANISOU  253  N   VAL A  32     2811   3310   2366    -83   -315   -272       N  
ATOM    254  CA  VAL A  32     -38.832 -29.704 -17.591  1.00 23.89           C  
ANISOU  254  CA  VAL A  32     3020   3484   2572    -82   -275   -289       C  
ATOM    255  C   VAL A  32     -38.209 -28.748 -16.587  1.00 22.64           C  
ANISOU  255  C   VAL A  32     2877   3265   2461    -41   -273   -223       C  
ATOM    256  O   VAL A  32     -38.779 -27.696 -16.270  1.00 34.80           O  
ANISOU  256  O   VAL A  32     4417   4813   3992    -19   -297   -155       O  
ATOM    257  CB  VAL A  32     -38.493 -29.253 -19.027  1.00 30.32           C  
ANISOU  257  CB  VAL A  32     3838   4389   3295   -113   -264   -292       C  
ATOM    258  CG1 VAL A  32     -38.978 -27.835 -19.277  1.00 29.71           C  
ANISOU  258  CG1 VAL A  32     3766   4356   3168    -96   -299   -194       C  
ATOM    259  CG2 VAL A  32     -36.987 -29.349 -19.262  1.00 26.18           C  
ANISOU  259  CG2 VAL A  32     3323   3838   2787   -118   -215   -330       C  
ATOM    260  H   VAL A  32     -40.653 -29.013 -17.331  1.00 27.62           H  
ATOM    261  N   ILE A  33     -37.038 -29.128 -16.087  1.00 17.68           N  
ANISOU  261  N   ILE A  33     2255   2575   1889    -32   -242   -248       N  
ATOM    262  CA  ILE A  33     -36.157 -28.239 -15.349  1.00 16.45           C  
ANISOU  262  CA  ILE A  33     2111   2374   1766     -2   -230   -199       C  
ATOM    263  C   ILE A  33     -35.016 -27.842 -16.268  1.00 31.53           C  
ANISOU  263  C   ILE A  33     4029   4310   3640    -10   -196   -212       C  
ATOM    264  O   ILE A  33     -34.293 -28.704 -16.781  1.00 24.17           O  
ANISOU  264  O   ILE A  33     3090   3374   2719    -30   -167   -281       O  
ATOM    265  CB  ILE A  33     -35.598 -28.905 -14.086  1.00 16.17           C  
ANISOU  265  CB  ILE A  33     2072   2256   1816      9   -224   -209       C  
ATOM    266  CG1 ILE A  33     -36.721 -29.354 -13.167  1.00 33.85           C  
ANISOU  266  CG1 ILE A  33     4303   4474   4083      4   -255   -199       C  
ATOM    267  CG2 ILE A  33     -34.666 -27.942 -13.366  1.00 18.12           C  
ANISOU  267  CG2 ILE A  33     2328   2469   2088     33   -210   -162       C  
ATOM    268  CD1 ILE A  33     -36.234 -30.156 -11.991  1.00 26.55           C  
ANISOU  268  CD1 ILE A  33     3374   3476   3236      3   -256   -203       C  
ATOM    269  H   ILE A  33     -36.724 -29.925 -16.167  1.00 22.04           H  
ATOM    270  N   LEU A  34     -34.833 -26.544 -16.443  1.00 24.85           N  
ANISOU  270  N   LEU A  34     3195   3487   2761      5   -196   -149       N  
ATOM    271  CA  LEU A  34     -33.674 -25.993 -17.128  1.00 25.49           C  
ANISOU  271  CA  LEU A  34     3287   3586   2812     -2   -162   -150       C  
ATOM    272  C   LEU A  34     -32.729 -25.468 -16.058  1.00 24.13           C  
ANISOU  272  C   LEU A  34     3121   3344   2704     29   -144   -124       C  
ATOM    273  O   LEU A  34     -33.006 -24.440 -15.432  1.00 30.18           O  
ANISOU  273  O   LEU A  34     3891   4094   3482     52   -155    -60       O  
ATOM    274  CB  LEU A  34     -34.094 -24.888 -18.087  1.00 18.45           C  
ANISOU  274  CB  LEU A  34     2403   2766   1840    -13   -177    -89       C  
ATOM    275  CG  LEU A  34     -35.251 -25.293 -18.991  1.00 17.80           C  
ANISOU  275  CG  LEU A  34     2311   2762   1692    -44   -209    -97       C  
ATOM    276  CD1 LEU A  34     -35.665 -24.107 -19.832  1.00 30.41           C  
ANISOU  276  CD1 LEU A  34     3912   4425   3219    -53   -234    -14       C  
ATOM    277  CD2 LEU A  34     -34.839 -26.473 -19.852  1.00 22.91           C  
ANISOU  277  CD2 LEU A  34     2951   3447   2307    -91   -180   -194       C  
ATOM    278  H   LEU A  34     -35.383 -25.943 -16.168  1.00 30.64           H  
ATOM    279  N   ASP A  35     -31.622 -26.180 -15.848  1.00 18.79           N  
ANISOU  279  N   ASP A  35     2439   2626   2074     27   -114   -177       N  
ATOM    280  CA  ASP A  35     -30.676 -25.908 -14.769  1.00 17.52           C  
ANISOU  280  CA  ASP A  35     2278   2401   1978     52   -100   -160       C  
ATOM    281  C   ASP A  35     -29.336 -25.527 -15.377  1.00 22.83           C  
ANISOU  281  C   ASP A  35     2955   3081   2640     47    -58   -182       C  
ATOM    282  O   ASP A  35     -28.656 -26.368 -15.979  1.00 23.53           O  
ANISOU  282  O   ASP A  35     3031   3168   2741     29    -32   -252       O  
ATOM    283  CB  ASP A  35     -30.530 -27.125 -13.854  1.00 23.08           C  
ANISOU  283  CB  ASP A  35     2965   3044   2762     54   -111   -193       C  
ATOM    284  CG  ASP A  35     -29.845 -26.798 -12.538  1.00 23.15           C  
ANISOU  284  CG  ASP A  35     2969   2997   2829     74   -113   -156       C  
ATOM    285  OD1 ASP A  35     -29.968 -25.648 -12.067  1.00 21.49           O  
ANISOU  285  OD1 ASP A  35     2770   2796   2601     85   -113   -104       O  
ATOM    286  OD2 ASP A  35     -29.196 -27.704 -11.971  1.00 31.16           O1-
ANISOU  286  OD2 ASP A  35     3966   3960   3912     74   -115   -180       O1-
ATOM    287  H   ASP A  35     -31.390 -26.849 -16.336  1.00 23.36           H  
ATOM    288  N   LYS A  36     -28.963 -24.260 -15.203  1.00 26.18           N  
ANISOU  288  N   LYS A  36     3392   3508   3048     61    -47   -127       N  
ATOM    289  CA  LYS A  36     -27.688 -23.749 -15.685  1.00 16.02           C  
ANISOU  289  CA  LYS A  36     2111   2226   1750     56     -5   -142       C  
ATOM    290  C   LYS A  36     -26.525 -24.639 -15.281  1.00 16.01           C  
ANISOU  290  C   LYS A  36     2090   2174   1818     59     18   -203       C  
ATOM    291  O   LYS A  36     -25.717 -25.057 -16.120  1.00 24.50           O  
ANISOU  291  O   LYS A  36     3158   3264   2887     38     53   -266       O  
ATOM    292  CB  LYS A  36     -27.488 -22.349 -15.118  1.00 15.69           C  
ANISOU  292  CB  LYS A  36     2081   2171   1711     76      2    -73       C  
ATOM    293  CG  LYS A  36     -26.156 -21.742 -15.408  1.00 32.20           C  
ANISOU  293  CG  LYS A  36     4178   4260   3798     73     46    -83       C  
ATOM    294  CD  LYS A  36     -26.140 -20.330 -14.890  1.00 38.01           C  
ANISOU  294  CD  LYS A  36     4922   4982   4539     91     53    -15       C  
ATOM    295  CE  LYS A  36     -25.925 -20.296 -13.391  1.00 21.62           C  
ANISOU  295  CE  LYS A  36     2832   2851   2533    112     49     -8       C  
ATOM    296  NZ  LYS A  36     -25.399 -18.955 -13.018  1.00 39.55           N1+
ANISOU  296  NZ  LYS A  36     5106   5107   4814    120     78     31       N1+
ATOM    297  H   LYS A  36     -29.440 -23.669 -14.802  1.00 32.24           H  
ATOM    298  HZ1 LYS A  36     -25.262 -18.915 -12.139  1.00 48.27           H  
ATOM    299  HZ2 LYS A  36     -24.629 -18.801 -13.437  1.00 48.27           H  
ATOM    300  HZ3 LYS A  36     -25.983 -18.323 -13.247  1.00 48.27           H  
ATOM    301  N   ASN A  37     -26.413 -24.907 -13.995  1.00 22.56           N  
ANISOU  301  N   ASN A  37     2908   2946   2718     80      0   -185       N  
ATOM    302  CA  ASN A  37     -25.299 -25.628 -13.409  1.00 26.30           C  
ANISOU  302  CA  ASN A  37     3358   3364   3272     88     11   -221       C  
ATOM    303  C   ASN A  37     -25.753 -26.183 -12.068  1.00 26.90           C  
ANISOU  303  C   ASN A  37     3420   3393   3407     99    -31   -188       C  
ATOM    304  O   ASN A  37     -26.095 -25.414 -11.160  1.00 14.85           O  
ANISOU  304  O   ASN A  37     1903   1866   1873    106    -45   -132       O  
ATOM    305  CB  ASN A  37     -24.095 -24.706 -13.247  1.00 31.15           C  
ANISOU  305  CB  ASN A  37     3973   3971   3891     97     44   -210       C  
ATOM    306  CG  ASN A  37     -22.824 -25.467 -12.978  1.00 31.05           C  
ANISOU  306  CG  ASN A  37     3929   3910   3959    102     59   -258       C  
ATOM    307  ND2 ASN A  37     -21.740 -25.052 -13.620  1.00 32.32           N  
ANISOU  307  ND2 ASN A  37     4087   4083   4111     96    104   -294       N  
ATOM    308  OD1 ASN A  37     -22.812 -26.421 -12.204  1.00 38.81           O  
ANISOU  308  OD1 ASN A  37     4887   4844   5015    109     30   -260       O  
ATOM    309  H   ASN A  37     -26.998 -24.671 -13.409  1.00 27.89           H  
ATOM    310 HD21 ASN A  37     -20.990 -25.453 -13.501  1.00 39.61           H  
ATOM    311 HD22 ASN A  37     -21.788 -24.381 -14.156  1.00 39.61           H  
ATOM    312  N   PRO A  38     -25.783 -27.510 -11.913  1.00 18.83           N  
ANISOU  312  N   PRO A  38     2375   2332   2447     94    -48   -224       N  
ATOM    313  CA  PRO A  38     -26.263 -28.094 -10.647  1.00 20.89           C  
ANISOU  313  CA  PRO A  38     2625   2552   2759     96    -91   -185       C  
ATOM    314  C   PRO A  38     -25.375 -27.763  -9.459  1.00 44.31           C  
ANISOU  314  C   PRO A  38     5578   5486   5770    103   -100   -142       C  
ATOM    315  O   PRO A  38     -25.850 -27.808  -8.315  1.00 41.21           O  
ANISOU  315  O   PRO A  38     5184   5085   5389     94   -134    -93       O  
ATOM    316  CB  PRO A  38     -26.288 -29.603 -10.936  1.00 19.22           C  
ANISOU  316  CB  PRO A  38     2388   2299   2616     88   -101   -237       C  
ATOM    317  CG  PRO A  38     -25.430 -29.806 -12.148  1.00 21.70           C  
ANISOU  317  CG  PRO A  38     2688   2619   2937     86    -55   -313       C  
ATOM    318  CD  PRO A  38     -25.341 -28.521 -12.891  1.00 17.13           C  
ANISOU  318  CD  PRO A  38     2139   2106   2263     83    -24   -305       C  
ATOM    319  N   ALA A  39     -24.117 -27.409  -9.692  1.00 34.33           N  
ANISOU  319  N   ALA A  39     4304   4214   4526    113    -70   -161       N  
ATOM    320  CA  ALA A  39     -23.190 -27.056  -8.629  1.00 44.07           C  
ANISOU  320  CA  ALA A  39     5521   5425   5798    117    -77   -124       C  
ATOM    321  C   ALA A  39     -23.236 -25.580  -8.243  1.00 36.62           C  
ANISOU  321  C   ALA A  39     4599   4522   4792    115    -58    -86       C  
ATOM    322  O   ALA A  39     -22.484 -25.171  -7.355  1.00 47.22           O  
ANISOU  322  O   ALA A  39     5928   5857   6155    112    -59    -59       O  
ATOM    323  CB  ALA A  39     -21.763 -27.432  -9.045  1.00 60.80           C  
ANISOU  323  CB  ALA A  39     7610   7512   7981    128    -52   -170       C  
ATOM    324  H   ALA A  39     -23.769 -27.366 -10.477  1.00 42.01           H  
ATOM    325  N   ALA A  40     -24.098 -24.771  -8.857  1.00 31.05           N  
ANISOU  325  N   ALA A  40     3923   3858   4017    115    -42    -81       N  
ATOM    326  CA  ALA A  40     -24.036 -23.324  -8.676  1.00 32.67           C  
ANISOU  326  CA  ALA A  40     4143   4090   4180    116    -16    -51       C  
ATOM    327  C   ALA A  40     -25.124 -22.759  -7.767  1.00 27.02           C  
ANISOU  327  C   ALA A  40     3432   3388   3445    105    -34     -9       C  
ATOM    328  O   ALA A  40     -25.100 -21.556  -7.479  1.00 18.78           O  
ANISOU  328  O   ALA A  40     2394   2359   2384    104    -10     11       O  
ATOM    329  CB  ALA A  40     -24.098 -22.626 -10.040  1.00 33.30           C  
ANISOU  329  CB  ALA A  40     4245   4202   4204    122     18    -67       C  
ATOM    330  H   ALA A  40     -24.726 -25.036  -9.381  1.00 38.08           H  
ATOM    331  N   GLY A  41     -26.071 -23.585  -7.306  1.00 36.74           N  
ANISOU  331  N   GLY A  41     4660   4614   4686     93    -73     -1       N  
ATOM    332  CA  GLY A  41     -27.092 -23.106  -6.398  1.00 18.54           C  
ANISOU  332  CA  GLY A  41     2354   2325   2367     75    -87     29       C  
ATOM    333  C   GLY A  41     -26.629 -23.092  -4.950  1.00 28.17           C  
ANISOU  333  C   GLY A  41     3554   3539   3610     48    -97     51       C  
ATOM    334  O   GLY A  41     -25.644 -23.729  -4.576  1.00 23.78           O  
ANISOU  334  O   GLY A  41     2983   2964   3090     44   -110     54       O  
ATOM    335  H   GLY A  41     -26.136 -24.419  -7.506  1.00 44.91           H  
ATOM    336  N   ALA A  42     -27.368 -22.346  -4.124  1.00 13.33           N  
ANISOU  336  N   ALA A  42     1669   1682   1713     24    -92     66       N  
ATOM    337  CA  ALA A  42     -26.963 -22.152  -2.734  1.00 16.57           C  
ANISOU  337  CA  ALA A  42     2059   2105   2130    -16    -95     84       C  
ATOM    338  C   ALA A  42     -26.887 -23.477  -1.994  1.00 13.46           C  
ANISOU  338  C   ALA A  42     1654   1702   1758    -44   -146    106       C  
ATOM    339  O   ALA A  42     -25.917 -23.758  -1.282  1.00 13.59           O  
ANISOU  339  O   ALA A  42     1652   1717   1795    -62   -161    127       O  
ATOM    340  CB  ALA A  42     -27.934 -21.205  -2.028  1.00 14.18           C  
ANISOU  340  CB  ALA A  42     1749   1832   1808    -46    -76     81       C  
ATOM    341  H   ALA A  42     -28.097 -21.947  -4.342  1.00 11.90           H  
ATOM    342  N   LEU A  43     -27.929 -24.297  -2.124  1.00 26.23           N  
ANISOU  342  N   LEU A  43     3279   3314   3375    -49   -176    107       N  
ATOM    343  CA  LEU A  43     -27.917 -25.580  -1.440  1.00 13.76           C  
ANISOU  343  CA  LEU A  43     1688   1717   1823    -77   -226    136       C  
ATOM    344  C   LEU A  43     -26.766 -26.440  -1.936  1.00 16.39           C  
ANISOU  344  C   LEU A  43     2010   2005   2211    -48   -241    137       C  
ATOM    345  O   LEU A  43     -26.118 -27.138  -1.152  1.00 20.58           O  
ANISOU  345  O   LEU A  43     2520   2520   2781    -70   -277    175       O  
ATOM    346  CB  LEU A  43     -29.252 -26.291  -1.638  1.00 16.06           C  
ANISOU  346  CB  LEU A  43     1989   2006   2106    -85   -249    129       C  
ATOM    347  CG  LEU A  43     -29.313 -27.700  -1.053  1.00 21.32           C  
ANISOU  347  CG  LEU A  43     2645   2645   2810   -113   -301    161       C  
ATOM    348  CD1 LEU A  43     -29.120 -27.638   0.453  1.00 21.23           C  
ANISOU  348  CD1 LEU A  43     2617   2665   2785   -175   -324    209       C  
ATOM    349  CD2 LEU A  43     -30.620 -28.383  -1.403  1.00 21.86           C  
ANISOU  349  CD2 LEU A  43     2725   2708   2871   -118   -316    145       C  
ATOM    350  H   LEU A  43     -28.633 -24.137  -2.590  1.00 32.30           H  
ATOM    351  N   ALA A  44     -26.482 -26.379  -3.240  1.00 37.69           N  
ANISOU  351  N   ALA A  44     4720   4684   4917     -3   -214     97       N  
ATOM    352  CA  ALA A  44     -25.422 -27.201  -3.811  1.00 14.30           C  
ANISOU  352  CA  ALA A  44     1741   1677   2016     23   -219     80       C  
ATOM    353  C   ALA A  44     -24.072 -26.876  -3.198  1.00 14.38           C  
ANISOU  353  C   ALA A  44     1728   1682   2054     20   -216    101       C  
ATOM    354  O   ALA A  44     -23.220 -27.768  -3.073  1.00 27.37           O  
ANISOU  354  O   ALA A  44     3345   3285   3771     27   -242    110       O  
ATOM    355  CB  ALA A  44     -25.364 -27.006  -5.327  1.00 21.02           C  
ANISOU  355  CB  ALA A  44     2607   2526   2852     59   -180     25       C  
ATOM    356  H   ALA A  44     -26.885 -25.874  -3.808  1.00 46.05           H  
ATOM    357  N   ILE A  45     -23.856 -25.619  -2.796  1.00 22.95           N  
ANISOU  357  N   ILE A  45     2819   2808   3093      9   -186    107       N  
ATOM    358  CA  ILE A  45     -22.551 -25.228  -2.286  1.00 22.87           C  
ANISOU  358  CA  ILE A  45     2786   2801   3104      5   -178    118       C  
ATOM    359  C   ILE A  45     -22.433 -25.316  -0.767  1.00 31.46           C  
ANISOU  359  C   ILE A  45     3851   3915   4189    -46   -216    173       C  
ATOM    360  O   ILE A  45     -21.340 -25.065  -0.235  1.00 41.89           O  
ANISOU  360  O   ILE A  45     5146   5244   5525    -57   -218    189       O  
ATOM    361  CB  ILE A  45     -22.143 -23.794  -2.702  1.00 30.53           C  
ANISOU  361  CB  ILE A  45     3769   3798   4032     18   -118     90       C  
ATOM    362  CG1 ILE A  45     -22.915 -22.721  -1.924  1.00 41.24           C  
ANISOU  362  CG1 ILE A  45     5134   5200   5335    -16   -100    103       C  
ATOM    363  CG2 ILE A  45     -22.337 -23.567  -4.201  1.00 27.47           C  
ANISOU  363  CG2 ILE A  45     3407   3400   3629     57    -82     46       C  
ATOM    364  CD1 ILE A  45     -22.644 -21.310  -2.431  1.00 52.96           C  
ANISOU  364  CD1 ILE A  45     6631   6700   6793      0    -39     76       C  
ATOM    365  H   ILE A  45     -24.443 -24.990  -2.811  1.00 28.36           H  
ATOM    366  N   THR A  46     -23.498 -25.635  -0.036  1.00 31.88           N  
ANISOU  366  N   THR A  46     3909   3988   4215    -86   -246    202       N  
ATOM    367  CA  THR A  46     -23.319 -25.816   1.400  1.00 36.29           C  
ANISOU  367  CA  THR A  46     4444   4581   4764   -148   -286    258       C  
ATOM    368  C   THR A  46     -22.690 -27.178   1.666  1.00 30.08           C  
ANISOU  368  C   THR A  46     3629   3748   4051   -148   -349    308       C  
ATOM    369  O   THR A  46     -23.248 -28.211   1.285  1.00 30.11           O  
ANISOU  369  O   THR A  46     3638   3708   4096   -134   -378    313       O  
ATOM    370  CB  THR A  46     -24.609 -25.704   2.198  1.00 52.59           C  
ANISOU  370  CB  THR A  46     6519   6690   6774   -203   -295    271       C  
ATOM    371  CG2 THR A  46     -24.242 -25.548   3.674  1.00 62.67           C  
ANISOU  371  CG2 THR A  46     7768   8024   8019   -280   -321    318       C  
ATOM    372  OG1 THR A  46     -25.346 -24.566   1.765  1.00 70.22           O  
ANISOU  372  OG1 THR A  46     8772   8946   8961   -192   -238    220       O  
ATOM    373  H   THR A  46     -24.296 -25.748  -0.335  1.00 39.07           H  
ATOM    374  HG1 THR A  46     -26.158 -24.659   1.960  1.00 85.08           H  
ATOM    375  N   HIS A  47     -21.552 -27.179   2.365  1.00 31.53           N  
ANISOU  375  N   HIS A  47     3778   3942   4259   -166   -373    347       N  
ATOM    376  CA  HIS A  47     -20.865 -28.444   2.597  1.00 35.61           C  
ANISOU  376  CA  HIS A  47     4260   4405   4867   -161   -438    402       C  
ATOM    377  C   HIS A  47     -21.604 -29.285   3.642  1.00 29.89           C  
ANISOU  377  C   HIS A  47     3528   3694   4134   -223   -504    478       C  
ATOM    378  O   HIS A  47     -21.515 -30.519   3.590  1.00 35.85           O  
ANISOU  378  O   HIS A  47     4263   4386   4974   -212   -556    520       O  
ATOM    379  CB  HIS A  47     -19.403 -28.200   2.988  1.00 60.09           C  
ANISOU  379  CB  HIS A  47     7319   7512   8002   -160   -449    425       C  
ATOM    380  CG  HIS A  47     -18.570 -27.606   1.882  1.00 87.17           C  
ANISOU  380  CG  HIS A  47    10751  10915  11456    -99   -389    351       C  
ATOM    381  CD2 HIS A  47     -18.488 -27.887   0.562  1.00100.55           C  
ANISOU  381  CD2 HIS A  47    12456  12551  13197    -39   -354    287       C  
ATOM    382  ND1 HIS A  47     -17.672 -26.586   2.115  1.00 94.08           N  
ANISOU  382  ND1 HIS A  47    11614  11832  12301   -106   -355    335       N  
ATOM    383  CE1 HIS A  47     -17.077 -26.258   0.982  1.00 99.98           C  
ANISOU  383  CE1 HIS A  47    12367  12545  13075    -51   -304    268       C  
ATOM    384  NE2 HIS A  47     -17.555 -27.031   0.022  1.00101.38           N  
ANISOU  384  NE2 HIS A  47    12558  12666  13296    -12   -302    238       N  
ATOM    385  H   HIS A  47     -21.172 -26.485   2.701  1.00 38.65           H  
ATOM    386  HD1 HIS A  47     -17.522 -26.221   2.879  1.00113.72           H  
ATOM    387  N   LYS A  48     -22.336 -28.667   4.559  1.00 34.94           N  
ANISOU  387  N   LYS A  48     4182   4412   4682   -290   -499    494       N  
ATOM    388  CA  LYS A  48     -23.102 -29.434   5.537  1.00 19.65           C  
ANISOU  388  CA  LYS A  48     2242   2499   2726   -359   -557    563       C  
ATOM    389  C   LYS A  48     -24.477 -28.798   5.720  1.00 24.60           C  
ANISOU  389  C   LYS A  48     2902   3181   3263   -398   -517    520       C  
ATOM    390  O   LYS A  48     -24.591 -27.574   5.842  1.00 33.14           O  
ANISOU  390  O   LYS A  48     3992   4319   4280   -412   -461    471       O  
ATOM    391  CB  LYS A  48     -22.362 -29.506   6.902  1.00 33.05           C  
ANISOU  391  CB  LYS A  48     3900   4253   4403   -436   -613    651       C  
ATOM    392  CG  LYS A  48     -23.022 -30.398   7.978  1.00 48.43           C  
ANISOU  392  CG  LYS A  48     5841   6229   6331   -520   -683    741       C  
ATOM    393  H   LYS A  48     -22.405 -27.814   4.637  1.00 42.75           H  
ATOM    394  N   ILE A  49     -25.529 -29.616   5.717  1.00 19.18           N  
ANISOU  394  N   ILE A  49     2232   2474   2582   -414   -543    535       N  
ATOM    395  CA  ILE A  49     -26.858 -29.146   6.089  1.00 27.98           C  
ANISOU  395  CA  ILE A  49     3369   3645   3617   -463   -515    503       C  
ATOM    396  C   ILE A  49     -27.399 -30.089   7.158  1.00 25.01           C  
ANISOU  396  C   ILE A  49     2984   3292   3225   -547   -578    579       C  
ATOM    397  O   ILE A  49     -27.465 -31.311   6.941  1.00 30.33           O  
ANISOU  397  O   ILE A  49     3655   3901   3967   -531   -628    625       O  
ATOM    398  CB  ILE A  49     -27.808 -29.014   4.881  1.00 23.33           C  
ANISOU  398  CB  ILE A  49     2811   3018   3036   -400   -471    427       C  
ATOM    399  CG1 ILE A  49     -29.179 -28.475   5.348  1.00 26.84           C  
ANISOU  399  CG1 ILE A  49     3269   3521   3407   -454   -444    393       C  
ATOM    400  CG2 ILE A  49     -27.980 -30.296   4.105  1.00 33.40           C  
ANISOU  400  CG2 ILE A  49     4091   4212   4386   -355   -504    438       C  
ATOM    401  CD1 ILE A  49     -30.012 -27.855   4.246  1.00 23.67           C  
ANISOU  401  CD1 ILE A  49     2891   3102   3000   -395   -391    316       C  
ATOM    402  H   ILE A  49     -25.495 -30.448   5.503  1.00 23.84           H  
ATOM    403  N   ALA A  50     -27.725 -29.539   8.315  1.00 21.97           N  
ANISOU  403  N   ALA A  50     2591   3000   2755   -641   -574    593       N  
ATOM    404  CA  ALA A  50     -28.154 -30.319   9.463  1.00 22.41           C  
ANISOU  404  CA  ALA A  50     2638   3099   2777   -741   -634    673       C  
ATOM    405  C   ALA A  50     -29.513 -29.868   9.977  1.00 20.09           C  
ANISOU  405  C   ALA A  50     2360   2876   2399   -813   -597    623       C  
ATOM    406  O   ALA A  50     -29.968 -30.355  11.018  1.00 33.06           O  
ANISOU  406  O   ALA A  50     3996   4575   3992   -914   -635    679       O  
ATOM    407  CB  ALA A  50     -27.107 -30.237  10.579  1.00 24.92           C  
ANISOU  407  CB  ALA A  50     2921   3482   3066   -813   -678    752       C  
ATOM    408  H   ALA A  50     -27.705 -28.692   8.465  1.00 27.18           H  
ATOM    409  N   ASN A  51     -30.174 -28.953   9.265  1.00 22.74           N  
ANISOU  409  N   ASN A  51     2711   3208   2720   -767   -524    523       N  
ATOM    410  CA  ASN A  51     -31.466 -28.417   9.679  1.00 19.34           C  
ANISOU  410  CA  ASN A  51     2286   2836   2225   -827   -481    462       C  
ATOM    411  C   ASN A  51     -32.511 -28.590   8.587  1.00 27.23           C  
ANISOU  411  C   ASN A  51     3311   3776   3260   -755   -457    404       C  
ATOM    412  O   ASN A  51     -33.475 -27.815   8.522  1.00 15.88           O  
ANISOU  412  O   ASN A  51     1874   2368   1792   -765   -404    329       O  
ATOM    413  CB  ASN A  51     -31.343 -26.947  10.070  1.00 23.28           C  
ANISOU  413  CB  ASN A  51     2767   3404   2673   -858   -412    392       C  
ATOM    414  CG  ASN A  51     -30.791 -26.099   8.959  1.00 20.56           C  
ANISOU  414  CG  ASN A  51     2429   3006   2375   -752   -364    339       C  
ATOM    415  ND2 ASN A  51     -30.499 -24.848   9.272  1.00 27.13           N  
ANISOU  415  ND2 ASN A  51     3242   3886   3179   -773   -305    286       N  
ATOM    416  OD1 ASN A  51     -30.626 -26.557   7.827  1.00 21.26           O  
ANISOU  416  OD1 ASN A  51     2538   3016   2525   -657   -376    342       O  
ATOM    417  H   ASN A  51     -29.888 -28.623   8.525  1.00 28.10           H  
ATOM    418 HD21 ASN A  51     -30.181 -24.318   8.674  1.00 33.37           H  
ATOM    419 HD22 ASN A  51     -30.628 -24.564  10.073  1.00 33.37           H  
ATOM    420  N   TYR A  52     -32.326 -29.558   7.695  1.00 29.46           N  
ANISOU  420  N   TYR A  52     3608   3974   3612   -682   -492    431       N  
ATOM    421  CA  TYR A  52     -33.388 -29.902   6.768  1.00 26.21           C  
ANISOU  421  CA  TYR A  52     3217   3517   3224   -632   -478    383       C  
ATOM    422  C   TYR A  52     -34.223 -30.979   7.431  1.00 17.80           C  
ANISOU  422  C   TYR A  52     2155   2460   2147   -703   -522    425       C  
ATOM    423  O   TYR A  52     -33.714 -32.085   7.684  1.00 35.97           O  
ANISOU  423  O   TYR A  52     4452   4724   4490   -716   -582    504       O  
ATOM    424  CB  TYR A  52     -32.865 -30.379   5.432  1.00 20.37           C  
ANISOU  424  CB  TYR A  52     2488   2692   2559   -528   -484    374       C  
ATOM    425  CG  TYR A  52     -34.001 -30.496   4.436  1.00 15.32           C  
ANISOU  425  CG  TYR A  52     1867   2026   1928   -483   -460    313       C  
ATOM    426  CD1 TYR A  52     -34.480 -29.379   3.761  1.00 20.22           C  
ANISOU  426  CD1 TYR A  52     2493   2664   2525   -442   -406    243       C  
ATOM    427  CD2 TYR A  52     -34.616 -31.716   4.201  1.00 15.57           C  
ANISOU  427  CD2 TYR A  52     1907   2016   1993   -486   -494    327       C  
ATOM    428  CE1 TYR A  52     -35.528 -29.485   2.857  1.00 20.43           C  
ANISOU  428  CE1 TYR A  52     2533   2674   2557   -405   -392    195       C  
ATOM    429  CE2 TYR A  52     -35.659 -31.830   3.307  1.00 15.37           C  
ANISOU  429  CE2 TYR A  52     1894   1975   1969   -450   -474    269       C  
ATOM    430  CZ  TYR A  52     -36.112 -30.713   2.637  1.00 14.93           C  
ANISOU  430  CZ  TYR A  52     1844   1945   1885   -410   -426    205       C  
ATOM    431  OH  TYR A  52     -37.154 -30.822   1.743  1.00 22.17           O  
ANISOU  431  OH  TYR A  52     2769   2852   2801   -377   -413    154       O  
ATOM    432  H   TYR A  52     -31.606 -30.020   7.612  1.00 36.17           H  
ATOM    433  HH  TYR A  52     -37.416 -31.619   1.704  1.00 27.42           H  
ATOM    434  N   PRO A  53     -35.484 -30.706   7.755  1.00 32.11           N  
ANISOU  434  N   PRO A  53     3971   4319   3911   -753   -495    378       N  
ATOM    435  CA  PRO A  53     -36.291 -31.665   8.513  1.00 21.92           C  
ANISOU  435  CA  PRO A  53     2684   3048   2598   -836   -533    417       C  
ATOM    436  C   PRO A  53     -36.574 -32.916   7.698  1.00 16.81           C  
ANISOU  436  C   PRO A  53     2052   2315   2019   -783   -569    438       C  
ATOM    437  O   PRO A  53     -36.969 -32.840   6.532  1.00 26.71           O  
ANISOU  437  O   PRO A  53     3318   3524   3308   -701   -542    376       O  
ATOM    438  CB  PRO A  53     -37.576 -30.891   8.824  1.00 26.70           C  
ANISOU  438  CB  PRO A  53     3284   3716   3144   -885   -480    335       C  
ATOM    439  CG  PRO A  53     -37.568 -29.697   7.933  1.00 25.60           C  
ANISOU  439  CG  PRO A  53     3141   3564   3021   -802   -421    255       C  
ATOM    440  CD  PRO A  53     -36.190 -29.446   7.466  1.00 25.05           C  
ANISOU  440  CD  PRO A  53     3073   3459   2987   -737   -428    285       C  
ATOM    441  N   GLY A  54     -36.392 -34.069   8.340  1.00 30.25           N  
ANISOU  441  N   GLY A  54     3752   3999   3743   -837   -630    525       N  
ATOM    442  CA  GLY A  54     -36.585 -35.356   7.716  1.00 28.31           C  
ANISOU  442  CA  GLY A  54     3514   3666   3575   -799   -665    551       C  
ATOM    443  C   GLY A  54     -35.305 -35.988   7.233  1.00 25.29           C  
ANISOU  443  C   GLY A  54     3120   3201   3289   -734   -702    606       C  
ATOM    444  O   GLY A  54     -35.304 -37.174   6.881  1.00 27.36           O  
ANISOU  444  O   GLY A  54     3379   3383   3634   -714   -737    639       O  
ATOM    445  H   GLY A  54     -36.148 -34.123   9.162  1.00 37.12           H  
ATOM    446  N   VAL A  55     -34.216 -35.228   7.234  1.00 26.94           N  
ANISOU  446  N   VAL A  55     3317   3424   3495   -705   -692    611       N  
ATOM    447  CA  VAL A  55     -32.926 -35.671   6.724  1.00 18.08           C  
ANISOU  447  CA  VAL A  55     2176   2226   2467   -638   -718    648       C  
ATOM    448  C   VAL A  55     -31.898 -35.550   7.844  1.00 24.57           C  
ANISOU  448  C   VAL A  55     2974   3088   3274   -696   -764    742       C  
ATOM    449  O   VAL A  55     -31.298 -34.484   8.041  1.00 22.91           O  
ANISOU  449  O   VAL A  55     2757   2932   3014   -695   -735    721       O  
ATOM    450  CB  VAL A  55     -32.553 -34.872   5.469  1.00 17.17           C  
ANISOU  450  CB  VAL A  55     2069   2089   2367   -540   -660    558       C  
ATOM    451  CG1 VAL A  55     -31.153 -35.185   5.041  1.00 29.25           C  
ANISOU  451  CG1 VAL A  55     3575   3552   3985   -482   -680    587       C  
ATOM    452  CG2 VAL A  55     -33.557 -35.202   4.362  1.00 26.78           C  
ANISOU  452  CG2 VAL A  55     3304   3268   3602   -492   -630    481       C  
ATOM    453  H   VAL A  55     -34.199 -34.423   7.535  1.00 33.15           H  
ATOM    454  N   PRO A  56     -31.670 -36.643   8.578  1.00 19.42           N  
ANISOU  454  N   PRO A  56     2304   2407   2667   -749   -836    850       N  
ATOM    455  CA  PRO A  56     -30.806 -36.612   9.765  1.00 19.70           C  
ANISOU  455  CA  PRO A  56     2313   2494   2678   -823   -892    956       C  
ATOM    456  C   PRO A  56     -29.339 -36.837   9.445  1.00 20.94           C  
ANISOU  456  C   PRO A  56     2436   2585   2935   -758   -924   1001       C  
ATOM    457  O   PRO A  56     -28.991 -37.092   8.291  1.00 47.86           O  
ANISOU  457  O   PRO A  56     5842   5903   6438   -658   -901    946       O  
ATOM    458  CB  PRO A  56     -31.365 -37.770  10.605  1.00 24.09           C  
ANISOU  458  CB  PRO A  56     2866   3044   3245   -910   -960   1058       C  
ATOM    459  CG  PRO A  56     -31.799 -38.772   9.558  1.00 20.52           C  
ANISOU  459  CG  PRO A  56     2421   2472   2905   -834   -957   1026       C  
ATOM    460  CD  PRO A  56     -32.226 -37.988   8.338  1.00 22.31           C  
ANISOU  460  CD  PRO A  56     2672   2692   3114   -747   -873    883       C  
ATOM    461  N   GLY A  57     -28.474 -36.753  10.458  1.00 32.89           N  
ANISOU  461  N   GLY A  57     3920   4148   4428   -819   -978   1098       N  
ATOM    462  CA  GLY A  57     -27.078 -37.121  10.310  1.00 38.94           C  
ANISOU  462  CA  GLY A  57     4645   4849   5302   -767  -1023   1159       C  
ATOM    463  C   GLY A  57     -26.258 -36.185   9.431  1.00 46.16           C  
ANISOU  463  C   GLY A  57     5556   5752   6231   -677   -962   1066       C  
ATOM    464  O   GLY A  57     -26.587 -35.010   9.226  1.00 39.72           O  
ANISOU  464  O   GLY A  57     4766   5005   5320   -674   -890    975       O  
ATOM    465  H   GLY A  57     -28.678 -36.481  11.248  1.00 40.28           H  
ATOM    466  N   GLU A  58     -25.160 -36.746   8.914  1.00 41.70           N  
ANISOU  466  N   GLU A  58     4953   5093   5797   -607   -991   1092       N  
ATOM    467  CA  GLU A  58     -24.227 -36.025   8.056  1.00 42.85           C  
ANISOU  467  CA  GLU A  58     5090   5217   5975   -523   -939   1013       C  
ATOM    468  C   GLU A  58     -24.791 -35.963   6.643  1.00 41.78           C  
ANISOU  468  C   GLU A  58     4985   5022   5867   -438   -866    889       C  
ATOM    469  O   GLU A  58     -25.015 -37.003   6.014  1.00 57.40           O  
ANISOU  469  O   GLU A  58     6955   6905   7949   -399   -879    883       O  
ATOM    470  CB  GLU A  58     -22.866 -36.714   8.026  1.00 61.53           C  
ANISOU  470  CB  GLU A  58     7397   7502   8479   -482   -997   1081       C  
ATOM    471  H   GLU A  58     -24.930 -37.564   9.051  1.00 50.85           H  
ATOM    472  N   MET A  59     -25.002 -34.757   6.132  1.00 37.63           N  
ANISOU  472  N   MET A  59     4490   4552   5254   -414   -790    793       N  
ATOM    473  CA  MET A  59     -25.540 -34.606   4.789  1.00 38.82           C  
ANISOU  473  CA  MET A  59     4670   4663   5417   -342   -725    683       C  
ATOM    474  C   MET A  59     -24.964 -33.343   4.177  1.00 24.61           C  
ANISOU  474  C   MET A  59     2880   2898   3572   -298   -659    606       C  
ATOM    475  O   MET A  59     -25.012 -32.278   4.797  1.00 39.82           O  
ANISOU  475  O   MET A  59     4817   4910   5403   -338   -637    604       O  
ATOM    476  CB  MET A  59     -27.072 -34.548   4.825  1.00 39.61           C  
ANISOU  476  CB  MET A  59     4810   4801   5440   -378   -704    651       C  
ATOM    477  CG  MET A  59     -27.743 -34.193   3.511  1.00 48.27           C  
ANISOU  477  CG  MET A  59     5937   5881   6523   -316   -638    542       C  
ATOM    478  SD  MET A  59     -27.311 -35.293   2.154  1.00 49.35           S  
ANISOU  478  SD  MET A  59     6056   5902   6794   -235   -633    495       S  
ATOM    479  CE  MET A  59     -28.311 -36.730   2.499  1.00 46.60           C  
ANISOU  479  CE  MET A  59     5705   5502   6499   -274   -682    540       C  
ATOM    480  H   MET A  59     -24.843 -34.017   6.542  1.00 45.97           H  
ATOM    481  N   SER A  60     -24.414 -33.470   2.976  1.00 19.85           N  
ANISOU  481  N   SER A  60     2271   2231   3040   -221   -626    542       N  
ATOM    482  CA  SER A  60     -23.942 -32.313   2.237  1.00 22.67           C  
ANISOU  482  CA  SER A  60     2642   2616   3354   -178   -560    467       C  
ATOM    483  C   SER A  60     -25.059 -31.791   1.348  1.00 27.35           C  
ANISOU  483  C   SER A  60     3278   3230   3882   -157   -503    387       C  
ATOM    484  O   SER A  60     -25.941 -32.539   0.911  1.00 24.64           O  
ANISOU  484  O   SER A  60     2947   2856   3559   -151   -510    370       O  
ATOM    485  CB  SER A  60     -22.723 -32.651   1.384  1.00 17.02           C  
ANISOU  485  CB  SER A  60     1895   1831   2740   -115   -549    434       C  
ATOM    486  OG  SER A  60     -23.020 -33.716   0.508  1.00 47.20           O  
ANISOU  486  OG  SER A  60     5711   5574   6647    -80   -549    398       O  
ATOM    487  H   SER A  60     -24.304 -34.220   2.569  1.00 24.64           H  
ATOM    488  HG  SER A  60     -23.632 -33.491  -0.021  1.00 57.45           H  
ATOM    489  N   GLY A  61     -25.006 -30.487   1.083  1.00 30.17           N  
ANISOU  489  N   GLY A  61     3655   3641   4166   -146   -449    343       N  
ATOM    490  CA  GLY A  61     -26.084 -29.849   0.355  1.00 20.69           C  
ANISOU  490  CA  GLY A  61     2492   2468   2903   -131   -403    282       C  
ATOM    491  C   GLY A  61     -26.266 -30.429  -1.031  1.00 15.22           C  
ANISOU  491  C   GLY A  61     1807   1724   2252    -77   -383    224       C  
ATOM    492  O   GLY A  61     -27.395 -30.595  -1.500  1.00 17.41           O  
ANISOU  492  O   GLY A  61     2105   2009   2501    -77   -375    196       O  
ATOM    493  H   GLY A  61     -24.364 -29.962   1.311  1.00 37.02           H  
ATOM    494  N   ASP A  62     -25.162 -30.755  -1.704  1.00 15.94           N  
ANISOU  494  N   ASP A  62     1877   1769   2411    -38   -374    201       N  
ATOM    495  CA  ASP A  62     -25.282 -31.253  -3.070  1.00 19.42           C  
ANISOU  495  CA  ASP A  62     2323   2172   2884      3   -346    132       C  
ATOM    496  C   ASP A  62     -25.799 -32.686  -3.115  1.00 17.14           C  
ANISOU  496  C   ASP A  62     2019   1827   2668     -4   -381    136       C  
ATOM    497  O   ASP A  62     -26.424 -33.076  -4.111  1.00 28.98           O  
ANISOU  497  O   ASP A  62     3529   3316   4167     11   -358     77       O  
ATOM    498  CB  ASP A  62     -23.948 -31.082  -3.810  1.00 21.94           C  
ANISOU  498  CB  ASP A  62     2621   2465   3250     40   -314     91       C  
ATOM    499  CG  ASP A  62     -22.824 -31.941  -3.265  1.00 25.13           C  
ANISOU  499  CG  ASP A  62     2976   2807   3765     43   -352    126       C  
ATOM    500  OD1 ASP A  62     -23.014 -32.718  -2.302  1.00 34.24           O  
ANISOU  500  OD1 ASP A  62     4111   3935   4962     16   -409    193       O  
ATOM    501  OD2 ASP A  62     -21.723 -31.822  -3.846  1.00 32.27           O1-
ANISOU  501  OD2 ASP A  62     3858   3688   4714     73   -324     86       O1-
ATOM    502  H   ASP A  62     -24.359 -30.699  -1.401  1.00 19.95           H  
ATOM    503  N   HIS A  63     -25.586 -33.485  -2.059  1.00 17.95           N  
ANISOU  503  N   HIS A  63     2095   1894   2831    -32   -437    208       N  
ATOM    504  CA AHIS A  63     -26.196 -34.806  -1.947  0.46 16.88           C  
ANISOU  504  CA AHIS A  63     1946   1702   2764    -47   -474    225       C  
ATOM    505  CA BHIS A  63     -26.212 -34.799  -2.018  0.54 16.87           C  
ANISOU  505  CA BHIS A  63     1945   1701   2762    -45   -472    220       C  
ATOM    506  C   HIS A  63     -27.680 -34.708  -1.632  1.00 16.58           C  
ANISOU  506  C   HIS A  63     1943   1712   2645    -84   -480    232       C  
ATOM    507  O   HIS A  63     -28.463 -35.596  -2.005  1.00 31.72           O  
ANISOU  507  O   HIS A  63     3863   3597   4594    -87   -487    210       O  
ATOM    508  CB AHIS A  63     -25.467 -35.611  -0.863  0.46 17.48           C  
ANISOU  508  CB AHIS A  63     1982   1729   2932    -70   -539    316       C  
ATOM    509  CB BHIS A  63     -25.477 -35.728  -1.049  0.54 19.98           C  
ANISOU  509  CB BHIS A  63     2296   2035   3260    -64   -535    304       C  
ATOM    510  CG AHIS A  63     -26.004 -36.995  -0.661  0.46 18.07           C  
ANISOU  510  CG AHIS A  63     2038   1735   3094    -88   -582    347       C  
ATOM    511  CG BHIS A  63     -24.213 -36.311  -1.608  0.54 20.76           C  
ANISOU  511  CG BHIS A  63     2347   2055   3486    -20   -531    279       C  
ATOM    512  CD2AHIS A  63     -25.392 -38.204  -0.687  0.46 26.25           C  
ANISOU  512  CD2AHIS A  63     3025   2671   4277    -74   -615    370       C  
ATOM    513  ND1AHIS A  63     -27.332 -37.243  -0.399  0.46 25.28           N  
ANISOU  513  ND1AHIS A  63     2981   2674   3952   -125   -592    356       N  
ATOM    514  CD2BHIS A  63     -23.157 -36.897  -0.994  0.54 18.82           C  
ANISOU  514  CD2BHIS A  63     2050   1751   3350    -18   -579    342       C  
ATOM    515  ND1BHIS A  63     -23.927 -36.330  -2.956  0.54 18.04           N  
ANISOU  515  ND1BHIS A  63     1998   1686   3170     23   -473    175       N  
ATOM    516  CE1AHIS A  63     -27.521 -38.545  -0.280  0.46 18.60           C  
ANISOU  516  CE1AHIS A  63     2109   1749   3208   -135   -628    384       C  
ATOM    517  NE2AHIS A  63     -26.359 -39.150  -0.444  0.46 19.18           N  
ANISOU  517  NE2AHIS A  63     2133   1742   3411   -103   -644    395       N  
ATOM    518  CE1BHIS A  63     -22.750 -36.899  -3.150  0.54 18.62           C  
ANISOU  518  CE1BHIS A  63     2019   1686   3370     51   -479    165       C  
ATOM    519  NE2BHIS A  63     -22.262 -37.252  -1.974  0.54 28.11           N  
ANISOU  519  NE2BHIS A  63     3189   2862   4628     30   -545    269       N  
ATOM    520  H  AHIS A  63     -25.088 -33.278  -1.390  0.46 22.36           H  
ATOM    521  H  BHIS A  63     -25.098 -33.288  -1.379  0.54 22.36           H  
ATOM    522  HD1AHIS A  63     -27.944 -36.644  -0.326  0.46 31.16           H  
ATOM    523  HE2BHIS A  63     -21.506 -37.641  -1.843  0.54 34.54           H  
ATOM    524  N   LEU A  64     -28.083 -33.667  -0.913  1.00 23.14           N  
ANISOU  524  N   LEU A  64     2797   2618   3378   -115   -476    259       N  
ATOM    525  CA  LEU A  64     -29.497 -33.489  -0.642  1.00 22.15           C  
ANISOU  525  CA  LEU A  64     2699   2539   3179   -149   -475    255       C  
ATOM    526  C   LEU A  64     -30.223 -33.061  -1.909  1.00 26.19           C  
ANISOU  526  C   LEU A  64     3234   3069   3648   -113   -428    174       C  
ATOM    527  O   LEU A  64     -31.287 -33.583  -2.232  1.00 28.08           O  
ANISOU  527  O   LEU A  64     3484   3307   3879   -121   -430    150       O  
ATOM    528  CB  LEU A  64     -29.705 -32.469   0.467  1.00 15.61           C  
ANISOU  528  CB  LEU A  64     1879   1784   2268   -197   -476    293       C  
ATOM    529  CG  LEU A  64     -31.168 -32.096   0.712  1.00 27.29           C  
ANISOU  529  CG  LEU A  64     3381   3315   3673   -232   -464    274       C  
ATOM    530  CD1 LEU A  64     -32.030 -33.287   1.116  1.00 24.36           C  
ANISOU  530  CD1 LEU A  64     3010   2921   3326   -272   -504    301       C  
ATOM    531  CD2 LEU A  64     -31.236 -31.000   1.771  1.00 25.09           C  
ANISOU  531  CD2 LEU A  64     3102   3108   3322   -281   -453    295       C  
ATOM    532  H   LEU A  64     -27.569 -33.065  -0.578  1.00 28.59           H  
ATOM    533  N   LEU A  65     -29.634 -32.112  -2.638  1.00 28.69           N  
ANISOU  533  N   LEU A  65     3557   3406   3936    -75   -386    137       N  
ATOM    534  CA  LEU A  65     -30.244 -31.695  -3.898  1.00 29.14           C  
ANISOU  534  CA  LEU A  65     3634   3487   3951    -45   -347     71       C  
ATOM    535  C   LEU A  65     -30.323 -32.848  -4.870  1.00 15.45           C  
ANISOU  535  C   LEU A  65     1890   1707   2274    -28   -345     22       C  
ATOM    536  O   LEU A  65     -31.328 -32.974  -5.605  1.00 22.26           O  
ANISOU  536  O   LEU A  65     2766   2591   3101    -27   -334    -20       O  
ATOM    537  CB  LEU A  65     -29.463 -30.519  -4.485  1.00 14.79           C  
ANISOU  537  CB  LEU A  65     1824   1696   2099    -14   -306     50       C  
ATOM    538  CG  LEU A  65     -30.038 -29.951  -5.781  1.00 16.49           C  
ANISOU  538  CG  LEU A  65     2060   1946   2261     11   -271     -2       C  
ATOM    539  CD1 LEU A  65     -31.299 -29.143  -5.570  1.00 26.77           C  
ANISOU  539  CD1 LEU A  65     3378   3298   3496     -3   -269      8       C  
ATOM    540  CD2 LEU A  65     -28.939 -29.103  -6.403  1.00 26.46           C  
ANISOU  540  CD2 LEU A  65     3324   3217   3513     38   -233    -19       C  
ATOM    541  H   LEU A  65     -28.904 -31.707  -2.430  1.00 35.24           H  
ATOM    542  N   GLU A  66     -29.304 -33.713  -4.927  1.00 15.88           N  
ANISOU  542  N   GLU A  66     1916   1697   2422    -16   -355     21       N  
ATOM    543  CA  GLU A  66     -29.346 -34.831  -5.858  1.00 28.15           C  
ANISOU  543  CA  GLU A  66     3451   3200   4043     -4   -345    -40       C  
ATOM    544  C   GLU A  66     -30.562 -35.713  -5.590  1.00 25.90           C  
ANISOU  544  C   GLU A  66     3170   2903   3768    -32   -371    -34       C  
ATOM    545  O   GLU A  66     -31.215 -36.199  -6.526  1.00 22.28           O  
ANISOU  545  O   GLU A  66     2713   2446   3305    -30   -350    -99       O  
ATOM    546  CB  GLU A  66     -28.078 -35.677  -5.755  1.00 20.71           C  
ANISOU  546  CB  GLU A  66     2466   2178   3226     11   -355    -36       C  
ATOM    547  CG  GLU A  66     -27.988 -36.811  -6.785  1.00 20.34           C  
ANISOU  547  CG  GLU A  66     2390   2071   3267     23   -332   -117       C  
ATOM    548  CD  GLU A  66     -28.807 -38.046  -6.413  1.00 37.54           C  
ANISOU  548  CD  GLU A  66     4555   4198   5511     -1   -365   -103       C  
ATOM    549  OE1 GLU A  66     -28.892 -38.366  -5.208  1.00 42.09           O  
ANISOU  549  OE1 GLU A  66     5127   4748   6119    -23   -417    -14       O  
ATOM    550  OE2 GLU A  66     -29.364 -38.697  -7.328  1.00 32.77           O1-
ANISOU  550  OE2 GLU A  66     3944   3582   4924     -4   -338   -180       O1-
ATOM    551  H   GLU A  66     -28.593 -33.672  -4.445  1.00 16.62           H  
ATOM    552  N   VAL A  67     -30.858 -35.948  -4.314  1.00 22.89           N  
ANISOU  552  N   VAL A  67     2789   2514   3396    -66   -416     43       N  
ATOM    553  CA  VAL A  67     -32.016 -36.747  -3.932  1.00 16.72           C  
ANISOU  553  CA  VAL A  67     2013   1723   2618   -101   -442     55       C  
ATOM    554  C   VAL A  67     -33.293 -36.101  -4.451  1.00 22.34           C  
ANISOU  554  C   VAL A  67     2754   2506   3229   -106   -418     11       C  
ATOM    555  O   VAL A  67     -34.187 -36.784  -4.966  1.00 17.45           O  
ANISOU  555  O   VAL A  67     2136   1880   2614   -114   -414    -31       O  
ATOM    556  CB  VAL A  67     -32.051 -36.916  -2.400  1.00 24.19           C  
ANISOU  556  CB  VAL A  67     2955   2665   3570   -148   -493    152       C  
ATOM    557  CG1 VAL A  67     -33.322 -37.631  -1.972  1.00 16.99           C  
ANISOU  557  CG1 VAL A  67     2053   1754   2649   -192   -516    165       C  
ATOM    558  CG2 VAL A  67     -30.813 -37.657  -1.893  1.00 20.82           C  
ANISOU  558  CG2 VAL A  67     2491   2164   3256   -144   -528    208       C  
ATOM    559  H   VAL A  67     -30.400 -35.655  -3.647  1.00 28.29           H  
ATOM    560  N   MET A  68     -33.388 -34.771  -4.326  1.00 27.77           N  
ANISOU  560  N   MET A  68     3462   3260   3831   -100   -401     21       N  
ATOM    561  CA  MET A  68     -34.583 -34.043  -4.752  1.00 20.42           C  
ANISOU  561  CA  MET A  68     2551   2392   2814   -102   -384    -10       C  
ATOM    562  C   MET A  68     -34.733 -34.080  -6.261  1.00 32.04           C  
ANISOU  562  C   MET A  68     4025   3878   4270    -71   -353    -82       C  
ATOM    563  O   MET A  68     -35.845 -34.240  -6.786  1.00 16.32           O  
ANISOU  563  O   MET A  68     2040   1916   2243    -79   -351   -117       O  
ATOM    564  CB  MET A  68     -34.482 -32.580  -4.310  1.00 26.63           C  
ANISOU  564  CB  MET A  68     3349   3232   3536   -100   -369     15       C  
ATOM    565  CG  MET A  68     -34.976 -32.259  -2.921  1.00 34.74           C  
ANISOU  565  CG  MET A  68     4377   4285   4537   -147   -389     63       C  
ATOM    566  SD  MET A  68     -35.169 -30.480  -2.678  1.00 35.87           S  
ANISOU  566  SD  MET A  68     4527   4491   4611   -143   -357     63       S  
ATOM    567  CE  MET A  68     -34.429 -30.261  -1.080  1.00 16.10           C  
ANISOU  567  CE  MET A  68     2012   1996   2111   -193   -373    122       C  
ATOM    568  H   MET A  68     -32.771 -34.267  -3.999  1.00 34.15           H  
ATOM    569  N   ARG A  69     -33.618 -33.883  -6.966  1.00 26.89           N  
ANISOU  569  N   ARG A  69     3366   3212   3638    -42   -328   -105       N  
ATOM    570  CA  ARG A  69     -33.587 -33.973  -8.418  1.00 17.89           C  
ANISOU  570  CA  ARG A  69     2226   2092   2480    -24   -296   -176       C  
ATOM    571  C   ARG A  69     -33.993 -35.358  -8.888  1.00 21.69           C  
ANISOU  571  C   ARG A  69     2689   2536   3018    -39   -297   -229       C  
ATOM    572  O   ARG A  69     -34.851 -35.505  -9.766  1.00 30.76           O  
ANISOU  572  O   ARG A  69     3841   3725   4121    -48   -285   -280       O  
ATOM    573  CB  ARG A  69     -32.178 -33.624  -8.912  1.00 15.95           C  
ANISOU  573  CB  ARG A  69     1971   1831   2258      1   -267   -193       C  
ATOM    574  CG  ARG A  69     -32.053 -33.426 -10.415  1.00 26.43           C  
ANISOU  574  CG  ARG A  69     3301   3200   3542      9   -228   -263       C  
ATOM    575  CD  ARG A  69     -30.596 -33.264 -10.859  1.00 22.78           C  
ANISOU  575  CD  ARG A  69     2825   2716   3116     26   -196   -289       C  
ATOM    576  NE  ARG A  69     -29.905 -32.214 -10.118  1.00 22.47           N  
ANISOU  576  NE  ARG A  69     2796   2680   3061     42   -199   -229       N  
ATOM    577  CZ  ARG A  69     -28.885 -32.421  -9.288  1.00 15.95           C  
ANISOU  577  CZ  ARG A  69     1951   1801   2307     50   -210   -199       C  
ATOM    578  NH1 ARG A  69     -28.418 -33.645  -9.085  1.00 29.48           N1+
ANISOU  578  NH1 ARG A  69     3633   3444   4125     49   -222   -216       N1+
ATOM    579  NH2 ARG A  69     -28.328 -31.399  -8.661  1.00 25.24           N  
ANISOU  579  NH2 ARG A  69     3138   2994   3459     59   -209   -150       N  
ATOM    580  H   ARG A  69     -32.854 -33.695  -6.618  1.00 33.08           H  
ATOM    581  HE  ARG A  69     -30.175 -31.404 -10.225  1.00 27.78           H  
ATOM    582 HH11 ARG A  69     -28.774 -34.314  -9.492  1.00 36.20           H  
