CNRS Nantes University UFIP UFIP
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***  fg32  ***

elNémo ID: 21050823393011762

Job options:

ID        	=	 21050823393011762
JOBID     	=	 fg32
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 25
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 2
CUTOFF    	=	 12
CAONLY    	=	 0


Input data for this run:

HEADER fg32

HEADER    ----                                    03-AUG-20   xxxx
TITLE     ---
REMARK   3  R VALUE : 0.127360
REMARK   3  FREE R VALUE : 0.188540
REMARK   4 xxxx COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 888
REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC)
CRYST1   47.621   98.726   66.492  90.00 105.99  90.00 P 1 21 1      0
ATOM      1  N   ASP A 449       3.941  25.108  35.438  1.00 60.46           N1+
ANISOU    1  N   ASP A 449    11138   7766   4065   -156   3696  -4669
ATOM      2  CA  ASP A 449       4.844  25.783  34.431  1.00 42.58           C  
ANISOU    2  CA  ASP A 449     4513   6627   5038  -1407   -911  -3412
ATOM      3  C   ASP A 449       4.409  25.294  33.031  1.00 32.30           C  
ANISOU    3  C   ASP A 449     4977   3652   3641    266    736  -1350
ATOM      4  O   ASP A 449       4.048  26.130  32.202  1.00 38.49           O  
ANISOU    4  O   ASP A 449     5310   2667   6647  -1016   -515    -58
ATOM      5  CB  ASP A 449       6.372  25.583  34.665  1.00  0.00           C  
ATOM      6  CG  ASP A 449       6.929  26.067  36.011  1.00  0.00           C  
ATOM      7  OD1 ASP A 449       7.839  25.497  36.607  1.00  0.00           O  
ATOM      8  OD2 ASP A 449       6.330  27.207  36.457  1.00  0.00           O  
ATOM      9  H1  ASP A 449       2.985  25.386  35.263  1.00  0.00           H  
ATOM     10  H2  ASP A 449       4.034  24.105  35.368  1.00  0.00           H  
ATOM     11  H3  ASP A 449       4.209  25.407  36.365  1.00  0.00           H  
ATOM     12  HA  ASP A 449       4.576  26.837  34.526  1.00  0.00           H  
ATOM     13  HB2 ASP A 449       6.642  24.530  34.558  1.00  0.00           H  
ATOM     14  HB3 ASP A 449       6.928  26.111  33.889  1.00  0.00           H  
ATOM     15  HD2 ASP A 449       6.706  27.516  37.285  1.00  0.00           H  
ATOM     16  N   TRP A 450       4.503  23.975  32.767  1.00 27.52           N  
ANISOU   16  N   TRP A 450     3252   3551   3650   -123    391  -1022
ATOM     17  CA  TRP A 450       4.123  23.354  31.497  1.00 23.03           C  
ANISOU   17  CA  TRP A 450     3584   2757   2407   -139    668   -155
ATOM     18  C   TRP A 450       2.717  22.749  31.527  1.00 25.30           C  
ANISOU   18  C   TRP A 450     3551   3635   2424   -123    608  -1170
ATOM     19  O   TRP A 450       2.286  22.222  30.501  1.00 24.72           O  
ANISOU   19  O   TRP A 450     3451   3818   2121  -1052    764   -770
ATOM     20  CB  TRP A 450       5.186  22.322  31.086  1.00 23.23           C  
ANISOU   20  CB  TRP A 450     3382   3062   2380     24   -406   -368
ATOM     21  CG  TRP A 450       6.553  22.906  30.968  1.00 20.19           C  
ANISOU   21  CG  TRP A 450     3420   2265   1985   -213    -14   -142
ATOM     22  CD1 TRP A 450       7.601  22.631  31.775  1.00 25.22           C  
ANISOU   22  CD1 TRP A 450     3865   3040   2676   -220   -537     31
ATOM     23  NE1 TRP A 450       8.664  23.437  31.433  1.00 25.47           N  
ANISOU   23  NE1 TRP A 450     3287   3765   2623    205   -403    966
ATOM     24  CE2 TRP A 450       8.355  24.264  30.374  1.00 19.74           C  
ANISOU   24  CE2 TRP A 450     2992   2450   2057    354   -209    133
ATOM     25  CD2 TRP A 450       7.002  23.950  30.056  1.00 21.09           C  
ANISOU   25  CD2 TRP A 450     3447   1998   2569   -308    -16    -96
ATOM     26  CE3 TRP A 450       6.399  24.683  29.003  1.00 21.88           C  
ANISOU   26  CE3 TRP A 450     3461   3042   1808    383    763   -342
ATOM     27  CZ3 TRP A 450       7.115  25.670  28.299  1.00 20.47           C  
ANISOU   27  CZ3 TRP A 450     3295   2809   1671    202    260   -373
ATOM     28  CH2 TRP A 450       8.458  25.937  28.628  1.00 19.15           C  
ANISOU   28  CH2 TRP A 450     3029   2171   2076   -125    499   -399
ATOM     29  CZ2 TRP A 450       9.081  25.235  29.674  1.00 21.90           C  
ANISOU   29  CZ2 TRP A 450     2927   2476   2916   -330   -176   -365
ATOM     30  H   TRP A 450       4.860  23.343  33.468  1.00  0.00           H  
ATOM     31  HA  TRP A 450       4.097  24.117  30.719  1.00  0.00           H  
ATOM     32  HB3 TRP A 450       4.942  21.891  30.119  1.00  0.00           H  
ATOM     33  HB2 TRP A 450       5.214  21.494  31.796  1.00  0.00           H  
ATOM     34  HD1 TRP A 450       7.577  21.907  32.574  1.00  0.00           H  
ATOM     35  HE1 TRP A 450       9.549  23.420  31.922  1.00  0.00           H  
ATOM     36  HE3 TRP A 450       5.375  24.478  28.732  1.00  0.00           H  
ATOM     37  HZ3 TRP A 450       6.642  26.211  27.493  1.00  0.00           H  
ATOM     38  HH2 TRP A 450       9.022  26.660  28.066  1.00  0.00           H  
ATOM     39  HZ2 TRP A 450      10.107  25.429  29.933  1.00  0.00           H  
ATOM     40  N   GLU A 451       2.010  22.866  32.666  1.00 22.83           N  
ANISOU   40  N   GLU A 451     3530   2681   2462   -216    770   -695
ATOM     41  CA  GLU A 451       0.602  22.511  32.758  1.00 21.20           C  
ANISOU   41  CA  GLU A 451     3392   2407   2254    145   1361  -1161
ATOM     42  C   GLU A 451      -0.252  23.510  31.962  1.00 22.98           C  
ANISOU   42  C   GLU A 451     3193   2266   3270   -379    934   -874
ATOM     43  O   GLU A 451      -0.241  24.706  32.250  1.00 25.92           O  
ANISOU   43  O   GLU A 451     4073   2386   3388   -653    732  -1355
ATOM     44  CB  GLU A 451       0.142  22.366  34.218  1.00 25.75           C  
ANISOU   44  CB  GLU A 451     3851   3631   2299   -172   1601   -768
ATOM     45  CG  GLU A 451      -1.322  21.866  34.309  1.00 31.77           C  
ANISOU   45  CG  GLU A 451     3754   4370   3948    547   1594   -422
ATOM     46  CD  GLU A 451      -1.801  21.417  35.697  1.00 44.27           C  
ANISOU   46  CD  GLU A 451     5438   8015   3367    251   1317   -284
ATOM     47  OE1 GLU A 451      -1.045  21.569  36.683  1.00 51.24           O  
ANISOU   47  OE1 GLU A 451     6011  10975   2480   1646   1405   1211
ATOM     48  OE2 GLU A 451      -2.942  20.905  35.738  1.00 59.23           O1-
ANISOU   48  OE2 GLU A 451     6028   9473   7000    353   3506   3215
ATOM     49  H   GLU A 451       2.415  23.315  33.472  1.00  0.00           H  
ATOM     50  HA  GLU A 451       0.512  21.519  32.319  1.00  0.00           H  
ATOM     51  HB3 GLU A 451       0.242  23.319  34.740  1.00  0.00           H  
ATOM     52  HB2 GLU A 451       0.807  21.668  34.726  1.00  0.00           H  
ATOM     53  HG3 GLU A 451      -1.451  21.022  33.629  1.00  0.00           H  
ATOM     54  HG2 GLU A 451      -2.003  22.644  33.961  1.00  0.00           H  
ATOM     55  N   ILE A 452      -0.958  22.963  30.970  1.00 25.28           N  
ANISOU   55  N   ILE A 452     4271   2139   3192   -499    406    -33
ATOM     56  CA  ILE A 452      -1.890  23.648  30.094  1.00 26.63           C  
ANISOU   56  CA  ILE A 452     4418   2729   2972    156    481    -38
ATOM     57  C   ILE A 452      -3.268  23.642  30.797  1.00 31.14           C  
ANISOU   57  C   ILE A 452     3733   3855   4244    748    476     29
ATOM     58  O   ILE A 452      -3.759  22.550  31.100  1.00 37.28           O  
ANISOU   58  O   ILE A 452     3715   5223   5226    561   1852    463
ATOM     59  CB  ILE A 452      -1.995  22.879  28.743  1.00 22.14           C  
ANISOU   59  CB  ILE A 452     3350   2088   2973   -345    242   -172
ATOM     60  CG1 ILE A 452      -0.627  22.868  28.014  1.00 23.10           C  
ANISOU   60  CG1 ILE A 452     4090   1967   2717    143    674   -103
ATOM     61  CG2 ILE A 452      -3.100  23.447  27.827  1.00 24.14           C  
ANISOU   61  CG2 ILE A 452     2773   2957   3440   -224    355   -298
ATOM     62  CD1 ILE A 452      -0.555  21.924  26.807  1.00 25.78           C  
ANISOU   62  CD1 ILE A 452     3152   3488   3154   -114    679  -1051
ATOM     63  H   ILE A 452      -0.887  21.963  30.820  1.00  0.00           H  
ATOM     64  HA  ILE A 452      -1.509  24.645  29.877  1.00  0.00           H  
ATOM     65  HB  ILE A 452      -2.250  21.840  28.951  1.00  0.00           H  
ATOM     66 HG13 ILE A 452       0.164  22.566  28.699  1.00  0.00           H  
ATOM     67 HG12 ILE A 452      -0.371  23.879  27.705  1.00  0.00           H  
ATOM     68 HG21 ILE A 452      -3.085  22.995  26.838  1.00  0.00           H  
ATOM     69 HG22 ILE A 452      -4.096  23.267  28.228  1.00  0.00           H  
ATOM     70 HG23 ILE A 452      -2.983  24.523  27.703  1.00  0.00           H  
ATOM     71 HD11 ILE A 452       0.473  21.812  26.463  1.00  0.00           H  
ATOM     72 HD12 ILE A 452      -0.925  20.932  27.066  1.00  0.00           H  
ATOM     73 HD13 ILE A 452      -1.134  22.297  25.963  1.00  0.00           H  
ATOM     74  N   PRO A 453      -3.856  24.835  31.068  1.00 34.01           N  
ANISOU   74  N   PRO A 453     5241   4407   3271   1180    457    -16
ATOM     75  CA  PRO A 453      -5.210  24.963  31.648  1.00 39.10           C  
ANISOU   75  CA  PRO A 453     4578   5924   4354   1720     87   -556
ATOM     76  C   PRO A 453      -6.309  24.185  30.904  1.00 36.12           C  
ANISOU   76  C   PRO A 453     4058   5620   4045     81   1522    669
ATOM     77  O   PRO A 453      -6.218  24.004  29.688  1.00 31.21           O  
ANISOU   77  O   PRO A 453     4402   3349   4107     13   1273   -750
ATOM     78  CB  PRO A 453      -5.493  26.473  31.609  1.00 45.25           C  
ANISOU   78  CB  PRO A 453     4793   6232   6167   1807   -358    -93
ATOM     79  CG  PRO A 453      -4.125  27.124  31.636  1.00 38.73           C  
ANISOU   79  CG  PRO A 453     4375   5227   5112    864     57  -2200
ATOM     80  CD  PRO A 453      -3.260  26.155  30.845  1.00 33.55           C  
ANISOU   80  CD  PRO A 453     3323   4021   5400   1001   -394   -809
ATOM     81  HA  PRO A 453      -5.148  24.626  32.685  1.00  0.00           H  
ATOM     82  HB3 PRO A 453      -6.125  26.803  32.435  1.00  0.00           H  
ATOM     83  HB2 PRO A 453      -6.001  26.746  30.683  1.00  0.00           H  
ATOM     84  HG3 PRO A 453      -3.771  27.163  32.666  1.00  0.00           H  
ATOM     85  HG2 PRO A 453      -4.117  28.140  31.239  1.00  0.00           H  
ATOM     86  HD2 PRO A 453      -3.291  26.382  29.780  1.00  0.00           H  
ATOM     87  HD3 PRO A 453      -2.227  26.227  31.183  1.00  0.00           H  
ATOM     88  N   ASP A 454      -7.314  23.740  31.673  1.00 44.50           N  
ANISOU   88  N   ASP A 454     6037   8074   2795   1333   3648    605
ATOM     89  CA  ASP A 454      -8.466  22.949  31.230  1.00 49.49           C  
ANISOU   89  CA  ASP A 454     5839   6533   6430   2038   2083    307
ATOM     90  C   ASP A 454      -9.200  23.541  30.008  1.00 37.96           C  
ANISOU   90  C   ASP A 454     5052   4275   5094    780   2647   -146
ATOM     91  O   ASP A 454      -9.468  24.742  29.963  1.00 42.35           O  
ANISOU   91  O   ASP A 454     5483   4457   6149    642   2570  -1161
ATOM     92  CB  ASP A 454      -9.473  22.633  32.376  1.00  0.00           C  
ATOM     93  CG  ASP A 454     -10.008  23.784  33.262  1.00  0.00           C  
ATOM     94  OD1 ASP A 454      -9.649  24.965  33.056  1.00  0.00           O  
ATOM     95  OD2 ASP A 454     -10.802  23.446  34.168  1.00  0.00           O1-
ATOM     96  H   ASP A 454      -7.322  23.986  32.653  1.00  0.00           H  
ATOM     97  HA  ASP A 454      -8.041  21.992  30.917  1.00  0.00           H  
ATOM     98  HB2 ASP A 454     -10.328  22.094  31.965  1.00  0.00           H  
ATOM     99  HB3 ASP A 454      -8.990  21.923  33.049  1.00  0.00           H  
ATOM    100  N   GLY A 455      -9.516  22.663  29.044  1.00 40.17           N  
ANISOU  100  N   GLY A 455     3021   5452   6789   -387   2574   -154
ATOM    101  CA  GLY A 455     -10.350  22.963  27.881  1.00 43.17           C  
ANISOU  101  CA  GLY A 455     2365   6855   7181    -15   2190   -974
ATOM    102  C   GLY A 455      -9.639  23.727  26.749  1.00 42.84           C  
ANISOU  102  C   GLY A 455     1702   7176   7396   -867    781   -251
ATOM    103  O   GLY A 455     -10.271  23.936  25.714  1.00 45.09           O  
ANISOU  103  O   GLY A 455     3679   6473   6977   -813   1078   -166
ATOM    104  H   GLY A 455      -9.223  21.702  29.148  1.00  0.00           H  
ATOM    105  HA3 GLY A 455     -11.229  23.530  28.193  1.00  0.00           H  
ATOM    106  HA2 GLY A 455     -10.719  22.020  27.478  1.00  0.00           H  
ATOM    107  N   GLN A 456      -8.367  24.142  26.908  1.00 28.21           N  
ANISOU  107  N   GLN A 456     1833   3695   5187   -747   1059  -1703
ATOM    108  CA  GLN A 456      -7.617  24.871  25.878  1.00 25.44           C  
ANISOU  108  CA  GLN A 456     2746   3330   3588     92    402  -1925
ATOM    109  C   GLN A 456      -7.244  24.025  24.651  1.00 23.15           C  
ANISOU  109  C   GLN A 456     1545   3436   3813     12    974  -1824
ATOM    110  O   GLN A 456      -7.241  24.563  23.543  1.00 33.60           O  
ANISOU  110  O   GLN A 456     3201   5193   4369    910     22   -662
ATOM    111  CB  GLN A 456      -6.349  25.507  26.468  1.00 26.45           C  
ANISOU  111  CB  GLN A 456     2161   3560   4328     12    988  -1725
ATOM    112  CG  GLN A 456      -6.624  26.674  27.433  1.00 27.77           C  
ANISOU  112  CG  GLN A 456     3126   3275   4149    337    851  -1510
ATOM    113  CD  GLN A 456      -5.353  27.449  27.784  1.00 25.20           C  
ANISOU  113  CD  GLN A 456     3725   2315   3534   -157    715   -501
ATOM    114  OE1 GLN A 456      -4.246  27.062  27.412  1.00 26.31           O  
ANISOU  114  OE1 GLN A 456     4207   3248   2541   -447    978   -558
ATOM    115  NE2 GLN A 456      -5.508  28.560  28.506  1.00 29.45           N  
ANISOU  115  NE2 GLN A 456     3201   2651   5334   -371   1454  -1440
ATOM    116  H   GLN A 456      -7.887  23.962  27.779  1.00  0.00           H  
ATOM    117  HA  GLN A 456      -8.257  25.679  25.517  1.00  0.00           H  
ATOM    118  HB3 GLN A 456      -5.746  25.887  25.642  1.00  0.00           H  
ATOM    119  HB2 GLN A 456      -5.745  24.746  26.965  1.00  0.00           H  
ATOM    120  HG3 GLN A 456      -7.087  26.306  28.350  1.00  0.00           H  
ATOM    121  HG2 GLN A 456      -7.331  27.370  26.979  1.00  0.00           H  
ATOM    122 HE22 GLN A 456      -4.709  29.132  28.744  1.00  0.00           H  
ATOM    123 HE21 GLN A 456      -6.429  28.856  28.796  1.00  0.00           H  
ATOM    124  N   ILE A 457      -6.927  22.737  24.864  1.00 26.39           N  
ANISOU  124  N   ILE A 457     3237   3730   3061    294    512  -1118
ATOM    125  CA  ILE A 457      -6.586  21.802  23.793  1.00 26.30           C  
ANISOU  125  CA  ILE A 457     2728   4070   3193    480    526  -1220
ATOM    126  C   ILE A 457      -7.880  21.344  23.094  1.00 26.36           C  
ANISOU  126  C   ILE A 457     2111   4900   3003     43    551   -279
ATOM    127  O   ILE A 457      -8.763  20.791  23.753  1.00 25.11           O  
ANISOU  127  O   ILE A 457     1860   3729   3951   -382    -28    173
ATOM    128  CB  ILE A 457      -5.838  20.540  24.324  1.00 25.51           C  
ANISOU  128  CB  ILE A 457     3047   3103   3540     98    659   -821
ATOM    129  CG1 ILE A 457      -4.536  20.909  25.075  1.00 27.45           C  
ANISOU  129  CG1 ILE A 457     3758   3414   3256   -121    551  -1210
ATOM    130  CG2 ILE A 457      -5.526  19.504  23.218  1.00 31.67           C  
ANISOU  130  CG2 ILE A 457     3871   4418   3742    470    323  -1630
ATOM    131  CD1 ILE A 457      -4.033  19.798  26.011  1.00 28.92           C  
ANISOU  131  CD1 ILE A 457     3468   4535   2982    417    350   -348
ATOM    132  H   ILE A 457      -6.952  22.359  25.802  1.00  0.00           H  
ATOM    133  HA  ILE A 457      -5.937  22.307  23.075  1.00  0.00           H  
ATOM    134  HB  ILE A 457      -6.494  20.052  25.048  1.00  0.00           H  
ATOM    135 HG13 ILE A 457      -4.686  21.799  25.682  1.00  0.00           H  
ATOM    136 HG12 ILE A 457      -3.756  21.173  24.361  1.00  0.00           H  
ATOM    137 HG21 ILE A 457      -4.978  18.652  23.617  1.00  0.00           H  
ATOM    138 HG22 ILE A 457      -6.425  19.097  22.756  1.00  0.00           H  
ATOM    139 HG23 ILE A 457      -4.918  19.946  22.428  1.00  0.00           H  
ATOM    140 HD11 ILE A 457      -3.253  20.176  26.672  1.00  0.00           H  
ATOM    141 HD12 ILE A 457      -4.836  19.416  26.641  1.00  0.00           H  
ATOM    142 HD13 ILE A 457      -3.618  18.959  25.456  1.00  0.00           H  
ATOM    143  N   THR A 458      -7.949  21.563  21.773  1.00 25.97           N  
ANISOU  143  N   THR A 458     2160   4941   2765    770    363  -1433
ATOM    144  CA  THR A 458      -9.010  21.030  20.922  1.00 30.25           C  
ANISOU  144  CA  THR A 458     2091   4723   4679    -29    575  -2040
ATOM    145  C   THR A 458      -8.467  19.775  20.224  1.00 30.08           C  
ANISOU  145  C   THR A 458     2923   4274   4231   -815   1200  -1937
ATOM    146  O   THR A 458      -7.453  19.858  19.536  1.00 29.78           O  
ANISOU  146  O   THR A 458     2168   4743   4403  -1027    763  -1979
ATOM    147  CB  THR A 458      -9.447  22.049  19.841  1.00 28.89           C  
ANISOU  147  CB  THR A 458     2382   4090   4503    423    -10  -2014
ATOM    148  OG1 THR A 458      -9.959  23.208  20.465  1.00 35.19           O  
ANISOU  148  OG1 THR A 458     4063   4293   5011    190    654  -2451
ATOM    149  CG2 THR A 458     -10.511  21.533  18.855  1.00 41.77           C  
ANISOU  149  CG2 THR A 458     2544   6241   7083   -132   -638  -1861
ATOM    150  H   THR A 458      -7.178  22.016  21.300  1.00  0.00           H  
ATOM    151  HA  THR A 458      -9.889  20.769  21.514  1.00  0.00           H  
ATOM    152  HB  THR A 458      -8.578  22.367  19.276  1.00  0.00           H  
ATOM    153  HG1 THR A 458      -9.245  23.641  20.942  1.00  0.00           H  
ATOM    154 HG21 THR A 458     -10.851  22.331  18.195  1.00  0.00           H  
ATOM    155 HG22 THR A 458     -10.121  20.738  18.219  1.00  0.00           H  
ATOM    156 HG23 THR A 458     -11.383  21.143  19.382  1.00  0.00           H  
ATOM    157  N   VAL A 459      -9.137  18.636  20.440  1.00 26.55           N  
ANISOU  157  N   VAL A 459     2587   3880   3618    -67    456   -373
ATOM    158  CA  VAL A 459      -8.728  17.330  19.929  1.00 30.53           C  
ANISOU  158  CA  VAL A 459     2929   4622   4050     66    433   -877
ATOM    159  C   VAL A 459      -9.451  17.052  18.597  1.00 26.07           C  
ANISOU  159  C   VAL A 459     2929   3372   3604    856    380    -18
ATOM    160  O   VAL A 459     -10.676  17.158  18.531  1.00 28.19           O  
ANISOU  160  O   VAL A 459     2857   3685   4168      8   -105   -977
ATOM    161  CB  VAL A 459      -9.081  16.219  20.956  1.00 32.89           C  
ANISOU  161  CB  VAL A 459     3673   5053   3769    759  -1292    114
ATOM    162  CG1 VAL A 459      -8.792  14.788  20.463  1.00 35.97           C  
ANISOU  162  CG1 VAL A 459     4245   5807   3614   1457   -710   -255
ATOM    163  CG2 VAL A 459      -8.348  16.457  22.291  1.00 37.83           C  
ANISOU  163  CG2 VAL A 459     4900   5549   3923    849  -1523    -97
ATOM    164  H   VAL A 459      -9.959  18.643  21.030  1.00  0.00           H  
ATOM    165  HA  VAL A 459      -7.648  17.312  19.764  1.00  0.00           H  
ATOM    166  HB  VAL A 459     -10.151  16.277  21.164  1.00  0.00           H  
ATOM    167 HG11 VAL A 459      -9.035  14.051  21.228  1.00  0.00           H  
ATOM    168 HG12 VAL A 459      -9.374  14.518  19.583  1.00  0.00           H  
ATOM    169 HG13 VAL A 459      -7.738  14.674  20.215  1.00  0.00           H  
ATOM    170 HG21 VAL A 459      -8.678  15.746  23.046  1.00  0.00           H  
ATOM    171 HG22 VAL A 459      -7.268  16.354  22.178  1.00  0.00           H  
ATOM    172 HG23 VAL A 459      -8.545  17.449  22.698  1.00  0.00           H  
ATOM    173  N   GLY A 460      -8.667  16.708  17.567  1.00 23.78           N  
ANISOU  173  N   GLY A 460     2598   3149   3286    853    333    236
ATOM    174  CA  GLY A 460      -9.122  16.452  16.203  1.00 30.27           C  
ANISOU  174  CA  GLY A 460     3883   3947   3669   1077    225   -633
ATOM    175  C   GLY A 460      -9.022  14.952  15.905  1.00 21.34           C  
ANISOU  175  C   GLY A 460     2138   3531   2437   1020    287     74
ATOM    176  O   GLY A 460      -9.427  14.125  16.723  1.00 30.45           O  
ANISOU  176  O   GLY A 460     3964   3082   4522   -553   1327   -628
ATOM    177  H   GLY A 460      -7.669  16.627  17.712  1.00  0.00           H  
ATOM    178  HA3 GLY A 460      -8.493  17.022  15.521  1.00  0.00           H  
ATOM    179  HA2 GLY A 460     -10.149  16.782  16.041  1.00  0.00           H  
ATOM    180  N   GLN A 461      -8.531  14.623  14.698  1.00 22.88           N  
ANISOU  180  N   GLN A 461     2334   3953   2405    504     82   -885
ATOM    181  CA  GLN A 461      -8.407  13.271  14.142  1.00 22.28           C  
ANISOU  181  CA  GLN A 461     2291   2953   3219    232    219   -278
ATOM    182  C   GLN A 461      -7.582  12.313  15.014  1.00 23.52           C  
ANISOU  182  C   GLN A 461     3469   2788   2676   -664    -55   -366
ATOM    183  O   GLN A 461      -6.485  12.678  15.432  1.00 22.49           O  
ANISOU  183  O   GLN A 461     3201   2544   2798   -516    250   -392
ATOM    184  CB  GLN A 461      -7.746  13.360  12.744  1.00  0.00           C  
ATOM    185  CG  GLN A 461      -8.568  14.077  11.653  1.00  0.00           C  
ATOM    186  CD  GLN A 461      -9.671  13.212  11.035  1.00  0.00           C  
ATOM    187  OE1 GLN A 461     -10.358  12.463  11.725  1.00  0.00           O  
ATOM    188  NE2 GLN A 461      -9.865  13.332   9.720  1.00  0.00           N  
ATOM    189  H   GLN A 461      -8.216  15.367  14.089  1.00  0.00           H  
ATOM    190  HA  GLN A 461      -9.416  12.868  14.053  1.00  0.00           H  
ATOM    191  HB2 GLN A 461      -6.793  13.883  12.846  1.00  0.00           H  
ATOM    192  HB3 GLN A 461      -7.484  12.361  12.387  1.00  0.00           H  
ATOM    193  HG2 GLN A 461      -9.011  14.997  12.036  1.00  0.00           H  
ATOM    194  HG3 GLN A 461      -7.887  14.379  10.857  1.00  0.00           H  
ATOM    195 HE22 GLN A 461     -10.587  12.792   9.266  1.00  0.00           H  
ATOM    196 HE21 GLN A 461      -9.295  13.960   9.171  1.00  0.00           H  
ATOM    197  N   ARG A 462      -8.102  11.090  15.211  1.00 23.34           N  
ANISOU  197  N   ARG A 462     1714   2724   4428   -514   -251   -200
ATOM    198  CA  ARG A 462      -7.383   9.957  15.799  1.00 23.37           C  
ANISOU  198  CA  ARG A 462     2335   3233   3311    317    345   -515
ATOM    199  C   ARG A 462      -6.273   9.498  14.838  1.00 20.40           C  
ANISOU  199  C   ARG A 462     1874   3292   2585   -235    230   -177
ATOM    200  O   ARG A 462      -6.557   9.262  13.665  1.00 20.92           O  
ANISOU  200  O   ARG A 462     1585   3461   2901    -21   -134   -791
ATOM    201  CB  ARG A 462      -8.413   8.842  16.102  1.00 26.69           C  
ANISOU  201  CB  ARG A 462     3283   3717   3140   -465   -971   -356
ATOM    202  CG  ARG A 462      -7.877   7.522  16.693  1.00 23.14           C  
ANISOU  202  CG  ARG A 462     3301   2819   2671   -621    -53   -555
ATOM    203  CD  ARG A 462      -7.137   7.668  18.034  1.00 21.20           C  
ANISOU  203  CD  ARG A 462     2617   2706   2731   -577     19  -1066
ATOM    204  NE  ARG A 462      -6.828   6.361  18.636  1.00 21.98           N  
ANISOU  204  NE  ARG A 462     2176   3579   2597    -76    106   -480
ATOM    205  CZ  ARG A 462      -7.617   5.589  19.405  1.00 25.42           C  
ANISOU  205  CZ  ARG A 462     2540   4153   2963   -169    246   -101
ATOM    206  NH1 ARG A 462      -8.829   5.988  19.815  1.00 22.31           N  
ANISOU  206  NH1 ARG A 462     2388   2986   3102   -183    176   -111
ATOM    207  NH2 ARG A 462      -7.174   4.381  19.770  1.00 26.59           N1+
ANISOU  207  NH2 ARG A 462     2806   3717   3580   -870    252    824
ATOM    208  H   ARG A 462      -9.017  10.884  14.837  1.00  0.00           H  
ATOM    209  HA  ARG A 462      -6.924  10.278  16.734  1.00  0.00           H  
ATOM    210  HB3 ARG A 462      -8.948   8.596  15.184  1.00  0.00           H  
ATOM    211  HB2 ARG A 462      -9.171   9.235  16.781  1.00  0.00           H  
ATOM    212  HG3 ARG A 462      -7.170   7.127  15.963  1.00  0.00           H  
ATOM    213  HG2 ARG A 462      -8.668   6.776  16.757  1.00  0.00           H  
ATOM    214  HD3 ARG A 462      -7.618   8.365  18.717  1.00  0.00           H  
ATOM    215  HD2 ARG A 462      -6.154   8.079  17.822  1.00  0.00           H  
ATOM    216  HE  ARG A 462      -5.907   6.004  18.413  1.00  0.00           H  
ATOM    217 HH12 ARG A 462      -9.406   5.383  20.382  1.00  0.00           H  
ATOM    218 HH11 ARG A 462      -9.169   6.902  19.558  1.00  0.00           H  
ATOM    219 HH22 ARG A 462      -7.725   3.779  20.367  1.00  0.00           H  
ATOM    220 HH21 ARG A 462      -6.286   4.039  19.424  1.00  0.00           H  
ATOM    221  N   ILE A 463      -5.037   9.407  15.346  1.00 19.34           N  
ANISOU  221  N   ILE A 463     2183   2541   2624      4   -249   -191
ATOM    222  CA  ILE A 463      -3.851   9.043  14.567  1.00 21.42           C  
ANISOU  222  CA  ILE A 463     2403   3252   2481    161    -52   -548
ATOM    223  C   ILE A 463      -3.403   7.610  14.888  1.00 18.41           C  
ANISOU  223  C   ILE A 463     1377   3109   2510   -342    -76   -475
ATOM    224  O   ILE A 463      -3.005   6.892  13.972  1.00 23.53           O  
ANISOU  224  O   ILE A 463     3169   2623   3144     23    447   -551
ATOM    225  CB  ILE A 463      -2.671  10.022  14.854  1.00 23.18           C  
ANISOU  225  CB  ILE A 463     2110   3195   3503    -44    506    268
ATOM    226  CG1 ILE A 463      -3.046  11.477  14.490  1.00 26.03           C  
ANISOU  226  CG1 ILE A 463     3321   3875   2693    145   1035    161
ATOM    227  CG2 ILE A 463      -1.319   9.633  14.211  1.00 31.50           C  
ANISOU  227  CG2 ILE A 463     3251   4048   4670    298   1443    378
ATOM    228  CD1 ILE A 463      -3.478  11.703  13.032  1.00 27.78           C  
ANISOU  228  CD1 ILE A 463     3252   4416   2886    -37  -1033  -1079
ATOM    229  H   ILE A 463      -4.877   9.625  16.321  1.00  0.00           H  
ATOM    230  HA  ILE A 463      -4.070   9.072  13.499  1.00  0.00           H  
ATOM    231  HB  ILE A 463      -2.504  10.017  15.931  1.00  0.00           H  
ATOM    232 HG13 ILE A 463      -2.223  12.144  14.743  1.00  0.00           H  
ATOM    233 HG12 ILE A 463      -3.868  11.794  15.127  1.00  0.00           H  
ATOM    234 HG21 ILE A 463      -0.567  10.404  14.382  1.00  0.00           H  
ATOM    235 HG22 ILE A 463      -0.912   8.711  14.629  1.00  0.00           H  
ATOM    236 HG23 ILE A 463      -1.409   9.494  13.134  1.00  0.00           H  
ATOM    237 HD11 ILE A 463      -3.389  12.754  12.759  1.00  0.00           H  
ATOM    238 HD12 ILE A 463      -2.878  11.127  12.329  1.00  0.00           H  
ATOM    239 HD13 ILE A 463      -4.522  11.424  12.890  1.00  0.00           H  
ATOM    240  N   GLY A 464      -3.504   7.207  16.162  1.00 20.49           N  
ANISOU  240  N   GLY A 464     2196   3200   2387   -344     38   -563
ATOM    241  CA  GLY A 464      -3.082   5.883  16.578  1.00 21.42           C  
ANISOU  241  CA  GLY A 464     2535   3361   2243   -262   -506   -737
ATOM    242  C   GLY A 464      -2.944   5.871  18.095  1.00 19.96           C  
ANISOU  242  C   GLY A 464     2462   2824   2295    139    214   -642
ATOM    243  O   GLY A 464      -3.805   6.389  18.803  1.00 17.86           O  
ANISOU  243  O   GLY A 464     2074   2786   1924     50     46   -602
ATOM    244  H   GLY A 464      -3.842   7.837  16.877  1.00  0.00           H  
ATOM    245  HA3 GLY A 464      -2.137   5.615  16.108  1.00  0.00           H  
ATOM    246  HA2 GLY A 464      -3.830   5.157  16.266  1.00  0.00           H  
ATOM    247  N   SER A 465      -1.881   5.226  18.588  1.00 19.52           N  
ANISOU  247  N   SER A 465     2184   2857   2374     30     66   -953
ATOM    248  CA  SER A 465      -1.616   5.043  20.012  1.00 21.15           C  
ANISOU  248  CA  SER A 465     2481   2710   2843   -176   -583   -574
ATOM    249  C   SER A 465      -0.113   5.121  20.296  1.00 19.15           C  
ANISOU  249  C   SER A 465     2287   2147   2840    -31   -142   -480
ATOM    250  O   SER A 465       0.698   5.022  19.377  1.00 24.22           O  
ANISOU  250  O   SER A 465     2456   4020   2724     80   -269   -669
ATOM    251  CB  SER A 465      -2.243   3.706  20.464  1.00 28.92           C  
ANISOU  251  CB  SER A 465     4570   2759   3658   -558   -126  -1074
ATOM    252  OG  SER A 465      -1.416   2.614  20.117  1.00 37.24           O  
ANISOU  252  OG  SER A 465     5492   2938   5717     32   -323  -1084
ATOM    253  H   SER A 465      -1.198   4.821  17.960  1.00  0.00           H  
ATOM    254  HA  SER A 465      -2.074   5.861  20.565  1.00  0.00           H  
ATOM    255  HB3 SER A 465      -3.239   3.563  20.042  1.00  0.00           H  
ATOM    256  HB2 SER A 465      -2.368   3.707  21.546  1.00  0.00           H  
ATOM    257  HG  SER A 465      -1.957   1.819  20.052  1.00  0.00           H  
ATOM    258  N   GLY A 466       0.224   5.257  21.582  1.00 20.59           N  
ANISOU  258  N   GLY A 466     2328   2888   2608   -174    -91   -291
ATOM    259  CA  GLY A 466       1.594   5.141  22.046  1.00 20.54           C  
ANISOU  259  CA  GLY A 466     2701   2243   2860    177   -541    114
ATOM    260  C   GLY A 466       1.546   5.035  23.566  1.00 22.24           C  
ANISOU  260  C   GLY A 466     2570   3015   2864    399   -432   -296
ATOM    261  O   GLY A 466       0.827   5.803  24.205  1.00 22.83           O  
ANISOU  261  O   GLY A 466     3225   2698   2748    293     66    170
ATOM    262  H   GLY A 466      -0.494   5.349  22.291  1.00  0.00           H  
ATOM    263  HA3 GLY A 466       2.172   6.017  21.748  1.00  0.00           H  
ATOM    264  HA2 GLY A 466       2.066   4.264  21.608  1.00  0.00           H  
ATOM    265  N   SER A 467       2.362   4.128  24.131  1.00 23.71           N  
ANISOU  265  N   SER A 467     3281   2490   3237    810     29   -520
ATOM    266  CA  SER A 467       2.580   3.909  25.568  1.00 25.47           C  
ANISOU  266  CA  SER A 467     3434   2996   3246    -75   -199   -121
ATOM    267  C   SER A 467       1.268   3.713  26.368  1.00 24.49           C  
ANISOU  267  C   SER A 467     3145   2794   3364   -318   -249     15
ATOM    268  O   SER A 467       0.574   2.727  26.125  1.00 24.19           O  
ANISOU  268  O   SER A 467     2864   2629   3695   -125   -376    202
ATOM    269  CB  SER A 467       3.560   4.974  26.124  1.00 24.00           C  