ATOM    583 HH12 ARG A  69     -27.759 -33.771  -8.548  1.00 36.20           H  
ATOM    584 HH21 ARG A  69     -28.624 -30.602  -8.791  1.00 31.11           H  
ATOM    585 HH22 ARG A  69     -27.669 -31.530  -8.126  1.00 31.11           H  
ATOM    586  N   ASP A  70     -33.395 -36.399  -8.311  1.00 16.74           N  
ANISOU  586  N   ASP A  70     2037   1829   2494    -45   -313   -217       N  
ATOM    587  CA  ASP A  70     -33.756 -37.748  -8.707  1.00 30.72           C  
ANISOU  587  CA  ASP A  70     3785   3550   4337    -60   -311   -269       C  
ATOM    588  C   ASP A  70     -35.232 -38.026  -8.423  1.00 20.02           C  
ANISOU  588  C   ASP A  70     2445   2224   2939    -89   -331   -263       C  
ATOM    589  O   ASP A  70     -35.920 -38.632  -9.246  1.00 33.60           O  
ANISOU  589  O   ASP A  70     4157   3955   4655   -102   -314   -331       O  
ATOM    590  CB  ASP A  70     -32.834 -38.743  -8.010  1.00 41.97           C  
ANISOU  590  CB  ASP A  70     5176   4874   5896    -59   -331   -239       C  
ATOM    591  CG  ASP A  70     -33.186 -40.176  -8.286  1.00 64.03           C  
ANISOU  591  CG  ASP A  70     7940   7600   8787    -76   -330   -286       C  
ATOM    592  OD1 ASP A  70     -34.343 -40.602  -8.137  1.00 73.08           O  
ANISOU  592  OD1 ASP A  70     9098   8759   9911   -103   -343   -288       O  
ATOM    593  OD2 ASP A  70     -32.264 -40.909  -8.576  1.00 84.46           O1-
ANISOU  593  OD2 ASP A  70    10489  10113  11489    -63   -316   -319       O1-
ATOM    594  H   ASP A  70     -32.790 -36.347  -7.702  1.00 18.61           H  
ATOM    595  N   GLN A  71     -35.752 -37.527  -7.291  1.00 28.00           N  
ANISOU  595  N   GLN A  71     3474   3255   3911   -105   -363   -190       N  
ATOM    596  CA  GLN A  71     -37.181 -37.689  -7.018  1.00 32.30           C  
ANISOU  596  CA  GLN A  71     4031   3833   4410   -136   -379   -190       C  
ATOM    597  C   GLN A  71     -38.019 -37.111  -8.151  1.00 28.53           C  
ANISOU  597  C   GLN A  71     3563   3432   3846   -127   -355   -249       C  
ATOM    598  O   GLN A  71     -38.912 -37.779  -8.688  1.00 31.89           O  
ANISOU  598  O   GLN A  71     3982   3868   4266   -144   -351   -300       O  
ATOM    599  CB  GLN A  71     -37.558 -37.003  -5.706  1.00 24.58           C  
ANISOU  599  CB  GLN A  71     3068   2881   3390   -159   -407   -115       C  
ATOM    600  CG  GLN A  71     -37.528 -37.875  -4.473  1.00 21.34           C  
ANISOU  600  CG  GLN A  71     2650   2418   3040   -199   -444    -54       C  
ATOM    601  CD  GLN A  71     -37.743 -37.063  -3.217  1.00 21.83           C  
ANISOU  601  CD  GLN A  71     2725   2523   3048   -231   -463     12       C  
ATOM    602  NE2 GLN A  71     -38.719 -37.459  -2.411  1.00 27.20           N  
ANISOU  602  NE2 GLN A  71     3409   3213   3711   -282   -485     35       N  
ATOM    603  OE1 GLN A  71     -37.047 -36.078  -2.980  1.00 25.99           O  
ANISOU  603  OE1 GLN A  71     3256   3075   3545   -215   -455     36       O  
ATOM    604  H   GLN A  71     -35.310 -37.103  -6.687  1.00 34.42           H  
ATOM    605 HE21 GLN A  71     -39.193 -38.148  -2.615  1.00 33.45           H  
ATOM    606 HE22 GLN A  71     -38.879 -37.029  -1.684  1.00 33.45           H  
ATOM    607  N   ALA A  72     -37.752 -35.855  -8.517  1.00 16.28           N  
ANISOU  607  N   ALA A  72     2024   1934   2227   -102   -342   -239       N  
ATOM    608  CA  ALA A  72     -38.507 -35.208  -9.583  1.00 16.25           C  
ANISOU  608  CA  ALA A  72     2027   2005   2141    -94   -328   -277       C  
ATOM    609  C   ALA A  72     -38.475 -36.033 -10.864  1.00 16.77           C  
ANISOU  609  C   ALA A  72     2079   2078   2216   -101   -304   -358       C  
ATOM    610  O   ALA A  72     -39.494 -36.172 -11.549  1.00 25.82           O  
ANISOU  610  O   ALA A  72     3222   3276   3313   -116   -304   -397       O  
ATOM    611  CB  ALA A  72     -37.950 -33.804  -9.825  1.00 20.55           C  
ANISOU  611  CB  ALA A  72     2585   2591   2633    -66   -315   -246       C  
ATOM    612  H   ALA A  72     -37.143 -35.362  -8.166  1.00 15.44           H  
ATOM    613  N   VAL A  73     -37.314 -36.619 -11.180  1.00 23.59           N  
ANISOU  613  N   VAL A  73     2928   2891   3146    -93   -281   -389       N  
ATOM    614  CA  VAL A  73     -37.145 -37.379 -12.417  1.00 17.67           C  
ANISOU  614  CA  VAL A  73     2157   2147   2409   -106   -247   -481       C  
ATOM    615  C   VAL A  73     -37.822 -38.740 -12.322  1.00 31.52           C  
ANISOU  615  C   VAL A  73     3890   3857   4228   -135   -250   -526       C  
ATOM    616  O   VAL A  73     -38.357 -39.251 -13.313  1.00 21.34           O  
ANISOU  616  O   VAL A  73     2587   2606   2916   -158   -228   -606       O  
ATOM    617  CB  VAL A  73     -35.644 -37.532 -12.732  1.00 30.40           C  
ANISOU  617  CB  VAL A  73     3751   3713   4085    -90   -217   -508       C  
ATOM    618  CG1 VAL A  73     -35.420 -38.527 -13.876  1.00 20.71           C  
ANISOU  618  CG1 VAL A  73     2492   2478   2897   -114   -174   -619       C  
ATOM    619  CG2 VAL A  73     -35.019 -36.185 -13.058  1.00 17.55           C  
ANISOU  619  CG2 VAL A  73     2145   2141   2384    -69   -206   -477       C  
ATOM    620  H   VAL A  73     -36.607 -36.589 -10.692  1.00 29.13           H  
ATOM    621  N   GLU A  74     -37.773 -39.374 -11.154  1.00 22.32           N  
ANISOU  621  N   GLU A  74     2721   2614   3147   -138   -277   -478       N  
ATOM    622  CA  GLU A  74     -38.436 -40.663 -11.013  1.00 33.33           C  
ANISOU  622  CA  GLU A  74     4096   3958   4609   -167   -281   -513       C  
ATOM    623  C   GLU A  74     -39.922 -40.541 -11.316  1.00 34.34           C  
ANISOU  623  C   GLU A  74     4236   4161   4650   -191   -288   -536       C  
ATOM    624  O   GLU A  74     -40.537 -41.500 -11.795  1.00 38.68           O  
ANISOU  624  O   GLU A  74     4767   4703   5227   -219   -274   -604       O  
ATOM    625  CB  GLU A  74     -38.177 -41.239  -9.622  1.00 48.98           C  
ANISOU  625  CB  GLU A  74     6075   5852   6684   -173   -317   -435       C  
ATOM    626  CG  GLU A  74     -38.321 -42.755  -9.542  1.00 69.58           C  
ANISOU  626  CG  GLU A  74     8653   8372   9413   -197   -314   -470       C  
ATOM    627  CD  GLU A  74     -37.010 -43.500  -9.725  1.00 94.11           C  
ANISOU  627  CD  GLU A  74    11720  11381  12655   -180   -297   -493       C  
ATOM    628  OE1 GLU A  74     -35.969 -42.846  -9.940  1.00 97.77           O  
ANISOU  628  OE1 GLU A  74    12182  11853  13114   -150   -285   -487       O  
ATOM    629  OE2 GLU A  74     -37.025 -44.750  -9.657  1.00102.44           O1-
ANISOU  629  OE2 GLU A  74    12742  12348  13832   -196   -293   -520       O1-
ATOM    630  H   GLU A  74     -37.374 -39.087 -10.448  1.00 27.61           H  
ATOM    631  N   PHE A  75     -40.519 -39.372 -11.088  1.00 33.94           N  
ANISOU  631  N   PHE A  75     4211   4184   4501   -182   -308   -488       N  
ATOM    632  CA  PHE A  75     -41.936 -39.179 -11.363  1.00 27.60           C  
ANISOU  632  CA  PHE A  75     3412   3452   3622   -201   -320   -506       C  
ATOM    633  C   PHE A  75     -42.192 -38.530 -12.724  1.00 26.84           C  
ANISOU  633  C   PHE A  75     3314   3451   3434   -197   -303   -552       C  
ATOM    634  O   PHE A  75     -43.340 -38.180 -13.021  1.00 29.67           O  
ANISOU  634  O   PHE A  75     3672   3878   3722   -209   -319   -558       O  
ATOM    635  CB  PHE A  75     -42.580 -38.377 -10.227  1.00 27.65           C  
ANISOU  635  CB  PHE A  75     3437   3475   3593   -200   -353   -429       C  
ATOM    636  CG  PHE A  75     -42.752 -39.181  -8.961  1.00 22.28           C  
ANISOU  636  CG  PHE A  75     2758   2727   2982   -228   -373   -392       C  
ATOM    637  CD1 PHE A  75     -43.644 -40.241  -8.919  1.00 24.44           C  
ANISOU  637  CD1 PHE A  75     3020   2982   3283   -263   -376   -429       C  
ATOM    638  CD2 PHE A  75     -41.998 -38.904  -7.831  1.00 24.70           C  
ANISOU  638  CD2 PHE A  75     3073   2990   3321   -224   -390   -317       C  
ATOM    639  CE1 PHE A  75     -43.796 -41.002  -7.771  1.00 26.80           C  
ANISOU  639  CE1 PHE A  75     3320   3219   3644   -294   -397   -387       C  
ATOM    640  CE2 PHE A  75     -42.147 -39.662  -6.675  1.00 33.05           C  
ANISOU  640  CE2 PHE A  75     4130   3993   4434   -259   -414   -273       C  
ATOM    641  CZ  PHE A  75     -43.047 -40.712  -6.648  1.00 36.14           C  
ANISOU  641  CZ  PHE A  75     4513   4363   4854   -295   -418   -304       C  
ATOM    642  H   PHE A  75     -40.122 -38.677 -10.774  1.00 41.55           H  
ATOM    643  N   GLY A  76     -41.164 -38.382 -13.560  1.00 30.02           N  
ANISOU  643  N   GLY A  76     3711   3861   3834   -186   -274   -584       N  
ATOM    644  CA  GLY A  76     -41.341 -38.059 -14.972  1.00 31.96           C  
ANISOU  644  CA  GLY A  76     3950   4199   3994   -200   -254   -639       C  
ATOM    645  C   GLY A  76     -40.758 -36.733 -15.422  1.00 36.65           C  
ANISOU  645  C   GLY A  76     4561   4849   4517   -176   -254   -594       C  
ATOM    646  O   GLY A  76     -40.843 -36.414 -16.618  1.00 37.97           O  
ANISOU  646  O   GLY A  76     4723   5100   4605   -194   -241   -629       O  
ATOM    647  H   GLY A  76     -40.341 -38.464 -13.327  1.00 36.84           H  
ATOM    648  N   THR A  77     -40.187 -35.940 -14.523  1.00 46.32           N  
ANISOU  648  N   THR A  77     5804   6035   5762   -142   -267   -518       N  
ATOM    649  CA  THR A  77     -39.564 -34.682 -14.907  1.00 56.68           C  
ANISOU  649  CA  THR A  77     7131   7388   7016   -120   -263   -475       C  
ATOM    650  C   THR A  77     -38.406 -34.917 -15.871  1.00 41.07           C  
ANISOU  650  C   THR A  77     5146   5418   5042   -129   -221   -532       C  
ATOM    651  O   THR A  77     -37.631 -35.865 -15.720  1.00 40.13           O  
ANISOU  651  O   THR A  77     5010   5229   5007   -133   -196   -581       O  
ATOM    652  CB  THR A  77     -39.051 -33.951 -13.667  1.00 70.28           C  
ANISOU  652  CB  THR A  77     8869   9058   8777    -87   -277   -396       C  
ATOM    653  CG2 THR A  77     -38.476 -32.595 -14.033  1.00 78.51           C  
ANISOU  653  CG2 THR A  77     9926  10139   9765    -64   -270   -351       C  
ATOM    654  OG1 THR A  77     -40.119 -33.781 -12.728  1.00 71.59           O  
ANISOU  654  OG1 THR A  77     9038   9220   8944    -89   -308   -355       O  
ATOM    655  H   THR A  77     -40.147 -36.108 -13.681  1.00 56.41           H  
ATOM    656  HG1 THR A  77     -40.404 -34.530 -12.477  1.00 86.73           H  
ATOM    657  N   VAL A  78     -38.294 -34.042 -16.862  1.00 26.62           N  
ANISOU  657  N   VAL A  78     3323   3669   3122   -135   -214   -526       N  
ATOM    658  CA  VAL A  78     -37.127 -33.983 -17.734  1.00 23.30           C  
ANISOU  658  CA  VAL A  78     2899   3266   2688   -147   -172   -570       C  
ATOM    659  C   VAL A  78     -36.155 -32.962 -17.146  1.00 18.64           C  
ANISOU  659  C   VAL A  78     2328   2641   2114   -109   -171   -501       C  
ATOM    660  O   VAL A  78     -36.484 -31.776 -17.042  1.00 19.08           O  
ANISOU  660  O   VAL A  78     2402   2733   2113    -91   -194   -426       O  
ATOM    661  CB  VAL A  78     -37.533 -33.604 -19.167  1.00 19.12           C  
ANISOU  661  CB  VAL A  78     2367   2856   2043   -188   -166   -597       C  
ATOM    662  CG1 VAL A  78     -36.320 -33.324 -20.030  1.00 21.10           C  
ANISOU  662  CG1 VAL A  78     2617   3136   2264   -207   -122   -634       C  
ATOM    663  CG2 VAL A  78     -38.362 -34.706 -19.798  1.00 20.68           C  
ANISOU  663  CG2 VAL A  78     2539   3091   2226   -234   -159   -683       C  
ATOM    664  H   VAL A  78     -38.896 -33.458 -17.056  1.00 32.76           H  
ATOM    665  N   TYR A  79     -34.973 -33.424 -16.731  1.00 27.52           N  
ANISOU  665  N   TYR A  79     3444   3690   3323    -96   -144   -526       N  
ATOM    666  CA  TYR A  79     -33.915 -32.543 -16.246  1.00 19.63           C  
ANISOU  666  CA  TYR A  79     2458   2660   2339    -65   -137   -474       C  
ATOM    667  C   TYR A  79     -32.950 -32.268 -17.389  1.00 22.58           C  
ANISOU  667  C   TYR A  79     2828   3079   2672    -85    -93   -523       C  
ATOM    668  O   TYR A  79     -32.373 -33.204 -17.954  1.00 34.12           O  
ANISOU  668  O   TYR A  79     4264   4524   4176   -109    -55   -614       O  
ATOM    669  CB  TYR A  79     -33.148 -33.144 -15.069  1.00 28.82           C  
ANISOU  669  CB  TYR A  79     3610   3721   3619    -42   -139   -463       C  
ATOM    670  CG  TYR A  79     -31.989 -32.273 -14.597  1.00 21.28           C  
ANISOU  670  CG  TYR A  79     2664   2741   2680    -15   -129   -418       C  
ATOM    671  CD1 TYR A  79     -32.204 -31.203 -13.735  1.00 21.80           C  
ANISOU  671  CD1 TYR A  79     2751   2811   2720      8   -154   -333       C  
ATOM    672  CD2 TYR A  79     -30.686 -32.513 -15.020  1.00 22.05           C  
ANISOU  672  CD2 TYR A  79     2745   2812   2822    -15    -91   -468       C  
ATOM    673  CE1 TYR A  79     -31.153 -30.402 -13.300  1.00 20.57           C  
ANISOU  673  CE1 TYR A  79     2602   2635   2578     28   -141   -297       C  
ATOM    674  CE2 TYR A  79     -29.630 -31.718 -14.588  1.00 32.94           C  
ANISOU  674  CE2 TYR A  79     4130   4171   4214      9    -81   -429       C  
ATOM    675  CZ  TYR A  79     -29.871 -30.666 -13.731  1.00 18.37           C  
ANISOU  675  CZ  TYR A  79     2308   2332   2338     30   -106   -343       C  
ATOM    676  OH  TYR A  79     -28.826 -29.878 -13.308  1.00 36.28           O  
ANISOU  676  OH  TYR A  79     4581   4584   4620     48    -92   -310       O  
ATOM    677  H   TYR A  79     -34.760 -34.257 -16.723  1.00 33.84           H  
ATOM    678  HH  TYR A  79     -29.104 -29.296 -12.770  1.00 44.36           H  
ATOM    679  N   ARG A  80     -32.759 -30.994 -17.717  1.00 24.34           N  
ANISOU  679  N   ARG A  80     3074   3354   2820    -78    -93   -467       N  
ATOM    680  CA  ARG A  80     -31.857 -30.587 -18.785  1.00 21.38           C  
ANISOU  680  CA  ARG A  80     2701   3031   2393   -103    -53   -503       C  
ATOM    681  C   ARG A  80     -30.876 -29.569 -18.234  1.00 32.48           C  
ANISOU  681  C   ARG A  80     4123   4403   3815    -69    -44   -444       C  
ATOM    682  O   ARG A  80     -31.283 -28.607 -17.576  1.00 25.77           O  
ANISOU  682  O   ARG A  80     3293   3549   2951    -40    -74   -357       O  
ATOM    683  CB  ARG A  80     -32.650 -29.998 -19.958  1.00 25.42           C  
ANISOU  683  CB  ARG A  80     3223   3657   2778   -141    -63   -487       C  
ATOM    684  CG  ARG A  80     -33.515 -31.016 -20.690  1.00 26.88           C  
ANISOU  684  CG  ARG A  80     3387   3893   2932   -186    -64   -561       C  
ATOM    685  CD  ARG A  80     -32.657 -32.067 -21.370  1.00 34.51           C  
ANISOU  685  CD  ARG A  80     4326   4854   3934   -227     -6   -686       C  
ATOM    686  NE  ARG A  80     -31.531 -31.462 -22.075  1.00 48.47           N  
ANISOU  686  NE  ARG A  80     6099   6659   5660   -249     36   -703       N  
ATOM    687  CZ  ARG A  80     -31.609 -30.916 -23.284  1.00 56.43           C  
ANISOU  687  CZ  ARG A  80     7115   7782   6544   -304     47   -707       C  
ATOM    688  NH1 ARG A  80     -32.763 -30.901 -23.939  1.00 51.00           N1+
ANISOU  688  NH1 ARG A  80     6428   7186   5764   -341     16   -693       N1+
ATOM    689  NH2 ARG A  80     -30.528 -30.388 -23.842  1.00 58.70           N  
ANISOU  689  NH2 ARG A  80     7408   8097   6798   -326     88   -723       N  
ATOM    690  H   ARG A  80     -33.149 -30.335 -17.326  1.00 30.03           H  
ATOM    691  HE  ARG A  80     -30.766 -31.459 -21.681  1.00 58.99           H  
ATOM    692 HH11 ARG A  80     -33.465 -31.246 -23.583  1.00 62.02           H  
ATOM    693 HH12 ARG A  80     -32.808 -30.548 -24.722  1.00 62.02           H  
ATOM    694 HH21 ARG A  80     -29.778 -30.398 -23.421  1.00 71.26           H  
ATOM    695 HH22 ARG A  80     -30.577 -30.035 -24.624  1.00 71.26           H  
ATOM    696  N   ARG A  81     -29.584 -29.766 -18.491  1.00 21.99           N  
ANISOU  696  N   ARG A  81     2782   3049   2523    -76      0   -497       N  
ATOM    697  CA  ARG A  81     -28.600 -28.747 -18.141  1.00 20.33           C  
ANISOU  697  CA  ARG A  81     2586   2821   2316    -51     14   -450       C  
ATOM    698  C   ARG A  81     -28.614 -27.690 -19.236  1.00 18.11           C  
ANISOU  698  C   ARG A  81     2328   2632   1922    -80     28   -424       C  
ATOM    699  O   ARG A  81     -28.185 -27.952 -20.366  1.00 37.88           O  
ANISOU  699  O   ARG A  81     4823   5192   4377   -127     65   -492       O  
ATOM    700  CB  ARG A  81     -27.207 -29.342 -17.955  1.00 17.95           C  
ANISOU  700  CB  ARG A  81     2258   2456   2105    -46     54   -514       C  
ATOM    701  CG  ARG A  81     -26.230 -28.382 -17.271  1.00 33.41           C  
ANISOU  701  CG  ARG A  81     4228   4381   4086    -14     62   -460       C  
ATOM    702  CD  ARG A  81     -24.780 -28.800 -17.481  1.00 27.71           C  
ANISOU  702  CD  ARG A  81     3477   3621   3430    -19    108   -534       C  
ATOM    703  NE  ARG A  81     -23.862 -27.700 -17.201  1.00 37.67           N  
ANISOU  703  NE  ARG A  81     4753   4881   4679     -2    125   -491       N  
ATOM    704  CZ  ARG A  81     -22.962 -27.697 -16.223  1.00 36.07           C  
ANISOU  704  CZ  ARG A  81     4533   4610   4562     29    124   -476       C  
ATOM    705  NH1 ARG A  81     -22.841 -28.744 -15.418  1.00 50.69           N1+
ANISOU  705  NH1 ARG A  81     6353   6387   6519     47    101   -490       N1+
ATOM    706  NH2 ARG A  81     -22.179 -26.641 -16.051  1.00 46.95           N  
ANISOU  706  NH2 ARG A  81     5925   5995   5919     39    143   -442       N  
ATOM    707  H   ARG A  81     -29.260 -30.471 -18.862  1.00 27.20           H  
ATOM    708  HE  ARG A  81     -23.906 -27.004 -17.706  1.00 46.02           H  
ATOM    709 HH11 ARG A  81     -23.347 -29.431 -15.527  1.00 61.64           H  
ATOM    710 HH12 ARG A  81     -22.257 -28.737 -14.787  1.00 61.64           H  
ATOM    711 HH21 ARG A  81     -22.254 -25.961 -16.572  1.00 57.16           H  
ATOM    712 HH22 ARG A  81     -21.596 -26.637 -15.419  1.00 57.16           H  
ATOM    713  N   ALA A  82     -29.122 -26.501 -18.915  1.00 24.09           N  
ANISOU  713  N   ALA A  82     3110   3406   2639    -58     -2   -326       N  
ATOM    714  CA  ALA A  82     -29.306 -25.457 -19.912  1.00 22.98           C  
ANISOU  714  CA  ALA A  82     2988   3348   2395    -84     -2   -278       C  
ATOM    715  C   ALA A  82     -29.501 -24.118 -19.216  1.00 17.64           C  
ANISOU  715  C   ALA A  82     2329   2647   1726    -45    -25   -173       C  
ATOM    716  O   ALA A  82     -30.328 -24.005 -18.304  1.00 27.04           O  
ANISOU  716  O   ALA A  82     3517   3800   2956    -12    -60   -129       O  
ATOM    717  CB  ALA A  82     -30.498 -25.763 -20.821  1.00 27.50           C  
ANISOU  717  CB  ALA A  82     3557   4003   2887   -122    -30   -281       C  
ATOM    718  H   ALA A  82     -29.368 -26.275 -18.123  1.00 29.73           H  
ATOM    719  N   GLN A  83     -28.726 -23.123 -19.638  1.00 25.92           N  
ANISOU  719  N   GLN A  83     3393   3716   2740    -52      0   -139       N  
ATOM    720  CA  GLN A  83     -28.793 -21.779 -19.087  1.00 23.26           C  
ANISOU  720  CA  GLN A  83     3069   3352   2416    -20    -11    -47       C  
ATOM    721  C   GLN A  83     -29.808 -20.965 -19.863  1.00 20.67           C  
ANISOU  721  C   GLN A  83     2748   3088   2017    -35    -48     34       C  
ATOM    722  O   GLN A  83     -29.737 -20.879 -21.095  1.00 25.25           O  
ANISOU  722  O   GLN A  83     3335   3748   2510    -82    -43     35       O  
ATOM    723  CB  GLN A  83     -27.426 -21.101 -19.158  1.00 23.78           C  
ANISOU  723  CB  GLN A  83     3146   3404   2487    -22     36    -49       C  
ATOM    724  CG  GLN A  83     -27.359 -19.761 -18.446  1.00 24.30           C  
ANISOU  724  CG  GLN A  83     3220   3428   2586     12     34     33       C  
ATOM    725  CD  GLN A  83     -25.936 -19.292 -18.209  1.00 28.50           C  
ANISOU  725  CD  GLN A  83     3756   3928   3144     15     84     14       C  
ATOM    726  NE2 GLN A  83     -25.776 -17.994 -17.964  1.00 31.70           N  
ANISOU  726  NE2 GLN A  83     4170   4314   3559     30     93     83       N  
ATOM    727  OE1 GLN A  83     -24.992 -20.084 -18.244  1.00 21.84           O  
ANISOU  727  OE1 GLN A  83     2905   3075   2319      5    115    -64       O  
ATOM    728  H   GLN A  83     -28.139 -23.207 -20.260  1.00 31.92           H  
ATOM    729 HE21 GLN A  83     -26.459 -17.473 -17.947  1.00 38.86           H  
ATOM    730 HE22 GLN A  83     -24.989 -17.677 -17.823  1.00 38.86           H  
ATOM    731  N   VAL A  84     -30.760 -20.381 -19.167  1.00 27.23           N  
ANISOU  731  N   VAL A  84     3573   3889   2886      1    -85    100       N  
ATOM    732  CA  VAL A  84     -31.741 -19.521 -19.806  1.00 25.80           C  
ANISOU  732  CA  VAL A  84     3389   3753   2660     -5   -126    188       C  
ATOM    733  C   VAL A  84     -31.195 -18.112 -19.859  1.00 23.67           C  
ANISOU  733  C   VAL A  84     3129   3464   2400      6   -111    266       C  
ATOM    734  O   VAL A  84     -30.790 -17.551 -18.826  1.00 18.87           O  
ANISOU  734  O   VAL A  84     2519   2782   1869     43    -90    275       O  
ATOM    735  CB  VAL A  84     -33.087 -19.576 -19.077  1.00 21.29           C  
ANISOU  735  CB  VAL A  84     2797   3155   2136     26   -172    216       C  
ATOM    736  CG1 VAL A  84     -34.089 -18.672 -19.784  1.00 31.95           C  
ANISOU  736  CG1 VAL A  84     4137   4550   3453     22   -219    312       C  
ATOM    737  CG2 VAL A  84     -33.564 -21.016 -19.019  1.00 34.44           C  
ANISOU  737  CG2 VAL A  84     4454   4836   3794     11   -182    136       C  
ATOM    738  H   VAL A  84     -30.862 -20.467 -18.317  1.00 33.50           H  
ATOM    739  N   TYR A  85     -31.189 -17.520 -21.051  1.00 23.21           N  
ANISOU  739  N   TYR A  85     3080   3475   2263    -31   -122    323       N  
ATOM    740  CA  TYR A  85     -30.723 -16.161 -21.244  1.00 19.17           C  
ANISOU  740  CA  TYR A  85     2578   2948   1759    -27   -111    407       C  
ATOM    741  C   TYR A  85     -31.840 -15.180 -21.565  1.00 27.44           C  
ANISOU  741  C   TYR A  85     3609   4005   2813    -16   -167    525       C  
ATOM    742  O   TYR A  85     -31.598 -13.969 -21.542  1.00 27.70           O  
ANISOU  742  O   TYR A  85     3641   4001   2881     -2   -162    605       O  
ATOM    743  CB  TYR A  85     -29.649 -16.114 -22.348  1.00 35.00           C  
ANISOU  743  CB  TYR A  85     4607   5018   3674    -84    -75    391       C  
ATOM    744  CG  TYR A  85     -30.076 -16.476 -23.764  1.00 20.66           C  
ANISOU  744  CG  TYR A  85     2794   3320   1736   -152   -103    404       C  
ATOM    745  CD1 TYR A  85     -30.613 -15.518 -24.618  1.00 21.47           C  
ANISOU  745  CD1 TYR A  85     2897   3477   1784   -178   -146    524       C  
ATOM    746  CD2 TYR A  85     -29.890 -17.763 -24.264  1.00 20.81           C  
ANISOU  746  CD2 TYR A  85     2812   3398   1696   -196    -84    297       C  
ATOM    747  CE1 TYR A  85     -30.981 -15.839 -25.921  1.00 27.40           C  
ANISOU  747  CE1 TYR A  85     3650   4350   2410   -252   -174    541       C  
ATOM    748  CE2 TYR A  85     -30.250 -18.090 -25.564  1.00 25.42           C  
ANISOU  748  CE2 TYR A  85     3396   4101   2161   -269   -103    299       C  
ATOM    749  CZ  TYR A  85     -30.795 -17.127 -26.388  1.00 34.86           C  
ANISOU  749  CZ  TYR A  85     4595   5362   3289   -300   -150    422       C  
ATOM    750  OH  TYR A  85     -31.158 -17.461 -27.675  1.00 36.46           O  
ANISOU  750  OH  TYR A  85     4795   5696   3361   -383   -173    427       O  
ATOM    751  H   TYR A  85     -31.458 -17.898 -21.776  1.00 28.67           H  
ATOM    752  HH  TYR A  85     -30.989 -18.271 -27.821  1.00 44.57           H  
ATOM    753  N   GLY A  86     -33.059 -15.653 -21.816  1.00 19.92           N  
ANISOU  753  N   GLY A  86     2638   3092   1840    -19   -221    539       N  
ATOM    754  CA  GLY A  86     -34.149 -14.738 -22.095  1.00 20.48           C  
ANISOU  754  CA  GLY A  86     2683   3166   1932     -5   -280    654       C  
ATOM    755  C   GLY A  86     -35.491 -15.434 -22.112  1.00 25.75           C  
ANISOU  755  C   GLY A  86     3324   3867   2593     -1   -334    644       C  
ATOM    756  O   GLY A  86     -35.583 -16.665 -22.148  1.00 32.45           O  
ANISOU  756  O   GLY A  86     4179   4753   3399    -22   -327    553       O  
ATOM    757  H   GLY A  86     -33.272 -16.486 -21.828  1.00 19.82           H  
ATOM    758  N   LEU A  87     -36.535 -14.607 -22.104  1.00 30.67           N  
ANISOU  758  N   LEU A  87     3914   4472   3268     25   -387    741       N  
ATOM    759  CA  LEU A  87     -37.913 -15.058 -22.006  1.00 28.41           C  
ANISOU  759  CA  LEU A  87     3594   4204   2996     36   -442    743       C  
ATOM    760  C   LEU A  87     -38.807 -14.196 -22.874  1.00 25.55           C  
ANISOU  760  C   LEU A  87     3200   3883   2623     29   -513    875       C  
ATOM    761  O   LEU A  87     -38.635 -12.970 -22.911  1.00 25.53           O  
ANISOU  761  O   LEU A  87     3187   3834   2681     49   -520    971       O  
ATOM    762  CB  LEU A  87     -38.432 -14.956 -20.576  1.00 26.96           C  
ANISOU  762  CB  LEU A  87     3383   3919   2941     94   -429    707       C  
ATOM    763  CG  LEU A  87     -37.656 -15.604 -19.444  1.00 21.60           C  
ANISOU  763  CG  LEU A  87     2726   3182   2300    109   -367    599       C  
ATOM    764  CD1 LEU A  87     -38.290 -15.165 -18.142  1.00 22.85           C  
ANISOU  764  CD1 LEU A  87     2850   3252   2580    154   -362    591       C  
ATOM    765  CD2 LEU A  87     -37.697 -17.096 -19.611  1.00 30.89           C  
ANISOU  765  CD2 LEU A  87     3918   4411   3407     79   -364    505       C  
ATOM    766  H   LEU A  87     -36.465 -13.751 -22.157  1.00 37.63           H  
ATOM    767  N   ASP A  88     -39.802 -14.808 -23.526  1.00 41.04           N  
ANISOU  767  N   ASP A  88     5143   5930   4522      2   -570    882       N  
ATOM    768  CA  ASP A  88     -40.890 -14.081 -24.180  1.00 33.49           C  
ANISOU  768  CA  ASP A  88     4144   5008   3574      2   -652   1009       C  
ATOM    769  C   ASP A  88     -42.181 -14.439 -23.470  1.00 37.23           C  
ANISOU  769  C   ASP A  88     4572   5447   4126     42   -685    979       C  
ATOM    770  O   ASP A  88     -42.656 -15.591 -23.576  1.00 24.26           O  
ANISOU  770  O   ASP A  88     2932   3865   2422     17   -693    897       O  
ATOM    771  CB  ASP A  88     -40.948 -14.394 -25.681  1.00 44.91           C  
ANISOU  771  CB  ASP A  88     5600   6600   4863    -77   -696   1056       C  
ATOM    772  CG  ASP A  88     -41.851 -13.433 -26.456  1.00 52.42           C  
ANISOU  772  CG  ASP A  88     6508   7590   5821    -82   -787   1218       C  
ATOM    773  OD1 ASP A  88     -42.746 -12.824 -25.824  1.00 57.76           O1-
ANISOU  773  OD1 ASP A  88     7135   8184   6628    -21   -823   1271       O1-
ATOM    774  OD2 ASP A  88     -41.677 -13.287 -27.684  1.00 46.51           O1-
ANISOU  774  OD2 ASP A  88     5769   6952   4949   -151   -823   1294       O1-
ATOM    775  H   ASP A  88     -39.867 -15.662 -23.603  1.00 50.07           H  
ATOM    776  N   LEU A  89     -42.761 -13.475 -22.736  1.00 37.87           N  
ANISOU  776  N   LEU A  89     4609   5430   4350    100   -700   1035       N  
ATOM    777  CA  LEU A  89     -43.900 -13.669 -21.853  1.00 29.32           C  
ANISOU  777  CA  LEU A  89     3478   4295   3366    142   -718    996       C  
ATOM    778  C   LEU A  89     -45.169 -13.001 -22.381  1.00 47.30           C  
ANISOU  778  C   LEU A  89     5690   6587   5693    156   -804   1109       C  
ATOM    779  O   LEU A  89     -46.142 -12.817 -21.638  1.00 53.30           O  
ANISOU  779  O   LEU A  89     6397   7285   6568    198   -819   1095       O  
ATOM    780  CB  LEU A  89     -43.584 -13.122 -20.460  1.00 25.28           C  
ANISOU  780  CB  LEU A  89     2957   3655   2994    193   -657    949       C  
ATOM    781  CG  LEU A  89     -42.366 -13.710 -19.762  1.00 34.60           C  
ANISOU  781  CG  LEU A  89     4193   4809   4146    185   -576    844       C  
ATOM    782  CD1 LEU A  89     -41.904 -12.817 -18.631  1.00 33.07           C  
ANISOU  782  CD1 LEU A  89     3986   4501   4078    224   -522    832       C  
ATOM    783  CD2 LEU A  89     -42.717 -15.086 -19.244  1.00 39.34           C  
ANISOU  783  CD2 LEU A  89     4804   5434   4708    172   -564    728       C  
ATOM    784  H   LEU A  89     -42.489 -12.659 -22.739  1.00 46.26           H  
ATOM    785  N   SER A  90     -45.137 -12.651 -23.672  1.00 56.19           N  
ANISOU  785  N   SER A  90     6818   7801   6732    117   -861   1220       N  
ATOM    786  CA  SER A  90     -46.101 -11.819 -24.378  1.00 48.81           C  
ANISOU  786  CA  SER A  90     5822   6885   5837    123   -952   1366       C  
ATOM    787  C   SER A  90     -47.405 -12.519 -24.687  1.00 53.77           C  
ANISOU  787  C   SER A  90     6409   7589   6434    111  -1019   1355       C  
ATOM    788  O   SER A  90     -48.400 -11.851 -25.005  1.00 69.43           O  
ANISOU  788  O   SER A  90     8324   9567   8488    132  -1098   1464       O  
ATOM    789  CB  SER A  90     -45.480 -11.415 -25.715  1.00 53.48           C  
ANISOU  789  CB  SER A  90     6441   7571   6307     64   -988   1481       C  
ATOM    790  OG  SER A  90     -45.030 -12.587 -26.404  1.00 68.47           O  
ANISOU  790  OG  SER A  90     8391   9598   8025     -9   -970   1401       O  
ATOM    791  H   SER A  90     -44.511 -12.907 -24.203  1.00 68.25           H  
ATOM    792  HG  SER A  90     -44.683 -12.374 -27.139  1.00 82.98           H  
ATOM    793  N   GLU A  91     -47.393 -13.832 -24.723  1.00 49.44           N  
ANISOU  793  N   GLU A  91     5894   7115   5776     74   -994   1236       N  
ATOM    794  CA  GLU A  91     -48.535 -14.627 -25.141  1.00 48.95           C  
ANISOU  794  CA  GLU A  91     5798   7142   5657     49  -1052   1215       C  
ATOM    795  C   GLU A  91     -48.724 -15.791 -24.192  1.00 33.05           C  
ANISOU  795  C   GLU A  91     3801   5101   3654     59   -996   1052       C  
ATOM    796  O   GLU A  91     -47.843 -16.111 -23.386  1.00 36.18           O  
ANISOU  796  O   GLU A  91     4242   5433   4071     72   -916    960       O  
ATOM    797  CB  GLU A  91     -48.337 -15.100 -26.587  1.00 52.66           C  
ANISOU  797  CB  GLU A  91     6292   7774   5942    -37  -1092   1254       C  
ATOM    798  CG  GLU A  91     -48.429 -13.957 -27.600  1.00 57.71           C  
ANISOU  798  CG  GLU A  91     6904   8458   6566    -56  -1171   1439       C  
ATOM    799  CD  GLU A  91     -47.901 -14.344 -28.961  1.00 73.44           C  
ANISOU  799  CD  GLU A  91     8933  10611   8360   -155  -1190   1470       C  
ATOM    800  OE1 GLU A  91     -47.579 -13.444 -29.768  1.00 83.07           O  
ANISOU  800  OE1 GLU A  91    10155  11850   9558   -182  -1217   1591       O  
ATOM    801  OE2 GLU A  91     -47.805 -15.561 -29.224  1.00 78.61           O1-
ANISOU  801  OE2 GLU A  91     9617  11356   8897   -209  -1158   1348       O1-
ATOM    802  H   GLU A  91     -46.711 -14.305 -24.501  1.00 60.15           H  
ATOM    803  N   PRO A  92     -49.882 -16.454 -24.267  1.00 33.48           N  
ANISOU  803  N   PRO A  92     3818   5207   3697     51  -1039   1018       N  
ATOM    804  CA  PRO A  92     -50.211 -17.502 -23.281  1.00 30.32           C  
ANISOU  804  CA  PRO A  92     3425   4770   3325     62   -991    873       C  
ATOM    805  C   PRO A  92     -49.190 -18.618 -23.178  1.00 29.71           C  
ANISOU  805  C   PRO A  92     3418   4717   3155     24   -918    755       C  
ATOM    806  O   PRO A  92     -48.935 -19.110 -22.070  1.00 34.56           O  
ANISOU  806  O   PRO A  92     4051   5252   3827     47   -858    657       O  
ATOM    807  CB  PRO A  92     -51.561 -18.035 -23.786  1.00 25.49           C  
ANISOU  807  CB  PRO A  92     2763   4244   2678     40  -1060    874       C  
ATOM    808  CG  PRO A  92     -52.121 -16.939 -24.638  1.00 30.22           C  
ANISOU  808  CG  PRO A  92     3308   4878   3297     46  -1149   1034       C  
ATOM    809  CD  PRO A  92     -50.959 -16.235 -25.247  1.00 29.78           C  
ANISOU  809  CD  PRO A  92     3292   4831   3191     28  -1138   1118       C  
ATOM    810  N   VAL A  93     -48.634 -19.069 -24.296  1.00 25.98           N  
ANISOU  810  N   VAL A  93     2978   4353   2542    -39   -922    757       N  
ATOM    811  CA  VAL A  93     -47.504 -19.988 -24.260  1.00 34.03           C  
ANISOU  811  CA  VAL A  93     4057   5382   3490    -73   -847    650       C  
ATOM    812  C   VAL A  93     -46.244 -19.157 -24.052  1.00 45.62           C  
ANISOU  812  C   VAL A  93     5561   6785   4989    -53   -804    690       C  
ATOM    813  O   VAL A  93     -45.942 -18.257 -24.845  1.00 39.07           O  
ANISOU  813  O   VAL A  93     4729   5992   4123    -68   -834    799       O  
ATOM    814  CB  VAL A  93     -47.414 -20.833 -25.537  1.00 34.09           C  
ANISOU  814  CB  VAL A  93     4078   5534   3340   -157   -859    617       C  
ATOM    815  CG1 VAL A  93     -46.115 -21.637 -25.558  1.00 28.41           C  
ANISOU  815  CG1 VAL A  93     3414   4815   2567   -190   -778    511       C  
ATOM    816  CG2 VAL A  93     -48.604 -21.773 -25.636  1.00 34.90           C  
ANISOU  816  CG2 VAL A  93     4148   5696   3418   -178   -891    555       C  
ATOM    817  H   VAL A  93     -48.894 -18.859 -25.089  1.00 32.00           H  
ATOM    818  N   LYS A  94     -45.534 -19.433 -22.964  1.00 43.29           N  
ANISOU  818  N   LYS A  94     5294   6393   4761    -21   -735    610       N  
ATOM    819  CA  LYS A  94     -44.306 -18.736 -22.621  1.00 47.77           C  
ANISOU  819  CA  LYS A  94     5894   6893   5362     -1   -686    630       C  
ATOM    820  C   LYS A  94     -43.135 -19.388 -23.344  1.00 52.77           C  
ANISOU  820  C   LYS A  94     6575   7589   5886    -55   -642    575       C  
ATOM    821  O   LYS A  94     -43.061 -20.614 -23.449  1.00 53.58           O  
ANISOU  821  O   LYS A  94     6691   7730   5936    -89   -617    471       O  
ATOM    822  CB  LYS A  94     -44.082 -18.770 -21.107  1.00 38.24           C  
ANISOU  822  CB  LYS A  94     4692   5566   4272     50   -635    566       C  
ATOM    823  CG  LYS A  94     -45.334 -18.511 -20.271  1.00 31.44           C  
ANISOU  823  CG  LYS A  94     3780   4651   3514     90   -664    574       C  
ATOM    824  CD  LYS A  94     -45.900 -17.131 -20.534  1.00 41.99           C  
ANISOU  824  CD  LYS A  94     5071   5965   4920    121   -713    696       C  
ATOM    825  CE  LYS A  94     -47.268 -16.949 -19.907  1.00 32.19           C  
ANISOU  825  CE  LYS A  94     3768   4686   3777    154   -748    697       C  
ATOM    826  NZ  LYS A  94     -47.906 -15.721 -20.455  1.00 34.58           N1+
ANISOU  826  NZ  LYS A  94     4016   4980   4141    177   -810    825       N1+
ATOM    827  H   LYS A  94     -45.752 -20.038 -22.393  1.00 52.77           H  
ATOM    828  HZ1 LYS A  94     -48.710 -15.606 -20.091  1.00 42.31           H  
ATOM    829  HZ2 LYS A  94     -47.403 -15.009 -20.273  1.00 42.31           H  
ATOM    830  HZ3 LYS A  94     -47.996 -15.793 -21.337  1.00 42.31           H  
ATOM    831  N   LYS A  95     -42.233 -18.558 -23.859  1.00 50.28           N  
ANISOU  831  N   LYS A  95     6281   7282   5543    -67   -630    641       N  
ATOM    832  CA  LYS A  95     -41.054 -19.021 -24.577  1.00 46.74           C  
ANISOU  832  CA  LYS A  95     5873   6891   4995   -122   -583    591       C  
ATOM    833  C   LYS A  95     -39.821 -18.767 -23.721  1.00 45.19           C  
ANISOU  833  C   LYS A  95     5707   6596   4867    -88   -515    553       C  
ATOM    834  O   LYS A  95     -39.653 -17.673 -23.176  1.00 34.87           O  
ANISOU  834  O   LYS A  95     4395   5213   3642    -43   -513    624       O  
ATOM    835  CB  LYS A  95     -40.903 -18.312 -25.927  1.00 49.99           C  
ANISOU  835  CB  LYS A  95     6286   7404   5303   -177   -621    694       C  
ATOM    836  CG  LYS A  95     -41.668 -18.954 -27.082  1.00 50.69           C  
ANISOU  836  CG  LYS A  95     6357   7636   5267   -249   -669    693       C  
ATOM    837  CD  LYS A  95     -43.042 -18.316 -27.267  1.00 61.29           C  
ANISOU  837  CD  LYS A  95     7651   8999   6638   -229   -760    808       C  
ATOM    838  CE  LYS A  95     -43.562 -18.465 -28.694  1.00 57.26           C  
ANISOU  838  CE  LYS A  95     7123   8651   5982   -314   -820    863       C  
ATOM    839  NZ  LYS A  95     -45.026 -18.740 -28.710  1.00 65.85           N1+
ANISOU  839  NZ  LYS A  95     8161   9775   7085   -304   -890    883       N1+
ATOM    840  H   LYS A  95     -42.286 -17.702 -23.804  1.00 61.16           H  
ATOM    841  HZ1 LYS A  95     -45.311 -18.822 -29.549  1.00 79.84           H  
ATOM    842  HZ2 LYS A  95     -45.198 -19.495 -28.272  1.00 79.84           H  
ATOM    843  HZ3 LYS A  95     -45.465 -18.073 -28.318  1.00 79.84           H  
ATOM    844  N   VAL A  96     -38.965 -19.779 -23.610  1.00 26.43           N  
ANISOU  844  N   VAL A  96     3358   4220   2463   -111   -457    439       N  
ATOM    845  CA  VAL A  96     -37.775 -19.726 -22.768  1.00 22.62           C  
ANISOU  845  CA  VAL A  96     2901   3651   2044    -81   -394    392       C  
ATOM    846  C   VAL A  96     -36.566 -19.973 -23.660  1.00 29.33           C  
ANISOU  846  C   VAL A  96     3778   4558   2808   -136   -350    351       C  
ATOM    847  O   VAL A  96     -36.396 -21.084 -24.187  1.00 30.40           O  
ANISOU  847  O   VAL A  96     3917   4751   2884   -183   -329    258       O  
ATOM    848  CB  VAL A  96     -37.843 -20.748 -21.627  1.00 19.75           C  
ANISOU  848  CB  VAL A  96     2535   3217   1752    -53   -368    293       C  
ATOM    849  CG1 VAL A  96     -36.582 -20.693 -20.798  1.00 30.63           C  
ANISOU  849  CG1 VAL A  96     3935   4514   3190    -28   -309    252       C  
ATOM    850  CG2 VAL A  96     -39.067 -20.496 -20.762  1.00 31.90           C  
ANISOU  850  CG2 VAL A  96     4044   4707   3368     -9   -407    326       C  
ATOM    851  H   VAL A  96     -39.055 -20.526 -24.026  1.00 32.53           H  
ATOM    852  N   TYR A  97     -35.709 -18.958 -23.807  1.00 26.61           N  
ANISOU  852  N   TYR A  97     3451   4195   2465   -133   -329    410       N  
ATOM    853  CA  TYR A  97     -34.557 -19.012 -24.704  1.00 21.50           C  
ANISOU  853  CA  TYR A  97     2828   3608   1734   -190   -286    381       C  
ATOM    854  C   TYR A  97     -33.343 -19.595 -23.995  1.00 27.78           C  
ANISOU  854  C   TYR A  97     3639   4334   2583   -174   -216    276       C  
ATOM    855  O   TYR A  97     -32.924 -19.080 -22.945  1.00 35.50           O  
ANISOU  855  O   TYR A  97     4620   5214   3654   -118   -196    291       O  
ATOM    856  CB  TYR A  97     -34.234 -17.614 -25.241  1.00 22.05           C  
ANISOU  856  CB  TYR A  97     2908   3692   1778   -200   -299    502       C  
ATOM    857  CG  TYR A  97     -35.284 -17.098 -26.190  1.00 33.65           C  
ANISOU  857  CG  TYR A  97     4359   5249   3178   -233   -373    614       C  
ATOM    858  CD1 TYR A  97     -35.221 -17.384 -27.547  1.00 29.68           C  
ANISOU  858  CD1 TYR A  97     3861   4881   2534   -322   -385    617       C  
ATOM    859  CD2 TYR A  97     -36.359 -16.354 -25.728  1.00 37.38           C  
ANISOU  859  CD2 TYR A  97     4802   5672   3728   -180   -432    712       C  
ATOM    860  CE1 TYR A  97     -36.195 -16.932 -28.417  1.00 38.10           C  
ANISOU  860  CE1 TYR A  97     4908   6036   3531   -358   -460    728       C  
ATOM    861  CE2 TYR A  97     -37.333 -15.895 -26.590  1.00 38.37           C  
ANISOU  861  CE2 TYR A  97     4904   5875   3801   -208   -507    821       C  
ATOM    862  CZ  TYR A  97     -37.248 -16.188 -27.933  1.00 34.98           C  
ANISOU  862  CZ  TYR A  97     4483   5585   3224   -297   -525    834       C  
ATOM    863  OH  TYR A  97     -38.221 -15.732 -28.793  1.00 47.31           O  
ANISOU  863  OH  TYR A  97     6017   7231   4726   -330   -607    953       O  
ATOM    864  H   TYR A  97     -35.778 -18.211 -23.388  1.00 32.75           H  
ATOM    865  HH  TYR A  97     -38.800 -15.299 -28.368  1.00 57.59           H  
ATOM    866  N   THR A  98     -32.782 -20.660 -24.563  1.00 24.37           N  
ANISOU  866  N   THR A  98     3210   3951   2097   -224   -177    169       N  
ATOM    867  CA  THR A  98     -31.522 -21.255 -24.152  1.00 28.36           C  
ANISOU  867  CA  THR A  98     3724   4405   2648   -220   -111     69       C  
ATOM    868  C   THR A  98     -30.664 -21.560 -25.369  1.00 27.62           C  
ANISOU  868  C   THR A  98     3636   4400   2457   -300    -67      6       C  
ATOM    869  O   THR A  98     -31.168 -21.637 -26.497  1.00 24.09           O  
ANISOU  869  O   THR A  98     3186   4066   1902   -366    -88     18       O  
ATOM    870  CB  THR A  98     -31.700 -22.562 -23.360  1.00 22.22           C  
ANISOU  870  CB  THR A  98     2929   3569   1944   -196   -100    -31       C  
ATOM    871  CG2 THR A  98     -32.880 -22.495 -22.420  1.00 20.08           C  
ANISOU  871  CG2 THR A  98     2647   3248   1736   -143   -151     18       C  
ATOM    872  OG1 THR A  98     -31.877 -23.661 -24.267  1.00 25.09           O  
ANISOU  872  OG1 THR A  98     3279   4010   2243   -257    -88   -122       O  
ATOM    873  H   THR A  98     -33.137 -21.075 -25.228  1.00 30.06           H  
ATOM    874  HG1 THR A  98     -32.556 -23.534 -24.744  1.00 30.92           H  
ATOM    875  N   PRO A  99     -29.355 -21.763 -25.166  1.00 34.44           N  
ANISOU  875  N   PRO A  99     4505   5222   3358   -300     -5    -67       N  
ATOM    876  CA  PRO A  99     -28.494 -22.264 -26.252  1.00 37.50           C  
ANISOU  876  CA  PRO A  99     4891   5689   3669   -380     50   -159       C  
ATOM    877  C   PRO A  99     -28.858 -23.659 -26.727  1.00 43.88           C  
ANISOU  877  C   PRO A  99     5673   6544   4457   -425     63   -278       C  
ATOM    878  O   PRO A  99     -28.575 -24.007 -27.878  1.00 46.70           O  
ANISOU  878  O   PRO A  99     6022   7003   4718   -512     96   -344       O  
ATOM    879  CB  PRO A  99     -27.090 -22.252 -25.622  1.00 37.71           C  
ANISOU  879  CB  PRO A  99     4919   5631   3777   -350    109   -216       C  
ATOM    880  CG  PRO A  99     -27.189 -21.324 -24.464  1.00 35.56           C  
ANISOU  880  CG  PRO A  99     4660   5265   3587   -271     82   -119       C  
ATOM    881  CD  PRO A  99     -28.587 -21.474 -23.945  1.00 40.19           C  
ANISOU  881  CD  PRO A  99     5238   5834   4198   -233     20    -67       C  
ATOM    882  N   GLU A 100     -29.404 -24.495 -25.843  1.00 47.74           N  
ANISOU  882  N   GLU A 100     6145   6958   5037   -375     47   -316       N  
ATOM    883  CA  GLU A 100     -29.882 -25.823 -26.215  1.00 43.93           C  
ANISOU  883  CA  GLU A 100     5635   6508   4550   -413     57   -424       C  
ATOM    884  C   GLU A 100     -31.185 -25.769 -27.013  1.00 46.72           C  
ANISOU  884  C   GLU A 100     5984   6971   4796   -459      5   -379       C  
ATOM    885  O   GLU A 100     -31.675 -26.825 -27.430  1.00 41.15           O  
ANISOU  885  O   GLU A 100     5254   6308   4072   -500     13   -469       O  
ATOM    886  CB  GLU A 100     -30.025 -26.704 -24.966  1.00 57.26           C  
ANISOU  886  CB  GLU A 100     7306   8075   6375   -346     53   -467       C  
ATOM    887  CG  GLU A 100     -28.726 -26.879 -24.125  1.00 70.15           C  
ANISOU  887  CG  GLU A 100     8934   9599   8121   -302     97   -511       C  
ATOM    888  CD  GLU A 100     -27.927 -28.142 -24.468  1.00 87.07           C  
ANISOU  888  CD  GLU A 100    11042  11724  10317   -338    158   -660       C  
ATOM    889  OE1 GLU A 100     -26.969 -28.480 -23.732  1.00 87.52           O  
ANISOU  889  OE1 GLU A 100    11084  11685  10484   -299    186   -699       O  
ATOM    890  OE2 GLU A 100     -28.256 -28.793 -25.480  1.00 95.24           O1-
ANISOU  890  OE2 GLU A 100    12058  12841  11287   -407    179   -740       O1-
ATOM    891  H   GLU A 100     -29.510 -24.312 -25.009  1.00 58.11           H  
ATOM    892  N   GLY A 101     -31.777 -24.586 -27.183  1.00 48.84           N  
ANISOU  892  N   GLY A 101     6272   7279   5007   -449    -50   -242       N  
ATOM    893  CA  GLY A 101     -33.003 -24.399 -27.933  1.00 32.52           C  
ANISOU  893  CA  GLY A 101     4197   5317   2842   -490   -109   -178       C  
ATOM    894  C   GLY A 101     -34.014 -23.558 -27.181  1.00 32.50           C  
ANISOU  894  C   GLY A 101     4198   5262   2887   -418   -180    -47       C  
ATOM    895  O   GLY A 101     -33.771 -23.074 -26.078  1.00 41.18           O  
ANISOU  895  O   GLY A 101     5307   6250   4090   -342   -180     -7       O  
ATOM    896  H   GLY A 101     -31.469 -23.852 -26.857  1.00 59.43           H  
ATOM    897  N   ILE A 102     -35.183 -23.399 -27.807  1.00 31.81           N  
ANISOU  897  N   ILE A 102     4097   5264   2725   -448   -241     15       N  
ATOM    898  CA  ILE A 102     -36.307 -22.668 -27.228  1.00 26.71           C  
ANISOU  898  CA  ILE A 102     3442   4580   2127   -387   -313    132       C  
ATOM    899  C   ILE A 102     -37.285 -23.668 -26.630  1.00 34.09           C  
ANISOU  899  C   ILE A 102     4355   5485   3114   -362   -331     69       C  
ATOM    900  O   ILE A 102     -37.829 -24.520 -27.343  1.00 23.42           O  
ANISOU  900  O   ILE A 102     2986   4222   1692   -420   -337      6       O  
ATOM    901  CB  ILE A 102     -37.029 -21.796 -28.263  1.00 31.38           C  
ANISOU  901  CB  ILE A 102     4025   5283   2614   -433   -379    256       C  
ATOM    902  CG1 ILE A 102     -36.074 -20.778 -28.863  1.00 34.39           C  
ANISOU  902  CG1 ILE A 102     4431   5694   2943   -464   -363    329       C  
ATOM    903  CG2 ILE A 102     -38.246 -21.122 -27.622  1.00 27.73           C  
ANISOU  903  CG2 ILE A 102     3542   4770   2225   -365   -451    365       C  
ATOM    904  CD1 ILE A 102     -36.582 -20.202 -30.155  1.00 38.06           C  
ANISOU  904  CD1 ILE A 102     4887   6299   3274   -541   -419    432       C  
ATOM    905  H   ILE A 102     -35.351 -23.714 -28.591  1.00 38.99           H  
ATOM    906  N   PHE A 103     -37.529 -23.532 -25.336  1.00 29.49           N  
ANISOU  906  N   PHE A 103     3771   4783   2650   -282   -338     86       N  
ATOM    907  CA  PHE A 103     -38.493 -24.342 -24.616  1.00 22.02           C  
ANISOU  907  CA  PHE A 103     2805   3797   1763   -253   -358     41       C  
ATOM    908  C   PHE A 103     -39.771 -23.560 -24.441  1.00 23.52           C  
ANISOU  908  C   PHE A 103     2975   3995   1967   -222   -429    147       C  
ATOM    909  O   PHE A 103     -39.733 -22.340 -24.172  1.00 34.14           O  
ANISOU  909  O   PHE A 103     4322   5301   3347   -183   -450    251       O  
ATOM    910  CB  PHE A 103     -37.928 -24.766 -23.266  1.00 23.61           C  
ANISOU  910  CB  PHE A 103     3016   3870   2083   -197   -319    -12       C  
ATOM    911  CG  PHE A 103     -36.800 -25.728 -23.374  1.00 26.42           C  
ANISOU  911  CG  PHE A 103     3380   4209   2449   -223   -255   -124       C  
ATOM    912  CD1 PHE A 103     -35.513 -25.283 -23.614  1.00 20.51           C  
ANISOU  912  CD1 PHE A 103     2650   3452   1691   -232   -212   -128       C  
ATOM    913  CD2 PHE A 103     -37.028 -27.087 -23.255  1.00 26.21           C  
ANISOU  913  CD2 PHE A 103     3338   4171   2448   -241   -236   -229       C  
ATOM    914  CE1 PHE A 103     -34.469 -26.177 -23.719  1.00 25.79           C  
ANISOU  914  CE1 PHE A 103     3317   4100   2382   -255   -152   -237       C  
ATOM    915  CE2 PHE A 103     -35.989 -27.988 -23.358  1.00 21.06           C  
ANISOU  915  CE2 PHE A 103     2683   3492   1825   -264   -177   -335       C  
ATOM    916  CZ  PHE A 103     -34.708 -27.534 -23.590  1.00 20.58           C  
ANISOU  916  CZ  PHE A 103     2637   3422   1759   -270   -135   -340       C  
ATOM    917  H   PHE A 103     -37.133 -22.956 -24.835  1.00 36.20           H  