ANISOU  269  CB  SER A 467     2595   2300   4223    117    430    -85
ATOM    270  OG  SER A 467       2.985   6.261  26.197  1.00 20.50           O  
ANISOU  270  OG  SER A 467     2458   2374   2955    433    261    405
ATOM    271  H   SER A 467       2.910   3.534  23.522  1.00  0.00           H  
ATOM    272  HA  SER A 467       3.099   2.952  25.630  1.00  0.00           H  
ATOM    273  HB3 SER A 467       4.459   5.025  25.508  1.00  0.00           H  
ATOM    274  HB2 SER A 467       3.889   4.693  27.125  1.00  0.00           H  
ATOM    275  HG  SER A 467       3.595   6.848  26.667  1.00  0.00           H  
ATOM    276  N   PHE A 468       0.951   4.632  27.296  1.00 21.04           N  
ANISOU  276  N   PHE A 468     3073   2095   2824   -423   -145    691
ATOM    277  CA  PHE A 468      -0.265   4.629  28.109  1.00 27.57           C  
ANISOU  277  CA  PHE A 468     2999   3157   4318   -488    263    651
ATOM    278  C   PHE A 468      -1.534   5.047  27.340  1.00 22.20           C  
ANISOU  278  C   PHE A 468     2508   2430   3495   -103    926    315
ATOM    279  O   PHE A 468      -2.624   4.699  27.793  1.00 26.43           O  
ANISOU  279  O   PHE A 468     1768   3784   4488   -586    372    452
ATOM    280  CB  PHE A 468      -0.047   5.528  29.358  1.00 24.93           C  
ANISOU  280  CB  PHE A 468     2887   2910   3674   -412    571    670
ATOM    281  CG  PHE A 468       0.075   7.033  29.127  1.00 25.27           C  
ANISOU  281  CG  PHE A 468     3649   2537   3413   -284    515   -345
ATOM    282  CD1 PHE A 468      -1.080   7.834  28.988  1.00 22.80           C  
ANISOU  282  CD1 PHE A 468     3083   3473   2107   -486    -90    269
ATOM    283  CE1 PHE A 468      -0.968   9.181  28.666  1.00 26.13           C  
ANISOU  283  CE1 PHE A 468     3051   3517   3358    -41    161    195
ATOM    284  CZ  PHE A 468       0.284   9.748  28.473  1.00 24.58           C  
ANISOU  284  CZ  PHE A 468     3600   2922   2816   -473    117   -422
ATOM    285  CD2 PHE A 468       1.337   7.621  28.902  1.00 27.05           C  
ANISOU  285  CD2 PHE A 468     3315   3680   3283   -217   -476   -421
ATOM    286  CE2 PHE A 468       1.429   8.973  28.594  1.00 22.73           C  
ANISOU  286  CE2 PHE A 468     3239   3570   1827   -273    281   -255
ATOM    287  H   PHE A 468       1.563   5.428  27.414  1.00  0.00           H  
ATOM    288  HA  PHE A 468      -0.419   3.608  28.462  1.00  0.00           H  
ATOM    289  HB3 PHE A 468       0.831   5.183  29.906  1.00  0.00           H  
ATOM    290  HB2 PHE A 468      -0.884   5.376  30.042  1.00  0.00           H  
ATOM    291  HD1 PHE A 468      -2.057   7.395  29.117  1.00  0.00           H  
ATOM    292  HE1 PHE A 468      -1.856   9.787  28.556  1.00  0.00           H  
ATOM    293  HZ  PHE A 468       0.365  10.794  28.218  1.00  0.00           H  
ATOM    294  HD2 PHE A 468       2.236   7.025  28.970  1.00  0.00           H  
ATOM    295  HE2 PHE A 468       2.397   9.422  28.436  1.00  0.00           H  
ATOM    296  N   GLY A 469      -1.385   5.832  26.259  1.00 21.39           N  
ANISOU  296  N   GLY A 469     2596   2565   2963   -177   1014   -190
ATOM    297  CA  GLY A 469      -2.466   6.660  25.733  1.00 23.33           C  
ANISOU  297  CA  GLY A 469     2969   2983   2912    -28    373   -319
ATOM    298  C   GLY A 469      -2.744   6.432  24.245  1.00 21.98           C  
ANISOU  298  C   GLY A 469     2762   2317   3270     29   -383   -438
ATOM    299  O   GLY A 469      -2.066   5.680  23.548  1.00 26.07           O  
ANISOU  299  O   GLY A 469     2650   3262   3992    378   -332   -956
ATOM    300  H   GLY A 469      -0.457   6.013  25.901  1.00  0.00           H  
ATOM    301  HA3 GLY A 469      -2.167   7.700  25.870  1.00  0.00           H  
ATOM    302  HA2 GLY A 469      -3.396   6.529  26.290  1.00  0.00           H  
ATOM    303  N   THR A 470      -3.772   7.146  23.776  1.00 19.81           N  
ANISOU  303  N   THR A 470     2249   2132   3145    -31    101   -345
ATOM    304  CA  THR A 470      -4.242   7.206  22.399  1.00 18.92           C  
ANISOU  304  CA  THR A 470     2586   2021   2579   -137    641   -239
ATOM    305  C   THR A 470      -3.892   8.591  21.828  1.00 19.78           C  
ANISOU  305  C   THR A 470     2734   2259   2523   -147    507    -98
ATOM    306  O   THR A 470      -4.136   9.608  22.479  1.00 21.36           O  
ANISOU  306  O   THR A 470     2464   2441   3209   -677    911   -374
ATOM    307  CB  THR A 470      -5.776   7.006  22.353  1.00 21.61           C  
ANISOU  307  CB  THR A 470     2769   2423   3018   -203    834   -412
ATOM    308  OG1 THR A 470      -6.455   7.899  23.217  1.00 21.25           O  
ANISOU  308  OG1 THR A 470     2407   2440   3225    -24    913   -630
ATOM    309  CG2 THR A 470      -6.163   5.575  22.753  1.00 23.37           C  
ANISOU  309  CG2 THR A 470     3084   2647   3146   -308     77    274
ATOM    310  H   THR A 470      -4.264   7.756  24.419  1.00  0.00           H  
ATOM    311  HA  THR A 470      -3.776   6.426  21.799  1.00  0.00           H  
ATOM    312  HB  THR A 470      -6.136   7.195  21.341  1.00  0.00           H  
ATOM    313  HG1 THR A 470      -6.213   8.796  22.972  1.00  0.00           H  
ATOM    314 HG21 THR A 470      -7.238   5.415  22.675  1.00  0.00           H  
ATOM    315 HG22 THR A 470      -5.666   4.852  22.108  1.00  0.00           H  
ATOM    316 HG23 THR A 470      -5.862   5.340  23.774  1.00  0.00           H  
ATOM    317  N   VAL A 471      -3.294   8.588  20.628  1.00 17.59           N  
ANISOU  317  N   VAL A 471     1934   2212   2537   -260    184   -157
ATOM    318  CA  VAL A 471      -2.700   9.760  19.991  1.00 18.36           C  
ANISOU  318  CA  VAL A 471     1983   2889   2103   -147    323    536
ATOM    319  C   VAL A 471      -3.657  10.354  18.947  1.00 18.04           C  
ANISOU  319  C   VAL A 471     1932   2174   2748    267   -253   -329
ATOM    320  O   VAL A 471      -4.224   9.619  18.140  1.00 18.26           O  
ANISOU  320  O   VAL A 471     1976   2452   2509     71     47   -220
ATOM    321  CB  VAL A 471      -1.361   9.399  19.291  1.00 17.79           C  
ANISOU  321  CB  VAL A 471     1762   2806   2191   -367    -91   -456
ATOM    322  CG1 VAL A 471      -0.728  10.565  18.500  1.00 20.26           C  
ANISOU  322  CG1 VAL A 471     2142   3151   2403     10    201     63
ATOM    323  CG2 VAL A 471      -0.336   8.870  20.312  1.00 20.50           C  
ANISOU  323  CG2 VAL A 471     1680   3452   2654   -105    126   -151
ATOM    324  H   VAL A 471      -3.181   7.715  20.130  1.00  0.00           H  
ATOM    325  HA  VAL A 471      -2.484  10.512  20.747  1.00  0.00           H  
ATOM    326  HB  VAL A 471      -1.556   8.595  18.579  1.00  0.00           H  
ATOM    327 HG11 VAL A 471       0.171  10.227  17.996  1.00  0.00           H  
ATOM    328 HG12 VAL A 471      -1.370  10.959  17.715  1.00  0.00           H  
ATOM    329 HG13 VAL A 471      -0.458  11.394  19.156  1.00  0.00           H  
ATOM    330 HG21 VAL A 471       0.584   8.552  19.823  1.00  0.00           H  
ATOM    331 HG22 VAL A 471      -0.077   9.638  21.042  1.00  0.00           H  
ATOM    332 HG23 VAL A 471      -0.716   8.011  20.864  1.00  0.00           H  
ATOM    333  N   TYR A 472      -3.773  11.687  18.980  1.00 17.98           N  
ANISOU  333  N   TYR A 472     2516   2083   2232    218    311   -237
ATOM    334  CA  TYR A 472      -4.591  12.506  18.097  1.00 17.53           C  
ANISOU  334  CA  TYR A 472     2352   2390   1919   -279    311   -132
ATOM    335  C   TYR A 472      -3.747  13.663  17.543  1.00 18.32           C  
ANISOU  335  C   TYR A 472     1821   2833   2303   -351    191    261
ATOM    336  O   TYR A 472      -2.795  14.094  18.192  1.00 20.03           O  
ANISOU  336  O   TYR A 472     2246   2765   2599   -493     18   -234
ATOM    337  CB  TYR A 472      -5.773  13.089  18.904  1.00 18.37           C  
ANISOU  337  CB  TYR A 472     2573   2514   1891     97    371   -167
ATOM    338  CG  TYR A 472      -6.748  12.075  19.478  1.00 21.24           C  
ANISOU  338  CG  TYR A 472     3532   2102   2434     99   1364   -159
ATOM    339  CD1 TYR A 472      -6.490  11.456  20.719  1.00 31.45           C  
ANISOU  339  CD1 TYR A 472     4260   4230   3458   1318   1007    541
ATOM    340  CE1 TYR A 472      -7.405  10.527  21.247  1.00 31.01           C  
ANISOU  340  CE1 TYR A 472     4992   3176   3612   1304   1814   -215
ATOM    341  CZ  TYR A 472      -8.583  10.212  20.543  1.00 37.05           C  
ANISOU  341  CZ  TYR A 472     4991   5469   3615    777   2110    -10
ATOM    342  OH  TYR A 472      -9.461   9.298  21.049  1.00 44.97           O  
ANISOU  342  OH  TYR A 472     5460   5846   5778   1481   3906    935
ATOM    343  CE2 TYR A 472      -8.854  10.843  19.315  1.00 28.03           C  
ANISOU  343  CE2 TYR A 472     4228   3252   3169   -756   1127  -1013
ATOM    344  CD2 TYR A 472      -7.937  11.770  18.787  1.00 29.38           C  
ANISOU  344  CD2 TYR A 472     4288   2692   4181    -51    813   -234
ATOM    345  H   TYR A 472      -3.265  12.202  19.689  1.00  0.00           H  
ATOM    346  HA  TYR A 472      -4.963  11.904  17.269  1.00  0.00           H  
ATOM    347  HB3 TYR A 472      -6.344  13.771  18.270  1.00  0.00           H  
ATOM    348  HB2 TYR A 472      -5.398  13.701  19.726  1.00  0.00           H  
ATOM    349  HD1 TYR A 472      -5.593  11.697  21.272  1.00  0.00           H  
ATOM    350  HE1 TYR A 472      -7.211  10.075  22.205  1.00  0.00           H  
ATOM    351  HH  TYR A 472     -10.280   9.253  20.551  1.00  0.00           H  
ATOM    352  HE2 TYR A 472      -9.759  10.618  18.771  1.00  0.00           H  
ATOM    353  HD2 TYR A 472      -8.149  12.248  17.845  1.00  0.00           H  
ATOM    354  N   LYS A 473      -4.173  14.205  16.392  1.00 17.70           N  
ANISOU  354  N   LYS A 473     2051   2867   1805   -346     41   -170
ATOM    355  CA  LYS A 473      -3.822  15.558  15.964  1.00 18.94           C  
ANISOU  355  CA  LYS A 473     2440   2690   2065   -204    102   -219
ATOM    356  C   LYS A 473      -4.801  16.527  16.644  1.00 20.02           C  
ANISOU  356  C   LYS A 473     2398   2603   2604    -56    239   -214
ATOM    357  O   LYS A 473      -5.990  16.220  16.707  1.00 21.60           O  
ANISOU  357  O   LYS A 473     2518   2887   2801     16    691   -463
ATOM    358  CB  LYS A 473      -3.908  15.650  14.428  1.00 17.84           C  
ANISOU  358  CB  LYS A 473     1711   3070   1996    368     15    251
ATOM    359  CG  LYS A 473      -3.461  17.016  13.874  1.00 19.70           C  
ANISOU  359  CG  LYS A 473     2244   3028   2212    316   -135    149
ATOM    360  CD  LYS A 473      -3.432  17.060  12.342  1.00 23.25           C  
ANISOU  360  CD  LYS A 473     2780   3745   2307    -19   -322    500
ATOM    361  CE  LYS A 473      -2.829  18.369  11.809  1.00 23.02           C  
ANISOU  361  CE  LYS A 473     2776   3683   2285     -6    468    214
ATOM    362  NZ  LYS A 473      -2.783  18.384  10.339  1.00 30.69           N1+
ANISOU  362  NZ  LYS A 473     3949   5100   2612      0    272    186
ATOM    363  H   LYS A 473      -4.962  13.788  15.915  1.00  0.00           H  
ATOM    364  HA  LYS A 473      -2.801  15.794  16.270  1.00  0.00           H  
ATOM    365  HB3 LYS A 473      -4.923  15.429  14.093  1.00  0.00           H  
ATOM    366  HB2 LYS A 473      -3.275  14.875  13.998  1.00  0.00           H  
ATOM    367  HG3 LYS A 473      -2.471  17.256  14.264  1.00  0.00           H  
ATOM    368  HG2 LYS A 473      -4.126  17.800  14.233  1.00  0.00           H  
ATOM    369  HD3 LYS A 473      -4.449  16.942  11.963  1.00  0.00           H  
ATOM    370  HD2 LYS A 473      -2.867  16.207  11.965  1.00  0.00           H  
ATOM    371  HE3 LYS A 473      -1.819  18.504  12.192  1.00  0.00           H  
ATOM    372  HE2 LYS A 473      -3.410  19.228  12.141  1.00  0.00           H  
ATOM    373  HZ1 LYS A 473      -2.295  17.564  10.005  1.00  0.00           H  
ATOM    374  HZ2 LYS A 473      -3.727  18.381   9.975  1.00  0.00           H  
ATOM    375  HZ3 LYS A 473      -2.302  19.215  10.016  1.00  0.00           H  
ATOM    376  N   GLY A 474      -4.297  17.663  17.138  1.00 17.16           N  
ANISOU  376  N   GLY A 474     1799   3012   1710     62   -202    -43
ATOM    377  CA  GLY A 474      -5.107  18.657  17.831  1.00 21.41           C  
ANISOU  377  CA  GLY A 474     2625   3403   2105    375    238     56
ATOM    378  C   GLY A 474      -4.615  20.068  17.503  1.00 18.42           C  
ANISOU  378  C   GLY A 474     2190   2898   1907    502    -91   -436
ATOM    379  O   GLY A 474      -3.696  20.265  16.706  1.00 20.50           O  
ANISOU  379  O   GLY A 474     2507   2942   2337    562    251    315
ATOM    380  H   GLY A 474      -3.307  17.858  17.051  1.00  0.00           H  
ATOM    381  HA3 GLY A 474      -5.039  18.485  18.906  1.00  0.00           H  
ATOM    382  HA2 GLY A 474      -6.160  18.589  17.552  1.00  0.00           H  
ATOM    383  N   LYS A 475      -5.258  21.046  18.152  1.00 20.65           N  
ANISOU  383  N   LYS A 475     2135   3347   2362    951     24   -560
ATOM    384  CA  LYS A 475      -4.934  22.466  18.112  1.00 22.07           C  
ANISOU  384  CA  LYS A 475     2130   3638   2616   -197    138   -701
ATOM    385  C   LYS A 475      -4.657  22.963  19.535  1.00 20.11           C  
ANISOU  385  C   LYS A 475     2196   2934   2509     57    132   -539
ATOM    386  O   LYS A 475      -5.477  22.746  20.428  1.00 23.46           O  
ANISOU  386  O   LYS A 475     2711   3721   2481   -727    267   -913
ATOM    387  CB  LYS A 475      -6.115  23.254  17.510  1.00 21.64           C  
ANISOU  387  CB  LYS A 475     2497   2660   3063   -114   -408   -830
ATOM    388  CG  LYS A 475      -6.267  23.164  15.986  1.00 25.00           C  
ANISOU  388  CG  LYS A 475     3241   3088   3170    139     98  -1284
ATOM    389  CD  LYS A 475      -5.140  23.882  15.227  1.00 39.76           C  
ANISOU  389  CD  LYS A 475     4540   5996   4569    121   -156   1256
ATOM    390  CE  LYS A 475      -5.549  24.252  13.794  1.00 45.81           C  
ANISOU  390  CE  LYS A 475     5688   6002   5714    650   -581   2214
ATOM    391  NZ  LYS A 475      -4.527  25.080  13.134  1.00 36.72           N1+
ANISOU  391  NZ  LYS A 475     5318   4517   4115    106  -1070    952
ATOM    392  H   LYS A 475      -6.010  20.793  18.781  1.00  0.00           H  
ATOM    393  HA  LYS A 475      -4.048  22.625  17.502  1.00  0.00           H  
ATOM    394  HB3 LYS A 475      -6.021  24.310  17.766  1.00  0.00           H  
ATOM    395  HB2 LYS A 475      -7.041  22.930  17.973  1.00  0.00           H  
ATOM    396  HG3 LYS A 475      -7.225  23.610  15.719  1.00  0.00           H  
ATOM    397  HG2 LYS A 475      -6.326  22.121  15.674  1.00  0.00           H  
ATOM    398  HD3 LYS A 475      -4.265  23.232  15.197  1.00  0.00           H  
ATOM    399  HD2 LYS A 475      -4.836  24.775  15.775  1.00  0.00           H  
ATOM    400  HE3 LYS A 475      -6.479  24.821  13.803  1.00  0.00           H  
ATOM    401  HE2 LYS A 475      -5.725  23.354  13.202  1.00  0.00           H  
ATOM    402  HZ1 LYS A 475      -3.669  24.549  13.064  1.00  0.00           H  
ATOM    403  HZ2 LYS A 475      -4.843  25.329  12.208  1.00  0.00           H  
ATOM    404  HZ3 LYS A 475      -4.371  25.923  13.667  1.00  0.00           H  
ATOM    405  N   TRP A 476      -3.538  23.685  19.681  1.00 21.19           N  
ANISOU  405  N   TRP A 476     2620   3817   1612   -687    688   -154
ATOM    406  CA  TRP A 476      -3.163  24.452  20.862  1.00 19.40           C  
ANISOU  406  CA  TRP A 476     1805   2991   2573    143   -225   -391
ATOM    407  C   TRP A 476      -2.032  25.399  20.436  1.00 19.55           C  
ANISOU  407  C   TRP A 476     2338   3163   1926    114   -605   -618
ATOM    408  O   TRP A 476      -0.878  24.974  20.361  1.00 21.35           O  
ANISOU  408  O   TRP A 476     2662   2847   2603    476     85   -362
ATOM    409  CB  TRP A 476      -2.786  23.531  22.046  1.00 20.74           C  
ANISOU  409  CB  TRP A 476     2210   3160   2509    177   -394   -645
ATOM    410  CG  TRP A 476      -2.537  24.266  23.327  1.00 20.64           C  
ANISOU  410  CG  TRP A 476     2476   2732   2631   -481      9   -631
ATOM    411  CD1 TRP A 476      -3.504  24.814  24.095  1.00 24.04           C  
ANISOU  411  CD1 TRP A 476     2896   3036   3199   -442    331   -561
ATOM    412  NE1 TRP A 476      -2.933  25.493  25.148  1.00 21.31           N  
ANISOU  412  NE1 TRP A 476     2777   2812   2506   -144    698   -557
ATOM    413  CE2 TRP A 476      -1.557  25.415  25.117  1.00 19.12           C  
ANISOU  413  CE2 TRP A 476     2694   2344   2225     30    423   -227
ATOM    414  CD2 TRP A 476      -1.273  24.629  23.958  1.00 17.54           C  
ANISOU  414  CD2 TRP A 476     1856   2316   2492    290     35   -519
ATOM    415  CE3 TRP A 476       0.090  24.390  23.665  1.00 17.23           C  
ANISOU  415  CE3 TRP A 476     1758   1854   2932   -218    118   -313
ATOM    416  CZ3 TRP A 476       1.113  24.906  24.486  1.00 17.62           C  
ANISOU  416  CZ3 TRP A 476     2211   2138   2345   -162   -194   -231
ATOM    417  CH2 TRP A 476       0.799  25.679  25.620  1.00 19.60           C  
ANISOU  417  CH2 TRP A 476     2242   2599   2604     35     86   -197
ATOM    418  CZ2 TRP A 476      -0.545  25.937  25.940  1.00 19.01           C  
ANISOU  418  CZ2 TRP A 476     2812   1901   2510    318    338   -532
ATOM    419  H   TRP A 476      -2.923  23.797  18.884  1.00  0.00           H  
ATOM    420  HA  TRP A 476      -4.027  25.052  21.155  1.00  0.00           H  
ATOM    421  HB3 TRP A 476      -1.907  22.932  21.804  1.00  0.00           H  
ATOM    422  HB2 TRP A 476      -3.585  22.818  22.244  1.00  0.00           H  
ATOM    423  HD1 TRP A 476      -4.559  24.743  23.881  1.00  0.00           H  
ATOM    424  HE1 TRP A 476      -3.479  25.984  25.846  1.00  0.00           H  
ATOM    425  HE3 TRP A 476       0.345  23.801  22.796  1.00  0.00           H  
ATOM    426  HZ3 TRP A 476       2.147  24.713  24.244  1.00  0.00           H  
ATOM    427  HH2 TRP A 476       1.589  26.073  26.243  1.00  0.00           H  
ATOM    428  HZ2 TRP A 476      -0.795  26.525  26.811  1.00  0.00           H  
ATOM    429  N   HIS A 477      -2.410  26.646  20.095  1.00 20.53           N  
ANISOU  429  N   HIS A 477     1975   2989   2835    407    268   -202
ATOM    430  CA  HIS A 477      -1.567  27.673  19.459  1.00 19.80           C  
ANISOU  430  CA  HIS A 477     2544   3150   1829    337   -343    591
ATOM    431  C   HIS A 477      -1.039  27.222  18.080  1.00 22.72           C  
ANISOU  431  C   HIS A 477     2232   3627   2773    282    -78   -178
ATOM    432  O   HIS A 477       0.143  27.389  17.789  1.00 24.81           O  
ANISOU  432  O   HIS A 477     1972   5540   1913    452   -293    -64
ATOM    433  CB  HIS A 477      -0.435  28.148  20.404  1.00 21.08           C  
ANISOU  433  CB  HIS A 477     2678   2794   2534   -279   -261     34
ATOM    434  CG  HIS A 477      -0.902  28.696  21.727  1.00 20.71           C  
ANISOU  434  CG  HIS A 477     2548   2769   2550     13   -195    -48
ATOM    435  ND1 HIS A 477      -1.608  29.879  21.841  1.00 20.27           N  
ANISOU  435  ND1 HIS A 477     2463   2504   2734   -494    -20     82
ATOM    436  CE1 HIS A 477      -1.845  30.075  23.138  1.00 20.99           C  
ANISOU  436  CE1 HIS A 477     3052   1859   3063    357    319    -54
ATOM    437  NE2 HIS A 477      -1.355  29.114  23.910  1.00 18.91           N  
ANISOU  437  NE2 HIS A 477     2391   2000   2793    466   -172    -71
ATOM    438  CD2 HIS A 477      -0.757  28.229  23.013  1.00 19.51           C  
ANISOU  438  CD2 HIS A 477     2553   2119   2741     79     20   -222
ATOM    439  H   HIS A 477      -3.381  26.900  20.202  1.00  0.00           H  
ATOM    440  HA  HIS A 477      -2.218  28.527  19.267  1.00  0.00           H  
ATOM    441  HB3 HIS A 477       0.140  28.938  19.920  1.00  0.00           H  
ATOM    442  HB2 HIS A 477       0.271  27.341  20.600  1.00  0.00           H  
ATOM    443  HD1 HIS A 477      -1.913  30.487  21.087  1.00  0.00           H  
ATOM    444  HE1 HIS A 477      -2.380  30.931  23.519  1.00  0.00           H  
ATOM    445  HD2 HIS A 477      -0.260  27.336  23.357  1.00  0.00           H  
ATOM    446  N   GLY A 478      -1.921  26.624  17.266  1.00 21.07           N  
ANISOU  446  N   GLY A 478     3002   2243   2758    195   -173     -6
ATOM    447  CA  GLY A 478      -1.563  25.960  16.015  1.00 23.63           C  
ANISOU  447  CA  GLY A 478     2863   3122   2990    640   -392   -104
ATOM    448  C   GLY A 478      -1.555  24.445  16.221  1.00 19.90           C  
ANISOU  448  C   GLY A 478     2564   2943   2052   1372    -43   -320
ATOM    449  O   GLY A 478      -1.942  23.940  17.274  1.00 21.52           O  
ANISOU  449  O   GLY A 478     2568   3073   2535    159   -121   -397
ATOM    450  H   GLY A 478      -2.884  26.536  17.566  1.00  0.00           H  
ATOM    451  HA3 GLY A 478      -0.592  26.280  15.639  1.00  0.00           H  
ATOM    452  HA2 GLY A 478      -2.298  26.201  15.250  1.00  0.00           H  
ATOM    453  N   ASP A 479      -1.129  23.722  15.177  1.00 19.37           N  
ANISOU  453  N   ASP A 479     3442   2488   1429   1373    456    425
ATOM    454  CA  ASP A 479      -1.097  22.258  15.106  1.00 20.50           C  
ANISOU  454  CA  ASP A 479     2773   2533   2482    556   -332    530
ATOM    455  C   ASP A 479      -0.166  21.634  16.153  1.00 19.47           C  
ANISOU  455  C   ASP A 479     3064   2784   1549      2   -307    187
ATOM    456  O   ASP A 479       0.973  22.073  16.305  1.00 20.34           O  
ANISOU  456  O   ASP A 479     2764   2609   2353    454    219    800
ATOM    457  CB  ASP A 479      -0.722  21.755  13.691  1.00 22.53           C  
ANISOU  457  CB  ASP A 479     3153   2465   2942    682   -560   -351
ATOM    458  CG  ASP A 479      -1.623  22.291  12.570  1.00 28.13           C  
ANISOU  458  CG  ASP A 479     4262   3680   2745    977   -159   1195
ATOM    459  OD1 ASP A 479      -2.855  22.348  12.780  1.00 27.22           O  
ANISOU  459  OD1 ASP A 479     3912   4123   2306    547   -691   -144
ATOM    460  OD2 ASP A 479      -1.093  22.534  11.466  1.00 39.48           O1-
ANISOU  460  OD2 ASP A 479     6542   5326   3132   2587    601    892
ATOM    461  H   ASP A 479      -0.783  24.201  14.358  1.00  0.00           H  
ATOM    462  HA  ASP A 479      -2.110  21.916  15.328  1.00  0.00           H  
ATOM    463  HB3 ASP A 479      -0.772  20.665  13.654  1.00  0.00           H  
ATOM    464  HB2 ASP A 479       0.311  22.036  13.471  1.00  0.00           H  
ATOM    465  N   VAL A 480      -0.685  20.610  16.841  1.00 18.69           N  
ANISOU  465  N   VAL A 480     2326   2745   2029    544     96    373
ATOM    466  CA  VAL A 480       0.018  19.832  17.853  1.00 16.63           C  
ANISOU  466  CA  VAL A 480     2305   2136   1875    439    180    248
ATOM    467  C   VAL A 480      -0.388  18.352  17.740  1.00 17.81           C  
ANISOU  467  C   VAL A 480     2103   2345   2318     67     35    165
ATOM    468  O   VAL A 480      -1.468  18.047  17.234  1.00 15.90           O  
ANISOU  468  O   VAL A 480     2139   2039   1862    360    199    -33
ATOM    469  CB  VAL A 480      -0.302  20.334  19.293  1.00 16.40           C  
ANISOU  469  CB  VAL A 480     1853   2237   2139    494    245    158
ATOM    470  CG1 VAL A 480       0.294  21.725  19.563  1.00 17.91           C  
ANISOU  470  CG1 VAL A 480     2531   1862   2412    640    408    518
ATOM    471  CG2 VAL A 480      -1.791  20.312  19.686  1.00 16.53           C  
ANISOU  471  CG2 VAL A 480     2005   1832   2441     60    512    -48
ATOM    472  H   VAL A 480      -1.637  20.319  16.658  1.00  0.00           H  
ATOM    473  HA  VAL A 480       1.095  19.890  17.682  1.00  0.00           H  
ATOM    474  HB  VAL A 480       0.202  19.654  19.975  1.00  0.00           H  
ATOM    475 HG11 VAL A 480       0.241  21.983  20.621  1.00  0.00           H  
ATOM    476 HG12 VAL A 480       1.340  21.761  19.262  1.00  0.00           H  
ATOM    477 HG13 VAL A 480      -0.235  22.501  19.011  1.00  0.00           H  
ATOM    478 HG21 VAL A 480      -1.924  20.593  20.731  1.00  0.00           H  
ATOM    479 HG22 VAL A 480      -2.358  21.021  19.086  1.00  0.00           H  
ATOM    480 HG23 VAL A 480      -2.241  19.330  19.558  1.00  0.00           H  
ATOM    481  N   ALA A 481       0.482  17.462  18.236  1.00 15.89           N  
ANISOU  481  N   ALA A 481     2083   2103   1848    -55   -358   -307
ATOM    482  CA  ALA A 481       0.141  16.074  18.534  1.00 15.18           C  
ANISOU  482  CA  ALA A 481     1851   2069   1847    193    193      1
ATOM    483  C   ALA A 481      -0.225  15.990  20.021  1.00 15.27           C  
ANISOU  483  C   ALA A 481     2245   1911   1643    107      6   -230
ATOM    484  O   ALA A 481       0.453  16.612  20.839  1.00 16.53           O  
ANISOU  484  O   ALA A 481     1876   2237   2166     28   -290   -120
ATOM    485  CB  ALA A 481       1.338  15.171  18.210  1.00 16.29           C  
ANISOU  485  CB  ALA A 481     1950   1928   2310    211     45     11
ATOM    486  H   ALA A 481       1.353  17.792  18.634  1.00  0.00           H  
ATOM    487  HA  ALA A 481      -0.707  15.747  17.930  1.00  0.00           H  
ATOM    488  HB1 ALA A 481       1.115  14.127  18.431  1.00  0.00           H  
ATOM    489  HB2 ALA A 481       1.606  15.232  17.156  1.00  0.00           H  
ATOM    490  HB3 ALA A 481       2.218  15.453  18.783  1.00  0.00           H  
ATOM    491  N   VAL A 482      -1.289  15.240  20.339  1.00 18.26           N  
ANISOU  491  N   VAL A 482     2145   2615   2176    256    205   -198
ATOM    492  CA  VAL A 482      -1.831  15.111  21.690  1.00 17.79           C  
ANISOU  492  CA  VAL A 482     2550   2044   2164    489    422    239
ATOM    493  C   VAL A 482      -2.011  13.617  22.000  1.00 16.20           C  
ANISOU  493  C   VAL A 482     2391   1952   1809   -202    347    -98
ATOM    494  O   VAL A 482      -2.774  12.950  21.305  1.00 19.01           O  
ANISOU  494  O   VAL A 482     2172   2490   2561   -959   -181    320
ATOM    495  CB  VAL A 482      -3.229  15.790  21.830  1.00 18.96           C  
ANISOU  495  CB  VAL A 482     2131   2871   2199    387    322    152
ATOM    496  CG1 VAL A 482      -3.744  15.789  23.285  1.00 25.27           C  
ANISOU  496  CG1 VAL A 482     2668   4015   2916     94   1160    327
ATOM    497  CG2 VAL A 482      -3.245  17.229  21.285  1.00 22.06           C  
ANISOU  497  CG2 VAL A 482     3173   2861   2344    792    627   -241
ATOM    498  H   VAL A 482      -1.798  14.755  19.609  1.00  0.00           H  
ATOM    499  HA  VAL A 482      -1.154  15.550  22.422  1.00  0.00           H  
ATOM    500  HB  VAL A 482      -3.956  15.235  21.232  1.00  0.00           H  
ATOM    501 HG11 VAL A 482      -4.748  16.208  23.347  1.00  0.00           H  
ATOM    502 HG12 VAL A 482      -3.790  14.789  23.711  1.00  0.00           H  
ATOM    503 HG13 VAL A 482      -3.096  16.384  23.929  1.00  0.00           H  
ATOM    504 HG21 VAL A 482      -4.223  17.689  21.421  1.00  0.00           H  
ATOM    505 HG22 VAL A 482      -2.505  17.854  21.786  1.00  0.00           H  
ATOM    506 HG23 VAL A 482      -3.038  17.248  20.216  1.00  0.00           H  
ATOM    507  N   LYS A 483      -1.341  13.131  23.053  1.00 15.45           N  
ANISOU  507  N   LYS A 483     2008   2033   1829   -186    290   -341
ATOM    508  CA  LYS A 483      -1.522  11.785  23.594  1.00 18.22           C  
ANISOU  508  CA  LYS A 483     2558   2044   2318     28    694   -394
ATOM    509  C   LYS A 483      -2.399  11.887  24.842  1.00 18.38           C  
ANISOU  509  C   LYS A 483     1876   2812   2292   -439    539   -193
ATOM    510  O   LYS A 483      -1.938  12.456  25.823  1.00 20.16           O  
ANISOU  510  O   LYS A 483     2805   3174   1681   -733    454     53
ATOM    511  CB  LYS A 483      -0.144  11.176  23.914  1.00 16.83           C  
ANISOU  511  CB  LYS A 483     2087   2369   1935   -518    485   -246
ATOM    512  CG  LYS A 483      -0.215   9.773  24.553  1.00 18.97           C  
ANISOU  512  CG  LYS A 483     2826   2547   1834    244    607   -105
ATOM    513  CD  LYS A 483       1.160   9.144  24.804  1.00 19.40           C  
ANISOU  513  CD  LYS A 483     2906   2526   1938   -118    441    576
ATOM    514  CE  LYS A 483       1.917   8.844  23.502  1.00 17.62           C  
ANISOU  514  CE  LYS A 483     2012   2484   2196    251    224      6
ATOM    515  NZ  LYS A 483       3.159   8.104  23.750  1.00 17.91           N1+
ANISOU  515  NZ  LYS A 483     2269   2085   2450    540    395    337
ATOM    516  H   LYS A 483      -0.737  13.746  23.586  1.00  0.00           H  
ATOM    517  HA  LYS A 483      -2.009  11.136  22.868  1.00  0.00           H  
ATOM    518  HB3 LYS A 483       0.407  11.838  24.583  1.00  0.00           H  
ATOM    519  HB2 LYS A 483       0.427  11.139  22.988  1.00  0.00           H  
ATOM    520  HG3 LYS A 483      -0.809   9.110  23.921  1.00  0.00           H  
ATOM    521  HG2 LYS A 483      -0.736   9.820  25.510  1.00  0.00           H  
ATOM    522  HD3 LYS A 483       1.024   8.231  25.387  1.00  0.00           H  
ATOM    523  HD2 LYS A 483       1.752   9.813  25.432  1.00  0.00           H  
ATOM    524  HE3 LYS A 483       2.177   9.764  22.978  1.00  0.00           H  
ATOM    525  HE2 LYS A 483       1.295   8.253  22.830  1.00  0.00           H  
ATOM    526  HZ1 LYS A 483       3.762   8.650  24.358  1.00  0.00           H  
ATOM    527  HZ2 LYS A 483       2.945   7.229  24.210  1.00  0.00           H  
ATOM    528  HZ3 LYS A 483       3.625   7.929  22.870  1.00  0.00           H  
ATOM    529  N   MET A 484      -3.616  11.330  24.779  1.00 20.01           N  
ANISOU  529  N   MET A 484     2220   2264   3119   -627    665   -144
ATOM    530  CA  MET A 484      -4.602  11.341  25.860  1.00 22.68           C  
ANISOU  530  CA  MET A 484     3546   2754   2316   -687   1047    -34
ATOM    531  C   MET A 484      -4.693   9.980  26.553  1.00 22.12           C  
ANISOU  531  C   MET A 484     3736   2235   2433    132    221    -39
ATOM    532  O   MET A 484      -4.505   8.955  25.902  1.00 22.28           O  
ANISOU  532  O   MET A 484     3557   2358   2549    -75   1148   -212
ATOM    533  CB  MET A 484      -5.994  11.610  25.264  1.00 29.12           C  
ANISOU  533  CB  MET A 484     3427   3711   3926    403   1665    595
ATOM    534  CG  MET A 484      -6.185  12.998  24.654  1.00 39.20           C  
ANISOU  534  CG  MET A 484     3942   6329   4621    292    947   2664
ATOM    535  SD  MET A 484      -7.732  13.161  23.727  1.00 56.11           S  
ANISOU  535  SD  MET A 484     4334   7993   8991   1405   -322   2845
ATOM    536  CE  MET A 484      -8.956  12.579  24.933  1.00 69.98           C  
ANISOU  536  CE  MET A 484     7557  13029   6002   2219   3960   3636
ATOM    537  H   MET A 484      -3.895  10.847  23.934  1.00  0.00           H  