ATOM    918  N   THR A 104     -40.910 -24.251 -24.551  1.00 24.14           N  
ANISOU  918  N   THR A 104     3029   4114   2030   -236   -463    118       N  
ATOM    919  CA  THR A 104     -42.235 -23.672 -24.423  1.00 29.69           C  
ANISOU  919  CA  THR A 104     3701   4828   2750   -210   -532    203       C  
ATOM    920  C   THR A 104     -42.932 -24.233 -23.220  1.00 27.72           C  
ANISOU  920  C   THR A 104     3440   4495   2599   -163   -532    156       C  
ATOM    921  O   THR A 104     -42.802 -25.446 -22.923  1.00 31.17           O  
ANISOU  921  O   THR A 104     3882   4914   3048   -179   -496     48       O  
ATOM    922  CB  THR A 104     -43.062 -23.958 -25.705  1.00 39.39           C  
ANISOU  922  CB  THR A 104     4906   6199   3861   -278   -578    215       C  
ATOM    923  CG2 THR A 104     -42.432 -23.312 -26.921  1.00 39.94           C  
ANISOU  923  CG2 THR A 104     4988   6367   3822   -336   -585    277       C  
ATOM    924  OG1 THR A 104     -43.141 -25.369 -25.910  1.00 51.08           O  
ANISOU  924  OG1 THR A 104     6384   7717   5308   -323   -545     85       O  
ATOM    925  H   THR A 104     -40.933 -25.096 -24.707  1.00 29.79           H  
ATOM    926  HG1 THR A 104     -43.591 -25.533 -26.601  1.00 62.12           H  
ATOM    927  N   GLY A 105     -43.654 -23.406 -22.478  1.00 27.88           N  
ANISOU  927  N   GLY A 105     3440   4457   2697   -110   -567    229       N  
ATOM    928  CA  GLY A 105     -44.472 -23.860 -21.388  1.00 30.37           C  
ANISOU  928  CA  GLY A 105     3738   4708   3095    -77   -572    189       C  
ATOM    929  C   GLY A 105     -45.789 -23.124 -21.327  1.00 23.09           C  
ANISOU  929  C   GLY A 105     2772   3795   2206    -52   -635    265       C  
ATOM    930  O   GLY A 105     -45.864 -21.929 -21.620  1.00 38.05           O  
ANISOU  930  O   GLY A 105     4651   5690   4115    -32   -666    367       O  
ATOM    931  H   GLY A 105     -43.683 -22.555 -22.596  1.00 34.28           H  
ATOM    932  N   ARG A 106     -46.842 -23.856 -20.945  1.00 28.04           N  
ANISOU  932  N   ARG A 106     3375   4426   2854    -54   -652    214       N  
ATOM    933  CA  ARG A 106     -48.119 -23.232 -20.613  1.00 41.89           C  
ANISOU  933  CA  ARG A 106     5081   6168   4669    -23   -704    268       C  
ATOM    934  C   ARG A 106     -48.037 -22.530 -19.265  1.00 41.12           C  
ANISOU  934  C   ARG A 106     4976   5954   4692     30   -679    280       C  
ATOM    935  O   ARG A 106     -48.778 -21.570 -19.010  1.00 46.13           O  
ANISOU  935  O   ARG A 106     5569   6561   5399     64   -713    344       O  
ATOM    936  CB  ARG A 106     -49.218 -24.297 -20.607  1.00 52.23           C  
ANISOU  936  CB  ARG A 106     6367   7519   5959    -48   -722    197       C  
ATOM    937  CG  ARG A 106     -49.390 -25.050 -21.928  1.00 54.34           C  
ANISOU  937  CG  ARG A 106     6633   7910   6104   -111   -743    171       C  
ATOM    938  CD  ARG A 106     -50.189 -26.347 -21.728  1.00 57.17           C  
ANISOU  938  CD  ARG A 106     6979   8289   6453   -139   -737     69       C  
ATOM    939  NE  ARG A 106     -51.593 -26.089 -21.400  1.00 66.60           N  
ANISOU  939  NE  ARG A 106     8124   9486   7696   -119   -787     94       N  
ATOM    940  CZ  ARG A 106     -52.319 -26.783 -20.523  1.00 55.06           C  
ANISOU  940  CZ  ARG A 106     6650   7981   6290   -113   -774     24       C  
ATOM    941  NH1 ARG A 106     -51.792 -27.802 -19.854  1.00 45.23           N1+
ANISOU  941  NH1 ARG A 106     5439   6683   5062   -125   -718    -67       N1+
ATOM    942  NH2 ARG A 106     -53.586 -26.449 -20.310  1.00 50.25           N  
ANISOU  942  NH2 ARG A 106     5989   7379   5723    -96   -821     48       N  
ATOM    943  H   ARG A 106     -46.840 -24.713 -20.871  1.00 34.47           H  
ATOM    944  HE  ARG A 106     -51.980 -25.437 -21.806  1.00 80.74           H  
ATOM    945 HH11 ARG A 106     -50.972 -28.024 -19.984  1.00 55.09           H  
ATOM    946 HH12 ARG A 106     -52.272 -28.242 -19.290  1.00 55.09           H  
ATOM    947 HH21 ARG A 106     -53.934 -25.789 -20.738  1.00 61.11           H  
ATOM    948 HH22 ARG A 106     -54.059 -26.892 -19.745  1.00 61.11           H  
ATOM    949  N   ALA A 107     -47.124 -22.980 -18.408  1.00 28.32           N  
ANISOU  949  N   ALA A 107     3393   4269   3100     35   -621    219       N  
ATOM    950  CA  ALA A 107     -46.768 -22.309 -17.172  1.00 22.06           C  
ANISOU  950  CA  ALA A 107     2600   3378   2403     73   -588    226       C  
ATOM    951  C   ALA A 107     -45.251 -22.241 -17.073  1.00 20.51           C  
ANISOU  951  C   ALA A 107     2450   3151   2193     73   -539    219       C  
ATOM    952  O   ALA A 107     -44.545 -23.165 -17.494  1.00 19.40           O  
ANISOU  952  O   ALA A 107     2341   3039   1992     43   -516    167       O  
ATOM    953  CB  ALA A 107     -47.337 -23.031 -15.948  1.00 21.02           C  
ANISOU  953  CB  ALA A 107     2460   3199   2328     72   -569    152       C  
ATOM    954  H   ALA A 107     -46.679 -23.706 -18.532  1.00 34.80           H  
ATOM    955  N   LEU A 108     -44.761 -21.140 -16.516  1.00 18.32           N  
ANISOU  955  N   LEU A 108     2168   2812   1979    104   -520    265       N  
ATOM    956  CA  LEU A 108     -43.338 -20.893 -16.349  1.00 17.95           C  
ANISOU  956  CA  LEU A 108     2159   2732   1930    107   -473    264       C  
ATOM    957  C   LEU A 108     -43.054 -20.617 -14.886  1.00 22.54           C  
ANISOU  957  C   LEU A 108     2738   3229   2597    127   -435    237       C  
ATOM    958  O   LEU A 108     -43.779 -19.843 -14.247  1.00 22.23           O  
ANISOU  958  O   LEU A 108     2662   3152   2632    148   -442    259       O  
ATOM    959  CB  LEU A 108     -42.891 -19.710 -17.202  1.00 22.91           C  
ANISOU  959  CB  LEU A 108     2787   3376   2542    117   -484    353       C  
ATOM    960  CG  LEU A 108     -41.475 -19.201 -16.949  1.00 22.62           C  
ANISOU  960  CG  LEU A 108     2782   3297   2517    125   -434    359       C  
ATOM    961  CD1 LEU A 108     -40.456 -20.259 -17.321  1.00 33.94           C  
ANISOU  961  CD1 LEU A 108     4255   4760   3879     94   -403    294       C  
ATOM    962  CD2 LEU A 108     -41.237 -17.933 -17.744  1.00 20.13           C  
ANISOU  962  CD2 LEU A 108     2460   2992   2198    134   -450    457       C  
ATOM    963  H   LEU A 108     -45.252 -20.501 -16.217  1.00 22.31           H  
ATOM    964  N   VAL A 109     -42.007 -21.235 -14.350  1.00 16.77           N  
ANISOU  964  N   VAL A 109     2041   2472   1860    117   -394    188       N  
ATOM    965  CA  VAL A 109     -41.601 -21.011 -12.969  1.00 24.26           C  
ANISOU  965  CA  VAL A 109     2989   3354   2876    125   -358    165       C  
ATOM    966  C   VAL A 109     -40.174 -20.507 -12.931  1.00 29.85           C  
ANISOU  966  C   VAL A 109     3723   4036   3584    132   -319    180       C  
ATOM    967  O   VAL A 109     -39.253 -21.170 -13.446  1.00 29.12           O  
ANISOU  967  O   VAL A 109     3661   3962   3443    119   -306    157       O  
ATOM    968  CB  VAL A 109     -41.752 -22.269 -12.098  1.00 36.35           C  
ANISOU  968  CB  VAL A 109     4528   4872   4412    101   -351     98       C  
ATOM    969  CG1 VAL A 109     -41.509 -21.903 -10.636  1.00 29.35           C  
ANISOU  969  CG1 VAL A 109     3633   3930   3587     99   -321     84       C  
ATOM    970  CG2 VAL A 109     -43.126 -22.879 -12.295  1.00 27.50           C  
ANISOU  970  CG2 VAL A 109     3384   3783   3280     89   -387     78       C  
ATOM    971  H   VAL A 109     -41.511 -21.796 -14.773  1.00 20.31           H  
ATOM    972  N   LEU A 110     -39.978 -19.362 -12.284  1.00 23.42           N  
ANISOU  972  N   LEU A 110     2891   3177   2829    150   -297    209       N  
ATOM    973  CA  LEU A 110     -38.677 -18.748 -12.079  1.00 20.79           C  
ANISOU  973  CA  LEU A 110     2577   2814   2508    157   -256    220       C  
ATOM    974  C   LEU A 110     -38.132 -19.189 -10.726  1.00 19.99           C  
ANISOU  974  C   LEU A 110     2481   2676   2437    142   -225    170       C  
ATOM    975  O   LEU A 110     -38.723 -18.871  -9.688  1.00 28.12           O  
ANISOU  975  O   LEU A 110     3484   3680   3520    137   -216    155       O  
ATOM    976  CB  LEU A 110     -38.804 -17.227 -12.132  1.00 15.98           C  
ANISOU  976  CB  LEU A 110     1942   2175   1955    181   -247    278       C  
ATOM    977  CG  LEU A 110     -39.544 -16.654 -13.341  1.00 16.68           C  
ANISOU  977  CG  LEU A 110     2013   2295   2028    194   -290    348       C  
ATOM    978  CD1 LEU A 110     -39.556 -15.134 -13.289  1.00 21.96           C  
ANISOU  978  CD1 LEU A 110     2652   2917   2775    219   -279    410       C  
ATOM    979  CD2 LEU A 110     -38.920 -17.135 -14.634  1.00 16.95           C  
ANISOU  979  CD2 LEU A 110     2084   2390   1966    177   -304    365       C  
ATOM    980  H   LEU A 110     -40.617 -18.902 -11.938  1.00 28.92           H  
ATOM    981  N   ALA A 111     -36.999 -19.896 -10.740  1.00 31.78           N  
ANISOU  981  N   ALA A 111     4005   4170   3900    132   -207    144       N  
ATOM    982  CA  ALA A 111     -36.476 -20.573  -9.554  1.00 23.13           C  
ANISOU  982  CA  ALA A 111     2915   3049   2826    113   -191    105       C  
ATOM    983  C   ALA A 111     -34.944 -20.547  -9.533  1.00 25.20           C  
ANISOU  983  C   ALA A 111     3197   3296   3083    114   -160    101       C  
ATOM    984  O   ALA A 111     -34.284 -21.553  -9.257  1.00 20.68           O  
ANISOU  984  O   ALA A 111     2636   2716   2506    102   -161     72       O  
ATOM    985  CB  ALA A 111     -36.997 -22.010  -9.497  1.00 26.35           C  
ANISOU  985  CB  ALA A 111     3328   3470   3214     93   -219     69       C  
ATOM    986  H   ALA A 111     -36.506 -20.000 -11.438  1.00 38.96           H  
ATOM    987  N   THR A 112     -34.360 -19.370  -9.781  1.00 29.61           N  
ANISOU  987  N   THR A 112     3756   3845   3651    130   -133    131       N  
ATOM    988  CA  THR A 112     -32.929 -19.215 -10.023  1.00 15.42           C  
ANISOU  988  CA  THR A 112     1976   2039   1842    133   -103    128       C  
ATOM    989  C   THR A 112     -32.138 -18.821  -8.785  1.00 19.33           C  
ANISOU  989  C   THR A 112     2462   2504   2377    124    -71    117       C  
ATOM    990  O   THR A 112     -30.903 -18.757  -8.850  1.00 15.77           O  
ANISOU  990  O   THR A 112     2023   2045   1922    125    -46    110       O  
ATOM    991  CB  THR A 112     -32.706 -18.161 -11.110  1.00 28.08           C  
ANISOU  991  CB  THR A 112     3588   3656   3427    149    -91    171       C  
ATOM    992  CG2 THR A 112     -33.105 -18.717 -12.464  1.00 21.91           C  
ANISOU  992  CG2 THR A 112     2819   2921   2584    145   -119    177       C  
ATOM    993  OG1 THR A 112     -33.497 -17.001 -10.815  1.00 25.96           O  
ANISOU  993  OG1 THR A 112     3293   3367   3202    161    -89    208       O  
ATOM    994  H   THR A 112     -34.789 -18.625  -9.814  1.00 36.35           H  
ATOM    995  HG1 THR A 112     -33.381 -16.416 -11.406  1.00 31.96           H  
ATOM    996  N   GLY A 113     -32.810 -18.537  -7.678  1.00 13.83           N  
ANISOU  996  N   GLY A 113     1743   1796   1716    109    -70    111       N  
ATOM    997  CA  GLY A 113     -32.132 -18.358  -6.417  1.00 18.09           C  
ANISOU  997  CA  GLY A 113     2270   2322   2280     86    -44     94       C  
ATOM    998  C   GLY A 113     -31.533 -16.975  -6.283  1.00 13.63           C  
ANISOU  998  C   GLY A 113     1695   1740   1744     92      1    105       C  
ATOM    999  O   GLY A 113     -31.843 -16.048  -7.041  1.00 14.44           O  
ANISOU  999  O   GLY A 113     1794   1834   1860    116     11    132       O  
ATOM   1000  H   GLY A 113     -33.664 -18.443  -7.637  1.00 12.61           H  
ATOM   1001  N   ALA A 114     -30.637 -16.839  -5.306  1.00 18.98           N  
ANISOU 1001  N   ALA A 114     2364   2414   2433     69     28     86       N  
ATOM   1002  CA  ALA A 114     -30.024 -15.556  -4.990  1.00 37.31           C  
ANISOU 1002  CA  ALA A 114     4670   4720   4785     67     78     85       C  
ATOM   1003  C   ALA A 114     -28.523 -15.697  -4.756  1.00 31.56           C  
ANISOU 1003  C   ALA A 114     3953   3995   4044     59     98     76       C  
ATOM   1004  O   ALA A 114     -27.982 -15.218  -3.756  1.00 44.91           O  
ANISOU 1004  O   ALA A 114     5624   5689   5752     30    128     57       O  
ATOM   1005  CB  ALA A 114     -30.691 -14.931  -3.765  1.00 51.99           C  
ANISOU 1005  CB  ALA A 114     6492   6578   6684     32    102     59       C  
ATOM   1006  H   ALA A 114     -30.367 -17.486  -4.807  1.00 23.59           H  
ATOM   1007  N   MET A 115     -27.818 -16.355  -5.672  1.00 19.24           N  
ANISOU 1007  N   MET A 115     2420   2437   2455     80     83     84       N  
ATOM   1008  CA  MET A 115     -26.361 -16.383  -5.642  1.00 16.95           C  
ANISOU 1008  CA  MET A 115     2135   2144   2161     79    105     73       C  
ATOM   1009  C   MET A 115     -25.757 -15.398  -6.630  1.00 28.81           C  
ANISOU 1009  C   MET A 115     3650   3637   3661    101    142     86       C  
ATOM   1010  O   MET A 115     -24.584 -15.529  -7.005  1.00 18.11           O  
ANISOU 1010  O   MET A 115     2305   2282   2295    106    159     74       O  
ATOM   1011  CB  MET A 115     -25.842 -17.795  -5.898  1.00 14.66           C  
ANISOU 1011  CB  MET A 115     1857   1858   1857     82     70     62       C  
ATOM   1012  CG  MET A 115     -26.524 -18.829  -5.042  1.00 27.67           C  
ANISOU 1012  CG  MET A 115     3493   3511   3508     59     27     61       C  
ATOM   1013  SD  MET A 115     -26.189 -18.556  -3.296  1.00 32.65           S  
ANISOU 1013  SD  MET A 115     4095   4157   4154     11     35     60       S  
ATOM   1014  CE  MET A 115     -24.427 -18.784  -3.240  1.00 24.04           C  
ANISOU 1014  CE  MET A 115     2999   3060   3075     14     45     55       C  
ATOM   1015  H   MET A 115     -28.165 -16.795  -6.324  1.00 23.91           H  
ATOM   1016  N   GLY A 116     -26.539 -14.413  -7.059  1.00 21.78           N  
ANISOU 1016  N   GLY A 116     2756   2735   2784    114    155    111       N  
ATOM   1017  CA  GLY A 116     -26.059 -13.484  -8.044  1.00 25.41           C  
ANISOU 1017  CA  GLY A 116     3230   3185   3241    130    185    137       C  
ATOM   1018  C   GLY A 116     -25.277 -12.354  -7.399  1.00 27.85           C  
ANISOU 1018  C   GLY A 116     3521   3472   3588    120    240    126       C  
ATOM   1019  O   GLY A 116     -25.545 -11.938  -6.272  1.00 33.23           O  
ANISOU 1019  O   GLY A 116     4173   4144   4308    100    259    105       O  
ATOM   1020  H   GLY A 116     -27.344 -14.272  -6.793  1.00 26.95           H  
ATOM   1021  N   ARG A 117     -24.254 -11.903  -8.119  1.00 30.19           N  
ANISOU 1021  N   ARG A 117     3835   3766   3871    126    270    133       N  
ATOM   1022  CA  ARG A 117     -23.485 -10.728  -7.744  1.00 36.04           C  
ANISOU 1022  CA  ARG A 117     4562   4484   4647    117    328    127       C  
ATOM   1023  C   ARG A 117     -23.807  -9.649  -8.772  1.00 27.38           C  
ANISOU 1023  C   ARG A 117     3474   3364   3567    133    344    180       C  
ATOM   1024  O   ARG A 117     -23.491  -9.796  -9.963  1.00 22.22           O  
ANISOU 1024  O   ARG A 117     2850   2726   2866    141    334    208       O  
ATOM   1025  CB  ARG A 117     -21.982 -11.021  -7.687  1.00 31.22           C  
ANISOU 1025  CB  ARG A 117     3960   3887   4014    107    352     93       C  
ATOM   1026  CG  ARG A 117     -21.201  -9.967  -6.882  1.00 30.17           C  
ANISOU 1026  CG  ARG A 117     3803   3738   3921     88    412     70       C  
ATOM   1027  CD  ARG A 117     -19.689 -10.217  -6.826  1.00 32.97           C  
ANISOU 1027  CD  ARG A 117     4161   4108   4257     78    435     36       C  
ATOM   1028  NE  ARG A 117     -19.360 -11.272  -5.869  1.00 38.42           N  
ANISOU 1028  NE  ARG A 117     4834   4823   4939     62    404      6       N  
ATOM   1029  CZ  ARG A 117     -18.212 -11.381  -5.202  1.00 45.64           C  
ANISOU 1029  CZ  ARG A 117     5730   5752   5858     44    421    -26       C  
ATOM   1030  NH1 ARG A 117     -17.234 -10.498  -5.360  1.00 51.05           N1+
ANISOU 1030  NH1 ARG A 117     6412   6431   6553     38    475    -42       N1+
ATOM   1031  NH2 ARG A 117     -18.047 -12.393  -4.365  1.00 48.93           N  
ANISOU 1031  NH2 ARG A 117     6129   6191   6271     29    380    -37       N  
ATOM   1032  H   ARG A 117     -23.984 -12.271  -8.849  1.00 37.05           H  
ATOM   1033  HE  ARG A 117     -19.957 -11.873  -5.725  1.00 46.92           H  
ATOM   1034 HH11 ARG A 117     -17.333  -9.838  -5.903  1.00 62.08           H  
ATOM   1035 HH12 ARG A 117     -16.500 -10.586  -4.920  1.00 62.08           H  
ATOM   1036 HH21 ARG A 117     -18.677 -12.969  -4.258  1.00 59.53           H  
ATOM   1037 HH22 ARG A 117     -17.311 -12.474  -3.928  1.00 59.53           H  
ATOM   1038  N   ILE A 118     -24.395  -8.548  -8.293  1.00 18.37           N  
ANISOU 1038  N   ILE A 118     2302   2183   2494    134    371    192       N  
ATOM   1039  CA  ILE A 118     -24.622  -7.381  -9.130  1.00 16.02           C  
ANISOU 1039  CA  ILE A 118     2004   1849   2233    148    388    251       C  
ATOM   1040  C   ILE A 118     -23.268  -6.858  -9.567  1.00 23.46           C  
ANISOU 1040  C   ILE A 118     2966   2790   3159    139    434    251       C  
ATOM   1041  O   ILE A 118     -22.290  -6.900  -8.801  1.00 31.59           O  
ANISOU 1041  O   ILE A 118     3989   3826   4189    121    472    195       O  
ATOM   1042  CB  ILE A 118     -25.419  -6.313  -8.374  1.00 24.01           C  
ANISOU 1042  CB  ILE A 118     2968   2808   3347    149    417    251       C  
ATOM   1043  CG1 ILE A 118     -26.869  -6.769  -8.179  1.00 19.76           C  
ANISOU 1043  CG1 ILE A 118     2410   2272   2827    160    368    259       C  
ATOM   1044  CG2 ILE A 118     -25.347  -4.973  -9.104  1.00 20.63           C  
ANISOU 1044  CG2 ILE A 118     2533   2328   2978    162    446    311       C  
ATOM   1045  CD1 ILE A 118     -27.706  -5.841  -7.319  1.00 27.36           C  
ANISOU 1045  CD1 ILE A 118     3314   3183   3898    156    399    238       C  
ATOM   1046  H   ILE A 118     -24.670  -8.456  -7.484  1.00 22.86           H  
ATOM   1047  N   ALA A 119     -23.204  -6.341 -10.786  1.00 18.12           N  
ANISOU 1047  N   ALA A 119     2312   2109   2465    146    431    314       N  
ATOM   1048  CA  ALA A 119     -21.935  -5.940 -11.375  1.00 20.30           C  
ANISOU 1048  CA  ALA A 119     2613   2391   2710    132    472    316       C  
ATOM   1049  C   ALA A 119     -21.112  -5.093 -10.413  1.00 22.34           C  
ANISOU 1049  C   ALA A 119     2845   2613   3029    119    540    270       C  
ATOM   1050  O   ALA A 119     -21.558  -4.042  -9.940  1.00 35.06           O  
ANISOU 1050  O   ALA A 119     4424   4172   4727    122    570    284       O  
ATOM   1051  CB  ALA A 119     -22.179  -5.190 -12.686  1.00 24.20           C  
ANISOU 1051  CB  ALA A 119     3125   2877   3193    133    462    406       C  
ATOM   1052  H   ALA A 119     -23.884  -6.210 -11.296  1.00 22.56           H  
ATOM   1053  N   SER A 120     -19.877  -5.578 -10.200  1.00 18.68           N  
ANISOU 1053  N   SER A 120     2394   2180   2523    104    565    215       N  
ATOM   1054  CA  SER A 120     -18.937  -5.234  -9.143  1.00 26.09           C  
ANISOU 1054  CA  SER A 120     3309   3111   3494     85    618    151       C  
ATOM   1055  C   SER A 120     -17.699  -4.529  -9.657  1.00 15.74           C  
ANISOU 1055  C   SER A 120     2012   1794   2176     71    674    147       C  
ATOM   1056  O   SER A 120     -16.971  -3.921  -8.867  1.00 18.66           O  
ANISOU 1056  O   SER A 120     2357   2149   2584     53    728    102       O  
ATOM   1057  CB  SER A 120     -18.453  -6.519  -8.455  1.00 32.09           C  
ANISOU 1057  CB  SER A 120     4066   3917   4211     77    592     92       C  
ATOM   1058  OG  SER A 120     -18.315  -7.575  -9.415  1.00 60.36           O  
ANISOU 1058  OG  SER A 120     7678   7531   7724     87    550    102       O  
ATOM   1059  H   SER A 120     -19.532  -6.173 -10.716  1.00 23.23           H  
ATOM   1060  HG  SER A 120     -19.072  -7.811  -9.692  1.00 73.25           H  
ATOM   1061  N   ILE A 121     -17.399  -4.691 -10.935  1.00 24.21           N  
ANISOU 1061  N   ILE A 121     3121   2886   3191     71    662    185       N  
ATOM   1062  CA  ILE A 121     -16.121  -4.311 -11.521  1.00 23.66           C  
ANISOU 1062  CA  ILE A 121     3070   2825   3093     51    710    172       C  
ATOM   1063  C   ILE A 121     -16.354  -3.137 -12.465  1.00 35.07           C  
ANISOU 1063  C   ILE A 121     4531   4238   4557     45    730    252       C  
ATOM   1064  O   ILE A 121     -17.229  -3.219 -13.326  1.00 18.85           O  
ANISOU 1064  O   ILE A 121     2495   2191   2478     52    684    323       O  
ATOM   1065  CB  ILE A 121     -15.477  -5.482 -12.286  1.00 16.20           C  
ANISOU 1065  CB  ILE A 121     2153   1937   2064     43    686    142       C  
ATOM   1066  CG1 ILE A 121     -15.134  -6.612 -11.323  1.00 22.64           C  
ANISOU 1066  CG1 ILE A 121     2947   2775   2880     49    665     71       C  
ATOM   1067  CG2 ILE A 121     -14.260  -4.996 -13.033  1.00 32.29           C  
ANISOU 1067  CG2 ILE A 121     4209   3986   4072     16    739    131       C  
ATOM   1068  CD1 ILE A 121     -14.956  -7.937 -12.013  1.00 35.33           C  
ANISOU 1068  CD1 ILE A 121     4571   4424   4428     50    627     46       C  
ATOM   1069  H   ILE A 121     -17.942  -5.034 -11.507  1.00 29.87           H  
ATOM   1070  N   PRO A 122     -15.577  -2.061 -12.356  1.00 25.55           N  
ANISOU 1070  N   PRO A 122     3318   2997   3392     28    795    248       N  
ATOM   1071  CA  PRO A 122     -15.680  -0.967 -13.331  1.00 22.25           C  
ANISOU 1071  CA  PRO A 122     2916   2546   2991     17    813    334       C  
ATOM   1072  C   PRO A 122     -15.619  -1.453 -14.773  1.00 22.94           C  
ANISOU 1072  C   PRO A 122     3050   2689   2979     -1    777    387       C  
ATOM   1073  O   PRO A 122     -14.675  -2.140 -15.179  1.00 33.89           O  
ANISOU 1073  O   PRO A 122     4458   4130   4290    -22    790    334       O  
ATOM   1074  CB  PRO A 122     -14.487  -0.078 -12.974  1.00 18.07           C  
ANISOU 1074  CB  PRO A 122     2377   1989   2500     -5    895    293       C  
ATOM   1075  CG  PRO A 122     -14.286  -0.305 -11.499  1.00 19.29           C  
ANISOU 1075  CG  PRO A 122     2491   2138   2700      1    917    201       C  
ATOM   1076  CD  PRO A 122     -14.639  -1.752 -11.260  1.00 21.14           C  
ANISOU 1076  CD  PRO A 122     2731   2428   2875     16    854    168       C  
ATOM   1077  N   GLY A 123     -16.634  -1.081 -15.562  1.00 31.88           N  
ANISOU 1077  N   GLY A 123     4191   3810   4113      4    733    489       N  
ATOM   1078  CA  GLY A 123     -16.752  -1.467 -16.954  1.00 20.17           C  
ANISOU 1078  CA  GLY A 123     2746   2389   2528    -23    694    549       C  
ATOM   1079  C   GLY A 123     -17.626  -2.680 -17.199  1.00 19.15           C  
ANISOU 1079  C   GLY A 123     2623   2313   2339    -11    623    544       C  
ATOM   1080  O   GLY A 123     -18.027  -2.923 -18.346  1.00 19.68           O  
ANISOU 1080  O   GLY A 123     2715   2433   2328    -35    582    606       O  
ATOM   1081  H   GLY A 123     -17.284  -0.586 -15.295  1.00 39.08           H  
ATOM   1082  N   GLU A 124     -17.935  -3.438 -16.149  1.00 18.41           N  
ANISOU 1082  N   GLU A 124     2506   2212   2277     20    609    473       N  
ATOM   1083  CA  GLU A 124     -18.774  -4.624 -16.285  1.00 18.15           C  
ANISOU 1083  CA  GLU A 124     2476   2223   2196     33    546    461       C  
ATOM   1084  C   GLU A 124     -20.183  -4.276 -16.760  1.00 24.68           C  
ANISOU 1084  C   GLU A 124     3297   3040   3041     46    487    561       C  
ATOM   1085  O   GLU A 124     -20.685  -4.855 -17.728  1.00 33.70           O  
ANISOU 1085  O   GLU A 124     4459   4240   4104     30    439    598       O  
ATOM   1086  CB  GLU A 124     -18.829  -5.371 -14.949  1.00 18.43           C  
ANISOU 1086  CB  GLU A 124     2485   2244   2275     59    544    376       C  
ATOM   1087  CG  GLU A 124     -19.556  -6.698 -15.018  1.00 27.30           C  
ANISOU 1087  CG  GLU A 124     3611   3409   3352     70    484    353       C  
ATOM   1088  CD  GLU A 124     -19.564  -7.442 -13.697  1.00 20.77           C  
ANISOU 1088  CD  GLU A 124     2758   2569   2564     89    480    279       C  
ATOM   1089  OE1 GLU A 124     -18.795  -7.074 -12.785  1.00 44.29           O  
ANISOU 1089  OE1 GLU A 124     5719   5521   5587     87    524    234       O  
ATOM   1090  OE2 GLU A 124     -20.344  -8.408 -13.573  1.00 35.10           O1-
ANISOU 1090  OE2 GLU A 124     4570   4404   4362    100    431    268       O1-
ATOM   1091  H   GLU A 124     -17.671  -3.288 -15.344  1.00 18.00           H  
ATOM   1092  N   ALA A 125     -20.863  -3.366 -16.054  1.00 29.55           N  
ANISOU 1092  N   ALA A 125     3880   3583   3766     74    492    598       N  
ATOM   1093  CA  ALA A 125     -22.199  -2.954 -16.485  1.00 21.22           C  
ANISOU 1093  CA  ALA A 125     2808   2507   2747     91    436    696       C  
ATOM   1094  C   ALA A 125     -22.147  -2.203 -17.809  1.00 25.91           C  
ANISOU 1094  C   ALA A 125     3425   3116   3304     62    421    810       C  
ATOM   1095  O   ALA A 125     -22.995  -2.415 -18.687  1.00 28.35           O  
ANISOU 1095  O   ALA A 125     3740   3465   3565     54    357    889       O  
ATOM   1096  CB  ALA A 125     -22.859  -2.094 -15.406  1.00 25.29           C  
ANISOU 1096  CB  ALA A 125     3272   2932   3404    124    454    698       C  
ATOM   1097  H   ALA A 125     -20.580  -2.983 -15.339  1.00 36.28           H  
ATOM   1098  N   GLU A 126     -21.108  -1.396 -17.992  1.00 30.35           N  
ANISOU 1098  N   GLU A 126     4175   4154   3204    532     97    932       N  
ATOM   1099  CA  GLU A 126     -21.008  -0.508 -19.143  1.00 19.67           C  
ANISOU 1099  CA  GLU A 126     2825   2849   1800    576    112    951       C  
ATOM   1100  C   GLU A 126     -20.850  -1.268 -20.449  1.00 18.59           C  
ANISOU 1100  C   GLU A 126     2721   2793   1551    600     93    944       C  
ATOM   1101  O   GLU A 126     -21.428  -0.874 -21.471  1.00 28.10           O  
ANISOU 1101  O   GLU A 126     3914   4082   2680    634     71    962       O  
ATOM   1102  CB  GLU A 126     -19.783   0.385 -18.943  1.00 24.71           C  
ANISOU 1102  CB  GLU A 126     3476   3410   2501    574    175    944       C  
ATOM   1103  CG  GLU A 126     -19.604   1.500 -19.934  1.00 36.80           C  
ANISOU 1103  CG  GLU A 126     5010   4971   4002    618    204    968       C  
ATOM   1104  CD  GLU A 126     -18.264   2.207 -19.786  1.00 39.50           C  
ANISOU 1104  CD  GLU A 126     5367   5245   4398    615    266    954       C  
ATOM   1105  OE1 GLU A 126     -17.436   1.774 -18.955  1.00 43.54           O  
ANISOU 1105  OE1 GLU A 126     5885   5692   4966    578    283    922       O  
ATOM   1106  OE2 GLU A 126     -18.043   3.199 -20.512  1.00 44.31           O1-
ANISOU 1106  OE2 GLU A 126     5978   5867   4991    651    298    975       O1-
ATOM   1107  H   GLU A 126     -20.437  -1.343 -17.457  1.00 37.24           H  
ATOM   1108  N   TYR A 127     -20.150  -2.393 -20.418  1.00 38.65           N  
ANISOU 1108  N   TYR A 127     5299   5314   4073    581     99    915       N  
ATOM   1109  CA  TYR A 127     -19.859  -3.151 -21.628  1.00 32.21           C  
ANISOU 1109  CA  TYR A 127     4522   4572   3144    599     92    895       C  
ATOM   1110  C   TYR A 127     -20.644  -4.449 -21.677  1.00 29.09           C  
ANISOU 1110  C   TYR A 127     4120   4245   2686    574     38    851       C  
ATOM   1111  O   TYR A 127     -20.296  -5.361 -22.435  1.00 39.76           O  
ANISOU 1111  O   TYR A 127     5492   5618   3997    545     34    775       O  
ATOM   1112  CB  TYR A 127     -18.353  -3.414 -21.736  1.00 24.97           C  
ANISOU 1112  CB  TYR A 127     3656   3580   2251    596    153    876       C  
ATOM   1113  CG  TYR A 127     -17.547  -2.168 -22.071  1.00 34.84           C  
ANISOU 1113  CG  TYR A 127     4906   4789   3543    615    201    894       C  
ATOM   1114  CD1 TYR A 127     -17.488  -1.676 -23.369  1.00 33.70           C  
ANISOU 1114  CD1 TYR A 127     4775   4710   3318    649    207    904       C  
ATOM   1115  CD2 TYR A 127     -16.859  -1.477 -21.081  1.00 34.01           C  
ANISOU 1115  CD2 TYR A 127     4784   4588   3551    597    239    895       C  
ATOM   1116  CE1 TYR A 127     -16.759  -0.530 -23.673  1.00 39.87           C  
ANISOU 1116  CE1 TYR A 127     5558   5454   4136    670    255    922       C  
ATOM   1117  CE2 TYR A 127     -16.132  -0.333 -21.376  1.00 27.73           C  
ANISOU 1117  CE2 TYR A 127     3986   3764   2786    615    285    903       C  
ATOM   1118  CZ  TYR A 127     -16.084   0.137 -22.671  1.00 32.55           C  
ANISOU 1118  CZ  TYR A 127     4614   4432   3320    653    295    920       C  
ATOM   1119  OH  TYR A 127     -15.356   1.271 -22.959  1.00 43.08           O  
ANISOU 1119  OH  TYR A 127     5949   5735   4685    674    344    931       O  
ATOM   1120  H   TYR A 127     -19.828  -2.742 -19.702  1.00 47.20           H  
ATOM   1121  HH  TYR A 127     -15.002   1.572 -22.259  1.00 52.51           H  
ATOM   1122  N   LEU A 128     -21.725  -4.528 -20.912  1.00 28.42           N  
ANISOU 1122  N   LEU A 128     3987   4171   2641    552     -6    852       N  
ATOM   1123  CA  LEU A 128     -22.627  -5.659 -21.017  1.00 18.66           C  
ANISOU 1123  CA  LEU A 128     2716   2983   1391    493    -64    763       C  
ATOM   1124  C   LEU A 128     -23.262  -5.678 -22.397  1.00 20.23           C  
ANISOU 1124  C   LEU A 128     2901   3324   1463    512   -107    741       C  
ATOM   1125  O   LEU A 128     -23.741  -4.649 -22.887  1.00 40.00           O  
ANISOU 1125  O   LEU A 128     5389   5907   3904    573   -121    818       O  
ATOM   1126  CB  LEU A 128     -23.698  -5.559 -19.942  1.00 25.02           C  
ANISOU 1126  CB  LEU A 128     3470   3777   2260    472    -99    778       C  
ATOM   1127  CG  LEU A 128     -24.552  -6.805 -19.747  1.00 45.44           C  
ANISOU 1127  CG  LEU A 128     6021   6383   4860    400   -148    680       C  
ATOM   1128  CD1 LEU A 128     -23.703  -7.983 -19.307  1.00 39.30           C  
ANISOU 1128  CD1 LEU A 128     5277   5505   4151    342   -116    606       C  
ATOM   1129  CD2 LEU A 128     -25.629  -6.486 -18.728  1.00 32.58           C  
ANISOU 1129  CD2 LEU A 128     4341   4749   3289    389   -177    709       C  
ATOM   1130  H   LEU A 128     -21.955  -3.941 -20.328  1.00 34.92           H  
ATOM   1131  N   GLY A 129     -23.269  -6.856 -23.020  1.00 40.22           N  
ANISOU 1131  N   GLY A 129     5437   5888   3958    458   -125    638       N  
ATOM   1132  CA  GLY A 129     -23.697  -6.997 -24.397  1.00 33.36           C  
ANISOU 1132  CA  GLY A 129     4560   5155   2960    465   -161    603       C  
ATOM   1133  C   GLY A 129     -22.755  -6.415 -25.424  1.00 43.18           C  
ANISOU 1133  C   GLY A 129     5856   6425   4127    517   -120    643       C  
ATOM   1134  O   GLY A 129     -23.119  -6.338 -26.603  1.00 44.89           O  
ANISOU 1134  O   GLY A 129     6066   6766   4223    533   -149    632       O  
ATOM   1135  H   GLY A 129     -23.026  -7.597 -22.657  1.00 49.09           H  
ATOM   1136  N   ARG A 130     -21.563  -5.987 -25.007  1.00 51.59           N  
ANISOU 1136  N   ARG A 130     6968   7380   5253    542    -53    688       N  
ATOM   1137  CA  ARG A 130     -20.544  -5.407 -25.876  1.00 54.98           C  
ANISOU 1137  CA  ARG A 130     7451   7814   5624    590     -1    727       C  
ATOM   1138  C   ARG A 130     -19.182  -5.981 -25.522  1.00 54.29           C  
ANISOU 1138  C   ARG A 130     7411   7601   5615    561     63    685       C  
ATOM   1139  O   ARG A 130     -18.165  -5.279 -25.542  1.00 55.50           O  
ANISOU 1139  O   ARG A 130     7604   7698   5785    602    123    741       O  
ATOM   1140  CB  ARG A 130     -20.504  -3.886 -25.760  1.00 61.02           C  
ANISOU 1140  CB  ARG A 130     8211   8561   6412    654     22    835       C  
ATOM   1141  CG  ARG A 130     -21.690  -3.172 -26.352  1.00 69.67           C  
ANISOU 1141  CG  ARG A 130     9255   9754   7464    675    -30    863       C  
ATOM   1142  CD  ARG A 130     -21.382  -1.690 -26.521  1.00 74.89           C  
ANISOU 1142  CD  ARG A 130     9911  10358   8185    713     12    926       C  
ATOM   1143  NE  ARG A 130     -21.217  -1.027 -25.229  1.00 63.03           N  
ANISOU 1143  NE  ARG A 130     8392   8739   6817    708     45    955       N  
ATOM   1144  CZ  ARG A 130     -20.471   0.056 -25.014  1.00 48.62           C  
ANISOU 1144  CZ  ARG A 130     6574   6828   5070    724    104    984       C  
ATOM   1145  NH1 ARG A 130     -19.804   0.631 -26.006  1.00 49.85           N1+
ANISOU 1145  NH1 ARG A 130     6758   6995   5189    751    138    997       N1+
ATOM   1146  NH2 ARG A 130     -20.398   0.568 -23.794  1.00 44.67           N  
ANISOU 1146  NH2 ARG A 130     6054   6237   4683    708    128    994       N  
ATOM   1147  H   ARG A 130     -21.311  -6.024 -24.186  1.00 62.72           H  
ATOM   1148  HE  ARG A 130     -21.631  -1.362 -24.554  1.00 76.45           H  
ATOM   1149 HH11 ARG A 130     -19.848   0.304 -26.800  1.00 60.64           H  
ATOM   1150 HH12 ARG A 130     -19.326   1.330 -25.855  1.00 60.64           H  
ATOM   1151 HH21 ARG A 130     -20.830   0.200 -23.147  1.00 54.43           H  
ATOM   1152 HH22 ARG A 130     -19.919   1.266 -23.650  1.00 54.43           H  
ATOM   1153  N   GLY A 131     -19.152  -7.262 -25.151  1.00 53.86           N  
ANISOU 1153  N   GLY A 131     7350   7498   5616    491     55    589       N  
ATOM   1154  CA  GLY A 131     -17.941  -7.937 -24.720  1.00 54.39           C  
ANISOU 1154  CA  GLY A 131     7452   7444   5769    463    112    548       C  
ATOM   1155  C   GLY A 131     -18.055  -8.592 -23.357  1.00 35.48           C  
ANISOU 1155  C   GLY A 131     5034   4950   3497    418    106    526       C  
ATOM   1156  O   GLY A 131     -17.372  -9.586 -23.098  1.00 40.63           O  
ANISOU 1156  O   GLY A 131     5704   5522   4213    377    136    463       O  
ATOM   1157  H   GLY A 131     -19.846  -7.771 -25.143  1.00 65.45           H  
ATOM   1158  N   VAL A 132     -18.912  -8.062 -22.484  1.00 24.84           N  
ANISOU 1158  N   VAL A 132     3648   3606   2183    426     71    578       N  
ATOM   1159  CA  VAL A 132     -19.133  -8.631 -21.156  1.00 18.14           C  
ANISOU 1159  CA  VAL A 132     2776   2671   1445    383     63    563       C  
ATOM   1160  C   VAL A 132     -20.355  -9.541 -21.192  1.00 18.79           C  
ANISOU 1160  C   VAL A 132     2819   2808   1512    328      7    487       C  
ATOM   1161  O   VAL A 132     -21.421  -9.146 -21.684  1.00 23.24           O  
ANISOU 1161  O   VAL A 132     3348   3479   2002    340    -42    495       O  
ATOM   1162  CB  VAL A 132     -19.305  -7.533 -20.091  1.00 25.35           C  
ANISOU 1162  CB  VAL A 132     3672   3547   2412    416     67    659       C  
ATOM   1163  CG1 VAL A 132     -19.714  -8.153 -18.751  1.00 29.46           C  
ANISOU 1163  CG1 VAL A 132     4166   3995   3032    366     50    639       C  
ATOM   1164  CG2 VAL A 132     -18.028  -6.725 -19.944  1.00 16.89           C  
ANISOU 1164  CG2 VAL A 132     2638   2411   1367    459    130    722       C  
ATOM   1165  H   VAL A 132     -19.386  -7.361 -22.642  1.00 30.62           H  
ATOM   1166  N   SER A 133     -20.209 -10.743 -20.633  1.00 18.70           N  
ANISOU 1166  N   SER A 133     2808   2721   1575    268     16    415       N  
ATOM   1167  CA  SER A 133     -21.207 -11.799 -20.757  1.00 29.38           C  
ANISOU 1167  CA  SER A 133     4130   4114   2919    206    -22    323       C  
ATOM   1168  C   SER A 133     -21.151 -12.696 -19.527  1.00 29.91           C  
ANISOU 1168  C   SER A 133     4192   4067   3104    156     -8    294       C  
ATOM   1169  O   SER A 133     -20.130 -12.776 -18.842  1.00 24.08           O  
ANISOU 1169  O   SER A 133     3481   3224   2443    165     36    324       O  
ATOM   1170  CB  SER A 133     -20.971 -12.611 -22.038  1.00 34.40           C  
ANISOU 1170  CB  SER A 133     4786   4801   3483    178    -11    230       C  
ATOM   1171  OG  SER A 133     -21.716 -13.815 -22.045  1.00 26.52           O  
ANISOU 1171  OG  SER A 133     3765   3814   2499    106    -30    127       O  
ATOM   1172  H   SER A 133     -19.525 -10.974 -20.166  1.00 23.26           H  
ATOM   1173  HG  SER A 133     -21.566 -14.242 -22.753  1.00 32.64           H  
ATOM   1174  N   TYR A 134     -22.275 -13.370 -19.250  1.00 28.04           N  
ANISOU 1174  N   TYR A 134     3918   3856   2879    104    -45    236       N  
ATOM   1175  CA  TYR A 134     -22.379 -14.325 -18.150  1.00 18.47           C  
ANISOU 1175  CA  TYR A 134     2701   2543   1772     51    -33    201       C  
ATOM   1176  C   TYR A 134     -22.769 -15.716 -18.640  1.00 19.25           C  
ANISOU 1176  C   TYR A 134     2796   2648   1869    -18    -28     79       C  
ATOM   1177  O   TYR A 134     -23.189 -16.561 -17.838  1.00 19.16           O  
ANISOU 1177  O   TYR A 134     2773   2574   1933    -70    -24     39       O  
ATOM   1178  CB  TYR A 134     -23.391 -13.842 -17.109  1.00 24.13           C  
ANISOU 1178  CB  TYR A 134     3378   3265   2527     45    -70    247       C  
ATOM   1179  CG  TYR A 134     -23.111 -12.457 -16.590  1.00 32.21           C  
ANISOU 1179  CG  TYR A 134     4402   4283   3555    107    -69    360       C  
ATOM   1180  CD1 TYR A 134     -22.080 -12.228 -15.691  1.00 24.65           C  
ANISOU 1180  CD1 TYR A 134     3472   3222   2672    124    -28    418       C  
ATOM   1181  CD2 TYR A 134     -23.877 -11.377 -16.999  1.00 29.79           C  
ANISOU 1181  CD2 TYR A 134     4065   4075   3179    147   -106    410       C  
ATOM   1182  CE1 TYR A 134     -21.822 -10.963 -15.214  1.00 16.66           C  
ANISOU 1182  CE1 TYR A 134     2459   2205   1666    172    -20    513       C  
ATOM   1183  CE2 TYR A 134     -23.627 -10.112 -16.531  1.00 31.92           C  
ANISOU 1183  CE2 TYR A 134     4336   4332   3459    201    -95    511       C  
ATOM   1184  CZ  TYR A 134     -22.599  -9.908 -15.641  1.00 26.08           C  
ANISOU 1184  CZ  TYR A 134     3626   3489   2795    210    -50    558       C  
ATOM   1185  OH  TYR A 134     -22.358  -8.639 -15.182  1.00 43.42           O  
ANISOU 1185  OH  TYR A 134     5823   5674   5002    257    -33    651       O  
ATOM   1186  H   TYR A 134     -23.004 -13.286 -19.698  1.00 34.46           H  
ATOM   1187  HH  TYR A 134     -21.717  -8.646 -14.639  1.00 52.93           H  
ATOM   1188  N   CYS A 135     -22.631 -15.967 -19.945  1.00 21.61           N  
ANISOU 1188  N   CYS A 135     3107   3021   2084    -24    -24     18       N  
ATOM   1189  CA  CYS A 135     -23.126 -17.201 -20.552  1.00 24.78           C  
ANISOU 1189  CA  CYS A 135     3499   3449   2468    -95    -20   -108       C  
ATOM   1190  C   CYS A 135     -22.215 -17.552 -21.726  1.00 24.67           C  
ANISOU 1190  C   CYS A 135     3525   3449   2401    -93     22   -159       C  
ATOM   1191  O   CYS A 135     -22.332 -16.971 -22.809  1.00 22.06           O  
ANISOU 1191  O   CYS A 135     3192   3231   1957    -68     -1   -158       O  
ATOM   1192  CB  CYS A 135     -24.572 -17.041 -20.996  1.00 21.59           C  
ANISOU 1192  CB  CYS A 135     3041   3179   1985   -120    -85   -146       C  
ATOM   1193  SG  CYS A 135     -25.305 -18.547 -21.620  1.00 37.55           S  
ANISOU 1193  SG  CYS A 135     5042   5236   3989   -220    -79   -310       S  
ATOM   1194  H   CYS A 135     -22.251 -15.434 -20.502  1.00 26.75           H  
ATOM   1195  N   ALA A 136     -21.325 -18.519 -21.493  1.00 28.89           N  
ANISOU 1195  N   ALA A 136     4094   3867   3017   -119     85   -202       N  
ATOM   1196  CA  ALA A 136     -20.371 -18.956 -22.502  1.00 23.87           C  
ANISOU 1196  CA  ALA A 136     3497   3222   2350   -121    137   -255       C  
ATOM   1197  C   ALA A 136     -21.014 -19.819 -23.573  1.00 23.16           C  
ANISOU 1197  C   ALA A 136     3395   3215   2189   -189    136   -385       C  
ATOM   1198  O   ALA A 136     -20.579 -19.787 -24.732  1.00 30.71           O  
ANISOU 1198  O   ALA A 136     4374   4232   3063   -186    154   -424       O  
ATOM   1199  CB  ALA A 136     -19.243 -19.743 -21.833  1.00 26.58           C  
ANISOU 1199  CB  ALA A 136     3875   3409   2816   -125    208   -256       C  
ATOM   1200  H   ALA A 136     -21.254 -18.941 -20.747  1.00 35.49           H  
ATOM   1201  N   THR A 137     -22.019 -20.615 -23.205  1.00 23.50           N  
ANISOU 1201  N   THR A 137     3406   3261   2263   -254    120   -458       N  
ATOM   1202  CA  THR A 137     -22.704 -21.437 -24.191  1.00 24.68           C  
ANISOU 1202  CA  THR A 137     3538   3496   2343   -327    120   -590       C  
ATOM   1203  C   THR A 137     -23.565 -20.582 -25.106  1.00 31.46           C  
ANISOU 1203  C   THR A 137     4361   4537   3057   -312     46   -584       C  
ATOM   1204  O   THR A 137     -23.899 -21.013 -26.216  1.00 29.38           O  
ANISOU 1204  O   THR A 137     4089   4374   2701   -359     43   -682       O  
ATOM   1205  CB  THR A 137     -23.541 -22.525 -23.502  1.00 24.92           C  
ANISOU 1205  CB  THR A 137     3541   3473   2454   -404    129   -672       C  
ATOM   1206  CG2 THR A 137     -22.630 -23.583 -22.863  1.00 24.69           C  
ANISOU 1206  CG2 THR A 137     3553   3270   2559   -425    215   -696       C  
ATOM   1207  OG1 THR A 137     -24.376 -21.959 -22.483  1.00 30.56           O  
ANISOU 1207  OG1 THR A 137     4218   4193   3199   -387     74   -601       O  
ATOM   1208  H   THR A 137     -22.317 -20.692 -22.402  1.00 24.11           H  
ATOM   1209  HG1 THR A 137     -23.902 -21.593 -21.894  1.00 37.48           H  
ATOM   1210  N   CYS A 138     -23.879 -19.357 -24.694  1.00 43.26           N  
ANISOU 1210  N   CYS A 138     5835   6077   4525   -246     -9   -468       N  
ATOM   1211  CA  CYS A 138     -24.675 -18.472 -25.530  1.00 51.98           C  
ANISOU 1211  CA  CYS A 138     6903   7352   5494   -219    -78   -445       C  
ATOM   1212  C   CYS A 138     -23.817 -17.544 -26.388  1.00 42.41           C  
ANISOU 1212  C   CYS A 138     5728   6188   4197   -149    -70   -376       C  
ATOM   1213  O   CYS A 138     -24.171 -17.292 -27.542  1.00 42.93           O  
ANISOU 1213  O   CYS A 138     5782   6395   4134   -149   -101   -405       O  
ATOM   1214  CB  CYS A 138     -25.640 -17.671 -24.652  1.00 72.80           C  
ANISOU 1214  CB  CYS A 138     9491  10018   8151   -188   -141   -362       C  
ATOM   1215  SG  CYS A 138     -27.066 -17.010 -25.524  1.00 91.14           S  
ANISOU 1215  SG  CYS A 138    11744  12555  10329   -182   -233   -368       S  
ATOM   1216  H   CYS A 138     -23.643 -19.019 -23.939  1.00 52.73           H  
ATOM   1217  N   ASP A 139     -22.674 -17.053 -25.892  1.00 52.51           N  
ANISOU 1217  N   ASP A 139     7051   7358   5541    -93    -26   -290       N  
ATOM   1218  CA  ASP A 139     -21.871 -16.086 -26.639  1.00 35.95           C  
ANISOU 1218  CA  ASP A 139     4990   5301   3369    -24    -14   -218       C  
ATOM   1219  C   ASP A 139     -20.522 -16.621 -27.113  1.00 32.06           C  
ANISOU 1219  C   ASP A 139     4555   4726   2900    -30     64   -258       C  
ATOM   1220  O   ASP A 139     -19.812 -15.909 -27.835  1.00 33.76           O  
ANISOU 1220  O   ASP A 139     4803   4975   3050     19     82   -211       O  
ATOM   1221  CB  ASP A 139     -21.648 -14.819 -25.792  1.00 41.15           C  
ANISOU 1221  CB  ASP A 139     5649   5919   4068     55    -26    -75       C  
ATOM   1222  CG  ASP A 139     -22.952 -14.165 -25.353  1.00 53.61           C  
ANISOU 1222  CG  ASP A 139     7169   7577   5624     70    -98    -26       C  
ATOM   1223  OD1 ASP A 139     -24.031 -14.662 -25.734  1.00 64.42           O  
ANISOU 1223  OD1 ASP A 139     8495   9042   6941     22   -143    -99       O  
ATOM   1224  OD2 ASP A 139     -22.903 -13.149 -24.626  1.00 62.25           O1-
ANISOU 1224  OD2 ASP A 139     8259   8640   6754    128   -106     84       O1-
ATOM   1225  H   ASP A 139     -22.347 -17.268 -25.126  1.00 63.83           H  
ATOM   1226  N   GLY A 140     -20.158 -17.857 -26.761  1.00 34.88           N  
ANISOU 1226  N   GLY A 140     4925   4977   3350    -89    115   -343       N  
ATOM   1227  CA  GLY A 140     -18.806 -18.335 -27.024  1.00 33.07           C  
ANISOU 1227  CA  GLY A 140     4748   4649   3168    -87    194   -367       C  
ATOM   1228  C   GLY A 140     -18.428 -18.349 -28.494  1.00 25.27           C  
ANISOU 1228  C   GLY A 140     3788   3750   2064    -95    217   -425       C  
ATOM   1229  O   GLY A 140     -17.296 -18.009 -28.857  1.00 42.36           O  
ANISOU 1229  O   GLY A 140     5995   5872   4227    -55    265   -391       O  
ATOM   1230  H   GLY A 140     -20.670 -18.429 -26.373  1.00 42.67           H  
ATOM   1231  N   ALA A 141     -19.358 -18.758 -29.360  1.00 41.35           N  
ANISOU 1231  N   ALA A 141     5799   5912   3999   -150    183   -516       N  
ATOM   1232  CA  ALA A 141     -19.068 -18.871 -30.788  1.00 40.19           C  
ANISOU 1232  CA  ALA A 141     5677   5860   3733   -169    204   -583       C  
ATOM   1233  C   ALA A 141     -18.621 -17.553 -31.390  1.00 43.85           C  
ANISOU 1233  C   ALA A 141     6164   6396   4100    -88    189   -479       C  
ATOM   1234  O   ALA A 141     -17.850 -17.539 -32.362  1.00 54.43           O  
ANISOU 1234  O   ALA A 141     7546   7758   5377    -84    233   -506       O  
ATOM   1235  CB  ALA A 141     -20.304 -19.392 -31.525  1.00 49.69           C  
ANISOU 1235  CB  ALA A 141     6838   7209   4833   -240    156   -689       C  
ATOM   1236  H   ALA A 141     -20.163 -18.976 -29.147  1.00 50.43           H  
ATOM   1237  N   PHE A 142     -19.080 -16.431 -30.859  1.00 39.98           N  
ANISOU 1237  N   PHE A 142     5651   5942   3599    -23    133   -361       N  
ATOM   1238  CA  PHE A 142     -18.665 -15.153 -31.419  1.00 35.09           C  
ANISOU 1238  CA  PHE A 142     5054   5384   2893     57    126   -257       C  
ATOM   1239  C   PHE A 142     -17.258 -14.752 -30.997  1.00 28.96           C  
ANISOU 1239  C   PHE A 142     4328   4473   2201    108    195   -189       C  
ATOM   1240  O   PHE A 142     -16.774 -13.707 -31.436  1.00 40.73           O  
ANISOU 1240  O   PHE A 142     5845   5997   3632    173    205   -105       O  
ATOM   1241  CB  PHE A 142     -19.678 -14.062 -31.063  1.00 32.42           C  
ANISOU 1241  CB  PHE A 142     4673   5135   2512    110     49   -155       C  
ATOM   1242  CG  PHE A 142     -21.107 -14.478 -31.293  1.00 47.13           C  
ANISOU 1242  CG  PHE A 142     6475   7122   4310     60    -23   -219       C  
ATOM   1243  CD1 PHE A 142     -21.768 -15.256 -30.359  1.00 51.79           C  
ANISOU 1243  CD1 PHE A 142     7027   7655   4995      6    -40   -272       C  
ATOM   1244  CD2 PHE A 142     -21.788 -14.090 -32.437  1.00 38.02           C  
ANISOU 1244  CD2 PHE A 142     5301   6146   2998     67    -73   -227       C  
ATOM   1245  CE1 PHE A 142     -23.076 -15.642 -30.553  1.00 50.54           C  
ANISOU 1245  CE1 PHE A 142     6811   7611   4782    -44   -103   -336       C  
ATOM   1246  CE2 PHE A 142     -23.104 -14.470 -32.636  1.00 41.70           C  
ANISOU 1246  CE2 PHE A 142     5705   6735   3405     19   -142   -288       C  
ATOM   1247  CZ  PHE A 142     -23.747 -15.246 -31.692  1.00 49.92           C  
ANISOU 1247  CZ  PHE A 142     6707   7714   4548    -38   -156   -346       C  
ATOM   1248  H   PHE A 142     -19.620 -16.383 -30.191  1.00 48.80           H  
ATOM   1249  N   TYR A 143     -16.563 -15.567 -30.200  1.00 30.41           N  
ANISOU 1249  N   TYR A 143     4525   4509   2521     80    248   -224       N  
ATOM   1250  CA  TYR A 143     -15.181 -15.283 -29.832  1.00 36.45           C  
ANISOU 1250  CA  TYR A 143     5331   5151   3367    124    314   -169       C  
ATOM   1251  C   TYR A 143     -14.224 -16.290 -30.460  1.00 32.10           C  
ANISOU 1251  C   TYR A 143     4818   4538   2840     82    391   -267       C  