ATOM    538  HA  MET A 484      -4.368  12.113  26.594  1.00  0.00           H  
ATOM    539  HB3 MET A 484      -6.737  11.489  26.054  1.00  0.00           H  
ATOM    540  HB2 MET A 484      -6.231  10.854  24.512  1.00  0.00           H  
ATOM    541  HG3 MET A 484      -5.377  13.217  23.958  1.00  0.00           H  
ATOM    542  HG2 MET A 484      -6.153  13.761  25.432  1.00  0.00           H  
ATOM    543  HE1 MET A 484      -9.962  12.765  24.559  1.00  0.00           H  
ATOM    544  HE2 MET A 484      -8.855  11.508  25.109  1.00  0.00           H  
ATOM    545  HE3 MET A 484      -8.837  13.105  25.881  1.00  0.00           H  
ATOM    546  N   LEU A 485      -5.112  10.004  27.824  1.00 24.38           N  
ANISOU  546  N   LEU A 485     3135   3017   3111   -930    866    -45
ATOM    547  CA  LEU A 485      -5.635   8.849  28.541  1.00 25.53           C  
ANISOU  547  CA  LEU A 485     3534   3401   2762   -336   1058    557
ATOM    548  C   LEU A 485      -7.137   9.091  28.747  1.00 31.35           C  
ANISOU  548  C   LEU A 485     3764   4647   3500   -641   2085    430
ATOM    549  O   LEU A 485      -7.519   9.813  29.668  1.00 31.16           O  
ANISOU  549  O   LEU A 485     4109   3912   3817    -71   2046    600
ATOM    550  CB  LEU A 485      -4.869   8.704  29.870  1.00 25.91           C  
ANISOU  550  CB  LEU A 485     4171   3011   2661    109   1168    957
ATOM    551  CG  LEU A 485      -5.168   7.410  30.653  1.00 31.25           C  
ANISOU  551  CG  LEU A 485     5116   3513   3242   -889   1507    882
ATOM    552  CD1 LEU A 485      -4.705   6.137  29.921  1.00 37.45           C  
ANISOU  552  CD1 LEU A 485     6540   3397   4291    212   1987   1531
ATOM    553  CD2 LEU A 485      -4.570   7.504  32.062  1.00 40.58           C  
ANISOU  553  CD2 LEU A 485     6893   4924   3601    264    361   1943
ATOM    554  H   LEU A 485      -5.222  10.895  28.292  1.00  0.00           H  
ATOM    555  HA  LEU A 485      -5.506   7.940  27.953  1.00  0.00           H  
ATOM    556  HB3 LEU A 485      -5.098   9.564  30.496  1.00  0.00           H  
ATOM    557  HB2 LEU A 485      -3.797   8.762  29.684  1.00  0.00           H  
ATOM    558  HG  LEU A 485      -6.245   7.334  30.767  1.00  0.00           H  
ATOM    559 HD11 LEU A 485      -5.546   5.473  29.720  1.00  0.00           H  
ATOM    560 HD12 LEU A 485      -4.235   6.364  28.965  1.00  0.00           H  
ATOM    561 HD13 LEU A 485      -3.977   5.572  30.504  1.00  0.00           H  
ATOM    562 HD21 LEU A 485      -4.975   6.734  32.718  1.00  0.00           H  
ATOM    563 HD22 LEU A 485      -3.486   7.402  32.031  1.00  0.00           H  
ATOM    564 HD23 LEU A 485      -4.785   8.470  32.518  1.00  0.00           H  
ATOM    565  N   ASN A 486      -7.958   8.505  27.862  1.00 29.95           N  
ANISOU  565  N   ASN A 486     3926   4104   3348    716    883   1006
ATOM    566  CA  ASN A 486      -9.412   8.654  27.852  1.00 34.51           C  
ANISOU  566  CA  ASN A 486     3870   4462   4780   -618   1381    281
ATOM    567  C   ASN A 486     -10.070   7.682  28.854  1.00 32.34           C  
ANISOU  567  C   ASN A 486     3867   3272   5149  -1262    482    581
ATOM    568  O   ASN A 486     -10.685   6.696  28.448  1.00 35.52           O  
ANISOU  568  O   ASN A 486     4177   4354   4964  -1806    848   -250
ATOM    569  CB  ASN A 486      -9.936   8.507  26.400  1.00 41.10           C  
ANISOU  569  CB  ASN A 486     3958   6250   5405    447   -176   -199
ATOM    570  CG  ASN A 486     -11.342   9.080  26.161  1.00 45.94           C  
ANISOU  570  CG  ASN A 486     5215   8979   3258   1792  -1831   -177
ATOM    571  OD1 ASN A 486     -12.005   9.577  27.070  1.00 47.64           O  
ANISOU  571  OD1 ASN A 486     4892   6950   6259    896    375    789
ATOM    572  ND2 ASN A 486     -11.809   9.009  24.913  1.00 49.58           N  
ANISOU  572  ND2 ASN A 486     5992   8894   3952   3296  -2247  -1908
ATOM    573  H   ASN A 486      -7.567   7.913  27.138  1.00  0.00           H  
ATOM    574  HA  ASN A 486      -9.671   9.649  28.198  1.00  0.00           H  
ATOM    575  HB3 ASN A 486      -9.890   7.470  26.065  1.00  0.00           H  
ATOM    576  HB2 ASN A 486      -9.272   9.064  25.737  1.00  0.00           H  
ATOM    577 HD22 ASN A 486     -12.727   9.371  24.699  1.00  0.00           H  
ATOM    578 HD21 ASN A 486     -11.251   8.600  24.178  1.00  0.00           H  
ATOM    579  N   VAL A 487      -9.906   7.988  30.150  1.00 34.68           N  
ANISOU  579  N   VAL A 487     4822   3313   5040  -1874   1057     56
ATOM    580  CA  VAL A 487     -10.457   7.237  31.279  1.00 36.98           C  
ANISOU  580  CA  VAL A 487     4268   5266   4516  -1944    885    239
ATOM    581  C   VAL A 487     -10.986   8.222  32.338  1.00 44.34           C  
ANISOU  581  C   VAL A 487     5792   6680   4374   -893   1563    785
ATOM    582  O   VAL A 487     -10.550   9.375  32.385  1.00 43.22           O  
ANISOU  582  O   VAL A 487     5816   5200   5405   1717   2545    522
ATOM    583  CB  VAL A 487      -9.386   6.324  31.953  1.00 36.21           C  
ANISOU  583  CB  VAL A 487     6480   4197   3080  -1425    970   -363
ATOM    584  CG1 VAL A 487      -8.777   5.305  30.972  1.00 44.28           C  
ANISOU  584  CG1 VAL A 487     8180   3665   4978   -115     32  -1142
ATOM    585  CG2 VAL A 487      -8.282   7.072  32.729  1.00 42.06           C  
ANISOU  585  CG2 VAL A 487     6603   7509   1867  -1299    313     75
ATOM    586  H   VAL A 487      -9.383   8.817  30.394  1.00  0.00           H  
ATOM    587  HA  VAL A 487     -11.297   6.626  30.943  1.00  0.00           H  
ATOM    588  HB  VAL A 487      -9.910   5.717  32.693  1.00  0.00           H  
ATOM    589 HG11 VAL A 487      -8.125   4.602  31.491  1.00  0.00           H  
ATOM    590 HG12 VAL A 487      -9.555   4.727  30.474  1.00  0.00           H  
ATOM    591 HG13 VAL A 487      -8.180   5.795  30.203  1.00  0.00           H  
ATOM    592 HG21 VAL A 487      -7.476   6.400  33.021  1.00  0.00           H  
ATOM    593 HG22 VAL A 487      -7.853   7.877  32.135  1.00  0.00           H  
ATOM    594 HG23 VAL A 487      -8.667   7.522  33.642  1.00  0.00           H  
ATOM    595  N   THR A 488     -11.904   7.730  33.186  1.00 49.93           N  
ANISOU  595  N   THR A 488     7569   5177   6222  -1918   2393    851
ATOM    596  CA  THR A 488     -12.492   8.476  34.301  1.00 57.86           C  
ANISOU  596  CA  THR A 488     8360   7769   5854   -685   1086    -83
ATOM    597  C   THR A 488     -11.484   8.740  35.437  1.00 57.32           C  
ANISOU  597  C   THR A 488     8468   5230   8080  -1110    343   -793
ATOM    598  O   THR A 488     -11.381   9.873  35.905  1.00 55.66           O  
ANISOU  598  O   THR A 488     8858   4651   7638   -165   2948     -8
ATOM    599  CB  THR A 488     -13.698   7.709  34.913  1.00 65.80           C  
ANISOU  599  CB  THR A 488     6806   9931   8262  -1394   1168   -743
ATOM    600  OG1 THR A 488     -14.631   7.411  33.894  1.00 58.45           O  
ANISOU  600  OG1 THR A 488     7561   7020   7625  -2420   3348  -1749
ATOM    601  CG2 THR A 488     -14.442   8.446  36.042  1.00 69.68           C  
ANISOU  601  CG2 THR A 488     5530  10092  10851   -802   1020  -1599
ATOM    602  H   THR A 488     -12.238   6.784  33.068  1.00  0.00           H  
ATOM    603  HA  THR A 488     -12.843   9.437  33.922  1.00  0.00           H  
ATOM    604  HB  THR A 488     -13.357   6.748  35.301  1.00  0.00           H  
ATOM    605  HG1 THR A 488     -15.432   7.072  34.301  1.00  0.00           H  
ATOM    606 HG21 THR A 488     -15.329   7.893  36.353  1.00  0.00           H  
ATOM    607 HG22 THR A 488     -13.819   8.570  36.928  1.00  0.00           H  
ATOM    608 HG23 THR A 488     -14.764   9.437  35.722  1.00  0.00           H  
ATOM    609  N   ALA A 489     -10.766   7.681  35.842  1.00 52.17           N  
ANISOU  609  N   ALA A 489     8227   5368   6225   -868   1147   -674
ATOM    610  CA  ALA A 489      -9.819   7.679  36.947  1.00 49.36           C  
ANISOU  610  CA  ALA A 489     6179   5430   7146   -770   1251    113
ATOM    611  C   ALA A 489      -8.588   6.870  36.508  1.00 45.77           C  
ANISOU  611  C   ALA A 489     6011   5975   5404   -678   2520    844
ATOM    612  O   ALA A 489      -8.690   5.644  36.428  1.00 52.43           O  
ANISOU  612  O   ALA A 489     6481   5193   8246     43   1708   1736
ATOM    613  CB  ALA A 489     -10.501   7.042  38.171  1.00 52.96           C  
ANISOU  613  CB  ALA A 489     5772   5322   9028   -851   1155   1804
ATOM    614  H   ALA A 489     -10.893   6.792  35.379  1.00  0.00           H  
ATOM    615  HA  ALA A 489      -9.544   8.695  37.231  1.00  0.00           H  
ATOM    616  HB1 ALA A 489      -9.812   6.977  39.014  1.00  0.00           H  
ATOM    617  HB2 ALA A 489     -11.355   7.638  38.493  1.00  0.00           H  
ATOM    618  HB3 ALA A 489     -10.865   6.036  37.960  1.00  0.00           H  
ATOM    619  N   PRO A 490      -7.455   7.551  36.215  1.00 40.28           N  
ANISOU  619  N   PRO A 490     6850   3729   4726   -489   2002   1851
ATOM    620  CA  PRO A 490      -6.162   6.887  35.974  1.00 41.14           C  
ANISOU  620  CA  PRO A 490     5876   4373   5380  -1413   1606   2791
ATOM    621  C   PRO A 490      -5.705   5.999  37.140  1.00 36.01           C  
ANISOU  621  C   PRO A 490     6014   3616   4051  -1063   1082   1247
ATOM    622  O   PRO A 490      -5.669   6.455  38.284  1.00 47.86           O  
ANISOU  622  O   PRO A 490     8802   5545   3837  -1111   1673   1511
ATOM    623  CB  PRO A 490      -5.179   8.048  35.742  1.00 36.16           C  
ANISOU  623  CB  PRO A 490     4853   5173   3713  -1724   2150   1612
ATOM    624  CG  PRO A 490      -6.053   9.189  35.259  1.00 36.73           C  
ANISOU  624  CG  PRO A 490     4803   4248   4903  -1789    818   -208
ATOM    625  CD  PRO A 490      -7.337   8.999  36.050  1.00 38.39           C  
ANISOU  625  CD  PRO A 490     6260   3674   4652   -710   1744    805
ATOM    626  HA  PRO A 490      -6.257   6.303  35.058  1.00  0.00           H  
ATOM    627  HB3 PRO A 490      -4.396   7.791  35.028  1.00  0.00           H  
ATOM    628  HB2 PRO A 490      -4.687   8.346  36.670  1.00  0.00           H  
ATOM    629  HG3 PRO A 490      -6.261   9.048  34.201  1.00  0.00           H  
ATOM    630  HG2 PRO A 490      -5.606  10.173  35.395  1.00  0.00           H  
ATOM    631  HD2 PRO A 490      -7.255   9.463  37.034  1.00  0.00           H  
ATOM    632  HD3 PRO A 490      -8.183   9.443  35.522  1.00  0.00           H  
ATOM    633  N   THR A 491      -5.349   4.753  36.802  1.00 39.26           N  
ANISOU  633  N   THR A 491     6656   3088   5172  -1234   1759   1011
ATOM    634  CA  THR A 491      -4.664   3.790  37.668  1.00 40.22           C  
ANISOU  634  CA  THR A 491     6627   4243   4409  -1535    911    719
ATOM    635  C   THR A 491      -3.290   4.364  38.115  1.00 42.12           C  
ANISOU  635  C   THR A 491     6695   4469   4836  -1830    245   2163
ATOM    636  O   THR A 491      -2.684   5.104  37.340  1.00 41.28           O  
ANISOU  636  O   THR A 491     5388   4905   5392   -304   1412   2843
ATOM    637  CB  THR A 491      -4.455   2.483  36.839  1.00 39.24           C  
ANISOU  637  CB  THR A 491     6441   1680   6787   -774   -147    889
ATOM    638  OG1 THR A 491      -5.629   1.704  36.932  1.00 50.08           O  
ANISOU  638  OG1 THR A 491     7253   4936   6836  -2389   2663    -43
ATOM    639  CG2 THR A 491      -3.258   1.569  37.146  1.00 50.60           C  
ANISOU  639  CG2 THR A 491     3988   8437   6800   -239   1949  -1542
ATOM    640  H   THR A 491      -5.452   4.467  35.838  1.00  0.00           H  
ATOM    641  HA  THR A 491      -5.321   3.598  38.515  1.00  0.00           H  
ATOM    642  HB  THR A 491      -4.360   2.747  35.788  1.00  0.00           H  
ATOM    643  HG1 THR A 491      -5.483   0.869  36.479  1.00  0.00           H  
ATOM    644 HG21 THR A 491      -3.308   0.650  36.560  1.00  0.00           H  
ATOM    645 HG22 THR A 491      -2.332   2.058  36.866  1.00  0.00           H  
ATOM    646 HG23 THR A 491      -3.206   1.285  38.195  1.00  0.00           H  
ATOM    647  N   PRO A 492      -2.811   4.036  39.340  1.00 40.10           N  
ANISOU  647  N   PRO A 492     6045   4783   4405     72   1324   2614
ATOM    648  CA  PRO A 492      -1.459   4.412  39.812  1.00 45.75           C  
ANISOU  648  CA  PRO A 492     7595   4688   5100  -1270    426   2655
ATOM    649  C   PRO A 492      -0.276   4.165  38.848  1.00 43.48           C  
ANISOU  649  C   PRO A 492     8284   4139   4096   -468   -114    541
ATOM    650  O   PRO A 492       0.597   5.027  38.764  1.00 52.29           O  
ANISOU  650  O   PRO A 492     8518   6309   5041  -1406   -695   1308
ATOM    651  CB  PRO A 492      -1.307   3.631  41.125  1.00 50.41           C  
ANISOU  651  CB  PRO A 492     8993   5863   4294   -146   -250   2448
ATOM    652  CG  PRO A 492      -2.724   3.543  41.661  1.00 50.00           C  
ANISOU  652  CG  PRO A 492    10206   6487   2304    256   1444   3650
ATOM    653  CD  PRO A 492      -3.564   3.363  40.402  1.00 46.00           C  
ANISOU  653  CD  PRO A 492     7145   5307   5026   -799   1473   2763
ATOM    654  HA  PRO A 492      -1.497   5.479  40.039  1.00  0.00           H  
ATOM    655  HB3 PRO A 492      -0.628   4.116  41.828  1.00  0.00           H  
ATOM    656  HB2 PRO A 492      -0.927   2.626  40.936  1.00  0.00           H  
ATOM    657  HG3 PRO A 492      -2.986   4.488  42.140  1.00  0.00           H  
ATOM    658  HG2 PRO A 492      -2.865   2.747  42.393  1.00  0.00           H  
ATOM    659  HD2 PRO A 492      -3.669   2.305  40.163  1.00  0.00           H  
ATOM    660  HD3 PRO A 492      -4.559   3.784  40.554  1.00  0.00           H  
ATOM    661  N   GLN A 493      -0.294   3.043  38.103  1.00 37.00           N  
ANISOU  661  N   GLN A 493     7911   2645   3501  -2381    -52   1624
ATOM    662  CA  GLN A 493       0.662   2.740  37.030  1.00 42.99           C  
ANISOU  662  CA  GLN A 493     7035   4570   4726   -735   -357   1909
ATOM    663  C   GLN A 493       0.523   3.701  35.833  1.00 36.76           C  
ANISOU  663  C   GLN A 493     4729   4679   4558  -1662   -719   1949
ATOM    664  O   GLN A 493       1.549   4.148  35.327  1.00 39.77           O  
ANISOU  664  O   GLN A 493     5060   5068   4981  -1393   -620   2345
ATOM    665  CB  GLN A 493       0.543   1.248  36.619  1.00  0.00           C  
ATOM    666  CG  GLN A 493       1.635   0.700  35.662  1.00  0.00           C  
ATOM    667  CD  GLN A 493       1.503   1.073  34.177  1.00  0.00           C  
ATOM    668  OE1 GLN A 493       2.495   1.407  33.535  1.00  0.00           O  
ATOM    669  NE2 GLN A 493       0.290   1.021  33.620  1.00  0.00           N  
ATOM    670  H   GLN A 493      -1.038   2.374  38.237  1.00  0.00           H  
ATOM    671  HA  GLN A 493       1.662   2.884  37.446  1.00  0.00           H  
ATOM    672  HB2 GLN A 493       0.604   0.655  37.533  1.00  0.00           H  
ATOM    673  HB3 GLN A 493      -0.446   1.038  36.215  1.00  0.00           H  
ATOM    674  HG2 GLN A 493       2.620   1.003  36.020  1.00  0.00           H  
ATOM    675  HG3 GLN A 493       1.625  -0.389  35.709  1.00  0.00           H  
ATOM    676 HE22 GLN A 493       0.175   1.260  32.646  1.00  0.00           H  
ATOM    677 HE21 GLN A 493      -0.512   0.732  34.160  1.00  0.00           H  
ATOM    678  N   GLN A 494      -0.718   4.009  35.410  1.00 33.30           N  
ANISOU  678  N   GLN A 494     4974   2410   5268  -1979   -635   2318
ATOM    679  CA  GLN A 494      -1.015   4.949  34.321  1.00 33.50           C  
ANISOU  679  CA  GLN A 494     4839   3161   4726  -2074  -1081   2091
ATOM    680  C   GLN A 494      -0.570   6.389  34.624  1.00 33.19           C  
ANISOU  680  C   GLN A 494     4300   3545   4764  -2076   -124   1420
ATOM    681  O   GLN A 494      -0.024   7.042  33.736  1.00 30.62           O  
ANISOU  681  O   GLN A 494     4906   3395   3332  -1602    421    623
ATOM    682  CB  GLN A 494      -2.516   4.924  33.968  1.00 33.29           C  
ANISOU  682  CB  GLN A 494     4580   2902   5165  -1936  -1123   1303
ATOM    683  CG  GLN A 494      -2.988   3.626  33.291  1.00 35.15           C  
ANISOU  683  CG  GLN A 494     5213   2573   5570  -1478   -574   1302
ATOM    684  CD  GLN A 494      -4.489   3.647  32.977  1.00 37.87           C  
ANISOU  684  CD  GLN A 494     5295   3689   5405  -2040   -512   -585
ATOM    685  OE1 GLN A 494      -5.292   4.148  33.761  1.00 36.94           O  
ANISOU  685  OE1 GLN A 494     4520   3586   5929  -1391    734   1250
ATOM    686  NE2 GLN A 494      -4.882   3.075  31.840  1.00 33.21           N  
ANISOU  686  NE2 GLN A 494     4981   3381   4255  -1269    458   -599
ATOM    687  H   GLN A 494      -1.517   3.628  35.896  1.00  0.00           H  
ATOM    688  HA  GLN A 494      -0.456   4.618  33.443  1.00  0.00           H  
ATOM    689  HB3 GLN A 494      -2.726   5.746  33.287  1.00  0.00           H  
ATOM    690  HB2 GLN A 494      -3.112   5.122  34.857  1.00  0.00           H  
ATOM    691  HG3 GLN A 494      -2.787   2.770  33.936  1.00  0.00           H  
ATOM    692  HG2 GLN A 494      -2.421   3.466  32.373  1.00  0.00           H  
ATOM    693 HE22 GLN A 494      -5.860   3.054  31.594  1.00  0.00           H  
ATOM    694 HE21 GLN A 494      -4.199   2.690  31.197  1.00  0.00           H  
ATOM    695  N   LEU A 495      -0.778   6.837  35.876  1.00 36.62           N  
ANISOU  695  N   LEU A 495     5898   2988   5028   -915    365   1122
ATOM    696  CA  LEU A 495      -0.312   8.124  36.391  1.00 34.57           C  
ANISOU  696  CA  LEU A 495     5346   4002   3784  -1047     29   1128
ATOM    697  C   LEU A 495       1.223   8.210  36.442  1.00 35.35           C  
ANISOU  697  C   LEU A 495     5517   4234   3677   -157    267   1857
ATOM    698  O   LEU A 495       1.770   9.255  36.091  1.00 33.91           O  
ANISOU  698  O   LEU A 495     5570   4270   3042   -352    799   1156
ATOM    699  CB  LEU A 495      -0.959   8.391  37.771  1.00 41.43           C  
ANISOU  699  CB  LEU A 495     6529   4987   4225  -1700   1749   1799
ATOM    700  CG  LEU A 495      -0.546   9.714  38.468  1.00 49.72           C  
ANISOU  700  CG  LEU A 495     8355   4735   5801  -2196   1305   2028
ATOM    701  CD1 LEU A 495      -0.859  10.958  37.607  1.00 43.98           C  
ANISOU  701  CD1 LEU A 495     9083   5842   1785   -604   1115   1000
ATOM    702  CD2 LEU A 495      -1.161   9.810  39.880  1.00 54.75           C  
ANISOU  702  CD2 LEU A 495     7192   6253   7355  -3393   2388    658
ATOM    703  H   LEU A 495      -1.253   6.237  36.539  1.00  0.00           H  
ATOM    704  HA  LEU A 495      -0.658   8.889  35.696  1.00  0.00           H  
ATOM    705  HB3 LEU A 495      -0.718   7.558  38.434  1.00  0.00           H  
ATOM    706  HB2 LEU A 495      -2.045   8.373  37.660  1.00  0.00           H  
ATOM    707  HG  LEU A 495       0.533   9.694  38.623  1.00  0.00           H  
ATOM    708 HD11 LEU A 495      -1.255  11.787  38.194  1.00  0.00           H  
ATOM    709 HD12 LEU A 495       0.043  11.323  37.115  1.00  0.00           H  
ATOM    710 HD13 LEU A 495      -1.591  10.740  36.830  1.00  0.00           H  
ATOM    711 HD21 LEU A 495      -0.387   9.972  40.630  1.00  0.00           H  
ATOM    712 HD22 LEU A 495      -1.880  10.624  39.972  1.00  0.00           H  
ATOM    713 HD23 LEU A 495      -1.687   8.895  40.157  1.00  0.00           H  
ATOM    714  N   GLN A 496       1.886   7.114  36.855  1.00 34.74           N  
ANISOU  714  N   GLN A 496     5416   4119   3664   -519    279   2918
ATOM    715  CA  GLN A 496       3.342   7.037  36.932  1.00 37.34           C  
ANISOU  715  CA  GLN A 496     5286   4743   4158  -1389   -645   2077
ATOM    716  C   GLN A 496       3.998   6.987  35.542  1.00 34.61           C  
ANISOU  716  C   GLN A 496     4780   4725   3643   -678  -1165   1380
ATOM    717  O   GLN A 496       5.006   7.661  35.349  1.00 36.70           O  
ANISOU  717  O   GLN A 496     5367   5139   3439  -1275  -1463   1195
ATOM    718  CB  GLN A 496       3.766   5.842  37.815  1.00 45.43           C  
ANISOU  718  CB  GLN A 496     6302   4364   6593  -2141  -1194   3077
ATOM    719  CG  GLN A 496       5.271   5.804  38.165  1.00 54.22           C  
ANISOU  719  CG  GLN A 496     5773   6872   7956  -2133    136   3660
ATOM    720  CD  GLN A 496       5.714   7.030  38.971  1.00 55.86           C  
ANISOU  720  CD  GLN A 496     6344   7612   7266  -2042   -667   3485
ATOM    721  OE1 GLN A 496       5.166   7.306  40.036  1.00 63.40           O  
ANISOU  721  OE1 GLN A 496     8230   8325   7532  -3870   -779   2703
ATOM    722  NE2 GLN A 496       6.704   7.774  38.478  1.00 58.76           N  
ANISOU  722  NE2 GLN A 496     6289   9074   6963  -2082  -1326   3519
ATOM    723  H   GLN A 496       1.373   6.291  37.143  1.00  0.00           H  
ATOM    724  HA  GLN A 496       3.674   7.958  37.416  1.00  0.00           H  
ATOM    725  HB3 GLN A 496       3.484   4.907  37.330  1.00  0.00           H  
ATOM    726  HB2 GLN A 496       3.197   5.868  38.746  1.00  0.00           H  
ATOM    727  HG3 GLN A 496       5.875   5.707  37.262  1.00  0.00           H  
ATOM    728  HG2 GLN A 496       5.479   4.917  38.764  1.00  0.00           H  
ATOM    729 HE22 GLN A 496       7.027   8.580  38.991  1.00  0.00           H  
ATOM    730 HE21 GLN A 496       7.141   7.549  37.594  1.00  0.00           H  
ATOM    731  N   ALA A 497       3.397   6.240  34.599  1.00 29.09           N  
ANISOU  731  N   ALA A 497     3972   3237   3842   -299    -50    778
ATOM    732  CA  ALA A 497       3.800   6.166  33.192  1.00 30.16           C  
ANISOU  732  CA  ALA A 497     4572   2926   3958  -1005   -185   1319
ATOM    733  C   ALA A 497       3.719   7.528  32.485  1.00 23.26           C  
ANISOU  733  C   ALA A 497     3384   2458   2994   -816    415    703
ATOM    734  O   ALA A 497       4.661   7.895  31.784  1.00 27.42           O  
ANISOU  734  O   ALA A 497     3965   3406   3046  -1950    186   1209
ATOM    735  CB  ALA A 497       2.935   5.119  32.471  1.00 29.66           C  
ANISOU  735  CB  ALA A 497     3890   2727   4651   -801    216    783
ATOM    736  H   ALA A 497       2.583   5.693  34.851  1.00  0.00           H  
ATOM    737  HA  ALA A 497       4.839   5.832  33.161  1.00  0.00           H  
ATOM    738  HB1 ALA A 497       3.197   5.038  31.417  1.00  0.00           H  
ATOM    739  HB2 ALA A 497       3.069   4.133  32.915  1.00  0.00           H  
ATOM    740  HB3 ALA A 497       1.874   5.365  32.528  1.00  0.00           H  
ATOM    741  N   PHE A 498       2.631   8.270  32.753  1.00 22.42           N  
ANISOU  741  N   PHE A 498     3511   2551   2454   -865    439   1002
ATOM    742  CA  PHE A 498       2.432   9.664  32.362  1.00 22.83           C  
ANISOU  742  CA  PHE A 498     3819   2782   2073   -662   -221   1028
ATOM    743  C   PHE A 498       3.509  10.619  32.913  1.00 25.88           C  
ANISOU  743  C   PHE A 498     4737   3426   1669   -986    -66    301
ATOM    744  O   PHE A 498       4.088  11.374  32.134  1.00 24.44           O  
ANISOU  744  O   PHE A 498     4193   3067   2022   -515    334    202
ATOM    745  CB  PHE A 498       0.982  10.084  32.704  1.00 27.58           C  
ANISOU  745  CB  PHE A 498     4546   3264   2667   -728    767   -187
ATOM    746  CG  PHE A 498       0.685  11.574  32.717  1.00 30.55           C  
ANISOU  746  CG  PHE A 498     4458   3628   3521   -388   1623    291
ATOM    747  CD1 PHE A 498       0.444  12.258  31.509  1.00 29.27           C  
ANISOU  747  CD1 PHE A 498     4740   3445   2935   -262   2246    174
ATOM    748  CE1 PHE A 498       0.270  13.633  31.518  1.00 30.28           C  
ANISOU  748  CE1 PHE A 498     4653   3629   3223    -25   1774    606
ATOM    749  CZ  PHE A 498       0.358  14.347  32.705  1.00 30.13           C  
ANISOU  749  CZ  PHE A 498     4714   3155   3578  -1035    892    426
ATOM    750  CD2 PHE A 498       0.810  12.316  33.913  1.00 32.74           C  
ANISOU  750  CD2 PHE A 498     5027   4124   3286   -510   1943    208
ATOM    751  CE2 PHE A 498       0.638  13.693  33.898  1.00 33.46           C  
ANISOU  751  CE2 PHE A 498     5618   3567   3527  -1161   1274    414
ATOM    752  H   PHE A 498       1.900   7.871  33.327  1.00  0.00           H  
ATOM    753  HA  PHE A 498       2.524   9.705  31.275  1.00  0.00           H  
ATOM    754  HB3 PHE A 498       0.699   9.685  33.678  1.00  0.00           H  
ATOM    755  HB2 PHE A 498       0.304   9.615  31.989  1.00  0.00           H  
ATOM    756  HD1 PHE A 498       0.392  11.715  30.577  1.00  0.00           H  
ATOM    757  HE1 PHE A 498       0.076  14.152  30.595  1.00  0.00           H  
ATOM    758  HZ  PHE A 498       0.217  15.416  32.700  1.00  0.00           H  
ATOM    759  HD2 PHE A 498       1.042  11.814  34.841  1.00  0.00           H  
ATOM    760  HE2 PHE A 498       0.721  14.257  34.815  1.00  0.00           H  
ATOM    761  N   LYS A 499       3.764  10.552  34.233  1.00 24.11           N  
ANISOU  761  N   LYS A 499     4142   3518   1499   -513    532   1190
ATOM    762  CA  LYS A 499       4.733  11.401  34.933  1.00 24.99           C  
ANISOU  762  CA  LYS A 499     5019   3545    931   -558      3    779
ATOM    763  C   LYS A 499       6.187  11.157  34.490  1.00 24.86           C  
ANISOU  763  C   LYS A 499     4854   2708   1883   -681     37    100
ATOM    764  O   LYS A 499       6.922  12.130  34.324  1.00 26.12           O  
ANISOU  764  O   LYS A 499     4526   2793   2605   -653     61    379
ATOM    765  CB  LYS A 499       4.558  11.257  36.462  1.00  0.00           C  
ATOM    766  CG  LYS A 499       5.486  12.177  37.281  1.00  0.00           C  
ATOM    767  CD  LYS A 499       5.254  12.090  38.799  1.00  0.00           C  
ATOM    768  CE  LYS A 499       6.116  13.075  39.616  1.00  0.00           C  
ATOM    769  NZ  LYS A 499       7.558  12.769  39.547  1.00  0.00           N1+
ATOM    770  H   LYS A 499       3.241   9.905  34.809  1.00  0.00           H  
ATOM    771  HA  LYS A 499       4.487  12.433  34.673  1.00  0.00           H  
ATOM    772  HB2 LYS A 499       3.523  11.485  36.719  1.00  0.00           H  
ATOM    773  HB3 LYS A 499       4.721  10.219  36.756  1.00  0.00           H  
ATOM    774  HG2 LYS A 499       6.526  11.928  37.073  1.00  0.00           H  
ATOM    775  HG3 LYS A 499       5.345  13.208  36.953  1.00  0.00           H  
ATOM    776  HD2 LYS A 499       4.203  12.289  39.009  1.00  0.00           H  
ATOM    777  HD3 LYS A 499       5.432  11.068  39.138  1.00  0.00           H  
ATOM    778  HE2 LYS A 499       5.950  14.097  39.273  1.00  0.00           H  
ATOM    779  HE3 LYS A 499       5.813  13.040  40.663  1.00  0.00           H  
ATOM    780  HZ1 LYS A 499       7.869  12.823  38.588  1.00  0.00           H  
ATOM    781  HZ2 LYS A 499       8.072  13.437  40.105  1.00  0.00           H  
ATOM    782  HZ3 LYS A 499       7.723  11.838  39.902  1.00  0.00           H  
ATOM    783  N   ASN A 500       6.564   9.881  34.287  1.00 23.37           N  
ANISOU  783  N   ASN A 500     4628   2358   1892   -420   -365    775
ATOM    784  CA  ASN A 500       7.874   9.465  33.769  1.00 28.30           C  
ANISOU  784  CA  ASN A 500     4616   3205   2930   -779   -347    590
ATOM    785  C   ASN A 500       8.131  10.008  32.360  1.00 24.85           C  
ANISOU  785  C   ASN A 500     3786   2483   3172   -240   -391    810
ATOM    786  O   ASN A 500       9.244  10.449  32.086  1.00 23.80           O  
ANISOU  786  O   ASN A 500     3415   2431   3193   -212   -939    704
ATOM    787  CB  ASN A 500       7.978   7.919  33.747  1.00 31.12           C  
ANISOU  787  CB  ASN A 500     5200   3120   3502   -113   -759   1654
ATOM    788  CG  ASN A 500       8.138   7.259  35.119  1.00 34.22           C  
ANISOU  788  CG  ASN A 500     6777   3476   2747    -75   -610    862
ATOM    789  OD1 ASN A 500       8.421   7.917  36.117  1.00 43.01           O  
ANISOU  789  OD1 ASN A 500     5782   3810   6748   -458    -90   1616
ATOM    790  ND2 ASN A 500       7.973   5.936  35.167  1.00 31.27           N  
ANISOU  790  ND2 ASN A 500     5072   3966   2840   -749  -1604    955
ATOM    791  H   ASN A 500       5.903   9.136  34.470  1.00  0.00           H  
ATOM    792  HA  ASN A 500       8.615   9.879  34.457  1.00  0.00           H  
ATOM    793  HB3 ASN A 500       8.859   7.624  33.176  1.00  0.00           H  
ATOM    794  HB2 ASN A 500       7.120   7.487  33.228  1.00  0.00           H  
ATOM    795 HD22 ASN A 500       8.081   5.441  36.040  1.00  0.00           H  
ATOM    796 HD21 ASN A 500       7.744   5.418  34.331  1.00  0.00           H  
ATOM    797  N   GLU A 501       7.100   9.971  31.507  1.00 25.54           N  
ANISOU  797  N   GLU A 501     4530   2641   2531   -112   -213    216
ATOM    798  CA  GLU A 501       7.180  10.365  30.109  1.00 20.63           C  
ANISOU  798  CA  GLU A 501     2795   2365   2679      0      1    363
ATOM    799  C   GLU A 501       7.231  11.883  29.890  1.00 19.71           C  
ANISOU  799  C   GLU A 501     2792   2355   2338    147   -241    187
ATOM    800  O   GLU A 501       8.024  12.328  29.060  1.00 20.57           O  
ANISOU  800  O   GLU A 501     2845   2904   2064    -38   -151    -10
ATOM    801  CB  GLU A 501       6.042   9.663  29.377  1.00 24.33           C  
ANISOU  801  CB  GLU A 501     3096   3129   3018   -452    228    146
ATOM    802  CG  GLU A 501       5.942   9.995  27.881  1.00 21.17           C  
ANISOU  802  CG  GLU A 501     2334   3079   2627   -719    -24    635
ATOM    803  CD  GLU A 501       4.990   9.075  27.121  1.00 20.67           C  
ANISOU  803  CD  GLU A 501     2917   2593   2344   -647     92    395
ATOM    804  OE1 GLU A 501       4.611   8.009  27.646  1.00 23.03           O  
ANISOU  804  OE1 GLU A 501     3242   2950   2557  -1172     -5    439
ATOM    805  OE2 GLU A 501       4.659   9.445  25.982  1.00 21.94           O1-
ANISOU  805  OE2 GLU A 501     2796   3073   2466   -724    160    729
ATOM    806  H   GLU A 501       6.214   9.590  31.812  1.00  0.00           H  
ATOM    807  HA  GLU A 501       8.111   9.962  29.704  1.00  0.00           H  
ATOM    808  HB3 GLU A 501       5.088   9.885  29.861  1.00  0.00           H  
ATOM    809  HB2 GLU A 501       6.214   8.595  29.512  1.00  0.00           H  
ATOM    810  HG3 GLU A 501       6.929   9.917  27.423  1.00  0.00           H  
ATOM    811  HG2 GLU A 501       5.616  11.027  27.746  1.00  0.00           H  
ATOM    812  N   VAL A 502       6.464  12.646  30.691  1.00 18.49           N  
ANISOU  812  N   VAL A 502     2566   1989   2471    -62     88    717
ATOM    813  CA  VAL A 502       6.609  14.100  30.825  1.00 16.99           C  
ANISOU  813  CA  VAL A 502     2535   1845   2075    287    321    475
ATOM    814  C   VAL A 502       7.997  14.479  31.385  1.00 21.26           C  
ANISOU  814  C   VAL A 502     3110   2319   2647   -121   -273    216
ATOM    815  O   VAL A 502       8.568  15.472  30.939  1.00 21.76           O  
ANISOU  815  O   VAL A 502     2899   2843   2523   -328    262     -1
ATOM    816  CB  VAL A 502       5.499  14.713  31.738  1.00 18.78           C  
ANISOU  816  CB  VAL A 502     2710   2581   1844    458    368    507
ATOM    817  CG1 VAL A 502       5.733  16.174  32.184  1.00 20.78           C  
ANISOU  817  CG1 VAL A 502     3105   2398   2392    799     92    394
ATOM    818  CG2 VAL A 502       4.122  14.624  31.064  1.00 19.58           C  
ANISOU  818  CG2 VAL A 502     2791   2710   1937    660    414    170
ATOM    819  H   VAL A 502       5.818  12.201  31.331  1.00  0.00           H  
ATOM    820  HA  VAL A 502       6.520  14.537  29.828  1.00  0.00           H  
ATOM    821  HB  VAL A 502       5.444  14.110  32.646  1.00  0.00           H  
ATOM    822 HG11 VAL A 502       4.867  16.559  32.724  1.00  0.00           H  
ATOM    823 HG12 VAL A 502       6.583  16.271  32.860  1.00  0.00           H  
ATOM    824 HG13 VAL A 502       5.903  16.827  31.327  1.00  0.00           H  
ATOM    825 HG21 VAL A 502       3.334  15.008  31.713  1.00  0.00           H  
ATOM    826 HG22 VAL A 502       4.103  15.203  30.140  1.00  0.00           H  
ATOM    827 HG23 VAL A 502       3.861  13.596  30.820  1.00  0.00           H  
ATOM    828  N   GLY A 503       8.522  13.652  32.308  1.00 19.64           N  
ANISOU  828  N   GLY A 503     3024   1937   2499     99    -75    229
ATOM    829  CA  GLY A 503       9.832  13.792  32.938  1.00 25.25           C  
ANISOU  829  CA  GLY A 503     3571   3601   2422   -779   -281     15
ATOM    830  C   GLY A 503      10.987  13.637  31.937  1.00 24.20           C  
ANISOU  830  C   GLY A 503     3636   2590   2967   -316   -311    -77
ATOM    831  O   GLY A 503      11.964  14.371  32.052  1.00 27.62           O  
ANISOU  831  O   GLY A 503     3838   3359   3297   -608   -215   -863
ATOM    832  H   GLY A 503       7.968  12.862  32.613  1.00  0.00           H  
ATOM    833  HA3 GLY A 503       9.930  13.027  33.708  1.00  0.00           H  
ATOM    834  HA2 GLY A 503       9.895  14.758  33.439  1.00  0.00           H  
ATOM    835  N   VAL A 504      10.878  12.730  30.949  1.00 21.06           N  
ANISOU  835  N   VAL A 504     3619   1938   2445   -561    154    421
ATOM    836  CA  VAL A 504      11.864  12.561  29.874  1.00 22.71           C  
ANISOU  836  CA  VAL A 504     2916   2349   3360     63    -74    123
ATOM    837  C   VAL A 504      11.794  13.720  28.861  1.00 20.12           C  
ANISOU  837  C   VAL A 504     2632   2139   2874    268   -195   -172
ATOM    838  O   VAL A 504      12.829  14.294  28.526  1.00 21.45           O  
ANISOU  838  O   VAL A 504     2352   2428   3370    476     20    -11
ATOM    839  CB  VAL A 504      11.674  11.211  29.112  1.00 27.79           C  
ANISOU  839  CB  VAL A 504     4402   1779   4375    816    796    141
ATOM    840  CG1 VAL A 504      12.487  11.075  27.803  1.00 33.98           C  
ANISOU  840  CG1 VAL A 504     3612   3602   5693    916   1340   -851
ATOM    841  CG2 VAL A 504      12.008  10.016  30.016  1.00 35.49           C  
ANISOU  841  CG2 VAL A 504     5367   3539   4577   -195    356   1322
ATOM    842  H   VAL A 504      10.059  12.139  30.904  1.00  0.00           H  
ATOM    843  HA  VAL A 504      12.862  12.564  30.319  1.00  0.00           H  
ATOM    844  HB  VAL A 504      10.620  11.118  28.845  1.00  0.00           H  
ATOM    845 HG11 VAL A 504      12.408  10.068  27.393  1.00  0.00           H  
ATOM    846 HG12 VAL A 504      12.136  11.751  27.022  1.00  0.00           H  
ATOM    847 HG13 VAL A 504      13.545  11.278  27.973  1.00  0.00           H  
ATOM    848 HG21 VAL A 504      11.794   9.070  29.518  1.00  0.00           H  
ATOM    849 HG22 VAL A 504      13.063  10.024  30.279  1.00  0.00           H  
ATOM    850 HG23 VAL A 504      11.441  10.029  30.942  1.00  0.00           H  
ATOM    851  N   LEU A 505      10.571  14.034  28.409  1.00 19.01           N  
ANISOU  851  N   LEU A 505     2657   2398   2165    413    115    508
ATOM    852  CA  LEU A 505      10.266  15.047  27.400  1.00 16.60           C  
ANISOU  852  CA  LEU A 505     2735   1996   1573    -86    -15     98
ATOM    853  C   LEU A 505      10.658  16.480  27.804  1.00 15.86           C  
ANISOU  853  C   LEU A 505     2275   1929   1819   -111   -186    191
ATOM    854  O   LEU A 505      11.143  17.223  26.950  1.00 13.99           O  
ANISOU  854  O   LEU A 505     2073   1708   1534   -277   -140    -82
ATOM    855  CB  LEU A 505       8.762  14.947  27.071  1.00 19.86           C  
ANISOU  855  CB  LEU A 505     2641   2485   2418   -331   -292     94
ATOM    856  CG  LEU A 505       8.405  13.878  26.014  1.00 21.97           C  
ANISOU  856  CG  LEU A 505     2840   2655   2850   -223   -655   -262
ATOM    857  CD1 LEU A 505       6.893  13.586  26.019  1.00 22.58           C  
ANISOU  857  CD1 LEU A 505     2631   2463   3483    -97  -1573   -208
ATOM    858  CD2 LEU A 505       8.875  14.268  24.598  1.00 26.42           C  
ANISOU  858  CD2 LEU A 505     4161   2353   3524   -411   -119   -337
ATOM    859  H   LEU A 505       9.776  13.508  28.748  1.00  0.00           H  
ATOM    860  HA  LEU A 505      10.850  14.807  26.511  1.00  0.00           H  
ATOM    861  HB3 LEU A 505       8.377  15.899  26.733  1.00  0.00           H  
ATOM    862  HB2 LEU A 505       8.218  14.757  27.997  1.00  0.00           H  
ATOM    863  HG  LEU A 505       8.909  12.951  26.290  1.00  0.00           H  
ATOM    864 HD11 LEU A 505       6.706  12.525  26.181  1.00  0.00           H  
ATOM    865 HD12 LEU A 505       6.374  14.127  26.811  1.00  0.00           H  
ATOM    866 HD13 LEU A 505       6.417  13.864  25.079  1.00  0.00           H  
ATOM    867 HD21 LEU A 505       8.445  13.607  23.845  1.00  0.00           H  
ATOM    868 HD22 LEU A 505       8.574  15.278  24.332  1.00  0.00           H  
ATOM    869 HD23 LEU A 505       9.959  14.213  24.501  1.00  0.00           H  
ATOM    870  N   ARG A 506      10.481  16.837  29.088  1.00 16.49           N  
ANISOU  870  N   ARG A 506     2326   1929   2009    396    252    170
ATOM    871  CA  ARG A 506      10.820  18.159  29.622  1.00 16.98           C  
ANISOU  871  CA  ARG A 506     2584   2002   1863   -201    386    401
ATOM    872  C   ARG A 506      12.332  18.402  29.810  1.00 17.67           C  
ANISOU  872  C   ARG A 506     2592   1464   2656    -35    300   -246
ATOM    873  O   ARG A 506      12.702  19.551  30.041  1.00 16.36           O  
ANISOU  873  O   ARG A 506     3027   1488   1701   -555    194    -30
ATOM    874  CB  ARG A 506      10.023  18.416  30.917  1.00 20.41           C  
ANISOU  874  CB  ARG A 506     3640   2360   1753   -183    712    351
ATOM    875  CG  ARG A 506      10.560  17.699  32.175  1.00 25.65           C  
ANISOU  875  CG  ARG A 506     4130   3348   2267    -83    654    547
ATOM    876  CD  ARG A 506       9.668  17.888  33.410  1.00 35.31           C  
ANISOU  876  CD  ARG A 506     4597   5170   3646   -141   1469  -1087
ATOM    877  NE  ARG A 506       9.734  19.268  33.934  1.00 36.73           N  
ANISOU  877  NE  ARG A 506     6594   4792   2570    676   1727  -1157
ATOM    878  CZ  ARG A 506       8.745  20.011  34.467  1.00 42.83           C  
ANISOU  878  CZ  ARG A 506     5356   5250   5665   2030    674    238
ATOM    879  NH1 ARG A 506       7.486  19.559  34.590  1.00 49.01           N  
ANISOU  879  NH1 ARG A 506     6841   6883   4898   1216   1831      6
ATOM    880  NH2 ARG A 506       9.034  21.246  34.896  1.00 42.64           N1+
ANISOU  880  NH2 ARG A 506     6721   5100   4378    275    746    291
ATOM    881  H   ARG A 506      10.063  16.182  29.736  1.00  0.00           H  
ATOM    882  HA  ARG A 506      10.472  18.891  28.892  1.00  0.00           H  
ATOM    883  HB3 ARG A 506       8.978  18.148  30.753  1.00  0.00           H  
ATOM    884  HB2 ARG A 506      10.016  19.490  31.106  1.00  0.00           H  
ATOM    885  HG3 ARG A 506      11.540  18.121  32.406  1.00  0.00           H  
ATOM    886  HG2 ARG A 506      10.741  16.642  31.996  1.00  0.00           H  
ATOM    887  HD3 ARG A 506       9.874  17.141  34.177  1.00  0.00           H  
ATOM    888  HD2 ARG A 506       8.643  17.711  33.086  1.00  0.00           H  
ATOM    889  HE  ARG A 506      10.658  19.676  33.913  1.00  0.00           H  
ATOM    890 HH12 ARG A 506       6.768  20.130  35.011  1.00  0.00           H  
ATOM    891 HH11 ARG A 506       7.255  18.628  34.276  1.00  0.00           H  
ATOM    892 HH22 ARG A 506       8.322  21.824  35.319  1.00  0.00           H  
ATOM    893 HH21 ARG A 506       9.978  21.600  34.836  1.00  0.00           H  
ATOM    894  N   LYS A 507      13.172  17.355  29.719  1.00 15.34           N  
ANISOU  894  N   LYS A 507     3134   1258   1434    129    218    286
ATOM    895  CA  LYS A 507      14.634  17.462  29.786  1.00 16.74           C  
ANISOU  895  CA  LYS A 507     3020   1677   1663     16     44    136
ATOM    896  C   LYS A 507      15.288  17.816  28.437  1.00 15.42           C  
ANISOU  896  C   LYS A 507     2374   1735   1751   -227   -126    168
ATOM    897  O   LYS A 507      16.493  18.067  28.431  1.00 17.24           O  
ANISOU  897  O   LYS A 507     2486   2433   1629    -29    121    132
ATOM    898  CB  LYS A 507      15.228  16.134  30.298  1.00 20.95           C  
ANISOU  898  CB  LYS A 507     3296   2266   2398     83    122    699
ATOM    899  CG  LYS A 507      14.944  15.838  31.775  1.00 27.51           C  
ANISOU  899  CG  LYS A 507     4187   3791   2473  -1182   -103   1062
ATOM    900  CD  LYS A 507      15.459  14.441  32.174  1.00 37.16           C  
ANISOU  900  CD  LYS A 507     5880   4229   4011   -800   -818   1557
ATOM    901  CE  LYS A 507      15.006  13.944  33.559  1.00 53.09           C  
ANISOU  901  CE  LYS A 507     8796   6985   4388  -2414   -416   1230
ATOM    902  NZ  LYS A 507      15.445  14.823  34.657  1.00 56.48           N1+
ANISOU  902  NZ  LYS A 507     8575   7778   5106  -2169  -1845    309
ATOM    903  H   LYS A 507      12.801  16.432  29.541  1.00  0.00           H  
ATOM    904  HA  LYS A 507      14.903  18.249  30.493  1.00  0.00           H  
ATOM    905  HB3 LYS A 507      16.314  16.140  30.180  1.00  0.00           H  
ATOM    906  HB2 LYS A 507      14.868  15.316  29.676  1.00  0.00           H  
ATOM    907  HG3 LYS A 507      13.878  15.925  31.970  1.00  0.00           H  
ATOM    908  HG2 LYS A 507      15.423  16.603  32.388  1.00  0.00           H  
ATOM    909  HD3 LYS A 507      16.549  14.434  32.125  1.00  0.00           H  
ATOM    910  HD2 LYS A 507      15.131  13.715  31.428  1.00  0.00           H  
ATOM    911  HE3 LYS A 507      15.411  12.949  33.742  1.00  0.00           H  
ATOM    912  HE2 LYS A 507      13.922  13.852  33.602  1.00  0.00           H  
ATOM    913  HZ1 LYS A 507      15.053  15.745  34.528  1.00  0.00           H  
ATOM    914  HZ2 LYS A 507      15.131  14.446  35.540  1.00  0.00           H  
ATOM    915  HZ3 LYS A 507      16.453  14.885  34.657  1.00  0.00           H  
ATOM    916  N   THR A 508      14.518  17.822  27.335  1.00 14.46           N  
ANISOU  916  N   THR A 508     2302   1423   1768    339    -54    261
ATOM    917  CA  THR A 508      15.060  17.918  25.980  1.00 15.07           C  
ANISOU  917  CA  THR A 508     2364   1745   1615    -22    -41    -51
ATOM    918  C   THR A 508      14.668  19.240  25.288  1.00 13.98           C  
ANISOU  918  C   THR A 508     2073   1405   1831   -179     -2   -192
ATOM    919  O   THR A 508      13.490  19.576  25.206  1.00 13.61           O  
ANISOU  919  O   THR A 508     2376   1870    925     64    -53   -232
ATOM    920  CB  THR A 508      14.598  16.714  25.116  1.00 15.86           C  
ANISOU  920  CB  THR A 508     2215   1893   1917   -106    -54   -220
ATOM    921  OG1 THR A 508      13.200  16.680  24.903  1.00 15.97           O  
ANISOU  921  OG1 THR A 508     2078   1905   2084   -469    -83    138
ATOM    922  CG2 THR A 508      15.018  15.357  25.704  1.00 17.21           C  
ANISOU  922  CG2 THR A 508     2395   2486   1658   -128    301    480
ATOM    923  H   THR A 508      13.528  17.633  27.410  1.00  0.00           H  
ATOM    924  HA  THR A 508      16.146  17.874  26.023  1.00  0.00           H  
ATOM    925  HB  THR A 508      15.063  16.812  24.135  1.00  0.00           H  
ATOM    926  HG1 THR A 508      12.766  16.463  25.733  1.00  0.00           H  
ATOM    927 HG21 THR A 508      14.718  14.535  25.054  1.00  0.00           H  
ATOM    928 HG22 THR A 508      16.099  15.303  25.827  1.00  0.00           H  
ATOM    929 HG23 THR A 508      14.568  15.180  26.680  1.00  0.00           H  
ATOM    930  N   ARG A 509      15.690  19.957  24.798  1.00 14.31           N  
ANISOU  930  N   ARG A 509     2260   1613   1563   -201   -212    304
ATOM    931  CA  ARG A 509      15.608  21.198  24.029  1.00 13.09           C  
ANISOU  931  CA  ARG A 509     2076   1336   1560    221     39    115
ATOM    932  C   ARG A 509      16.687  21.132  22.945  1.00 13.25           C  
ANISOU  932  C   ARG A 509     2015   1498   1522     99    -35   -254
ATOM    933  O   ARG A 509      17.806  21.603  23.155  1.00 14.15           O  
ANISOU  933  O   ARG A 509     1766   2079   1529    171     96   -197
ATOM    934  CB  ARG A 509      15.850  22.418  24.937  1.00 13.57           C  
ANISOU  934  CB  ARG A 509     1912   1698   1543    -91     56    -62
ATOM    935  CG  ARG A 509      14.656  22.827  25.792  1.00 15.66           C  
ANISOU  935  CG  ARG A 509     2042   1689   2216    322      3   -111
ATOM    936  CD  ARG A 509      14.998  24.033  26.679  1.00 17.04           C  
ANISOU  936  CD  ARG A 509     2897   1584   1992    135   -157    149
ATOM    937  NE  ARG A 509      13.802  24.663  27.239  1.00 16.68           N  
ANISOU  937  NE  ARG A 509     2811   1954   1570    180   -211    153
ATOM    938  CZ  ARG A 509      13.002  25.535  26.605  1.00 17.28           C  
ANISOU  938  CZ  ARG A 509     2289   2062   2213    588     13   -115
ATOM    939  NH1 ARG A 509      13.201  25.913  25.333  1.00 15.73           N  
ANISOU  939  NH1 ARG A 509     2336   1426   2214    347   -312   -169
ATOM    940  NH2 ARG A 509      11.971  26.048  27.275  1.00 16.59           N1+
ANISOU  940  NH2 ARG A 509     2588   2216   1499    123     51   -739
ATOM    941  H   ARG A 509      16.631  19.609  24.938  1.00  0.00           H  
ATOM    942  HA  ARG A 509      14.638  21.295  23.537  1.00  0.00           H  
ATOM    943  HB3 ARG A 509      16.084  23.272  24.302  1.00  0.00           H  
ATOM    944  HB2 ARG A 509      16.725  22.260  25.568  1.00  0.00           H  
ATOM    945  HG3 ARG A 509      14.452  21.980  26.441  1.00  0.00           H  
ATOM    946  HG2 ARG A 509      13.753  22.982  25.199  1.00  0.00           H  
ATOM    947  HD3 ARG A 509      15.697  24.735  26.233  1.00  0.00           H  
ATOM    948  HD2 ARG A 509      15.511  23.671  27.563  1.00  0.00           H  
ATOM    949  HE  ARG A 509      13.564  24.401  28.187  1.00  0.00           H  
ATOM    950 HH12 ARG A 509      12.583  26.583  24.891  1.00  0.00           H  
ATOM    951 HH11 ARG A 509      14.007  25.573  24.823  1.00  0.00           H  
ATOM    952 HH22 ARG A 509      11.347  26.695  26.810  1.00  0.00           H  
ATOM    953 HH21 ARG A 509      11.817  25.806  28.245  1.00  0.00           H  
ATOM    954  N   HIS A 510      16.336  20.524  21.807  1.00 13.47           N  
ANISOU  954  N   HIS A 510     1689   1683   1745    319     44   -531
ATOM    955  CA  HIS A 510      17.248  20.319  20.688  1.00 12.48           C  
ANISOU  955  CA  HIS A 510     1773   1661   1305     71    -54   -177
ATOM    956  C   HIS A 510      16.427  20.112  19.413  1.00 13.29           C  
ANISOU  956  C   HIS A 510     1750   1838   1458   -156   -231      2
ATOM    957  O   HIS A 510      15.381  19.464  19.461  1.00 15.08           O  
ANISOU  957  O   HIS A 510     2022   1880   1828   -359     80    -11
ATOM    958  CB  HIS A 510      18.166  19.126  21.016  1.00 13.60           C  
ANISOU  958  CB  HIS A 510     2332   1482   1353    341    153    -85
ATOM    959  CG  HIS A 510      19.299  18.899  20.054  1.00 13.63           C  
ANISOU  959  CG  HIS A 510     2300   1325   1553    219    204   -237
ATOM    960  ND1 HIS A 510      19.151  18.172  18.869  1.00 17.45           N  
ANISOU  960  ND1 HIS A 510     2266   2196   2165    383    230    -47
ATOM    961  CE1 HIS A 510      20.347  18.206  18.300  1.00 13.45           C  
ANISOU  961  CE1 HIS A 510     1638   1428   2042    482   -113   -132
ATOM    962  NE2 HIS A 510      21.241  18.877  19.019  1.00 19.08           N  
ANISOU  962  NE2 HIS A 510     2587   2447   2214   -197     56    236
ATOM    963  CD2 HIS A 510      20.603  19.329  20.155  1.00 11.25           C  
ANISOU  963  CD2 HIS A 510     1966    954   1352    -16   -249    -96
ATOM    964  H   HIS A 510      15.399  20.159  21.692  1.00  0.00           H  
ATOM    965  HA  HIS A 510      17.853  21.220  20.562  1.00  0.00           H  
ATOM    966  HB3 HIS A 510      17.580  18.214  21.101  1.00  0.00           H  
ATOM    967  HB2 HIS A 510      18.624  19.272  21.993  1.00  0.00           H  
ATOM    968  HE1 HIS A 510      20.579  17.735  17.359  1.00  0.00           H  
ATOM    969  HD2 HIS A 510      21.112  19.903  20.915  1.00  0.00           H  
ATOM    970  HE2 HIS A 510      22.210  19.040  18.766  1.00  0.00           H  
ATOM    971  N   VAL A 511      16.924  20.658  18.291  1.00 12.68           N  
ANISOU  971  N   VAL A 511     2196   1137   1485   -355   -361    -62
ATOM    972  CA  VAL A 511      16.262  20.615  16.985  1.00 11.29           C  
ANISOU  972  CA  VAL A 511     1224   1348   1717     10   -251   -327
ATOM    973  C   VAL A 511      16.075  19.196  16.403  1.00 12.43           C  
ANISOU  973  C   VAL A 511     1698   1323   1702   -240   -157   -167
ATOM    974  O   VAL A 511      15.183  19.018  15.578  1.00 15.05           O  
ANISOU  974  O   VAL A 511     2226   1814   1678   -385   -508   -432
ATOM    975  CB  VAL A 511      16.996  21.514  15.945  1.00 17.03           C  
ANISOU  975  CB  VAL A 511     1578   2864   2025   -306     -5    447
ATOM    976  CG1 VAL A 511      18.363  20.966  15.482  1.00 17.23           C  
ANISOU  976  CG1 VAL A 511     2557   1697   2293   -322    627    -20
ATOM    977  CG2 VAL A 511      16.123  21.811  14.712  1.00 26.90           C  
ANISOU  977  CG2 VAL A 511     2111   5218   2890   -483   -308    589
ATOM    978  H   VAL A 511      17.799  21.169  18.326  1.00  0.00           H  
ATOM    979  HA  VAL A 511      15.262  21.027  17.138  1.00  0.00           H  
ATOM    980  HB  VAL A 511      17.180  22.471  16.435  1.00  0.00           H  
ATOM    981 HG11 VAL A 511      18.896  21.708  14.887  1.00  0.00           H  
ATOM    982 HG12 VAL A 511      19.001  20.702  16.325  1.00  0.00           H  
ATOM    983 HG13 VAL A 511      18.258  20.075  14.863  1.00  0.00           H  
ATOM    984 HG21 VAL A 511      16.532  22.630  14.125  1.00  0.00           H  
ATOM    985 HG22 VAL A 511      16.053  20.950  14.048  1.00  0.00           H  
ATOM    986 HG23 VAL A 511      15.113  22.084  15.004  1.00  0.00           H  
ATOM    987  N   ASN A 512      16.870  18.210  16.853  1.00 13.22           N  
ANISOU  987  N   ASN A 512     2189   1841    992    173      6   -239
ATOM    988  CA  ASN A 512      16.739  16.810  16.436  1.00 12.90           C  
ANISOU  988  CA  ASN A 512     1986   1473   1443    238    368     66
ATOM    989  C   ASN A 512      15.949  15.938  17.416  1.00 12.46           C  
ANISOU  989  C   ASN A 512     1731   1432   1569    288    405     21
ATOM    990  O   ASN A 512      15.906  14.726  17.213  1.00 14.72           O  
ANISOU  990  O   ASN A 512     2126   1695   1770    -60    -62   -315
ATOM    991  CB  ASN A 512      18.105  16.199  16.055  1.00 11.29           C  
ANISOU  991  CB  ASN A 512     1729   1352   1208     41     -1    -52
ATOM    992  CG  ASN A 512      18.762  16.906  14.869  1.00 11.83           C  
ANISOU  992  CG  ASN A 512     2117   1115   1262    -11     10     21
ATOM    993  OD1 ASN A 512      19.942  17.235  14.922  1.00 14.70           O  
ANISOU  993  OD1 ASN A 512     2107   2246   1231    152    196   -294
ATOM    994  ND2 ASN A 512      18.009  17.125  13.788  1.00 13.71           N  
ANISOU  994  ND2 ASN A 512     1643   1807   1758    -57   -269   -395
ATOM    995  H   ASN A 512      17.584  18.409  17.543  1.00  0.00           H  
ATOM    996  HA  ASN A 512      16.130  16.793  15.549  1.00  0.00           H  
ATOM    997  HB3 ASN A 512      17.986  15.156  15.758  1.00  0.00           H  
ATOM    998  HB2 ASN A 512      18.779  16.192  16.911  1.00  0.00           H  
ATOM    999 HD22 ASN A 512      18.400  17.554  12.961  1.00  0.00           H  
ATOM   1000 HD21 ASN A 512      17.037  16.842  13.776  1.00  0.00           H  
ATOM   1001  N   ILE A 513      15.289  16.557  18.404  1.00 12.90           N  
ANISOU 1001  N   ILE A 513     1625   1773   1502     28    382   -154
ATOM   1002  CA  ILE A 513      14.358  15.892  19.307  1.00 13.29           C  
ANISOU 1002  CA  ILE A 513     1789   1798   1460    -52    371   -190
ATOM   1003  C   ILE A 513      12.977  16.542  19.135  1.00 13.33           C  
ANISOU 1003  C   ILE A 513     2064   1643   1356     72     48    114
ATOM   1004  O   ILE A 513      12.890  17.769  19.080  1.00 12.43           O  
ANISOU 1004  O   ILE A 513     1820   1470   1433    -91    274     -3
ATOM   1005  CB  ILE A 513      14.783  16.051  20.796  1.00 14.19           C  
ANISOU 1005  CB  ILE A 513     2152   1724   1513   -317    165   -314
ATOM   1006  CG1 ILE A 513      16.245  15.621  21.046  1.00 14.57           C  
ANISOU 1006  CG1 ILE A 513     2298   1809   1427   -115   -134   -434
ATOM   1007  CG2 ILE A 513      13.827  15.313  21.755  1.00 13.41           C  
ANISOU 1007  CG2 ILE A 513     1903   1816   1375   -313    -63    -26
ATOM   1008  CD1 ILE A 513      16.566  14.165  20.710  1.00 15.46           C  
ANISOU 1008  CD1 ILE A 513     2231   1752   1889   -203     66   -174
ATOM   1009  H   ILE A 513      15.361  17.561  18.505  1.00  0.00           H  
ATOM   1010  HA  ILE A 513      14.273  14.831  19.071  1.00  0.00           H  
ATOM   1011  HB  ILE A 513      14.741  17.110  21.059  1.00  0.00           H  
ATOM   1012 HG13 ILE A 513      16.503  15.814  22.088  1.00  0.00           H  
ATOM   1013 HG12 ILE A 513      16.917  16.245  20.460  1.00  0.00           H  
ATOM   1014 HG21 ILE A 513      14.256  15.205  22.748  1.00  0.00           H  
ATOM   1015 HG22 ILE A 513      12.878  15.836  21.867  1.00  0.00           H  
ATOM   1016 HG23 ILE A 513      13.609  14.311  21.392  1.00  0.00           H  
ATOM   1017 HD11 ILE A 513      17.607  13.966  20.937  1.00  0.00           H  
ATOM   1018 HD12 ILE A 513      15.960  13.469  21.286  1.00  0.00           H  
ATOM   1019 HD13 ILE A 513      16.429  13.951  19.654  1.00  0.00           H  
ATOM   1020  N   LEU A 514      11.930  15.700  19.086  1.00 13.26           N  
ANISOU 1020  N   LEU A 514     2130   1726   1182    127    235   -196
ATOM   1021  CA  LEU A 514      10.512  16.068  19.052  1.00 13.66           C  
ANISOU 1021  CA  LEU A 514     1919   1772   1497    -87    302     64
ATOM   1022  C   LEU A 514      10.158  17.035  20.198  1.00 14.20           C  
ANISOU 1022  C   LEU A 514     1950   2033   1412     47     91     -3
ATOM   1023  O   LEU A 514      10.318  16.667  21.363  1.00 13.15           O  
ANISOU 1023  O   LEU A 514     1846   1914   1234      2    186     79
ATOM   1024  CB  LEU A 514       9.693  14.754  19.110  1.00 13.40           C  
ANISOU 1024  CB  LEU A 514     2199   1253   1637    146     41    -12
ATOM   1025  CG  LEU A 514       8.151  14.879  19.162  1.00 16.10           C  
ANISOU 1025  CG  LEU A 514     2066   1915   2134    218    -36   -257
ATOM   1026  CD1 LEU A 514       7.555  15.487  17.877  1.00 16.39           C  
ANISOU 1026  CD1 LEU A 514     2327   1657   2241     25   -316   -265
ATOM   1027  CD2 LEU A 514       7.506  13.525  19.512  1.00 17.17           C  
ANISOU 1027  CD2 LEU A 514     1846   2153   2522    119   -211     30
ATOM   1028  H   LEU A 514      12.112  14.706  19.151  1.00  0.00           H  
ATOM   1029  HA  LEU A 514      10.332  16.566  18.098  1.00  0.00           H  
ATOM   1030  HB3 LEU A 514      10.015  14.201  19.995  1.00  0.00           H  
ATOM   1031  HB2 LEU A 514       9.966  14.125  18.260  1.00  0.00           H  
ATOM   1032  HG  LEU A 514       7.894  15.552  19.980  1.00  0.00           H  
ATOM   1033 HD11 LEU A 514       6.797  16.229  18.124  1.00  0.00           H  
ATOM   1034 HD12 LEU A 514       8.307  15.977  17.260  1.00  0.00           H  
ATOM   1035 HD13 LEU A 514       7.073  14.741  17.245  1.00  0.00           H  
ATOM   1036 HD21 LEU A 514       6.732  13.228  18.805  1.00  0.00           H  
ATOM   1037 HD22 LEU A 514       8.230  12.714  19.543  1.00  0.00           H  
ATOM   1038 HD23 LEU A 514       7.045  13.576  20.497  1.00  0.00           H  
ATOM   1039  N   LEU A 515       9.735  18.259  19.836  1.00 13.69           N  
ANISOU 1039  N   LEU A 515     1902   1806   1491     90    138   -385
ATOM   1040  CA  LEU A 515       9.465  19.359  20.761  1.00 13.89           C  
ANISOU 1040  CA  LEU A 515     2122   1216   1939    -58     18   -319
ATOM   1041  C   LEU A 515       8.263  19.055  21.664  1.00 14.87           C  
ANISOU 1041  C   LEU A 515     2483   1458   1706    263     40     59
ATOM   1042  O   LEU A 515       7.130  19.125  21.196  1.00 14.32           O  
ANISOU 1042  O   LEU A 515     2595   1371   1472   -277    342    211
ATOM   1043  CB  LEU A 515       9.260  20.675  19.971  1.00 15.63           C  
ANISOU 1043  CB  LEU A 515     2544   1658   1735     73   -106    -33
ATOM   1044  CG  LEU A 515       8.899  21.920  20.821  1.00 14.45           C  
ANISOU 1044  CG  LEU A 515     2098   1627   1764    110    100     34
ATOM   1045  CD1 LEU A 515      10.076  22.371  21.711  1.00 16.17           C  
ANISOU 1045  CD1 LEU A 515     2274   1422   2446   -359    319   -370
ATOM   1046  CD2 LEU A 515       8.352  23.048  19.930  1.00 20.75           C  
ANISOU 1046  CD2 LEU A 515     3277   2202   2402    502   -331    236
ATOM   1047  H   LEU A 515       9.627  18.474  18.854  1.00  0.00           H  
ATOM   1048  HA  LEU A 515      10.351  19.495  21.381  1.00  0.00           H  
ATOM   1049  HB3 LEU A 515       8.454  20.515  19.259  1.00  0.00           H  
ATOM   1050  HB2 LEU A 515      10.144  20.888  19.370  1.00  0.00           H  
ATOM   1051  HG  LEU A 515       8.071  21.687  21.489  1.00  0.00           H  
ATOM   1052 HD11 LEU A 515      10.164  23.455  21.783  1.00  0.00           H  
ATOM   1053 HD12 LEU A 515       9.947  22.003  22.727  1.00  0.00           H  
ATOM   1054 HD13 LEU A 515      11.031  21.987  21.353  1.00  0.00           H  
ATOM   1055 HD21 LEU A 515       8.625  24.033  20.298  1.00  0.00           H  
ATOM   1056 HD22 LEU A 515       8.703  22.966  18.901  1.00  0.00           H  
ATOM   1057 HD23 LEU A 515       7.262  23.021  19.902  1.00  0.00           H  
ATOM   1058  N   PHE A 516       8.541  18.814  22.952  1.00 14.08           N  
ANISOU 1058  N   PHE A 516     2069   1579   1699    290    160    308
ATOM   1059  CA  PHE A 516       7.568  18.870  24.039  1.00 15.25           C  
ANISOU 1059  CA  PHE A 516     2445   1921   1427     30    159     96
ATOM   1060  C   PHE A 516       7.049  20.298  24.222  1.00 12.32           C  
ANISOU 1060  C   PHE A 516     2012   1726    942   -264    183    116
ATOM   1061  O   PHE A 516       7.837  21.233  24.103  1.00 15.79           O  
ANISOU 1061  O   PHE A 516     2706   1774   1518   -593    318      7
ATOM   1062  CB  PHE A 516       8.235  18.326  25.313  1.00 14.08           C  
ANISOU 1062  CB  PHE A 516     2094   1587   1668    375      5    -18
ATOM   1063  CG  PHE A 516       7.467  18.483  26.617  1.00 16.25           C  
ANISOU 1063  CG  PHE A 516     2570   2129   1472    -65     75    -92
ATOM   1064  CD1 PHE A 516       6.307  17.720  26.867  1.00 15.14           C  
ANISOU 1064  CD1 PHE A 516     2834   1562   1356    -59    389   -264
ATOM   1065  CE1 PHE A 516       5.600  17.907  28.047  1.00 15.55           C  
ANISOU 1065  CE1 PHE A 516     2902   1451   1553   -477    768     22
ATOM   1066  CZ  PHE A 516       6.009  18.867  28.965  1.00 17.44           C  
ANISOU 1066  CZ  PHE A 516     2669   1864   2093   -147    396   -409
ATOM   1067  CD2 PHE A 516       7.852  19.471  27.547  1.00 15.67           C  
ANISOU 1067  CD2 PHE A 516     3141   2005    805   -238    155    223
ATOM   1068  CE2 PHE A 516       7.125  19.653  28.713  1.00 18.65           C  
ANISOU 1068  CE2 PHE A 516     2553   2981   1552   -214    127   -465
ATOM   1069  H   PHE A 516       9.510  18.752  23.238  1.00  0.00           H  
ATOM   1070  HA  PHE A 516       6.723  18.230  23.786  1.00  0.00           H  
ATOM   1071  HB3 PHE A 516       9.221  18.772  25.442  1.00  0.00           H  
ATOM   1072  HB2 PHE A 516       8.428  17.274  25.147  1.00  0.00           H  
ATOM   1073  HD1 PHE A 516       5.974  16.981  26.151  1.00  0.00           H  
ATOM   1074  HE1 PHE A 516       4.724  17.310  28.251  1.00  0.00           H  
ATOM   1075  HZ  PHE A 516       5.455  19.011  29.877  1.00  0.00           H  
ATOM   1076  HD2 PHE A 516       8.722  20.079  27.359  1.00  0.00           H  
ATOM   1077  HE2 PHE A 516       7.430  20.404  29.427  1.00  0.00           H  
ATOM   1078  N   MET A 517       5.746  20.432  24.498  1.00 14.62           N  
ANISOU 1078  N   MET A 517     2144   1625   1784   -331    176    189
ATOM   1079  CA  MET A 517       5.087  21.721  24.670  1.00 15.75           C  
ANISOU 1079  CA  MET A 517     2557   1861   1566      4    138   -278
ATOM   1080  C   MET A 517       4.388  21.811  26.029  1.00 14.55           C  
ANISOU 1080  C   MET A 517     2413   1605   1510    -26    191    215
ATOM   1081  O   MET A 517       4.467  22.862  26.661  1.00 15.99           O  
ANISOU 1081  O   MET A 517     2583   1948   1544     51    363     75
ATOM   1082  CB  MET A 517       4.111  21.970  23.507  1.00 17.93           C  
ANISOU 1082  CB  MET A 517     2463   2248   2099   -193   -139    -18
ATOM   1083  CG  MET A 517       4.809  22.070  22.139  1.00 16.46           C  
ANISOU 1083  CG  MET A 517     2042   2045   2165    -67   -165     73
ATOM   1084  SD  MET A 517       3.701  22.381  20.745  1.00 17.27           S  
ANISOU 1084  SD  MET A 517     2798   2049   1715    213    -34    110
ATOM   1085  CE  MET A 517       3.115  24.051  21.130  1.00 18.36           C  
ANISOU 1085  CE  MET A 517     3199   2089   1687    580    -11    553
ATOM   1086  H   MET A 517       5.157  19.612  24.566  1.00  0.00           H  
ATOM   1087  HA  MET A 517       5.818  22.531  24.658  1.00  0.00           H  
ATOM   1088  HB3 MET A 517       3.560  22.889  23.700  1.00  0.00           H  
ATOM   1089  HB2 MET A 517       3.368  21.174  23.475  1.00  0.00           H  
ATOM   1090  HG3 MET A 517       5.333  21.141  21.918  1.00  0.00           H  
ATOM   1091  HG2 MET A 517       5.569  22.851  22.158  1.00  0.00           H  