ATOM   1252  O   TYR A 143     -13.137 -16.542 -29.934  1.00 36.17           O  
ANISOU 1252  O   TYR A 143     5356   4924   3463     95    451   -254       O  
ATOM   1253  CB  TYR A 143     -15.052 -15.233 -28.316  1.00 29.44           C  
ANISOU 1253  CB  TYR A 143     4425   4143   2619    140    312   -107       C  
ATOM   1254  CG  TYR A 143     -15.861 -14.082 -27.778  1.00 22.78           C  
ANISOU 1254  CG  TYR A 143     3550   3358   1748    188    249     -4       C  
ATOM   1255  CD1 TYR A 143     -15.350 -12.791 -27.778  1.00 23.65           C  
ANISOU 1255  CD1 TYR A 143     3678   3474   1833    261    258    104       C  
ATOM   1256  CD2 TYR A 143     -17.159 -14.272 -27.332  1.00 30.39           C  
ANISOU 1256  CD2 TYR A 143     4465   4373   2708    159    184    -18       C  
ATOM   1257  CE1 TYR A 143     -16.098 -11.729 -27.315  1.00 24.27           C  
ANISOU 1257  CE1 TYR A 143     3728   3602   1891    305    208    197       C  
ATOM   1258  CE2 TYR A 143     -17.912 -13.218 -26.866  1.00 25.43           C  
ANISOU 1258  CE2 TYR A 143     3807   3798   2058    203    131     74       C  
ATOM   1259  CZ  TYR A 143     -17.379 -11.949 -26.859  1.00 24.53           C  
ANISOU 1259  CZ  TYR A 143     3711   3684   1924    277    144    183       C  
ATOM   1260  OH  TYR A 143     -18.136 -10.901 -26.394  1.00 47.82           O  
ANISOU 1260  OH  TYR A 143     6630   6680   4858    320     99    274       O  
ATOM   1261  H   TYR A 143     -16.875 -16.294 -29.861  1.00 37.31           H  
ATOM   1262  HH  TYR A 143     -18.891 -11.177 -26.152  1.00 58.20           H  
ATOM   1263  N   ARG A 144     -14.614 -16.847 -31.605  1.00 35.34           N  
ANISOU 1263  N   ARG A 144     5234   5045   3150     30    391   -367       N  
ATOM   1264  CA  ARG A 144     -13.705 -17.697 -32.357  1.00 32.85           C  
ANISOU 1264  CA  ARG A 144     4957   4682   2842     -9    470   -461       C  
ATOM   1265  C   ARG A 144     -12.476 -16.891 -32.748  1.00 37.70           C  
ANISOU 1265  C   ARG A 144     5618   5265   3443     53    521   -394       C  
ATOM   1266  O   ARG A 144     -12.588 -15.808 -33.341  1.00 35.78           O  
ANISOU 1266  O   ARG A 144     5386   5119   3091    101    494   -325       O  
ATOM   1267  CB  ARG A 144     -14.378 -18.287 -33.596  1.00 45.39           C  
ANISOU 1267  CB  ARG A 144     6543   6400   4304    -77    460   -578       C  
ATOM   1268  CG  ARG A 144     -13.535 -19.415 -34.217  1.00 62.41           C  
ANISOU 1268  CG  ARG A 144     8734   8486   6494   -135    551   -698       C  
ATOM   1269  CD  ARG A 144     -14.205 -20.100 -35.399  1.00 70.67           C  
ANISOU 1269  CD  ARG A 144     9776   9657   7420   -216    547   -829       C  
ATOM   1270  NE  ARG A 144     -15.579 -20.483 -35.096  1.00 81.03           N  
ANISOU 1270  NE  ARG A 144    11033  11043   8712   -265    478   -873       N  
ATOM   1271  CZ  ARG A 144     -15.938 -21.609 -34.484  1.00 84.95           C  
ANISOU 1271  CZ  ARG A 144    11508  11460   9311   -330    499   -957       C  
ATOM   1272  NH1 ARG A 144     -15.027 -22.499 -34.106  1.00 86.19           N1+
ANISOU 1272  NH1 ARG A 144    11691  11458   9599   -351    587  -1003       N1+
ATOM   1273  NH2 ARG A 144     -17.222 -21.846 -34.257  1.00 80.54           N  
ANISOU 1273  NH2 ARG A 144    10898  10980   8722   -372    434   -994       N  
ATOM   1274  H   ARG A 144     -15.391 -16.747 -31.961  1.00 43.23           H  
ATOM   1275  HE  ARG A 144     -16.204 -19.941 -35.330  1.00 98.06           H  
ATOM   1276 HH11 ARG A 144     -14.193 -22.351 -34.254  1.00104.25           H  
ATOM   1277 HH12 ARG A 144     -15.272 -23.223 -33.711  1.00104.25           H  
ATOM   1278 HH21 ARG A 144     -17.815 -21.275 -34.504  1.00 97.46           H  
ATOM   1279 HH22 ARG A 144     -17.462 -22.573 -33.863  1.00 97.46           H  
ATOM   1280  N   ASN A 145     -11.312 -17.419 -32.359  1.00 54.86           N  
ANISOU 1280  N   ASN A 145     7815   7297   5734     54    597   -409       N  
ATOM   1281  CA  ASN A 145      -9.989 -16.853 -32.636  1.00 55.20           C  
ANISOU 1281  CA  ASN A 145     7899   7283   5791    104    660   -361       C  
ATOM   1282  C   ASN A 145      -9.826 -15.447 -32.071  1.00 45.04           C  
ANISOU 1282  C   ASN A 145     6611   6002   4502    184    631   -221       C  
ATOM   1283  O   ASN A 145      -9.074 -14.623 -32.604  1.00 41.48           O  
ANISOU 1283  O   ASN A 145     6193   5563   4004    230    665   -172       O  
ATOM   1284  CB  ASN A 145      -9.680 -16.917 -34.123  1.00 57.68           C  
ANISOU 1284  CB  ASN A 145     8252   7679   5983     82    699   -429       C  
ATOM   1285  CG  ASN A 145      -9.205 -18.294 -34.527  1.00 70.25           C  
ANISOU 1285  CG  ASN A 145     9860   9204   7629     13    771   -560       C  
ATOM   1286  ND2 ASN A 145      -8.134 -18.751 -33.883  1.00 71.73           N  
ANISOU 1286  ND2 ASN A 145    10055   9240   7958     25    837   -556       N  
ATOM   1287  OD1 ASN A 145      -9.819 -18.967 -35.354  1.00 70.70           O  
ANISOU 1287  OD1 ASN A 145     9916   9342   7606    -53    768   -664       O  
ATOM   1288  H   ASN A 145     -11.259 -18.148 -31.906  1.00 66.66           H  
ATOM   1289 HD21 ASN A 145      -7.819 -19.528 -34.072  1.00 86.89           H  
ATOM   1290 HD22 ASN A 145      -7.757 -18.268 -33.279  1.00 86.89           H  
ATOM   1291  N   ARG A 146     -10.446 -15.218 -30.919  1.00 48.78           N  
ANISOU 1291  N   ARG A 146     7046   6449   5041    198    578   -162       N  
ATOM   1292  CA  ARG A 146     -10.345 -13.971 -30.186  1.00 32.60           C  
ANISOU 1292  CA  ARG A 146     4988   4389   3010    266    555    -35       C  
ATOM   1293  C   ARG A 146      -9.918 -14.239 -28.762  1.00 32.52           C  
ANISOU 1293  C   ARG A 146     4957   4248   3152    272    565      1       C  
ATOM   1294  O   ARG A 146     -10.079 -15.347 -28.234  1.00 36.46           O  
ANISOU 1294  O   ARG A 146     5438   4683   3732    226    569    -60       O  
ATOM   1295  CB  ARG A 146     -11.673 -13.233 -30.178  1.00 46.76           C  
ANISOU 1295  CB  ARG A 146     6751   6299   4716    281    473     15       C  
ATOM   1296  CG  ARG A 146     -12.131 -12.853 -31.547  1.00 59.20           C  
ANISOU 1296  CG  ARG A 146     8343   8018   6134    284    454     -4       C  
ATOM   1297  CD  ARG A 146     -13.430 -12.102 -31.476  1.00 64.65           C  
ANISOU 1297  CD  ARG A 146     8996   8822   6747    307    372     56       C  
ATOM   1298  NE  ARG A 146     -13.974 -11.893 -32.808  1.00 65.68           N  
ANISOU 1298  NE  ARG A 146     9134   9103   6717    304    346     30       N  
ATOM   1299  CZ  ARG A 146     -13.528 -10.979 -33.661  1.00 67.44           C  
ANISOU 1299  CZ  ARG A 146     9394   9384   6847    355    369     88       C  
ATOM   1300  NH1 ARG A 146     -12.526 -10.177 -33.323  1.00 72.75           N1+
ANISOU 1300  NH1 ARG A 146    10097   9971   7572    411    422    169       N1+
ATOM   1301  NH2 ARG A 146     -14.088 -10.867 -34.854  1.00 68.00           N  
ANISOU 1301  NH2 ARG A 146     9469   9600   6767    348    340     63       N  
ATOM   1302  H   ARG A 146     -10.950 -15.796 -30.530  1.00 59.36           H  
ATOM   1303  HE  ARG A 146     -14.627 -12.394 -33.059  1.00 79.63           H  
ATOM   1304 HH11 ARG A 146     -12.162 -10.247 -32.548  1.00 88.11           H  
ATOM   1305 HH12 ARG A 146     -12.242  -9.587 -33.881  1.00 88.11           H  
ATOM   1306 HH21 ARG A 146     -14.737 -11.386 -35.076  1.00 82.42           H  
ATOM   1307 HH22 ARG A 146     -13.802 -10.277 -35.410  1.00 82.42           H  
ATOM   1308  N   GLU A 147      -9.363 -13.226 -28.118  1.00 28.62           N  
ANISOU 1308  N   GLU A 147     4465   3715   2696    328    574    101       N  
ATOM   1309  CA  GLU A 147      -8.915 -13.383 -26.746  1.00 25.07           C  
ANISOU 1309  CA  GLU A 147     3993   3152   2381    336    581    142       C  
ATOM   1310  C   GLU A 147     -10.009 -13.015 -25.770  1.00 24.26           C  
ANISOU 1310  C   GLU A 147     3851   3072   2294    336    512    195       C  
ATOM   1311  O   GLU A 147     -10.668 -11.962 -25.910  1.00 34.69           O  
ANISOU 1311  O   GLU A 147     5165   4474   3541    368    474    257       O  
ATOM   1312  CB  GLU A 147      -7.653 -12.571 -26.468  1.00 35.68           C  
ANISOU 1312  CB  GLU A 147     5354   4434   3770    386    633    212       C  
ATOM   1313  CG  GLU A 147      -6.563 -12.746 -27.509  1.00 53.06           C  
ANISOU 1313  CG  GLU A 147     7595   6619   5945    392    705    167       C  
ATOM   1314  CD  GLU A 147      -5.428 -13.639 -27.043  1.00 80.11           C  
ANISOU 1314  CD  GLU A 147    11020   9925   9495    380    763    132       C  
ATOM   1315  OE1 GLU A 147      -4.920 -14.434 -27.865  1.00 84.05           O  
ANISOU 1315  OE1 GLU A 147    11542  10405   9989    355    812     52       O  
ATOM   1316  OE2 GLU A 147      -5.044 -13.550 -25.855  1.00 94.64           O1-
ANISOU 1316  OE2 GLU A 147    12833  11689  11435    396    760    185       O1-
ATOM   1317  H   GLU A 147      -9.238 -12.443 -28.451  1.00 35.17           H  
ATOM   1318  N   VAL A 148     -10.195 -13.856 -24.756  1.00 31.10           N  
ANISOU 1318  N   VAL A 148     4691   3864   3261    304    501    175       N  
ATOM   1319  CA  VAL A 148     -11.220 -13.692 -23.746  1.00 36.67           C  
ANISOU 1319  CA  VAL A 148     5359   4579   3995    295    441    213       C  
ATOM   1320  C   VAL A 148     -10.652 -13.862 -22.344  1.00 30.66           C  
ANISOU 1320  C   VAL A 148     4582   3707   3361    300    454    259       C  
ATOM   1321  O   VAL A 148      -9.590 -14.457 -22.134  1.00 33.80           O  
ANISOU 1321  O   VAL A 148     4991   4017   3836    300    504    243       O  
ATOM   1322  CB  VAL A 148     -12.394 -14.683 -23.939  1.00 19.78           C  
ANISOU 1322  CB  VAL A 148     3199   2482   1834    236    401    129       C  
ATOM   1323  CG1 VAL A 148     -12.895 -14.652 -25.365  1.00 20.72           C  
ANISOU 1323  CG1 VAL A 148     3331   2717   1823    223    389     72       C  
ATOM   1324  CG2 VAL A 148     -11.970 -16.102 -23.564  1.00 32.87           C  
ANISOU 1324  CG2 VAL A 148     4859   4038   3592    190    440     57       C  
ATOM   1325  H   VAL A 148      -9.715 -14.558 -24.630  1.00 38.14           H  
ATOM   1326  N   VAL A 149     -11.405 -13.335 -21.384  1.00 23.21           N  
ANISOU 1326  N   VAL A 149     3609   2773   2437    304    407    317       N  
ATOM   1327  CA  VAL A 149     -11.080 -13.368 -19.967  1.00 21.60           C  
ANISOU 1327  CA  VAL A 149     3385   2484   2339    306    407    369       C  
ATOM   1328  C   VAL A 149     -12.214 -14.050 -19.223  1.00 21.24           C  
ANISOU 1328  C   VAL A 149     3310   2433   2326    262    361    345       C  
ATOM   1329  O   VAL A 149     -13.393 -13.763 -19.468  1.00 34.15           O  
ANISOU 1329  O   VAL A 149     4929   4149   3898    250    313    337       O  
ATOM   1330  CB  VAL A 149     -10.863 -11.952 -19.398  1.00 16.36           C  
ANISOU 1330  CB  VAL A 149     2715   1832   1670    351    403    467       C  
ATOM   1331  CG1 VAL A 149     -10.581 -12.025 -17.907  1.00 26.86           C  
ANISOU 1331  CG1 VAL A 149     4021   3084   3102    344    400    514       C  
ATOM   1332  CG2 VAL A 149      -9.748 -11.260 -20.128  1.00 24.70           C  
ANISOU 1332  CG2 VAL A 149     3800   2890   2694    392    455    489       C  
ATOM   1333  H   VAL A 149     -12.149 -12.932 -21.541  1.00 28.67           H  
ATOM   1334  N   VAL A 150     -11.856 -14.940 -18.306  1.00 17.40           N  
ANISOU 1334  N   VAL A 150     2816   1854   1942    239    376    336       N  
ATOM   1335  CA  VAL A 150     -12.788 -15.554 -17.370  1.00 16.63           C  
ANISOU 1335  CA  VAL A 150     2693   1733   1894    200    341    326       C  
ATOM   1336  C   VAL A 150     -12.386 -15.108 -15.974  1.00 16.09           C  
ANISOU 1336  C   VAL A 150     2608   1605   1900    216    338    409       C  
ATOM   1337  O   VAL A 150     -11.208 -15.191 -15.609  1.00 18.81           O  
ANISOU 1337  O   VAL A 150     2960   1884   2303    238    376    438       O  
ATOM   1338  CB  VAL A 150     -12.778 -17.088 -17.482  1.00 19.73           C  
ANISOU 1338  CB  VAL A 150     3092   2064   2341    154    368    242       C  
ATOM   1339  CG1 VAL A 150     -13.638 -17.700 -16.399  1.00 27.55           C  
ANISOU 1339  CG1 VAL A 150     4058   3017   3392    115    340    240       C  
ATOM   1340  CG2 VAL A 150     -13.266 -17.512 -18.850  1.00 18.07           C  
ANISOU 1340  CG2 VAL A 150     2893   1923   2049    128    370    150       C  
ATOM   1341  H   VAL A 150     -11.047 -15.214 -18.202  1.00 21.70           H  
ATOM   1342  N   VAL A 151     -13.354 -14.605 -15.207  1.00 23.32           N  
ANISOU 1342  N   VAL A 151     3500   2549   2813    205    293    447       N  
ATOM   1343  CA  VAL A 151     -13.116 -14.166 -13.839  1.00 25.61           C  
ANISOU 1343  CA  VAL A 151     3773   2793   3166    212    286    521       C  
ATOM   1344  C   VAL A 151     -13.872 -15.090 -12.904  1.00 18.35           C  
ANISOU 1344  C   VAL A 151     2836   1829   2306    166    264    502       C  
ATOM   1345  O   VAL A 151     -15.095 -15.241 -13.024  1.00 21.36           O  
ANISOU 1345  O   VAL A 151     3204   2255   2656    136    229    468       O  
ATOM   1346  CB  VAL A 151     -13.564 -12.718 -13.594  1.00 29.63           C  
ANISOU 1346  CB  VAL A 151     4269   3361   3628    237    262    588       C  
ATOM   1347  CG1 VAL A 151     -12.868 -12.176 -12.349  1.00 21.42           C  
ANISOU 1347  CG1 VAL A 151     3217   2270   2650    248    275    660       C  
ATOM   1348  CG2 VAL A 151     -13.290 -11.839 -14.783  1.00 26.85           C  
ANISOU 1348  CG2 VAL A 151     3934   3073   3193    277    277    594       C  
ATOM   1349  H   VAL A 151     -14.169 -14.510 -15.464  1.00 28.81           H  
ATOM   1350  N   GLY A 152     -13.156 -15.670 -11.953  1.00 20.93           N  
ANISOU 1350  N   GLY A 152     3162   2073   2718    162    285    528       N  
ATOM   1351  CA  GLY A 152     -13.784 -16.400 -10.868  1.00 24.37           C  
ANISOU 1351  CA  GLY A 152     3583   2462   3214    124    268    530       C  
ATOM   1352  C   GLY A 152     -13.189 -17.781 -10.721  1.00 20.02           C  
ANISOU 1352  C   GLY A 152     3044   1824   2740    110    305    497       C  
ATOM   1353  O   GLY A 152     -12.728 -18.395 -11.687  1.00 26.64           O  
ANISOU 1353  O   GLY A 152     3900   2649   3573    115    339    441       O  
ATOM   1354  H   GLY A 152     -12.297 -15.656 -11.915  1.00 25.93           H  
ATOM   1355  N   LEU A 153     -13.208 -18.284  -9.495  1.00 25.46           N  
ANISOU 1355  N   LEU A 153     3722   2451   3499     94    303    533       N  
ATOM   1356  CA  LEU A 153     -12.745 -19.629  -9.175  1.00 14.97           C  
ANISOU 1356  CA  LEU A 153     2403   1032   2254     83    340    515       C  
ATOM   1357  C   LEU A 153     -13.895 -20.365  -8.505  1.00 21.06           C  
ANISOU 1357  C   LEU A 153     3168   1778   3056     33    323    491       C  
ATOM   1358  O   LEU A 153     -14.138 -20.201  -7.306  1.00 39.85           O  
ANISOU 1358  O   LEU A 153     5535   4139   5466     23    303    549       O  
ATOM   1359  CB  LEU A 153     -11.521 -19.573  -8.281  1.00 18.33           C  
ANISOU 1359  CB  LEU A 153     2821   1403   2740    117    357    592       C  
ATOM   1360  CG  LEU A 153     -10.958 -20.900  -7.788  1.00 18.88           C  
ANISOU 1360  CG  LEU A 153     2882   1405   2887    111    379    578       C  
ATOM   1361  CD1 LEU A 153     -10.659 -21.816  -8.946  1.00 22.85           C  
ANISOU 1361  CD1 LEU A 153     3418   1844   3419    116    444    516       C  
ATOM   1362  CD2 LEU A 153      -9.706 -20.603  -6.981  1.00 26.14           C  
ANISOU 1362  CD2 LEU A 153     3756   2373   3804    136    346    609       C  
ATOM   1363  H   LEU A 153     -13.494 -17.851  -8.809  1.00 31.37           H  
ATOM   1364  N   ASN A 154     -14.599 -21.163  -9.288  1.00 15.74           N  
ANISOU 1364  N   ASN A 154     2504   1106   2371     -2    335    403       N  
ATOM   1365  CA  ASN A 154     -15.733 -21.953  -8.838  1.00 16.02           C  
ANISOU 1365  CA  ASN A 154     2535   1118   2434    -56    328    361       C  
ATOM   1366  C   ASN A 154     -16.054 -22.910  -9.979  1.00 18.04           C  
ANISOU 1366  C   ASN A 154     2804   1370   2681    -88    361    253       C  
ATOM   1367  O   ASN A 154     -15.530 -22.743 -11.090  1.00 30.60           O  
ANISOU 1367  O   ASN A 154     4405   2993   4227    -68    377    216       O  
ATOM   1368  CB  ASN A 154     -16.928 -21.075  -8.476  1.00 23.70           C  
ANISOU 1368  CB  ASN A 154     3485   2165   3354    -78    272    375       C  
ATOM   1369  CG  ASN A 154     -17.226 -20.037  -9.528  1.00 19.88           C  
ANISOU 1369  CG  ASN A 154     2994   1787   2774    -60    242    356       C  
ATOM   1370  ND2 ASN A 154     -17.127 -18.767  -9.153  1.00 21.09           N  
ANISOU 1370  ND2 ASN A 154     3135   1986   2892    -30    212    428       N  
ATOM   1371  OD1 ASN A 154     -17.553 -20.369 -10.663  1.00 22.36           O  
ANISOU 1371  OD1 ASN A 154     3313   2141   3043    -75    248    278       O  
ATOM   1372  H   ASN A 154     -14.433 -21.270 -10.126  1.00 19.57           H  
ATOM   1373 HD21 ASN A 154     -17.287 -18.138  -9.717  1.00 26.12           H  
ATOM   1374 HD22 ASN A 154     -16.903 -18.573  -8.345  1.00 26.12           H  
ATOM   1375  N   PRO A 155     -16.897 -23.915  -9.751  1.00 28.55           N  
ANISOU 1375  N   PRO A 155     4136   2661   4052   -140    375    195       N  
ATOM   1376  CA  PRO A 155     -17.182 -24.884 -10.825  1.00 26.51           C  
ANISOU 1376  CA  PRO A 155     3889   2396   3788   -179    415     82       C  
ATOM   1377  C   PRO A 155     -17.828 -24.270 -12.057  1.00 18.45           C  
ANISOU 1377  C   PRO A 155     2858   1495   2659   -192    381     15       C  
ATOM   1378  O   PRO A 155     -17.571 -24.743 -13.175  1.00 26.61           O  
ANISOU 1378  O   PRO A 155     3905   2539   3667   -203    415    -63       O  
ATOM   1379  CB  PRO A 155     -18.112 -25.892 -10.132  1.00 22.51           C  
ANISOU 1379  CB  PRO A 155     3379   1830   3342   -236    431     43       C  
ATOM   1380  CG  PRO A 155     -17.722 -25.796  -8.671  1.00 18.00           C  
ANISOU 1380  CG  PRO A 155     2808   1191   2839   -211    426    150       C  
ATOM   1381  CD  PRO A 155     -17.468 -24.332  -8.461  1.00 17.16           C  
ANISOU 1381  CD  PRO A 155     2686   1163   2670   -168    370    231       C  
ATOM   1382  N   GLU A 156     -18.653 -23.232 -11.905  1.00 22.54           N  
ANISOU 1382  N   GLU A 156     3352   2103   3111   -190    317     45       N  
ATOM   1383  CA  GLU A 156     -19.213 -22.574 -13.081  1.00 18.27           C  
ANISOU 1383  CA  GLU A 156     2798   1682   2461   -193    282     -3       C  
ATOM   1384  C   GLU A 156     -18.107 -21.970 -13.938  1.00 28.60           C  
ANISOU 1384  C   GLU A 156     4125   3017   3724   -140    296     20       C  
ATOM   1385  O   GLU A 156     -18.035 -22.214 -15.151  1.00 25.70           O  
ANISOU 1385  O   GLU A 156     3768   2696   3302   -150    313    -54       O  
ATOM   1386  CB  GLU A 156     -20.215 -21.489 -12.678  1.00 18.24           C  
ANISOU 1386  CB  GLU A 156     2763   1764   2405   -189    214     42       C  
ATOM   1387  CG  GLU A 156     -21.066 -21.032 -13.864  1.00 38.74           C  
ANISOU 1387  CG  GLU A 156     5338   4488   4894   -201    175    -18       C  
ATOM   1388  CD  GLU A 156     -21.971 -19.842 -13.587  1.00 35.21           C  
ANISOU 1388  CD  GLU A 156     4857   4129   4391   -184    112     36       C  
ATOM   1389  OE1 GLU A 156     -21.992 -19.331 -12.447  1.00 34.51           O  
ANISOU 1389  OE1 GLU A 156     4761   4002   4348   -169     99    114       O  
ATOM   1390  OE2 GLU A 156     -22.674 -19.424 -14.534  1.00 45.75           O1-
ANISOU 1390  OE2 GLU A 156     6171   5575   5637   -187     76     -2       O1-
ATOM   1391  H   GLU A 156     -18.897 -22.900 -11.151  1.00 27.87           H  
ATOM   1392  N   ALA A 157     -17.232 -21.172 -13.314  1.00 25.87           N  
ANISOU 1392  N   ALA A 157     3785   2647   3399    -86    293    119       N  
ATOM   1393  CA  ALA A 157     -16.121 -20.556 -14.028  1.00 17.38           C  
ANISOU 1393  CA  ALA A 157     2727   1589   2287    -35    312    147       C  
ATOM   1394  C   ALA A 157     -15.297 -21.599 -14.769  1.00 19.78           C  
ANISOU 1394  C   ALA A 157     3057   1835   2625    -42    375     80       C  
ATOM   1395  O   ALA A 157     -14.906 -21.387 -15.924  1.00 18.41           O  
ANISOU 1395  O   ALA A 157     2898   1709   2389    -29    391     42       O  
ATOM   1396  CB  ALA A 157     -15.240 -19.776 -13.049  1.00 16.56           C  
ANISOU 1396  CB  ALA A 157     2621   1446   2224     13    310    255       C  
ATOM   1397  H   ALA A 157     -17.265 -20.973 -12.478  1.00 31.87           H  
ATOM   1398  N   VAL A 158     -15.039 -22.741 -14.127  1.00 18.26           N  
ANISOU 1398  N   VAL A 158     2871   1537   2531    -63    417     66       N  
ATOM   1399  CA  VAL A 158     -14.222 -23.771 -14.759  1.00 24.89           C  
ANISOU 1399  CA  VAL A 158     3733   2307   3416    -68    487      7       C  
ATOM   1400  C   VAL A 158     -14.926 -24.347 -15.976  1.00 32.48           C  
ANISOU 1400  C   VAL A 158     4700   3321   4319   -120    501   -115       C  
ATOM   1401  O   VAL A 158     -14.309 -24.568 -17.022  1.00 26.68           O  
ANISOU 1401  O   VAL A 158     3985   2593   3558   -117    541   -169       O  
ATOM   1402  CB  VAL A 158     -13.880 -24.891 -13.760  1.00 25.24           C  
ANISOU 1402  CB  VAL A 158     3782   2224   3584    -77    532     24       C  
ATOM   1403  CG1 VAL A 158     -13.309 -26.095 -14.507  1.00 26.58           C  
ANISOU 1403  CG1 VAL A 158     3974   2321   3805    -95    612    -58       C  
ATOM   1404  CG2 VAL A 158     -12.911 -24.404 -12.720  1.00 23.68           C  
ANISOU 1404  CG2 VAL A 158     3578   1978   3440    -22    527    139       C  
ATOM   1405  H   VAL A 158     -15.322 -22.939 -13.339  1.00 22.52           H  
ATOM   1406  N   GLU A 159     -16.217 -24.648 -15.852  1.00 32.35           N  
ANISOU 1406  N   GLU A 159     4667   3342   4284   -174    471   -166       N  
ATOM   1407  CA  GLU A 159     -16.928 -25.282 -16.954  1.00 25.00           C  
ANISOU 1407  CA  GLU A 159     3735   2464   3298   -233    485   -291       C  
ATOM   1408  C   GLU A 159     -17.159 -24.310 -18.098  1.00 24.80           C  
ANISOU 1408  C   GLU A 159     3705   2576   3142   -219    442   -308       C  
ATOM   1409  O   GLU A 159     -17.080 -24.706 -19.265  1.00 21.87           O  
ANISOU 1409  O   GLU A 159     3347   2245   2719   -245    471   -397       O  
ATOM   1410  CB  GLU A 159     -18.203 -25.913 -16.403  1.00 33.19           C  
ANISOU 1410  CB  GLU A 159     4752   3497   4362   -295    470   -340       C  
ATOM   1411  CG  GLU A 159     -17.806 -27.075 -15.483  1.00 42.26           C  
ANISOU 1411  CG  GLU A 159     5916   4497   5645   -310    534   -334       C  
ATOM   1412  CD  GLU A 159     -18.926 -27.602 -14.634  1.00 53.09           C  
ANISOU 1412  CD  GLU A 159     7269   5842   7059   -361    522   -354       C  
ATOM   1413  OE1 GLU A 159     -19.973 -27.943 -15.211  1.00 52.12           O  
ANISOU 1413  OE1 GLU A 159     7131   5781   6890   -423    512   -453       O  
ATOM   1414  OE2 GLU A 159     -18.755 -27.696 -13.397  1.00 69.81           O1-
ANISOU 1414  OE2 GLU A 159     9389   7880   9256   -343    524   -273       O1-
ATOM   1415  H   GLU A 159     -16.694 -24.498 -15.152  1.00 39.64           H  
ATOM   1416  N   GLU A 160     -17.393 -23.035 -17.782  1.00 24.81           N  
ANISOU 1416  N   GLU A 160     3690   2648   3090   -176    379   -221       N  
ATOM   1417  CA  GLU A 160     -17.587 -22.032 -18.820  1.00 20.49           C  
ANISOU 1417  CA  GLU A 160     3139   2229   2419   -153    340   -220       C  
ATOM   1418  C   GLU A 160     -16.289 -21.731 -19.553  1.00 20.53           C  
ANISOU 1418  C   GLU A 160     3175   2220   2404   -108    381   -203       C  
ATOM   1419  O   GLU A 160     -16.297 -21.471 -20.763  1.00 23.84           O  
ANISOU 1419  O   GLU A 160     3604   2726   2728   -109    380   -249       O  
ATOM   1420  CB  GLU A 160     -18.149 -20.762 -18.193  1.00 25.90           C  
ANISOU 1420  CB  GLU A 160     3798   2974   3067   -116    272   -125       C  
ATOM   1421  CG  GLU A 160     -19.558 -20.939 -17.693  1.00 33.54           C  
ANISOU 1421  CG  GLU A 160     4730   3980   4034   -162    226   -151       C  
ATOM   1422  CD  GLU A 160     -20.576 -20.819 -18.809  1.00 32.18           C  
ANISOU 1422  CD  GLU A 160     4535   3943   3750   -192    187   -226       C  
ATOM   1423  OE1 GLU A 160     -21.028 -19.685 -19.064  1.00 30.11           O  
ANISOU 1423  OE1 GLU A 160     4253   3780   3408   -156    133   -173       O  
ATOM   1424  OE2 GLU A 160     -20.926 -21.845 -19.434  1.00 41.00           O1-
ANISOU 1424  OE2 GLU A 160     5651   5068   4859   -252    211   -337       O1-
ATOM   1425  H   GLU A 160     -17.443 -22.730 -16.980  1.00 30.60           H  
ATOM   1426  N   ALA A 161     -15.167 -21.743 -18.833  1.00 31.13           N  
ANISOU 1426  N   ALA A 161     4534   3461   3834    -68    418   -136       N  
ATOM   1427  CA  ALA A 161     -13.872 -21.559 -19.476  1.00 23.29           C  
ANISOU 1427  CA  ALA A 161     3569   2444   2836    -28    466   -125       C  
ATOM   1428  C   ALA A 161     -13.570 -22.711 -20.422  1.00 21.02           C  
ANISOU 1428  C   ALA A 161     3302   2126   2557    -70    529   -236       C  
ATOM   1429  O   ALA A 161     -13.022 -22.505 -21.512  1.00 28.92           O  
ANISOU 1429  O   ALA A 161     4325   3168   3496    -59    555   -269       O  
ATOM   1430  CB  ALA A 161     -12.781 -21.423 -18.415  1.00 28.02           C  
ANISOU 1430  CB  ALA A 161     4171   2941   3533     18    490    -34       C  
ATOM   1431  H   ALA A 161     -15.131 -21.853 -17.981  1.00 38.18           H  
ATOM   1432  N   GLN A 162     -13.923 -23.939 -20.024  1.00 27.48           N  
ANISOU 1432  N   GLN A 162     4117   2869   3455   -120    561   -297       N  
ATOM   1433  CA  GLN A 162     -13.762 -25.079 -20.917  1.00 28.85           C  
ANISOU 1433  CA  GLN A 162     4310   3013   3640   -169    628   -414       C  
ATOM   1434  C   GLN A 162     -14.536 -24.871 -22.207  1.00 36.00           C  
ANISOU 1434  C   GLN A 162     5213   4052   4414   -208    603   -502       C  
ATOM   1435  O   GLN A 162     -14.033 -25.162 -23.299  1.00 40.70           O  
ANISOU 1435  O   GLN A 162     5831   4665   4969   -222    649   -572       O  
ATOM   1436  CB  GLN A 162     -14.229 -26.355 -20.225  1.00 33.33           C  
ANISOU 1436  CB  GLN A 162     4870   3484   4309   -220    664   -464       C  
ATOM   1437  CG  GLN A 162     -13.359 -26.712 -19.049  1.00 41.23           C  
ANISOU 1437  CG  GLN A 162     5875   4350   5441   -180    699   -381       C  
ATOM   1438  CD  GLN A 162     -13.353 -28.185 -18.745  1.00 43.58           C  
ANISOU 1438  CD  GLN A 162     6181   4528   5848   -223    773   -444       C  
ATOM   1439  NE2 GLN A 162     -14.055 -28.572 -17.689  1.00 47.57           N  
ANISOU 1439  NE2 GLN A 162     6673   4989   6414   -244    757   -419       N  
ATOM   1440  OE1 GLN A 162     -12.709 -28.971 -19.438  1.00 50.80           O  
ANISOU 1440  OE1 GLN A 162     7116   5387   6798   -236    850   -512       O  
ATOM   1441  H   GLN A 162     -14.251 -24.131 -19.253  1.00 33.80           H  
ATOM   1442 HE21 GLN A 162     -14.481 -27.990 -17.221  1.00 57.91           H  
ATOM   1443 HE22 GLN A 162     -14.084 -29.404 -17.473  1.00 57.91           H  
ATOM   1444  N   VAL A 163     -15.773 -24.376 -22.097  1.00 46.63           N  
ANISOU 1444  N   VAL A 163     6529   5497   5690   -228    529   -499       N  
ATOM   1445  CA  VAL A 163     -16.556 -24.045 -23.282  1.00 40.01           C  
ANISOU 1445  CA  VAL A 163     5681   4805   4715   -258    491   -568       C  
ATOM   1446  C   VAL A 163     -15.783 -23.072 -24.159  1.00 36.16           C  
ANISOU 1446  C   VAL A 163     5217   4383   4141   -204    489   -525       C  
ATOM   1447  O   VAL A 163     -15.667 -23.255 -25.373  1.00 33.85           O  
ANISOU 1447  O   VAL A 163     4940   4155   3767   -229    512   -603       O  
ATOM   1448  CB  VAL A 163     -17.925 -23.464 -22.885  1.00 40.02           C  
ANISOU 1448  CB  VAL A 163     5641   4902   4662   -270    406   -544       C  
ATOM   1449  CG1 VAL A 163     -18.646 -22.914 -24.118  1.00 36.58           C  
ANISOU 1449  CG1 VAL A 163     5190   4633   4074   -284    357   -590       C  
ATOM   1450  CG2 VAL A 163     -18.788 -24.501 -22.193  1.00 42.94           C  
ANISOU 1450  CG2 VAL A 163     5989   5219   5107   -336    413   -606       C  
ATOM   1451  H   VAL A 163     -16.176 -24.225 -21.353  1.00 56.77           H  
ATOM   1452  N   LEU A 164     -15.230 -22.024 -23.546  1.00 35.93           N  
ANISOU 1452  N   LEU A 164     5190   4337   4126   -132    465   -403       N  
ATOM   1453  CA  LEU A 164     -14.568 -20.984 -24.322  1.00 36.66           C  
ANISOU 1453  CA  LEU A 164     5303   4493   4133    -79    463   -355       C  
ATOM   1454  C   LEU A 164     -13.282 -21.476 -24.982  1.00 34.46           C  
ANISOU 1454  C   LEU A 164     5062   4148   3882    -73    544   -395       C  
ATOM   1455  O   LEU A 164     -12.892 -20.917 -26.015  1.00 32.26           O  
ANISOU 1455  O   LEU A 164     4805   3940   3512    -53    553   -401       O  
ATOM   1456  CB  LEU A 164     -14.286 -19.776 -23.428  1.00 34.55           C  
ANISOU 1456  CB  LEU A 164     5027   4213   3886    -10    427   -221       C  
ATOM   1457  CG  LEU A 164     -15.550 -19.035 -22.976  1.00 36.03           C  
ANISOU 1457  CG  LEU A 164     5178   4485   4025     -7    347   -175       C  
ATOM   1458  CD1 LEU A 164     -15.244 -18.027 -21.876  1.00 38.78           C  
ANISOU 1458  CD1 LEU A 164     5518   4794   4421     50    326    -51       C  
ATOM   1459  CD2 LEU A 164     -16.226 -18.354 -24.162  1.00 36.29           C  
ANISOU 1459  CD2 LEU A 164     5206   4671   3913     -3    305   -194       C  
ATOM   1460  H   LEU A 164     -15.226 -21.895 -22.696  1.00 43.94           H  
ATOM   1461  N   THR A 165     -12.633 -22.518 -24.448  1.00 37.23           N  
ANISOU 1461  N   THR A 165     5422   4368   4357    -89    607   -423       N  
ATOM   1462  CA  THR A 165     -11.434 -23.041 -25.103  1.00 27.27           C  
ANISOU 1462  CA  THR A 165     4193   3040   3128    -85    690   -466       C  
ATOM   1463  C   THR A 165     -11.732 -23.686 -26.448  1.00 28.14           C  
ANISOU 1463  C   THR A 165     4319   3215   3158   -146    723   -596       C  
ATOM   1464  O   THR A 165     -10.797 -24.003 -27.190  1.00 33.89           O  
ANISOU 1464  O   THR A 165     5077   3909   3892   -146    791   -639       O  
ATOM   1465  CB  THR A 165     -10.709 -24.085 -24.247  1.00 32.77           C  
ANISOU 1465  CB  THR A 165     4892   3581   3980    -87    754   -467       C  
ATOM   1466  CG2 THR A 165     -10.270 -23.485 -22.931  1.00 23.10           C  
ANISOU 1466  CG2 THR A 165     3651   2294   2832    -29    726   -341       C  
ATOM   1467  OG1 THR A 165     -11.564 -25.212 -24.020  1.00 30.89           O  
ANISOU 1467  OG1 THR A 165     4641   3310   3785   -154    765   -549       O  
ATOM   1468  H   THR A 165     -12.863 -22.927 -23.728  1.00 45.50           H  
ATOM   1469  HG1 THR A 165     -12.261 -24.967 -23.621  1.00 37.88           H  
ATOM   1470  N   LYS A 166     -13.001 -23.905 -26.770  1.00 29.42           N  
ANISOU 1470  N   LYS A 166     4460   3469   3248   -202    678   -662       N  
ATOM   1471  CA  LYS A 166     -13.363 -24.445 -28.069  1.00 26.30           C  
ANISOU 1471  CA  LYS A 166     4076   3157   2761   -266    701   -788       C  
ATOM   1472  C   LYS A 166     -13.436 -23.369 -29.138  1.00 26.53           C  
ANISOU 1472  C   LYS A 166     4115   3331   2634   -239    660   -767       C  
ATOM   1473  O   LYS A 166     -13.540 -23.710 -30.321  1.00 30.79           O  
ANISOU 1473  O   LYS A 166     4668   3947   3084   -286    684   -865       O  
ATOM   1474  CB  LYS A 166     -14.703 -25.165 -27.954  1.00 27.49           C  
ANISOU 1474  CB  LYS A 166     4194   3352   2900   -341    671   -873       C  
ATOM   1475  CG  LYS A 166     -14.688 -26.228 -26.875  1.00 33.48           C  
ANISOU 1475  CG  LYS A 166     4945   3963   3811   -367    715   -889       C  
ATOM   1476  CD  LYS A 166     -16.077 -26.638 -26.443  1.00 52.24           C  
ANISOU 1476  CD  LYS A 166     7283   6381   6184   -425    669   -936       C  
ATOM   1477  CE  LYS A 166     -16.022 -27.851 -25.518  1.00 72.60           C  
ANISOU 1477  CE  LYS A 166     9862   8807   8914   -460    731   -967       C  
ATOM   1478  NZ  LYS A 166     -16.673 -27.591 -24.199  1.00 67.61           N1+
ANISOU 1478  NZ  LYS A 166     9202   8144   8341   -441    675   -884       N1+
ATOM   1479  H   LYS A 166     -13.668 -23.748 -26.252  1.00 36.12           H  
ATOM   1480  HZ1 LYS A 166     -16.625 -28.318 -23.688  1.00 81.95           H  
ATOM   1481  HZ2 LYS A 166     -16.263 -26.919 -23.785  1.00 81.95           H  
ATOM   1482  HZ3 LYS A 166     -17.529 -27.378 -24.319  1.00 81.95           H  
ATOM   1483  N   PHE A 167     -13.313 -22.097 -28.755  1.00 27.71           N  
ANISOU 1483  N   PHE A 167     4260   3516   2752   -165    608   -643       N  
ATOM   1484  CA  PHE A 167     -13.414 -20.994 -29.699  1.00 25.89           C  
ANISOU 1484  CA  PHE A 167     4040   3420   2377   -131    570   -607       C  
ATOM   1485  C   PHE A 167     -12.260 -20.004 -29.622  1.00 29.00           C  
ANISOU 1485  C   PHE A 167     4462   3774   2783    -52    593   -503       C  
ATOM   1486  O   PHE A 167     -11.707 -19.601 -30.653  1.00 26.03           O  
ANISOU 1486  O   PHE A 167     4117   3450   2322    -36    621   -513       O  
ATOM   1487  CB  PHE A 167     -14.719 -20.231 -29.458  1.00 35.96           C  
ANISOU 1487  CB  PHE A 167     5275   4812   3575   -121    473   -558       C  
ATOM   1488  CG  PHE A 167     -15.932 -21.094 -29.454  1.00 37.58           C  
ANISOU 1488  CG  PHE A 167     5444   5065   3769   -198    442   -654       C  
ATOM   1489  CD1 PHE A 167     -16.365 -21.687 -30.622  1.00 33.19           C  
ANISOU 1489  CD1 PHE A 167     4890   4606   3116   -263    451   -774       C  
ATOM   1490  CD2 PHE A 167     -16.642 -21.316 -28.289  1.00 31.90           C  
ANISOU 1490  CD2 PHE A 167     4690   4297   3133   -209    407   -629       C  
ATOM   1491  CE1 PHE A 167     -17.486 -22.485 -30.631  1.00 30.03           C  
ANISOU 1491  CE1 PHE A 167     4453   4254   2704   -340    427   -870       C  
ATOM   1492  CE2 PHE A 167     -17.765 -22.114 -28.291  1.00 26.39           C  
ANISOU 1492  CE2 PHE A 167     3959   3642   2427   -283    384   -722       C  
ATOM   1493  CZ  PHE A 167     -18.188 -22.698 -29.465  1.00 27.60           C  
ANISOU 1493  CZ  PHE A 167     4109   3892   2484   -349    394   -844       C  
ATOM   1494  H   PHE A 167     -13.168 -21.849 -27.945  1.00 34.07           H  
ATOM   1495  N   ALA A 168     -11.901 -19.601 -28.409  1.00 24.88           N  
ANISOU 1495  N   ALA A 168     3929   3163   2361     -5    584   -406       N  
ATOM   1496  CA  ALA A 168     -10.992 -18.481 -28.223  1.00 30.61           C  
ANISOU 1496  CA  ALA A 168     4672   3868   3090     70    594   -299       C  
ATOM   1497  C   ALA A 168      -9.553 -18.801 -28.609  1.00 34.05           C  
ANISOU 1497  C   ALA A 168     5143   4216   3577     84    681   -320       C  
ATOM   1498  O   ALA A 168      -9.098 -19.954 -28.531  1.00 47.07           O  
ANISOU 1498  O   ALA A 168     6799   5774   5313     47    738   -392       O  
ATOM   1499  CB  ALA A 168     -11.026 -18.014 -26.765  1.00 38.61           C  
ANISOU 1499  CB  ALA A 168     5660   4813   4198    108    562   -198       C  
ATOM   1500  H   ALA A 168     -12.170 -19.963 -27.676  1.00 30.67           H  
ATOM   1501  N   SER A 169      -8.867 -17.750 -29.078  1.00 31.75           N  
ANISOU 1501  N   SER A 169     4877   3958   3230    137    694   -258       N  
ATOM   1502  CA  SER A 169      -7.419 -17.719 -29.268  1.00 39.83           C  
ANISOU 1502  CA  SER A 169     5929   4898   4306    167    771   -248       C  
ATOM   1503  C   SER A 169      -6.677 -18.020 -27.977  1.00 37.67           C  
ANISOU 1503  C   SER A 169     5636   4489   4186    189    794   -199       C  
ATOM   1504  O   SER A 169      -5.642 -18.686 -27.967  1.00 29.61           O  
ANISOU 1504  O   SER A 169     4627   3373   3251    189    863   -230       O  
ATOM   1505  CB  SER A 169      -6.990 -16.326 -29.731  1.00 35.82           C  
ANISOU 1505  CB  SER A 169     5444   4451   3716    226    770   -167       C  
ATOM   1506  OG  SER A 169      -7.468 -16.012 -31.014  1.00 54.57           O  
ANISOU 1506  OG  SER A 169     7842   6948   5945    214    758   -204       O  
ATOM   1507  H   SER A 169      -9.237 -17.007 -29.303  1.00 38.93           H  
ATOM   1508  HG  SER A 169      -7.220 -15.241 -31.233  1.00 66.31           H  
ATOM   1509  N   THR A 170      -7.107 -17.337 -26.921  1.00 34.62           N  
ANISOU 1509  N   THR A 170     5222   4104   3827    219    738   -110       N  
ATOM   1510  CA  THR A 170      -6.560 -17.497 -25.592  1.00 30.98           C  
ANISOU 1510  CA  THR A 170     4738   3536   3498    240    745    -51       C  
ATOM   1511  C   THR A 170      -7.665 -17.200 -24.593  1.00 20.37           C  
ANISOU 1511  C   THR A 170     3361   2218   2161    235    670     -1       C  
ATOM   1512  O   THR A 170      -8.457 -16.266 -24.772  1.00 29.48           O  
ANISOU 1512  O   THR A 170     4510   3466   3226    249    618     39       O  
ATOM   1513  CB  THR A 170      -5.360 -16.589 -25.350  1.00 39.73           C  
ANISOU 1513  CB  THR A 170     5853   4606   4635    297    778     26       C  
ATOM   1514  CG2 THR A 170      -4.904 -16.719 -23.909  1.00 41.37           C  
ANISOU 1514  CG2 THR A 170     6030   4721   4968    316    774     89       C  
ATOM   1515  OG1 THR A 170      -4.293 -16.981 -26.220  1.00 58.67           O  
ANISOU 1515  OG1 THR A 170     8282   6969   7042    299    854    -27       O  
ATOM   1516  H   THR A 170      -7.739 -16.755 -26.956  1.00 42.36           H  
ATOM   1517  HG1 THR A 170      -4.075 -17.778 -26.066  1.00 71.23           H  
ATOM   1518  N   VAL A 171      -7.695 -18.009 -23.546  1.00 20.09           N  
ANISOU 1518  N   VAL A 171     3303   2096   2235    217    670      0       N  
ATOM   1519  CA  VAL A 171      -8.582 -17.825 -22.410  1.00 21.81           C  
ANISOU 1519  CA  VAL A 171     3488   2315   2482    212    609     51       C  
ATOM   1520  C   VAL A 171      -7.709 -17.420 -21.230  1.00 27.51           C  
ANISOU 1520  C   VAL A 171     4196   2960   3298    252    619    141       C  
ATOM   1521  O   VAL A 171      -7.020 -18.258 -20.632  1.00 27.56           O  
ANISOU 1521  O   VAL A 171     4195   2869   3408    250    654    136       O  
ATOM   1522  CB  VAL A 171      -9.384 -19.089 -22.092  1.00 19.88           C  
ANISOU 1522  CB  VAL A 171     3231   2038   2286    155    601    -18       C  
ATOM   1523  CG1 VAL A 171     -10.219 -18.850 -20.852  1.00 19.23           C  
ANISOU 1523  CG1 VAL A 171     3117   1951   2240    151    543     40       C  
ATOM   1524  CG2 VAL A 171     -10.248 -19.496 -23.266  1.00 26.83           C  
ANISOU 1524  CG2 VAL A 171     4120   3003   3070    107    593   -116       C  
ATOM   1525  H   VAL A 171      -7.189 -18.700 -23.467  1.00 20.02           H  
ATOM   1526  N   HIS A 172      -7.736 -16.134 -20.894  1.00 37.43           N  
ANISOU 1526  N   HIS A 172     5445   4261   4516    289    589    223       N  
ATOM   1527  CA  HIS A 172      -7.086 -15.622 -19.698  1.00 22.80           C  
ANISOU 1527  CA  HIS A 172     3572   2352   2738    320    589    307       C  
ATOM   1528  C   HIS A 172      -7.956 -15.920 -18.489  1.00 16.88           C  
ANISOU 1528  C   HIS A 172     2793   1583   2038    296    540    334       C  
ATOM   1529  O   HIS A 172      -9.080 -15.414 -18.399  1.00 41.50           O  
ANISOU 1529  O   HIS A 172     5901   4768   5101    284    489    346       O  
ATOM   1530  CB  HIS A 172      -6.891 -14.116 -19.797  1.00 29.63           C  
ANISOU 1530  CB  HIS A 172     4441   3274   3543    361    581    378       C  
ATOM   1531  CG  HIS A 172      -5.962 -13.691 -20.883  1.00 17.23           C  
ANISOU 1531  CG  HIS A 172     2901   1719   1926    389    633    364       C  
ATOM   1532  CD2 HIS A 172      -6.190 -13.054 -22.054  1.00 17.81           C  
ANISOU 1532  CD2 HIS A 172     3002   1872   1894    402    638    350       C  
ATOM   1533  ND1 HIS A 172      -4.602 -13.898 -20.816  1.00 17.17           N  
ANISOU 1533  ND1 HIS A 172     2897   1641   1985    409    691    366       N  
ATOM   1534  CE1 HIS A 172      -4.031 -13.411 -21.901  1.00 17.53           C  
ANISOU 1534  CE1 HIS A 172     2973   1717   1969    429    732    351       C  
ATOM   1535  NE2 HIS A 172      -4.973 -12.895 -22.671  1.00 17.79           N  
ANISOU 1535  NE2 HIS A 172     3023   1842   1895    426    702    342       N  
ATOM   1536  H   HIS A 172      -8.133 -15.526 -21.355  1.00 45.73           H  
ATOM   1537  HE2 HIS A 172      -4.845 -12.519 -23.434  1.00 17.54           H  
ATOM   1538  N   TRP A 173      -7.448 -16.691 -17.540  1.00 20.59           N  
ANISOU 1538  N   TRP A 173     3247   1964   2612    290    556    347       N  
ATOM   1539  CA  TRP A 173      -8.223 -17.056 -16.363  1.00 18.24           C  
ANISOU 1539  CA  TRP A 173     2925   1640   2365    265    515    372       C  
ATOM   1540  C   TRP A 173      -7.709 -16.331 -15.133  1.00 32.39           C  
ANISOU 1540  C   TRP A 173     4694   3408   4204    291    503    464       C  
ATOM   1541  O   TRP A 173      -6.556 -16.528 -14.727  1.00 34.64           O  
ANISOU 1541  O   TRP A 173     4973   3634   4556    314    537    493       O  
ATOM   1542  CB  TRP A 173      -8.175 -18.558 -16.131  1.00 23.10           C  
ANISOU 1542  CB  TRP A 173     3541   2174   3062    235    542    321       C  
ATOM   1543  CG  TRP A 173      -9.150 -19.022 -15.138  1.00 16.68           C  
ANISOU 1543  CG  TRP A 173     2709   1342   2287    202    505    331       C  
ATOM   1544  CD1 TRP A 173     -10.246 -18.356 -14.674  1.00 16.28           C  
ANISOU 1544  CD1 TRP A 173     2643   1350   2192    187    448    358       C  
ATOM   1545  CD2 TRP A 173      -9.129 -20.278 -14.479  1.00 28.92           C  
ANISOU 1545  CD2 TRP A 173     4254   2804   3930    179    526    314       C  
ATOM   1546  CE2 TRP A 173     -10.244 -20.323 -13.624  1.00 33.76           C  
ANISOU 1546  CE2 TRP A 173     4851   3428   4548    148    480    330       C  
ATOM   1547  CE3 TRP A 173      -8.270 -21.377 -14.526  1.00 22.89           C  
ANISOU 1547  CE3 TRP A 173     3498   1950   3250    184    585    289       C  
ATOM   1548  NE1 TRP A 173     -10.914 -19.134 -13.761  1.00 20.24           N  
ANISOU 1548  NE1 TRP A 173     3131   1807   2752    152    432    355       N  
ATOM   1549  CZ2 TRP A 173     -10.521 -21.422 -12.822  1.00 25.73           C  
ANISOU 1549  CZ2 TRP A 173     3829   2334   3614    120    492    323       C  
ATOM   1550  CZ3 TRP A 173      -8.542 -22.462 -13.734  1.00 18.55           C  
ANISOU 1550  CZ3 TRP A 173     2941   1322   2784    160    597    286       C  
ATOM   1551  CH2 TRP A 173      -9.657 -22.480 -12.891  1.00 21.29           C  
ANISOU 1551  CH2 TRP A 173     3276   1682   3132    128    551    303       C  
ATOM   1552  H   TRP A 173      -6.652 -17.017 -17.556  1.00 25.52           H  
ATOM   1553  HE1 TRP A 173     -11.633 -18.912 -13.345  1.00 25.10           H  
ATOM   1554  N   ILE A 174      -8.574 -15.538 -14.515  1.00 50.54           N  
ANISOU 1554  N   ILE A 174     6978   5754   6472    284    455    508       N  
ATOM   1555  CA  ILE A 174      -8.213 -14.725 -13.363  1.00 75.90           C  
ANISOU 1555  CA  ILE A 174    10168   8955   9716    301    442    590       C  
ATOM   1556  C   ILE A 174      -8.839 -15.347 -12.117  1.00 85.75           C  
ANISOU 1556  C   ILE A 174    11394  10164  11023    269    411    610       C  
ATOM   1557  O   ILE A 174     -10.070 -15.395 -11.989  1.00 88.63           O  
ANISOU 1557  O   ILE A 174    11754  10560  11361    239    374    593       O  
ATOM   1558  CB  ILE A 174      -8.649 -13.267 -13.541  1.00 94.34           C  
ANISOU 1558  CB  ILE A 174    12502  11366  11976    318    422    631       C  
ATOM   1559  CG1 ILE A 174      -7.950 -12.671 -14.763  1.00 92.53           C  
ANISOU 1559  CG1 ILE A 174    12298  11170  11690    352    460    617       C  
ATOM   1560  CG2 ILE A 174      -8.307 -12.467 -12.306  1.00113.74           C  
ANISOU 1560  CG2 ILE A 174    14921  13827  14468    317    404    687       C  
ATOM   1561  CD1 ILE A 174      -8.468 -11.320 -15.164  1.00 92.15           C  
ANISOU 1561  CD1 ILE A 174    12255  11196  11560    372    447    652       C  
ATOM   1562  H   ILE A 174      -9.397 -15.453 -14.750  1.00 61.47           H  
ATOM   1563  N   THR A 175      -7.974 -15.791 -11.196  1.00 60.16           N  
ANISOU 1563  N   THR A 175     8136   6861   7862    276    425    645       N  
ATOM   1564  CA  THR A 175      -8.297 -16.434  -9.941  1.00 42.96           C  
ANISOU 1564  CA  THR A 175     5918   4672   5734    240    384    645       C  
ATOM   1565  C   THR A 175      -7.651 -15.669  -8.785  1.00 30.86           C  
ANISOU 1565  C   THR A 175     4326   3203   4197    228    335    659       C  
ATOM   1566  O   THR A 175      -6.555 -15.119  -8.941  1.00 31.52           O  
ANISOU 1566  O   THR A 175     4392   3309   4274    249    349    662       O  
ATOM   1567  CB  THR A 175      -7.793 -17.894  -9.921  1.00 40.03           C  
ANISOU 1567  CB  THR A 175     5555   4217   5439    239    419    621       C  
ATOM   1568  CG2 THR A 175      -8.230 -18.643 -11.170  1.00 37.21           C  
ANISOU 1568  CG2 THR A 175     5244   3822   5073    234    462    558       C  
ATOM   1569  OG1 THR A 175      -6.363 -17.919  -9.845  1.00 65.38           O  
ANISOU 1569  OG1 THR A 175     8737   7429   8675    265    434    624       O  
ATOM   1570  H   THR A 175      -7.123 -15.721 -11.294  1.00 73.01           H  
ATOM   1571  HG1 THR A 175      -6.111 -17.673  -9.082  1.00 79.27           H  
ATOM   1572  N   PRO A 176      -8.324 -15.584  -7.627  1.00 29.98           N  
ANISOU 1572  N   PRO A 176     4189   3118   4085    192    284    664       N  
ATOM   1573  CA  PRO A 176      -7.688 -14.956  -6.452  1.00 21.79           C  
ANISOU 1573  CA  PRO A 176     3110   2128   3040    177    248    669       C  
ATOM   1574  C   PRO A 176      -6.723 -15.869  -5.717  1.00 28.47           C  
ANISOU 1574  C   PRO A 176     3938   2946   3934    182    251    673       C  
ATOM   1575  O   PRO A 176      -5.998 -15.393  -4.830  1.00 30.60           O  
ANISOU 1575  O   PRO A 176     4178   3251   4197    177    233    679       O  
ATOM   1576  CB  PRO A 176      -8.889 -14.614  -5.558  1.00 38.11           C  
ANISOU 1576  CB  PRO A 176     5173   4225   5083    139    203    667       C  
ATOM   1577  CG  PRO A 176      -9.889 -15.701  -5.896  1.00 34.91           C  
ANISOU 1577  CG  PRO A 176     4795   3764   4705    129    212    665       C  
ATOM   1578  CD  PRO A 176      -9.728 -15.958  -7.375  1.00 25.07           C  
ANISOU 1578  CD  PRO A 176     3582   2481   3461    162    264    663       C  
ATOM   1579  N   LYS A 177      -6.770 -17.172  -5.974  1.00 20.04           N  
ANISOU 1579  N   LYS A 177     2886   1813   2914    188    274    669       N  
ATOM   1580  CA  LYS A 177      -5.871 -18.133  -5.349  1.00 26.40           C  
ANISOU 1580  CA  LYS A 177     3674   2587   3769    198    281    677       C  
ATOM   1581  C   LYS A 177      -5.541 -19.221  -6.359  1.00 28.92           C  
ANISOU 1581  C   LYS A 177     4016   2831   4141    223    337    662       C  
ATOM   1582  O   LYS A 177      -6.078 -19.249  -7.473  1.00 30.84           O  
ANISOU 1582  O   LYS A 177     4295   3044   4379    228    370    643       O  
ATOM   1583  CB  LYS A 177      -6.481 -18.689  -4.067  1.00 35.17           C  
ANISOU 1583  CB  LYS A 177     4778   3698   4887    168    245    684       C  
ATOM   1584  CG  LYS A 177      -7.645 -19.607  -4.318  1.00 29.92           C  
ANISOU 1584  CG  LYS A 177     4143   2980   4247    149    254    670       C  
ATOM   1585  CD  LYS A 177      -8.262 -20.076  -3.019  1.00 31.37           C  