ATOM   1092  HE1 MET A 517       2.471  24.418  20.332  1.00  0.00           H  
ATOM   1093  HE2 MET A 517       2.537  24.054  22.050  1.00  0.00           H  
ATOM   1094  HE3 MET A 517       3.954  24.736  21.245  1.00  0.00           H  
ATOM   1095  N   GLY A 518       3.748  20.731  26.492  1.00 13.98           N  
ANISOU 1095  N   GLY A 518     2482   1425   1403    157    333   -132
ATOM   1096  CA  GLY A 518       3.099  20.776  27.791  1.00 16.48           C  
ANISOU 1096  CA  GLY A 518     2781   1399   2078    164    986    173
ATOM   1097  C   GLY A 518       2.307  19.507  28.050  1.00 16.58           C  
ANISOU 1097  C   GLY A 518     2649   1637   2013     62    699    138
ATOM   1098  O   GLY A 518       2.454  18.500  27.360  1.00 16.74           O  
ANISOU 1098  O   GLY A 518     2695   1620   2045   -221    162    155
ATOM   1099  H   GLY A 518       3.700  19.870  25.962  1.00  0.00           H  
ATOM   1100  HA3 GLY A 518       2.433  21.637  27.856  1.00  0.00           H  
ATOM   1101  HA2 GLY A 518       3.854  20.870  28.567  1.00  0.00           H  
ATOM   1102  N   TYR A 519       1.478  19.579  29.095  1.00 17.80           N  
ANISOU 1102  N   TYR A 519     3242   1684   1836     17    884   -277
ATOM   1103  CA  TYR A 519       0.618  18.499  29.549  1.00 18.52           C  
ANISOU 1103  CA  TYR A 519     3163   2070   1801   -234    927   -595
ATOM   1104  C   TYR A 519      -0.646  19.087  30.185  1.00 20.26           C  
ANISOU 1104  C   TYR A 519     3006   2827   1865   -170    856   -699
ATOM   1105  O   TYR A 519      -0.649  20.243  30.589  1.00 20.90           O  
ANISOU 1105  O   TYR A 519     3981   1806   2153   -479    941    334
ATOM   1106  CB  TYR A 519       1.405  17.585  30.525  1.00 19.11           C  
ANISOU 1106  CB  TYR A 519     3279   2075   1908   -708    984     27
ATOM   1107  CG  TYR A 519       1.801  18.206  31.859  1.00 21.41           C  
ANISOU 1107  CG  TYR A 519     3688   2892   1552   -426    630    102
ATOM   1108  CD1 TYR A 519       0.914  18.173  32.957  1.00 24.12           C  
ANISOU 1108  CD1 TYR A 519     3294   3637   2232    -71    771    259
ATOM   1109  CE1 TYR A 519       1.279  18.759  34.184  1.00 29.97           C  
ANISOU 1109  CE1 TYR A 519     5136   3769   2480   -543    603    -11
ATOM   1110  CZ  TYR A 519       2.539  19.373  34.323  1.00 27.08           C  
ANISOU 1110  CZ  TYR A 519     4720   2790   2775   -394    963   -982
ATOM   1111  OH  TYR A 519       2.894  19.949  35.508  1.00 38.22           O  
ANISOU 1111  OH  TYR A 519     6714   5351   2457    322   1177  -1391
ATOM   1112  CE2 TYR A 519       3.431  19.402  33.233  1.00 27.23           C  
ANISOU 1112  CE2 TYR A 519     4378   3197   2769   -331    664    493
ATOM   1113  CD2 TYR A 519       3.059  18.824  32.004  1.00 25.42           C  
ANISOU 1113  CD2 TYR A 519     3854   3125   2679   -805    623    668
ATOM   1114  H   TYR A 519       1.418  20.437  29.629  1.00  0.00           H  
ATOM   1115  HA  TYR A 519       0.305  17.933  28.674  1.00  0.00           H  
ATOM   1116  HB3 TYR A 519       2.300  17.203  30.032  1.00  0.00           H  
ATOM   1117  HB2 TYR A 519       0.810  16.701  30.748  1.00  0.00           H  
ATOM   1118  HD1 TYR A 519      -0.057  17.711  32.858  1.00  0.00           H  
ATOM   1119  HE1 TYR A 519       0.587  18.741  35.013  1.00  0.00           H  
ATOM   1120  HH  TYR A 519       2.203  19.889  36.172  1.00  0.00           H  
ATOM   1121  HE2 TYR A 519       4.397  19.872  33.337  1.00  0.00           H  
ATOM   1122  HD2 TYR A 519       3.740  18.858  31.169  1.00  0.00           H  
ATOM   1123  N   SER A 520      -1.682  18.254  30.310  1.00 27.40           N  
ANISOU 1123  N   SER A 520     3395   2740   4273   -502   1062  -1615
ATOM   1124  CA  SER A 520      -2.867  18.527  31.114  1.00 24.99           C  
ANISOU 1124  CA  SER A 520     3784   3319   2389  -1072   1291  -1528
ATOM   1125  C   SER A 520      -3.067  17.365  32.093  1.00 32.42           C  
ANISOU 1125  C   SER A 520     4359   4284   3672   -785   2174   -712
ATOM   1126  O   SER A 520      -2.578  16.261  31.852  1.00 27.47           O  
ANISOU 1126  O   SER A 520     3211   4217   3009  -1080   1806   -426
ATOM   1127  CB  SER A 520      -4.097  18.689  30.198  1.00 35.51           C  
ANISOU 1127  CB  SER A 520     4020   5089   4381   1391   1117    448
ATOM   1128  OG  SER A 520      -4.077  19.943  29.547  1.00 46.95           O  
ANISOU 1128  OG  SER A 520     6183   6596   5059   1404   1205   1404
ATOM   1129  H   SER A 520      -1.600  17.309  29.955  1.00  0.00           H  
ATOM   1130  HA  SER A 520      -2.737  19.431  31.712  1.00  0.00           H  
ATOM   1131  HB3 SER A 520      -5.021  18.639  30.777  1.00  0.00           H  
ATOM   1132  HB2 SER A 520      -4.149  17.892  29.457  1.00  0.00           H  
ATOM   1133  HG  SER A 520      -4.124  20.638  30.212  1.00  0.00           H  
ATOM   1134  N   THR A 521      -3.804  17.647  33.174  1.00 39.37           N  
ANISOU 1134  N   THR A 521     5174   6176   3606  -1228   1937  -2397
ATOM   1135  CA  THR A 521      -4.294  16.650  34.129  1.00 43.35           C  
ANISOU 1135  CA  THR A 521     6363   5710   4395  -2666   1352  -2429
ATOM   1136  C   THR A 521      -5.825  16.754  34.305  1.00 42.71           C  
ANISOU 1136  C   THR A 521     6252   5236   4738  -2183   2816  -1497
ATOM   1137  O   THR A 521      -6.413  15.825  34.859  1.00 53.87           O  
ANISOU 1137  O   THR A 521     7774   7531   5163  -4235   3610  -1663
ATOM   1138  CB  THR A 521      -3.604  16.785  35.515  1.00 48.19           C  
ANISOU 1138  CB  THR A 521     6274   6458   5576  -2448    819  -2137
ATOM   1139  OG1 THR A 521      -4.021  17.933  36.235  1.00 49.93           O  
ANISOU 1139  OG1 THR A 521     8247   7625   3098   -982   2963  -2484
ATOM   1140  CG2 THR A 521      -2.068  16.761  35.438  1.00 50.89           C  
ANISOU 1140  CG2 THR A 521     6236   7469   5628   -966    -76  -2042
ATOM   1141  H   THR A 521      -4.129  18.594  33.317  1.00  0.00           H  
ATOM   1142  HA  THR A 521      -4.104  15.646  33.750  1.00  0.00           H  
ATOM   1143  HB  THR A 521      -3.904  15.927  36.118  1.00  0.00           H  
ATOM   1144  HG1 THR A 521      -3.575  18.711  35.885  1.00  0.00           H  
ATOM   1145 HG21 THR A 521      -1.626  16.756  36.434  1.00  0.00           H  
ATOM   1146 HG22 THR A 521      -1.716  15.872  34.915  1.00  0.00           H  
ATOM   1147 HG23 THR A 521      -1.679  17.633  34.911  1.00  0.00           H  
ATOM   1148  N   LYS A 522      -6.439  17.839  33.796  1.00 48.47           N  
ANISOU 1148  N   LYS A 522     5025   5747   7643   -950   2103  -2478
ATOM   1149  CA  LYS A 522      -7.882  18.060  33.758  1.00 50.71           C  
ANISOU 1149  CA  LYS A 522     5630   6311   7327   -444   1403  -3370
ATOM   1150  C   LYS A 522      -8.315  18.502  32.344  1.00 48.87           C  
ANISOU 1150  C   LYS A 522     4079   5921   8565  -1458   1004  -2238
ATOM   1151  O   LYS A 522      -7.646  19.358  31.762  1.00 49.34           O  
ANISOU 1151  O   LYS A 522     5119   3731   9895   -508    162  -1310
ATOM   1152  CB  LYS A 522      -8.270  19.122  34.803  1.00 50.73           C  
ANISOU 1152  CB  LYS A 522     4628   6867   7779   -613   -498  -4756
ATOM   1153  CG  LYS A 522      -8.428  18.526  36.211  1.00 66.77           C  
ANISOU 1153  CG  LYS A 522     8176   9484   7709    268   1912  -4845
ATOM   1154  CD  LYS A 522      -9.137  19.477  37.183  1.00 77.75           C  
ANISOU 1154  CD  LYS A 522     8989  12906   7647   2360   2498  -3942
ATOM   1155  CE  LYS A 522      -9.572  18.765  38.472  1.00 81.65           C  
ANISOU 1155  CE  LYS A 522     8826  14384   7811   2042   2555  -3145
ATOM   1156  NZ  LYS A 522     -10.301  19.671  39.375  1.00 85.92           N1+
ANISOU 1156  NZ  LYS A 522     9640  14284   8719   1889   3483  -3513
ATOM   1157  H   LYS A 522      -5.889  18.562  33.353  1.00  0.00           H  
ATOM   1158  HA  LYS A 522      -8.359  17.128  34.038  1.00  0.00           H  
ATOM   1159  HB3 LYS A 522      -9.242  19.535  34.525  1.00  0.00           H  
ATOM   1160  HB2 LYS A 522      -7.577  19.965  34.798  1.00  0.00           H  
ATOM   1161  HG3 LYS A 522      -7.449  18.251  36.608  1.00  0.00           H  
ATOM   1162  HG2 LYS A 522      -9.000  17.600  36.148  1.00  0.00           H  
ATOM   1163  HD3 LYS A 522     -10.007  19.919  36.693  1.00  0.00           H  
ATOM   1164  HD2 LYS A 522      -8.466  20.305  37.421  1.00  0.00           H  
ATOM   1165  HE3 LYS A 522      -8.702  18.366  38.996  1.00  0.00           H  
ATOM   1166  HE2 LYS A 522     -10.221  17.920  38.237  1.00  0.00           H  
ATOM   1167  HZ1 LYS A 522     -11.124  20.024  38.907  1.00  0.00           H  
ATOM   1168  HZ2 LYS A 522     -10.576  19.170  40.208  1.00  0.00           H  
ATOM   1169  HZ3 LYS A 522      -9.703  20.444  39.629  1.00  0.00           H  
ATOM   1170  N   PRO A 523      -9.435  17.948  31.819  1.00 50.86           N  
ANISOU 1170  N   PRO A 523     3898   5138  10287   -210   -156  -1784
ATOM   1171  CA  PRO A 523     -10.296  16.919  32.444  1.00 56.91           C  
ANISOU 1171  CA  PRO A 523     4894   6632  10097    350   1520   -889
ATOM   1172  C   PRO A 523      -9.695  15.496  32.480  1.00 52.50           C  
ANISOU 1172  C   PRO A 523     5391   5655   8902   -691   3068  -1523
ATOM   1173  O   PRO A 523     -10.216  14.655  33.211  1.00 55.41           O  
ANISOU 1173  O   PRO A 523     5211   6743   9096  -2475   3601  -1904
ATOM   1174  CB  PRO A 523     -11.581  16.973  31.603  1.00 58.32           C  
ANISOU 1174  CB  PRO A 523     4587   6501  11070   -368   1639    162
ATOM   1175  CG  PRO A 523     -11.112  17.406  30.223  1.00 58.01           C  
ANISOU 1175  CG  PRO A 523     4874   5491  11674    228    875   1185
ATOM   1176  CD  PRO A 523      -9.983  18.384  30.534  1.00 52.73           C  
ANISOU 1176  CD  PRO A 523     4027   4150  11856   2041   -358     -3
ATOM   1177  HA  PRO A 523     -10.545  17.202  33.468  1.00  0.00           H  
ATOM   1178  HB3 PRO A 523     -12.249  17.730  32.015  1.00  0.00           H  
ATOM   1179  HB2 PRO A 523     -12.134  16.032  31.577  1.00  0.00           H  
ATOM   1180  HG3 PRO A 523     -11.902  17.838  29.609  1.00  0.00           H  
ATOM   1181  HG2 PRO A 523     -10.708  16.543  29.691  1.00  0.00           H  
ATOM   1182  HD2 PRO A 523      -9.235  18.399  29.740  1.00  0.00           H  
ATOM   1183  HD3 PRO A 523     -10.377  19.396  30.648  1.00  0.00           H  
ATOM   1184  N   GLN A 524      -8.613  15.263  31.718  1.00 47.45           N  
ANISOU 1184  N   GLN A 524     5243   5407   7377    114   2469    -45
ATOM   1185  CA  GLN A 524      -7.898  13.991  31.614  1.00 39.61           C  
ANISOU 1185  CA  GLN A 524     2770   5598   6679   -649   1381   -624
ATOM   1186  C   GLN A 524      -6.388  14.241  31.503  1.00 36.55           C  
ANISOU 1186  C   GLN A 524     2914   5532   5439   -148   2214   -513
ATOM   1187  O   GLN A 524      -5.977  15.344  31.132  1.00 35.22           O  
ANISOU 1187  O   GLN A 524     2836   6499   4043  -1675   1854   -317
ATOM   1188  CB  GLN A 524      -8.429  13.217  30.386  1.00 42.57           C  
ANISOU 1188  CB  GLN A 524     3590   4852   7731    426    707   -900
ATOM   1189  CG  GLN A 524      -9.832  12.617  30.612  1.00 48.80           C  
ANISOU 1189  CG  GLN A 524     2953   6234   9352    276     51  -1309
ATOM   1190  CD  GLN A 524     -10.457  11.993  29.368  1.00 48.60           C  
ANISOU 1190  CD  GLN A 524     3032   7486   7944    418   -268    529
ATOM   1191  OE1 GLN A 524     -10.060  12.277  28.239  1.00 69.06           O  
ANISOU 1191  OE1 GLN A 524     7021   7955  11262   -472   -182   5243
ATOM   1192  NE2 GLN A 524     -11.470  11.150  29.575  1.00 56.75           N  
ANISOU 1192  NE2 GLN A 524     3957   9919   7684   -326   1787   3309
ATOM   1193  H   GLN A 524      -8.230  16.013  31.161  1.00  0.00           H  
ATOM   1194  HA  GLN A 524      -8.060  13.402  32.519  1.00  0.00           H  
ATOM   1195  HB3 GLN A 524      -7.744  12.408  30.127  1.00  0.00           H  
ATOM   1196  HB2 GLN A 524      -8.435  13.884  29.521  1.00  0.00           H  
ATOM   1197  HG3 GLN A 524     -10.531  13.387  30.931  1.00  0.00           H  
ATOM   1198  HG2 GLN A 524      -9.790  11.877  31.412  1.00  0.00           H  
ATOM   1199 HE22 GLN A 524     -11.919  10.702  28.786  1.00  0.00           H  
ATOM   1200 HE21 GLN A 524     -11.778  10.935  30.512  1.00  0.00           H  
ATOM   1201  N   LEU A 525      -5.587  13.196  31.789  1.00 30.89           N  
ANISOU 1201  N   LEU A 525     4033   4252   3451   -994   2027    -82
ATOM   1202  CA  LEU A 525      -4.147  13.187  31.522  1.00 27.30           C  
ANISOU 1202  CA  LEU A 525     3759   4018   2595   -977   1074   -445
ATOM   1203  C   LEU A 525      -3.897  13.281  30.013  1.00 25.11           C  
ANISOU 1203  C   LEU A 525     3001   3772   2766  -1017   1234   -202
ATOM   1204  O   LEU A 525      -4.433  12.466  29.262  1.00 24.07           O  
ANISOU 1204  O   LEU A 525     3493   3494   2156   -108    273     20
ATOM   1205  CB  LEU A 525      -3.460  11.913  32.066  1.00 32.39           C  
ANISOU 1205  CB  LEU A 525     4173   5476   2657  -1181    131   -162
ATOM   1206  CG  LEU A 525      -3.478  11.714  33.594  1.00 39.79           C  
ANISOU 1206  CG  LEU A 525     4978   7304   2836  -1218   -306    681
ATOM   1207  CD1 LEU A 525      -2.705  10.432  33.968  1.00 41.80           C  
ANISOU 1207  CD1 LEU A 525     5438   6824   3621  -1361   -133   2451
ATOM   1208  CD2 LEU A 525      -2.962  12.933  34.384  1.00 38.11           C  
ANISOU 1208  CD2 LEU A 525     5209   8324    945  -1110    239   -497
ATOM   1209  H   LEU A 525      -5.994  12.319  32.090  1.00  0.00           H  
ATOM   1210  HA  LEU A 525      -3.715  14.058  32.005  1.00  0.00           H  
ATOM   1211  HB3 LEU A 525      -2.417  11.923  31.747  1.00  0.00           H  
ATOM   1212  HB2 LEU A 525      -3.900  11.036  31.595  1.00  0.00           H  
ATOM   1213  HG  LEU A 525      -4.519  11.559  33.878  1.00  0.00           H  
ATOM   1214 HD11 LEU A 525      -3.213   9.884  34.760  1.00  0.00           H  
ATOM   1215 HD12 LEU A 525      -2.595   9.753  33.122  1.00  0.00           H  
ATOM   1216 HD13 LEU A 525      -1.699  10.653  34.324  1.00  0.00           H  
ATOM   1217 HD21 LEU A 525      -2.308  12.646  35.208  1.00  0.00           H  
ATOM   1218 HD22 LEU A 525      -2.394  13.620  33.759  1.00  0.00           H  
ATOM   1219 HD23 LEU A 525      -3.793  13.489  34.819  1.00  0.00           H  
ATOM   1220  N   ALA A 526      -3.086  14.266  29.612  1.00 22.45           N  
ANISOU 1220  N   ALA A 526     3613   2612   2302  -1108    332   -271
ATOM   1221  CA  ALA A 526      -2.669  14.436  28.230  1.00 22.29           C  
ANISOU 1221  CA  ALA A 526     3188   3043   2238   -787    354   -156
ATOM   1222  C   ALA A 526      -1.270  15.041  28.171  1.00 19.97           C  
ANISOU 1222  C   ALA A 526     2742   2749   2097   -190    631   -171
ATOM   1223  O   ALA A 526      -0.919  15.820  29.049  1.00 23.61           O  
ANISOU 1223  O   ALA A 526     3595   2967   2409   -627   1041   -489
ATOM   1224  CB  ALA A 526      -3.691  15.280  27.450  1.00 25.70           C  
ANISOU 1224  CB  ALA A 526     3211   3947   2607   -309    507     92
ATOM   1225  H   ALA A 526      -2.693  14.910  30.286  1.00  0.00           H  
ATOM   1226  HA  ALA A 526      -2.619  13.442  27.804  1.00  0.00           H  
ATOM   1227  HB1 ALA A 526      -3.413  15.355  26.397  1.00  0.00           H  
ATOM   1228  HB2 ALA A 526      -4.685  14.834  27.490  1.00  0.00           H  
ATOM   1229  HB3 ALA A 526      -3.762  16.292  27.846  1.00  0.00           H  
ATOM   1230  N   ILE A 527      -0.506  14.675  27.134  1.00 16.05           N  
ANISOU 1230  N   ILE A 527     2478   2169   1449   -288     10   -184
ATOM   1231  CA  ILE A 527       0.815  15.222  26.836  1.00 16.85           C  
ANISOU 1231  CA  ILE A 527     2447   2115   1838   -256    376    -81
ATOM   1232  C   ILE A 527       0.753  15.796  25.415  1.00 14.98           C  
ANISOU 1232  C   ILE A 527     1883   1877   1932   -197   -408    -73
ATOM   1233  O   ILE A 527       0.240  15.129  24.518  1.00 16.03           O  
ANISOU 1233  O   ILE A 527     2367   2056   1665   -492    103   -355
ATOM   1234  CB  ILE A 527       1.928  14.135  26.894  1.00 18.45           C  
ANISOU 1234  CB  ILE A 527     2483   2214   2312   -176    117    236
ATOM   1235  CG1 ILE A 527       1.998  13.490  28.296  1.00 21.28           C  
ANISOU 1235  CG1 ILE A 527     3093   3008   1984   -836    120     58
ATOM   1236  CG2 ILE A 527       3.320  14.673  26.480  1.00 16.56           C  
ANISOU 1236  CG2 ILE A 527     2416   1563   2312   -336     69   -211
ATOM   1237  CD1 ILE A 527       3.002  12.334  28.417  1.00 21.90           C  
ANISOU 1237  CD1 ILE A 527     3392   2771   2155   -498    -73   -194
ATOM   1238  H   ILE A 527      -0.873  14.013  26.461  1.00  0.00           H  
ATOM   1239  HA  ILE A 527       1.073  16.024  27.530  1.00  0.00           H  
ATOM   1240  HB  ILE A 527       1.653  13.339  26.203  1.00  0.00           H  
ATOM   1241 HG13 ILE A 527       1.019  13.105  28.577  1.00  0.00           H  
ATOM   1242 HG12 ILE A 527       2.233  14.258  29.031  1.00  0.00           H  
ATOM   1243 HG21 ILE A 527       4.071  13.886  26.512  1.00  0.00           H  
ATOM   1244 HG22 ILE A 527       3.342  15.062  25.463  1.00  0.00           H  
ATOM   1245 HG23 ILE A 527       3.647  15.470  27.147  1.00  0.00           H  
ATOM   1246 HD11 ILE A 527       2.771  11.710  29.281  1.00  0.00           H  
ATOM   1247 HD12 ILE A 527       2.986  11.696  27.532  1.00  0.00           H  
ATOM   1248 HD13 ILE A 527       4.019  12.703  28.548  1.00  0.00           H  
ATOM   1249  N   VAL A 528       1.274  17.018  25.251  1.00 14.28           N  
ANISOU 1249  N   VAL A 528     2066   1736   1621    -83    146     81
ATOM   1250  CA  VAL A 528       1.260  17.769  24.002  1.00 14.41           C  
ANISOU 1250  CA  VAL A 528     2333   1656   1485    -69    208    -88
ATOM   1251  C   VAL A 528       2.706  17.971  23.519  1.00 15.12           C  
ANISOU 1251  C   VAL A 528     2091   1975   1676     80    -62   -300
ATOM   1252  O   VAL A 528       3.562  18.400  24.295  1.00 13.84           O  
ANISOU 1252  O   VAL A 528     1927   1683   1646   -215     68    149
ATOM   1253  CB  VAL A 528       0.597  19.164  24.193  1.00 15.90           C  
ANISOU 1253  CB  VAL A 528     2306   1756   1978   -240    312   -450
ATOM   1254  CG1 VAL A 528       0.540  20.009  22.905  1.00 16.92           C  
ANISOU 1254  CG1 VAL A 528     2017   2312   2099   -175    326     16
ATOM   1255  CG2 VAL A 528      -0.834  19.024  24.741  1.00 21.55           C  
ANISOU 1255  CG2 VAL A 528     2843   2776   2567   -182    620   -811
ATOM   1256  H   VAL A 528       1.700  17.492  26.039  1.00  0.00           H  
ATOM   1257  HA  VAL A 528       0.698  17.225  23.244  1.00  0.00           H  
ATOM   1258  HB  VAL A 528       1.173  19.731  24.926  1.00  0.00           H  
ATOM   1259 HG11 VAL A 528       0.074  20.978  23.090  1.00  0.00           H  
ATOM   1260 HG12 VAL A 528       1.520  20.207  22.474  1.00  0.00           H  
ATOM   1261 HG13 VAL A 528      -0.058  19.496  22.154  1.00  0.00           H  
ATOM   1262 HG21 VAL A 528      -1.333  19.992  24.790  1.00  0.00           H  
ATOM   1263 HG22 VAL A 528      -1.438  18.377  24.106  1.00  0.00           H  
ATOM   1264 HG23 VAL A 528      -0.843  18.606  25.748  1.00  0.00           H  
ATOM   1265  N   THR A 529       2.925  17.682  22.229  1.00 13.74           N  
ANISOU 1265  N   THR A 529     2000   1710   1509     18    -85   -130
ATOM   1266  CA  THR A 529       4.151  17.977  21.489  1.00 13.83           C  
ANISOU 1266  CA  THR A 529     1898   2012   1344     31   -207     35
ATOM   1267  C   THR A 529       3.776  18.697  20.179  1.00 13.36           C  
ANISOU 1267  C   THR A 529     1918   1798   1358   -127    -65    -13
ATOM   1268  O   THR A 529       2.593  18.821  19.863  1.00 14.35           O  
ANISOU 1268  O   THR A 529     1744   1827   1881    380    182   -220
ATOM   1269  CB  THR A 529       4.955  16.681  21.149  1.00 13.23           C  
ANISOU 1269  CB  THR A 529     2208   1385   1430   -582    -87    212
ATOM   1270  OG1 THR A 529       4.400  15.917  20.094  1.00 14.52           O  
ANISOU 1270  OG1 THR A 529     2100   2003   1412   -404   -231     -7
ATOM   1271  CG2 THR A 529       5.233  15.781  22.363  1.00 13.37           C  
ANISOU 1271  CG2 THR A 529     1970   1510   1599   -326    -87    343
ATOM   1272  H   THR A 529       2.160  17.330  21.668  1.00  0.00           H  
ATOM   1273  HA  THR A 529       4.777  18.656  22.068  1.00  0.00           H  
ATOM   1274  HB  THR A 529       5.932  16.979  20.773  1.00  0.00           H  
ATOM   1275  HG1 THR A 529       4.406  16.446  19.291  1.00  0.00           H  
ATOM   1276 HG21 THR A 529       5.840  14.920  22.087  1.00  0.00           H  
ATOM   1277 HG22 THR A 529       5.774  16.319  23.140  1.00  0.00           H  
ATOM   1278 HG23 THR A 529       4.311  15.410  22.809  1.00  0.00           H  
ATOM   1279  N   GLN A 530       4.791  19.137  19.418  1.00 14.21           N  
ANISOU 1279  N   GLN A 530     2067   1863   1467   -158    157   -332
ATOM   1280  CA  GLN A 530       4.625  19.682  18.068  1.00 15.00           C  
ANISOU 1280  CA  GLN A 530     2224   1815   1658    -59    243      0
ATOM   1281  C   GLN A 530       3.994  18.658  17.104  1.00 13.98           C  
ANISOU 1281  C   GLN A 530     2022   1849   1441    -99     82    232
ATOM   1282  O   GLN A 530       4.179  17.451  17.283  1.00 14.87           O  
ANISOU 1282  O   GLN A 530     1799   1817   2033    143    129     50
ATOM   1283  CB  GLN A 530       5.998  20.161  17.542  1.00 14.11           C  
ANISOU 1283  CB  GLN A 530     1915   1858   1584   -103      6    214
ATOM   1284  CG  GLN A 530       7.011  19.035  17.215  1.00 14.34           C  
ANISOU 1284  CG  GLN A 530     1773   2087   1586   -138    130    -45
ATOM   1285  CD  GLN A 530       8.319  19.523  16.596  1.00 14.70           C  
ANISOU 1285  CD  GLN A 530     1767   1859   1959    199    367   -304
ATOM   1286  OE1 GLN A 530       9.390  19.068  16.988  1.00 15.44           O  
ANISOU 1286  OE1 GLN A 530     2075   2144   1646    152   -102    323
ATOM   1287  NE2 GLN A 530       8.255  20.431  15.623  1.00 17.44           N  
ANISOU 1287  NE2 GLN A 530     2287   2252   2085     46    293     90
ATOM   1288  H   GLN A 530       5.741  19.037  19.750  1.00  0.00           H  
ATOM   1289  HA  GLN A 530       3.960  20.544  18.142  1.00  0.00           H  
ATOM   1290  HB3 GLN A 530       6.430  20.863  18.255  1.00  0.00           H  
ATOM   1291  HB2 GLN A 530       5.816  20.747  16.644  1.00  0.00           H  
ATOM   1292  HG3 GLN A 530       6.596  18.314  16.512  1.00  0.00           H  
ATOM   1293  HG2 GLN A 530       7.242  18.486  18.128  1.00  0.00           H  
ATOM   1294 HE22 GLN A 530       9.106  20.814  15.228  1.00  0.00           H  
ATOM   1295 HE21 GLN A 530       7.364  20.770  15.280  1.00  0.00           H  
ATOM   1296  N   TRP A 531       3.308  19.173  16.073  1.00 13.00           N  
ANISOU 1296  N   TRP A 531     1504   1764   1672    433    106     56
ATOM   1297  CA  TRP A 531       2.868  18.371  14.939  1.00 14.97           C  
ANISOU 1297  CA  TRP A 531     1798   1958   1931    108    188   -183
ATOM   1298  C   TRP A 531       3.932  18.456  13.840  1.00 15.57           C  
ANISOU 1298  C   TRP A 531     2050   1726   2139   -134    342   -559
ATOM   1299  O   TRP A 531       4.125  19.528  13.268  1.00 18.10           O  
ANISOU 1299  O   TRP A 531     2820   1634   2421     21    185   -498
ATOM   1300  CB  TRP A 531       1.502  18.855  14.430  1.00 17.03           C  
ANISOU 1300  CB  TRP A 531     2120   1930   2420    543    -57     30
ATOM   1301  CG  TRP A 531       0.953  18.001  13.333  1.00 17.99           C  
ANISOU 1301  CG  TRP A 531     1949   2191   2695    204   -118    -45
ATOM   1302  CD1 TRP A 531       1.026  18.262  12.009  1.00 20.00           C  
ANISOU 1302  CD1 TRP A 531     2427   2449   2723    230    -28   -296
ATOM   1303  NE1 TRP A 531       0.555  17.178  11.298  1.00 18.81           N  
ANISOU 1303  NE1 TRP A 531     2202   3071   1872    179     57   -236
ATOM   1304  CE2 TRP A 531       0.165  16.152  12.135  1.00 20.03           C  
ANISOU 1304  CE2 TRP A 531     2457   2880   2271   -149   -187   -111
ATOM   1305  CD2 TRP A 531       0.396  16.660  13.448  1.00 19.07           C  
ANISOU 1305  CD2 TRP A 531     2525   2338   2383    -38   -126   -162
ATOM   1306  CE3 TRP A 531       0.092  15.808  14.534  1.00 17.05           C  
ANISOU 1306  CE3 TRP A 531     1949   2487   2041    193    -15   -445
ATOM   1307  CZ3 TRP A 531      -0.407  14.508  14.324  1.00 18.92           C  
ANISOU 1307  CZ3 TRP A 531     2525   2900   1763   -187   -186   -578
ATOM   1308  CH2 TRP A 531      -0.617  14.032  13.015  1.00 17.45           C  
ANISOU 1308  CH2 TRP A 531     1903   3183   1543     58   -594   -160
ATOM   1309  CZ2 TRP A 531      -0.335  14.858  11.911  1.00 20.48           C  
ANISOU 1309  CZ2 TRP A 531     2741   3415   1625   -547   -332   -252
ATOM   1310  H   TRP A 531       3.207  20.175  15.982  1.00  0.00           H  
ATOM   1311  HA  TRP A 531       2.747  17.328  15.244  1.00  0.00           H  
ATOM   1312  HB3 TRP A 531       1.553  19.892  14.096  1.00  0.00           H  
ATOM   1313  HB2 TRP A 531       0.780  18.828  15.241  1.00  0.00           H  
ATOM   1314  HD1 TRP A 531       1.432  19.171  11.592  1.00  0.00           H  
ATOM   1315  HE1 TRP A 531       0.544  17.152  10.286  1.00  0.00           H  
ATOM   1316  HE3 TRP A 531       0.253  16.161  15.541  1.00  0.00           H  
ATOM   1317  HZ3 TRP A 531      -0.619  13.872  15.172  1.00  0.00           H  
ATOM   1318  HH2 TRP A 531      -0.980  13.029  12.855  1.00  0.00           H  
ATOM   1319  HZ2 TRP A 531      -0.487  14.497  10.906  1.00  0.00           H  
ATOM   1320  N   CYS A 532       4.587  17.325  13.555  1.00 15.03           N  
ANISOU 1320  N   CYS A 532     1907   1606   2196    128   -105   -336
ATOM   1321  CA  CYS A 532       5.581  17.214  12.492  1.00 16.63           C  
ANISOU 1321  CA  CYS A 532     2711   1815   1791   -469     37   -711
ATOM   1322  C   CYS A 532       4.883  17.059  11.128  1.00 17.22           C  
ANISOU 1322  C   CYS A 532     3407   1494   1642   -443   -133   -658
ATOM   1323  O   CYS A 532       3.865  16.376  11.041  1.00 20.92           O  
ANISOU 1323  O   CYS A 532     2682   2789   2475   -456    185    654
ATOM   1324  CB  CYS A 532       6.537  16.037  12.735  1.00 18.95           C  
ANISOU 1324  CB  CYS A 532     2746   2340   2114   -355     26   -377
ATOM   1325  SG  CYS A 532       7.436  16.245  14.296  1.00 22.41           S  
ANISOU 1325  SG  CYS A 532     2419   3668   2428    329    -72   -938
ATOM   1326  H   CYS A 532       4.353  16.470  14.041  1.00  0.00           H  
ATOM   1327  HA  CYS A 532       6.169  18.130  12.487  1.00  0.00           H  
ATOM   1328  HB3 CYS A 532       7.276  15.999  11.935  1.00  0.00           H  
ATOM   1329  HB2 CYS A 532       6.007  15.084  12.750  1.00  0.00           H  
ATOM   1330  HG  CYS A 532       6.372  16.101  15.091  1.00  0.00           H  
ATOM   1331  N   GLU A 533       5.447  17.686  10.087  1.00 25.34           N  
ANISOU 1331  N   GLU A 533     4327   2879   2420   -331   -148    278
ATOM   1332  CA  GLU A 533       4.934  17.641   8.718  1.00 19.92           C  
ANISOU 1332  CA  GLU A 533     2910   2422   2235     82   -160    296
ATOM   1333  C   GLU A 533       5.743  16.646   7.883  1.00 19.21           C  
ANISOU 1333  C   GLU A 533     2820   2606   1871     33   -234    674
ATOM   1334  O   GLU A 533       6.970  16.709   7.902  1.00 23.72           O  
ANISOU 1334  O   GLU A 533     2922   3841   2246    184   -115   -392
ATOM   1335  CB  GLU A 533       5.010  19.053   8.096  1.00 25.21           C  
ANISOU 1335  CB  GLU A 533     3080   3086   3411    398    593   1094
ATOM   1336  CG  GLU A 533       4.102  20.103   8.776  1.00 39.55           C  
ANISOU 1336  CG  GLU A 533     4087   5065   5875    658   1097    112
ATOM   1337  CD  GLU A 533       2.585  19.891   8.627  1.00 36.95           C  
ANISOU 1337  CD  GLU A 533     3783   5757   4497   1194     98    709
ATOM   1338  OE1 GLU A 533       2.149  19.073   7.785  1.00 36.08           O  
ANISOU 1338  OE1 GLU A 533     4368   5046   4295   1405   -683    579
ATOM   1339  OE2 GLU A 533       1.858  20.579   9.374  1.00 38.89           O1-
ANISOU 1339  OE2 GLU A 533     5210   6260   3305   2033    165    545
ATOM   1340  H   GLU A 533       6.296  18.219  10.225  1.00  0.00           H  
ATOM   1341  HA  GLU A 533       3.895  17.309   8.718  1.00  0.00           H  
ATOM   1342  HB3 GLU A 533       4.786  19.010   7.028  1.00  0.00           H  
ATOM   1343  HB2 GLU A 533       6.039  19.410   8.154  1.00  0.00           H  
ATOM   1344  HG3 GLU A 533       4.333  21.083   8.359  1.00  0.00           H  
ATOM   1345  HG2 GLU A 533       4.350  20.167   9.837  1.00  0.00           H  
ATOM   1346  N   GLY A 534       5.044  15.766   7.152  1.00 19.42           N  
ANISOU 1346  N   GLY A 534     2600   2963   1814     81    149    166
ATOM   1347  CA  GLY A 534       5.664  14.770   6.284  1.00 22.09           C  
ANISOU 1347  CA  GLY A 534     3707   2922   1762    479    -54    209
ATOM   1348  C   GLY A 534       5.485  13.372   6.887  1.00 19.40           C  
ANISOU 1348  C   GLY A 534     2730   2514   2127    479      0   -357
ATOM   1349  O   GLY A 534       4.381  13.018   7.300  1.00 20.99           O  
ANISOU 1349  O   GLY A 534     2572   3006   2395    319   -627   -327
ATOM   1350  H   GLY A 534       4.035  15.764   7.201  1.00  0.00           H  
ATOM   1351  HA3 GLY A 534       6.710  15.000   6.099  1.00  0.00           H  
ATOM   1352  HA2 GLY A 534       5.165  14.795   5.314  1.00  0.00           H  
ATOM   1353  N   SER A 535       6.553  12.559   6.858  1.00 17.28           N  
ANISOU 1353  N   SER A 535     1848   2664   2050    157     26   -105
ATOM   1354  CA  SER A 535       6.537  11.131   7.180  1.00 17.13           C  
ANISOU 1354  CA  SER A 535     2477   2457   1572      3   -195   -272
ATOM   1355  C   SER A 535       7.767  10.704   7.996  1.00 15.32           C  
ANISOU 1355  C   SER A 535     2167   2209   1444   -267   -271   -328
ATOM   1356  O   SER A 535       8.765  11.425   8.050  1.00 14.03           O  
ANISOU 1356  O   SER A 535     1895   1935   1501    -28   -356      6
ATOM   1357  CB  SER A 535       6.494  10.335   5.859  1.00 18.81           C  
ANISOU 1357  CB  SER A 535     2610   2210   2323   -151   -713   -790
ATOM   1358  OG  SER A 535       5.267  10.517   5.186  1.00 22.98           O  
ANISOU 1358  OG  SER A 535     3165   2881   2683    423   -755   -278
ATOM   1359  H   SER A 535       7.431  12.910   6.491  1.00  0.00           H  
ATOM   1360  HA  SER A 535       5.665  10.890   7.787  1.00  0.00           H  
ATOM   1361  HB3 SER A 535       6.608   9.271   6.050  1.00  0.00           H  
ATOM   1362  HB2 SER A 535       7.310  10.624   5.197  1.00  0.00           H  
ATOM   1363  HG  SER A 535       5.333  11.322   4.663  1.00  0.00           H  
ATOM   1364  N   SER A 536       7.677   9.496   8.580  1.00 15.82           N  
ANISOU 1364  N   SER A 536     2262   2026   1723    158   -363   -147
ATOM   1365  CA  SER A 536       8.781   8.795   9.235  1.00 15.59           C  
ANISOU 1365  CA  SER A 536     1603   2299   2021   -104   -180    -15
ATOM   1366  C   SER A 536       9.861   8.330   8.242  1.00 13.23           C  
ANISOU 1366  C   SER A 536     2033   1506   1488   -155    -21    374
ATOM   1367  O   SER A 536       9.577   8.158   7.056  1.00 14.69           O  
ANISOU 1367  O   SER A 536     1706   2045   1831   -153   -170     10
ATOM   1368  CB  SER A 536       8.219   7.647  10.101  1.00 15.78           C  
ANISOU 1368  CB  SER A 536     2084   2143   1768     31    -32    -65
ATOM   1369  OG  SER A 536       7.856   6.502   9.352  1.00 15.07           O  
ANISOU 1369  OG  SER A 536     1735   1801   2188    -79    180   -229
ATOM   1370  H   SER A 536       6.818   8.967   8.491  1.00  0.00           H  
ATOM   1371  HA  SER A 536       9.244   9.501   9.910  1.00  0.00           H  
ATOM   1372  HB3 SER A 536       7.360   7.985  10.681  1.00  0.00           H  
ATOM   1373  HB2 SER A 536       8.976   7.346  10.826  1.00  0.00           H  
ATOM   1374  HG  SER A 536       7.476   5.853   9.952  1.00  0.00           H  
ATOM   1375  N   LEU A 537      11.079   8.099   8.760  1.00 14.45           N  
ANISOU 1375  N   LEU A 537     2179   1979   1332   -325   -192    -46
ATOM   1376  CA  LEU A 537      12.192   7.515   8.013  1.00 15.08           C  
ANISOU 1376  CA  LEU A 537     1641   2129   1960   -281   -132    111
ATOM   1377  C   LEU A 537      11.897   6.073   7.551  1.00 14.21           C  
ANISOU 1377  C   LEU A 537     1690   1787   1922   -131   -134    273
ATOM   1378  O   LEU A 537      12.331   5.716   6.460  1.00 16.57           O  
ANISOU 1378  O   LEU A 537     2235   2131   1928   -518   -387    -10
ATOM   1379  CB  LEU A 537      13.499   7.628   8.836  1.00 16.06           C  
ANISOU 1379  CB  LEU A 537     2100   2261   1738   -521   -323    251
ATOM   1380  CG  LEU A 537      14.766   7.091   8.138  1.00 17.37           C  
ANISOU 1380  CG  LEU A 537     1904   2580   2114   -334   -151    612
ATOM   1381  CD1 LEU A 537      15.087   7.869   6.849  1.00 14.50           C  
ANISOU 1381  CD1 LEU A 537     1550   2317   1643   -134     29    162
ATOM   1382  CD2 LEU A 537      15.964   7.040   9.101  1.00 18.19           C  
ANISOU 1382  CD2 LEU A 537     2061   3062   1787   -434   -254    418
ATOM   1383  H   LEU A 537      11.250   8.284   9.741  1.00  0.00           H  
ATOM   1384  HA  LEU A 537      12.314   8.123   7.116  1.00  0.00           H  
ATOM   1385  HB3 LEU A 537      13.381   7.099   9.776  1.00  0.00           H  
ATOM   1386  HB2 LEU A 537      13.662   8.669   9.109  1.00  0.00           H  
ATOM   1387  HG  LEU A 537      14.582   6.053   7.869  1.00  0.00           H  
ATOM   1388 HD11 LEU A 537      16.157   7.925   6.663  1.00  0.00           H  
ATOM   1389 HD12 LEU A 537      14.639   7.393   5.980  1.00  0.00           H  
ATOM   1390 HD13 LEU A 537      14.704   8.887   6.883  1.00  0.00           H  
ATOM   1391 HD21 LEU A 537      16.655   6.243   8.823  1.00  0.00           H  
ATOM   1392 HD22 LEU A 537      16.521   7.975   9.101  1.00  0.00           H  
ATOM   1393 HD23 LEU A 537      15.653   6.854  10.129  1.00  0.00           H  
ATOM   1394  N   TYR A 538      11.122   5.300   8.339  1.00 14.68           N  
ANISOU 1394  N   TYR A 538     2197   1499   1882   -187    260    -48
ATOM   1395  CA  TYR A 538      10.622   3.973   7.959  1.00 15.67           C  
ANISOU 1395  CA  TYR A 538     2443   1813   1695   -257   -399    -93
ATOM   1396  C   TYR A 538       9.768   4.034   6.687  1.00 15.84           C  
ANISOU 1396  C   TYR A 538     1847   2243   1928   -256   -403   -707
ATOM   1397  O   TYR A 538       9.990   3.242   5.774  1.00 15.21           O  
ANISOU 1397  O   TYR A 538     2354   1602   1823     65    180   -351
ATOM   1398  CB  TYR A 538       9.814   3.335   9.113  1.00 16.31           C  
ANISOU 1398  CB  TYR A 538     2234   2021   1939   -308   -235   -116
ATOM   1399  CG  TYR A 538       9.322   1.917   8.858  1.00 17.80           C  
ANISOU 1399  CG  TYR A 538     2414   2009   2337   -294   -292    -50
ATOM   1400  CD1 TYR A 538       8.142   1.696   8.118  1.00 20.66           C  
ANISOU 1400  CD1 TYR A 538     3256   2204   2388    114   -753   -619
ATOM   1401  CE1 TYR A 538       7.727   0.388   7.811  1.00 18.34           C  
ANISOU 1401  CE1 TYR A 538     2388   2081   2498     99   -718    -75
ATOM   1402  CZ  TYR A 538       8.471  -0.710   8.280  1.00 19.16           C  
ANISOU 1402  CZ  TYR A 538     2922   1411   2945    315     86   -367
ATOM   1403  OH  TYR A 538       8.056  -1.977   7.998  1.00 24.95           O  
ANISOU 1403  OH  TYR A 538     3795   1798   3884   -243    228   -844
ATOM   1404  CE2 TYR A 538       9.630  -0.499   9.050  1.00 19.15           C  
ANISOU 1404  CE2 TYR A 538     2765   1656   2853   -228    394   -220
ATOM   1405  CD2 TYR A 538      10.056   0.811   9.337  1.00 17.70           C  
ANISOU 1405  CD2 TYR A 538     2431   1843   2449   -125   -109   -395
ATOM   1406  H   TYR A 538      10.806   5.662   9.228  1.00  0.00           H  
ATOM   1407  HA  TYR A 538      11.489   3.343   7.755  1.00  0.00           H  
ATOM   1408  HB3 TYR A 538       8.956   3.959   9.357  1.00  0.00           H  
ATOM   1409  HB2 TYR A 538      10.418   3.309  10.012  1.00  0.00           H  
ATOM   1410  HD1 TYR A 538       7.564   2.534   7.759  1.00  0.00           H  
ATOM   1411  HE1 TYR A 538       6.833   0.230   7.225  1.00  0.00           H  
ATOM   1412  HH  TYR A 538       8.518  -2.652   8.510  1.00  0.00           H  
ATOM   1413  HE2 TYR A 538      10.198  -1.341   9.416  1.00  0.00           H  
ATOM   1414  HD2 TYR A 538      10.955   0.957   9.915  1.00  0.00           H  
ATOM   1415  N   HIS A 539       8.818   4.983   6.661  1.00 16.08           N  
ANISOU 1415  N   HIS A 539     1817   2681   1609    -49   -354    171
ATOM   1416  CA  HIS A 539       7.938   5.232   5.528  1.00 15.98           C  
ANISOU 1416  CA  HIS A 539     2110   2519   1441    238   -422   -140
ATOM   1417  C   HIS A 539       8.710   5.671   4.273  1.00 15.39           C  
ANISOU 1417  C   HIS A 539     2154   1955   1737      3   -247     52
ATOM   1418  O   HIS A 539       8.413   5.172   3.191  1.00 16.26           O  
ANISOU 1418  O   HIS A 539     2243   2546   1387   -508    111    119
ATOM   1419  CB  HIS A 539       6.849   6.238   5.946  1.00 18.33           C  
ANISOU 1419  CB  HIS A 539     2444   2363   2154    360   -675   -299
ATOM   1420  CG  HIS A 539       5.885   6.621   4.852  1.00 19.60           C  
ANISOU 1420  CG  HIS A 539     2364   2669   2413    525   -950   -745
ATOM   1421  ND1 HIS A 539       6.194   7.581   3.883  1.00 24.65           N  
ANISOU 1421  ND1 HIS A 539     2886   3355   3125    259  -1208  -1117
ATOM   1422  CE1 HIS A 539       5.129   7.627   3.100  1.00 25.60           C  
ANISOU 1422  CE1 HIS A 539     2660   3847   3220      5  -1282   -963
ATOM   1423  NE2 HIS A 539       4.168   6.782   3.473  1.00 24.21           N  
ANISOU 1423  NE2 HIS A 539     2778   3307   3113    829   -964   -733
ATOM   1424  CD2 HIS A 539       4.624   6.124   4.601  1.00 21.67           C  
ANISOU 1424  CD2 HIS A 539     2774   2861   2597    370   -775   -624
ATOM   1425  H   HIS A 539       8.707   5.601   7.455  1.00  0.00           H  
ATOM   1426  HA  HIS A 539       7.447   4.288   5.289  1.00  0.00           H  
ATOM   1427  HB3 HIS A 539       7.310   7.147   6.327  1.00  0.00           H  
ATOM   1428  HB2 HIS A 539       6.273   5.829   6.777  1.00  0.00           H  
ATOM   1429  HE1 HIS A 539       5.053   8.289   2.253  1.00  0.00           H  
ATOM   1430  HD2 HIS A 539       4.035   5.376   5.113  1.00  0.00           H  
ATOM   1431  HE2 HIS A 539       3.270   6.662   3.025  1.00  0.00           H  
ATOM   1432  N   HIS A 540       9.704   6.557   4.436  1.00 15.00           N  
ANISOU 1432  N   HIS A 540     2295   2039   1364   -140   -265   -140
ATOM   1433  CA  HIS A 540      10.576   6.987   3.345  1.00 17.46           C  
ANISOU 1433  CA  HIS A 540     2329   2200   2104    132    207    -54
ATOM   1434  C   HIS A 540      11.446   5.873   2.759  1.00 17.55           C  
ANISOU 1434  C   HIS A 540     2044   2591   2031    266    202     33
ATOM   1435  O   HIS A 540      11.618   5.846   1.544  1.00 19.15           O  
ANISOU 1435  O   HIS A 540     2333   2966   1975      0   -214      0
ATOM   1436  CB  HIS A 540      11.445   8.171   3.782  1.00 17.50           C  
ANISOU 1436  CB  HIS A 540     2580   2613   1454     21    -29   -289
ATOM   1437  CG  HIS A 540      10.720   9.483   3.746  1.00 15.61           C  
ANISOU 1437  CG  HIS A 540     1931   2487   1512     92   -111    178
ATOM   1438  ND1 HIS A 540      10.229  10.022   2.570  1.00 18.49           N  
ANISOU 1438  ND1 HIS A 540     2845   2173   2008    646   -569     80
ATOM   1439  CE1 HIS A 540       9.652  11.183   2.872  1.00 19.21           C  
ANISOU 1439  CE1 HIS A 540     3201   2155   1941    671    -50    256
ATOM   1440  NE2 HIS A 540       9.720  11.458   4.165  1.00 19.11           N  
ANISOU 1440  NE2 HIS A 540     3197   2135   1929    485   -260   -260
ATOM   1441  CD2 HIS A 540      10.394  10.379   4.733  1.00 16.87           C  
ANISOU 1441  CD2 HIS A 540     2278   2325   1803    -69    149    302
ATOM   1442  H   HIS A 540       9.886   6.949   5.351  1.00  0.00           H  
ATOM   1443  HA  HIS A 540       9.941   7.324   2.527  1.00  0.00           H  
ATOM   1444  HB3 HIS A 540      12.296   8.272   3.110  1.00  0.00           H  
ATOM   1445  HB2 HIS A 540      11.857   8.009   4.779  1.00  0.00           H  
ATOM   1446  HD1 HIS A 540      10.285   9.607   1.644  1.00  0.00           H  
ATOM   1447  HE1 HIS A 540       9.179  11.827   2.146  1.00  0.00           H  
ATOM   1448  HD2 HIS A 540      10.592  10.336   5.793  1.00  0.00           H  
ATOM   1449  N   LEU A 541      11.974   4.982   3.610  1.00 15.90           N  
ANISOU 1449  N   LEU A 541     1889   2413   1739     34      3    -13
ATOM   1450  CA  LEU A 541      12.862   3.906   3.179  1.00 15.85           C  
ANISOU 1450  CA  LEU A 541     1916   2658   1448    -41    160    -63
ATOM   1451  C   LEU A 541      12.116   2.695   2.605  1.00 17.91           C  
ANISOU 1451  C   LEU A 541     2221   2826   1757    109    -85   -317
ATOM   1452  O   LEU A 541      12.624   2.109   1.652  1.00 20.22           O  
ANISOU 1452  O   LEU A 541     2764   3144   1772     22    386   -380
ATOM   1453  CB  LEU A 541      13.814   3.509   4.327  1.00 16.77           C  
ANISOU 1453  CB  LEU A 541     2380   2309   1682   -194   -142    197
ATOM   1454  CG  LEU A 541      14.866   4.591   4.660  1.00 16.32           C  
ANISOU 1454  CG  LEU A 541     2208   2363   1628   -389     -2    201
ATOM   1455  CD1 LEU A 541      15.658   4.223   5.924  1.00 17.13           C  
ANISOU 1455  CD1 LEU A 541     2323   2239   1947    257     97    259
ATOM   1456  CD2 LEU A 541      15.809   4.913   3.485  1.00 17.42           C  
ANISOU 1456  CD2 LEU A 541     2310   2697   1611   -370    163   -104
ATOM   1457  H   LEU A 541      11.808   5.064   4.604  1.00  0.00           H  
ATOM   1458  HA  LEU A 541      13.479   4.280   2.369  1.00  0.00           H  
ATOM   1459  HB3 LEU A 541      14.341   2.589   4.068  1.00  0.00           H  
ATOM   1460  HB2 LEU A 541      13.222   3.275   5.213  1.00  0.00           H  
ATOM   1461  HG  LEU A 541      14.323   5.505   4.885  1.00  0.00           H  
ATOM   1462 HD11 LEU A 541      16.022   5.113   6.432  1.00  0.00           H  
ATOM   1463 HD12 LEU A 541      15.059   3.653   6.635  1.00  0.00           H  
ATOM   1464 HD13 LEU A 541      16.531   3.628   5.675  1.00  0.00           H  
ATOM   1465 HD21 LEU A 541      16.850   4.981   3.797  1.00  0.00           H  
ATOM   1466 HD22 LEU A 541      15.759   4.153   2.705  1.00  0.00           H  
ATOM   1467 HD23 LEU A 541      15.550   5.869   3.028  1.00  0.00           H  
ATOM   1468  N   HIS A 542      10.958   2.328   3.182  1.00 18.06           N  
ANISOU 1468  N   HIS A 542     2014   2336   2512    -87   -283   -693
ATOM   1469  CA  HIS A 542      10.332   1.020   2.950  1.00 15.68           C  
ANISOU 1469  CA  HIS A 542     1791   1981   2183     82    -74    -65
ATOM   1470  C   HIS A 542       8.917   1.086   2.362  1.00 16.76           C  
ANISOU 1470  C   HIS A 542     2085   2722   1558    326   -404   -726
ATOM   1471  O   HIS A 542       8.525   0.115   1.716  1.00 21.47           O  
ANISOU 1471  O   HIS A 542     3231   2483   2442    -71   -245   -569
ATOM   1472  CB  HIS A 542      10.355   0.199   4.258  1.00 14.58           C  
ANISOU 1472  CB  HIS A 542     1927   1697   1917     92   -159   -229
ATOM   1473  CG  HIS A 542      11.708   0.152   4.923  1.00 15.03           C  
ANISOU 1473  CG  HIS A 542     1634   2043   2033   -294    -83    -92
ATOM   1474  ND1 HIS A 542      12.856  -0.305   4.263  1.00 18.12           N  
ANISOU 1474  ND1 HIS A 542     2051   2537   2295    232   -266   -392
ATOM   1475  CE1 HIS A 542      13.845  -0.113   5.123  1.00 14.91           C  
ANISOU 1475  CE1 HIS A 542     1672   1946   2045    -31    133   -709
ATOM   1476  NE2 HIS A 542      13.429   0.409   6.273  1.00 15.31           N  
ANISOU 1476  NE2 HIS A 542     2178   1923   1713    296    329   -133
ATOM   1477  CD2 HIS A 542      12.062   0.582   6.182  1.00 15.84           C  
ANISOU 1477  CD2 HIS A 542     2411   1874   1731    306    -20     42
ATOM   1478  H   HIS A 542      10.597   2.861   3.963  1.00  0.00           H  
ATOM   1479  HA  HIS A 542      10.920   0.457   2.223  1.00  0.00           H  
ATOM   1480  HB3 HIS A 542      10.036  -0.826   4.065  1.00  0.00           H  
ATOM   1481  HB2 HIS A 542       9.641   0.610   4.973  1.00  0.00           H  
ATOM   1482  HE1 HIS A 542      14.878  -0.342   4.912  1.00  0.00           H  
ATOM   1483  HD2 HIS A 542      11.477   1.005   6.982  1.00  0.00           H  
ATOM   1484  HE2 HIS A 542      14.001   0.616   7.085  1.00  0.00           H  
ATOM   1485  N   ALA A 543       8.165   2.179   2.575  1.00 17.53           N  
ANISOU 1485  N   ALA A 543     2644   2466   1549    399   -569   -198
ATOM   1486  CA  ALA A 543       6.805   2.318   2.044  1.00 16.35           C  
ANISOU 1486  CA  ALA A 543     2077   2049   2086     99   -177   -434
ATOM   1487  C   ALA A 543       6.819   3.047   0.695  1.00 15.84           C  
ANISOU 1487  C   ALA A 543     2094   1956   1968    305    -26   -468
ATOM   1488  O   ALA A 543       6.558   2.418  -0.329  1.00 19.59           O  
ANISOU 1488  O   ALA A 543     2648   2869   1925     11   -178   -658
ATOM   1489  CB  ALA A 543       5.888   2.994   3.075  1.00 15.25           C  
ANISOU 1489  CB  ALA A 543     1824   2241   1727   -205   -142    -35
ATOM   1490  H   ALA A 543       8.535   2.961   3.097  1.00  0.00           H  
ATOM   1491  HA  ALA A 543       6.375   1.331   1.866  1.00  0.00           H  
ATOM   1492  HB1 ALA A 543       4.851   2.985   2.739  1.00  0.00           H  
ATOM   1493  HB2 ALA A 543       5.925   2.463   4.026  1.00  0.00           H  
ATOM   1494  HB3 ALA A 543       6.155   4.030   3.265  1.00  0.00           H  
ATOM   1495  N   SER A 544       7.134   4.351   0.719  1.00 17.92           N  
ANISOU 1495  N   SER A 544     2573   2038   2196     88   -224   -520
ATOM   1496  CA  SER A 544       7.231   5.202  -0.467  1.00 19.69           C  
ANISOU 1496  CA  SER A 544     2728   2925   1827    -99    197   -147
ATOM   1497  C   SER A 544       8.516   4.977  -1.287  1.00 18.93           C  
ANISOU 1497  C   SER A 544     2813   2650   1728    187   -145     50
ATOM   1498  O   SER A 544       8.479   5.207  -2.495  1.00 21.95           O  
ANISOU 1498  O   SER A 544     3816   3132   1391    -28   -355   -261
ATOM   1499  CB  SER A 544       7.035   6.674  -0.052  1.00 21.54           C  
ANISOU 1499  CB  SER A 544     2961   2836   2385    -37   -254     16
ATOM   1500  OG  SER A 544       8.085   7.152   0.762  1.00 24.35           O  
ANISOU 1500  OG  SER A 544     3325   3333   2592    -27   -564    579
ATOM   1501  H   SER A 544       7.363   4.787   1.603  1.00  0.00           H  
ATOM   1502  HA  SER A 544       6.394   4.946  -1.121  1.00  0.00           H  
ATOM   1503  HB3 SER A 544       6.089   6.799   0.476  1.00  0.00           H  
ATOM   1504  HB2 SER A 544       6.980   7.309  -0.938  1.00  0.00           H  
ATOM   1505  HG  SER A 544       7.977   6.796   1.649  1.00  0.00           H  
ATOM   1506  N   GLU A 545       9.607   4.532  -0.632  1.00 19.58           N  
ANISOU 1506  N   GLU A 545     2426   2719   2292   -149   -196    500
ATOM   1507  CA  GLU A 545      10.934   4.281  -1.215  1.00 20.55           C  
ANISOU 1507  CA  GLU A 545     2246   3512   2048     95   -550    228
ATOM   1508  C   GLU A 545      11.509   5.524  -1.932  1.00 21.79           C  
ANISOU 1508  C   GLU A 545     3062   3244   1972      4    245   -407
ATOM   1509  O   GLU A 545      11.937   5.442  -3.084  1.00 25.45           O  
ANISOU 1509  O   GLU A 545     4112   4185   1370    -82   -246   -695
ATOM   1510  CB  GLU A 545      10.938   3.009  -2.095  1.00 25.97           C  
ANISOU 1510  CB  GLU A 545     2976   2974   3916   -227    -30   -297
ATOM   1511  CG  GLU A 545      10.445   1.742  -1.354  1.00 23.37           C  
ANISOU 1511  CG  GLU A 545     3373   3189   2316    408      1   -193
ATOM   1512  CD  GLU A 545      10.568   0.428  -2.145  1.00 30.77           C  
ANISOU 1512  CD  GLU A 545     4639   3872   3179   -499  -1246  -1028
ATOM   1513  OE1 GLU A 545      11.212   0.414  -3.219  1.00 46.41           O  
ANISOU 1513  OE1 GLU A 545     8378   5097   4158    473    585    424
ATOM   1514  OE2 GLU A 545      10.000  -0.573  -1.655  1.00 49.70           O1-
ANISOU 1514  OE2 GLU A 545     6039   3982   8861  -1453  -1312  -2402
ATOM   1515  H   GLU A 545       9.537   4.366   0.362  1.00  0.00           H  
ATOM   1516  HA  GLU A 545      11.601   4.082  -0.377  1.00  0.00           H  
ATOM   1517  HB3 GLU A 545      11.956   2.845  -2.452  1.00  0.00           H  
ATOM   1518  HB2 GLU A 545      10.325   3.169  -2.983  1.00  0.00           H  
ATOM   1519  HG3 GLU A 545       9.400   1.870  -1.067  1.00  0.00           H  
ATOM   1520  HG2 GLU A 545      11.004   1.624  -0.426  1.00  0.00           H  
ATOM   1521  N   THR A 546      11.466   6.662  -1.219  1.00 20.80           N  
ANISOU 1521  N   THR A 546     3112   3127   1661     92   -337   -235
ATOM   1522  CA  THR A 546      11.898   7.991  -1.648  1.00 20.90           C  
ANISOU 1522  CA  THR A 546     3145   3079   1716     72     79    -17
ATOM   1523  C   THR A 546      13.370   8.018  -2.086  1.00 22.10           C  
ANISOU 1523  C   THR A 546     3592   3225   1577   -306     50   -384
ATOM   1524  O   THR A 546      14.235   7.573  -1.332  1.00 24.44           O  
ANISOU 1524  O   THR A 546     3048   3519   2717    -72    509   -247
ATOM   1525  CB  THR A 546      11.739   9.009  -0.490  1.00 22.40           C  
ANISOU 1525  CB  THR A 546     3571   3449   1489   -376    388    -96
ATOM   1526  OG1 THR A 546      10.402   8.972  -0.047  1.00 22.56           O  
ANISOU 1526  OG1 THR A 546     2884   3768   1916    341     45    268
ATOM   1527  CG2 THR A 546      12.076  10.470  -0.842  1.00 26.14           C  
ANISOU 1527  CG2 THR A 546     4328   3800   1804   -843     80    -39
ATOM   1528  H   THR A 546      11.092   6.622  -0.280  1.00  0.00           H  
ATOM   1529  HA  THR A 546      11.264   8.293  -2.484  1.00  0.00           H  
ATOM   1530  HB  THR A 546      12.357   8.704   0.357  1.00  0.00           H  
ATOM   1531  HG1 THR A 546       9.824   9.303  -0.745  1.00  0.00           H  
ATOM   1532 HG21 THR A 546      11.854  11.133  -0.004  1.00  0.00           H  
ATOM   1533 HG22 THR A 546      13.132  10.599  -1.078  1.00  0.00           H  
ATOM   1534 HG23 THR A 546      11.497  10.815  -1.699  1.00  0.00           H  
ATOM   1535  N   LYS A 547      13.615   8.531  -3.300  1.00 27.52           N  
ANISOU 1535  N   LYS A 547     4167   5024   1263  -1067   -337   -109
ATOM   1536  CA  LYS A 547      14.933   8.593  -3.927  1.00 29.10           C  
ANISOU 1536  CA  LYS A 547     4346   4557   2152  -1230    277     11
ATOM   1537  C   LYS A 547      15.808   9.685  -3.287  1.00 29.96           C  
ANISOU 1537  C   LYS A 547     4714   4733   1935   -992   -545    -34
ATOM   1538  O   LYS A 547      15.854  10.809  -3.788  1.00 44.46           O  
ANISOU 1538  O   LYS A 547     7052   5059   4779  -3300  -2789    497
ATOM   1539  CB  LYS A 547      14.757   8.797  -5.446  1.00  0.00           C  
ATOM   1540  CG  LYS A 547      14.079   7.608  -6.149  1.00  0.00           C  
ATOM   1541  CD  LYS A 547      13.940   7.828  -7.662  1.00  0.00           C  
ATOM   1542  CE  LYS A 547      13.242   6.654  -8.366  1.00  0.00           C  
ATOM   1543  NZ  LYS A 547      13.110   6.885  -9.816  1.00  0.00           N1+
ATOM   1544  H   LYS A 547      12.847   8.879  -3.855  1.00  0.00           H  
ATOM   1545  HA  LYS A 547      15.434   7.634  -3.776  1.00  0.00           H  
ATOM   1546  HB2 LYS A 547      14.187   9.708  -5.637  1.00  0.00           H  
ATOM   1547  HB3 LYS A 547      15.737   8.950  -5.902  1.00  0.00           H  
ATOM   1548  HG2 LYS A 547      14.654   6.700  -5.963  1.00  0.00           H  
ATOM   1549  HG3 LYS A 547      13.091   7.436  -5.720  1.00  0.00           H  
ATOM   1550  HD2 LYS A 547      13.384   8.751  -7.838  1.00  0.00           H  
ATOM   1551  HD3 LYS A 547      14.931   7.981  -8.093  1.00  0.00           H  
ATOM   1552  HE2 LYS A 547      13.804   5.733  -8.209  1.00  0.00           H  
ATOM   1553  HE3 LYS A 547      12.247   6.499  -7.946  1.00  0.00           H  
ATOM   1554  HZ1 LYS A 547      14.026   6.999 -10.226  1.00  0.00           H  
ATOM   1555  HZ2 LYS A 547      12.647   6.094 -10.242  1.00  0.00           H  
ATOM   1556  HZ3 LYS A 547      12.563   7.719  -9.978  1.00  0.00           H  
ATOM   1557  N   PHE A 548      16.482   9.324  -2.184  1.00 28.24           N  
ANISOU 1557  N   PHE A 548     3734   4396   2597   -356    195   1239
ATOM   1558  CA  PHE A 548      17.469  10.164  -1.517  1.00 26.91           C  
ANISOU 1558  CA  PHE A 548     3640   4712   1872   -428    757    824
ATOM   1559  C   PHE A 548      18.845   9.946  -2.155  1.00 21.75           C  
ANISOU 1559  C   PHE A 548     2948   3585   1729    344   -167    162
ATOM   1560  O   PHE A 548      19.251   8.797  -2.346  1.00 24.69           O  
ANISOU 1560  O   PHE A 548     3356   3437   2587    454    674    375
ATOM   1561  CB  PHE A 548      17.537   9.807  -0.017  1.00 25.30           C  
ANISOU 1561  CB  PHE A 548     2707   4579   2326    176    126   1294
ATOM   1562  CG  PHE A 548      16.280  10.058   0.801  1.00 24.93           C  
ANISOU 1562  CG  PHE A 548     2721   3803   2948   -719    398    522
ATOM   1563  CD1 PHE A 548      15.588  11.287   0.718  1.00 31.99           C  
ANISOU 1563  CD1 PHE A 548     4471   4296   3387   -191   1082     71
ATOM   1564  CE1 PHE A 548      14.500  11.529   1.547  1.00 29.50           C  
ANISOU 1564  CE1 PHE A 548     4255   3815   3137  -1113    740   -856
ATOM   1565  CZ  PHE A 548      14.104  10.577   2.476  1.00 25.70           C  
ANISOU 1565  CZ  PHE A 548     3541   3672   2550   -670     86   -510
ATOM   1566  CD2 PHE A 548      15.882   9.116   1.773  1.00 23.75           C  
ANISOU 1566  CD2 PHE A 548     2748   4298   1974   -202    -42    815
ATOM   1567  CE2 PHE A 548      14.799   9.381   2.597  1.00 25.01           C  
ANISOU 1567  CE2 PHE A 548     2494   4180   2826  -1272     51    206
ATOM   1568  H   PHE A 548      16.360   8.394  -1.806  1.00  0.00           H  
ATOM   1569  HA  PHE A 548      17.195  11.213  -1.622  1.00  0.00           H  
ATOM   1570  HB3 PHE A 548      18.346  10.361   0.462  1.00  0.00           H  
ATOM   1571  HB2 PHE A 548      17.802   8.753   0.078  1.00  0.00           H  
ATOM   1572  HD1 PHE A 548      15.894  12.045   0.015  1.00  0.00           H  
ATOM   1573  HE1 PHE A 548      13.963  12.463   1.474  1.00  0.00           H  
ATOM   1574  HZ  PHE A 548      13.256  10.774   3.116  1.00  0.00           H  
ATOM   1575  HD2 PHE A 548      16.415   8.183   1.882  1.00  0.00           H  
ATOM   1576  HE2 PHE A 548      14.506   8.654   3.340  1.00  0.00           H  
ATOM   1577  N   GLU A 549      19.564  11.052  -2.402  1.00 25.65           N  
ANISOU 1577  N   GLU A 549     3491   4522   1731   -100    306    617
ATOM   1578  CA  GLU A 549      20.999  11.029  -2.688  1.00 29.28           C  
ANISOU 1578  CA  GLU A 549     3034   5450   2639    383   -409   1054
ATOM   1579  C   GLU A 549      21.806  10.572  -1.462  1.00 22.96           C  
ANISOU 1579  C   GLU A 549     2641   4056   2023    105   -119    450
ATOM   1580  O   GLU A 549      21.329  10.694  -0.334  1.00 22.88           O  
ANISOU 1580  O   GLU A 549     3175   3824   1692   -669    138    409
ATOM   1581  CB  GLU A 549      21.472  12.421  -3.150  1.00 30.73           C  
ANISOU 1581  CB  GLU A 549     3000   6037   2638    496    -69   2305
ATOM   1582  CG  GLU A 549      21.057  12.767  -4.597  1.00 43.41           C  
ANISOU 1582  CG  GLU A 549     3822   9282   3388    329  -1140   2766
ATOM   1583  CD  GLU A 549      21.844  13.925  -5.239  1.00 63.63           C  
ANISOU 1583  CD  GLU A 549     8514  10867   4793   -266    493   4301
ATOM   1584  OE1 GLU A 549      22.512  14.690  -4.505  1.00 88.74           O  
ANISOU 1584  OE1 GLU A 549    13151   9658  10906  -2286   -817   5794
ATOM   1585  OE2 GLU A 549      21.772  14.018  -6.484  1.00 90.00           O1-
ANISOU 1585  OE2 GLU A 549    14457  14743   4994   3190  -2572     27
ATOM   1586  H   GLU A 549      19.158  11.962  -2.228  1.00  0.00           H  
ATOM   1587  HA  GLU A 549      21.182  10.308  -3.486  1.00  0.00           H  
ATOM   1588  HB3 GLU A 549      22.555  12.474  -3.058  1.00  0.00           H  
ATOM   1589  HB2 GLU A 549      21.083  13.184  -2.474  1.00  0.00           H  
ATOM   1590  HG3 GLU A 549      19.993  13.007  -4.629  1.00  0.00           H  
ATOM   1591  HG2 GLU A 549      21.189  11.885  -5.227  1.00  0.00           H  
ATOM   1592  N   MET A 550      23.029  10.076  -1.706  1.00 24.65           N  
ANISOU 1592  N   MET A 550     3052   4056   2255    396    131    515
ATOM   1593  CA  MET A 550      23.956   9.622  -0.667  1.00 23.67           C  
ANISOU 1593  CA  MET A 550     2582   3711   2698     19    -60    381
ATOM   1594  C   MET A 550      24.326  10.720   0.352  1.00 21.85           C  
ANISOU 1594  C   MET A 550     2915   3492   1895     97    287    507
ATOM   1595  O   MET A 550      24.440  10.410   1.536  1.00 21.50           O  
ANISOU 1595  O   MET A 550     2399   4006   1761    450    136    197
ATOM   1596  CB  MET A 550      25.184   8.972  -1.340  1.00 28.82           C  
ANISOU 1596  CB  MET A 550     3238   5167   2546    129    661    -66
ATOM   1597  CG  MET A 550      26.226   8.363  -0.384  1.00 26.48           C  
ANISOU 1597  CG  MET A 550     2315   4964   2782   -652    358   -441
ATOM   1598  SD  MET A 550      25.595   7.188   0.851  1.00 30.54           S  
ANISOU 1598  SD  MET A 550     4106   4756   2740    192    467     48
ATOM   1599  CE  MET A 550      24.967   5.868  -0.218  1.00 35.80           C  
ANISOU 1599  CE  MET A 550     5013   5257   3330   1698    271   -959
ATOM   1600  H   MET A 550      23.360  10.008  -2.660  1.00  0.00           H  
ATOM   1601  HA  MET A 550      23.427   8.843  -0.116  1.00  0.00           H  
ATOM   1602  HB3 MET A 550      25.683   9.716  -1.963  1.00  0.00           H  
ATOM   1603  HB2 MET A 550      24.847   8.198  -2.029  1.00  0.00           H  
ATOM   1604  HG3 MET A 550      26.744   9.162   0.145  1.00  0.00           H  
ATOM   1605  HG2 MET A 550      26.992   7.853  -0.968  1.00  0.00           H  
ATOM   1606  HE1 MET A 550      24.615   5.032   0.387  1.00  0.00           H  
ATOM   1607  HE2 MET A 550      24.137   6.223  -0.828  1.00  0.00           H  
ATOM   1608  HE3 MET A 550      25.755   5.507  -0.875  1.00  0.00           H  
ATOM   1609  N   LYS A 551      24.422  11.981  -0.108  1.00 22.34           N  
ANISOU 1609  N   LYS A 551     2736   3454   2296   -361    769    325
ATOM   1610  CA  LYS A 551      24.563  13.179   0.725  1.00 24.53           C  
ANISOU 1610  CA  LYS A 551     3223   3439   2654   -215    777    293
ATOM   1611  C   LYS A 551      23.412  13.339   1.739  1.00 21.41           C  
ANISOU 1611  C   LYS A 551     3042   2985   2108  -1065    413    545
ATOM   1612  O   LYS A 551      23.684  13.612   2.906  1.00 23.51           O  
ANISOU 1612  O   LYS A 551     3264   3603   2063   -172    584    152
ATOM   1613  CB  LYS A 551      24.688  14.417  -0.195  1.00 30.48           C  
ANISOU 1613  CB  LYS A 551     3455   4080   4046   -544   1395   1174
ATOM   1614  CG  LYS A 551      24.916  15.753   0.540  1.00 44.10           C  
ANISOU 1614  CG  LYS A 551     6629   5008   5118  -1185    415   1390
ATOM   1615  CD  LYS A 551      24.856  16.968  -0.396  1.00 53.86           C  
ANISOU 1615  CD  LYS A 551     7369   5459   7636    -49    324   2407
ATOM   1616  CE  LYS A 551      25.041  18.292   0.365  1.00 57.90           C  
ANISOU 1616  CE  LYS A 551     9145   5700   7153  -2215   1517   2987
ATOM   1617  NZ  LYS A 551      24.868  19.459  -0.517  1.00 71.72           N1+
ANISOU 1617  NZ  LYS A 551    11066   6644   9541   -318   1336   2515
ATOM   1618  H   LYS A 551      24.339  12.145  -1.103  1.00  0.00           H  
ATOM   1619  HA  LYS A 551      25.494  13.076   1.286  1.00  0.00           H  
ATOM   1620  HB3 LYS A 551      23.789  14.494  -0.810  1.00  0.00           H  
ATOM   1621  HB2 LYS A 551      25.513  14.264  -0.892  1.00  0.00           H  
ATOM   1622  HG3 LYS A 551      25.884  15.724   1.040  1.00  0.00           H  
ATOM   1623  HG2 LYS A 551      24.172  15.894   1.324  1.00  0.00           H  
ATOM   1624  HD3 LYS A 551      23.897  16.967  -0.918  1.00  0.00           H  
ATOM   1625  HD2 LYS A 551      25.625  16.868  -1.164  1.00  0.00           H  
ATOM   1626  HE3 LYS A 551      26.033  18.333   0.818  1.00  0.00           H  
ATOM   1627  HE2 LYS A 551      24.315  18.366   1.175  1.00  0.00           H  
ATOM   1628  HZ1 LYS A 551      23.939  19.447  -0.914  1.00  0.00           H  
ATOM   1629  HZ2 LYS A 551      24.996  20.308   0.015  1.00  0.00           H  
ATOM   1630  HZ3 LYS A 551      25.549  19.423  -1.262  1.00  0.00           H  
ATOM   1631  N   LYS A 552      22.164  13.147   1.277  1.00 19.22           N  
ANISOU 1631  N   LYS A 552     2727   2551   2024    -63    373    169