ANISOU 1585  CD  LYS A 177     4322   3167   4431    119    221    678       C  
ATOM   1586  CE  LYS A 177      -9.290 -19.094  -2.490  1.00 30.01           C  
ANISOU 1586  CE  LYS A 177     4151   3047   4203     86    181    674       C  
ATOM   1587  NZ  LYS A 177     -10.005 -19.686  -1.324  1.00 48.48           N1+
ANISOU 1587  NZ  LYS A 177     6497   5379   6546     57    161    676       N1+
ATOM   1588  H   LYS A 177      -7.328 -17.532  -6.519  1.00 24.86           H  
ATOM   1589  HZ1 LYS A 177     -10.607 -19.109  -1.011  1.00 59.00           H  
ATOM   1590  HZ2 LYS A 177     -10.422 -20.433  -1.570  1.00 59.00           H  
ATOM   1591  HZ3 LYS A 177      -9.426 -19.878  -0.677  1.00 59.00           H  
ATOM   1592  N   ASP A 178      -4.651 -20.128  -5.977  1.00 46.70           N  
ANISOU 1592  N   ASP A 178     6251   5050   6444    240    353    671       N  
ATOM   1593  CA  ASP A 178      -4.300 -21.207  -6.891  1.00 44.80           C  
ANISOU 1593  CA  ASP A 178     6031   4732   6260    261    413    649       C  
ATOM   1594  C   ASP A 178      -5.481 -22.146  -7.093  1.00 32.33           C  
ANISOU 1594  C   ASP A 178     4484   3092   4707    235    429    623       C  
ATOM   1595  O   ASP A 178      -6.068 -22.630  -6.112  1.00 41.53           O  
ANISOU 1595  O   ASP A 178     5641   4256   5882    211    398    634       O  
ATOM   1596  CB  ASP A 178      -3.094 -21.993  -6.409  1.00 49.83           C  
ANISOU 1596  CB  ASP A 178     6637   5346   6950    286    430    667       C  
ATOM   1597  CG  ASP A 178      -2.684 -23.060  -7.402  1.00 59.64           C  
ANISOU 1597  CG  ASP A 178     7899   6506   8254    308    499    638       C  
ATOM   1598  OD1 ASP A 178      -3.273 -24.160  -7.365  1.00 57.25           O  
ANISOU 1598  OD1 ASP A 178     7614   6144   7994    294    520    620       O  
ATOM   1599  OD2 ASP A 178      -1.796 -22.790  -8.240  1.00 72.12           O1-
ANISOU 1599  OD2 ASP A 178     9480   8080   9842    336    538    628       O1-
ATOM   1600  H   ASP A 178      -4.247 -20.140  -5.218  1.00 56.87           H  
ATOM   1601  N   PRO A 179      -5.806 -22.494  -8.340  1.00 32.42           N  
ANISOU 1601  N   PRO A 179     4537   3047   4735    238    485    582       N  
ATOM   1602  CA  PRO A 179      -7.006 -23.286  -8.652  1.00 30.08           C  
ANISOU 1602  CA  PRO A 179     4278   2690   4462    205    509    543       C  
ATOM   1603  C   PRO A 179      -6.960 -24.776  -8.307  1.00 22.48           C  
ANISOU 1603  C   PRO A 179     3313   1656   3573    195    541    523       C  
ATOM   1604  O   PRO A 179      -8.008 -25.426  -8.414  1.00 22.51           O  
ANISOU 1604  O   PRO A 179     3343   1613   3597    159    559    486       O  
ATOM   1605  CB  PRO A 179      -7.163 -23.109 -10.173  1.00 22.78           C  
ANISOU 1605  CB  PRO A 179     3407   1726   3523    212    571    495       C  
ATOM   1606  CG  PRO A 179      -6.112 -22.084 -10.591  1.00 32.95           C  
ANISOU 1606  CG  PRO A 179     4683   3064   4771    252    570    521       C  
ATOM   1607  CD  PRO A 179      -5.056 -22.119  -9.551  1.00 34.27           C  
ANISOU 1607  CD  PRO A 179     4792   3269   4961    269    535    563       C  
ATOM   1608  N   HIS A 180      -5.794 -25.364  -8.003  1.00 28.48           N  
ANISOU 1608  N   HIS A 180     4044   2401   4375    225    556    542       N  
ATOM   1609  CA  HIS A 180      -5.735 -26.746  -7.508  1.00 46.74           C  
ANISOU 1609  CA  HIS A 180     6351   4655   6754    221    582    537       C  
ATOM   1610  C   HIS A 180      -6.545 -26.902  -6.229  1.00 41.58           C  
ANISOU 1610  C   HIS A 180     5686   4026   6088    194    529    567       C  
ATOM   1611  O   HIS A 180      -6.827 -28.044  -5.818  1.00 42.93           O  
ANISOU 1611  O   HIS A 180     5859   4143   6308    182    552    560       O  
ATOM   1612  CB  HIS A 180      -4.265 -27.170  -7.412  1.00 49.73           C  
ANISOU 1612  CB  HIS A 180     6698   5022   7174    264    607    562       C  
ATOM   1613  CG  HIS A 180      -3.564 -27.184  -8.747  1.00 61.37           C  
ANISOU 1613  CG  HIS A 180     8190   6460   8669    286    672    520       C  
ATOM   1614  CD2 HIS A 180      -3.653 -28.036  -9.800  1.00 64.57           C  
ANISOU 1614  CD2 HIS A 180     8627   6786   9119    277    749    454       C  
ATOM   1615  ND1 HIS A 180      -2.665 -26.210  -9.125  1.00 67.44           N  
ANISOU 1615  ND1 HIS A 180     8944   7275   9405    315    665    537       N  
ATOM   1616  CE1 HIS A 180      -2.219 -26.467 -10.342  1.00 64.26           C  
ANISOU 1616  CE1 HIS A 180     8566   6823   9026    327    733    489       C  
ATOM   1617  NE2 HIS A 180      -2.804 -27.568 -10.776  1.00 64.10           N  
ANISOU 1617  NE2 HIS A 180     8575   6728   9052    303    786    434       N  
ATOM   1618  H   HIS A 180      -5.026 -24.984  -8.073  1.00 34.99           H  
ATOM   1619  HD1 HIS A 180      -2.430 -25.539  -8.641  1.00 81.75           H  
ATOM   1620  N   THR A 181      -6.885 -25.763  -5.606  1.00 38.99           N  
ANISOU 1620  N   THR A 181     5345   3776   5695    183    463    599       N  
ATOM   1621  CA  THR A 181      -7.830 -25.640  -4.504  1.00 38.90           C  
ANISOU 1621  CA  THR A 181     5330   3796   5655    150    411    618       C  
ATOM   1622  C   THR A 181      -9.205 -26.248  -4.778  1.00 46.38           C  
ANISOU 1622  C   THR A 181     6309   4693   6622    108    432    576       C  
ATOM   1623  O   THR A 181      -9.886 -26.684  -3.841  1.00 49.55           O  
ANISOU 1623  O   THR A 181     6708   5091   7026     82    410    587       O  
ATOM   1624  CB  THR A 181      -8.079 -24.139  -4.229  1.00 39.16           C  
ANISOU 1624  CB  THR A 181     5352   3916   5611    142    354    637       C  
ATOM   1625  CG2 THR A 181      -6.984 -23.479  -3.412  1.00 30.34           C  
ANISOU 1625  CG2 THR A 181     4199   2862   4465    164    320    676       C  
ATOM   1626  OG1 THR A 181      -8.203 -23.435  -5.488  1.00 53.78           O  
ANISOU 1626  OG1 THR A 181     7223   5770   7442    148    377    613       O  
ATOM   1627  H   THR A 181      -6.557 -24.998  -5.823  1.00 47.61           H  
ATOM   1628  HG1 THR A 181      -8.246 -22.607  -5.351  1.00 65.36           H  
ATOM   1629  N   LEU A 182      -9.611 -26.327  -6.051  1.00 47.39           N  
ANISOU 1629  N   LEU A 182     6467   4775   6763     97    481    523       N  
ATOM   1630  CA  LEU A 182     -10.864 -26.970  -6.441  1.00 51.45           C  
ANISOU 1630  CA  LEU A 182     7013   5232   7303     50    515    466       C  
ATOM   1631  C   LEU A 182     -10.633 -28.455  -6.738  1.00 51.68           C  
ANISOU 1631  C   LEU A 182     7054   5174   7407     45    584    421       C  
ATOM   1632  O   LEU A 182     -11.495 -29.112  -7.330  1.00 53.99           O  
ANISOU 1632  O   LEU A 182     7376   5410   7728      1    632    349       O  
ATOM   1633  CB  LEU A 182     -11.482 -26.243  -7.652  1.00 53.78           C  
ANISOU 1633  CB  LEU A 182     7344   5524   7565     32    538    420       C  
ATOM   1634  CG  LEU A 182     -12.436 -25.052  -7.429  1.00 48.42           C  
ANISOU 1634  CG  LEU A 182     6666   4908   6822     12    486    445       C  
ATOM   1635  CD1 LEU A 182     -13.280 -24.779  -8.684  1.00 44.13           C  
ANISOU 1635  CD1 LEU A 182     6136   4423   6207    -20    482    354       C  
ATOM   1636  CD2 LEU A 182     -13.365 -25.229  -6.234  1.00 50.92           C  
ANISOU 1636  CD2 LEU A 182     6964   5245   7140    -24    439    464       C  
ATOM   1637  H   LEU A 182      -9.167 -26.009  -6.715  1.00 57.68           H  
ATOM   1638  N   ASP A 183      -9.433 -28.937  -6.387  1.00 51.00           N  
ANISOU 1638  N   ASP A 183     6944   5081   7352     87    594    458       N  
ATOM   1639  CA  ASP A 183      -8.986 -30.337  -6.214  1.00 66.52           C  
ANISOU 1639  CA  ASP A 183     8906   6979   9390     97    647    448       C  
ATOM   1640  C   ASP A 183      -9.305 -31.293  -7.369  1.00 66.76           C  
ANISOU 1640  C   ASP A 183     8969   6924   9473     69    735    357       C  
ATOM   1641  O   ASP A 183      -9.882 -32.372  -7.212  1.00 76.88           O  
ANISOU 1641  O   ASP A 183    10260   8150  10801     39    775    320       O  
ATOM   1642  CB  ASP A 183      -9.469 -30.924  -4.884  1.00 75.86           C  
ANISOU 1642  CB  ASP A 183    10077   8164  10584     83    617    487       C  
ATOM   1643  CG  ASP A 183      -8.934 -32.335  -4.664  1.00 95.36           C  
ANISOU 1643  CG  ASP A 183    12542  10565  13127    101    675    488       C  
ATOM   1644  OD1 ASP A 183      -9.445 -33.276  -5.301  1.00 95.77           O  
ANISOU 1644  OD1 ASP A 183    12616  10544  13227     72    743    423       O  
ATOM   1645  OD2 ASP A 183      -7.994 -32.517  -3.869  1.00101.37           O1-
ANISOU 1645  OD2 ASP A 183    13276  11342  13898    141    658    552       O1-
ATOM   1646  H   ASP A 183      -8.774 -28.410  -6.222  1.00 62.01           H  
ATOM   1647  N   GLY A 184      -8.764 -30.928  -8.518  1.00 59.15           N  
ANISOU 1647  N   GLY A 184     8020   5952   8503     82    772    318       N  
ATOM   1648  CA  GLY A 184      -8.783 -31.710  -9.725  1.00 65.22           C  
ANISOU 1648  CA  GLY A 184     8819   6648   9312     59    860    223       C  
ATOM   1649  C   GLY A 184      -9.831 -31.285 -10.722  1.00 48.19           C  
ANISOU 1649  C   GLY A 184     6707   4485   7118      3    879    131       C  
ATOM   1650  O   GLY A 184      -9.640 -31.507 -11.924  1.00 48.77           O  
ANISOU 1650  O   GLY A 184     6811   4523   7196    -13    944     45       O  
ATOM   1651  H   GLY A 184      -8.355 -30.179  -8.625  1.00 71.80           H  
ATOM   1652  N   HIS A 185     -10.843 -30.553 -10.267  1.00 45.91           N  
ANISOU 1652  N   HIS A 185     6423   4239   6782    -25    822    149       N  
ATOM   1653  CA  HIS A 185     -11.899 -30.063 -11.146  1.00 54.54           C  
ANISOU 1653  CA  HIS A 185     7534   5392   7796    -78    805     60       C  
ATOM   1654  C   HIS A 185     -11.341 -29.153 -12.238  1.00 52.07           C  
ANISOU 1654  C   HIS A 185     7221   5166   7397    -53    787     38       C  
ATOM   1655  O   HIS A 185     -11.929 -29.080 -13.321  1.00 39.69           O  
ANISOU 1655  O   HIS A 185     5660   3664   5756    -94    785    -58       O  
ATOM   1656  CB  HIS A 185     -12.954 -29.333 -10.283  1.00 56.52           C  
ANISOU 1656  CB  HIS A 185     7768   5708   7998   -100    726    104       C  
ATOM   1657  CG  HIS A 185     -14.360 -29.362 -10.819  1.00 68.43           C  
ANISOU 1657  CG  HIS A 185     9275   7285   9442   -169    702      6       C  
ATOM   1658  CD2 HIS A 185     -15.421 -30.150 -10.516  1.00 74.92           C  
ANISOU 1658  CD2 HIS A 185    10098   8074  10294   -230    718    -50       C  
ATOM   1659  ND1 HIS A 185     -14.823 -28.442 -11.736  1.00 65.51           N  
ANISOU 1659  ND1 HIS A 185     8896   7036   8959   -180    652    -38       N  
ATOM   1660  CE1 HIS A 185     -16.095 -28.685 -12.003  1.00 67.53           C  
ANISOU 1660  CE1 HIS A 185     9144   7336   9177   -244    636   -119       C  
ATOM   1661  NE2 HIS A 185     -16.482 -29.718 -11.277  1.00 73.87           N  
ANISOU 1661  NE2 HIS A 185     9953   8047  10067   -277    676   -132       N  
ATOM   1662  H   HIS A 185     -10.944 -30.324  -9.443  1.00 55.91           H  
ATOM   1663  HE2 HIS A 185     -17.269 -30.065 -11.280  1.00 89.46           H  
ATOM   1664  N   ALA A 186     -10.171 -28.539 -12.022  1.00 41.53           N  
ANISOU 1664  N   ALA A 186     5878   3828   6073     11    780    122       N  
ATOM   1665  CA  ALA A 186      -9.614 -27.576 -12.966  1.00 30.70           C  
ANISOU 1665  CA  ALA A 186     4508   2537   4620     38    763    112       C  
ATOM   1666  C   ALA A 186      -8.411 -28.106 -13.739  1.00 37.82           C  
ANISOU 1666  C   ALA A 186     5422   3379   5568     67    838     82       C  
ATOM   1667  O   ALA A 186      -7.805 -27.348 -14.510  1.00 34.14           O  
ANISOU 1667  O   ALA A 186     4960   2970   5043     93    834     77       O  
ATOM   1668  CB  ALA A 186      -9.216 -26.292 -12.227  1.00 36.19           C  
ANISOU 1668  CB  ALA A 186     5183   3288   5281     85    700    221       C  
ATOM   1669  H   ALA A 186      -9.681 -28.668 -11.327  1.00 50.65           H  
ATOM   1670  N   ASP A 187      -8.091 -29.396 -13.597  1.00 55.99           N  
ANISOU 1670  N   ASP A 187     7522   6851   6901    938    623    -86       N  
ATOM   1671  CA  ASP A 187      -6.874 -29.953 -14.190  1.00 49.76           C  
ANISOU 1671  CA  ASP A 187     6698   6111   6098   1026    711    -85       C  
ATOM   1672  C   ASP A 187      -6.956 -30.012 -15.712  1.00 44.38           C  
ANISOU 1672  C   ASP A 187     6088   5446   5329   1036    791    -74       C  
ATOM   1673  O   ASP A 187      -5.970 -29.729 -16.407  1.00 48.52           O  
ANISOU 1673  O   ASP A 187     6546   6032   5858   1067    878    -44       O  
ATOM   1674  CB  ASP A 187      -6.632 -31.363 -13.643  1.00 57.52           C  
ANISOU 1674  CB  ASP A 187     7736   7063   7057   1121    701   -133       C  
ATOM   1675  CG  ASP A 187      -6.160 -31.373 -12.201  1.00 66.80           C  
ANISOU 1675  CG  ASP A 187     8824   8240   8317   1138    641   -140       C  
ATOM   1676  OD1 ASP A 187      -6.151 -30.301 -11.562  1.00 69.21           O  
ANISOU 1676  OD1 ASP A 187     9037   8564   8697   1068    597   -113       O  
ATOM   1677  OD2 ASP A 187      -5.799 -32.464 -11.705  1.00 72.75           O1-
ANISOU 1677  OD2 ASP A 187     9595   8984   9064   1177    610   -164       O1-
ATOM   1678  H   ASP A 187      -8.561 -29.970 -13.164  1.00 68.01           H  
ATOM   1679  N   GLU A 188      -8.118 -30.410 -16.243  1.00 48.10           N  
ANISOU 1679  N   GLU A 188     6695   5865   5716   1011    763    -98       N  
ATOM   1680  CA  GLU A 188      -8.330 -30.463 -17.688  1.00 55.84           C  
ANISOU 1680  CA  GLU A 188     7760   6856   6601   1017    825    -91       C  
ATOM   1681  C   GLU A 188      -8.218 -29.074 -18.295  1.00 54.57           C  
ANISOU 1681  C   GLU A 188     7531   6741   6463    950    859    -30       C  
ATOM   1682  O   GLU A 188      -7.510 -28.866 -19.289  1.00 57.29           O  
ANISOU 1682  O   GLU A 188     7860   7134   6774    979    951     -2       O  
ATOM   1683  CB  GLU A 188      -9.709 -31.074 -17.982  1.00 65.45           C  
ANISOU 1683  CB  GLU A 188     9126   8007   7734    987    765   -129       C  
ATOM   1684  CG  GLU A 188      -9.989 -31.414 -19.456  1.00 75.64           C  
ANISOU 1684  CG  GLU A 188    10533   9298   8907   1006    817   -138       C  
ATOM   1685  CD  GLU A 188     -11.432 -31.874 -19.736  1.00 86.60           C  
ANISOU 1685  CD  GLU A 188    12050  10628  10225    950    736   -170       C  
ATOM   1686  OE1 GLU A 188     -12.229 -32.043 -18.786  1.00 88.77           O  
ANISOU 1686  OE1 GLU A 188    12333  10860  10537    908    652   -190       O  
ATOM   1687  OE2 GLU A 188     -11.764 -32.072 -20.927  1.00 81.75           O1-
ANISOU 1687  OE2 GLU A 188    11521  10018   9524    943    751   -172       O1-
ATOM   1688  H   GLU A 188      -8.802 -30.656 -15.783  1.00 58.54           H  
ATOM   1689  N   LEU A 189      -8.921 -28.111 -17.699  1.00 62.84           N  
ANISOU 1689  N   LEU A 189     8541   7770   7564    863    787     -8       N  
ATOM   1690  CA  LEU A 189      -8.882 -26.735 -18.171  1.00 43.69           C  
ANISOU 1690  CA  LEU A 189     6059   5375   5165    795    810     52       C  
ATOM   1691  C   LEU A 189      -7.453 -26.231 -18.268  1.00 43.36           C  
ANISOU 1691  C   LEU A 189     5891   5398   5186    814    892     91       C  
ATOM   1692  O   LEU A 189      -7.051 -25.646 -19.281  1.00 47.75           O  
ANISOU 1692  O   LEU A 189     6436   5993   5715    803    971    136       O  
ATOM   1693  CB  LEU A 189      -9.684 -25.844 -17.223  1.00 39.02           C  
ANISOU 1693  CB  LEU A 189     5435   4751   4641    715    717     64       C  
ATOM   1694  CG  LEU A 189      -9.644 -24.361 -17.578  1.00 36.80           C  
ANISOU 1694  CG  LEU A 189     5098   4488   4396    643    734    126       C  
ATOM   1695  CD1 LEU A 189     -10.206 -24.141 -18.970  1.00 37.39           C  
ANISOU 1695  CD1 LEU A 189     5265   4567   4373    633    772    150       C  
ATOM   1696  CD2 LEU A 189     -10.411 -23.544 -16.564  1.00 35.45           C  
ANISOU 1696  CD2 LEU A 189     4901   4279   4290    576    642    132       C  
ATOM   1697  H   LEU A 189      -9.430 -28.231 -17.016  1.00 76.22           H  
ATOM   1698  N   LEU A 190      -6.672 -26.446 -17.210  1.00 36.89           N  
ANISOU 1698  N   LEU A 190     4973   4593   4450    841    875     78       N  
ATOM   1699  CA  LEU A 190      -5.320 -25.911 -17.155  1.00 31.83           C  
ANISOU 1699  CA  LEU A 190     4191   4019   3885    847    940    116       C  
ATOM   1700  C   LEU A 190      -4.370 -26.634 -18.100  1.00 37.79           C  
ANISOU 1700  C   LEU A 190     4944   4828   4588    937   1053    118       C  
ATOM   1701  O   LEU A 190      -3.314 -26.083 -18.427  1.00 45.79           O  
ANISOU 1701  O   LEU A 190     5845   5906   5646    935   1131    162       O  
ATOM   1702  CB  LEU A 190      -4.799 -25.972 -15.721  1.00 20.33           C  
ANISOU 1702  CB  LEU A 190     2631   2566   2528    853    877     97       C  
ATOM   1703  CG  LEU A 190      -5.393 -24.938 -14.763  1.00 26.18           C  
ANISOU 1703  CG  LEU A 190     3337   3271   3341    759    784    108       C  
ATOM   1704  CD1 LEU A 190      -5.073 -25.340 -13.331  1.00 31.45           C  
ANISOU 1704  CD1 LEU A 190     3944   3929   4076    785    710     74       C  
ATOM   1705  CD2 LEU A 190      -4.894 -23.528 -15.041  1.00 34.07           C  
ANISOU 1705  CD2 LEU A 190     4241   4301   4402    677    816    168       C  
ATOM   1706  H   LEU A 190      -6.903 -26.898 -16.515  1.00 45.09           H  
ATOM   1707  N   ALA A 191      -4.706 -27.848 -18.540  1.00 35.42           N  
ANISOU 1707  N   ALA A 191     4763   4501   4194   1015   1067     72       N  
ATOM   1708  CA  ALA A 191      -3.912 -28.527 -19.556  1.00 33.60           C  
ANISOU 1708  CA  ALA A 191     4554   4315   3897   1106   1180     72       C  
ATOM   1709  C   ALA A 191      -4.173 -27.985 -20.955  1.00 34.85           C  
ANISOU 1709  C   ALA A 191     4779   4490   3974   1078   1252    109       C  
ATOM   1710  O   ALA A 191      -3.420 -28.311 -21.881  1.00 40.42           O  
ANISOU 1710  O   ALA A 191     5488   5243   4626   1146   1361    122       O  
ATOM   1711  CB  ALA A 191      -4.192 -30.033 -19.532  1.00 34.15           C  
ANISOU 1711  CB  ALA A 191     4746   4340   3891   1201   1166      5       C  
ATOM   1712  H   ALA A 191      -5.388 -28.295 -18.266  1.00 43.32           H  
ATOM   1713  N   HIS A 192      -5.207 -27.177 -21.137  1.00 30.52           N  
ANISOU 1713  N   HIS A 192     4283   3905   3409    987   1196    129       N  
ATOM   1714  CA  HIS A 192      -5.521 -26.674 -22.465  1.00 28.36           C  
ANISOU 1714  CA  HIS A 192     4084   3643   3047    964   1256    165       C  
ATOM   1715  C   HIS A 192      -4.517 -25.621 -22.939  1.00 23.19           C  
ANISOU 1715  C   HIS A 192     3314   3055   2441    933   1353    239       C  
ATOM   1716  O   HIS A 192      -4.225 -24.676 -22.196  1.00 35.93           O  
ANISOU 1716  O   HIS A 192     4809   4679   4164    863   1323    274       O  
ATOM   1717  CB  HIS A 192      -6.928 -26.099 -22.510  1.00 21.38           C  
ANISOU 1717  CB  HIS A 192     3286   2703   2133    881   1164    168       C  
ATOM   1718  CG  HIS A 192      -7.473 -26.059 -23.896  1.00 28.12           C  
ANISOU 1718  CG  HIS A 192     4265   3556   2862    885   1204    182       C  
ATOM   1719  CD2 HIS A 192      -8.366 -26.849 -24.528  1.00 28.17           C  
ANISOU 1719  CD2 HIS A 192     4422   3527   2755    911   1173    138       C  
ATOM   1720  ND1 HIS A 192      -6.997 -25.177 -24.840  1.00 24.08           N  
ANISOU 1720  ND1 HIS A 192     3731   3089   2329    865   1293    248       N  
ATOM   1721  CE1 HIS A 192      -7.609 -25.400 -25.990  1.00 24.15           C  
ANISOU 1721  CE1 HIS A 192     3875   3089   2210    882   1312    244       C  
ATOM   1722  NE2 HIS A 192      -8.445 -26.406 -25.828  1.00 35.07           N  
ANISOU 1722  NE2 HIS A 192     5364   4425   3537    909   1237    176       N  
ATOM   1723  H   HIS A 192      -5.736 -26.907 -20.515  1.00 37.44           H  
ATOM   1724  HE2 HIS A 192      -8.958 -26.733 -26.437  1.00 42.91           H  
ATOM   1725  N   PRO A 193      -3.995 -25.731 -24.167  1.00 40.62           N  
ANISOU 1725  N   PRO A 193     5557   5308   4570    980   1469    266       N  
ATOM   1726  CA  PRO A 193      -2.944 -24.796 -24.621  1.00 34.71           C  
ANISOU 1726  CA  PRO A 193     4689   4628   3870    953   1576    340       C  
ATOM   1727  C   PRO A 193      -3.419 -23.364 -24.796  1.00 33.22           C  
ANISOU 1727  C   PRO A 193     4488   4422   3711    838   1554    403       C  
ATOM   1728  O   PRO A 193      -2.577 -22.470 -24.982  1.00 30.76           O  
ANISOU 1728  O   PRO A 193     4069   4158   3461    794   1629    468       O  
ATOM   1729  CB  PRO A 193      -2.496 -25.388 -25.966  1.00 29.22           C  
ANISOU 1729  CB  PRO A 193     4072   3974   3056   1039   1702    346       C  
ATOM   1730  CG  PRO A 193      -2.972 -26.805 -25.946  1.00 29.67           C  
ANISOU 1730  CG  PRO A 193     4247   3984   3044   1111   1633    262       C  
ATOM   1731  CD  PRO A 193      -4.259 -26.768 -25.180  1.00 30.10           C  
ANISOU 1731  CD  PRO A 193     4373   3966   3098   1065   1516    227       C  
ATOM   1732  N   SER A 194      -4.731 -23.130 -24.791  1.00 33.97           N  
ANISOU 1732  N   SER A 194     4694   4453   3761    791   1459    389       N  
ATOM   1733  CA  SER A 194      -5.290 -21.793 -24.928  1.00 39.13           C  
ANISOU 1733  CA  SER A 194     5350   5080   4437    693   1429    446       C  
ATOM   1734  C   SER A 194      -5.306 -21.022 -23.624  1.00 30.70           C  
ANISOU 1734  C   SER A 194     4175   3987   3504    616   1344    452       C  
ATOM   1735  O   SER A 194      -5.441 -19.794 -23.645  1.00 34.13           O  
ANISOU 1735  O   SER A 194     4582   4405   3981    533   1337    508       O  
ATOM   1736  CB  SER A 194      -6.726 -21.885 -25.435  1.00 51.26           C  
ANISOU 1736  CB  SER A 194     7044   6564   5870    683   1355    426       C  
ATOM   1737  OG  SER A 194      -6.746 -22.386 -26.750  1.00 71.38           O  
ANISOU 1737  OG  SER A 194     9703   9134   8286    742   1431    428       O  
ATOM   1738  H   SER A 194      -5.328 -23.744 -24.707  1.00 41.59           H  
ATOM   1739  HG  SER A 194      -7.539 -22.437 -27.026  1.00 86.48           H  
ATOM   1740  N   VAL A 195      -5.175 -21.709 -22.502  1.00 33.11           N  
ANISOU 1740  N   VAL A 195     4427   4282   3870    643   1280    397       N  
ATOM   1741  CA  VAL A 195      -5.428 -21.121 -21.197  1.00 22.06           C  
ANISOU 1741  CA  VAL A 195     2957   2847   2579    579   1179    388       C  
ATOM   1742  C   VAL A 195      -4.157 -20.497 -20.650  1.00 25.59           C  
ANISOU 1742  C   VAL A 195     3240   3339   3144    544   1219    423       C  
ATOM   1743  O   VAL A 195      -3.110 -21.152 -20.570  1.00 40.58           O  
ANISOU 1743  O   VAL A 195     5056   5294   5067    603   1277    411       O  
ATOM   1744  CB  VAL A 195      -5.971 -22.177 -20.222  1.00 25.67           C  
ANISOU 1744  CB  VAL A 195     3447   3269   3038    625   1085    313       C  
ATOM   1745  CG1 VAL A 195      -5.999 -21.625 -18.801  1.00 35.20           C  
ANISOU 1745  CG1 VAL A 195     4567   4449   4359    570    994    304       C  
ATOM   1746  CG2 VAL A 195      -7.342 -22.631 -20.665  1.00 26.35           C  
ANISOU 1746  CG2 VAL A 195     3685   3305   3022    634   1030    282       C  
ATOM   1747  H   VAL A 195      -4.937 -22.535 -22.470  1.00 40.54           H  
ATOM   1748  N   LYS A 196      -4.248 -19.230 -20.273  1.00 23.88           N  
ANISOU 1748  N   LYS A 196     2975   3097   3001    448   1186    465       N  
ATOM   1749  CA  LYS A 196      -3.243 -18.577 -19.449  1.00 27.06           C  
ANISOU 1749  CA  LYS A 196     3225   3527   3531    394   1184    486       C  
ATOM   1750  C   LYS A 196      -3.861 -18.341 -18.079  1.00 21.29           C  
ANISOU 1750  C   LYS A 196     2486   2738   2866    356   1052    446       C  
ATOM   1751  O   LYS A 196      -4.925 -17.719 -17.970  1.00 28.88           O  
ANISOU 1751  O   LYS A 196     3528   3635   3809    309    988    451       O  
ATOM   1752  CB  LYS A 196      -2.765 -17.277 -20.086  1.00 28.11           C  
ANISOU 1752  CB  LYS A 196     3312   3670   3698    307   1255    566       C  
ATOM   1753  CG  LYS A 196      -1.870 -17.512 -21.294  1.00 24.63           C  
ANISOU 1753  CG  LYS A 196     2845   3302   3210    345   1400    610       C  
ATOM   1754  CD  LYS A 196      -1.206 -16.232 -21.765  1.00 25.66           C  
ANISOU 1754  CD  LYS A 196     2906   3449   3396    250   1475    694       C  
ATOM   1755  CE  LYS A 196      -0.108 -16.511 -22.789  1.00 31.49           C  
ANISOU 1755  CE  LYS A 196     3584   4273   4106    290   1628    738       C  
ATOM   1756  NZ  LYS A 196      -0.624 -16.418 -24.181  1.00 48.65           N1+
ANISOU 1756  NZ  LYS A 196     5894   6440   6152    312   1707    778       N1+
ATOM   1757  H   LYS A 196      -4.901 -18.714 -20.490  1.00 29.47           H  
ATOM   1758  HZ1 LYS A 196       0.032 -16.580 -24.760  1.00 59.20           H  
ATOM   1759  HZ2 LYS A 196      -1.273 -17.014 -24.305  1.00 59.20           H  
ATOM   1760  HZ3 LYS A 196      -0.947 -15.602 -24.332  1.00 59.20           H  
ATOM   1761  N   LEU A 197      -3.200 -18.848 -17.045  1.00 30.47           N  
ANISOU 1761  N   LEU A 197     3553   3924   4099    383   1013    407       N  
ATOM   1762  CA  LEU A 197      -3.676 -18.707 -15.678  1.00 20.30           C  
ANISOU 1762  CA  LEU A 197     2255   2587   2872    356    892    367       C  
ATOM   1763  C   LEU A 197      -3.014 -17.496 -15.041  1.00 29.16           C  
ANISOU 1763  C   LEU A 197     3264   3709   4106    261    869    399       C  
ATOM   1764  O   LEU A 197      -1.781 -17.407 -14.988  1.00 29.61           O  
ANISOU 1764  O   LEU A 197     3192   3829   4230    252    918    418       O  
ATOM   1765  CB  LEU A 197      -3.374 -19.953 -14.854  1.00 20.04           C  
ANISOU 1765  CB  LEU A 197     2195   2575   2846    442    853    305       C  
ATOM   1766  CG  LEU A 197      -3.699 -19.788 -13.369  1.00 19.24           C  
ANISOU 1766  CG  LEU A 197     2071   2430   2809    416    733    267       C  
ATOM   1767  CD1 LEU A 197      -5.194 -19.638 -13.181  1.00 23.56           C  
ANISOU 1767  CD1 LEU A 197     2747   2901   3305    396    662    249       C  
ATOM   1768  CD2 LEU A 197      -3.178 -20.973 -12.591  1.00 29.65           C  
ANISOU 1768  CD2 LEU A 197     3349   3776   4139    504    706    217       C  
ATOM   1769  H   LEU A 197      -2.462 -19.285 -17.113  1.00 37.38           H  
ATOM   1770  N   TRP A 198      -3.836 -16.585 -14.540  1.00 28.34           N  
ANISOU 1770  N   TRP A 198     3209   3535   4024    192    794    403       N  
ATOM   1771  CA  TRP A 198      -3.395 -15.419 -13.782  1.00 21.02           C  
ANISOU 1771  CA  TRP A 198     2201   2586   3200     98    750    423       C  
ATOM   1772  C   TRP A 198      -3.907 -15.631 -12.362  1.00 20.67           C  
ANISOU 1772  C   TRP A 198     2168   2498   3186    109    629    363       C  
ATOM   1773  O   TRP A 198      -4.934 -15.078 -11.951  1.00 22.74           O  
ANISOU 1773  O   TRP A 198     2512   2690   3437     78    561    355       O  
ATOM   1774  CB  TRP A 198      -3.898 -14.155 -14.412  1.00 26.77           C  
ANISOU 1774  CB  TRP A 198     2988   3262   3920     16    771    479       C  
ATOM   1775  CG  TRP A 198      -3.453 -14.006 -15.836  1.00 21.46           C  
ANISOU 1775  CG  TRP A 198     2318   2631   3203     13    894    540       C  
ATOM   1776  CD1 TRP A 198      -4.147 -14.372 -16.951  1.00 21.31           C  
ANISOU 1776  CD1 TRP A 198     2411   2611   3076     60    945    556       C  
ATOM   1777  CD2 TRP A 198      -2.212 -13.460 -16.297  1.00 35.87           C  
ANISOU 1777  CD2 TRP A 198     4031   4509   5089    -42    982    594       C  
ATOM   1778  CE2 TRP A 198      -2.226 -13.522 -17.705  1.00 23.39           C  
ANISOU 1778  CE2 TRP A 198     2506   2954   3426    -20   1092    644       C  
ATOM   1779  CE3 TRP A 198      -1.091 -12.922 -15.658  1.00 23.63           C  
ANISOU 1779  CE3 TRP A 198     2337   2987   3653   -111    978    606       C  
ATOM   1780  NE1 TRP A 198      -3.419 -14.083 -18.080  1.00 22.46           N  
ANISOU 1780  NE1 TRP A 198     2528   2802   3203     44   1063    617       N  
ATOM   1781  CZ2 TRP A 198      -1.167 -13.068 -18.480  1.00 24.77           C  
ANISOU 1781  CZ2 TRP A 198     2598   3183   3630    -62   1206    708       C  
ATOM   1782  CZ3 TRP A 198      -0.040 -12.471 -16.431  1.00 25.01           C  
ANISOU 1782  CZ3 TRP A 198     2422   3218   3864   -159   1087    669       C  
ATOM   1783  CH2 TRP A 198      -0.086 -12.544 -17.828  1.00 25.57           C  
ANISOU 1783  CH2 TRP A 198     2551   3314   3851   -134   1205    721       C  
ATOM   1784  H   TRP A 198      -4.691 -16.619 -14.630  1.00 34.83           H  
ATOM   1785  HE1 TRP A 198      -3.670 -14.229 -18.889  1.00 22.86           H  
ATOM   1786  N   GLU A 199      -3.200 -16.497 -11.634  1.00 34.43           N  
ANISOU 1786  N   GLU A 199     3833   4286   4961    163    605    322       N  
ATOM   1787  CA  GLU A 199      -3.503 -16.818 -10.250  1.00 20.62           C  
ANISOU 1787  CA  GLU A 199     2087   2507   3240    184    497    266       C  
ATOM   1788  C   GLU A 199      -3.111 -15.662  -9.336  1.00 30.46           C  
ANISOU 1788  C   GLU A 199     3264   3727   4582     92    431    271       C  
ATOM   1789  O   GLU A 199      -2.154 -14.925  -9.600  1.00 32.89           O  
ANISOU 1789  O   GLU A 199     3473   4067   4956     25    470    310       O  
ATOM   1790  CB  GLU A 199      -2.777 -18.102  -9.829  1.00 29.30           C  
ANISOU 1790  CB  GLU A 199     3126   3666   4340    276    497    227       C  
ATOM   1791  CG  GLU A 199      -1.279 -18.135 -10.154  1.00 53.06           C  
ANISOU 1791  CG  GLU A 199     5988   6763   7409    279    565    253       C  
ATOM   1792  CD  GLU A 199      -0.575 -19.389  -9.640  1.00 74.60           C  
ANISOU 1792  CD  GLU A 199     8656   9548  10140    382    556    214       C  
ATOM   1793  H   GLU A 199      -2.517 -16.926 -11.934  1.00 42.13           H  
ATOM   1794  N   LYS A 200      -3.874 -15.519  -8.254  1.00 28.85           N  
ANISOU 1794  N   LYS A 200     3116   3463   4381     88    331    232       N  
ATOM   1795  CA  LYS A 200      -3.677 -14.479  -7.248  1.00 34.58           C  
ANISOU 1795  CA  LYS A 200     3805   4149   5185     10    253    224       C  
ATOM   1796  C   LYS A 200      -3.632 -13.090  -7.876  1.00 31.12           C  
ANISOU 1796  C   LYS A 200     3369   3676   4781    -93    288    279       C  
ATOM   1797  O   LYS A 200      -2.840 -12.232  -7.482  1.00 28.59           O  
ANISOU 1797  O   LYS A 200     2967   3353   4543   -175    267    291       O  
ATOM   1798  CB  LYS A 200      -2.402 -14.710  -6.432  1.00 29.90           C  
ANISOU 1798  CB  LYS A 200     3075   3615   4669      9    217    202       C  
ATOM   1799  CG  LYS A 200      -2.283 -16.041  -5.710  1.00 38.18           C  
ANISOU 1799  CG  LYS A 200     4115   4700   5693    113    178    150       C  
ATOM   1800  CD  LYS A 200      -1.324 -15.895  -4.526  1.00 40.03           C  
ANISOU 1800  CD  LYS A 200     4239   4964   6008     95     97    122       C  
ATOM   1801  CE  LYS A 200      -0.370 -17.071  -4.386  1.00 53.42           C  
ANISOU 1801  CE  LYS A 200     5842   6745   7710    185    112    104       C  
ATOM   1802  NZ  LYS A 200       0.993 -16.723  -4.885  1.00 62.62           N1+
ANISOU 1802  NZ  LYS A 200     6850   7993   8951    144    168    141       N1+
ATOM   1803  H   LYS A 200      -4.539 -16.033  -8.074  1.00 35.43           H  
ATOM   1804  HZ1 LYS A 200       1.538 -17.420  -4.793  1.00 75.97           H  
ATOM   1805  HZ2 LYS A 200       0.954 -16.498  -5.744  1.00 75.97           H  
ATOM   1806  HZ3 LYS A 200       1.321 -16.038  -4.421  1.00 75.97           H  
ATOM   1807  N   THR A 201      -4.500 -12.853  -8.853  1.00 28.18           N  
ANISOU 1807  N   THR A 201     3095   3271   4343    -92    339    313       N  
ATOM   1808  CA  THR A 201      -4.640 -11.518  -9.402  1.00 29.02           C  
ANISOU 1808  CA  THR A 201     3230   3326   4470   -182    365    366       C  
ATOM   1809  C   THR A 201      -6.105 -11.115  -9.378  1.00 33.54           C  
ANISOU 1809  C   THR A 201     3940   3820   4985   -171    325    363       C  
ATOM   1810  O   THR A 201      -7.017 -11.948  -9.287  1.00 38.80           O  
ANISOU 1810  O   THR A 201     4677   4483   5583    -96    301    331       O  
ATOM   1811  CB  THR A 201      -4.038 -11.402 -10.820  1.00 40.50           C  
ANISOU 1811  CB  THR A 201     4652   4828   5908   -201    485    429       C  
ATOM   1812  CG2 THR A 201      -2.651 -12.049 -10.867  1.00 44.75           C  
ANISOU 1812  CG2 THR A 201     5048   5461   6494   -185    533    428       C  
ATOM   1813  OG1 THR A 201      -4.882 -12.028 -11.790  1.00 56.73           O  
ANISOU 1813  OG1 THR A 201     6806   6889   7861   -133    534    440       O  
ATOM   1814  H   THR A 201      -5.012 -13.445  -9.208  1.00 34.64           H  
ATOM   1815  HG1 THR A 201      -4.966 -12.845 -11.614  1.00 68.90           H  
ATOM   1816  N   ARG A 202      -6.295  -9.804  -9.403  1.00 27.15           N  
ANISOU 1816  N   ARG A 202     3165   2944   4208   -250    313    397       N  
ATOM   1817  CA  ARG A 202      -7.587  -9.166  -9.251  1.00 27.05           C  
ANISOU 1817  CA  ARG A 202     3271   2850   4157   -248    268    398       C  
ATOM   1818  C   ARG A 202      -7.851  -8.348 -10.500  1.00 18.30           C  
ANISOU 1818  C   ARG A 202     2221   1716   3018   -285    340    468       C  
ATOM   1819  O   ARG A 202      -6.972  -7.624 -10.979  1.00 25.56           O  
ANISOU 1819  O   ARG A 202     3090   2637   3986   -359    393    515       O  
ATOM   1820  CB  ARG A 202      -7.612  -8.260  -8.005  1.00 30.32           C  
ANISOU 1820  CB  ARG A 202     3690   3194   4636   -301    180    370       C  
ATOM   1821  CG  ARG A 202      -8.949  -8.264  -7.256  1.00 48.07           C  
ANISOU 1821  CG  ARG A 202     6040   5385   6841   -250    107    332       C  
ATOM   1822  CD  ARG A 202      -9.362  -6.899  -6.695  1.00 42.67           C  
ANISOU 1822  CD  ARG A 202     5418   4603   6191   -305     56    338       C  
ATOM   1823  NE  ARG A 202      -8.678  -6.570  -5.446  1.00 49.05           N  
ANISOU 1823  NE  ARG A 202     6177   5389   7070   -348    -16    294       N  
ATOM   1824  CZ  ARG A 202      -9.189  -6.708  -4.225  1.00 48.52           C  
ANISOU 1824  CZ  ARG A 202     6146   5292   6999   -312    -98    238       C  
ATOM   1825  NH1 ARG A 202     -10.414  -7.182  -4.033  1.00 56.21           N1+
ANISOU 1825  NH1 ARG A 202     7197   6254   7905   -233   -116    219       N1+
ATOM   1826  NH2 ARG A 202      -8.455  -6.367  -3.180  1.00 49.62           N  
ANISOU 1826  NH2 ARG A 202     6240   5414   7200   -357   -163    200       N  
ATOM   1827  H   ARG A 202      -5.658  -9.237  -9.513  1.00 33.40           H  
ATOM   1828  HE  ARG A 202      -7.878  -6.261  -5.506  1.00 59.68           H  
ATOM   1829 HH11 ARG A 202     -10.898  -7.408  -4.707  1.00 68.27           H  
ATOM   1830 HH12 ARG A 202     -10.723  -7.264  -3.235  1.00 68.27           H  
ATOM   1831 HH21 ARG A 202      -7.660  -6.060  -3.295  1.00 60.37           H  
ATOM   1832 HH22 ARG A 202      -8.773  -6.451  -2.385  1.00 60.37           H  
ATOM   1833  N   LEU A 203      -9.082  -8.413 -10.976  1.00 23.77           N  
ANISOU 1833  N   LEU A 203     3019   2381   3632   -236    336    478       N  
ATOM   1834  CA  LEU A 203      -9.530  -7.611 -12.103  1.00 25.47           C  
ANISOU 1834  CA  LEU A 203     3309   2564   3805   -258    390    544       C  
ATOM   1835  C   LEU A 203     -10.027  -6.273 -11.566  1.00 31.39           C  
ANISOU 1835  C   LEU A 203     4120   3216   4592   -308    338    558       C  
ATOM   1836  O   LEU A 203     -11.029  -6.216 -10.850  1.00 38.86           O  
ANISOU 1836  O   LEU A 203     5126   4119   5519   -269    267    524       O  
ATOM   1837  CB  LEU A 203     -10.617  -8.359 -12.867  1.00 25.06           C  
ANISOU 1837  CB  LEU A 203     3337   2535   3649   -178    402    544       C  
ATOM   1838  CG  LEU A 203     -11.433  -7.638 -13.932  1.00 33.36           C  
ANISOU 1838  CG  LEU A 203     4487   3552   4637   -177    433    604       C  
ATOM   1839  CD1 LEU A 203     -10.555  -7.023 -14.988  1.00 26.97           C  
ANISOU 1839  CD1 LEU A 203     3661   2752   3834   -232    526    674       C  
ATOM   1840  CD2 LEU A 203     -12.397  -8.643 -14.542  1.00 28.25           C  
ANISOU 1840  CD2 LEU A 203     3897   2945   3890    -96    431    588       C  
ATOM   1841  H   LEU A 203      -9.693  -8.926 -10.656  1.00 29.34           H  
ATOM   1842  N   ILE A 204      -9.309  -5.204 -11.938  1.00 41.18           N  
ANISOU 1842  N   ILE A 204     5345   4420   5882   -394    379    611       N  
ATOM   1843  CA  ILE A 204      -9.579  -3.847 -11.476  1.00 39.78           C  
ANISOU 1843  CA  ILE A 204     5228   4140   5747   -454    338    628       C  
ATOM   1844  C   ILE A 204     -10.611  -3.161 -12.354  1.00 33.13           C  
ANISOU 1844  C   ILE A 204     4507   3244   4838   -430    361    683       C  
ATOM   1845  O   ILE A 204     -11.350  -2.287 -11.882  1.00 32.69           O  
ANISOU 1845  O   ILE A 204     4532   3102   4787   -432    309    683       O  
ATOM   1846  CB  ILE A 204      -8.291  -2.997 -11.563  1.00 49.88           C  
ANISOU 1846  CB  ILE A 204     6439   5400   7113   -568    377    665       C  
ATOM   1847  CG1 ILE A 204      -7.132  -3.570 -10.770  1.00 56.06           C  
ANISOU 1847  CG1 ILE A 204     7087   6243   7971   -600    356    619       C  
ATOM   1848  CG2 ILE A 204      -8.553  -1.529 -11.183  1.00 59.60           C  
ANISOU 1848  CG2 ILE A 204     7750   6511   8386   -637    340    687       C  
ATOM   1849  CD1 ILE A 204      -7.473  -3.851  -9.369  1.00 58.31           C  
ANISOU 1849  CD1 ILE A 204     7372   6508   8277   -568    251    541       C  
ATOM   1850  H   ILE A 204      -8.639  -5.243 -12.476  1.00 50.24           H  
ATOM   1851  N   ARG A 205     -10.634  -3.515 -13.639  1.00 31.88           N  
ANISOU 1851  N   ARG A 205     4364   3135   4614   -406    439    732       N  
ATOM   1852  CA  ARG A 205     -11.298  -2.695 -14.639  1.00 20.86           C  
ANISOU 1852  CA  ARG A 205     3074   1691   3162   -402    475    801       C  
ATOM   1853  C   ARG A 205     -11.441  -3.428 -15.962  1.00 33.92           C  
ANISOU 1853  C   ARG A 205     4745   3418   4724   -352    548    836       C  
ATOM   1854  O   ARG A 205     -10.536  -4.148 -16.387  1.00 29.12           O  
ANISOU 1854  O   ARG A 205     4060   2885   4118   -360    610    837       O  
ATOM   1855  CB  ARG A 205     -10.489  -1.409 -14.859  1.00 29.30           C  
ANISOU 1855  CB  ARG A 205     4146   2691   4294   -507    518    862       C  
ATOM   1856  CG  ARG A 205     -11.128  -0.379 -15.761  1.00 39.87           C  
ANISOU 1856  CG  ARG A 205     5606   3959   5584   -510    550    939       C  
ATOM   1857  CD  ARG A 205     -10.626   1.021 -15.379  1.00 40.41           C  
ANISOU 1857  CD  ARG A 205     5700   3920   5733   -611    546    972       C  
ATOM   1858  NE  ARG A 205     -10.906   1.322 -13.973  1.00 39.49           N  
ANISOU 1858  NE  ARG A 205     5587   3742   5674   -616    447    905       N  
ATOM   1859  CZ  ARG A 205      -9.986   1.482 -13.021  1.00 45.34           C  
ANISOU 1859  CZ  ARG A 205     6249   4470   6510   -694    415    865       C  
ATOM   1860  NH1 ARG A 205      -8.688   1.387 -13.291  1.00 38.67           N1+
ANISOU 1860  NH1 ARG A 205     5299   3670   5722   -779    474    886       N1+
ATOM   1861  NH2 ARG A 205     -10.377   1.743 -11.785  1.00 42.90           N  
ANISOU 1861  NH2 ARG A 205     5962   4103   6235   -685    323    804       N  
ATOM   1862  H   ARG A 205     -10.270  -4.228 -13.954  1.00 39.07           H  
ATOM   1863  HE  ARG A 205     -11.731   1.402 -13.743  1.00 48.20           H  
ATOM   1864 HH11 ARG A 205      -8.427   1.220 -14.093  1.00 47.22           H  
ATOM   1865 HH12 ARG A 205      -8.110   1.493 -12.664  1.00 47.22           H  
ATOM   1866 HH21 ARG A 205     -11.215   1.808 -11.605  1.00 52.30           H  
ATOM   1867 HH22 ARG A 205      -9.793   1.848 -11.163  1.00 52.30           H  
ATOM   1868  N   ILE A 206     -12.574  -3.184 -16.618  1.00 33.78           N  
ANISOU 1868  N   ILE A 206     4833   3377   4625   -297    538    867       N  
ATOM   1869  CA  ILE A 206     -12.836  -3.593 -17.990  1.00 20.37           C  
ANISOU 1869  CA  ILE A 206     3181   1729   2828   -255    601    912       C  
ATOM   1870  C   ILE A 206     -12.917  -2.328 -18.829  1.00 21.41           C  
ANISOU 1870  C   ILE A 206     3399   1795   2940   -291    647   1000       C  
ATOM   1871  O   ILE A 206     -13.707  -1.409 -18.492  1.00 21.82           O  
ANISOU 1871  O   ILE A 206     3527   1764   2998   -285    594   1014       O  
ATOM   1872  CB  ILE A 206     -14.114  -4.446 -18.086  1.00 24.18           C  
ANISOU 1872  CB  ILE A 206     3714   2249   3226   -159    545    873       C  
ATOM   1873  CG1 ILE A 206     -13.970  -5.704 -17.220  1.00 31.33           C  
ANISOU 1873  CG1 ILE A 206     4540   3211   4154   -129    505    789       C  
ATOM   1874  CG2 ILE A 206     -14.398  -4.833 -19.526  1.00 24.26           C  
ANISOU 1874  CG2 ILE A 206     3782   2308   3128   -117    601    916       C  
ATOM   1875  CD1 ILE A 206     -15.292  -6.390 -16.905  1.00 24.04           C  
ANISOU 1875  CD1 ILE A 206     3657   2301   3175    -54    429    742       C  
ATOM   1876  H   ILE A 206     -13.236  -2.762 -16.268  1.00 41.35           H  
ATOM   1877  N   LYS A 207     -12.162  -2.306 -19.958  1.00 31.83           N  
ANISOU 1877  N   LYS A 207     4715   3150   4228   -319    748   1060       N  
ATOM   1878  CA  LYS A 207     -11.880  -1.162 -20.822  1.00 23.52           C  
ANISOU 1878  CA  LYS A 207     3729   2041   3165   -372    817   1154       C  
ATOM   1879  C   LYS A 207     -12.421  -1.427 -22.209  1.00 23.81           C  
ANISOU 1879  C   LYS A 207     3840   2133   3074   -308    850   1189       C  
ATOM   1880  O   LYS A 207     -12.734  -2.583 -22.549  1.00 40.56           O  
ANISOU 1880  O   LYS A 207     5963   4321   5128   -240    861   1164       O  
ATOM   1881  CB  LYS A 207     -10.318  -0.960 -20.875  1.00 25.46           C  
ANISOU 1881  CB  LYS A 207     3875   2305   3492   -472    905   1182       C  
ATOM   1882  CG  LYS A 207      -9.664  -0.538 -19.564  1.00 42.18           C  
ANISOU 1882  CG  LYS A 207     5909   4379   5739   -551    856   1140       C  
ATOM   1883  CD  LYS A 207      -8.165  -0.323 -19.732  1.00 52.90           C  
ANISOU 1883  CD  LYS A 207     7163   5764   7174   -652    943   1175       C  
ATOM   1884  CE  LYS A 207      -7.734   1.018 -19.158  1.00 57.90           C  
ANISOU 1884  CE  LYS A 207     7800   6303   7897   -761    914   1194       C  
ATOM   1885  NZ  LYS A 207      -7.749   1.021 -17.666  1.00 59.38           N1+
ANISOU 1885  NZ  LYS A 207     7940   6446   8177   -783    818   1122       N1+
ATOM   1886  H   LYS A 207     -11.774  -3.012 -20.258  1.00 39.01           H  
ATOM   1887  HZ1 LYS A 207      -7.491   1.816 -17.360  1.00 72.08           H  
ATOM   1888  HZ2 LYS A 207      -8.571   0.851 -17.370  1.00 72.08           H  
ATOM   1889  HZ3 LYS A 207      -7.195   0.398 -17.354  1.00 72.08           H  
ATOM   1890  N   GLY A 208     -12.619  -0.388 -23.020  1.00 24.74           N  
ANISOU 1890  N   GLY A 208     4027   2222   3152   -323    855   1241       N  
ATOM   1891  CA  GLY A 208     -13.040  -0.617 -24.388  1.00 34.45           C  
ANISOU 1891  CA  GLY A 208     5323   3505   4262   -266    888   1275       C  
ATOM   1892  C   GLY A 208     -13.288   0.664 -25.144  1.00 42.62           C  
ANISOU 1892  C   GLY A 208     6433   4494   5267   -285    884   1334       C  
ATOM   1893  O   GLY A 208     -12.905   1.743 -24.692  1.00 29.71           O  
ANISOU 1893  O   GLY A 208     4794   2787   3706   -355    875   1357       O  
ATOM   1894  H   GLY A 208     -12.518   0.438 -22.802  1.00 28.68           H  
ATOM   1895  N   GLU A 209     -13.932   0.527 -26.308  1.00 40.70           N  
ANISOU 1895  N   GLU A 209     6261   4292   4912   -221    888   1359       N  
ATOM   1896  CA  GLU A 209     -14.337   1.601 -27.214  1.00 42.66           C  
ANISOU 1896  CA  GLU A 209     6592   4507   5109   -216    883   1418       C  
ATOM   1897  C   GLU A 209     -15.856   1.484 -27.409  1.00 43.04           C  
ANISOU 1897  C   GLU A 209     6704   4567   5084   -120    789   1394       C  
ATOM   1898  O   GLU A 209     -16.511   0.648 -26.788  1.00 56.44           O  
ANISOU 1898  O   GLU A 209     8376   6291   6777    -71    730   1334       O  
ATOM   1899  CB  GLU A 209     -13.565   1.515 -28.533  1.00 51.83           C  
ANISOU 1899  CB  GLU A 209     7771   5718   6204   -233    987   1472       C  
ATOM   1900  CG  GLU A 209     -12.041   1.553 -28.392  1.00 61.75           C  
ANISOU 1900  CG  GLU A 209     8947   6982   7535   -328   1088   1496       C  
ATOM   1901  CD  GLU A 209     -11.320   1.334 -29.719  1.00 79.52           C  
ANISOU 1901  CD  GLU A 209    11209   9295   9711   -332   1196   1545       C  
ATOM   1902  OE1 GLU A 209     -10.309   2.026 -29.980  1.00 78.77           O  
ANISOU 1902  OE1 GLU A 209    11087   9183   9658   -415   1270   1598       O  
ATOM   1903  OE2 GLU A 209     -11.765   0.468 -30.502  1.00 84.68           O1-
ANISOU 1903  OE2 GLU A 209    11900  10015  10261   -253   1203   1529       O1-
ATOM   1904  H   GLU A 209     -14.161  -0.242 -26.617  1.00 49.66           H  
ATOM   1905  N   GLU A 210     -16.416   2.297 -28.315  1.00 45.54           N  
ANISOU 1905  N   GLU A 210     7098   4867   5339    -93    776   1443       N  
ATOM   1906  CA  GLU A 210     -17.844   2.168 -28.611  1.00 49.80           C  
ANISOU 1906  CA  GLU A 210     7688   5429   5806     -1    691   1424       C  
ATOM   1907  C   GLU A 210     -18.177   0.778 -29.153  1.00 52.83           C  
ANISOU 1907  C   GLU A 210     8067   5904   6102     57    690   1385       C  
ATOM   1908  O   GLU A 210     -19.217   0.201 -28.804  1.00 48.14           O  
ANISOU 1908  O   GLU A 210     7468   5338   5485    117    609   1337       O  
ATOM   1909  CB  GLU A 210     -18.267   3.268 -29.593  1.00 65.30           C  
ANISOU 1909  CB  GLU A 210     9733   7362   7715     17    689   1489       C  
ATOM   1910  CG  GLU A 210     -19.746   3.266 -29.978  1.00 82.29           C  
ANISOU 1910  CG  GLU A 210    11933   9539   9795    110    601   1478       C  
ATOM   1911  CD  GLU A 210     -20.564   4.349 -29.286  1.00 96.02           C  
ANISOU 1911  CD  GLU A 210    13688  11208  11587    130    527   1481       C  
ATOM   1912  OE1 GLU A 210     -20.083   5.499 -29.173  1.00 97.94           O  
ANISOU 1912  OE1 GLU A 210    13957  11374  11882     82    554   1526       O  
ATOM   1913  OE2 GLU A 210     -21.703   4.048 -28.869  1.00 99.15           O1-
ANISOU 1913  OE2 GLU A 210    14071  11627  11973    196    445   1438       O1-
ATOM   1914  H   GLU A 210     -16.004   2.909 -28.755  1.00 55.47           H  
ATOM   1915  N   ALA A 211     -17.290   0.198 -29.974  1.00 54.03           N  
ANISOU 1915  N   ALA A 211     8218   6105   6206     38    780   1404       N  
ATOM   1916  CA  ALA A 211     -17.512  -1.145 -30.509  1.00 50.49           C  
ANISOU 1916  CA  ALA A 211     7773   5740   5672     92    784   1364       C  
ATOM   1917  C   ALA A 211     -17.550  -2.215 -29.420  1.00 48.41           C  
ANISOU 1917  C   ALA A 211     7442   5496   5454    100    754   1293       C  
ATOM   1918  O   ALA A 211     -18.252  -3.228 -29.572  1.00 53.45           O  
ANISOU 1918  O   ALA A 211     8092   6189   6029    157    708   1246       O  
ATOM   1919  CB  ALA A 211     -16.426  -1.485 -31.533  1.00 50.46           C  
ANISOU 1919  CB  ALA A 211     7776   5780   5615     70    897   1397       C  
ATOM   1920  H   ALA A 211     -16.556   0.563 -30.235  1.00 65.66           H  
ATOM   1921  N   GLY A 212     -16.776  -2.045 -28.350  1.00 31.58           N  
ANISOU 1921  N   GLY A 212     5244   3324   3431     42    779   1283       N  
ATOM   1922  CA  GLY A 212     -16.836  -2.942 -27.209  1.00 31.11           C  
ANISOU 1922  CA  GLY A 212     5124   3273   3424     49    745   1220       C  
ATOM   1923  C   GLY A 212     -15.501  -3.047 -26.485  1.00 24.08           C  
ANISOU 1923  C   GLY A 212     4155   2366   2630    -21    820   1220       C  
ATOM   1924  O   GLY A 212     -14.613  -2.214 -26.652  1.00 24.99           O  
ANISOU 1924  O   GLY A 212     4253   2449   2792    -87    883   1268       O  
ATOM   1925  H   GLY A 212     -16.203  -1.410 -28.264  1.00 38.72           H  
ATOM   1926  N   VAL A 213     -15.413  -4.107 -25.668  1.00 38.99           N  
ANISOU 1926  N   VAL A 213     5990   4277   4547     -5    809   1165       N  
ATOM   1927  CA  VAL A 213     -14.252  -4.341 -24.817  1.00 22.95           C  
ANISOU 1927  CA  VAL A 213     3870   2234   2616    -62    867   1157       C  
ATOM   1928  C   VAL A 213     -13.005  -4.517 -25.660  1.00 23.96           C  
ANISOU 1928  C   VAL A 213     3965   2410   2730    -96    990   1196       C  
ATOM   1929  O   VAL A 213     -13.007  -5.245 -26.660  1.00 31.27           O  
ANISOU 1929  O   VAL A 213     4925   3401   3557    -48   1033   1196       O  
ATOM   1930  CB  VAL A 213     -14.461  -5.602 -23.959  1.00 22.68           C  
ANISOU 1930  CB  VAL A 213     3771   2245   2601    -25    811   1065       C  
ATOM   1931  CG1 VAL A 213     -13.197  -5.932 -23.162  1.00 21.82           C  
ANISOU 1931  CG1 VAL A 213     3540   2155   2597    -78    848   1030       C  
ATOM   1932  CG2 VAL A 213     -15.650  -5.465 -23.050  1.00 26.58           C  
ANISOU 1932  CG2 VAL A 213     4284   2700   3116      5    694   1023       C  
ATOM   1933  H   VAL A 213     -16.022  -4.710 -25.591  1.00 47.60           H  
ATOM   1934  N   THR A 214     -11.909  -3.897 -25.225  1.00 31.62           N  
ANISOU 1934  N   THR A 214     4862   3352   3802   -179   1046   1224       N  
ATOM   1935  CA  THR A 214     -10.606  -4.112 -25.835  1.00 25.78           C  
ANISOU 1935  CA  THR A 214     4059   2665   3070   -217   1166   1257       C  
ATOM   1936  C   THR A 214      -9.568  -4.648 -24.866  1.00 30.47           C  
ANISOU 1936  C   THR A 214     4514   3289   3774   -257   1186   1212       C  
ATOM   1937  O   THR A 214      -8.553  -5.194 -25.317  1.00 29.69           O  
ANISOU 1937  O   THR A 214     4346   3260   3675   -263   1280   1221       O  
ATOM   1938  CB  THR A 214     -10.067  -2.804 -26.430  1.00 27.71           C  
ANISOU 1938  CB  THR A 214     4319   2874   3335   -291   1208   1324       C  
ATOM   1939  CG2 THR A 214     -10.972  -2.302 -27.536  1.00 43.50           C  
ANISOU 1939  CG2 THR A 214     6438   4866   5223   -245   1180   1356       C  
ATOM   1940  OG1 THR A 214      -9.996  -1.819 -25.394  1.00 40.64           O  
ANISOU 1940  OG1 THR A 214     5929   4428   5083   -363   1154   1324       O  
ATOM   1941  H   THR A 214     -11.897  -3.341 -24.569  1.00 38.77           H  
ATOM   1942  HG1 THR A 214      -9.702  -1.096 -25.703  1.00 49.58           H  
ATOM   1943  N   ALA A 215      -9.785  -4.513 -23.559  1.00 40.97           N  
ANISOU 1943  N   ALA A 215     5793   4577   5195   -280   1091   1157       N  
ATOM   1944  CA  ALA A 215      -8.770  -4.900 -22.594  1.00 25.74           C  
ANISOU 1944  CA  ALA A 215     3726   2679   3375   -322   1090   1109       C  
ATOM   1945  C   ALA A 215      -9.338  -4.900 -21.187  1.00 23.22           C  
ANISOU 1945  C   ALA A 215     3384   2314   3123   -320    966   1037       C  
ATOM   1946  O   ALA A 215     -10.396  -4.320 -20.917  1.00 29.66           O  
ANISOU 1946  O   ALA A 215     4285   3063   3922   -305    892   1038       O  
ATOM   1947  CB  ALA A 215      -7.560  -3.960 -22.656  1.00 26.33           C  
ANISOU 1947  CB  ALA A 215     3733   2733   3538   -429   1169   1172       C  
ATOM   1948  H   ALA A 215     -10.507  -4.201 -23.214  1.00 49.98           H  
ATOM   1949  N   VAL A 216      -8.592  -5.548 -20.293  1.00 39.07           N  
ANISOU 1949  N   VAL A 216     5275   4362   5206   -331    948    979       N  
ATOM   1950  CA  VAL A 216      -8.830  -5.505 -18.859  1.00 24.83           C  
ANISOU 1950  CA  VAL A 216     3432   2520   3481   -343    842    914       C  
ATOM   1951  C   VAL A 216      -7.557  -5.012 -18.189  1.00 37.05           C  
ANISOU 1951  C   VAL A 216     4864   4064   5149   -435    860    918       C  
ATOM   1952  O   VAL A 216      -6.446  -5.171 -18.708  1.00 26.87           O  
ANISOU 1952  O   VAL A 216     3494   2833   3883   -469    950    949       O  
ATOM   1953  CB  VAL A 216      -9.224  -6.873 -18.258  1.00 20.96           C  
ANISOU 1953  CB  VAL A 216     2915   2083   2965   -261    783    829       C  
ATOM   1954  CG1 VAL A 216     -10.557  -7.328 -18.796  1.00 28.89           C  
ANISOU 1954  CG1 VAL A 216     4028   3087   3860   -182    750    819       C  
ATOM   1955  CG2 VAL A 216      -8.139  -7.906 -18.526  1.00 27.19           C  
ANISOU 1955  CG2 VAL A 216     3607   2965   3759   -241    853    812       C  
ATOM   1956  H   VAL A 216      -7.916  -6.035 -20.505  1.00 47.70           H  
ATOM   1957  N   GLU A 217      -7.734  -4.429 -17.009  1.00 28.58           N  
ANISOU 1957  N   GLU A 217     3783   2926   4151   -475    771    883       N  
ATOM   1958  CA  GLU A 217      -6.658  -4.032 -16.110  1.00 31.47           C  
ANISOU 1958  CA  GLU A 217     4039   3283   4634   -560    753    867       C  
ATOM   1959  C   GLU A 217      -6.678  -4.999 -14.935  1.00 23.90           C  
ANISOU 1959  C   GLU A 217     3017   2362   3703   -510    670    777       C  
ATOM   1960  O   GLU A 217      -7.708  -5.133 -14.265  1.00 25.39           O  
ANISOU 1960  O   GLU A 217     3271   2510   3865   -460    585    731       O  
ATOM   1961  CB  GLU A 217      -6.873  -2.588 -15.654  1.00 23.48           C  
ANISOU 1961  CB  GLU A 217     3086   2157   3678   -642    710    893       C  
ATOM   1962  CG  GLU A 217      -5.729  -1.951 -14.897  1.00 27.73           C  
ANISOU 1962  CG  GLU A 217     3525   2675   4337   -754    697    889       C  
ATOM   1963  CD  GLU A 217      -5.979  -0.475 -14.607  1.00 32.40           C  
ANISOU 1963  CD  GLU A 217     4198   3139   4972   -838    664    921       C  
ATOM   1964  OE1 GLU A 217      -7.065   0.035 -14.962  1.00 31.00           O  
ANISOU 1964  OE1 GLU A 217     4155   2894   4731   -797    650    947       O  
ATOM   1965  OE2 GLU A 217      -5.087   0.173 -14.020  1.00 33.87           O1-
ANISOU 1965  OE2 GLU A 217     4317   3295   5257   -943    648    920       O1-
ATOM   1966  H   GLU A 217      -8.511  -4.243 -16.691  1.00 35.12           H  
ATOM   1967  N   VAL A 218      -5.566  -5.703 -14.709  1.00 35.56           N  
ANISOU 1967  N   VAL A 218     4365   3918   5228   -517    698    754       N  
ATOM   1968  CA  VAL A 218      -5.435  -6.615 -13.578  1.00 24.96           C  
ANISOU 1968  CA  VAL A 218     2956   2612   3915   -471    622    674       C  
ATOM   1969  C   VAL A 218      -4.244  -6.203 -12.725  1.00 24.25           C  
ANISOU 1969  C   VAL A 218     2741   2531   3941   -555    596    661       C  
ATOM   1970  O   VAL A 218      -3.319  -5.530 -13.185  1.00 33.08           O  
ANISOU 1970  O   VAL A 218     3795   3658   5114   -642    660    714       O  
ATOM   1971  CB  VAL A 218      -5.274  -8.086 -14.021  1.00 37.18           C  
ANISOU 1971  CB  VAL A 218     4468   4256   5402   -376    665    648       C  
ATOM   1972  CG1 VAL A 218      -6.449  -8.513 -14.872  1.00 35.99           C  
ANISOU 1972  CG1 VAL A 218     4441   4098   5136   -300    682    657       C  
ATOM   1973  CG2 VAL A 218      -3.946  -8.272 -14.760  1.00 38.83           C  
ANISOU 1973  CG2 VAL A 218     4567   4546   5641   -403    771    689       C  
ATOM   1974  H   VAL A 218      -4.866  -5.666 -15.207  1.00 43.49           H  
ATOM   1975  N   ARG A 219      -4.261  -6.637 -11.464  1.00 28.69           N  
ANISOU 1975  N   ARG A 219     3267   3094   4539   -531    500    590       N  
ATOM   1976  CA  ARG A 219      -3.206  -6.278 -10.526  1.00 37.08           C  
ANISOU 1976  CA  ARG A 219     4216   4165   5708   -607    454    567       C  
ATOM   1977  C   ARG A 219      -3.087  -7.343  -9.439  1.00 32.27           C  
ANISOU 1977  C   ARG A 219     3552   3604   5107   -535    377    490       C  
ATOM   1978  O   ARG A 219      -4.091  -7.773  -8.871  1.00 30.56           O  
ANISOU 1978  O   ARG A 219     3419   3354   4838   -465    312    444       O  
ATOM   1979  CB  ARG A 219      -3.472  -4.905  -9.895  1.00 40.68           C  
ANISOU 1979  CB  ARG A 219     4730   4510   6215   -699    388    571       C  
ATOM   1980  CG  ARG A 219      -2.503  -4.540  -8.783  1.00 52.79           C  
ANISOU 1980  CG  ARG A 219     6160   6044   7854   -778    316    535       C  
ATOM   1981  CD  ARG A 219      -3.031  -3.402  -7.932  1.00 58.01           C  
ANISOU 1981  CD  ARG A 219     6910   6585   8545   -839    227    514       C  
ATOM   1982  NE  ARG A 219      -2.958  -2.126  -8.636  1.00 54.94           N  
ANISOU 1982  NE  ARG A 219     6572   6121   8181   -938    278    582       N  
ATOM   1983  CZ  ARG A 219      -3.545  -1.011  -8.218  1.00 51.52           C  
ANISOU 1983  CZ  ARG A 219     6248   5568   7759   -987    225    582       C  
ATOM   1984  NH1 ARG A 219      -4.249  -1.010  -7.094  1.00 45.17           N1+
ANISOU 1984  NH1 ARG A 219     5510   4711   6943   -943    122    516       N1+
ATOM   1985  NH2 ARG A 219      -3.426   0.105  -8.925  1.00 54.84           N  
ANISOU 1985  NH2 ARG A 219     6718   5918   8201  -1076    279    650       N  
ATOM   1986  H   ARG A 219      -4.874  -7.139 -11.131  1.00 35.24           H  
ATOM   1987  HE  ARG A 219      -2.507  -2.094  -9.367  1.00 66.74           H  
ATOM   1988 HH11 ARG A 219      -4.325  -1.733  -6.634  1.00 55.03           H  
ATOM   1989 HH12 ARG A 219      -4.628  -0.287  -6.824  1.00 55.03           H  
ATOM   1990 HH21 ARG A 219      -2.969   0.106  -9.653  1.00 66.63           H  
ATOM   1991 HH22 ARG A 219      -3.806   0.828  -8.654  1.00 66.63           H  
ATOM   1992  N   HIS A 220      -1.849  -7.731  -9.138  1.00 43.44           N  
ANISOU 1992  N   HIS A 220     4822   5095   6587   -555    384    478       N  
ATOM   1993  CA  HIS A 220      -1.563  -8.616  -8.000  1.00 46.21           C  
ANISOU 1993  CA  HIS A 220     5111   5489   6959   -497    302    408       C  
ATOM   1994  C   HIS A 220      -1.792  -7.859  -6.696  1.00 42.41           C  
ANISOU 1994  C   HIS A 220     4658   4930   6526   -550    183    365       C  
ATOM   1995  O   HIS A 220      -1.270  -6.753  -6.531  1.00 50.61           O  
ANISOU 1995  O   HIS A 220     5664   5928   7636   -661    167    385       O  
ATOM   1996  CB  HIS A 220      -0.111  -9.097  -8.098  1.00 53.30           C  
ANISOU 1996  CB  HIS A 220     5839   6493   7921   -507    344    417       C  
ATOM   1997  CG  HIS A 220       0.114 -10.510  -7.650  1.00 62.85           C  
ANISOU 1997  CG  HIS A 220     6998   7778   9103   -392    323    367       C  
ATOM   1998  CD2 HIS A 220       0.428 -11.021  -6.437  1.00 65.98           C  
ANISOU 1998  CD2 HIS A 220     7342   8197   9531   -358    228    307       C  
ATOM   1999  ND1 HIS A 220       0.104 -11.578  -8.524  1.00 66.31           N  
ANISOU 1999  ND1 HIS A 220     7439   8280   9474   -298    408    378       N  
ATOM   2000  CE1 HIS A 220       0.369 -12.689  -7.859  1.00 72.44           C  
ANISOU 2000  CE1 HIS A 220     8172   9108  10242   -208    367    328       C  
ATOM   2001  NE2 HIS A 220       0.567 -12.380  -6.591  1.00 66.14           N  
ANISOU 2001  NE2 HIS A 220     7338   8288   9503   -241    258    286       N  
ATOM   2002  H   HIS A 220      -1.147  -7.498  -9.578  1.00 52.94           H  
ATOM   2003  HE2 HIS A 220       0.752 -12.937  -5.964  1.00 80.18           H  
ATOM   2004  N   PRO A 221      -2.577  -8.400  -5.761  1.00 32.54           N  
ANISOU 2004  N   PRO A 221     3475   3653   5235   -476    100    305       N  
ATOM   2005  CA  PRO A 221      -2.843  -7.674  -4.510  1.00 33.44           C  
ANISOU 2005  CA  PRO A 221     3630   3690   5384   -519    -11    261       C  
ATOM   2006  C   PRO A 221      -1.569  -7.226  -3.811  1.00 40.68           C  
ANISOU 2006  C   PRO A 221     4421   4633   6401   -604    -62    246       C  
ATOM   2007  O   PRO A 221      -0.661  -8.025  -3.565  1.00 41.26           O  
ANISOU 2007  O   PRO A 221     4375   4798   6504   -574    -68    228       O  
ATOM   2008  CB  PRO A 221      -3.611  -8.703  -3.665  1.00 39.11           C  
ANISOU 2008  CB  PRO A 221     4405   4414   6041   -408    -74    200       C  
ATOM   2009  CG  PRO A 221      -4.236  -9.625  -4.667  1.00 40.08           C  
ANISOU 2009  CG  PRO A 221     4572   4573   6082   -323      6    222       C  
ATOM   2010  CD  PRO A 221      -3.253  -9.712  -5.799  1.00 36.75           C  
ANISOU 2010  CD  PRO A 221     4055   4222   5685   -353    106    274       C  
ATOM   2011  N   GLY A 222      -1.508  -5.936  -3.466  1.00 47.10           N  
ANISOU 2011  N   GLY A 222     5264   5364   7266   -711   -105    252       N  
ATOM   2012  CA  GLY A 222      -0.349  -5.376  -2.808  1.00 39.93           C  
ANISOU 2012  CA  GLY A 222     4245   4469   6456   -811   -163    237       C  
ATOM   2013  C   GLY A 222       0.726  -4.835  -3.725  1.00 31.01           C  
ANISOU 2013  C   GLY A 222     3002   3380   5399   -915    -81    301       C  
ATOM   2014  O   GLY A 222       1.648  -4.163  -3.241  1.00 39.16           O  
ANISOU 2014  O   GLY A 222     3946   4412   6522  -1024   -129    295       O  
ATOM   2015  H   GLY A 222      -2.137  -5.368  -3.610  1.00 57.33           H  
ATOM   2016  N   GLU A 223       0.601  -5.013  -5.039  1.00 50.51           N  
ANISOU 2016  N   GLU A 223     5480   5880   7832   -896     41    364       N  
ATOM   2017  CA  GLU A 223       1.710  -4.643  -5.910  1.00 62.92           C  
ANISOU 2017  CA  GLU A 223     6929   7508   9469   -986    131    428       C  
ATOM   2018  C   GLU A 223       1.697  -3.159  -6.263  1.00 59.90           C  
ANISOU 2018  C   GLU A 223     6603   7026   9132  -1123    149    477       C  
ATOM   2019  O   GLU A 223       2.755  -2.523  -6.246  1.00 78.44           O  
ANISOU 2019  O   GLU A 223     8840   9390  11573  -1244    155    501       O  
ATOM   2020  CB  GLU A 223       1.689  -5.510  -7.168  1.00 88.53           C  
ANISOU 2020  CB  GLU A 223    10156  10832  12651   -903    259    475       C  
ATOM   2021  CG  GLU A 223       2.483  -6.800  -7.002  1.00115.36           C  
ANISOU 2021  CG  GLU A 223    13418  14359  16056   -818    269    447       C  
ATOM   2022  CD  GLU A 223       3.970  -6.545  -6.807  1.00131.11           C  
ANISOU 2022  CD  GLU A 223    15222  16431  18162   -908    271    462       C  
ATOM   2023  OE1 GLU A 223       4.401  -5.382  -6.958  1.00137.63           O  
ANISOU 2023  OE1 GLU A 223    16021  17213  19058  -1045    280    500       O  
ATOM   2024  OE2 GLU A 223       4.715  -7.502  -6.513  1.00135.30           O1-
ANISOU 2024  OE2 GLU A 223    15629  17067  18712   -841    264    436       O1-
ATOM   2025  H   GLU A 223      -0.091  -5.335  -5.435  1.00 61.43           H  
ATOM   2026  N   SER A 224       0.529  -2.566  -6.539  1.00 53.94           N  
ANISOU 2026  N   SER A 224     6017   6164   8315  -1110    154    492       N  
ATOM   2027  CA  SER A 224       0.347  -1.116  -6.796  1.00 61.13           C  
ANISOU 2027  CA  SER A 224     7013   6956   9256  -1226    162    536       C  
ATOM   2028  C   SER A 224       0.678  -0.735  -8.242  1.00 56.37           C  
ANISOU 2028  C   SER A 224     6397   6369   8651  -1278    300    631       C  
ATOM   2029  O   SER A 224       0.720   0.462  -8.560  1.00 63.69           O  
ANISOU 2029  O   SER A 224     7380   7206   9612  -1387    322    679       O  
ATOM   2030  CB  SER A 224       1.141  -0.216  -5.843  1.00 58.79           C  
ANISOU 2030  CB  SER A 224     6661   6612   9065  -1359     73    508       C  
ATOM   2031  OG  SER A 224       1.095   1.152  -6.242  1.00 53.75           O  
ANISOU 2031  OG  SER A 224     6101   5861   8460  -1480     98    559       O  
ATOM   2032  H   SER A 224      -0.212  -3.000  -6.587  1.00 65.55           H  
ATOM   2033  HG  SER A 224       1.532   1.624  -5.702  1.00 65.31           H  
ATOM   2034  N   ASP A 225       0.996  -1.685  -9.110  1.00 53.82           N  
ANISOU 2034  N   ASP A 225     6000   6157   8291  -1210    396    661       N  
ATOM   2035  CA  ASP A 225       1.129  -1.367 -10.530  1.00 43.36           C  
ANISOU 2035  CA  ASP A 225     4691   4843   6940  -1239    532    751       C  
ATOM   2036  C   ASP A 225       0.349  -2.403 -11.334  1.00 52.66           C  
ANISOU 2036  C   ASP A 225     5934   6073   8002  -1096    594    757       C  
ATOM   2037  O   ASP A 225       0.535  -3.607 -11.155  1.00 43.56           O  
ANISOU 2037  O   ASP A 225     4710   5014   6825  -1001    591    716       O  
ATOM   2038  CB  ASP A 225       2.585  -1.309 -10.979  1.00 45.44           C  
ANISOU 2038  CB  ASP A 225     4779   5197   7290  -1331    612    799       C  
ATOM   2039  H   ASP A 225       1.138  -2.508  -8.907  1.00 65.40           H  
ATOM   2040  N   SER A 226      -0.423  -1.908 -12.297  1.00 51.78           N  
ANISOU 2040  N   SER A 226     5952   5902   7821  -1087    658    815       N  
ATOM   2041  CA  SER A 226      -1.391  -2.709 -13.024  1.00 40.59           C  
ANISOU 2041  CA  SER A 226     4629   4509   6285   -959    697    817       C  
ATOM   2042  C   SER A 226      -0.807  -3.249 -14.321  1.00 40.63           C  
ANISOU 2042  C   SER A 226     4579   4608   6251   -935    833    877       C  
ATOM   2043  O   SER A 226       0.129  -2.690 -14.898  1.00 64.91           O  
ANISOU 2043  O   SER A 226     7580   7704   9378  -1027    918    940       O  
ATOM   2044  CB  SER A 226      -2.628  -1.850 -13.318  1.00 39.29           C  
ANISOU 2044  CB  SER A 226     4641   4227   6060   -955    678    845       C  
ATOM   2045  OG  SER A 226      -3.257  -1.422 -12.118  1.00 52.66           O  
ANISOU 2045  OG  SER A 226     6395   5835   7777   -958    557    786       O  
ATOM   2046  H   SER A 226      -0.401  -1.087 -12.552  1.00 62.96           H  
ATOM   2047  HG  SER A 226      -3.930  -0.952 -12.299  1.00 64.01           H  
ATOM   2048  N   GLN A 227      -1.423  -4.326 -14.803  1.00 46.04           N  
ANISOU 2048  N   GLN A 227     5311   5345   6837   -810    857    858       N  
ATOM   2049  CA  GLN A 227      -1.034  -5.019 -16.024  1.00 50.45           C  
ANISOU 2049  CA  GLN A 227     5841   5993   7334   -758    981    901       C  
ATOM   2050  C   GLN A 227      -2.264  -5.090 -16.912  1.00 38.58           C  
ANISOU 2050  C   GLN A 227     4501   4450   5707   -686   1005    924       C  
ATOM   2051  O   GLN A 227      -3.327  -5.533 -16.467  1.00 45.73           O  
ANISOU 2051  O   GLN A 227     5492   5325   6559   -610    923    871       O  
ATOM   2052  CB  GLN A 227      -0.517  -6.423 -15.707  1.00 60.67           C  
ANISOU 2052  CB  GLN A 227     7032   7396   8625   -668    980    844       C  
ATOM   2053  CG  GLN A 227       0.546  -6.920 -16.649  1.00 73.14           C  
ANISOU 2053  CG  GLN A 227     8507   9080  10201   -656   1110    889       C  
ATOM   2054  CD  GLN A 227       0.451  -8.404 -16.868  1.00 78.61           C  
ANISOU 2054  CD  GLN A 227     9194   9855  10819   -519   1131    844       C  
ATOM   2055  NE2 GLN A 227       1.422  -9.135 -16.345  1.00 76.26           N  
ANISOU 2055  NE2 GLN A 227     8753   9643  10580   -492   1130    810       N  
ATOM   2056  OE1 GLN A 227      -0.491  -8.896 -17.491  1.00 82.37           O  
ANISOU 2056  OE1 GLN A 227     9795  10315  11185   -438   1144    838       O  
ATOM   2057  H   GLN A 227      -2.102  -4.691 -14.420  1.00 56.06           H  
ATOM   2058 HE21 GLN A 227       2.059  -8.756 -15.908  1.00 92.33           H  
ATOM   2059 HE22 GLN A 227       1.416  -9.990 -16.441  1.00 92.33           H  
ATOM   2060  N   GLU A 228      -2.134  -4.636 -18.156  1.00 34.28           N  
ANISOU 2060  N   GLU A 228     4000   3908   5118   -710   1114   1005       N  
ATOM   2061  CA  GLU A 228      -3.240  -4.628 -19.108  1.00 37.21           C  
ANISOU 2061  CA  GLU A 228     4525   4246   5367   -646   1139   1036       C  
ATOM   2062  C   GLU A 228      -3.189  -5.846 -20.016  1.00 29.58           C  
ANISOU 2062  C   GLU A 228     3558   3375   4305   -544   1215   1031       C  
ATOM   2063  O   GLU A 228      -2.157  -6.127 -20.632  1.00 43.31           O  
ANISOU 2063  O   GLU A 228     5209   5191   6055   -554   1321   1066       O  
ATOM   2064  CB  GLU A 228      -3.198  -3.334 -19.926  1.00 46.77           C  
ANISOU 2064  CB  GLU A 228     5805   5390   6575   -731   1208   1130       C  
ATOM   2065  CG  GLU A 228      -4.407  -3.093 -20.808  1.00 57.11           C  
ANISOU 2065  CG  GLU A 228     7283   6650   7766   -672   1214   1166       C  
ATOM   2066  CD  GLU A 228      -4.481  -1.670 -21.329  1.00 68.69           C  
ANISOU 2066  CD  GLU A 228     8833   8025   9242   -759   1254   1254       C  
ATOM   2067  OE1 GLU A 228      -4.325  -0.730 -20.520  1.00 69.11           O  
ANISOU 2067  OE1 GLU A 228     8874   7996   9388   -847   1199   1253       O  
ATOM   2068  OE2 GLU A 228      -4.701  -1.493 -22.547  1.00 82.03           O1-
ANISOU 2068  OE2 GLU A 228    10607   9723  10839   -734   1330   1316       O1-
ATOM   2069  H   GLU A 228      -1.401  -4.322 -18.477  1.00 41.96           H  
ATOM   2070  N   LEU A 229      -4.309  -6.548 -20.138  1.00 25.40           N  
ANISOU 2070  N   LEU A 229     3131   2840   3680   -446   1165    990       N  
ATOM   2071  CA  LEU A 229      -4.412  -7.675 -21.052  1.00 43.06           C  
ANISOU 2071  CA  LEU A 229     5397   5151   5811   -348   1229    981       C  
ATOM   2072  C   LEU A 229      -5.457  -7.360 -22.094  1.00 34.29           C  
ANISOU 2072  C   LEU A 229     4441   4002   4584   -315   1246   1024       C  
ATOM   2073  O   LEU A 229      -6.605  -7.042 -21.752  1.00 34.57           O  
ANISOU 2073  O   LEU A 229     4570   3971   4594   -300   1155   1006       O  
ATOM   2074  CB  LEU A 229      -4.787  -8.970 -20.334  1.00 27.57           C  
ANISOU 2074  CB  LEU A 229     3420   3225   3830   -258   1153    889       C  
ATOM   2075  CG  LEU A 229      -3.743  -9.566 -19.399  1.00 25.45           C  
ANISOU 2075  CG  LEU A 229     3003   3013   3655   -261   1139    842       C  
ATOM   2076  CD1 LEU A 229      -4.400 -10.579 -18.479  1.00 24.78           C  
ANISOU 2076  CD1 LEU A 229     2934   2926   3554   -184   1037    754       C  
ATOM   2077  CD2 LEU A 229      -2.622 -10.214 -20.183  1.00 35.54           C  
ANISOU 2077  CD2 LEU A 229     4196   4388   4920   -231   1261    866       C  
ATOM   2078  H   LEU A 229      -5.030  -6.386 -19.697  1.00 28.96           H  
ATOM   2079  N   LEU A 230      -5.092  -7.437 -23.366  1.00 35.00           N  
ANISOU 2079  N   LEU A 230     4561   4136   4600   -299   1362   1083       N  
ATOM   2080  CA  LEU A 230      -6.085  -7.213 -24.395  1.00 33.39           C  
ANISOU 2080  CA  LEU A 230     4509   3903   4275   -258   1373   1122       C  
ATOM   2081  C   LEU A 230      -7.013  -8.405 -24.492  1.00 25.08           C  
ANISOU 2081  C   LEU A 230     3525   2879   3126   -152   1314   1053       C  
ATOM   2082  O   LEU A 230      -6.579  -9.570 -24.463  1.00 35.89           O  
ANISOU 2082  O   LEU A 230     4842   4317   4478    -94   1337   1003       O  
ATOM   2083  CB  LEU A 230      -5.470  -6.925 -25.757  1.00 32.91           C  
ANISOU 2083  CB  LEU A 230     4476   3878   4151   -270   1515   1207       C  
ATOM   2084  CG  LEU A 230      -4.414  -5.827 -25.731  1.00 29.73           C  
ANISOU 2084  CG  LEU A 230     3993   3456   3848   -384   1591   1280       C  
ATOM   2085  CD1 LEU A 230      -3.349  -6.152 -26.772  1.00 43.31           C  
ANISOU 2085  CD1 LEU A 230     5660   5264   5530   -376   1731   1323       C  
ATOM   2086  CD2 LEU A 230      -4.982  -4.424 -25.943  1.00 47.07           C  
ANISOU 2086  CD2 LEU A 230     6287   5554   6043   -449   1558   1338       C  
ATOM   2087  H   LEU A 230      -4.300  -7.613 -23.646  1.00 42.82           H  
ATOM   2088  N   ALA A 231      -8.289  -8.093 -24.647  1.00 24.46           N  
ANISOU 2088  N   ALA A 231     3565   2746   2982   -127   1241   1054       N  
ATOM   2089  CA  ALA A 231      -9.369  -9.051 -24.668  1.00 23.46           C  
ANISOU 2089  CA  ALA A 231     3510   2633   2770    -43   1165    992       C  
ATOM   2090  C   ALA A 231     -10.576  -8.388 -25.304  1.00 23.40           C  
ANISOU 2090  C   ALA A 231     3636   2576   2678    -27   1124   1031       C  
ATOM   2091  O   ALA A 231     -10.718  -7.161 -25.272  1.00 37.43           O  
ANISOU 2091  O   ALA A 231     5442   4289   4490    -81   1120   1089       O  
ATOM   2092  CB  ALA A 231      -9.703  -9.528 -23.254  1.00 24.72           C  
ANISOU 2092  CB  ALA A 231     3611   2776   3005    -35   1056    909       C  
ATOM   2093  H   ALA A 231      -8.568  -7.286 -24.748  1.00 27.51           H  
ATOM   2094  N   GLU A 232     -11.427  -9.216 -25.899  1.00 33.22           N  
ANISOU 2094  N   GLU A 232     4963   3850   3810     47   1094   1000       N  
ATOM   2095  CA  GLU A 232     -12.682  -8.776 -26.487  1.00 41.44           C  
ANISOU 2095  CA  GLU A 232     6125   4858   4762     76   1038   1027       C  
ATOM   2096  C   GLU A 232     -13.886  -9.353 -25.776  1.00 36.52           C  
ANISOU 2096  C   GLU A 232     5521   4224   4130    117    913    956       C  
ATOM   2097  O   GLU A 232     -15.003  -8.842 -25.971  1.00 46.34           O  
ANISOU 2097  O   GLU A 232     6843   5436   5329    135    846    975       O  
ATOM   2098  CB  GLU A 232     -12.737  -9.172 -27.967  1.00 44.89           C  
ANISOU 2098  CB  GLU A 232     6655   5342   5059    125   1107   1060       C  
ATOM   2099  CG  GLU A 232     -11.884  -8.288 -28.842  1.00 54.67           C  
ANISOU 2099  CG  GLU A 232     7903   6580   6291     84   1217   1145       C  
ATOM   2100  CD  GLU A 232     -11.470  -8.976 -30.113  1.00 65.68           C  
ANISOU 2100  CD  GLU A 232     9333   8044   7577    130   1291   1143       C  
ATOM   2101  OE1 GLU A 232     -10.559  -9.830 -30.056  1.00 68.34           O  
ANISOU 2101  OE1 GLU A 232     9609   8432   7924    146   1370   1120       O  
ATOM   2102  OE2 GLU A 232     -12.061  -8.665 -31.166  1.00 75.08           O1-
ANISOU 2102  OE2 GLU A 232    10613   9239   8675    154   1270   1162       O1-
ATOM   2103  H   GLU A 232     -11.294 -10.062 -25.978  1.00 40.69           H  
ATOM   2104  N   GLY A 233     -13.711 -10.388 -24.978  1.00 28.38           N  
ANISOU 2104  N   GLY A 233     4422   3222   3139    134    880    878       N  
ATOM   2105  CA  GLY A 233     -14.789 -10.950 -24.182  1.00 37.82           C  
ANISOU 2105  CA  GLY A 233     5625   4406   4337    164    767    812       C  
ATOM   2106  C   GLY A 233     -14.355 -11.120 -22.747  1.00 19.82           C  
ANISOU 2106  C   GLY A 233     3244   2110   2177    137    730    761       C  
ATOM   2107  O   GLY A 233     -13.233 -11.538 -22.467  1.00 37.40           O  
ANISOU 2107  O   GLY A 233     5392   4365   4455    125    785    745       O  
ATOM   2108  H   GLY A 233     -12.961 -10.795 -24.877  1.00 34.87           H  
ATOM   2109  N   VAL A 234     -15.247 -10.746 -21.828  1.00 18.88           N  
ANISOU 2109  N   VAL A 234     3126   1946   2100    132    636    739       N  
ATOM   2110  CA  VAL A 234     -15.009 -10.896 -20.395  1.00 17.65           C  
ANISOU 2110  CA  VAL A 234     2889   1771   2046    113    587    688       C  
ATOM   2111  C   VAL A 234     -16.198 -11.627 -19.796  1.00 19.95           C  
ANISOU 2111  C   VAL A 234     3203   2063   2313    154    494    628       C  
ATOM   2112  O   VAL A 234     -17.320 -11.106 -19.802  1.00 19.43           O  
ANISOU 2112  O   VAL A 234     3190   1970   2222    165    435    643       O  
ATOM   2113  CB  VAL A 234     -14.799  -9.552 -19.682  1.00 17.79           C  
ANISOU 2113  CB  VAL A 234     2880   1724   2156     56    571    722       C  
ATOM   2114  CG1 VAL A 234     -14.449  -9.783 -18.208  1.00 20.94           C  
ANISOU 2114  CG1 VAL A 234     3196   2107   2652     38    521    664       C  
ATOM   2115  CG2 VAL A 234     -13.711  -8.749 -20.369  1.00 27.66           C  
ANISOU 2115  CG2 VAL A 234     4114   2968   3427      4    665    790       C  
ATOM   2116  H   VAL A 234     -16.010 -10.396 -22.016  1.00 23.47           H  
ATOM   2117  N   PHE A 235     -15.961 -12.824 -19.276  1.00 16.93           N  
ANISOU 2117  N   PHE A 235     2781   1711   1939    177    482    565       N  
ATOM   2118  CA  PHE A 235     -17.002 -13.668 -18.703  1.00 20.65           C  
ANISOU 2118  CA  PHE A 235     3271   2186   2388    210    403    507       C  
ATOM   2119  C   PHE A 235     -16.807 -13.710 -17.196  1.00 18.20           C  
ANISOU 2119  C   PHE A 235     2893   1850   2173    196    357    465       C  
ATOM   2120  O   PHE A 235     -15.771 -14.182 -16.719  1.00 31.03           O  
ANISOU 2120  O   PHE A 235     4454   3490   3845    192    387    440       O  
ATOM   2121  CB  PHE A 235     -16.952 -15.055 -19.340  1.00 15.43           C  
ANISOU 2121  CB  PHE A 235     2640   1572   1650    249    424    467       C  
ATOM   2122  CG  PHE A 235     -17.271 -15.027 -20.805  1.00 23.21           C  
ANISOU 2122  CG  PHE A 235     3706   2582   2530    267    458    503       C  
ATOM   2123  CD1 PHE A 235     -16.334 -14.577 -21.723  1.00 38.32           C  
ANISOU 2123  CD1 PHE A 235     5625   4512   4422    259    549    554       C  
ATOM   2124  CD2 PHE A 235     -18.524 -15.390 -21.259  1.00 31.14           C  
ANISOU 2124  CD2 PHE A 235     4780   3595   3455    289    397    490       C  
ATOM   2125  CE1 PHE A 235     -16.637 -14.518 -23.070  1.00 29.21           C  
ANISOU 2125  CE1 PHE A 235     4556   3380   3164    278    581    590       C  
ATOM   2126  CE2 PHE A 235     -18.831 -15.334 -22.606  1.00 23.41           C  
ANISOU 2126  CE2 PHE A 235     3882   2640   2374    307    420    522       C  
ATOM   2127  CZ  PHE A 235     -17.886 -14.897 -23.511  1.00 21.39           C  
ANISOU 2127  CZ  PHE A 235     3640   2397   2089    304    512    572       C  
ATOM   2128  H   PHE A 235     -15.179 -13.180 -19.242  1.00 21.13           H  
ATOM   2129  N   VAL A 236     -17.791 -13.196 -16.454  1.00 23.44           N  
ANISOU 2129  N   VAL A 236     3569   2477   2861    194    285    459       N  
ATOM   2130  CA  VAL A 236     -17.669 -12.959 -15.015  1.00 14.25           C  
ANISOU 2130  CA  VAL A 236     2353   1279   1783    179    241    428       C  
ATOM   2131  C   VAL A 236     -18.542 -13.952 -14.256  1.00 23.41           C  
ANISOU 2131  C   VAL A 236     3518   2449   2929    211    180    371       C  
ATOM   2132  O   VAL A 236     -19.768 -13.978 -14.427  1.00 23.56           O  
ANISOU 2132  O   VAL A 236     3580   2467   2903    230    136    372       O  
ATOM   2133  CB  VAL A 236     -18.048 -11.518 -14.640  1.00 33.27           C  
ANISOU 2133  CB  VAL A 236     4775   3631   4234    154    214    466       C  
ATOM   2134  CG1 VAL A 236     -17.829 -11.285 -13.145  1.00 17.87           C  
ANISOU 2134  CG1 VAL A 236     2778   1644   2367    140    170    430       C  
ATOM   2135  CG2 VAL A 236     -17.250 -10.528 -15.478  1.00 21.90           C  
ANISOU 2135  CG2 VAL A 236     3342   2175   2803    116    278    530       C  
ATOM   2136  H   VAL A 236     -18.558 -12.971 -16.771  1.00 28.95           H  
ATOM   2137  N   TYR A 237     -17.908 -14.733 -13.375  1.00 23.61           N  
ANISOU 2137  N   TYR A 237     3494   2480   2995    217    175    324       N  
ATOM   2138  CA  TYR A 237     -18.565 -15.810 -12.638  1.00 20.12           C  
ANISOU 2138  CA  TYR A 237     3058   2045   2540    245    128    270       C  
ATOM   2139  C   TYR A 237     -18.257 -15.687 -11.154  1.00 11.56           C  
ANISOU 2139  C   TYR A 237     1927    934   1531    240     92    240       C  
ATOM   2140  O   TYR A 237     -17.535 -16.503 -10.581  1.00 18.37           O  
ANISOU 2140  O   TYR A 237     2755   1808   2416    253     98    203       O  
ATOM   2141  CB  TYR A 237     -18.123 -17.155 -13.174  1.00 28.25           C  
ANISOU 2141  CB  TYR A 237     4098   3114   3523    270    162    240       C  
ATOM   2142  CG  TYR A 237     -18.445 -17.302 -14.620  1.00 26.79           C  
ANISOU 2142  CG  TYR A 237     3970   2955   3255    277    194    265       C  
ATOM   2143  CD1 TYR A 237     -19.762 -17.408 -15.035  1.00 19.25           C  
ANISOU 2143  CD1 TYR A 237     3069   2004   2242    283    149    267       C  
ATOM   2144  CD2 TYR A 237     -17.447 -17.309 -15.580  1.00 22.35           C  
ANISOU 2144  CD2 TYR A 237     3405   2418   2670    279    267    289       C  
ATOM   2145  CE1 TYR A 237     -20.076 -17.536 -16.361  1.00 24.87           C  
ANISOU 2145  CE1 TYR A 237     3838   2741   2870    290    169    288       C  
ATOM   2146  CE2 TYR A 237     -17.751 -17.438 -16.913  1.00 28.18           C  
ANISOU 2146  CE2 TYR A 237     4205   3180   3322    290    296    312       C  
ATOM   2147  CZ  TYR A 237     -19.069 -17.549 -17.298  1.00 22.97           C  
ANISOU 2147  CZ  TYR A 237     3606   2521   2602    295    243    309       C  
ATOM   2148  OH  TYR A 237     -19.383 -17.674 -18.628  1.00 29.72           O  
ANISOU 2148  OH  TYR A 237     4527   3400   3364    306    263    330       O  
ATOM   2149  H   TYR A 237     -17.074 -14.653 -13.184  1.00 29.14           H  
ATOM   2150  HH  TYR A 237     -20.216 -17.733 -18.722  1.00 36.48           H  
ATOM   2151  N   LEU A 238     -18.765 -14.642 -10.529  1.00 18.53           N  
ANISOU 2151  N   LEU A 238     2813   1778   2451    226     56    254       N  
ATOM   2152  CA  LEU A 238     -18.584 -14.446  -9.104  1.00 27.89           C  
ANISOU 2152  CA  LEU A 238     3967   2932   3697    224     16    224       C  
ATOM   2153  C   LEU A 238     -19.879 -14.639  -8.337  1.00 27.75           C  
ANISOU 2153  C   LEU A 238     3978   2902   3665    249    -38    202       C  
ATOM   2154  O   LEU A 238     -20.974 -14.293  -8.816  1.00 33.29           O  
ANISOU 2154  O   LEU A 238     4716   3604   4330    258    -52    225       O  
ATOM   2155  CB  LEU A 238     -17.990 -13.070  -8.812  1.00 33.78           C  
ANISOU 2155  CB  LEU A 238     4695   3637   4504    186     17    252       C  
ATOM   2156  CG  LEU A 238     -16.780 -12.684  -9.662  1.00 40.97           C  
ANISOU 2156  CG  LEU A 238     5573   4560   5433    150     76    286       C  
ATOM   2157  CD1 LEU A 238     -16.562 -11.184  -9.580  1.00 46.09           C  
ANISOU 2157  CD1 LEU A 238     6227   5156   6129    106     75    324       C  
ATOM   2158  CD2 LEU A 238     -15.522 -13.417  -9.236  1.00 40.83           C  
ANISOU 2158  CD2 LEU A 238     5487   4573   5454    148     94    255       C  
ATOM   2159  H   LEU A 238     -19.225 -14.025 -10.912  1.00 23.06           H  
ATOM   2160  N   GLN A 239     -19.751 -15.168  -7.126  1.00 27.38           N  
ANISOU 2160  N   GLN A 239     3912   2846   3646    262    -67    160       N  
ATOM   2161  CA  GLN A 239     -20.877 -15.546  -6.288  1.00 26.81           C  
ANISOU 2161  CA  GLN A 239     3861   2767   3560    287   -108    136       C  
ATOM   2162  C   GLN A 239     -21.284 -14.401  -5.370  1.00 11.53           C  
ANISOU 2162  C   GLN A 239     1931    787   1661    288   -141    142       C  
ATOM   2163  O   GLN A 239     -20.439 -13.661  -4.861  1.00 21.87           O  
ANISOU 2163  O   GLN A 239     3223   2066   3020    269   -146    141       O  
ATOM   2164  CB  GLN A 239     -20.512 -16.791  -5.477  1.00 18.18           C  
ANISOU 2164  CB  GLN A 239     2755   1685   2469    305   -116     90       C  
ATOM   2165  CG  GLN A 239     -20.351 -18.003  -6.391  1.00 10.66           C  
ANISOU 2165  CG  GLN A 239     1814    768   1468    313    -86     81       C  
ATOM   2166  CD  GLN A 239     -19.835 -19.235  -5.698  1.00 22.60           C  
ANISOU 2166  CD  GLN A 239     3321   2285   2982    336    -88     40       C  
ATOM   2167  NE2 GLN A 239     -20.419 -20.381  -6.030  1.00 32.78           N  
ANISOU 2167  NE2 GLN A 239     4646   3588   4222    347    -85     23       N  
ATOM   2168  OE1 GLN A 239     -18.914 -19.171  -4.887  1.00 45.79           O  
ANISOU 2168  OE1 GLN A 239     6224   5212   5962    343    -95     24       O  
ATOM   2169  H   GLN A 239     -18.991 -15.322  -6.753  1.00 33.68           H  
ATOM   2170 HE21 GLN A 239     -21.053 -20.388  -6.611  1.00 40.16           H  
ATOM   2171 HE22 GLN A 239     -20.163 -21.116  -5.665  1.00 40.16           H  
ATOM   2172  N   GLY A 240     -22.597 -14.243  -5.205  1.00 20.23           N  
ANISOU 2172  N   GLY A 240     3033   1916   2737    296   -153    145       N  
ATOM   2173  CA  GLY A 240     -23.145 -13.178  -4.394  1.00 24.00           C  
ANISOU 2173  CA  GLY A 240     3494   2389   3236    293   -164    146       C  
ATOM   2174  C   GLY A 240     -24.415 -13.551  -3.656  1.00 11.03           C  
ANISOU 2174  C   GLY A 240     1835    785   1569    308   -175    128       C  
ATOM   2175  O   GLY A 240     -24.710 -14.733  -3.456  1.00 24.95           O  
ANISOU 2175  O   GLY A 240     3594   2577   3309    313   -177    106       O  
ATOM   2176  H   GLY A 240     -23.193 -14.751  -5.560  1.00 25.10           H  
ATOM   2177  N   SER A 241     -25.185 -12.513  -3.296  1.00 15.09           N  
ANISOU 2177  N   SER A 241     2348   1297   2090    318   -179    141       N  
ATOM   2178  CA  SER A 241     -26.311 -12.568  -2.367  1.00 28.70           C  
ANISOU 2178  CA  SER A 241     4056   3047   3801    335   -185    128       C  
ATOM   2179  C   SER A 241     -27.634 -12.197  -3.020  1.00 21.53           C  
ANISOU 2179  C   SER A 241     3155   2156   2871    359   -192    158       C  
ATOM   2180  O   SER A 241     -28.643 -12.038  -2.318  1.00 14.48           O  
ANISOU 2180  O   SER A 241     2249   1279   1972    380   -195    155       O  
ATOM   2181  CB  SER A 241     -26.060 -11.618  -1.193  1.00 11.97           C  
ANISOU 2181  CB  SER A 241     1933    907   1708    335   -183    113       C  
ATOM   2182  OG  SER A 241     -26.095 -10.266  -1.640  1.00 45.09           O  
ANISOU 2182  OG  SER A 241     6145   5068   5918    339   -181    141       O  
ATOM   2183  H   SER A 241     -25.062 -11.717  -3.597  1.00 18.93           H  
ATOM   2184  HG  SER A 241     -25.511 -10.143  -2.231  1.00 54.92           H  
ATOM   2185  N   LYS A 242     -27.643 -11.970  -4.316  1.00 24.99           N  
ANISOU 2185  N   LYS A 242     3614   2589   3293    361   -195    192       N  
ATOM   2186  CA  LYS A 242     -28.776 -11.275  -4.888  1.00 24.63           C  
ANISOU 2186  CA  LYS A 242     3574   2555   3229    389   -206    227       C  
ATOM   2187  C   LYS A 242     -29.563 -12.169  -5.831  1.00 22.89           C  
ANISOU 2187  C   LYS A 242     3362   2370   2965    400   -225    242       C  
ATOM   2188  O   LYS A 242     -28.995 -13.023  -6.523  1.00 30.76           O  
ANISOU 2188  O   LYS A 242     4380   3367   3940    384   -226    239       O  
ATOM   2189  CB  LYS A 242     -28.338 -10.026  -5.656  1.00 36.71           C  
ANISOU 2189  CB  LYS A 242     5129   4051   4770    387   -198    263       C  
ATOM   2190  CG  LYS A 242     -27.517  -9.072  -4.832  1.00 50.15           C  
ANISOU 2190  CG  LYS A 242     6831   5707   6515    372   -185    251       C  
ATOM   2191  CD  LYS A 242     -28.383  -8.089  -4.080  1.00 62.16           C  
ANISOU 2191  CD  LYS A 242     8348   7223   8046    399   -188    252       C  
ATOM   2192  CE  LYS A 242     -27.700  -7.671  -2.797  1.00 66.44           C  
ANISOU 2192  CE  LYS A 242     8888   7735   8620    385   -181    217       C  
ATOM   2193  NZ  LYS A 242     -28.499  -8.098  -1.621  1.00 69.83           N1+
ANISOU 2193  NZ  LYS A 242     9297   8195   9041    406   -184    188       N1+
ATOM   2194  H   LYS A 242     -27.025 -12.199  -4.869  1.00 30.81           H  
ATOM   2195  HZ1 LYS A 242     -28.094  -7.846  -0.870  1.00 84.62           H  
ATOM   2196  HZ2 LYS A 242     -29.308  -7.728  -1.652  1.00 84.62           H  
ATOM   2197  HZ3 LYS A 242     -28.587  -8.984  -1.618  1.00 84.62           H  
ATOM   2198  N   PRO A 243     -30.872 -11.963  -5.891  1.00 12.73           N  
ANISOU 2198  N   PRO A 243     2063   1112   1662    432   -243    261       N  
ATOM   2199  CA  PRO A 243     -31.718 -12.767  -6.780  1.00 10.25           C  
ANISOU 2199  CA  PRO A 243     1755    837   1303    443   -273    279       C  
ATOM   2200  C   PRO A 243     -31.272 -12.650  -8.227  1.00 20.58           C  
ANISOU 2200  C   PRO A 243     3102   2143   2575    436   -279    310       C  
ATOM   2201  O   PRO A 243     -31.044 -11.552  -8.743  1.00 24.67           O  
ANISOU 2201  O   PRO A 243     3633   2643   3096    443   -267    341       O  
ATOM   2202  CB  PRO A 243     -33.121 -12.186  -6.572  1.00 10.69           C  
ANISOU 2202  CB  PRO A 243     1779    924   1357    485   -291    303       C  
ATOM   2203  CG  PRO A 243     -32.950 -10.934  -5.787  1.00 16.82           C  
ANISOU 2203  CG  PRO A 243     2547   1670   2173    496   -265    302       C  
ATOM   2204  CD  PRO A 243     -31.628 -10.959  -5.122  1.00 11.09           C  
ANISOU 2204  CD  PRO A 243     1833    903   1476    460   -239    268       C  
ATOM   2205  N   ILE A 244     -31.152 -13.799  -8.883  1.00 14.66           N  
ANISOU 2205  N   ILE A 244     2378   1407   1784    421   -295    303       N  
ATOM   2206  CA  ILE A 244     -30.736 -13.877 -10.280  1.00 20.19           C  
ANISOU 2206  CA  ILE A 244     3113   2122   2438    405   -291    324       C  
ATOM   2207  C   ILE A 244     -31.965 -13.604 -11.138  1.00 25.95           C  
ANISOU 2207  C   ILE A 244     3836   2902   3122    427   -330    359       C  
ATOM   2208  O   ILE A 244     -32.809 -14.483 -11.339  1.00 19.89           O  
ANISOU 2208  O   ILE A 244     3044   2188   2327    412   -361    344       O  
ATOM   2209  CB  ILE A 244     -30.088 -15.227 -10.597  1.00 22.42           C  
ANISOU 2209  CB  ILE A 244     3403   2419   2696    362   -276    285       C  
ATOM   2210  CG1 ILE A 244     -28.816 -15.376  -9.757  1.00 15.11           C  
ANISOU 2210  CG1 ILE A 244     2478   1447   1818    351   -240    256       C  
ATOM   2211  CG2 ILE A 244     -29.738 -15.325 -12.057  1.00 11.00           C  
ANISOU 2211  CG2 ILE A 244     1993    993   1192    349   -267    304       C  
ATOM   2212  CD1 ILE A 244     -28.326 -16.795  -9.592  1.00 21.35           C  
ANISOU 2212  CD1 ILE A 244     3270   2246   2597    324   -229    210       C  
ATOM   2213  H   ILE A 244     -31.310 -14.569  -8.532  1.00 18.41           H  
ATOM   2214  N   THR A 245     -32.069 -12.371 -11.653  1.00 24.17           N  
ANISOU 2214  N   THR A 245     3629   2663   2892    458   -329    405       N  
ATOM   2215  CA  THR A 245     -33.260 -11.901 -12.346  1.00 14.45           C  
ANISOU 2215  CA  THR A 245     2384   1481   1627    490   -367    441       C  
ATOM   2216  C   THR A 245     -32.998 -11.185 -13.665  1.00 27.08           C  
ANISOU 2216  C   THR A 245     4027   3081   3183    496   -360    485       C  
ATOM   2217  O   THR A 245     -33.967 -10.841 -14.354  1.00 20.18           O  
ANISOU 2217  O   THR A 245     3142   2253   2273    523   -396    515       O  
ATOM   2218  CB  THR A 245     -34.043 -10.937 -11.441  1.00 25.20           C  
ANISOU 2218  CB  THR A 245     3696   2841   3038    525   -364    449       C  
ATOM   2219  CG2 THR A 245     -34.477 -11.642 -10.171  1.00 31.95           C  
ANISOU 2219  CG2 THR A 245     4509   3705   3927    524   -369    412       C  
ATOM   2220  OG1 THR A 245     -33.207  -9.818 -11.105  1.00 25.38           O  
ANISOU 2220  OG1 THR A 245     3737   2804   3104    521   -322    454       O  
ATOM   2221  H   THR A 245     -31.445 -11.781 -11.609  1.00 29.82           H  
ATOM   2222  HG1 THR A 245     -33.626  -9.285 -10.610  1.00 31.28           H  
ATOM   2223  N   ASP A 246     -31.743 -10.933 -14.035  1.00 42.57           N  
ANISOU 2223  N   ASP A 246     6033   4997   5145    473   -316    492       N  
ATOM   2224  CA  ASP A 246     -31.487 -10.081 -15.194  1.00 44.81           C  
ANISOU 2224  CA  ASP A 246     6359   5275   5393    480   -301    539       C  
ATOM   2225  C   ASP A 246     -32.011 -10.715 -16.481  1.00 31.54           C  
ANISOU 2225  C   ASP A 246     4708   3653   3623    485   -335    555       C  
ATOM   2226  O   ASP A 246     -32.470  -9.998 -17.379  1.00 27.59           O  
ANISOU 2226  O   ASP A 246     4223   3173   3087    507   -348    595       O  
ATOM   2227  CB  ASP A 246     -29.987  -9.779 -15.296  1.00 62.93           C  
ANISOU 2227  CB  ASP A 246     8691   7511   7707    449   -242    545       C  
ATOM   2228  CG  ASP A 246     -29.530  -8.686 -14.320  1.00 68.80           C  
ANISOU 2228  CG  ASP A 246     9414   8196   8531    444   -216    544       C  
ATOM   2229  OD1 ASP A 246     -30.378  -8.110 -13.602  1.00 70.94           O  
ANISOU 2229  OD1 ASP A 246     9649   8470   8835    469   -238    539       O  
ATOM   2230  OD2 ASP A 246     -28.313  -8.402 -14.273  1.00 71.90           O1-
ANISOU 2230  OD2 ASP A 246     9827   8541   8950    413   -173    549       O1-
ATOM   2231  H   ASP A 246     -31.040 -11.234 -13.642  1.00 51.91           H  
ATOM   2232  N   PHE A 247     -31.992 -12.047 -16.573  1.00 31.84           N  
ANISOU 2232  N   PHE A 247     4751   3721   3627    460   -353    518       N  
ATOM   2233  CA  PHE A 247     -32.489 -12.742 -17.758  1.00 34.40           C  
ANISOU 2233  CA  PHE A 247     5098   4105   3867    451   -389    516       C  
ATOM   2234  C   PHE A 247     -33.983 -12.530 -17.979  1.00 36.88           C  
ANISOU 2234  C   PHE A 247     5380   4477   4154    485   -463    538       C  
ATOM   2235  O   PHE A 247     -34.483 -12.803 -19.078  1.00 38.05           O  
ANISOU 2235  O   PHE A 247     5550   4677   4229    484   -502    548       O  
ATOM   2236  CB  PHE A 247     -32.173 -14.239 -17.635  1.00 32.46           C  
ANISOU 2236  CB  PHE A 247     4844   3878   3610    400   -384    453       C  
ATOM   2237  CG  PHE A 247     -33.099 -14.990 -16.710  1.00 28.08           C  
ANISOU 2237  CG  PHE A 247     4227   3353   3090    385   -426    413       C  
ATOM   2238  CD1 PHE A 247     -32.827 -15.089 -15.353  1.00 23.56           C  
ANISOU 2238  CD1 PHE A 247     3613   2744   2593    379   -401    387       C  
ATOM   2239  CD2 PHE A 247     -34.240 -15.606 -17.203  1.00 23.44           C  
ANISOU 2239  CD2 PHE A 247     3620   2829   2456    373   -491    404       C  
ATOM   2240  CE1 PHE A 247     -33.680 -15.783 -14.504  1.00 34.06           C  
ANISOU 2240  CE1 PHE A 247     4890   4100   3951    364   -432    356       C  
ATOM   2241  CE2 PHE A 247     -35.098 -16.300 -16.362  1.00 23.11           C  
ANISOU 2241  CE2 PHE A 247     3516   2815   2449    351   -524    373       C  
ATOM   2242  CZ  PHE A 247     -34.818 -16.390 -15.012  1.00 24.12           C  
ANISOU 2242  CZ  PHE A 247     3608   2905   2651    348   -490    350       C  
ATOM   2243  H   PHE A 247     -31.694 -12.572 -15.961  1.00 39.03           H  
ATOM   2244  N   VAL A 248     -34.702 -12.052 -16.962  1.00 36.94           N  
ANISOU 2244  N   VAL A 248     5323   4485   4226    509   -476    539       N  
ATOM   2245  CA  VAL A 248     -36.126 -11.767 -17.094  1.00 39.18           C  
ANISOU 2245  CA  VAL A 248     5553   4833   4502    541   -534    558       C  
ATOM   2246  C   VAL A 248     -36.364 -10.424 -17.758  1.00 42.12           C  
ANISOU 2246  C   VAL A 248     5934   5200   4868    580   -526    610       C  
ATOM   2247  O   VAL A 248     -37.475 -10.158 -18.235  1.00 40.21           O  
ANISOU 2247  O   VAL A 248     5658   5017   4602    609   -576    635       O  
ATOM   2248  CB  VAL A 248     -36.782 -11.800 -15.704  1.00 35.34           C  
ANISOU 2248  CB  VAL A 248     4994   4348   4084    556   -541    540       C  
ATOM   2249  CG1 VAL A 248     -38.259 -11.489 -15.784  1.00 36.90           C  
ANISOU 2249  CG1 VAL A 248     5124   4618   4280    594   -595    564       C  
ATOM   2250  CG2 VAL A 248     -36.550 -13.148 -15.055  1.00 34.00           C  
ANISOU 2250  CG2 VAL A 248     4810   4181   3927    505   -541    485       C  