ATOM   1632  CA  LYS A 552      20.940  13.219   2.077  1.00 20.83           C  
ANISOU 1632  CA  LYS A 552     2444   2868   2601    285    186    298
ATOM   1633  C   LYS A 552      20.808  12.053   3.079  1.00 17.07           C  
ANISOU 1633  C   LYS A 552     2197   2254   2032   -195     16   -258
ATOM   1634  O   LYS A 552      20.388  12.298   4.207  1.00 19.48           O  
ANISOU 1634  O   LYS A 552     2839   2026   2534    -89    758    -46
ATOM   1635  CB  LYS A 552      19.729  13.350   1.120  1.00 21.40           C  
ANISOU 1635  CB  LYS A 552     2335   3033   2762    132    -46    583
ATOM   1636  CG  LYS A 552      18.323  13.394   1.752  1.00 29.23           C  
ANISOU 1636  CG  LYS A 552     3780   3860   3465    444   1180   1412
ATOM   1637  CD  LYS A 552      18.099  14.575   2.714  1.00 36.15           C  
ANISOU 1637  CD  LYS A 552     5129   2780   5824   -729   2107     54
ATOM   1638  CE  LYS A 552      16.632  14.767   3.146  1.00 37.01           C  
ANISOU 1638  CE  LYS A 552     4935   3327   5797  -1125   1803     69
ATOM   1639  NZ  LYS A 552      15.806  15.406   2.106  1.00 47.17           N1+
ANISOU 1639  NZ  LYS A 552     6050   4764   7106    453   2256    277
ATOM   1640  H   LYS A 552      22.037  12.895   0.307  1.00  0.00           H  
ATOM   1641  HA  LYS A 552      20.997  14.140   2.660  1.00  0.00           H  
ATOM   1642  HB3 LYS A 552      19.739  12.522   0.412  1.00  0.00           H  
ATOM   1643  HB2 LYS A 552      19.860  14.248   0.516  1.00  0.00           H  
ATOM   1644  HG3 LYS A 552      18.113  12.455   2.266  1.00  0.00           H  
ATOM   1645  HG2 LYS A 552      17.598  13.449   0.940  1.00  0.00           H  
ATOM   1646  HD3 LYS A 552      18.492  15.495   2.278  1.00  0.00           H  
ATOM   1647  HD2 LYS A 552      18.691  14.407   3.615  1.00  0.00           H  
ATOM   1648  HE3 LYS A 552      16.604  15.415   4.022  1.00  0.00           H  
ATOM   1649  HE2 LYS A 552      16.182  13.819   3.443  1.00  0.00           H  
ATOM   1650  HZ1 LYS A 552      14.872  15.549   2.468  1.00  0.00           H  
ATOM   1651  HZ2 LYS A 552      16.200  16.304   1.859  1.00  0.00           H  
ATOM   1652  HZ3 LYS A 552      15.766  14.815   1.288  1.00  0.00           H  
ATOM   1653  N   LEU A 553      21.211  10.832   2.681  1.00 15.42           N  
ANISOU 1653  N   LEU A 553     2441   2086   1331   -485    526    -88
ATOM   1654  CA  LEU A 553      21.244   9.643   3.544  1.00 17.73           C  
ANISOU 1654  CA  LEU A 553     2230   2585   1920    238    368    141
ATOM   1655  C   LEU A 553      22.254   9.783   4.699  1.00 17.89           C  
ANISOU 1655  C   LEU A 553     1639   2989   2170   -190    448    123
ATOM   1656  O   LEU A 553      21.917   9.450   5.835  1.00 19.58           O  
ANISOU 1656  O   LEU A 553     2857   2787   1793   -125     83    117
ATOM   1657  CB  LEU A 553      21.575   8.387   2.709  1.00 20.89           C  
ANISOU 1657  CB  LEU A 553     2941   3131   1864    489    542   -420
ATOM   1658  CG  LEU A 553      20.517   7.974   1.665  1.00 19.92           C  
ANISOU 1658  CG  LEU A 553     3001   2858   1707    150    442     24
ATOM   1659  CD1 LEU A 553      21.091   6.937   0.677  1.00 24.58           C  
ANISOU 1659  CD1 LEU A 553     4499   2923   1915    364    796     -8
ATOM   1660  CD2 LEU A 553      19.231   7.455   2.328  1.00 21.36           C  
ANISOU 1660  CD2 LEU A 553     2696   4159   1261   -306   -527    214
ATOM   1661  H   LEU A 553      21.536  10.704   1.732  1.00  0.00           H  
ATOM   1662  HA  LEU A 553      20.255   9.522   3.990  1.00  0.00           H  
ATOM   1663  HB3 LEU A 553      21.723   7.543   3.381  1.00  0.00           H  
ATOM   1664  HB2 LEU A 553      22.532   8.545   2.209  1.00  0.00           H  
ATOM   1665  HG  LEU A 553      20.245   8.849   1.079  1.00  0.00           H  
ATOM   1666 HD11 LEU A 553      20.481   6.034   0.626  1.00  0.00           H  
ATOM   1667 HD12 LEU A 553      21.139   7.350  -0.331  1.00  0.00           H  
ATOM   1668 HD13 LEU A 553      22.099   6.621   0.948  1.00  0.00           H  
ATOM   1669 HD21 LEU A 553      18.576   6.970   1.605  1.00  0.00           H  
ATOM   1670 HD22 LEU A 553      19.451   6.722   3.102  1.00  0.00           H  
ATOM   1671 HD23 LEU A 553      18.664   8.268   2.782  1.00  0.00           H  
ATOM   1672  N   ILE A 554      23.453  10.308   4.387  1.00 16.07           N  
ANISOU 1672  N   ILE A 554     1543   2948   1613    -11    320    345
ATOM   1673  CA  ILE A 554      24.507  10.634   5.352  1.00 16.37           C  
ANISOU 1673  CA  ILE A 554     1576   2860   1781   -129    378    -57
ATOM   1674  C   ILE A 554      24.109  11.800   6.279  1.00 17.59           C  
ANISOU 1674  C   ILE A 554     1586   3056   2039   -113    297   -217
ATOM   1675  O   ILE A 554      24.481  11.773   7.450  1.00 19.45           O  
ANISOU 1675  O   ILE A 554     1764   3629   1994     16    240   -311
ATOM   1676  CB  ILE A 554      25.860  10.950   4.635  1.00 19.44           C  
ANISOU 1676  CB  ILE A 554     1729   3742   1916   -414    377    112
ATOM   1677  CG1 ILE A 554      26.431   9.668   3.984  1.00 24.45           C  
ANISOU 1677  CG1 ILE A 554     2820   4600   1870    266     44   -197
ATOM   1678  CG2 ILE A 554      26.949  11.617   5.513  1.00 21.71           C  
ANISOU 1678  CG2 ILE A 554     2129   4155   1961    112     54   -265
ATOM   1679  CD1 ILE A 554      27.505   9.932   2.919  1.00 28.81           C  
ANISOU 1679  CD1 ILE A 554     3720   3803   3423   -124    824    -88
ATOM   1680  H   ILE A 554      23.656  10.535   3.422  1.00  0.00           H  
ATOM   1681  HA  ILE A 554      24.656   9.755   5.983  1.00  0.00           H  
ATOM   1682  HB  ILE A 554      25.636  11.650   3.827  1.00  0.00           H  
ATOM   1683 HG13 ILE A 554      25.635   9.091   3.514  1.00  0.00           H  
ATOM   1684 HG12 ILE A 554      26.835   9.013   4.756  1.00  0.00           H  
ATOM   1685 HG21 ILE A 554      27.871  11.778   4.956  1.00  0.00           H  
ATOM   1686 HG22 ILE A 554      26.649  12.599   5.876  1.00  0.00           H  
ATOM   1687 HG23 ILE A 554      27.193  10.997   6.376  1.00  0.00           H  
ATOM   1688 HD11 ILE A 554      27.672   9.039   2.318  1.00  0.00           H  
ATOM   1689 HD12 ILE A 554      27.212  10.737   2.244  1.00  0.00           H  
ATOM   1690 HD13 ILE A 554      28.460  10.200   3.368  1.00  0.00           H  
ATOM   1691  N   ASP A 555      23.339  12.773   5.760  1.00 16.94           N  
ANISOU 1691  N   ASP A 555     2228   2310   1897   -186    739    -26
ATOM   1692  CA  ASP A 555      22.816  13.911   6.518  1.00 18.20           C  
ANISOU 1692  CA  ASP A 555     2501   1864   2549   -518    717   -193
ATOM   1693  C   ASP A 555      21.735  13.492   7.534  1.00 17.18           C  
ANISOU 1693  C   ASP A 555     2946   2144   1435   -167    592    -60
ATOM   1694  O   ASP A 555      21.744  14.003   8.652  1.00 16.53           O  
ANISOU 1694  O   ASP A 555     2194   2897   1190   -396    145    -20
ATOM   1695  CB  ASP A 555      22.310  15.039   5.587  1.00 21.17           C  
ANISOU 1695  CB  ASP A 555     3220   2824   1997   -448    864    487
ATOM   1696  CG  ASP A 555      21.977  16.349   6.313  1.00 24.14           C  
ANISOU 1696  CG  ASP A 555     3466   2570   3136   -281    857    412
ATOM   1697  OD1 ASP A 555      22.907  16.898   6.942  1.00 28.85           O  
ANISOU 1697  OD1 ASP A 555     4803   2339   3817   -848    814   -702
ATOM   1698  OD2 ASP A 555      20.802  16.769   6.261  1.00 28.17           O1-
ANISOU 1698  OD2 ASP A 555     4315   3391   2997   1080    504    682
ATOM   1699  H   ASP A 555      23.082  12.734   4.783  1.00  0.00           H  
ATOM   1700  HA  ASP A 555      23.656  14.301   7.095  1.00  0.00           H  
ATOM   1701  HB3 ASP A 555      21.451  14.691   5.012  1.00  0.00           H  
ATOM   1702  HB2 ASP A 555      23.074  15.261   4.841  1.00  0.00           H  
ATOM   1703  N   ILE A 556      20.855  12.550   7.152  1.00 15.41           N  
ANISOU 1703  N   ILE A 556     2247   2491   1116     74    206    163
ATOM   1704  CA  ILE A 556      19.860  11.955   8.047  1.00 15.83           C  
ANISOU 1704  CA  ILE A 556     2251   2228   1534   -156     86    -40
ATOM   1705  C   ILE A 556      20.524  11.150   9.185  1.00 15.52           C  
ANISOU 1705  C   ILE A 556     2154   2132   1609    138    131      3
ATOM   1706  O   ILE A 556      20.101  11.294  10.331  1.00 15.05           O  
ANISOU 1706  O   ILE A 556     1961   2230   1525   -360     69   -250
ATOM   1707  CB  ILE A 556      18.836  11.063   7.283  1.00 15.44           C  
ANISOU 1707  CB  ILE A 556     2304   2393   1169    -80     67   -265
ATOM   1708  CG1 ILE A 556      17.941  11.911   6.347  1.00 19.45           C  
ANISOU 1708  CG1 ILE A 556     2405   3048   1934     82   -258   -147
ATOM   1709  CG2 ILE A 556      17.939  10.196   8.193  1.00 14.49           C  
ANISOU 1709  CG2 ILE A 556     2006   2034   1465    282    -31     41
ATOM   1710  CD1 ILE A 556      17.304  11.103   5.205  1.00 18.53           C  
ANISOU 1710  CD1 ILE A 556     3301   2602   1136    -45    -12     87
ATOM   1711  H   ILE A 556      20.882  12.192   6.206  1.00  0.00           H  
ATOM   1712  HA  ILE A 556      19.306  12.775   8.510  1.00  0.00           H  
ATOM   1713  HB  ILE A 556      19.410  10.381   6.653  1.00  0.00           H  
ATOM   1714 HG13 ILE A 556      18.509  12.729   5.907  1.00  0.00           H  
ATOM   1715 HG12 ILE A 556      17.156  12.396   6.931  1.00  0.00           H  
ATOM   1716 HG21 ILE A 556      17.172   9.690   7.614  1.00  0.00           H  
ATOM   1717 HG22 ILE A 556      18.500   9.419   8.713  1.00  0.00           H  
ATOM   1718 HG23 ILE A 556      17.428  10.802   8.941  1.00  0.00           H  
ATOM   1719 HD11 ILE A 556      16.976  11.760   4.400  1.00  0.00           H  
ATOM   1720 HD12 ILE A 556      18.007  10.390   4.774  1.00  0.00           H  
ATOM   1721 HD13 ILE A 556      16.431  10.546   5.547  1.00  0.00           H  
ATOM   1722  N   ALA A 557      21.585  10.386   8.865  1.00 14.70           N  
ANISOU 1722  N   ALA A 557     1812   2217   1556   -126     15   -144
ATOM   1723  CA  ALA A 557      22.435   9.695   9.839  1.00 15.30           C  
ANISOU 1723  CA  ALA A 557     1960   2231   1622    -70     97     93
ATOM   1724  C   ALA A 557      23.153  10.651  10.810  1.00 16.37           C  
ANISOU 1724  C   ALA A 557     2509   2332   1377    -95    288     34
ATOM   1725  O   ALA A 557      23.239  10.337  11.995  1.00 15.60           O  
ANISOU 1725  O   ALA A 557     1798   2763   1363     82   -254    154
ATOM   1726  CB  ALA A 557      23.458   8.820   9.099  1.00 20.08           C  
ANISOU 1726  CB  ALA A 557     2423   2986   2221    236     76   -466
ATOM   1727  H   ALA A 557      21.866  10.311   7.896  1.00  0.00           H  
ATOM   1728  HA  ALA A 557      21.794   9.038  10.431  1.00  0.00           H  
ATOM   1729  HB1 ALA A 557      24.117   8.314   9.803  1.00  0.00           H  
ATOM   1730  HB2 ALA A 557      22.968   8.055   8.498  1.00  0.00           H  
ATOM   1731  HB3 ALA A 557      24.089   9.404   8.432  1.00  0.00           H  
ATOM   1732  N   ARG A 558      23.625  11.799  10.293  1.00 15.14           N  
ANISOU 1732  N   ARG A 558     1816   2645   1291   -421   -309    278
ATOM   1733  CA  ARG A 558      24.314  12.854  11.037  1.00 16.60           C  
ANISOU 1733  CA  ARG A 558     1831   2283   2191   -451    206     64
ATOM   1734  C   ARG A 558      23.399  13.546  12.054  1.00 15.26           C  
ANISOU 1734  C   ARG A 558     1918   2186   1694   -285     46    368
ATOM   1735  O   ARG A 558      23.784  13.666  13.213  1.00 16.77           O  
ANISOU 1735  O   ARG A 558     1882   2770   1718   -353    262   -160
ATOM   1736  CB  ARG A 558      24.911  13.862  10.035  1.00 19.14           C  
ANISOU 1736  CB  ARG A 558     2717   2665   1890   -539    134    281
ATOM   1737  CG  ARG A 558      25.905  14.877  10.621  1.00 22.78           C  
ANISOU 1737  CG  ARG A 558     3321   2777   2554   -862    191    211
ATOM   1738  CD  ARG A 558      26.487  15.744   9.493  1.00 32.94           C  
ANISOU 1738  CD  ARG A 558     4473   4048   3993  -3015   2523   -209
ATOM   1739  NE  ARG A 558      27.609  16.585   9.933  1.00 42.72           N  
ANISOU 1739  NE  ARG A 558     5478   6148   4606  -3352   1566    804
ATOM   1740  CZ  ARG A 558      28.276  17.495   9.198  1.00 52.33           C  
ANISOU 1740  CZ  ARG A 558     8315   6695   4870  -4476   1783   1627
ATOM   1741  NH1 ARG A 558      29.295  18.162   9.751  1.00 56.92           N  
ANISOU 1741  NH1 ARG A 558     7833   5013   8781  -3246   1030    314
ATOM   1742  NH2 ARG A 558      27.953  17.761   7.923  1.00 48.23           N1+
ANISOU 1742  NH2 ARG A 558     6917   6936   4471  -2774   1594   1111
ATOM   1743  H   ARG A 558      23.522  11.961   9.300  1.00  0.00           H  
ATOM   1744  HA  ARG A 558      25.133  12.384  11.585  1.00  0.00           H  
ATOM   1745  HB3 ARG A 558      24.114  14.407   9.532  1.00  0.00           H  
ATOM   1746  HB2 ARG A 558      25.424  13.313   9.249  1.00  0.00           H  
ATOM   1747  HG3 ARG A 558      26.687  14.402  11.216  1.00  0.00           H  
ATOM   1748  HG2 ARG A 558      25.347  15.521  11.301  1.00  0.00           H  
ATOM   1749  HD3 ARG A 558      25.714  16.449   9.186  1.00  0.00           H  
ATOM   1750  HD2 ARG A 558      26.746  15.149   8.617  1.00  0.00           H  
ATOM   1751  HE  ARG A 558      27.882  16.472  10.902  1.00  0.00           H  
ATOM   1752 HH12 ARG A 558      29.821  18.835   9.214  1.00  0.00           H  
ATOM   1753 HH11 ARG A 558      29.559  17.983  10.711  1.00  0.00           H  
ATOM   1754 HH22 ARG A 558      28.468  18.447   7.391  1.00  0.00           H  
ATOM   1755 HH21 ARG A 558      27.192  17.263   7.478  1.00  0.00           H  
ATOM   1756  N   GLN A 559      22.200  13.952  11.604  1.00 15.90           N  
ANISOU 1756  N   GLN A 559     1970   2402   1668   -418   -418    -57
ATOM   1757  CA  GLN A 559      21.162  14.560  12.434  1.00 14.76           C  
ANISOU 1757  CA  GLN A 559     2187   2145   1275   -399    -91     51
ATOM   1758  C   GLN A 559      20.599  13.612  13.506  1.00 14.49           C  
ANISOU 1758  C   GLN A 559     2199   1619   1685    -94     48     88
ATOM   1759  O   GLN A 559      20.352  14.059  14.625  1.00 14.65           O  
ANISOU 1759  O   GLN A 559     1614   2188   1762   -313    309   -165
ATOM   1760  CB  GLN A 559      20.018  15.068  11.547  1.00 13.74           C  
ANISOU 1760  CB  GLN A 559     2504   1240   1474   -212   -143   -159
ATOM   1761  CG  GLN A 559      20.340  16.317  10.711  1.00 15.22           C  
ANISOU 1761  CG  GLN A 559     2591   1528   1660   -485    195    -56
ATOM   1762  CD  GLN A 559      19.063  16.858  10.072  1.00 16.80           C  
ANISOU 1762  CD  GLN A 559     2705   1924   1754    -82    399    187
ATOM   1763  OE1 GLN A 559      18.132  17.228  10.783  1.00 19.14           O  
ANISOU 1763  OE1 GLN A 559     2796   2785   1690     11    650    131
ATOM   1764  NE2 GLN A 559      19.004  16.916   8.742  1.00 19.43           N  
ANISOU 1764  NE2 GLN A 559     2469   3279   1631    266   -188     82
ATOM   1765  H   GLN A 559      21.968  13.822  10.627  1.00  0.00           H  
ATOM   1766  HA  GLN A 559      21.604  15.413  12.952  1.00  0.00           H  
ATOM   1767  HB3 GLN A 559      19.187  15.312  12.203  1.00  0.00           H  
ATOM   1768  HB2 GLN A 559      19.667  14.268  10.892  1.00  0.00           H  
ATOM   1769  HG3 GLN A 559      21.096  16.111   9.954  1.00  0.00           H  
ATOM   1770  HG2 GLN A 559      20.747  17.099  11.353  1.00  0.00           H  
ATOM   1771 HE22 GLN A 559      18.165  17.249   8.283  1.00  0.00           H  
ATOM   1772 HE21 GLN A 559      19.787  16.629   8.167  1.00  0.00           H  
ATOM   1773  N   THR A 560      20.433  12.322  13.162  1.00 14.02           N  
ANISOU 1773  N   THR A 560     1689   2049   1587   -445     32    -92
ATOM   1774  CA  THR A 560      20.028  11.285  14.112  1.00 13.27           C  
ANISOU 1774  CA  THR A 560     2082   1586   1372    110     76     44
ATOM   1775  C   THR A 560      21.117  11.045  15.178  1.00 14.68           C  
ANISOU 1775  C   THR A 560     1386   2186   2005   -394    -19   -259
ATOM   1776  O   THR A 560      20.777  10.970  16.356  1.00 14.63           O  
ANISOU 1776  O   THR A 560     1927   1848   1782   -374   -124    -47
ATOM   1777  CB  THR A 560      19.685   9.939  13.419  1.00 13.42           C  
ANISOU 1777  CB  THR A 560     2169   1567   1360     58   -215    243
ATOM   1778  OG1 THR A 560      18.631  10.129  12.497  1.00 13.34           O  
ANISOU 1778  OG1 THR A 560     1720   1707   1641     68   -324     85
ATOM   1779  CG2 THR A 560      19.252   8.805  14.369  1.00 14.72           C  
ANISOU 1779  CG2 THR A 560     2443   1179   1969   -316    187     76
ATOM   1780  H   THR A 560      20.642  12.020  12.220  1.00  0.00           H  
ATOM   1781  HA  THR A 560      19.136  11.636  14.631  1.00  0.00           H  
ATOM   1782  HB  THR A 560      20.544   9.614  12.834  1.00  0.00           H  
ATOM   1783  HG1 THR A 560      18.964  10.651  11.759  1.00  0.00           H  
ATOM   1784 HG21 THR A 560      19.060   7.888  13.813  1.00  0.00           H  
ATOM   1785 HG22 THR A 560      20.014   8.568  15.110  1.00  0.00           H  
ATOM   1786 HG23 THR A 560      18.342   9.067  14.910  1.00  0.00           H  
ATOM   1787  N   ALA A 561      22.397  11.015  14.764  1.00 16.02           N  
ANISOU 1787  N   ALA A 561     1534   2481   2071   -575    179   -264
ATOM   1788  CA  ALA A 561      23.550  10.939  15.662  1.00 15.20           C  
ANISOU 1788  CA  ALA A 561     1750   2324   1700   -240    139   -478
ATOM   1789  C   ALA A 561      23.694  12.157  16.592  1.00 15.18           C  
ANISOU 1789  C   ALA A 561     2327   2064   1374    109   -241   -128
ATOM   1790  O   ALA A 561      24.113  11.957  17.729  1.00 15.23           O  
ANISOU 1790  O   ALA A 561     1935   2659   1189     66     17    343
ATOM   1791  CB  ALA A 561      24.838  10.705  14.859  1.00 18.13           C  
ANISOU 1791  CB  ALA A 561     1989   2862   2037   -558    406   -674
ATOM   1792  H   ALA A 561      22.608  11.083  13.777  1.00  0.00           H  
ATOM   1793  HA  ALA A 561      23.401  10.065  16.299  1.00  0.00           H  
ATOM   1794  HB1 ALA A 561      25.710  10.652  15.512  1.00  0.00           H  
ATOM   1795  HB2 ALA A 561      24.789   9.764  14.313  1.00  0.00           H  
ATOM   1796  HB3 ALA A 561      25.017  11.500  14.135  1.00  0.00           H  
ATOM   1797  N   ARG A 562      23.301  13.365  16.138  1.00 14.23           N  
ANISOU 1797  N   ARG A 562     1670   2184   1550   -143     -3    385
ATOM   1798  CA  ARG A 562      23.250  14.564  16.981  1.00 16.37           C  
ANISOU 1798  CA  ARG A 562     1283   2282   2654    246   -212   -164
ATOM   1799  C   ARG A 562      22.176  14.490  18.070  1.00 14.84           C  
ANISOU 1799  C   ARG A 562     2293   1458   1888    -90   -290     20
ATOM   1800  O   ARG A 562      22.456  14.885  19.201  1.00 15.99           O  
ANISOU 1800  O   ARG A 562     2194   2298   1581   -441    -74     22
ATOM   1801  CB  ARG A 562      22.982  15.848  16.177  1.00 21.96           C  
ANISOU 1801  CB  ARG A 562     2231   3319   2793    209   -341    588
ATOM   1802  CG  ARG A 562      24.144  16.338  15.322  1.00 31.35           C  
ANISOU 1802  CG  ARG A 562     4188   2347   5377   -116   -650    803
ATOM   1803  CD  ARG A 562      23.864  17.745  14.797  1.00 31.11           C  
ANISOU 1803  CD  ARG A 562     3910   1584   6325  -1032   -160   1391
ATOM   1804  NE  ARG A 562      24.868  18.163  13.810  1.00 35.29           N  
ANISOU 1804  NE  ARG A 562     4546   2389   6473  -1457    409    449
ATOM   1805  CZ  ARG A 562      24.658  18.470  12.519  1.00 41.92           C  
ANISOU 1805  CZ  ARG A 562     3134   7189   5605    389   -325   -775
ATOM   1806  NH1 ARG A 562      23.434  18.472  11.976  1.00 45.38           N  
ANISOU 1806  NH1 ARG A 562     2341   9912   4988   -499    357  -1327
ATOM   1807  NH2 ARG A 562      25.703  18.775  11.745  1.00 49.99           N1+
ANISOU 1807  NH2 ARG A 562     3136   9021   6833  -1427    372  -3472
ATOM   1808  H   ARG A 562      22.985  13.465  15.182  1.00  0.00           H  
ATOM   1809  HA  ARG A 562      24.222  14.641  17.465  1.00  0.00           H  
ATOM   1810  HB3 ARG A 562      22.750  16.658  16.873  1.00  0.00           H  
ATOM   1811  HB2 ARG A 562      22.094  15.729  15.557  1.00  0.00           H  
ATOM   1812  HG3 ARG A 562      24.429  15.648  14.532  1.00  0.00           H  
ATOM   1813  HG2 ARG A 562      24.997  16.409  15.996  1.00  0.00           H  
ATOM   1814  HD3 ARG A 562      24.019  18.422  15.633  1.00  0.00           H  
ATOM   1815  HD2 ARG A 562      22.824  17.884  14.503  1.00  0.00           H  
ATOM   1816  HE  ARG A 562      25.820  18.171  14.153  1.00  0.00           H  
ATOM   1817 HH12 ARG A 562      23.323  18.630  10.980  1.00  0.00           H  
ATOM   1818 HH11 ARG A 562      22.617  18.311  12.550  1.00  0.00           H  
ATOM   1819 HH22 ARG A 562      25.560  19.003  10.770  1.00  0.00           H  
ATOM   1820 HH21 ARG A 562      26.644  18.689  12.107  1.00  0.00           H  
ATOM   1821  N   GLY A 563      20.974  14.012  17.707  1.00 15.33           N  
ANISOU 1821  N   GLY A 563     2268   1796   1759     37   -297    -38
ATOM   1822  CA  GLY A 563      19.848  13.882  18.626  1.00 14.02           C  
ANISOU 1822  CA  GLY A 563     2008   1654   1664    116   -381     84
ATOM   1823  C   GLY A 563      20.160  12.829  19.698  1.00 12.79           C  
ANISOU 1823  C   GLY A 563     1667   1583   1608    129   -123    104
ATOM   1824  O   GLY A 563      19.957  13.099  20.877  1.00 15.53           O  
ANISOU 1824  O   GLY A 563     2105   2081   1712   -208    -21      2
ATOM   1825  H   GLY A 563      20.822  13.726  16.748  1.00  0.00           H  
ATOM   1826  HA3 GLY A 563      18.957  13.596  18.070  1.00  0.00           H  
ATOM   1827  HA2 GLY A 563      19.634  14.845  19.094  1.00  0.00           H  
ATOM   1828  N   MET A 564      20.717  11.671  19.306  1.00 12.14           N  
ANISOU 1828  N   MET A 564     1738   1751   1124     40    110   -127
ATOM   1829  CA  MET A 564      21.140  10.611  20.224  1.00 12.16           C  
ANISOU 1829  CA  MET A 564     1606   1583   1430    -94    113   -140
ATOM   1830  C   MET A 564      22.337  10.989  21.114  1.00 13.67           C  
ANISOU 1830  C   MET A 564     1820   2038   1337    -14    -59    -78
ATOM   1831  O   MET A 564      22.347  10.594  22.279  1.00 14.70           O  
ANISOU 1831  O   MET A 564     2409   1839   1335   -113    290    137
ATOM   1832  CB  MET A 564      21.448   9.328  19.437  1.00 12.20           C  
ANISOU 1832  CB  MET A 564     1579   1603   1453    -66    397   -137
ATOM   1833  CG  MET A 564      20.238   8.675  18.750  1.00 15.85           C  
ANISOU 1833  CG  MET A 564     2003   2455   1562   -249     27   -200
ATOM   1834  SD  MET A 564      18.790   8.327  19.789  1.00 15.00           S  
ANISOU 1834  SD  MET A 564     1972   2135   1590   -158    -32    -56
ATOM   1835  CE  MET A 564      19.586   7.325  21.063  1.00 18.73           C  
ANISOU 1835  CE  MET A 564     2801   2596   1716     84    200    738
ATOM   1836  H   MET A 564      20.873  11.500  18.321  1.00  0.00           H  
ATOM   1837  HA  MET A 564      20.310  10.415  20.904  1.00  0.00           H  
ATOM   1838  HB3 MET A 564      21.910   8.596  20.099  1.00  0.00           H  
ATOM   1839  HB2 MET A 564      22.196   9.556  18.677  1.00  0.00           H  
ATOM   1840  HG3 MET A 564      20.563   7.737  18.301  1.00  0.00           H  
ATOM   1841  HG2 MET A 564      19.897   9.291  17.925  1.00  0.00           H  
ATOM   1842  HE1 MET A 564      18.841   6.777  21.636  1.00  0.00           H  
ATOM   1843  HE2 MET A 564      20.261   6.612  20.592  1.00  0.00           H  
ATOM   1844  HE3 MET A 564      20.160   7.954  21.743  1.00  0.00           H  
ATOM   1845  N   ASP A 565      23.291  11.771  20.578  1.00 14.28           N  
ANISOU 1845  N   ASP A 565     2061   1434   1930   -207    -27   -223
ATOM   1846  CA  ASP A 565      24.411  12.354  21.323  1.00 15.47           C  
ANISOU 1846  CA  ASP A 565     1939   1898   2038   -250     65   -120
ATOM   1847  C   ASP A 565      23.914  13.317  22.418  1.00 15.71           C  
ANISOU 1847  C   ASP A 565     2252   1843   1873   -182     36      1
ATOM   1848  O   ASP A 565      24.396  13.254  23.548  1.00 15.60           O  
ANISOU 1848  O   ASP A 565     2216   1960   1752    -37     23    -90
ATOM   1849  CB  ASP A 565      25.417  13.053  20.372  1.00 16.57           C  
ANISOU 1849  CB  ASP A 565     2104   2246   1946   -265     92     58
ATOM   1850  CG  ASP A 565      26.643  13.682  21.046  1.00 18.55           C  
ANISOU 1850  CG  ASP A 565     2374   2932   1742   -168   -147   -288
ATOM   1851  OD1 ASP A 565      27.292  12.983  21.850  1.00 22.84           O  
ANISOU 1851  OD1 ASP A 565     2099   2993   3586    302   -659   -112
ATOM   1852  OD2 ASP A 565      26.954  14.842  20.704  1.00 24.62           O1-
ANISOU 1852  OD2 ASP A 565     3162   3258   2934   -612   -354   -471
ATOM   1853  H   ASP A 565      23.231  12.028  19.601  1.00  0.00           H  
ATOM   1854  HA  ASP A 565      24.922  11.532  21.828  1.00  0.00           H  
ATOM   1855  HB3 ASP A 565      24.885  13.795  19.779  1.00  0.00           H  
ATOM   1856  HB2 ASP A 565      25.790  12.341  19.638  1.00  0.00           H  
ATOM   1857  N   TYR A 566      22.928  14.155  22.061  1.00 15.67           N  
ANISOU 1857  N   TYR A 566     1929   2117   1907   -278    212   -329
ATOM   1858  CA  TYR A 566      22.243  15.064  22.968  1.00 15.75           C  
ANISOU 1858  CA  TYR A 566     2285   2143   1557    325    202    142
ATOM   1859  C   TYR A 566      21.475  14.334  24.091  1.00 13.84           C  
ANISOU 1859  C   TYR A 566     2404   1639   1212    194     64   -118
ATOM   1860  O   TYR A 566      21.591  14.751  25.242  1.00 14.37           O  
ANISOU 1860  O   TYR A 566     2402   1961   1096     19    -76   -147
ATOM   1861  CB  TYR A 566      21.361  16.032  22.152  1.00 15.92           C  
ANISOU 1861  CB  TYR A 566     2377   2473   1197    278   -192    124
ATOM   1862  CG  TYR A 566      20.515  16.940  23.014  1.00 13.45           C  
ANISOU 1862  CG  TYR A 566     1861   1680   1566    136   -252    229
ATOM   1863  CD1 TYR A 566      21.086  18.101  23.565  1.00 14.37           C  
ANISOU 1863  CD1 TYR A 566     1993   1683   1781     -9     17    262
ATOM   1864  CE1 TYR A 566      20.351  18.879  24.473  1.00 14.70           C  
ANISOU 1864  CE1 TYR A 566     2217   1736   1630   -299     70    -15
ATOM   1865  CZ  TYR A 566      19.041  18.501  24.823  1.00 14.07           C  
ANISOU 1865  CZ  TYR A 566     1932   1955   1457    189    218    -40
ATOM   1866  OH  TYR A 566      18.339  19.247  25.718  1.00 13.81           O  
ANISOU 1866  OH  TYR A 566     2102   1743   1402    254    131   -159
ATOM   1867  CE2 TYR A 566      18.460  17.353  24.252  1.00 16.61           C  
ANISOU 1867  CE2 TYR A 566     2161   2328   1820    117     96   -113
ATOM   1868  CD2 TYR A 566      19.194  16.575  23.342  1.00 14.25           C  
ANISOU 1868  CD2 TYR A 566     1949   1235   2230    210   -378    -33
ATOM   1869  H   TYR A 566      22.593  14.147  21.106  1.00  0.00           H  
ATOM   1870  HA  TYR A 566      23.015  15.666  23.452  1.00  0.00           H  
ATOM   1871  HB3 TYR A 566      20.697  15.480  21.488  1.00  0.00           H  
ATOM   1872  HB2 TYR A 566      21.986  16.645  21.501  1.00  0.00           H  
ATOM   1873  HD1 TYR A 566      22.098  18.378  23.320  1.00  0.00           H  
ATOM   1874  HE1 TYR A 566      20.814  19.749  24.911  1.00  0.00           H  
ATOM   1875  HH  TYR A 566      18.783  20.081  25.913  1.00  0.00           H  
ATOM   1876  HE2 TYR A 566      17.459  17.050  24.507  1.00  0.00           H  
ATOM   1877  HD2 TYR A 566      18.761  15.675  22.930  1.00  0.00           H  
ATOM   1878  N   LEU A 567      20.732  13.261  23.753  1.00 15.31           N  
ANISOU 1878  N   LEU A 567     2078   2070   1669   -171     90    263
ATOM   1879  CA  LEU A 567      19.998  12.434  24.721  1.00 15.20           C  
ANISOU 1879  CA  LEU A 567     2296   1596   1881    -91    204    285
ATOM   1880  C   LEU A 567      20.928  11.768  25.744  1.00 15.95           C  
ANISOU 1880  C   LEU A 567     2049   2288   1723     69    200    153
ATOM   1881  O   LEU A 567      20.628  11.816  26.934  1.00 15.94           O  
ANISOU 1881  O   LEU A 567     2820   1629   1606   -551    187     31
ATOM   1882  CB  LEU A 567      19.150  11.352  24.011  1.00 15.22           C  
ANISOU 1882  CB  LEU A 567     2670   1573   1539    -19     48    249
ATOM   1883  CG  LEU A 567      17.902  11.868  23.269  1.00 16.22           C  
ANISOU 1883  CG  LEU A 567     1965   2217   1979    281     52   -198
ATOM   1884  CD1 LEU A 567      17.245  10.738  22.446  1.00 19.13           C  
ANISOU 1884  CD1 LEU A 567     1951   2642   2672    236     11   -695
ATOM   1885  CD2 LEU A 567      16.898  12.585  24.194  1.00 16.57           C  
ANISOU 1885  CD2 LEU A 567     2686   2290   1317    589    173    357
ATOM   1886  H   LEU A 567      20.666  12.983  22.782  1.00  0.00           H  
ATOM   1887  HA  LEU A 567      19.339  13.099  25.281  1.00  0.00           H  
ATOM   1888  HB3 LEU A 567      18.812  10.614  24.740  1.00  0.00           H  
ATOM   1889  HB2 LEU A 567      19.790  10.804  23.318  1.00  0.00           H  
ATOM   1890  HG  LEU A 567      18.246  12.612  22.560  1.00  0.00           H  
ATOM   1891 HD11 LEU A 567      17.113  11.044  21.407  1.00  0.00           H  
ATOM   1892 HD12 LEU A 567      17.851   9.832  22.436  1.00  0.00           H  
ATOM   1893 HD13 LEU A 567      16.266  10.452  22.829  1.00  0.00           H  
ATOM   1894 HD21 LEU A 567      15.870  12.261  24.039  1.00  0.00           H  
ATOM   1895 HD22 LEU A 567      17.124  12.418  25.245  1.00  0.00           H  
ATOM   1896 HD23 LEU A 567      16.921  13.661  24.020  1.00  0.00           H  
ATOM   1897  N   HIS A 568      22.047  11.195  25.274  1.00 13.68           N  
ANISOU 1897  N   HIS A 568     2687   1266   1242    139    304   -122
ATOM   1898  CA  HIS A 568      23.035  10.512  26.114  1.00 15.22           C  
ANISOU 1898  CA  HIS A 568     2520   1700   1560    -38    347    144
ATOM   1899  C   HIS A 568      23.834  11.467  27.012  1.00 16.93           C  
ANISOU 1899  C   HIS A 568     2383   2114   1935   -281   -158    356
ATOM   1900  O   HIS A 568      24.195  11.075  28.121  1.00 18.10           O  
ANISOU 1900  O   HIS A 568     2992   2089   1794   -363   -498     40
ATOM   1901  CB  HIS A 568      23.959   9.658  25.232  1.00 16.08           C  
ANISOU 1901  CB  HIS A 568     2170   1694   2246    336     44    112
ATOM   1902  CG  HIS A 568      23.289   8.460  24.607  1.00 15.00           C  
ANISOU 1902  CG  HIS A 568     1871   1904   1924   -140    -81    227