ATOM   2251  H   VAL A 248     -34.385 -11.883 -16.181  1.00 45.14           H  
ATOM   2252  N   ALA A 249     -35.346  -9.569 -17.781  1.00 42.01           N  
ANISOU 2252  N   ALA A 249     5964   5118   4878    579   -466    628       N  
ATOM   2253  CA  ALA A 249     -35.379  -8.324 -18.536  1.00 36.25           C  
ANISOU 2253  CA  ALA A 249     5265   4372   4136    608   -455    678       C  
ATOM   2254  C   ALA A 249     -36.582  -7.460 -18.162  1.00 35.77           C  
ANISOU 2254  C   ALA A 249     5152   4332   4107    657   -487    701       C  
ATOM   2255  O   ALA A 249     -37.189  -6.810 -19.016  1.00 35.14           O  
ANISOU 2255  O   ALA A 249     5083   4278   3992    689   -514    741       O  
ATOM   2256  CB  ALA A 249     -35.360  -8.611 -20.039  1.00 33.83           C  
ANISOU 2256  CB  ALA A 249     5010   4106   3739    602   -475    701       C  
ATOM   2257  H   ALA A 249     -34.609  -9.691 -17.356  1.00 51.22           H  
ATOM   2258  N   GLY A 250     -36.929  -7.452 -16.873  1.00 41.88           N  
ANISOU 2258  N   GLY A 250     5872   5095   4946    666   -482    676       N  
ATOM   2259  CA  GLY A 250     -37.921  -6.532 -16.346  1.00 38.17           C  
ANISOU 2259  CA  GLY A 250     5359   4630   4515    716   -497    694       C  
ATOM   2260  C   GLY A 250     -39.359  -6.844 -16.688  1.00 36.23           C  
ANISOU 2260  C   GLY A 250     5053   4472   4241    749   -563    708       C  
ATOM   2261  O   GLY A 250     -40.222  -5.971 -16.559  1.00 45.65           O  
ANISOU 2261  O   GLY A 250     6218   5674   5453    798   -579    733       O  
ATOM   2262  H   GLY A 250     -36.595  -7.979 -16.281  1.00 51.08           H  
ATOM   2263  N   GLN A 251     -39.646  -8.074 -17.101  1.00 34.14           N  
ANISOU 2263  N   GLN A 251     4767   4272   3932    720   -605    691       N  
ATOM   2264  CA  GLN A 251     -40.975  -8.438 -17.565  1.00 27.29           C  
ANISOU 2264  CA  GLN A 251     3838   3497   3033    739   -678    704       C  
ATOM   2265  C   GLN A 251     -41.914  -8.824 -16.432  1.00 30.76           C  
ANISOU 2265  C   GLN A 251     4187   3977   3523    753   -697    685       C  
ATOM   2266  O   GLN A 251     -43.136  -8.765 -16.619  1.00 21.12           O  
ANISOU 2266  O   GLN A 251     2900   2826   2298    781   -751    703       O  
ATOM   2267  CB  GLN A 251     -40.864  -9.583 -18.575  1.00 25.04           C  
ANISOU 2267  CB  GLN A 251     3576   3267   2672    694   -721    689       C  
ATOM   2268  CG  GLN A 251     -40.151  -9.186 -19.864  1.00 30.69           C  
ANISOU 2268  CG  GLN A 251     4377   3959   3325    689   -708    715       C  
ATOM   2269  CD  GLN A 251     -40.034 -10.333 -20.844  1.00 37.82           C  
ANISOU 2269  CD  GLN A 251     5311   4911   4146    644   -747    692       C  
ATOM   2270  NE2 GLN A 251     -38.884 -10.995 -20.844  1.00 50.56           N  
ANISOU 2270  NE2 GLN A 251     6986   6481   5745    602   -704    659       N  
ATOM   2271  OE1 GLN A 251     -40.967 -10.624 -21.592  1.00 35.25           O  
ANISOU 2271  OE1 GLN A 251     4958   4664   3772    645   -817    700       O  
ATOM   2272  H   GLN A 251     -39.080  -8.721 -17.123  1.00 41.78           H  
ATOM   2273 HE21 GLN A 251     -38.255 -10.765 -20.305  1.00 61.50           H  
ATOM   2274 HE22 GLN A 251     -38.767 -11.656 -21.382  1.00 61.50           H  
ATOM   2275  N   VAL A 252     -41.382  -9.201 -15.270  1.00 37.34           N  
ANISOU 2275  N   VAL A 252     5015   4768   4404    735   -654    650       N  
ATOM   2276  CA  VAL A 252     -42.184  -9.365 -14.063  1.00 38.82           C  
ANISOU 2276  CA  VAL A 252     5125   4980   4645    756   -654    635       C  
ATOM   2277  C   VAL A 252     -41.777  -8.292 -13.057  1.00 27.40           C  
ANISOU 2277  C   VAL A 252     3700   3453   3259    786   -590    632       C  
ATOM   2278  O   VAL A 252     -40.636  -7.809 -13.051  1.00 26.81           O  
ANISOU 2278  O   VAL A 252     3694   3301   3193    768   -544    625       O  
ATOM   2279  CB  VAL A 252     -42.064 -10.776 -13.443  1.00 34.30           C  
ANISOU 2279  CB  VAL A 252     4526   4434   4073    711   -664    594       C  
ATOM   2280  CG1 VAL A 252     -42.262 -11.849 -14.510  1.00 21.47           C  
ANISOU 2280  CG1 VAL A 252     2903   2875   2379    666   -730    585       C  
ATOM   2281  CG2 VAL A 252     -40.739 -10.964 -12.737  1.00 15.45           C  
ANISOU 2281  CG2 VAL A 252     2200   1959   1712    681   -603    560       C  
ATOM   2282  H   VAL A 252     -40.546  -9.369 -15.156  1.00 45.63           H  
ATOM   2283  N   GLU A 253     -42.736  -7.901 -12.217  1.00 31.09           N  
ANISOU 2283  N   GLU A 253     4105   3940   3766    831   -590    634       N  
ATOM   2284  CA  GLU A 253     -42.497  -6.863 -11.225  1.00 32.85           C  
ANISOU 2284  CA  GLU A 253     4351   4092   4039    862   -536    625       C  
ATOM   2285  C   GLU A 253     -41.595  -7.357 -10.105  1.00 31.97           C  
ANISOU 2285  C   GLU A 253     4258   3928   3960    824   -488    581       C  
ATOM   2286  O   GLU A 253     -41.698  -8.498  -9.648  1.00 29.32           O  
ANISOU 2286  O   GLU A 253     3887   3628   3626    799   -496    559       O  
ATOM   2287  CB  GLU A 253     -43.814  -6.360 -10.634  1.00 51.36           C  
ANISOU 2287  CB  GLU A 253     6628   6478   6409    926   -545    636       C  
ATOM   2288  CG  GLU A 253     -44.342  -5.122 -11.336  1.00 75.03           C  
ANISOU 2288  CG  GLU A 253     9643   9471   9395    982   -561    674       C  
ATOM   2289  CD  GLU A 253     -45.655  -4.625 -10.772  1.00 96.22           C  
ANISOU 2289  CD  GLU A 253    12260  12198  12101   1054   -567    684       C  
ATOM   2290  OE1 GLU A 253     -45.732  -4.342  -9.559  1.00102.13           O  
ANISOU 2290  OE1 GLU A 253    13001  12917  12887   1076   -523    661       O  
ATOM   2291  OE2 GLU A 253     -46.614  -4.512 -11.558  1.00104.49           O1-
ANISOU 2291  OE2 GLU A 253    13262  13312  13126   1089   -617    716       O1-
ATOM   2292  H   GLU A 253     -43.533  -8.224 -12.203  1.00 38.12           H  
ATOM   2293  N   MET A 254     -40.720  -6.477  -9.656  1.00 30.79           N  
ANISOU 2293  N   MET A 254     4165   3696   3838    820   -442    570       N  
ATOM   2294  CA  MET A 254     -39.820  -6.776  -8.561  1.00 28.68           C  
ANISOU 2294  CA  MET A 254     3918   3376   3604    784   -400    527       C  
ATOM   2295  C   MET A 254     -40.178  -5.910  -7.364  1.00 28.17           C  
ANISOU 2295  C   MET A 254     3847   3278   3577    822   -370    512       C  
ATOM   2296  O   MET A 254     -40.634  -4.772  -7.503  1.00 30.00           O  
ANISOU 2296  O   MET A 254     4091   3495   3812    867   -370    534       O  
ATOM   2297  CB  MET A 254     -38.366  -6.543  -8.934  1.00 48.68           C  
ANISOU 2297  CB  MET A 254     6519   5843   6136    737   -374    518       C  
ATOM   2298  CG  MET A 254     -37.994  -7.190 -10.224  1.00 48.11           C  
ANISOU 2298  CG  MET A 254     6468   5796   6016    709   -397    536       C  
ATOM   2299  SD  MET A 254     -37.863  -8.959  -9.992  1.00 59.41           S  
ANISOU 2299  SD  MET A 254     7875   7268   7430    669   -413    502       S  
ATOM   2300  CE  MET A 254     -36.925  -9.390 -11.440  1.00 66.20           C  
ANISOU 2300  CE  MET A 254     8795   8123   8235    629   -423    514       C  
ATOM   2301  H   MET A 254     -40.627  -5.685  -9.978  1.00 37.77           H  
ATOM   2302  N   LYS A 255     -40.008  -6.503  -6.194  1.00 28.93           N  
ANISOU 2302  N   LYS A 255     3929   3367   3697    806   -346    475       N  
ATOM   2303  CA  LYS A 255     -40.095  -5.783  -4.945  1.00 23.23           C  
ANISOU 2303  CA  LYS A 255     3215   2606   3004    831   -313    452       C  
ATOM   2304  C   LYS A 255     -38.964  -4.767  -4.837  1.00 28.08           C  
ANISOU 2304  C   LYS A 255     3896   3140   3634    808   -289    440       C  
ATOM   2305  O   LYS A 255     -37.937  -4.894  -5.509  1.00 33.94           O  
ANISOU 2305  O   LYS A 255     4670   3855   4370    761   -289    442       O  
ATOM   2306  CB  LYS A 255     -40.023  -6.766  -3.782  1.00 34.25           C  
ANISOU 2306  CB  LYS A 255     4588   4012   4414    812   -293    414       C  
ATOM   2307  CG  LYS A 255     -41.225  -7.691  -3.680  1.00 33.31           C  
ANISOU 2307  CG  LYS A 255     4398   3974   4286    841   -311    427       C  
ATOM   2308  CD  LYS A 255     -41.120  -8.605  -2.469  1.00 26.78           C  
ANISOU 2308  CD  LYS A 255     3558   3148   3471    826   -286    393       C  
ATOM   2309  CE  LYS A 255     -40.164  -9.758  -2.721  1.00 38.32           C  
ANISOU 2309  CE  LYS A 255     5039   4597   4923    764   -293    374       C  
ATOM   2310  NZ  LYS A 255     -39.494 -10.197  -1.464  1.00 41.98           N1+
ANISOU 2310  NZ  LYS A 255     5527   5021   5401    738   -259    332       N1+
ATOM   2311  H   LYS A 255     -39.838  -7.340  -6.098  1.00 35.54           H  
ATOM   2312  HZ1 LYS A 255     -38.940 -10.872  -1.635  1.00 51.19           H  
ATOM   2313  HZ2 LYS A 255     -39.029  -9.523  -1.116  1.00 51.19           H  
ATOM   2314  HZ3 LYS A 255     -40.102 -10.465  -0.872  1.00 51.19           H  
ATOM   2315  N   PRO A 256     -39.169  -3.692  -4.074  1.00 35.54           N  
ANISOU 2315  N   PRO A 256     4862   4046   4594    843   -270    432       N  
ATOM   2316  CA  PRO A 256     -38.088  -2.705  -3.934  1.00 30.19           C  
ANISOU 2316  CA  PRO A 256     4246   3292   3932    818   -253    422       C  
ATOM   2317  C   PRO A 256     -36.763  -3.344  -3.547  1.00 29.67           C  
ANISOU 2317  C   PRO A 256     4196   3198   3881    748   -238    387       C  
ATOM   2318  O   PRO A 256     -35.705  -2.886  -3.987  1.00 32.95           O  
ANISOU 2318  O   PRO A 256     4650   3566   4304    712   -233    391       O  
ATOM   2319  CB  PRO A 256     -38.610  -1.757  -2.840  1.00 31.12           C  
ANISOU 2319  CB  PRO A 256     4381   3383   4062    867   -235    406       C  
ATOM   2320  CG  PRO A 256     -40.088  -1.972  -2.803  1.00 38.65           C  
ANISOU 2320  CG  PRO A 256     5283   4402   5002    931   -244    424       C  
ATOM   2321  CD  PRO A 256     -40.311  -3.407  -3.188  1.00 35.44           C  
ANISOU 2321  CD  PRO A 256     4820   4059   4586    905   -261    428       C  
ATOM   2322  N   ASP A 257     -36.801  -4.381  -2.695  1.00 40.54           N  
ANISOU 2322  N   ASP A 257     5542   4602   5261    732   -231    355       N  
ATOM   2323  CA  ASP A 257     -35.607  -5.124  -2.278  1.00 26.90           C  
ANISOU 2323  CA  ASP A 257     3822   2855   3543    672   -219    321       C  
ATOM   2324  C   ASP A 257     -34.933  -5.875  -3.424  1.00 30.51           C  
ANISOU 2324  C   ASP A 257     4280   3324   3987    632   -230    335       C  
ATOM   2325  O   ASP A 257     -33.837  -6.417  -3.209  1.00 28.70           O  
ANISOU 2325  O   ASP A 257     4060   3076   3767    585   -220    309       O  
ATOM   2326  CB  ASP A 257     -35.907  -6.015  -1.070  1.00 30.87           C  
ANISOU 2326  CB  ASP A 257     4298   3383   4048    672   -208    287       C  
ATOM   2327  CG  ASP A 257     -36.806  -7.198  -1.371  1.00 30.70           C  
ANISOU 2327  CG  ASP A 257     4232   3424   4009    686   -221    299       C  
ATOM   2328  OD1 ASP A 257     -36.592  -7.890  -2.390  1.00 36.80           O  
ANISOU 2328  OD1 ASP A 257     4997   4217   4768    662   -239    315       O  
ATOM   2329  OD2 ASP A 257     -37.714  -7.472  -0.554  1.00 29.41           O1-
ANISOU 2329  OD2 ASP A 257     4041   3288   3844    721   -214    293       O1-
ATOM   2330  H   ASP A 257     -37.524  -4.679  -2.337  1.00 49.47           H  
ATOM   2331  N   GLY A 258     -35.587  -6.008  -4.574  1.00 34.97           N  
ANISOU 2331  N   GLY A 258     4834   3924   4528    652   -252    373       N  
ATOM   2332  CA  GLY A 258     -35.000  -6.637  -5.736  1.00 25.77           C  
ANISOU 2332  CA  GLY A 258     3681   2771   3341    620   -263    388       C  
ATOM   2333  C   GLY A 258     -35.445  -8.053  -6.001  1.00 28.52           C  
ANISOU 2333  C   GLY A 258     3999   3175   3663    613   -283    383       C  
ATOM   2334  O   GLY A 258     -35.082  -8.613  -7.045  1.00 39.69           O  
ANISOU 2334  O   GLY A 258     5429   4603   5048    592   -297    397       O  
ATOM   2335  H   GLY A 258     -36.391  -5.732  -4.702  1.00 42.78           H  
ATOM   2336  N   GLY A 259     -36.197  -8.649  -5.092  1.00 25.90           N  
ANISOU 2336  N   GLY A 259     3630   2872   3338    630   -284    366       N  
ATOM   2337  CA  GLY A 259     -36.744  -9.958  -5.345  1.00 26.35           C  
ANISOU 2337  CA  GLY A 259     3659   2982   3372    626   -309    366       C  
ATOM   2338  C   GLY A 259     -38.000  -9.895  -6.188  1.00 31.98           C  
ANISOU 2338  C   GLY A 259     4336   3758   4058    666   -347    407       C  
ATOM   2339  O   GLY A 259     -38.637  -8.846  -6.308  1.00 26.86           O  
ANISOU 2339  O   GLY A 259     3677   3114   3416    707   -349    432       O  
ATOM   2340  H   GLY A 259     -36.402  -8.315  -4.326  1.00 31.90           H  
ATOM   2341  N   VAL A 260     -38.346 -11.036  -6.784  1.00 30.51           N  
ANISOU 2341  N   VAL A 260     4132   3621   3838    653   -383    412       N  
ATOM   2342  CA  VAL A 260     -39.555 -11.138  -7.595  1.00 28.96           C  
ANISOU 2342  CA  VAL A 260     3889   3502   3612    683   -432    448       C  
ATOM   2343  C   VAL A 260     -40.790 -11.053  -6.703  1.00 22.78           C  
ANISOU 2343  C   VAL A 260     3035   2766   2853    729   -432    456       C  
ATOM   2344  O   VAL A 260     -40.952 -11.852  -5.770  1.00 23.23           O  
ANISOU 2344  O   VAL A 260     3068   2835   2924    725   -420    434       O  
ATOM   2345  CB  VAL A 260     -39.570 -12.447  -8.390  1.00 21.00           C  
ANISOU 2345  CB  VAL A 260     2882   2539   2557    647   -482    443       C  
ATOM   2346  CG1 VAL A 260     -40.903 -12.603  -9.123  1.00 24.40           C  
ANISOU 2346  CG1 VAL A 260     3242   3067   2961    658   -535    471       C  
ATOM   2347  CG2 VAL A 260     -38.408 -12.524  -9.359  1.00 21.28           C  
ANISOU 2347  CG2 VAL A 260     2991   2533   2563    607   -479    437       C  
ATOM   2348  H   VAL A 260     -37.896 -11.768  -6.732  1.00 37.43           H  
ATOM   2349  N   TRP A 261     -41.683 -10.118  -7.021  1.00 27.70           N  
ANISOU 2349  N   TRP A 261     3626   3420   3479    777   -444    488       N  
ATOM   2350  CA  TRP A 261     -42.971 -10.022  -6.344  1.00 36.31           C  
ANISOU 2350  CA  TRP A 261     4640   4569   4589    827   -445    499       C  
ATOM   2351  C   TRP A 261     -43.888 -11.191  -6.708  1.00 26.90           C  
ANISOU 2351  C   TRP A 261     3363   3482   3374    817   -494    514       C  
ATOM   2352  O   TRP A 261     -43.987 -11.578  -7.875  1.00 27.26           O  
ANISOU 2352  O   TRP A 261     3402   3573   3381    792   -548    530       O  
ATOM   2353  CB  TRP A 261     -43.650  -8.697  -6.719  1.00 34.91           C  
ANISOU 2353  CB  TRP A 261     4455   4395   4416    882   -450    528       C  
ATOM   2354  CG  TRP A 261     -44.963  -8.563  -6.070  1.00 35.26           C  
ANISOU 2354  CG  TRP A 261     4418   4501   4477    939   -447    539       C  
ATOM   2355  CD1 TRP A 261     -45.216  -7.984  -4.868  1.00 25.45           C  
ANISOU 2355  CD1 TRP A 261     3176   3230   3263    980   -398    524       C  
ATOM   2356  CD2 TRP A 261     -46.219  -9.059  -6.555  1.00 39.71           C  
ANISOU 2356  CD2 TRP A 261     4882   5175   5030    958   -493    567       C  
ATOM   2357  CE2 TRP A 261     -47.192  -8.735  -5.589  1.00 40.58           C  
ANISOU 2357  CE2 TRP A 261     4930   5320   5167   1015   -461    570       C  
ATOM   2358  CE3 TRP A 261     -46.616  -9.743  -7.711  1.00 32.33           C  
ANISOU 2358  CE3 TRP A 261     3903   4318   4062    928   -559    587       C  
ATOM   2359  NE1 TRP A 261     -46.554  -8.079  -4.569  1.00 33.02           N  
ANISOU 2359  NE1 TRP A 261     4042   4274   4230   1031   -402    543       N  
ATOM   2360  CZ2 TRP A 261     -48.540  -9.069  -5.742  1.00 31.21           C  
ANISOU 2360  CZ2 TRP A 261     3626   4247   3984   1042   -489    596       C  
ATOM   2361  CZ3 TRP A 261     -47.956 -10.073  -7.864  1.00 35.94           C  
ANISOU 2361  CZ3 TRP A 261     4246   4887   4522    947   -596    609       C  
ATOM   2362  CH2 TRP A 261     -48.901  -9.735  -6.884  1.00 36.67           C  
ANISOU 2362  CH2 TRP A 261     4267   5015   4650   1003   -558    615       C  
ATOM   2363  H   TRP A 261     -41.566  -9.524  -7.631  1.00 34.06           H  
ATOM   2364  HE1 TRP A 261     -46.930  -7.775  -3.858  1.00 40.44           H  
ATOM   2365  N   VAL A 262     -44.589 -11.741  -5.707  1.00 24.53           N  
ANISOU 2365  N   VAL A 262     2994   3230   3096    834   -476    510       N  
ATOM   2366  CA  VAL A 262     -45.563 -12.805  -5.934  1.00 15.96           C  
ANISOU 2366  CA  VAL A 262     1808   2251   2006    788   -510    517       C  
ATOM   2367  C   VAL A 262     -46.743 -12.630  -4.985  1.00 20.77           C  
ANISOU 2367  C   VAL A 262     2319   2925   2648    845   -483    538       C  
ATOM   2368  O   VAL A 262     -46.638 -11.985  -3.939  1.00 31.77           O  
ANISOU 2368  O   VAL A 262     3738   4269   4063    906   -427    532       O  
ATOM   2369  CB  VAL A 262     -44.985 -14.233  -5.749  1.00 25.33           C  
ANISOU 2369  CB  VAL A 262     3013   3418   3192    671   -500    469       C  
ATOM   2370  CG1 VAL A 262     -43.759 -14.451  -6.620  1.00 17.83           C  
ANISOU 2370  CG1 VAL A 262     2159   2404   2210    622   -517    446       C  
ATOM   2371  CG2 VAL A 262     -44.673 -14.510  -4.276  1.00 17.03           C  
ANISOU 2371  CG2 VAL A 262     1977   2319   2173    672   -434    443       C  
ATOM   2372  H   VAL A 262     -44.512 -11.510  -4.882  1.00 30.25           H  
ATOM   2373  N   ASP A 263     -47.879 -13.221  -5.366  1.00 24.16           N  
ANISOU 2373  N   ASP A 263     2635   3464   3079    813   -520    555       N  
ATOM   2374  CA  ASP A 263     -49.065 -13.267  -4.522  1.00 23.87           C  
ANISOU 2374  CA  ASP A 263     2485   3509   3076    849   -491    576       C  
ATOM   2375  C   ASP A 263     -49.000 -14.498  -3.623  1.00 30.66           C  
ANISOU 2375  C   ASP A 263     3327   4365   3958    756   -447    542       C  
ATOM   2376  O   ASP A 263     -48.006 -15.229  -3.602  1.00 33.06           O  
ANISOU 2376  O   ASP A 263     3714   4598   4251    677   -440    502       O  
ATOM   2377  CB  ASP A 263     -50.338 -13.232  -5.379  1.00 18.94           C  
ANISOU 2377  CB  ASP A 263     1737   3011   2448    861   -555    616       C  
ATOM   2378  CG  ASP A 263     -50.523 -14.481  -6.235  1.00 28.79           C  
ANISOU 2378  CG  ASP A 263     2946   4313   3681    730   -616    596       C  
ATOM   2379  OD1 ASP A 263     -49.867 -15.509  -5.964  1.00 26.53           O  
ANISOU 2379  OD1 ASP A 263     2710   3977   3395    629   -596    554       O  
ATOM   2380  OD2 ASP A 263     -51.340 -14.437  -7.182  1.00 22.32           O1-
ANISOU 2380  OD2 ASP A 263     2049   3586   2846    729   -688    623       O1-
ATOM   2381  H   ASP A 263     -47.986 -13.608  -6.126  1.00 29.81           H  
ATOM   2382  N   GLU A 264     -50.042 -14.714  -2.814  1.00 42.33           N  
ANISOU 2382  N   GLU A 264     4700   5918   5467    770   -411    561       N  
ATOM   2383  CA  GLU A 264     -50.015 -15.821  -1.858  1.00 37.23           C  
ANISOU 2383  CA  GLU A 264     4043   5263   4839    689   -360    535       C  
ATOM   2384  C   GLU A 264     -49.849 -17.192  -2.538  1.00 24.03           C  
ANISOU 2384  C   GLU A 264     2371   3603   3158    544   -404    507       C  
ATOM   2385  O   GLU A 264     -49.504 -18.156  -1.849  1.00 31.04           O  
ANISOU 2385  O   GLU A 264     3289   4451   4052    469   -365    480       O  
ATOM   2386  CB  GLU A 264     -51.228 -15.732  -0.918  1.00 54.87           C  
ANISOU 2386  CB  GLU A 264     6158   7583   7106    736   -308    568       C  
ATOM   2387  H   GLU A 264     -50.762 -14.244  -2.800  1.00 51.62           H  
ATOM   2388  N   MET A 265     -50.161 -17.335  -3.830  1.00 29.64           N  
ANISOU 2388  N   MET A 265     3047   4365   3848    504   -484    515       N  
ATOM   2389  CA  MET A 265     -49.981 -18.615  -4.520  1.00 23.71           C  
ANISOU 2389  CA  MET A 265     2311   3617   3082    368   -530    483       C  
ATOM   2390  C   MET A 265     -48.695 -18.660  -5.354  1.00 25.06           C  
ANISOU 2390  C   MET A 265     2614   3698   3210    347   -560    450       C  
ATOM   2391  O   MET A 265     -48.546 -19.530  -6.221  1.00 40.05           O  
ANISOU 2391  O   MET A 265     4534   5601   5082    254   -610    426       O  
ATOM   2392  CB  MET A 265     -51.221 -18.921  -5.358  1.00 23.79           C  
ANISOU 2392  CB  MET A 265     2195   3750   3095    322   -602    507       C  
ATOM   2393  CG  MET A 265     -52.495 -18.753  -4.519  1.00 38.08           C  
ANISOU 2393  CG  MET A 265     3859   5658   4951    357   -564    547       C  
ATOM   2394  SD  MET A 265     -53.989 -19.509  -5.187  1.00 63.35           S  
ANISOU 2394  SD  MET A 265     6889   9010   8173    262   -638    569       S  
ATOM   2395  CE  MET A 265     -54.760 -20.203  -3.716  1.00 41.22           C  
ANISOU 2395  CE  MET A 265     3987   6248   5427    216   -545    583       C  
ATOM   2396  H   MET A 265     -50.476 -16.707  -4.326  1.00 36.38           H  
ATOM   2397  N   MET A 266     -47.763 -17.742  -5.085  1.00 29.93           N  
ANISOU 2397  N   MET A 266     3319   4233   3819    430   -526    448       N  
ATOM   2398  CA  MET A 266     -46.424 -17.657  -5.665  1.00 30.42           C  
ANISOU 2398  CA  MET A 266     3505   4204   3849    421   -534    421       C  
ATOM   2399  C   MET A 266     -46.444 -17.198  -7.099  1.00 29.28           C  
ANISOU 2399  C   MET A 266     3373   4087   3665    433   -603    437       C  
ATOM   2400  O   MET A 266     -45.434 -17.317  -7.805  1.00 35.13           O  
ANISOU 2400  O   MET A 266     4207   4769   4372    408   -616    416       O  
ATOM   2401  CB  MET A 266     -45.671 -18.987  -5.559  1.00 29.21           C  
ANISOU 2401  CB  MET A 266     3414   3997   3686    316   -522    373       C  
ATOM   2402  CG  MET A 266     -45.488 -19.452  -4.120  1.00 32.36           C  
ANISOU 2402  CG  MET A 266     3823   4356   4118    307   -452    357       C  
ATOM   2403  SD  MET A 266     -44.091 -18.679  -3.293  1.00 37.23           S  
ANISOU 2403  SD  MET A 266     4549   4859   4738    382   -397    340       S  
ATOM   2404  CE  MET A 266     -44.847 -18.056  -1.794  1.00 36.89           C  
ANISOU 2404  CE  MET A 266     4450   4836   4731    461   -335    363       C  
ATOM   2405  H   MET A 266     -47.898 -17.106  -4.521  1.00 36.73           H  
ATOM   2406  N   GLN A 267     -47.551 -16.661  -7.583  1.00 37.11           N  
ANISOU 2406  N   GLN A 267     4274   5170   4655    477   -648    477       N  
ATOM   2407  CA  GLN A 267     -47.592 -16.229  -8.958  1.00 45.31           C  
ANISOU 2407  CA  GLN A 267     5331   6237   5649    493   -718    495       C  
ATOM   2408  C   GLN A 267     -47.247 -14.764  -9.098  1.00 53.64           C  
ANISOU 2408  C   GLN A 267     6434   7252   6695    611   -705    530       C  
ATOM   2409  O   GLN A 267     -47.771 -13.900  -8.360  1.00 62.95           O  
ANISOU 2409  O   GLN A 267     7569   8444   7906    703   -674    560       O  
ATOM   2410  CB  GLN A 267     -48.943 -16.502  -9.604  1.00 50.51           C  
ANISOU 2410  CB  GLN A 267     5870   7020   6302    470   -790    519       C  
ATOM   2411  CG  GLN A 267     -48.911 -16.159 -11.075  1.00 42.35           C  
ANISOU 2411  CG  GLN A 267     4870   6012   5210    482   -868    534       C  
ATOM   2412  CD  GLN A 267     -50.281 -16.086 -11.700  1.00 45.60           C  
ANISOU 2412  CD  GLN A 267     5159   6553   5615    491   -947    568       C  
ATOM   2413  NE2 GLN A 267     -51.309 -15.920 -10.876  1.00 35.46           N  
ANISOU 2413  NE2 GLN A 267     3751   5341   4383    526   -928    593       N  
ATOM   2414  OE1 GLN A 267     -50.415 -16.181 -12.912  1.00 48.39           O  
ANISOU 2414  OE1 GLN A 267     5527   6944   5916    470  -1025    571       O  
ATOM   2415  H   GLN A 267     -48.278 -16.541  -7.138  1.00 45.34           H  
ATOM   2416 HE21 GLN A 267     -51.176 -15.857 -10.029  1.00 43.37           H  
ATOM   2417 HE22 GLN A 267     -52.108 -15.874 -11.191  1.00 43.37           H  
ATOM   2418  N   THR A 268     -46.414 -14.465 -10.084  1.00 51.47           N  
ANISOU 2418  N   THR A 268     6252   6929   6376    611   -729    529       N  
ATOM   2419  CA  THR A 268     -45.917 -13.142 -10.388  1.00 59.34           C  
ANISOU 2419  CA  THR A 268     7316   7872   7358    706   -719    562       C  
ATOM   2420  C   THR A 268     -47.013 -12.244 -10.970  1.00 62.80           C  
ANISOU 2420  C   THR A 268     7696   8374   7791    775   -762    606       C  
ATOM   2421  O   THR A 268     -48.179 -12.625 -11.109  1.00 81.72           O  
ANISOU 2421  O   THR A 268     9985  10873  10192    767   -807    618       O  
ATOM   2422  CB  THR A 268     -44.778 -13.213 -11.408  1.00 71.85           C  
ANISOU 2422  CB  THR A 268     9010   9395   8893    668   -730    549       C  
ATOM   2423  CG2 THR A 268     -43.738 -14.247 -11.022  1.00 83.97           C  
ANISOU 2423  CG2 THR A 268    10602  10868  10436    579   -690    494       C  
ATOM   2424  OG1 THR A 268     -45.318 -13.541 -12.702  1.00 80.70           O  
ANISOU 2424  OG1 THR A 268    10113  10590   9961    641   -806    561       O  
ATOM   2425  H   THR A 268     -46.102 -15.054 -10.628  1.00 62.58           H  
ATOM   2426  HG1 THR A 268     -45.716 -14.280 -12.668  1.00 97.67           H  
ATOM   2427  N   SER A 269     -46.544 -11.043 -11.351  1.00 55.13           N  
ANISOU 2427  N   SER A 269     6805   7325   6818    818   -739    620       N  
ATOM   2428  CA  SER A 269     -47.289  -9.981 -12.020  1.00 38.27           C  
ANISOU 2428  CA  SER A 269     4657   5207   4678    873   -764    654       C  
ATOM   2429  C   SER A 269     -47.849 -10.388 -13.361  1.00 26.40           C  
ANISOU 2429  C   SER A 269     3126   3781   3122    847   -849    669       C  
ATOM   2430  O   SER A 269     -48.728  -9.689 -13.904  1.00 30.61           O  
ANISOU 2430  O   SER A 269     3626   4353   3653    894   -884    698       O  
ATOM   2431  CB  SER A 269     -46.323  -8.831 -12.328  1.00 36.99           C  
ANISOU 2431  CB  SER A 269     4605   4939   4511    896   -723    665       C  
ATOM   2432  OG  SER A 269     -45.618  -9.102 -13.558  1.00 60.56           O  
ANISOU 2432  OG  SER A 269     7655   7915   7439    853   -753    672       O  
ATOM   2433  H   SER A 269     -45.728 -10.804 -11.220  1.00 66.98           H  
ATOM   2434  HG  SER A 269     -45.102  -8.465 -13.739  1.00 73.49           H  
ATOM   2435  N   VAL A 270     -47.279 -11.415 -13.955  1.00 22.03           N  
ANISOU 2435  N   VAL A 270     2604   3243   2524    776   -881    650       N  
ATOM   2436  CA  VAL A 270     -47.610 -11.895 -15.278  1.00 37.50           C  
ANISOU 2436  CA  VAL A 270     4563   5265   4422    737   -962    655       C  
ATOM   2437  C   VAL A 270     -48.379 -13.207 -15.119  1.00 47.29           C  
ANISOU 2437  C   VAL A 270     5703   6607   5659    671  -1017    629       C  
ATOM   2438  O   VAL A 270     -47.821 -14.173 -14.588  1.00 36.55           O  
ANISOU 2438  O   VAL A 270     4347   5241   4298    612   -997    600       O  
ATOM   2439  CB  VAL A 270     -46.360 -12.096 -16.141  1.00 32.09           C  
ANISOU 2439  CB  VAL A 270     3996   4522   3676    697   -955    648       C  
ATOM   2440  CG1 VAL A 270     -46.761 -12.404 -17.568  1.00 35.56           C  
ANISOU 2440  CG1 VAL A 270     4445   5022   4044    666  -1035    657       C  
ATOM   2441  CG2 VAL A 270     -45.481 -10.869 -16.076  1.00 38.30           C  
ANISOU 2441  CG2 VAL A 270     4868   5206   4478    744   -883    670       C  
ATOM   2442  H   VAL A 270     -46.657 -11.881 -13.586  1.00 27.26           H  
ATOM   2443  N   PRO A 271     -49.624 -13.276 -15.564  1.00 35.02           N  
ANISOU 2443  N   PRO A 271     4056   5145   4106    672  -1083    638       N  
ATOM   2444  CA  PRO A 271     -50.373 -14.530 -15.432  1.00 37.37           C  
ANISOU 2444  CA  PRO A 271     4250   5540   4409    587  -1132    613       C  
ATOM   2445  C   PRO A 271     -49.660 -15.652 -16.167  1.00 35.53           C  
ANISOU 2445  C   PRO A 271     4084   5304   4111    485  -1172    579       C  
ATOM   2446  O   PRO A 271     -49.099 -15.455 -17.247  1.00 33.59           O  
ANISOU 2446  O   PRO A 271     3939   5024   3800    491  -1200    576       O  
ATOM   2447  CB  PRO A 271     -51.732 -14.198 -16.065  1.00 44.58           C  
ANISOU 2447  CB  PRO A 271     5074   6540   5326    613  -1201    630       C  
ATOM   2448  CG  PRO A 271     -51.787 -12.692 -16.126  1.00 43.70           C  
ANISOU 2448  CG  PRO A 271     5001   6375   5229    727  -1170    670       C  
ATOM   2449  CD  PRO A 271     -50.380 -12.243 -16.289  1.00 38.75           C  
ANISOU 2449  CD  PRO A 271     4517   5635   4573    739  -1119    673       C  
ATOM   2450  N   GLY A 272     -49.671 -16.837 -15.555  1.00 27.48           N  
ANISOU 2450  N   GLY A 272     3030   4292   3121    382  -1159    539       N  
ATOM   2451  CA  GLY A 272     -48.970 -17.983 -16.087  1.00 20.95           C  
ANISOU 2451  CA  GLY A 272     2290   3419   2252    272  -1171    483       C  
ATOM   2452  C   GLY A 272     -47.518 -18.087 -15.680  1.00 33.02           C  
ANISOU 2452  C   GLY A 272     3943   4822   3781    267  -1084    454       C  
ATOM   2453  O   GLY A 272     -46.835 -19.023 -16.123  1.00 25.46           O  
ANISOU 2453  O   GLY A 272     3068   3820   2787    188  -1086    407       O  
ATOM   2454  H   GLY A 272     -50.087 -16.996 -14.819  1.00 33.80           H  
ATOM   2455  N   VAL A 273     -47.022 -17.161 -14.863  1.00 19.29           N  
ANISOU 2455  N   VAL A 273     2221   3025   2084    350  -1010    478       N  
ATOM   2456  CA  VAL A 273     -45.624 -17.134 -14.448  1.00 17.87           C  
ANISOU 2456  CA  VAL A 273     2149   2731   1909    351   -931    454       C  
ATOM   2457  C   VAL A 273     -45.561 -17.131 -12.927  1.00 17.23           C  
ANISOU 2457  C   VAL A 273     2030   2615   1903    363   -857    446       C  
ATOM   2458  O   VAL A 273     -46.163 -16.271 -12.272  1.00 25.18           O  
ANISOU 2458  O   VAL A 273     2972   3647   2949    440   -840    482       O  
ATOM   2459  CB  VAL A 273     -44.877 -15.917 -15.018  1.00 32.40           C  
ANISOU 2459  CB  VAL A 273     4072   4521   3718    437   -914    489       C  
ATOM   2460  CG1 VAL A 273     -43.407 -15.965 -14.615  1.00 23.96           C  
ANISOU 2460  CG1 VAL A 273     3102   3342   2659    426   -836    462       C  
ATOM   2461  CG2 VAL A 273     -45.017 -15.868 -16.530  1.00 25.71           C  
ANISOU 2461  CG2 VAL A 273     3265   3715   2789    435   -986    503       C  
ATOM   2462  H   VAL A 273     -47.488 -16.522 -14.527  1.00 23.97           H  
ATOM   2463  N   TRP A 274     -44.809 -18.076 -12.373  1.00 17.18           N  
ANISOU 2463  N   TRP A 274     2071   2547   1911    294   -813    399       N  
ATOM   2464  CA  TRP A 274     -44.636 -18.205 -10.939  1.00 18.38           C  
ANISOU 2464  CA  TRP A 274     2203   2658   2123    298   -743    387       C  
ATOM   2465  C   TRP A 274     -43.186 -17.940 -10.554  1.00 19.29           C  
ANISOU 2465  C   TRP A 274     2420   2667   2243    320   -680    368       C  
ATOM   2466  O   TRP A 274     -42.265 -18.106 -11.361  1.00 24.73           O  
ANISOU 2466  O   TRP A 274     3192   3313   2890    300   -684    352       O  
ATOM   2467  CB  TRP A 274     -45.059 -19.599 -10.460  1.00 30.29           C  
ANISOU 2467  CB  TRP A 274     3672   4186   3649    198   -744    351       C  
ATOM   2468  CG  TRP A 274     -46.548 -19.753 -10.310  1.00 30.68           C  
ANISOU 2468  CG  TRP A 274     3594   4340   3724    180   -783    375       C  
ATOM   2469  CD1 TRP A 274     -47.268 -19.682  -9.150  1.00 38.60           C  
ANISOU 2469  CD1 TRP A 274     4510   5375   4783    198   -743    391       C  
ATOM   2470  CD2 TRP A 274     -47.499 -20.001 -11.355  1.00 27.00           C  
ANISOU 2470  CD2 TRP A 274     3066   3965   3227    142   -870    385       C  
ATOM   2471  CE2 TRP A 274     -48.772 -20.067 -10.755  1.00 20.97           C  
ANISOU 2471  CE2 TRP A 274     2168   3290   2509    135   -879    409       C  
ATOM   2472  CE3 TRP A 274     -47.396 -20.173 -12.741  1.00 29.40           C  
ANISOU 2472  CE3 TRP A 274     3416   4288   3466    113   -943    376       C  
ATOM   2473  NE1 TRP A 274     -48.604 -19.872  -9.409  1.00 28.64           N  
ANISOU 2473  NE1 TRP A 274     3128   4222   3532    171   -795    414       N  
ATOM   2474  CZ2 TRP A 274     -49.935 -20.295 -11.490  1.00 29.19           C  
ANISOU 2474  CZ2 TRP A 274     3111   4441   3540     97   -963    425       C  
ATOM   2475  CZ3 TRP A 274     -48.553 -20.400 -13.469  1.00 19.60           C  
ANISOU 2475  CZ3 TRP A 274     2088   3151   2207     77  -1030    388       C  
ATOM   2476  CH2 TRP A 274     -49.804 -20.458 -12.842  1.00 31.15           C  
ANISOU 2476  CH2 TRP A 274     3408   4704   3723     67  -1042    412       C  
ATOM   2477  H   TRP A 274     -44.378 -18.669 -12.825  1.00 21.44           H  
ATOM   2478  HE1 TRP A 274     -49.232 -19.869  -8.821  1.00 35.19           H  
ATOM   2479  N   GLY A 275     -43.008 -17.511  -9.306  1.00 22.24           N  
ANISOU 2479  N   GLY A 275     2783   3001   2665    364   -622    371       N  
ATOM   2480  CA  GLY A 275     -41.704 -17.258  -8.727  1.00 17.40           C  
ANISOU 2480  CA  GLY A 275     2252   2293   2066    383   -565    352       C  
ATOM   2481  C   GLY A 275     -41.595 -17.900  -7.360  1.00 18.86           C  
ANISOU 2481  C   GLY A 275     2426   2449   2292    360   -517    325       C  
ATOM   2482  O   GLY A 275     -42.491 -17.736  -6.524  1.00 13.43           O  
ANISOU 2482  O   GLY A 275     1669   1799   1636    385   -503    341       O  
ATOM   2483  H   GLY A 275     -43.653 -17.354  -8.759  1.00 27.50           H  
ATOM   2484  N   ILE A 276     -40.504 -18.629  -7.118  1.00 29.16           N  
ANISOU 2484  N   ILE A 276     3799   3688   3594    317   -488    286       N  
ATOM   2485  CA  ILE A 276     -40.373 -19.465  -5.932  1.00 19.49           C  
ANISOU 2485  CA  ILE A 276     2574   2435   2396    285   -448    258       C  
ATOM   2486  C   ILE A 276     -38.933 -19.475  -5.441  1.00 11.39           C  
ANISOU 2486  C   ILE A 276     1628   1322   1377    296   -408    230       C  
ATOM   2487  O   ILE A 276     -37.985 -19.340  -6.220  1.00 25.97           O  
ANISOU 2487  O   ILE A 276     3532   3135   3202    293   -413    222       O  
ATOM   2488  CB  ILE A 276     -40.828 -20.916  -6.198  1.00 17.09           C  
ANISOU 2488  CB  ILE A 276     2257   2160   2078    192   -469    233       C  
ATOM   2489  CG1 ILE A 276     -40.056 -21.521  -7.375  1.00 12.38           C  
ANISOU 2489  CG1 ILE A 276     1730   1539   1435    146   -495    207       C  
ATOM   2490  CG2 ILE A 276     -42.317 -20.976  -6.476  1.00 18.36           C  
ANISOU 2490  CG2 ILE A 276     2321   2413   2242    172   -509    259       C  
ATOM   2491  CD1 ILE A 276     -40.252 -23.017  -7.500  1.00 20.11           C  
ANISOU 2491  CD1 ILE A 276     2725   2517   2397     55   -508    172       C  
ATOM   2492  H   ILE A 276     -39.819 -18.655  -7.636  1.00 35.82           H  
ATOM   2493  N   GLY A 277     -38.777 -19.663  -4.133  1.00 11.07           N  
ANISOU 2493  N   GLY A 277     1591   1249   1366    308   -367    217       N  
ATOM   2494  CA  GLY A 277     -37.454 -19.783  -3.558  1.00 10.43           C  
ANISOU 2494  CA  GLY A 277     1578   1093   1293    316   -336    188       C  
ATOM   2495  C   GLY A 277     -36.773 -18.434  -3.407  1.00 18.08           C  
ANISOU 2495  C   GLY A 277     2572   2021   2277    382   -325    201       C  
ATOM   2496  O   GLY A 277     -37.417 -17.390  -3.309  1.00 17.17           O  
ANISOU 2496  O   GLY A 277     2426   1925   2172    435   -330    232       O  
ATOM   2497  H   GLY A 277     -39.420 -19.724  -3.565  1.00  9.19           H  
ATOM   2498  N   ASP A 278     -35.443 -18.461  -3.406  1.00  9.75           N  
ANISOU 2498  N   ASP A 278     1573    908   1223    378   -311    179       N  
ATOM   2499  CA  ASP A 278     -34.677 -17.292  -2.990  1.00 26.40           C  
ANISOU 2499  CA  ASP A 278     3710   2966   3354    428   -298    185       C  
ATOM   2500  C   ASP A 278     -34.637 -16.191  -4.052  1.00 19.01           C  
ANISOU 2500  C   ASP A 278     2780   2035   2409    452   -315    218       C  
ATOM   2501  O   ASP A 278     -34.261 -15.060  -3.722  1.00 24.77           O  
ANISOU 2501  O   ASP A 278     3514   2738   3161    477   -296    224       O  
ATOM   2502  CB  ASP A 278     -33.271 -17.747  -2.564  1.00 29.51           C  
ANISOU 2502  CB  ASP A 278     4151   3305   3757    411   -280    150       C  
ATOM   2503  CG  ASP A 278     -33.240 -18.287  -1.117  1.00 40.69           C  
ANISOU 2503  CG  ASP A 278     5567   4704   5188    414   -257    123       C  
ATOM   2504  OD1 ASP A 278     -34.273 -18.197  -0.415  1.00 46.47           O  
ANISOU 2504  OD1 ASP A 278     6277   5455   5925    440   -254    136       O  
ATOM   2505  OD2 ASP A 278     -32.182 -18.796  -0.679  1.00 42.98           O1-
ANISOU 2505  OD2 ASP A 278     5872   4977   5482    387   -236     91       O1-
ATOM   2506  H   ASP A 278     -34.967 -19.138  -3.639  1.00  8.60           H  
ATOM   2507  N   ILE A 279     -35.073 -16.467  -5.287  1.00 41.92           N  
ANISOU 2507  N   ILE A 279     5669   4982   5278    427   -341    234       N  
ATOM   2508  CA  ILE A 279     -35.288 -15.405  -6.271  1.00 22.79           C  
ANISOU 2508  CA  ILE A 279     3250   2571   2839    458   -359    273       C  
ATOM   2509  C   ILE A 279     -36.264 -14.359  -5.739  1.00 26.19           C  
ANISOU 2509  C   ILE A 279     3648   3015   3289    523   -365    304       C  
ATOM   2510  O   ILE A 279     -36.251 -13.204  -6.181  1.00 25.96           O  
ANISOU 2510  O   ILE A 279     3626   2977   3261    553   -361    332       O  
ATOM   2511  CB  ILE A 279     -35.788 -16.002  -7.601  1.00 17.77           C  
ANISOU 2511  CB  ILE A 279     2604   1992   2157    422   -393    283       C  
ATOM   2512  CG1 ILE A 279     -35.659 -14.975  -8.729  1.00 24.41           C  
ANISOU 2512  CG1 ILE A 279     3471   2833   2971    452   -408    322       C  
ATOM   2513  CG2 ILE A 279     -37.243 -16.459  -7.478  1.00 23.17           C  
ANISOU 2513  CG2 ILE A 279     3221   2747   2836    415   -423    291       C  
ATOM   2514  CD1 ILE A 279     -36.176 -15.458 -10.070  1.00 18.94           C  
ANISOU 2514  CD1 ILE A 279     2776   2199   2223    424   -447    333       C  
ATOM   2515  H   ILE A 279     -35.251 -17.257  -5.577  1.00 51.13           H  
ATOM   2516  N   ARG A 280     -37.134 -14.753  -4.805  1.00 29.10           N  
ANISOU 2516  N   ARG A 280     3969   3414   3673    532   -359    297       N  
ATOM   2517  CA  ARG A 280     -38.073 -13.825  -4.182  1.00 21.60           C  
ANISOU 2517  CA  ARG A 280     2986   2481   2741    603   -355    324       C  
ATOM   2518  C   ARG A 280     -37.408 -12.905  -3.165  1.00 19.66           C  
ANISOU 2518  C   ARG A 280     2761   2178   2530    608   -305    302       C  
ATOM   2519  O   ARG A 280     -37.986 -11.866  -2.816  1.00 26.37           O  
ANISOU 2519  O   ARG A 280     3591   3032   3395    647   -292    317       O  
ATOM   2520  CB  ARG A 280     -39.195 -14.599  -3.481  1.00 14.94           C  
ANISOU 2520  CB  ARG A 280     2074   1698   1906    594   -350    320       C  
ATOM   2521  CG  ARG A 280     -40.031 -15.509  -4.370  1.00 27.32           C  
ANISOU 2521  CG  ARG A 280     3585   3345   3451    539   -385    327       C  
ATOM   2522  CD  ARG A 280     -41.023 -16.303  -3.513  1.00 32.75           C  
ANISOU 2522  CD  ARG A 280     4205   4085   4155    519   -370    322       C  
ATOM   2523  NE  ARG A 280     -41.666 -15.422  -2.541  1.00 36.39           N  
ANISOU 2523  NE  ARG A 280     4634   4553   4640    600   -341    344       N  
ATOM   2524  CZ  ARG A 280     -42.066 -15.779  -1.325  1.00 17.83           C  
ANISOU 2524  CZ  ARG A 280     2258   2208   2307    607   -301    335       C  
ATOM   2525  NH1 ARG A 280     -41.910 -17.022  -0.892  1.00 18.85           N1+
ANISOU 2525  NH1 ARG A 280     2390   2334   2437    535   -285    308       N1+
ATOM   2526  NH2 ARG A 280     -42.627 -14.875  -0.538  1.00 32.46           N  
ANISOU 2526  NH2 ARG A 280     4091   4068   4176    692   -273    355       N  
ATOM   2527  H   ARG A 280     -37.199 -15.559  -4.513  1.00 35.73           H  
ATOM   2528  HE  ARG A 280     -41.797 -14.605  -2.775  1.00 44.49           H  
ATOM   2529 HH11 ARG A 280     -41.546 -17.612  -1.401  1.00 23.44           H  
ATOM   2530 HH12 ARG A 280     -42.174 -17.239  -0.102  1.00 23.44           H  
ATOM   2531 HH21 ARG A 280     -42.729 -14.068  -0.816  1.00 39.77           H  
ATOM   2532 HH22 ARG A 280     -42.890 -15.095   0.251  1.00 39.77           H  
ATOM   2533  N   ASN A 281     -36.238 -13.280  -2.654  1.00 23.08           N  
ANISOU 2533  N   ASN A 281     3230   2564   2974    566   -281    264       N  
ATOM   2534  CA  ASN A 281     -35.455 -12.451  -1.737  1.00 20.00           C  
ANISOU 2534  CA  ASN A 281     2856   2132   2612    557   -246    239       C  
ATOM   2535  C   ASN A 281     -36.215 -12.116  -0.452  1.00 27.56           C  
ANISOU 2535  C   ASN A 281     3794   3095   3583    592   -225    232       C  
ATOM   2536  O   ASN A 281     -36.247 -10.965  -0.012  1.00 42.26           O  
ANISOU 2536  O   ASN A 281     5662   4937   5459    611   -211    233       O  
ATOM   2537  CB  ASN A 281     -34.992 -11.163  -2.433  1.00 21.77           C  
ANISOU 2537  CB  ASN A 281     3097   2330   2843    558   -244    258       C  
ATOM   2538  CG  ASN A 281     -33.807 -10.518  -1.739  1.00 16.99           C  
ANISOU 2538  CG  ASN A 281     2516   1677   2261    530   -219    230       C  
ATOM   2539  ND2 ASN A 281     -33.777  -9.188  -1.727  1.00 25.84           N  
ANISOU 2539  ND2 ASN A 281     3650   2771   3396    547   -214    243       N  
ATOM   2540  OD1 ASN A 281     -32.927 -11.205  -1.228  1.00 27.33           O  
ANISOU 2540  OD1 ASN A 281     3833   2974   3576    496   -210    198       O  
ATOM   2541  H   ASN A 281     -35.863 -14.034  -2.829  1.00 28.51           H  
ATOM   2542 HD21 ASN A 281     -33.125  -8.776  -1.346  1.00 31.82           H  
ATOM   2543 HD22 ASN A 281     -34.409  -8.740  -2.099  1.00 31.82           H  
ATOM   2544  N   THR A 282     -36.833 -13.135   0.155  1.00 35.96           N  
ANISOU 2544  N   THR A 282     4840   4183   4640    603   -224    227       N  
ATOM   2545  CA  THR A 282     -37.331 -12.993   1.517  1.00 16.31           C  
ANISOU 2545  CA  THR A 282     2343   1694   2159    631   -196    214       C  
ATOM   2546  C   THR A 282     -36.168 -13.193   2.479  1.00 22.56           C  
ANISOU 2546  C   THR A 282     3170   2446   2956    591   -176    171       C  
ATOM   2547  O   THR A 282     -35.127 -13.740   2.101  1.00 26.13           O  
ANISOU 2547  O   THR A 282     3640   2881   3407    545   -183    153       O  
ATOM   2548  CB  THR A 282     -38.420 -14.016   1.836  1.00 19.27           C  
ANISOU 2548  CB  THR A 282     2686   2113   2524    663   -196    231       C  
ATOM   2549  CG2 THR A 282     -39.383 -14.200   0.681  1.00 25.33           C  
ANISOU 2549  CG2 THR A 282     3406   2939   3280    689   -233    274       C  
ATOM   2550  OG1 THR A 282     -37.815 -15.275   2.156  1.00 34.91           O  
ANISOU 2550  OG1 THR A 282     4694   4073   4497    625   -195    206       O  
ATOM   2551  H   THR A 282     -36.971 -13.906  -0.200  1.00 43.97           H  
ATOM   2552  HG1 THR A 282     -37.359 -15.548   1.506  1.00 42.71           H  
ATOM   2553  N   PRO A 283     -36.311 -12.771   3.740  1.00 27.31           N  
ANISOU 2553  N   PRO A 283     3780   3038   3559    611   -153    154       N  
ATOM   2554  CA  PRO A 283     -35.245 -13.043   4.723  1.00 23.72           C  
ANISOU 2554  CA  PRO A 283     3354   2556   3102    576   -142    116       C  
ATOM   2555  C   PRO A 283     -35.133 -14.507   5.097  1.00 27.75           C  
ANISOU 2555  C   PRO A 283     3869   3075   3600    557   -137    103       C  
ATOM   2556  O   PRO A 283     -34.150 -14.895   5.743  1.00 25.43           O  
ANISOU 2556  O   PRO A 283     3595   2765   3301    524   -134     74       O  
ATOM   2557  CB  PRO A 283     -35.645 -12.195   5.937  1.00 16.48           C  
ANISOU 2557  CB  PRO A 283     2451   1632   2180    613   -123    106       C  
ATOM   2558  CG  PRO A 283     -37.074 -11.818   5.729  1.00 14.11           C  
ANISOU 2558  CG  PRO A 283     2124   1360   1878    672   -115    137       C  
ATOM   2559  CD  PRO A 283     -37.432 -11.989   4.289  1.00 15.63           C  
ANISOU 2559  CD  PRO A 283     2286   1574   2079    670   -138    170       C  
ATOM   2560  N   PHE A 284     -36.098 -15.324   4.696  1.00 37.73           N  
ANISOU 2560  N   PHE A 284     5116   4362   4857    578   -140    126       N  
ATOM   2561  CA  PHE A 284     -36.190 -16.717   5.124  1.00 14.45           C  
ANISOU 2561  CA  PHE A 284     2182   1412   1895    568   -132    119       C  
ATOM   2562  C   PHE A 284     -35.533 -17.634   4.099  1.00 17.42           C  
ANISOU 2562  C   PHE A 284     2573   1778   2268    523   -157    113       C  
ATOM   2563  O   PHE A 284     -36.162 -18.507   3.503  1.00 33.91           O  
ANISOU 2563  O   PHE A 284     4663   3873   4348    526   -174    133       O  
ATOM   2564  CB  PHE A 284     -37.652 -17.076   5.343  1.00 18.83           C  
ANISOU 2564  CB  PHE A 284     2713   1999   2444    624   -117    154       C  
ATOM   2565  CG  PHE A 284     -38.365 -16.122   6.247  1.00 10.98           C  
ANISOU 2565  CG  PHE A 284     1701   1021   1450    676    -87    161       C  
ATOM   2566  CD1 PHE A 284     -38.065 -16.091   7.594  1.00 17.74           C  
ANISOU 2566  CD1 PHE A 284     2591   1859   2292    679    -59    135       C  
ATOM   2567  CD2 PHE A 284     -39.312 -15.241   5.757  1.00 18.90           C  
ANISOU 2567  CD2 PHE A 284     2659   2061   2461    724    -90    194       C  
ATOM   2568  CE1 PHE A 284     -38.707 -15.217   8.439  1.00 21.47           C  
ANISOU 2568  CE1 PHE A 284     3059   2342   2756    730    -31    138       C  
ATOM   2569  CE2 PHE A 284     -39.959 -14.364   6.605  1.00 14.74           C  
ANISOU 2569  CE2 PHE A 284     2123   1546   1930    775    -59    196       C  
ATOM   2570  CZ  PHE A 284     -39.652 -14.349   7.945  1.00 11.55           C  
ANISOU 2570  CZ  PHE A 284     1761   1118   1510    778    -29    168       C  
ATOM   2571  H   PHE A 284     -36.729 -15.091   4.160  1.00 46.10           H  
ATOM   2572  N   LYS A 285     -34.232 -17.422   3.912  1.00 27.72           N  
ANISOU 2572  N   LYS A 285     3889   3066   3578    482   -161     88       N  
ATOM   2573  CA  LYS A 285     -33.445 -18.189   2.950  1.00 20.65           C  
ANISOU 2573  CA  LYS A 285     3008   2161   2677    443   -179     78       C  
ATOM   2574  C   LYS A 285     -33.003 -19.480   3.621  1.00 19.85           C  
ANISOU 2574  C   LYS A 285     2933   2047   2563    419   -168     54       C  
ATOM   2575  O   LYS A 285     -31.912 -19.578   4.183  1.00 19.14           O  
ANISOU 2575  O   LYS A 285     2845   1954   2473    398   -159     29       O  
ATOM   2576  CB  LYS A 285     -32.261 -17.373   2.449  1.00 24.30           C  
ANISOU 2576  CB  LYS A 285     3465   2616   3150    420   -181     69       C  
ATOM   2577  CG  LYS A 285     -32.696 -16.097   1.756  1.00 35.27           C  
ANISOU 2577  CG  LYS A 285     4840   4010   4550    442   -189     96       C  
ATOM   2578  CD  LYS A 285     -31.595 -15.449   0.943  1.00 43.20           C  
ANISOU 2578  CD  LYS A 285     5849   5001   5564    419   -193     95       C  
ATOM   2579  CE  LYS A 285     -32.180 -14.380   0.031  1.00 41.88           C  
ANISOU 2579  CE  LYS A 285     5676   4836   5400    442   -204    129       C  
ATOM   2580  NZ  LYS A 285     -32.555 -13.182   0.826  1.00 44.07           N1+
ANISOU 2580  NZ  LYS A 285     5946   5106   5692    468   -192    133       N1+
ATOM   2581  H   LYS A 285     -33.776 -16.829   4.337  1.00 34.09           H  
ATOM   2582  HZ1 LYS A 285     -32.899 -12.559   0.292  1.00 53.70           H  
ATOM   2583  HZ2 LYS A 285     -33.160 -13.402   1.440  1.00 53.70           H  
ATOM   2584  HZ3 LYS A 285     -31.837 -12.850   1.233  1.00 53.70           H  
ATOM   2585  N   GLN A 286     -33.882 -20.479   3.571  1.00 29.42           N  
ANISOU 2585  N   GLN A 286     4165   3251   3764    425   -172     66       N  
ATOM   2586  CA  GLN A 286     -33.591 -21.824   4.047  1.00 35.26           C  
ANISOU 2586  CA  GLN A 286     4940   3968   4488    399   -162     48       C  
ATOM   2587  C   GLN A 286     -34.183 -22.814   3.052  1.00 36.80           C  
ANISOU 2587  C   GLN A 286     5137   4175   4672    352   -175     57       C  
ATOM   2588  O   GLN A 286     -35.183 -22.527   2.387  1.00 50.00           O  
ANISOU 2588  O   GLN A 286     6755   5896   6345    335   -184     81       O  
ATOM   2589  CB  GLN A 286     -34.151 -22.085   5.454  1.00 37.03           C  
ANISOU 2589  CB  GLN A 286     5176   4188   4704    422   -131     50       C  
ATOM   2590  CG  GLN A 286     -33.760 -21.063   6.517  1.00 33.01           C  
ANISOU 2590  CG  GLN A 286     4645   3697   4199    442   -116     39       C  
ATOM   2591  CD  GLN A 286     -32.325 -21.182   6.983  1.00 17.98           C  
ANISOU 2591  CD  GLN A 286     2745   1796   2291    414   -119      9       C  
ATOM   2592  NE2 GLN A 286     -31.721 -20.041   7.269  1.00 24.54           N  
ANISOU 2592  NE2 GLN A 286     3556   2637   3132    418   -125      1       N  
ATOM   2593  OE1 GLN A 286     -31.763 -22.275   7.089  1.00 21.64           O  
ANISOU 2593  OE1 GLN A 286     3230   2252   2742    391   -118     -4       O  
ATOM   2594  H   GLN A 286     -34.678 -20.398   3.255  1.00 36.12           H  
ATOM   2595 HE21 GLN A 286     -32.145 -19.298   7.184  1.00 30.27           H  
ATOM   2596 HE22 GLN A 286     -30.905 -20.042   7.539  1.00 30.27           H  
ATOM   2597  N   ALA A 287     -33.560 -23.992   2.968  1.00 28.31           N  
ANISOU 2597  N   ALA A 287     4104   3070   3581    317   -173     34       N  
ATOM   2598  CA  ALA A 287     -33.895 -24.946   1.913  1.00 22.39           C  
ANISOU 2598  CA  ALA A 287     3353   2338   2815    253   -185     31       C  
ATOM   2599  C   ALA A 287     -35.340 -25.426   2.001  1.00 21.84           C  
ANISOU 2599  C   ALA A 287     3241   2313   2744    208   -177     53       C  
ATOM   2600  O   ALA A 287     -36.017 -25.556   0.973  1.00 29.35           O  
ANISOU 2600  O   ALA A 287     4157   3305   3688    164   -200     62       O  
ATOM   2601  CB  ALA A 287     -32.934 -26.134   1.964  1.00 23.35           C  
ANISOU 2601  CB  ALA A 287     3542   2411   2920    236   -179      2       C  
ATOM   2602  H   ALA A 287     -32.945 -24.261   3.506  1.00 34.78           H  
ATOM   2603  N   VAL A 288     -35.824 -25.719   3.212  1.00 21.97           N  
ANISOU 2603  N   VAL A 288     3260   2324   2763    216   -144     61       N  
ATOM   2604  CA  VAL A 288     -37.179 -26.250   3.358  1.00 23.17           C  
ANISOU 2604  CA  VAL A 288     3365   2521   2918    165   -129     85       C  
ATOM   2605  C   VAL A 288     -38.214 -25.175   3.058  1.00 22.33           C  
ANISOU 2605  C   VAL A 288     3172   2484   2829    187   -138    116       C  
ATOM   2606  O   VAL A 288     -39.347 -25.488   2.666  1.00 29.25           O  
ANISOU 2606  O   VAL A 288     3986   3416   3711    137   -143    136       O  
ATOM   2607  CB  VAL A 288     -37.401 -26.838   4.764  1.00 27.08           C  
ANISOU 2607  CB  VAL A 288     3889   2991   3409    171    -83     91       C  
ATOM   2608  CG1 VAL A 288     -37.433 -25.737   5.819  1.00 21.79           C  
ANISOU 2608  CG1 VAL A 288     3207   2326   2746    253    -59    103       C  
ATOM   2609  CG2 VAL A 288     -38.705 -27.640   4.789  1.00 18.94           C  
ANISOU 2609  CG2 VAL A 288     2814   2002   2382     97    -64    114       C  
ATOM   2610  H   VAL A 288     -35.395 -25.622   3.952  1.00 27.18           H  
ATOM   2611  N   VAL A 289     -37.862 -23.906   3.264  1.00 10.14           N  
ANISOU 2611  N   VAL A 289     1621    936   1295    262   -140    121       N  
ATOM   2612  CA  VAL A 289     -38.750 -22.809   2.885  1.00 10.45           C  
ANISOU 2612  CA  VAL A 289     1587   1034   1348    296   -151    150       C  
ATOM   2613  C   VAL A 289     -38.827 -22.703   1.375  1.00 14.32           C  
ANISOU 2613  C   VAL A 289     2053   1555   1832    262   -198    154       C  
ATOM   2614  O   VAL A 289     -39.907 -22.534   0.793  1.00 26.40           O  
ANISOU 2614  O   VAL A 289     3512   3152   3367    245   -216    179       O  
ATOM   2615  CB  VAL A 289     -38.259 -21.487   3.501  1.00 10.17           C  
ANISOU 2615  CB  VAL A 289     1572    972   1322    384   -142    151       C  
ATOM   2616  CG1 VAL A 289     -39.049 -20.319   2.939  1.00 18.22           C  
ANISOU 2616  CG1 VAL A 289     2529   2041   2353    427   -157    182       C  
ATOM   2617  CG2 VAL A 289     -38.366 -21.529   5.004  1.00 30.09           C  
ANISOU 2617  CG2 VAL A 289     4118   3473   3843    423    -97    150       C  
ATOM   2618  H   VAL A 289     -37.119 -23.655   3.618  1.00 10.90           H  
ATOM   2619  N   ALA A 290     -37.667 -22.771   0.722  1.00 20.08           N  
ANISOU 2619  N   ALA A 290     2840   2240   2550    257   -218    130       N  
ATOM   2620  CA  ALA A 290     -37.609 -22.763  -0.731  1.00 10.19           C  
ANISOU 2620  CA  ALA A 290     1580   1010   1281    225   -258    130       C  
ATOM   2621  C   ALA A 290     -38.420 -23.908  -1.313  1.00 11.64           C  
ANISOU 2621  C   ALA A 290     1742   1231   1451    144   -277    127       C  
ATOM   2622  O   ALA A 290     -39.226 -23.713  -2.230  1.00 20.11           O  
ANISOU 2622  O   ALA A 290     2763   2361   2515    122   -312    145       O  
ATOM   2623  CB  ALA A 290     -36.152 -22.856  -1.182  1.00  9.69           C  
ANISOU 2623  CB  ALA A 290     1587    890   1206    230   -262    103       C  
ATOM   2624  H   ALA A 290     -36.897 -22.821   1.101  1.00 24.92           H  
ATOM   2625  N   ALA A 291     -38.200 -25.119  -0.793  1.00 28.25           N  
ANISOU 2625  N   ALA A 291     3888   3298   3547     97   -257    105       N  
ATOM   2626  CA  ALA A 291     -38.950 -26.288  -1.240  1.00 15.39           C  
ANISOU 2626  CA  ALA A 291     2249   1692   1907     10   -273     99       C  
ATOM   2627  C   ALA A 291     -40.444 -26.072  -1.061  1.00 12.75           C  
ANISOU 2627  C   ALA A 291     1817   1435   1592    -12   -277    134       C  
ATOM   2628  O   ALA A 291     -41.245 -26.447  -1.931  1.00 20.46           O  
ANISOU 2628  O   ALA A 291     2751   2461   2561    -74   -317    139       O  
ATOM   2629  CB  ALA A 291     -38.486 -27.521  -0.464  1.00 21.00           C  
ANISOU 2629  CB  ALA A 291     3029   2340   2611    -25   -241     76       C  
ATOM   2630  H   ALA A 291     -37.621 -25.289  -0.180  1.00 34.72           H  
ATOM   2631  N   GLY A 292     -40.836 -25.465   0.059  1.00 21.69           N  
ANISOU 2631  N   GLY A 292     2912   2581   2750     41   -237    157       N  
ATOM   2632  CA  GLY A 292     -42.236 -25.164   0.292  1.00 43.24           C  
ANISOU 2632  CA  GLY A 292     5538   5390   5500     35   -232    193       C  
ATOM   2633  C   GLY A 292     -42.837 -24.261  -0.767  1.00 58.56           C  
ANISOU 2633  C   GLY A 292     7409   7400   7441     58   -281    215       C  
ATOM   2634  O   GLY A 292     -43.960 -24.489  -1.220  1.00 68.81           O  
ANISOU 2634  O   GLY A 292     8625   8773   8747     11   -307    235       O  
ATOM   2635  H   GLY A 292     -40.309 -25.221   0.695  1.00 26.85           H  
ATOM   2636  N   ASP A 293     -42.110 -23.198  -1.148  1.00 64.22           N  
ANISOU 2636  N   ASP A 293     8157   8094   8151    131   -294    215       N  
ATOM   2637  CA  ASP A 293     -42.574 -22.325  -2.224  1.00 58.86           C  
ANISOU 2637  CA  ASP A 293     7429   7471   7465    159   -341    238       C  
ATOM   2638  C   ASP A 293     -42.884 -23.146  -3.463  1.00 45.32           C  
ANISOU 2638  C   ASP A 293     5706   5789   5725     74   -397    226       C  
ATOM   2639  O   ASP A 293     -43.912 -22.955  -4.128  1.00 47.01           O  
ANISOU 2639  O   ASP A 293     5841   6082   5938     59   -440    250       O  
ATOM   2640  CB  ASP A 293     -41.502 -21.294  -2.596  1.00 59.90           C  
ANISOU 2640  CB  ASP A 293     7621   7552   7585    228   -346    233       C  
ATOM   2641  CG  ASP A 293     -41.423 -20.119  -1.645  1.00 58.27           C  
ANISOU 2641  CG  ASP A 293     7412   7327   7402    322   -310    251       C  
ATOM   2642  OD1 ASP A 293     -42.161 -20.070  -0.642  1.00 59.31           O  
ANISOU 2642  OD1 ASP A 293     7498   7483   7553    345   -276    265       O  
ATOM   2643  OD2 ASP A 293     -40.591 -19.226  -1.916  1.00 59.62           O1-
ANISOU 2643  OD2 ASP A 293     7631   7453   7568    372   -315    250       O1-
ATOM   2644  H   ASP A 293     -41.356 -22.969  -0.803  1.00 77.89           H  
ATOM   2645  N   GLY A 294     -41.965 -24.051  -3.804  1.00 30.61           N  
ANISOU 2645  N   GLY A 294     3928   3864   3837     23   -401    188       N  
ATOM   2646  CA  GLY A 294     -42.100 -24.817  -5.026  1.00 21.01           C  
ANISOU 2646  CA  GLY A 294     2729   2666   2587    -52   -454    170       C  
ATOM   2647  C   GLY A 294     -43.336 -25.684  -5.016  1.00 18.63           C  
ANISOU 2647  C   GLY A 294     2360   2423   2297   -138   -477    175       C  
ATOM   2648  O   GLY A 294     -44.016 -25.830  -6.034  1.00 27.90           O  
ANISOU 2648  O   GLY A 294     3495   3655   3452   -184   -537    178       O  
ATOM   2649  H   GLY A 294     -41.261 -24.234  -3.345  1.00 37.55           H  
ATOM   2650  N   CYS A 295     -43.655 -26.255  -3.856  1.00 14.14           N  
ANISOU 2650  N   CYS A 295     1774   1840   1757   -164   -429    178       N  
ATOM   2651  CA  CYS A 295     -44.838 -27.093  -3.732  1.00 15.03           C  
ANISOU 2651  CA  CYS A 295     1817   2007   1887   -256   -441    188       C  
ATOM   2652  C   CYS A 295     -46.096 -26.267  -3.929  1.00 15.76           C  
ANISOU 2652  C   CYS A 295     1777   2209   2003   -231   -468    231       C  
ATOM   2653  O   CYS A 295     -46.987 -26.646  -4.703  1.00 17.59           O  
ANISOU 2653  O   CYS A 295     1944   2508   2231   -302   -526    235       O  
ATOM   2654  CB  CYS A 295     -44.826 -27.758  -2.355  1.00 27.00           C  
ANISOU 2654  CB  CYS A 295     3351   3481   3428   -275   -371    189       C  
ATOM   2655  SG  CYS A 295     -46.281 -28.713  -1.945  1.00 26.79           S  
ANISOU 2655  SG  CYS A 295     3230   3516   3432   -388   -364    211       S  
ATOM   2656  H   CYS A 295     -43.204 -26.173  -3.129  1.00 12.87           H  
ATOM   2657  N   ILE A 296     -46.159 -25.108  -3.279  1.00 28.71           N  
ANISOU 2657  N   ILE A 296     3377   3867   3664   -127   -432    261       N  
ATOM   2658  CA  ILE A 296     -47.315 -24.228  -3.416  1.00 19.08           C  
ANISOU 2658  CA  ILE A 296     2034   2750   2466    -81   -451    305       C  
ATOM   2659  C   ILE A 296     -47.546 -23.883  -4.879  1.00 23.75           C  
ANISOU 2659  C   ILE A 296     2604   3391   3028    -87   -536    307       C  
ATOM   2660  O   ILE A 296     -48.674 -23.957  -5.383  1.00 23.08           O  
ANISOU 2660  O   ILE A 296     2415   3401   2952   -124   -585    328       O  
ATOM   2661  CB  ILE A 296     -47.126 -22.957  -2.567  1.00 15.79           C  
ANISOU 2661  CB  ILE A 296     1610   2323   2067     46   -399    330       C  
ATOM   2662  CG1 ILE A 296     -47.300 -23.295  -1.089  1.00 15.76           C  
ANISOU 2662  CG1 ILE A 296     1598   2300   2090     50   -320    336       C  
ATOM   2663  CG2 ILE A 296     -48.117 -21.894  -3.015  1.00 26.60           C  
ANISOU 2663  CG2 ILE A 296     2873   3788   3447    114   -432    372       C  
ATOM   2664  CD1 ILE A 296     -46.929 -22.179  -0.136  1.00 16.42           C  
ANISOU 2664  CD1 ILE A 296     1706   2352   2182    171   -265    349       C  
ATOM   2665  H   ILE A 296     -45.548 -24.808  -2.754  1.00 35.27           H  
ATOM   2666  N   ALA A 297     -46.483 -23.480  -5.577  1.00 19.21           N  
ANISOU 2666  N   ALA A 297     2124   2757   2417    -48   -555    288       N  
ATOM   2667  CA  ALA A 297     -46.619 -23.063  -6.968  1.00 28.07           C  
ANISOU 2667  CA  ALA A 297     3241   3921   3502    -41   -630    293       C  
ATOM   2668  C   ALA A 297     -47.087 -24.218  -7.841  1.00 21.39           C  
ANISOU 2668  C   ALA A 297     2389   3107   2631   -159   -694    268       C  
ATOM   2669  O   ALA A 297     -47.976 -24.052  -8.681  1.00 29.42           O  
ANISOU 2669  O   ALA A 297     3333   4210   3636   -176   -764    286       O  
ATOM   2670  CB  ALA A 297     -45.286 -22.503  -7.467  1.00 15.47           C  
ANISOU 2670  CB  ALA A 297     1759   2247   1871     15   -623    278       C  
ATOM   2671  H   ALA A 297     -45.681 -23.442  -5.270  1.00 23.87           H  
ATOM   2672  N   ALA A 298     -46.499 -25.400  -7.644  1.00 33.28           N  
ANISOU 2672  N   ALA A 298     3974   4542   4127   -240   -674    226       N  
ATOM   2673  CA  ALA A 298     -46.911 -26.600  -8.368  1.00 26.75           C  
ANISOU 2673  CA  ALA A 298     3157   3729   3276   -360   -731    196       C  
ATOM   2674  C   ALA A 298     -48.404 -26.851  -8.249  1.00 18.61           C  
ANISOU 2674  C   ALA A 298     1989   2801   2280   -424   -766    222       C  
ATOM   2675  O   ALA A 298     -49.064 -27.241  -9.223  1.00 22.21           O  
ANISOU 2675  O   ALA A 298     2411   3315   2714   -494   -847    213       O  
ATOM   2676  CB  ALA A 298     -46.136 -27.803  -7.827  1.00 31.92           C  
ANISOU 2676  CB  ALA A 298     3915   4286   3928   -425   -686    154       C  
ATOM   2677  H   ALA A 298     -45.853 -25.535  -7.091  1.00 40.75           H  
ATOM   2678  N   MET A 299     -48.959 -26.652  -7.061  1.00 24.83           N  
ANISOU 2678  N   MET A 299     2696   3616   3123   -403   -706    254       N  
ATOM   2679  CA  MET A 299     -50.367 -26.952  -6.852  1.00 36.39           C  
ANISOU 2679  CA  MET A 299     4019   5180   4626   -468   -727    281       C  
ATOM   2680  C   MET A 299     -51.253 -25.850  -7.428  1.00 32.64           C  
ANISOU 2680  C   MET A 299     3423   4820   4157   -397   -780    324       C  
ATOM   2681  O   MET A 299     -52.318 -26.142  -7.984  1.00 22.89           O  
ANISOU 2681  O   MET A 299     2085   3681   2931   -465   -848    335       O  
ATOM   2682  CB  MET A 299     -50.612 -27.171  -5.359  1.00 26.55           C  
ANISOU 2682  CB  MET A 299     2735   3921   3431   -467   -633    302       C  
ATOM   2683  CG  MET A 299     -49.752 -28.293  -4.764  1.00 27.67           C  
ANISOU 2683  CG  MET A 299     3001   3949   3565   -533   -582    264       C  
ATOM   2684  SD  MET A 299     -50.491 -29.021  -3.292  1.00 48.43           S  
ANISOU 2684  SD  MET A 299     5567   6587   6247   -594   -498    290       S  
ATOM   2685  CE  MET A 299     -50.251 -27.717  -2.110  1.00 39.40           C  
ANISOU 2685  CE  MET A 299     4401   5446   5125   -435   -412    327       C  
ATOM   2686  H   MET A 299     -48.549 -26.349  -6.369  1.00 30.62           H  
ATOM   2687  N   ALA A 300     -50.817 -24.592  -7.341  1.00 28.23           N  
ANISOU 2687  N   ALA A 300     2882   4253   3593   -262   -756    347       N  
ATOM   2688  CA  ALA A 300     -51.510 -23.514  -8.043  1.00 31.17           C  
ANISOU 2688  CA  ALA A 300     3167   4719   3959   -183   -813    385       C  
ATOM   2689  C   ALA A 300     -51.469 -23.723  -9.552  1.00 20.97           C  
ANISOU 2689  C   ALA A 300     1909   3448   2609   -227   -916    365       C  
ATOM   2690  O   ALA A 300     -52.434 -23.410 -10.262  1.00 24.12           O  
ANISOU 2690  O   ALA A 300     2209   3953   3004   -225   -991    391       O  
ATOM   2691  CB  ALA A 300     -50.880 -22.167  -7.684  1.00 25.91           C  
ANISOU 2691  CB  ALA A 300     2543   4011   3290    -35   -765    409       C  
ATOM   2692  H   ALA A 300     -50.132 -24.340  -6.887  1.00 34.70           H  
ATOM   2693  N   ILE A 301     -50.338 -24.227 -10.056  1.00 39.14           N  
ANISOU 2693  N   ILE A 301     4355   5653   4863   -261   -918    320       N  
ATOM   2694  CA  ILE A 301     -50.167 -24.466 -11.487  1.00 25.67           C  
ANISOU 2694  CA  ILE A 301     2707   3956   3092   -299  -1007    296       C  
ATOM   2695  C   ILE A 301     -51.095 -25.583 -11.948  1.00 21.78           C  
ANISOU 2695  C   ILE A 301     2155   3523   2597   -435  -1081    274       C  
ATOM   2696  O   ILE A 301     -51.771 -25.465 -12.979  1.00 39.54           O  
ANISOU 2696  O   ILE A 301     4355   5853   4814   -454  -1176    281       O  
ATOM   2697  CB  ILE A 301     -48.695 -24.801 -11.786  1.00 24.75           C  
ANISOU 2697  CB  ILE A 301     2758   3718   2928   -299   -976    252       C  
ATOM   2698  CG1 ILE A 301     -47.788 -23.624 -11.419  1.00 32.24           C  
ANISOU 2698  CG1 ILE A 301     3758   4612   3880   -172   -912    275       C  
ATOM   2699  CG2 ILE A 301     -48.489 -25.152 -13.250  1.00 20.05           C  
ANISOU 2699  CG2 ILE A 301     2235   3126   2256   -341  -1059    223       C  
ATOM   2700  CD1 ILE A 301     -46.362 -24.024 -11.085  1.00 35.38           C  
ANISOU 2700  CD1 ILE A 301     4288   4891   4265   -173   -848    238       C  
ATOM   2701  H   ILE A 301     -49.650 -24.439  -9.586  1.00 47.79           H  
ATOM   2702  N   ASP A 302     -51.128 -26.690 -11.201  1.00 26.08           N  
ANISOU 2702  N   ASP A 302     2709   4026   3174   -535  -1041    249       N  
ATOM   2703  CA  ASP A 302     -52.051 -27.778 -11.516  1.00 28.82           C  
ANISOU 2703  CA  ASP A 302     2997   4425   3529   -678  -1105    230       C  
ATOM   2704  C   ASP A 302     -53.488 -27.274 -11.583  1.00 24.26           C  
ANISOU 2704  C   ASP A 302     2233   3993   2990   -674  -1158    277       C  
ATOM   2705  O   ASP A 302     -54.245 -27.661 -12.481  1.00 40.58           O  
ANISOU 2705  O   ASP A 302     4246   6134   5037   -754  -1260    267       O  
ATOM   2706  CB  ASP A 302     -51.902 -28.896 -10.478  1.00 37.48           C  
ANISOU 2706  CB  ASP A 302     4126   5451   4665   -771  -1035    208       C  
ATOM   2707  CG  ASP A 302     -52.954 -29.994 -10.619  1.00 37.45           C  
ANISOU 2707  CG  ASP A 302     4048   5499   4684   -928  -1090    196       C  
ATOM   2708  OD1 ASP A 302     -53.015 -30.655 -11.679  1.00 43.53           O  
ANISOU 2708  OD1 ASP A 302     4869   6265   5405  -1015  -1178    155       O  
ATOM   2709  OD2 ASP A 302     -53.711 -30.212  -9.647  1.00 44.19           O1-
ANISOU 2709  OD2 ASP A 302     4794   6394   5602   -968  -1043    226       O1-
ATOM   2710  H   ASP A 302     -50.631 -26.833 -10.514  1.00 32.11           H  
ATOM   2711  N   ARG A 303     -53.887 -26.406 -10.650  1.00 25.57           N  
ANISOU 2711  N   ARG A 303     2300   4206   3211   -580  -1094    328       N  
ATOM   2712  CA  ARG A 303     -55.248 -25.882 -10.706  1.00 27.91           C  
ANISOU 2712  CA  ARG A 303     2412   4648   3546   -562  -1139    377       C  
ATOM   2713  C   ARG A 303     -55.470 -25.072 -11.979  1.00 25.82           C  
ANISOU 2713  C   ARG A 303     2131   4451   3229   -494  -1240    391       C  
ATOM   2714  O   ARG A 303     -56.530 -25.161 -12.609  1.00 29.75           O  
ANISOU 2714  O   ARG A 303     2508   5064   3730   -540  -1333    405       O  
ATOM   2715  CB  ARG A 303     -55.561 -25.010  -9.492  1.00 37.05           C  
ANISOU 2715  CB  ARG A 303     3480   5835   4761   -451  -1044    429       C  
ATOM   2716  CG  ARG A 303     -56.912 -24.316  -9.665  1.00 34.26           C  
ANISOU 2716  CG  ARG A 303     2938   5638   4442   -404  -1092    483       C  
ATOM   2717  CD  ARG A 303     -57.363 -23.575  -8.434  1.00 46.82           C  
ANISOU 2717  CD  ARG A 303     4432   7268   6091   -302   -995    532       C  
ATOM   2718  NE  ARG A 303     -56.548 -22.389  -8.226  1.00 61.40           N  
ANISOU 2718  NE  ARG A 303     6368   9047   7914   -144   -946    545       N  
ATOM   2719  CZ  ARG A 303     -56.852 -21.403  -7.392  1.00 60.94           C  
ANISOU 2719  CZ  ARG A 303     6248   9018   7889    -16   -876    588       C  
ATOM   2720  NH1 ARG A 303     -57.966 -21.446  -6.673  1.00 55.47           N1+
ANISOU 2720  NH1 ARG A 303     5396   8427   7252    -17   -841    626       N1+
ATOM   2721  NH2 ARG A 303     -56.031 -20.370  -7.281  1.00 57.95           N  
ANISOU 2721  NH2 ARG A 303     5970   8563   7484    114   -840    593       N  
ATOM   2722  H   ARG A 303     -53.406 -26.115  -9.999  1.00 31.50           H  
ATOM   2723  HE  ARG A 303     -55.818 -22.322  -8.675  1.00 74.50           H  
ATOM   2724 HH11 ARG A 303     -58.499 -22.117  -6.745  1.00 67.38           H  
ATOM   2725 HH12 ARG A 303     -58.156 -20.802  -6.135  1.00 67.38           H  
ATOM   2726 HH21 ARG A 303     -55.309 -20.343  -7.747  1.00 70.36           H  
ATOM   2727 HH22 ARG A 303     -56.219 -19.727  -6.743  1.00 70.36           H  
ATOM   2728  N   PHE A 304     -54.475 -24.259 -12.346  1.00 39.67           N  
ANISOU 2728  N   PHE A 304     4002   6135   4935   -385  -1223    389       N  
ATOM   2729  CA  PHE A 304     -54.541 -23.377 -13.514  1.00 29.02           C  
ANISOU 2729  CA  PHE A 304     2661   4834   3530   -303  -1305    408       C  
ATOM   2730  C   PHE A 304     -54.617 -24.165 -14.808  1.00 25.93           C  
ANISOU 2730  C   PHE A 304     2319   4459   3073   -406  -1416    367       C  
ATOM   2731  O   PHE A 304     -55.496 -23.927 -15.648  1.00 42.00           O  
ANISOU 2731  O   PHE A 304     4293   6570   5095   -391  -1486    368       O  
ATOM   2732  CB  PHE A 304     -53.291 -22.489 -13.495  1.00 23.84           C  
ANISOU 2732  CB  PHE A 304     2142   4076   2842   -185  -1243    412       C  
ATOM   2733  CG  PHE A 304     -53.160 -21.557 -14.663  1.00 36.98           C  
ANISOU 2733  CG  PHE A 304     3845   5765   4441    -96  -1310    434       C  
ATOM   2734  CD1 PHE A 304     -54.114 -20.587 -14.899  1.00 40.01           C  
ANISOU 2734  CD1 PHE A 304     4117   6248   4836     -4  -1350    484       C  
ATOM   2735  CD2 PHE A 304     -52.049 -21.615 -15.495  1.00 39.08           C  
ANISOU 2735  CD2 PHE A 304     4268   5944   4635    -95  -1319    403       C  
ATOM   2736  CE1 PHE A 304     -53.981 -19.710 -15.958  1.00 42.09           C  
ANISOU 2736  CE1 PHE A 304     4446   6501   5044     87  -1388    492       C  
ATOM   2737  CE2 PHE A 304     -51.911 -20.740 -16.559  1.00 28.70           C  
ANISOU 2737  CE2 PHE A 304     2997   4650   3257    -12  -1374    429       C  
ATOM   2738  CZ  PHE A 304     -52.877 -19.786 -16.788  1.00 27.50           C  
ANISOU 2738  CZ  PHE A 304     2751   4578   3121     81  -1403    469       C  
ATOM   2739  H   PHE A 304     -53.728 -24.196 -11.924  1.00 48.42           H  
ATOM   2740  N   LEU A 305     -53.685 -25.105 -14.987  1.00 39.39           N  
ANISOU 2740  N   LEU A 305     4168   6056   4742   -488  -1399    310       N  
ATOM   2741  CA  LEU A 305     -53.536 -25.832 -16.229  1.00 25.85           C  
ANISOU 2741  CA  LEU A 305     2540   4329   2951   -570  -1491    261       C  
ATOM   2742  C   LEU A 305     -54.620 -26.880 -16.452  1.00 29.33           C  
ANISOU 2742  C   LEU A 305     2905   4820   3418   -698  -1542    227       C  
ATOM   2743  O   LEU A 305     -54.820 -27.314 -17.571  1.00 48.96           O  
ANISOU 2743  O   LEU A 305     5442   7309   5851   -738  -1611    184       O  
ATOM   2744  CB  LEU A 305     -52.177 -26.523 -16.268  1.00 24.76           C  
ANISOU 2744  CB  LEU A 305     2584   4051   2771   -603  -1438    208       C  
ATOM   2745  CG  LEU A 305     -50.950 -25.617 -16.341  1.00 30.08           C  
ANISOU 2745  CG  LEU A 305     3371   4645   3412   -477  -1371    220       C  
ATOM   2746  CD1 LEU A 305     -49.708 -26.487 -16.523  1.00 25.89           C  
ANISOU 2746  CD1 LEU A 305     3010   3991   2837   -523  -1331    161       C  
ATOM   2747  CD2 LEU A 305     -51.060 -24.583 -17.455  1.00 25.24           C  
ANISOU 2747  CD2 LEU A 305     2763   4090   2738   -385  -1439    251       C  
ATOM   2748  H   LEU A 305     -53.117 -25.339 -14.385  1.00 48.08           H  
ATOM   2749  N   ASN A 306     -55.288 -27.347 -15.401  1.00 31.36           N  
ANISOU 2749  N   ASN A 306     3050   5110   3754   -768  -1505    243       N  
ATOM   2750  CA  ASN A 306     -56.399 -28.259 -15.660  1.00 49.14           C  
ANISOU 2750  CA  ASN A 306     5222   7413   6035   -887  -1554    215       C  
ATOM   2751  C   ASN A 306     -57.741 -27.615 -15.330  1.00 41.64           C  
ANISOU 2751  C   ASN A 306     4077   6591   5152   -842  -1562    266       C  
ATOM   2752  O   ASN A 306     -58.764 -28.301 -15.355  1.00 48.09           O  
ANISOU 2752  O   ASN A 306     4801   7462   6010   -939  -1594    253       O  
ATOM   2753  CB  ASN A 306     -56.167 -29.598 -14.955  1.00 31.22           C  
ANISOU 2753  CB  ASN A 306     3002   5066   3794  -1031  -1512    180       C  
ATOM   2754  CG  ASN A 306     -54.966 -30.332 -15.568  1.00 37.71           C  
ANISOU 2754  CG  ASN A 306     4028   5760   4539  -1072  -1519    117       C  
ATOM   2755  ND2 ASN A 306     -54.038 -30.727 -14.701  1.00 36.68           N  
ANISOU 2755  ND2 ASN A 306     3984   5535   4418  -1096  -1446    110       N  
ATOM   2756  OD1 ASN A 306     -54.872 -30.539 -16.779  1.00 62.49           O  
ANISOU 2756  OD1 ASN A 306     7247   8885   7611  -1076  -1583     75       O  
ATOM   2757  H   ASN A 306     -55.126 -27.161 -14.578  1.00 38.45           H  
ATOM   2758 HD21 ASN A 306     -53.340 -31.145 -14.980  1.00 44.84           H  
ATOM   2759 HD22 ASN A 306     -54.137 -30.564 -13.862  1.00 44.84           H  
ATOM   2760  N   SER A 307     -57.755 -26.303 -15.096  1.00 35.92           N  
ANISOU 2760  N   SER A 307     3298   5912   4438   -693  -1536    320       N  
ATOM   2761  CA  SER A 307     -58.981 -25.542 -14.893  1.00 51.01           C  
ANISOU 2761  CA  SER A 307     5039   7939   6404   -621  -1542    367       C  
ATOM   2762  C   SER A 307     -59.832 -26.153 -13.787  1.00 45.72           C  
ANISOU 2762  C   SER A 307     4232   7318   5822   -707  -1489    385       C  
ATOM   2763  O   SER A 307     -61.031 -26.374 -13.941  1.00 55.47           O  
ANISOU 2763  O   SER A 307     5339   8639   7097   -750  -1526    389       O  
ATOM   2764  CB  SER A 307     -59.784 -25.443 -16.200  1.00 47.34           C  
ANISOU 2764  CB  SER A 307     4545   7538   5905   -618  -1650    346       C  
ATOM   2765  OG  SER A 307     -59.032 -24.841 -17.240  1.00 49.05           O  
ANISOU 2765  OG  SER A 307     4889   7712   6036   -533  -1693    333       O  
ATOM   2766  H   SER A 307     -57.045 -25.821 -15.047  1.00 43.92           H  
ATOM   2767  HG  SER A 307     -59.494 -24.797 -17.940  1.00 59.68           H  
ATOM   2768  N   ARG A 308     -59.185 -26.432 -12.657  1.00 40.54           N  
ANISOU 2768  N   ARG A 308     3604   6605   5194   -731  -1399    398       N  
ATOM   2769  CA  ARG A 308     -59.858 -27.075 -11.541  1.00 33.43           C  
ANISOU 2769  CA  ARG A 308     2592   5737   4371   -817  -1334    418       C  
ATOM   2770  C   ARG A 308     -60.701 -26.071 -10.758  1.00 39.93           C  
ANISOU 2770  C   ARG A 308     3258   6659   5256   -698  -1275    482       C  
ATOM   2771  O   ARG A 308     -60.493 -24.854 -10.818  1.00 46.74           O  
ANISOU 2771  O   ARG A 308     4124   7535   6101   -541  -1262    513       O  
ATOM   2772  CB  ARG A 308     -58.848 -27.748 -10.607  1.00 41.84           C  
ANISOU 2772  CB  ARG A 308     3753   6702   5441   -883  -1259    408       C  
ATOM   2773  CG  ARG A 308     -58.010 -28.841 -11.270  1.00 39.68           C  
ANISOU 2773  CG  ARG A 308     3649   6318   5111  -1002  -1304    340       C  
ATOM   2774  CD  ARG A 308     -57.157 -29.572 -10.247  1.00 47.57           C  
ANISOU 2774  CD  ARG A 308     4759   7190   6124  -1048  -1200    320       C  
ATOM   2775  NE  ARG A 308     -56.321 -30.617 -10.836  1.00 46.09           N  
ANISOU 2775  NE  ARG A 308     4745   6886   5881  -1146  -1232    253       N  
ATOM   2776  CZ  ARG A 308     -56.759 -31.825 -11.171  1.00 45.92           C  
ANISOU 2776  CZ  ARG A 308     4731   6855   5861  -1311  -1286    217       C  
ATOM   2777  NH1 ARG A 308     -58.033 -32.142 -10.987  1.00 51.12           N1+
ANISOU 2777  NH1 ARG A 308     5248   7597   6578  -1376  -1291    235       N1+
ATOM   2778  NH2 ARG A 308     -55.924 -32.716 -11.690  1.00 47.81           N  
ANISOU 2778  NH2 ARG A 308     5147   6975   6044  -1376  -1304    154       N  
ATOM   2779  H   ARG A 308     -58.355 -26.257 -12.514  1.00 49.46           H  
ATOM   2780  HE  ARG A 308     -55.491 -30.437 -10.974  1.00 56.13           H  
ATOM   2781 HH11 ARG A 308     -58.576 -31.567 -10.651  1.00 62.16           H  
ATOM   2782 HH12 ARG A 308     -58.318 -32.925 -11.205  1.00 62.16           H  
ATOM   2783 HH21 ARG A 308     -55.098 -32.511 -11.810  1.00 58.19           H  
ATOM   2784 HH22 ARG A 308     -56.210 -33.498 -11.907  1.00 58.19           H  
ATOM   2785  N   LYS A 309     -61.647 -26.617  -9.985  1.00 53.20           N  
ANISOU 2785  N   LYS A 309     4810   8397   7007   -775  -1229    500       N  
ATOM   2786  CA  LYS A 309     -62.529 -25.809  -9.156  1.00 56.32           C  
ANISOU 2786  CA  LYS A 309     5054   8884   7461   -673  -1160    558       C  
ATOM   2787  C   LYS A 309     -61.830 -25.349  -7.891  1.00 54.75           C  
ANISOU 2787  C   LYS A 309     4879   8645   7280   -590  -1043    594       C  
ATOM   2788  O   LYS A 309     -62.116 -24.257  -7.384  1.00 61.63           O  
ANISOU 2788  O   LYS A 309     5688   9560   8170   -440   -988    637       O  
ATOM   2789  CB  LYS A 309     -63.755 -26.640  -8.756  1.00 58.74           C  
ANISOU 2789  CB  LYS A 309     5220   9263   7836   -793  -1145    564       C  
ATOM   2790  CG  LYS A 309     -64.570 -27.143  -9.932  1.00 66.65           C  
ANISOU 2790  CG  LYS A 309     6180  10313   8831   -880  -1262    528       C  
ATOM   2791  CD  LYS A 309     -65.877 -27.798  -9.506  1.00 71.72           C  
ANISOU 2791  CD  LYS A 309     6664  11038   9549   -982  -1245    542       C  
ATOM   2792  CE  LYS A 309     -66.419 -28.697 -10.611  1.00 73.89           C  
ANISOU 2792  CE  LYS A 309     6937  11324   9813  -1117  -1361    490       C  
ATOM   2793  NZ  LYS A 309     -65.448 -29.768 -10.982  1.00 70.13           N1+
ANISOU 2793  NZ  LYS A 309     6634  10724   9287  -1243  -1388    432       N1+
ATOM   2794  H   LYS A 309     -61.797 -27.462  -9.926  1.00 64.66           H  
ATOM   2795  HZ1 LYS A 309     -65.854 -30.389 -11.474  1.00 84.97           H  
ATOM   2796  HZ2 LYS A 309     -64.777 -29.421 -11.452  1.00 84.97           H  
ATOM   2797  HZ3 LYS A 309     -65.120 -30.149 -10.248  1.00 84.97           H  
ATOM   2798  N   ALA A 310     -60.847 -26.123  -7.443  1.00 44.62           N  
ANISOU 2798  N   ALA A 310     3702   7268   5983   -677  -1010    574       N  
ATOM   2799  CA  ALA A 310     -60.152 -25.864  -6.198  1.00 46.98           C  
ANISOU 2799  CA  ALA A 310     4067   7488   6296   -604   -882    588       C  
ATOM   2800  C   ALA A 310     -58.738 -26.419  -6.282  1.00 32.64           C  
ANISOU 2800  C   ALA A 310     2472   5503   4427   -639   -865    529       C  
ATOM   2801  O   ALA A 310     -58.412 -27.215  -7.167  1.00 30.98           O  
ANISOU 2801  O   ALA A 310     2341   5249   4181   -747   -943    483       O  
ATOM   2802  CB  ALA A 310     -60.907 -26.498  -5.024  1.00 39.19           C  
ANISOU 2802  CB  ALA A 310     2970   6545   5377   -680   -791    618       C  
ATOM   2803  H   ALA A 310     -60.560 -26.821  -7.855  1.00 54.36           H  
ATOM   2804  N   ILE A 311     -57.895 -25.988  -5.340  1.00 31.00           N  
ANISOU 2804  N   ILE A 311     2363   5201   4215   -542   -761    530       N  
ATOM   2805  CA  ILE A 311     -56.573 -26.585  -5.215  1.00 26.71           C  
ANISOU 2805  CA  ILE A 311     2014   4503   3633   -575   -730    479       C  
ATOM   2806  C   ILE A 311     -56.740 -28.049  -4.838  1.00 32.01           C  
ANISOU 2806  C   ILE A 311     2702   5137   4325   -743   -711    457       C  
ATOM   2807  O   ILE A 311     -57.504 -28.380  -3.919  1.00 44.91           O  
ANISOU 2807  O   ILE A 311     4234   6818   6010   -786   -646    491       O  
ATOM   2808  CB  ILE A 311     -55.725 -25.852  -4.165  1.00 27.00           C  
ANISOU 2808  CB  ILE A 311     2136   4455   3666   -443   -625    487       C  
ATOM   2809  CG1 ILE A 311     -55.559 -24.367  -4.500  1.00 30.48           C  
ANISOU 2809  CG1 ILE A 311     2570   4922   4089   -278   -641    510       C  
ATOM   2810  CG2 ILE A 311     -54.388 -26.575  -4.014  1.00 29.30           C  
ANISOU 2810  CG2 ILE A 311     2615   4596   3922   -485   -597    435       C  
ATOM   2811  CD1 ILE A 311     -54.541 -24.050  -5.569  1.00 40.12           C  
ANISOU 2811  CD1 ILE A 311     3922   6071   5250   -247   -705    476       C  
ATOM   2812  H   ILE A 311     -58.065 -25.363  -4.775  1.00 38.02           H  
ATOM   2813  N   LYS A 312     -56.014 -28.937  -5.525  1.00 36.26           N  
ANISOU 2813  N   LYS A 312     3374   5583   4820   -837   -760    402       N  
ATOM   2814  CA  LYS A 312     -56.132 -30.362  -5.248  1.00 31.25           C  
ANISOU 2814  CA  LYS A 312     2776   4899   4200  -1000   -748    378       C  
ATOM   2815  C   LYS A 312     -54.919 -30.859  -4.478  1.00 27.96           C  
ANISOU 2815  C   LYS A 312     2531   4331   3762   -987   -664    349       C  
ATOM   2816  O   LYS A 312     -53.792 -30.798  -4.999  1.00 35.82           O  
ANISOU 2816  O   LYS A 312     3671   5234   4704   -944   -684    308       O  
ATOM   2817  CB  LYS A 312     -56.289 -31.167  -6.532  1.00 36.23           C  
ANISOU 2817  CB  LYS A 312     3436   5532   4798  -1128   -866    334       C  
ATOM   2818  CG  LYS A 312     -56.703 -32.609  -6.248  1.00 41.21           C  
ANISOU 2818  CG  LYS A 312     4074   6129   5455  -1310   -861    317       C  
ATOM   2819  CD  LYS A 312     -55.967 -33.611  -7.115  1.00 38.09           C  
ANISOU 2819  CD  LYS A 312     3845   5626   5002  -1407   -924    249       C  
ATOM   2820  CE  LYS A 312     -56.789 -34.000  -8.327  1.00 35.69           C  
ANISOU 2820  CE  LYS A 312     3474   5401   4686  -1522  -1057    228       C  
ATOM   2821  NZ  LYS A 312     -56.642 -35.453  -8.610  1.00 44.46           N1+
ANISOU 2821  NZ  LYS A 312     4698   6415   5778  -1686  -1086    174       N1+
ATOM   2822  H   LYS A 312     -55.453 -28.737  -6.146  1.00 44.33           H  
ATOM   2823  HZ1 LYS A 312     -57.126 -35.674  -9.322  1.00 54.16           H  
ATOM   2824  HZ2 LYS A 312     -55.788 -35.647  -8.769  1.00 54.16           H  
ATOM   2825  HZ3 LYS A 312     -56.921 -35.928  -7.911  1.00 54.16           H  
ATOM   2826  N   PRO A 313     -55.113 -31.406  -3.282  1.00 32.71           N  
ANISOU 2826  N   PRO A 313     3122   4906   4400  -1028   -571    370       N  
ATOM   2827  CA  PRO A 313     -53.982 -31.928  -2.512  1.00 33.10           C  
ANISOU 2827  CA  PRO A 313     3335   4814   4426  -1014   -495    344       C  
ATOM   2828  C   PRO A 313     -53.421 -33.199  -3.126  1.00 31.89           C  
ANISOU 2828  C   PRO A 313     3317   4560   4239  -1138   -540    289       C  
ATOM   2829  O   PRO A 313     -54.127 -33.968  -3.781  1.00 27.11           O  
ANISOU 2829  O   PRO A 313     2670   3989   3642  -1273   -607    277       O  
ATOM   2830  CB  PRO A 313     -54.599 -32.203  -1.137  1.00 24.24           C  
ANISOU 2830  CB  PRO A 313     2145   3712   3353  -1036   -391    389       C  
ATOM   2831  CG  PRO A 313     -56.028 -32.565  -1.471  1.00 39.00           C  
ANISOU 2831  CG  PRO A 313     3845   5704   5269  -1154   -434    419       C  
ATOM   2832  CD  PRO A 313     -56.403 -31.665  -2.617  1.00 32.70           C  
ANISOU 2832  CD  PRO A 313     2958   5005   4461  -1098   -533    419       C  
ATOM   2833  N   ASP A 314     -52.129 -33.409  -2.902  1.00 28.05           N  
ANISOU 2833  N   ASP A 314     2996   3947   3713  -1087   -505    255       N  
ATOM   2834  CA  ASP A 314     -51.396 -34.598  -3.331  1.00 34.49           C  
ANISOU 2834  CA  ASP A 314     3966   4647   4490  -1177   -529    202       C  
ATOM   2835  C   ASP A 314     -51.088 -35.431  -2.082  1.00 22.35           C  
ANISOU 2835  C   ASP A 314     2506   3019   2967  -1210   -434    210       C  
ATOM   2836  O   ASP A 314     -50.025 -35.289  -1.473  1.00 38.89           O  
ANISOU 2836  O   ASP A 314     4709   5028   5040  -1119   -377    200       O  
ATOM   2837  CB  ASP A 314     -50.124 -34.178  -4.088  1.00 24.11           C  
ANISOU 2837  CB  ASP A 314     2777   3266   3118  -1083   -561    159       C  
ATOM   2838  CG  ASP A 314     -49.353 -35.353  -4.653  1.00 31.89           C  
ANISOU 2838  CG  ASP A 314     3922   4136   4057  -1160   -589    101       C  
ATOM   2839  OD1 ASP A 314     -49.855 -36.492  -4.575  1.00 36.43           O  
ANISOU 2839  OD1 ASP A 314     4516   4682   4643  -1294   -596     91       O  
ATOM   2840  OD2 ASP A 314     -48.238 -35.137  -5.174  1.00 32.04           O1-
ANISOU 2840  OD2 ASP A 314     4051   4094   4030  -1086   -600     67       O1-
ATOM   2841  H   ASP A 314     -51.629 -32.848  -2.484  1.00 34.47           H  
ATOM   2842  N   TRP A 315     -52.024 -36.303  -1.705  1.00 23.55           N  
ANISOU 2842  N   TRP A 315     2602   3190   3155  -1343   -418    230       N  
ATOM   2843  CA  TRP A 315     -51.897 -37.193  -0.555  1.00 23.70           C  
ANISOU 2843  CA  TRP A 315     2691   3126   3187  -1393   -329    244       C  
ATOM   2844  C   TRP A 315     -51.742 -38.638  -1.025  1.00 28.76           C  
ANISOU 2844  C   TRP A 315     3451   3668   3808  -1539   -364    202       C  
ATOM   2845  O   TRP A 315     -52.085 -38.981  -2.160  1.00 43.24           O  
ANISOU 2845  O   TRP A 315     5275   5523   5630  -1628   -458    169       O  
ATOM   2846  CB  TRP A 315     -53.118 -37.058   0.371  1.00 24.68           C  
ANISOU 2846  CB  TRP A 315     2659   3347   3371  -1431   -265    309       C  
ATOM   2847  CG  TRP A 315     -53.214 -35.727   1.089  1.00 24.07           C  
ANISOU 2847  CG  TRP A 315     2489   3347   3310  -1276   -207    351       C  
ATOM   2848  CD1 TRP A 315     -52.387 -34.650   0.935  1.00 22.82           C  
ANISOU 2848  CD1 TRP A 315     2368   3181   3122  -1123   -216    337       C  
ATOM   2849  CD2 TRP A 315     -54.188 -35.341   2.072  1.00 24.78           C  
ANISOU 2849  CD2 TRP A 315     2440   3529   3447  -1262   -129    414       C  
ATOM   2850  CE2 TRP A 315     -53.888 -34.022   2.465  1.00 23.89           C  
ANISOU 2850  CE2 TRP A 315     2297   3455   3327  -1091    -98    430       C  
ATOM   2851  CE3 TRP A 315     -55.283 -35.986   2.659  1.00 27.18           C  
ANISOU 2851  CE3 TRP A 315     2645   3886   3798  -1377    -80    458       C  
ATOM   2852  NE1 TRP A 315     -52.782 -33.624   1.758  1.00 46.51           N  
ANISOU 2852  NE1 TRP A 315     5271   6255   6147  -1014   -154    383       N  
ATOM   2853  CZ2 TRP A 315     -54.639 -33.334   3.415  1.00 27.65           C  
ANISOU 2853  CZ2 TRP A 315     2652   4018   3836  -1023    -18    487       C  
ATOM   2854  CZ3 TRP A 315     -56.029 -35.302   3.604  1.00 26.59           C  
ANISOU 2854  CZ3 TRP A 315     2440   3905   3758  -1311      4    518       C  
ATOM   2855  CH2 TRP A 315     -55.704 -33.989   3.971  1.00 29.32           C  
ANISOU 2855  CH2 TRP A 315     2764   4286   4091  -1131     33    530       C  
ATOM   2856  H   TRP A 315     -52.771 -36.401  -2.118  1.00 24.17           H  
ATOM   2857  HE1 TRP A 315     -52.399 -32.857   1.819  1.00 56.64           H  
ATOM   2858  N   ALA A 316     -51.213 -39.488  -0.143  1.00 46.88           N  
ANISOU 2858  N   ALA A 316     5869   5849   6094  -1561   -291    202       N  
ATOM   2859  CA  ALA A 316     -50.988 -40.892  -0.481  1.00 61.65           C  
ANISOU 2859  CA  ALA A 316     7877   7606   7942  -1690   -315    163       C  
ATOM   2860  C   ALA A 316     -52.306 -41.643  -0.643  1.00 76.32           C  
ANISOU 2860  C   ALA A 316     9640   9513   9844  -1873   -341    181       C  
ATOM   2861  O   ALA A 316     -53.230 -41.474   0.155  1.00 81.70           O  
ANISOU 2861  O   ALA A 316    10192  10273  10578  -1907   -284    240       O  
ATOM   2862  CB  ALA A 316     -50.153 -41.568   0.606  1.00 66.84           C  
ANISOU 2862  CB  ALA A 316     8684   8133   8581  -1658   -224    167       C  
ATOM   2863  H   ALA A 316     -50.976 -39.276   0.656  1.00 57.07           H  
ATOM   2864  N   HIS A 317     -52.380 -42.495  -1.671  1.00 90.23           N  
ANISOU 2864  N   HIS A 317    11471  11228  11584  -1994   -426    131       N  
ATOM   2865  CA  HIS A 317     -53.594 -43.265  -1.964  1.00 90.90           C  
ANISOU 2865  CA  HIS A 317    11473  11357  11707  -2116   -453    134       C  
ATOM   2866  C   HIS A 317     -53.598 -44.619  -1.254  1.00 91.16           C  
ANISOU 2866  C   HIS A 317    11617  11272  11746  -2181   -385    135       C  
ATOM   2867  O   HIS A 317     -54.010 -45.632  -1.826  1.00 88.71           O  
ANISOU 2867  O   HIS A 317    11348  10923  11434  -2268   -425    102       O  
ATOM   2868  CB  HIS A 317     -53.752 -43.499  -3.474  1.00 97.21           C  
ANISOU 2868  CB  HIS A 317    12288  12173  12474  -2145   -570     74       C  
ATOM   2869  CG  HIS A 317     -53.854 -42.244  -4.281  1.00103.71           C  
ANISOU 2869  CG  HIS A 317    13002  13116  13288  -2083   -647     74       C  
ATOM   2870  CD2 HIS A 317     -54.828 -41.306  -4.351  1.00103.87           C  
ANISOU 2870  CD2 HIS A 317    12819  13293  13352  -2083   -676    117       C  
ATOM   2871  ND1 HIS A 317     -52.865 -41.841  -5.154  1.00105.34           N  
ANISOU 2871  ND1 HIS A 317    13308  13285  13430  -1998   -701     27       N  
ATOM   2872  CE1 HIS A 317     -53.228 -40.704  -5.728  1.00107.48           C  
ANISOU 2872  CE1 HIS A 317    13450  13683  13706  -1953   -764     42       C  
ATOM   2873  NE2 HIS A 317     -54.407 -40.360  -5.256  1.00106.05           N  
ANISOU 2873  NE2 HIS A 317    13085  13621  13590  -1998   -751     97       N  
ATOM   2874  H   HIS A 317     -51.734 -42.648  -2.218  1.00109.10           H  
ATOM   2875  HE2 HIS A 317     -54.845 -39.654  -5.478  1.00128.08           H  
TER    2876      HIS A 317 
HETATM 2877  P   FAD A 401     -33.480 -22.084  -4.631  1.00 13.63           P  
HETATM 2878  PA  FAD A 401     -30.687 -22.347  -5.442  1.00 18.21           P  
HETATM 2879  O1P FAD A 401     -33.956 -23.279  -5.463  1.00 19.82           O1-
HETATM 2880  O2P FAD A 401     -34.406 -20.923  -4.543  1.00 22.95           O  
HETATM 2881  O3P FAD A 401     -32.067 -21.604  -5.199  1.00 16.78           O  
HETATM 2882  C5' FAD A 401     -32.555 -21.702  -2.208  1.00 52.86           C  
HETATM 2883  O5' FAD A 401     -33.138 -22.589  -3.183  1.00 37.49           O  
HETATM 2884  C4' FAD A 401     -31.839 -22.523  -1.159  1.00 68.82           C  
HETATM 2885  O4' FAD A 401     -30.833 -23.325  -1.776  1.00 92.90           O  
HETATM 2886  C3' FAD A 401     -31.207 -21.648  -0.076  1.00 65.05           C  
HETATM 2887  O3' FAD A 401     -32.234 -20.908   0.569  1.00 63.09           O  
HETATM 2888  C2' FAD A 401     -30.457 -22.494   0.952  1.00 63.78           C  
HETATM 2889  O2' FAD A 401     -29.373 -23.160   0.319  1.00 78.55           O  
HETATM 2890  C1' FAD A 401     -29.884 -21.596   2.020  1.00 54.67           C  
HETATM 2891  C1B FAD A 401     -29.940 -22.371 -11.381  1.00 49.21           C  
HETATM 2892  N1  FAD A 401     -30.354 -23.443   3.963  1.00 38.46           N  
HETATM 2893  N1A FAD A 401     -30.864 -20.608 -16.110  1.00 56.69           N  
HETATM 2894  O1A FAD A 401     -30.470 -23.407  -4.427  1.00 31.91           O1-
HETATM 2895  C2  FAD A 401     -30.632 -24.357   4.941  1.00 36.39           C  
HETATM 2896  C2A FAD A 401     -31.024 -21.816 -15.565  1.00 47.92           C  
HETATM 2897  C2B FAD A 401     -28.688 -22.554 -10.533  1.00 53.01           C  
HETATM 2898  O2  FAD A 401     -31.790 -24.695   5.206  1.00 35.42           O  
HETATM 2899  O2A FAD A 401     -29.609 -21.258  -5.513  1.00 15.46           O  
HETATM 2900  O2B FAD A 401     -27.620 -23.139 -11.272  1.00 53.64           O  
HETATM 2901  C3B FAD A 401     -29.246 -23.460  -9.430  1.00 57.37           C  
HETATM 2902  N3  FAD A 401     -29.598 -24.929   5.661  1.00 45.12           N  
HETATM 2903  N3A FAD A 401     -30.772 -22.201 -14.313  1.00 49.84           N  
HETATM 2904  O3B FAD A 401     -29.221 -24.820  -9.847  1.00 65.23           O  
HETATM 2905  C4  FAD A 401     -28.261 -24.669   5.496  1.00 58.56           C  
HETATM 2906  C4A FAD A 401     -30.278 -21.194 -13.585  1.00 62.44           C  
HETATM 2907  C4B FAD A 401     -30.691 -22.973  -9.275  1.00 42.93           C  
HETATM 2908  C4X FAD A 401     -27.970 -23.703   4.462  1.00 53.61           C  
HETATM 2909  O4  FAD A 401     -27.424 -25.237   6.193  1.00 89.58           O  
HETATM 2910  O4B FAD A 401     -30.980 -22.185 -10.452  1.00 40.86           O  
HETATM 2911  C5A FAD A 401     -30.058 -19.896 -14.009  1.00 69.99           C  
HETATM 2912  C5B FAD A 401     -30.950 -22.138  -8.044  1.00 27.85           C  
HETATM 2913  C5X FAD A 401     -26.442 -22.485   3.265  1.00 48.49           C  
HETATM 2914  N5  FAD A 401     -26.733 -23.407   4.248  1.00 53.03           N  
HETATM 2915  O5B FAD A 401     -30.826 -22.970  -6.874  1.00 22.78           O  
HETATM 2916  C6  FAD A 401     -25.106 -22.158   3.036  1.00 32.92           C  
HETATM 2917  C6A FAD A 401     -30.373 -19.606 -15.349  1.00 68.53           C  
HETATM 2918  N6A FAD A 401     -30.213 -18.403 -15.903  1.00 70.11           N  
HETATM 2919  C7  FAD A 401     -24.752 -21.241   2.055  1.00 24.27           C  
HETATM 2920  C7M FAD A 401     -23.299 -20.918   1.831  1.00 20.27           C  
HETATM 2921  N7A FAD A 401     -29.550 -19.122 -12.976  1.00 88.99           N  
HETATM 2922  C8  FAD A 401     -25.757 -20.625   1.290  1.00 28.25           C  
HETATM 2923  C8A FAD A 401     -29.478 -19.958 -11.969  1.00 70.43           C  
HETATM 2924  C8M FAD A 401     -25.411 -19.622   0.223  1.00 24.61           C  
HETATM 2925  C9  FAD A 401     -27.092 -20.945   1.521  1.00 37.47           C  
HETATM 2926  C9A FAD A 401     -27.441 -21.870   2.498  1.00 44.14           C  
HETATM 2927  N9A FAD A 401     -29.902 -21.223 -12.267  1.00 62.67           N  
HETATM 2928  C10 FAD A 401     -29.083 -23.143   3.740  1.00 44.43           C  
HETATM 2929  N10 FAD A 401     -28.784 -22.215   2.768  1.00 48.79           N  
HETATM 2930  HN3 FAD A 401     -29.813 -25.507   6.274  1.00 54.96           H  
HETATM 2931 HO2' FAD A 401     -29.453 -23.977   0.448  1.00 95.08           H  
HETATM 2932 HO2A FAD A 401     -27.007 -22.580 -11.349  1.00 65.19           H  
HETATM 2933 HO3A FAD A 401     -28.774 -25.271  -9.311  1.00 79.09           H  
HETATM 2934 HO4' FAD A 401     -31.169 -24.039  -2.041  1.00112.30           H  
HETATM 2935 H61A FAD A 401     -29.904 -17.745 -15.430  1.00 84.95           H  
HETATM 2936 H62A FAD A 401     -30.417 -18.282 -16.738  1.00 84.95           H  
CONECT 2877 2879 2880 2881 2883
CONECT 2878 2881 2894 2899 2915
CONECT 2879 2877
CONECT 2880 2877
CONECT 2881 2877 2878
CONECT 2882 2883 2884
CONECT 2883 2877 2882
CONECT 2884 2882 2885 2886
CONECT 2885 2884 2934
CONECT 2886 2884 2887 2888
CONECT 2887 2886
CONECT 2888 2886 2889 2890
CONECT 2889 2888 2931
CONECT 2890 2888 2929
CONECT 2891 2897 2910 2927
CONECT 2892 2895 2928
CONECT 2893 2896 2917
CONECT 2894 2878
CONECT 2895 2892 2898 2902
CONECT 2896 2893 2903
CONECT 2897 2891 2900 2901
CONECT 2898 2895
CONECT 2899 2878
CONECT 2900 2897 2932
CONECT 2901 2897 2904 2907
CONECT 2902 2895 2905 2930
CONECT 2903 2896 2906
CONECT 2904 2901 2933
CONECT 2905 2902 2908 2909
CONECT 2906 2903 2911 2927
CONECT 2907 2901 2910 2912
CONECT 2908 2905 2914 2928
CONECT 2909 2905
CONECT 2910 2891 2907
CONECT 2911 2906 2917 2921
CONECT 2912 2907 2915
CONECT 2913 2914 2916 2926
CONECT 2914 2908 2913
CONECT 2915 2878 2912
CONECT 2916 2913 2919
CONECT 2917 2893 2911 2918
CONECT 2918 2917 2935 2936
CONECT 2919 2916 2920 2922
CONECT 2920 2919
CONECT 2921 2911 2923
CONECT 2922 2919 2924 2925
CONECT 2923 2921 2927
CONECT 2924 2922
CONECT 2925 2922 2926
CONECT 2926 2913 2925 2929
CONECT 2927 2891 2906 2923
CONECT 2928 2892 2908 2929
CONECT 2929 2890 2926 2928
CONECT 2930 2902
CONECT 2931 2889
CONECT 2932 2900
CONECT 2933 2904
CONECT 2934 2885
CONECT 2935 2918
CONECT 2936 2918
END



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.