ATOM   1903  ND1 HIS A 568      24.026   7.403  24.075  1.00 15.77           N  
ANISOU 1903  ND1 HIS A 568     2381   1333   2276   -745    -85   -400
ATOM   1904  CE1 HIS A 568      23.124   6.546  23.625  1.00 11.87           C  
ANISOU 1904  CE1 HIS A 568     1896   1430   1181   -415   -329   -448
ATOM   1905  NE2 HIS A 568      21.877   6.951  23.835  1.00 15.64           N  
ANISOU 1905  NE2 HIS A 568     2435   1854   1653   -767   -318   -112
ATOM   1906  CD2 HIS A 568      21.947   8.178  24.457  1.00 10.90           C  
ANISOU 1906  CD2 HIS A 568     1293   1940    906   -461     74    109
ATOM   1907  H   HIS A 568      22.229  11.198  24.279  1.00  0.00           H  
ATOM   1908  HA  HIS A 568      22.498   9.840  26.787  1.00  0.00           H  
ATOM   1909  HB3 HIS A 568      24.801   9.291  25.821  1.00  0.00           H  
ATOM   1910  HB2 HIS A 568      24.384  10.264  24.430  1.00  0.00           H  
ATOM   1911  HE1 HIS A 568      23.377   5.621  23.136  1.00  0.00           H  
ATOM   1912  HD2 HIS A 568      21.061   8.727  24.731  1.00  0.00           H  
ATOM   1913  HE2 HIS A 568      21.030   6.434  23.620  1.00  0.00           H  
ATOM   1914  N   ALA A 569      24.029  12.715  26.553  1.00 15.10           N  
ANISOU 1914  N   ALA A 569     2399   1931   1404   -311   -333    201
ATOM   1915  CA  ALA A 569      24.574  13.816  27.347  1.00 19.65           C  
ANISOU 1915  CA  ALA A 569     3580   2017   1869    -84   -261   -435
ATOM   1916  C   ALA A 569      23.619  14.293  28.460  1.00 17.23           C  
ANISOU 1916  C   ALA A 569     3224   1744   1579   -503   -355     63
ATOM   1917  O   ALA A 569      24.100  14.758  29.492  1.00 20.64           O  
ANISOU 1917  O   ALA A 569     3888   2540   1412   -430   -581    -14
ATOM   1918  CB  ALA A 569      24.945  14.970  26.409  1.00 19.69           C  
ANISOU 1918  CB  ALA A 569     3593   2314   1572   -473   -389   -745
ATOM   1919  H   ALA A 569      23.707  12.955  25.625  1.00  0.00           H  
ATOM   1920  HA  ALA A 569      25.489  13.467  27.828  1.00  0.00           H  
ATOM   1921  HB1 ALA A 569      25.315  15.824  26.971  1.00  0.00           H  
ATOM   1922  HB2 ALA A 569      25.730  14.667  25.716  1.00  0.00           H  
ATOM   1923  HB3 ALA A 569      24.093  15.310  25.820  1.00  0.00           H  
ATOM   1924  N   LYS A 570      22.300  14.129  28.250  1.00 17.84           N  
ANISOU 1924  N   LYS A 570     2982   1930   1864   -727    324   -824
ATOM   1925  CA  LYS A 570      21.237  14.357  29.235  1.00 20.28           C  
ANISOU 1925  CA  LYS A 570     4021   2378   1303   -455    532   -577
ATOM   1926  C   LYS A 570      20.905  13.107  30.080  1.00 21.25           C  
ANISOU 1926  C   LYS A 570     3564   2961   1547   -512    465   -130
ATOM   1927  O   LYS A 570      19.968  13.165  30.876  1.00 21.19           O  
ANISOU 1927  O   LYS A 570     4239   1898   1913   -773   1066   -238
ATOM   1928  CB  LYS A 570      19.980  14.897  28.505  1.00 23.78           C  
ANISOU 1928  CB  LYS A 570     3988   2844   2200   -314    775   -292
ATOM   1929  CG  LYS A 570      20.119  16.316  27.919  1.00 25.12           C  
ANISOU 1929  CG  LYS A 570     4324   3097   2121   -837    215   -151
ATOM   1930  CD  LYS A 570      20.436  17.390  28.972  1.00 31.41           C  
ANISOU 1930  CD  LYS A 570     5813   4141   1978  -1383   -975   -347
ATOM   1931  CE  LYS A 570      20.320  18.819  28.423  1.00 35.50           C  
ANISOU 1931  CE  LYS A 570     6068   4137   3281  -1207  -1959   -595
ATOM   1932  NZ  LYS A 570      20.706  19.817  29.434  1.00 40.72           N1+
ANISOU 1932  NZ  LYS A 570     7243   5053   3175    941  -2231   -914
ATOM   1933  H   LYS A 570      21.994  13.754  27.362  1.00  0.00           H  
ATOM   1934  HA  LYS A 570      21.575  15.102  29.955  1.00  0.00           H  
ATOM   1935  HB3 LYS A 570      19.134  14.922  29.194  1.00  0.00           H  
ATOM   1936  HB2 LYS A 570      19.689  14.209  27.712  1.00  0.00           H  
ATOM   1937  HG3 LYS A 570      19.188  16.573  27.411  1.00  0.00           H  
ATOM   1938  HG2 LYS A 570      20.892  16.333  27.152  1.00  0.00           H  
ATOM   1939  HD3 LYS A 570      21.451  17.238  29.340  1.00  0.00           H  
ATOM   1940  HD2 LYS A 570      19.773  17.264  29.830  1.00  0.00           H  
ATOM   1941  HE3 LYS A 570      19.294  19.021  28.119  1.00  0.00           H  
ATOM   1942  HE2 LYS A 570      20.956  18.943  27.546  1.00  0.00           H  
ATOM   1943  HZ1 LYS A 570      20.082  19.754  30.228  1.00  0.00           H  
ATOM   1944  HZ2 LYS A 570      21.656  19.640  29.730  1.00  0.00           H  
ATOM   1945  HZ3 LYS A 570      20.653  20.747  29.038  1.00  0.00           H  
ATOM   1946  N   SER A 571      21.668  12.010  29.907  1.00 18.70           N  
ANISOU 1946  N   SER A 571     3474   2450   1180   -644    -81    176
ATOM   1947  CA  SER A 571      21.531  10.716  30.593  1.00 20.23           C  
ANISOU 1947  CA  SER A 571     3514   2122   2050   -780   -175     10
ATOM   1948  C   SER A 571      20.206   9.976  30.302  1.00 18.89           C  
ANISOU 1948  C   SER A 571     3511   2053   1613   -673   -303    113
ATOM   1949  O   SER A 571      19.745   9.184  31.125  1.00 26.37           O  
ANISOU 1949  O   SER A 571     4632   3370   2016  -1380    365    251
ATOM   1950  CB  SER A 571      21.848  10.846  32.103  1.00 27.61           C  
ANISOU 1950  CB  SER A 571     4505   3832   2152  -1104   -117   -294
ATOM   1951  OG  SER A 571      23.230  11.075  32.294  1.00 32.78           O  
ANISOU 1951  OG  SER A 571     5023   5565   1865  -1284   -764   -621
ATOM   1952  H   SER A 571      22.425  12.057  29.239  1.00  0.00           H  
ATOM   1953  HA  SER A 571      22.291  10.078  30.148  1.00  0.00           H  
ATOM   1954  HB3 SER A 571      21.611   9.927  32.640  1.00  0.00           H  
ATOM   1955  HB2 SER A 571      21.274  11.641  32.579  1.00  0.00           H  
ATOM   1956  HG  SER A 571      23.707  10.268  32.083  1.00  0.00           H  
ATOM   1957  N   ILE A 572      19.630  10.237  29.119  1.00 16.31           N  
ANISOU 1957  N   ILE A 572     2873   1769   1555    447     56    251
ATOM   1958  CA  ILE A 572      18.400   9.631  28.626  1.00 16.63           C  
ANISOU 1958  CA  ILE A 572     2876   1776   1664     71    443   -152
ATOM   1959  C   ILE A 572      18.776   8.519  27.636  1.00 15.11           C  
ANISOU 1959  C   ILE A 572     2496   1330   1915   -126    324   -184
ATOM   1960  O   ILE A 572      19.404   8.795  26.615  1.00 15.74           O  
ANISOU 1960  O   ILE A 572     2265   2184   1530   -328     72   -380
ATOM   1961  CB  ILE A 572      17.500  10.681  27.904  1.00 18.50           C  
ANISOU 1961  CB  ILE A 572     2503   1690   2836    190    370    -91
ATOM   1962  CG1 ILE A 572      17.021  11.771  28.893  1.00 23.46           C  
ANISOU 1962  CG1 ILE A 572     3888   2382   2643    738    597   -131
ATOM   1963  CG2 ILE A 572      16.288  10.079  27.154  1.00 21.09           C  
ANISOU 1963  CG2 ILE A 572     2697   2479   2834    351    338   -245
ATOM   1964  CD1 ILE A 572      16.577  13.077  28.220  1.00 24.55           C  
ANISOU 1964  CD1 ILE A 572     4510   1845   2970    343    685   -199
ATOM   1965  H   ILE A 572      20.077  10.887  28.484  1.00  0.00           H  
ATOM   1966  HA  ILE A 572      17.827   9.206  29.452  1.00  0.00           H  
ATOM   1967  HB  ILE A 572      18.115  11.178  27.153  1.00  0.00           H  
ATOM   1968 HG13 ILE A 572      17.812  12.024  29.598  1.00  0.00           H  
ATOM   1969 HG12 ILE A 572      16.206  11.378  29.501  1.00  0.00           H  
ATOM   1970 HG21 ILE A 572      15.669  10.858  26.710  1.00  0.00           H  
ATOM   1971 HG22 ILE A 572      16.588   9.427  26.333  1.00  0.00           H  
ATOM   1972 HG23 ILE A 572      15.656   9.498  27.826  1.00  0.00           H  
ATOM   1973 HD11 ILE A 572      16.600  13.898  28.935  1.00  0.00           H  
ATOM   1974 HD12 ILE A 572      17.237  13.352  27.398  1.00  0.00           H  
ATOM   1975 HD13 ILE A 572      15.561  13.002  27.832  1.00  0.00           H  
ATOM   1976  N   ILE A 573      18.346   7.291  27.954  1.00 13.52           N  
ANISOU 1976  N   ILE A 573     2460   1413   1261     -9    -47    -45
ATOM   1977  CA  ILE A 573      18.368   6.153  27.042  1.00 13.97           C  
ANISOU 1977  CA  ILE A 573     2321   1175   1809    193    235   -134
ATOM   1978  C   ILE A 573      16.984   6.119  26.361  1.00 13.85           C  
ANISOU 1978  C   ILE A 573     2293   1600   1368    251    392   -279
ATOM   1979  O   ILE A 573      15.971   6.199  27.058  1.00 14.54           O  
ANISOU 1979  O   ILE A 573     2126   1977   1420    341    381   -198
ATOM   1980  CB  ILE A 573      18.595   4.811  27.806  1.00 15.21           C  
ANISOU 1980  CB  ILE A 573     2317   1619   1841     -8    -12    196
ATOM   1981  CG1 ILE A 573      19.910   4.821  28.626  1.00 15.33           C  
ANISOU 1981  CG1 ILE A 573     2597   1756   1472    -30   -259     95
ATOM   1982  CG2 ILE A 573      18.583   3.575  26.880  1.00 16.03           C  
ANISOU 1982  CG2 ILE A 573     2293   2080   1718    -13    169    -20
ATOM   1983  CD1 ILE A 573      19.919   3.830  29.799  1.00 18.46           C  
ANISOU 1983  CD1 ILE A 573     3125   1604   2283    199     88    214
ATOM   1984  H   ILE A 573      17.855   7.143  28.826  1.00  0.00           H  
ATOM   1985  HA  ILE A 573      19.155   6.279  26.299  1.00  0.00           H  
ATOM   1986  HB  ILE A 573      17.773   4.690  28.513  1.00  0.00           H  
ATOM   1987 HG13 ILE A 573      20.096   5.808  29.048  1.00  0.00           H  
ATOM   1988 HG12 ILE A 573      20.759   4.626  27.971  1.00  0.00           H  
ATOM   1989 HG21 ILE A 573      18.674   2.646  27.441  1.00  0.00           H  
ATOM   1990 HG22 ILE A 573      17.673   3.500  26.292  1.00  0.00           H  
ATOM   1991 HG23 ILE A 573      19.415   3.613  26.179  1.00  0.00           H  
ATOM   1992 HD11 ILE A 573      20.933   3.684  30.172  1.00  0.00           H  
ATOM   1993 HD12 ILE A 573      19.317   4.207  30.626  1.00  0.00           H  
ATOM   1994 HD13 ILE A 573      19.526   2.853  29.521  1.00  0.00           H  
ATOM   1995  N   HIS A 574      16.960   6.018  25.021  1.00 15.33           N  
ANISOU 1995  N   HIS A 574     2476   1987   1361    329    168   -291
ATOM   1996  CA  HIS A 574      15.732   5.939  24.226  1.00 15.26           C  
ANISOU 1996  CA  HIS A 574     2734   1619   1444    124    -42   -196
ATOM   1997  C   HIS A 574      14.957   4.644  24.514  1.00 17.09           C  
ANISOU 1997  C   HIS A 574     2530   2150   1812     45    587   -127
ATOM   1998  O   HIS A 574      13.781   4.726  24.853  1.00 13.38           O  
ANISOU 1998  O   HIS A 574     2231   2001    851    286    195    -71
ATOM   1999  CB  HIS A 574      16.055   6.099  22.724  1.00 15.39           C  
ANISOU 1999  CB  HIS A 574     2351   2156   1338    155   -177   -193
ATOM   2000  CG  HIS A 574      14.877   6.375  21.816  1.00 15.11           C  
ANISOU 2000  CG  HIS A 574     1995   2054   1690     -7     66    -11
ATOM   2001  ND1 HIS A 574      13.664   5.679  21.883  1.00 13.58           N  
ANISOU 2001  ND1 HIS A 574     2068   1893   1200   -262     31     28
ATOM   2002  CE1 HIS A 574      12.899   6.213  20.942  1.00 15.46           C  
ANISOU 2002  CE1 HIS A 574     2156   1387   2329    176   -156     52
ATOM   2003  NE2 HIS A 574      13.518   7.177  20.264  1.00 15.98           N  
ANISOU 2003  NE2 HIS A 574     2571   1781   1718   -275    238    -93
ATOM   2004  CD2 HIS A 574      14.789   7.299  20.798  1.00 17.64           C  
ANISOU 2004  CD2 HIS A 574     2730   1965   2005    -99    240    133
ATOM   2005  H   HIS A 574      17.833   5.925  24.514  1.00  0.00           H  
ATOM   2006  HA  HIS A 574      15.107   6.785  24.523  1.00  0.00           H  
ATOM   2007  HB3 HIS A 574      16.574   5.222  22.340  1.00  0.00           H  
ATOM   2008  HB2 HIS A 574      16.746   6.934  22.603  1.00  0.00           H  
ATOM   2009  HE1 HIS A 574      11.885   5.895  20.744  1.00  0.00           H  
ATOM   2010  HD2 HIS A 574      15.515   8.006  20.432  1.00  0.00           H  
ATOM   2011  HE2 HIS A 574      13.118   7.718  19.508  1.00  0.00           H  
ATOM   2012  N   ARG A 575      15.639   3.492  24.391  1.00 14.47           N  
ANISOU 2012  N   ARG A 575     2307   2050   1141    159   -203    -83
ATOM   2013  CA  ARG A 575      15.120   2.125  24.554  1.00 18.29           C  
ANISOU 2013  CA  ARG A 575     3229   2223   1495    -81   -126    164
ATOM   2014  C   ARG A 575      14.311   1.590  23.364  1.00 16.71           C  
ANISOU 2014  C   ARG A 575     2683   1953   1710    -20   -140     80
ATOM   2015  O   ARG A 575      13.997   0.399  23.371  1.00 16.16           O  
ANISOU 2015  O   ARG A 575     2602   1845   1691   -305   -105   -163
ATOM   2016  CB  ARG A 575      14.354   1.902  25.882  1.00 18.03           C  
ANISOU 2016  CB  ARG A 575     3577   2014   1260   -296   -181    213
ATOM   2017  CG  ARG A 575      15.121   2.369  27.122  1.00 18.33           C  
ANISOU 2017  CG  ARG A 575     2584   2605   1775   -457   -498    623
ATOM   2018  CD  ARG A 575      14.435   1.970  28.435  1.00 21.98           C  
ANISOU 2018  CD  ARG A 575     4170   2791   1389   -764   -190    237
ATOM   2019  NE  ARG A 575      15.266   2.332  29.596  1.00 20.93           N  
ANISOU 2019  NE  ARG A 575     3438   3031   1480   -116   -197    346
ATOM   2020  CZ  ARG A 575      15.451   3.558  30.122  1.00 23.88           C  
ANISOU 2020  CZ  ARG A 575     3420   3164   2487   -543   -299    576
ATOM   2021  NH1 ARG A 575      14.827   4.651  29.656  1.00 25.85           N  
ANISOU 2021  NH1 ARG A 575     4213   3201   2408   -226   -393    280
ATOM   2022  NH2 ARG A 575      16.300   3.695  31.146  1.00 25.29           N1+
ANISOU 2022  NH2 ARG A 575     5184   2383   2040    463   -649    198
ATOM   2023  H   ARG A 575      16.609   3.548  24.106  1.00  0.00           H  
ATOM   2024  HA  ARG A 575      16.005   1.496  24.601  1.00  0.00           H  
ATOM   2025  HB3 ARG A 575      14.149   0.837  25.994  1.00  0.00           H  
ATOM   2026  HB2 ARG A 575      13.377   2.386  25.853  1.00  0.00           H  
ATOM   2027  HG3 ARG A 575      15.199   3.454  27.086  1.00  0.00           H  
ATOM   2028  HG2 ARG A 575      16.141   1.997  27.098  1.00  0.00           H  
ATOM   2029  HD3 ARG A 575      14.209   0.903  28.450  1.00  0.00           H  
ATOM   2030  HD2 ARG A 575      13.478   2.486  28.523  1.00  0.00           H  
ATOM   2031  HE  ARG A 575      15.803   1.575  29.994  1.00  0.00           H  
ATOM   2032 HH12 ARG A 575      15.012   5.561  30.056  1.00  0.00           H  
ATOM   2033 HH11 ARG A 575      14.203   4.578  28.866  1.00  0.00           H  
ATOM   2034 HH22 ARG A 575      16.495   4.611  31.527  1.00  0.00           H  
ATOM   2035 HH21 ARG A 575      16.816   2.893  31.487  1.00  0.00           H  
ATOM   2036  N   ASP A 576      14.005   2.431  22.364  1.00 14.63           N  
ANISOU 2036  N   ASP A 576     1933   1738   1885    258    153     81
ATOM   2037  CA  ASP A 576      13.268   2.008  21.179  1.00 15.85           C  
ANISOU 2037  CA  ASP A 576     2217   1936   1869    -30    -41    297
ATOM   2038  C   ASP A 576      13.598   2.917  19.982  1.00 13.74           C  
ANISOU 2038  C   ASP A 576     1822   1508   1889   -336    -50     88
ATOM   2039  O   ASP A 576      12.693   3.349  19.272  1.00 15.77           O  
ANISOU 2039  O   ASP A 576     2051   1920   2019    184   -109    -60
ATOM   2040  CB  ASP A 576      11.744   1.847  21.458  1.00 15.09           C  
ANISOU 2040  CB  ASP A 576     2273   1791   1670    486    226    464
ATOM   2041  CG  ASP A 576      10.931   1.060  20.414  1.00 19.56           C  
ANISOU 2041  CG  ASP A 576     2463   2073   2895     91    242    184
ATOM   2042  OD1 ASP A 576      11.537   0.367  19.569  1.00 21.00           O  
ANISOU 2042  OD1 ASP A 576     2655   2415   2907   -100    101   -388
ATOM   2043  OD2 ASP A 576       9.689   1.085  20.523  1.00 23.90           O1-
ANISOU 2043  OD2 ASP A 576     2404   2564   4111   -151    576   -780
ATOM   2044  H   ASP A 576      14.273   3.404  22.410  1.00  0.00           H  
ATOM   2045  HA  ASP A 576      13.675   1.035  20.907  1.00  0.00           H  
ATOM   2046  HB3 ASP A 576      11.301   2.834  21.590  1.00  0.00           H  
ATOM   2047  HB2 ASP A 576      11.598   1.351  22.419  1.00  0.00           H  
ATOM   2048  N   LEU A 577      14.892   3.188  19.747  1.00 13.34           N  
ANISOU 2048  N   LEU A 577     1782   1714   1573    -66    -36    -66
ATOM   2049  CA  LEU A 577      15.341   3.863  18.531  1.00 13.79           C  
ANISOU 2049  CA  LEU A 577     1789   1765   1682   -155     57    137
ATOM   2050  C   LEU A 577      15.153   2.931  17.322  1.00 13.49           C  
ANISOU 2050  C   LEU A 577     1996   1828   1301   -184    151    381
ATOM   2051  O   LEU A 577      15.547   1.768  17.363  1.00 16.10           O  
ANISOU 2051  O   LEU A 577     2693   2004   1420    -26    -92    110
ATOM   2052  CB  LEU A 577      16.800   4.346  18.683  1.00 14.55           C  
ANISOU 2052  CB  LEU A 577     1760   1805   1963   -109    201    -44
ATOM   2053  CG  LEU A 577      17.346   5.131  17.464  1.00 15.32           C  
ANISOU 2053  CG  LEU A 577     2312   1709   1798   -190    521   -363
ATOM   2054  CD1 LEU A 577      16.605   6.470  17.251  1.00 16.95           C  
ANISOU 2054  CD1 LEU A 577     2143   1955   2342   -514   -361    178
ATOM   2055  CD2 LEU A 577      18.867   5.310  17.574  1.00 17.16           C  
ANISOU 2055  CD2 LEU A 577     2424   1628   2467     73    246   -155
ATOM   2056  H   LEU A 577      15.611   2.797  20.344  1.00  0.00           H  
ATOM   2057  HA  LEU A 577      14.711   4.746  18.398  1.00  0.00           H  
ATOM   2058  HB3 LEU A 577      17.439   3.479  18.851  1.00  0.00           H  
ATOM   2059  HB2 LEU A 577      16.891   4.961  19.579  1.00  0.00           H  
ATOM   2060  HG  LEU A 577      17.195   4.540  16.561  1.00  0.00           H  
ATOM   2061 HD11 LEU A 577      17.282   7.311  17.097  1.00  0.00           H  
ATOM   2062 HD12 LEU A 577      15.957   6.415  16.376  1.00  0.00           H  
ATOM   2063 HD13 LEU A 577      15.974   6.729  18.102  1.00  0.00           H  
ATOM   2064 HD21 LEU A 577      19.214   6.244  17.136  1.00  0.00           H  
ATOM   2065 HD22 LEU A 577      19.212   5.275  18.608  1.00  0.00           H  
ATOM   2066 HD23 LEU A 577      19.365   4.503  17.040  1.00  0.00           H  
ATOM   2067  N   LYS A 578      14.536   3.480  16.276  1.00 13.45           N  
ANISOU 2067  N   LYS A 578     1969   1809   1332    -23    -72    141
ATOM   2068  CA  LYS A 578      14.237   2.820  15.014  1.00 13.38           C  
ANISOU 2068  CA  LYS A 578     1819   2023   1240    221    169   -111
ATOM   2069  C   LYS A 578      13.826   3.902  14.014  1.00 15.56           C  
ANISOU 2069  C   LYS A 578     2379   1979   1553     30   -351    -32
ATOM   2070  O   LYS A 578      13.541   5.032  14.414  1.00 14.09           O  
ANISOU 2070  O   LYS A 578     1943   2174   1233   -193     12   -111
ATOM   2071  CB  LYS A 578      13.173   1.705  15.197  1.00 17.04           C  
ANISOU 2071  CB  LYS A 578     2491   2279   1702    106      6    471
ATOM   2072  CG  LYS A 578      11.817   2.126  15.791  1.00 16.08           C  
ANISOU 2072  CG  LYS A 578     2217   2102   1790    172    131   1008
ATOM   2073  CD  LYS A 578      10.935   0.907  16.109  1.00 22.04           C  
ANISOU 2073  CD  LYS A 578     2694   1953   3727   -180   -315    703
ATOM   2074  CE  LYS A 578       9.589   1.308  16.731  1.00 24.49           C  
ANISOU 2074  CE  LYS A 578     2627   2625   4053   -422   -253    350
ATOM   2075  NZ  LYS A 578       8.820   0.146  17.205  1.00 29.33           N1+
ANISOU 2075  NZ  LYS A 578     2662   3985   4494   -504   -225   1530
ATOM   2076  H   LYS A 578      14.244   4.446  16.326  1.00  0.00           H  
ATOM   2077  HA  LYS A 578      15.161   2.371  14.646  1.00  0.00           H  
ATOM   2078  HB3 LYS A 578      13.593   0.920  15.825  1.00  0.00           H  
ATOM   2079  HB2 LYS A 578      12.982   1.236  14.233  1.00  0.00           H  
ATOM   2080  HG3 LYS A 578      11.296   2.789  15.100  1.00  0.00           H  
ATOM   2081  HG2 LYS A 578      11.975   2.696  16.706  1.00  0.00           H  
ATOM   2082  HD3 LYS A 578      11.477   0.240  16.782  1.00  0.00           H  
ATOM   2083  HD2 LYS A 578      10.762   0.337  15.195  1.00  0.00           H  
ATOM   2084  HE3 LYS A 578       8.994   1.855  16.002  1.00  0.00           H  
ATOM   2085  HE2 LYS A 578       9.748   1.967  17.583  1.00  0.00           H  
ATOM   2086  HZ1 LYS A 578       8.650  -0.497  16.445  1.00  0.00           H  
ATOM   2087  HZ2 LYS A 578       9.344  -0.326  17.930  1.00  0.00           H  
ATOM   2088  HZ3 LYS A 578       7.940   0.455  17.600  1.00  0.00           H  
ATOM   2089  N   SER A 579      13.807   3.544  12.724  1.00 13.20           N  
ANISOU 2089  N   SER A 579     1662   1946   1406   -183     69    109
ATOM   2090  CA  SER A 579      13.437   4.449  11.635  1.00 15.29           C  
ANISOU 2090  CA  SER A 579     2242   1887   1677      6   -148    151
ATOM   2091  C   SER A 579      11.996   4.991  11.716  1.00 13.61           C  
ANISOU 2091  C   SER A 579     2363   1487   1319     -3     78   -213
ATOM   2092  O   SER A 579      11.759   6.107  11.261  1.00 14.58           O  
ANISOU 2092  O   SER A 579     2177   1392   1968    246    -84   -167
ATOM   2093  CB  SER A 579      13.741   3.759  10.301  1.00 16.90           C  
ANISOU 2093  CB  SER A 579     2801   1879   1738    114   -500    -28
ATOM   2094  OG  SER A 579      12.884   2.657  10.113  1.00 15.24           O  
ANISOU 2094  OG  SER A 579     2431   1957   1399   -220    -72   -372
ATOM   2095  H   SER A 579      14.053   2.601  12.453  1.00  0.00           H  
ATOM   2096  HA  SER A 579      14.097   5.313  11.700  1.00  0.00           H  
ATOM   2097  HB3 SER A 579      14.780   3.432  10.263  1.00  0.00           H  
ATOM   2098  HB2 SER A 579      13.604   4.450   9.471  1.00  0.00           H  
ATOM   2099  HG  SER A 579      13.372   1.981   9.622  1.00  0.00           H  
ATOM   2100  N   ASN A 580      11.062   4.243  12.331  1.00 15.38           N  
ANISOU 2100  N   ASN A 580     2013   1760   2070   -124   -163   -113
ATOM   2101  CA AASN A 580       9.696   4.728  12.549  0.50 13.95           C  
ANISOU 2101  CA AASN A 580     1992   1442   1866    -68   -129    294
ATOM   2102  CA BASN A 580       9.687   4.433  12.695  0.50 15.07           C  
ANISOU 2102  CA BASN A 580     2227   1514   1983    221   -193    143
ATOM   2103  C   ASN A 580       9.614   5.786  13.670  1.00 13.57           C  
ANISOU 2103  C   ASN A 580     1728   1416   2012     74   -125    205
ATOM   2104  O   ASN A 580       8.682   6.587  13.667  1.00 14.43           O  
ANISOU 2104  O   ASN A 580     1423   2123   1938    175   -446   -322
ATOM   2105  CB AASN A 580       8.735   3.552  12.815  0.50 16.07           C  
ANISOU 2105  CB AASN A 580     1941   1417   2748   -325   -363     82
ATOM   2106  CB BASN A 580       9.054   3.198  13.338  0.50 16.69           C  
ANISOU 2106  CB BASN A 580     2519   1486   2336    -70   -363     97
ATOM   2107  CG AASN A 580       7.302   3.869  12.374  0.50 15.15           C  
ANISOU 2107  CG AASN A 580     1680   1518   2555   -256    432    315
ATOM   2108  CG BASN A 580       9.437   1.896  12.627  0.50 20.98           C  
ANISOU 2108  CG BASN A 580     3999   1343   2627   -680   -604   -453
ATOM   2109  OD1AASN A 580       7.064   4.202  11.215  0.50 20.53           O  
ANISOU 2109  OD1AASN A 580     2216   2886   2698    -70    877    233
ATOM   2110  OD1BASN A 580      10.589   1.317  12.713  0.50 14.94           O  
ANISOU 2110  OD1BASN A 580     3727    269   1680   -829   -590    -31
ATOM   2111  ND2AASN A 580       6.344   3.775  13.293  0.50 13.67           N  
ANISOU 2111  ND2AASN A 580     2265   1385   1543   -429    814   -881
ATOM   2112  ND2BASN A 580       8.465   1.466  11.836  0.50 30.21           N  
ANISOU 2112  ND2BASN A 580     4810   3272   3394  -2157   -662   -241
ATOM   2113  H   ASN A 580      11.296   3.328  12.688  1.00  0.00           H  
ATOM   2114  HA AASN A 580       9.359   5.261  11.660  0.50  0.00           H  
ATOM   2115  HA BASN A 580       9.163   4.669  11.769  0.50  0.00           H  
ATOM   2116  HB3AASN A 580       8.782   3.220  13.854  0.50  0.00           H  
ATOM   2117  HB3BASN A 580       7.969   3.305  13.338  0.50  0.00           H  
ATOM   2118  HB2AASN A 580       9.039   2.695  12.212  0.50  0.00           H  
ATOM   2119  HB2BASN A 580       9.353   3.141  14.384  0.50  0.00           H  
ATOM   2120 HD22AASN A 580       5.385   3.981  13.044  0.50  0.00           H  
ATOM   2121 HD22BASN A 580       8.585   0.615  11.305  0.50  0.00           H  
ATOM   2122 HD21AASN A 580       6.572   3.553  14.255  0.50  0.00           H  
ATOM   2123 HD21BASN A 580       7.604   1.989  11.764  0.50  0.00           H  
ATOM   2124  N   ASN A 581      10.615   5.800  14.565  1.00 12.65           N  
ANISOU 2124  N   ASN A 581     1665   1665   1475    107     60   -294
ATOM   2125  CA  ASN A 581      10.793   6.767  15.651  1.00 13.31           C  
ANISOU 2125  CA  ASN A 581     1792   1468   1797     43     21   -301
ATOM   2126  C   ASN A 581      11.762   7.909  15.286  1.00 14.95           C  
ANISOU 2126  C   ASN A 581     2063   1814   1803    -56     80    -99
ATOM   2127  O   ASN A 581      12.120   8.689  16.169  1.00 16.25           O  
ANISOU 2127  O   ASN A 581     2064   2286   1823    -22    143   -395
ATOM   2128  CB  ASN A 581      11.202   5.965  16.913  1.00 14.71           C  
ANISOU 2128  CB  ASN A 581     2009   1761   1817   -182   -196    -77
ATOM   2129  CG  ASN A 581      10.000   5.351  17.645  1.00 13.63           C  
ANISOU 2129  CG  ASN A 581     1902   1827   1447     63   -121    381
ATOM   2130  OD1 ASN A 581       8.851   5.720  17.415  1.00 13.80           O  
ANISOU 2130  OD1 ASN A 581     1930   1722   1590    -13     81    115
ATOM   2131  ND2 ASN A 581      10.245   4.422  18.563  1.00 13.59           N  
ANISOU 2131  ND2 ASN A 581     1760   1848   1553   -433   -198    482
ATOM   2132  H   ASN A 581      11.362   5.127  14.465  1.00  0.00           H  
ATOM   2133  HA  ASN A 581       9.819   7.226  15.796  1.00  0.00           H  
ATOM   2134  HB3 ASN A 581      11.715   6.598  17.631  1.00  0.00           H  
ATOM   2135  HB2 ASN A 581      11.927   5.190  16.662  1.00  0.00           H  
ATOM   2136 HD22 ASN A 581       9.476   3.993  19.064  1.00  0.00           H  
ATOM   2137 HD21 ASN A 581      11.191   4.119  18.771  1.00  0.00           H  
ATOM   2138  N   ILE A 582      12.116   8.027  13.996  1.00 13.41           N  
ANISOU 2138  N   ILE A 582     1369   2132   1594   -188    -56   -232
ATOM   2139  CA  ILE A 582      12.856   9.141  13.409  1.00 12.31           C  
ANISOU 2139  CA  ILE A 582     1816   1519   1342   -323   -412   -465
ATOM   2140  C   ILE A 582      11.929   9.771  12.357  1.00 15.06           C  
ANISOU 2140  C   ILE A 582     2047   1914   1759     -4   -298   -143
ATOM   2141  O   ILE A 582      11.671   9.139  11.334  1.00 17.38           O  
ANISOU 2141  O   ILE A 582     2675   2193   1732    366   -181   -302
ATOM   2142  CB  ILE A 582      14.168   8.635  12.732  1.00 15.40           C  
ANISOU 2142  CB  ILE A 582     2260   1919   1671   -115      1      0
ATOM   2143  CG1 ILE A 582      15.166   8.120  13.796  1.00 14.07           C  
ANISOU 2143  CG1 ILE A 582     2342   1386   1618    -18     68    -28
ATOM   2144  CG2 ILE A 582      14.864   9.670  11.816  1.00 16.08           C  
ANISOU 2144  CG2 ILE A 582     1939   1986   2182   -386    178   -331
ATOM   2145  CD1 ILE A 582      16.255   7.198  13.237  1.00 14.89           C  
ANISOU 2145  CD1 ILE A 582     2795   1717   1142   -284    248   -305
ATOM   2146  H   ILE A 582      11.771   7.346  13.335  1.00  0.00           H  
ATOM   2147  HA  ILE A 582      13.106   9.892  14.161  1.00  0.00           H  
ATOM   2148  HB  ILE A 582      13.904   7.784  12.103  1.00  0.00           H  
ATOM   2149 HG13 ILE A 582      14.643   7.569  14.577  1.00  0.00           H  
ATOM   2150 HG12 ILE A 582      15.632   8.966  14.301  1.00  0.00           H  
ATOM   2151 HG21 ILE A 582      15.773   9.268  11.371  1.00  0.00           H  
ATOM   2152 HG22 ILE A 582      14.238   9.991  10.985  1.00  0.00           H  
ATOM   2153 HG23 ILE A 582      15.142  10.557  12.377  1.00  0.00           H  
ATOM   2154 HD11 ILE A 582      16.844   6.766  14.047  1.00  0.00           H  
ATOM   2155 HD12 ILE A 582      15.832   6.372  12.669  1.00  0.00           H  
ATOM   2156 HD13 ILE A 582      16.941   7.738  12.586  1.00  0.00           H  
ATOM   2157  N   PHE A 583      11.417  10.981  12.634  1.00 15.53           N  
ANISOU 2157  N   PHE A 583     2500   1938   1461      0   -709   -315
ATOM   2158  CA  PHE A 583      10.476  11.676  11.754  1.00 15.19           C  
ANISOU 2158  CA  PHE A 583     2766   1753   1252    184   -310    -39
ATOM   2159  C   PHE A 583      11.241  12.710  10.918  1.00 15.05           C  
ANISOU 2159  C   PHE A 583     2095   2331   1293     39   -434   -118
ATOM   2160  O   PHE A 583      11.948  13.531  11.492  1.00 16.74           O  
ANISOU 2160  O   PHE A 583     2433   2598   1326   -573    -99     81
ATOM   2161  CB  PHE A 583       9.375  12.334  12.609  1.00 17.85           C  
ANISOU 2161  CB  PHE A 583     2595   2152   2033    409   -505   -439
ATOM   2162  CG  PHE A 583       8.069  12.582  11.878  1.00 15.45           C  
ANISOU 2162  CG  PHE A 583     2511   1752   1608    451   -355   -478
ATOM   2163  CD1 PHE A 583       7.968  13.605  10.913  1.00 20.62           C  
ANISOU 2163  CD1 PHE A 583     2855   2659   2320    765    -62    232
ATOM   2164  CE1 PHE A 583       6.785  13.781  10.211  1.00 22.19           C  
ANISOU 2164  CE1 PHE A 583     2775   2724   2930    547   -165   -702
ATOM   2165  CZ  PHE A 583       5.698  12.952  10.450  1.00 21.88           C  
ANISOU 2165  CZ  PHE A 583     2667   2985   2660    164   -352   -896
ATOM   2166  CD2 PHE A 583       6.975  11.712  12.070  1.00 23.36           C  
ANISOU 2166  CD2 PHE A 583     2803   2858   3211    106   -494    109
ATOM   2167  CE2 PHE A 583       5.795  11.914  11.367  1.00 24.65           C  
ANISOU 2167  CE2 PHE A 583     2421   3759   3186    -40   -401     55
ATOM   2168  H   PHE A 583      11.650  11.445  13.503  1.00  0.00           H  
ATOM   2169  HA  PHE A 583       9.994  10.970  11.092  1.00  0.00           H  
ATOM   2170  HB3 PHE A 583       9.714  13.289  13.001  1.00  0.00           H  
ATOM   2171  HB2 PHE A 583       9.163  11.714  13.481  1.00  0.00           H  
ATOM   2172  HD1 PHE A 583       8.800  14.266  10.729  1.00  0.00           H  
ATOM   2173  HE1 PHE A 583       6.710  14.573   9.484  1.00  0.00           H  
ATOM   2174  HZ  PHE A 583       4.773  13.106   9.913  1.00  0.00           H  
ATOM   2175  HD2 PHE A 583       7.043  10.895  12.774  1.00  0.00           H  
ATOM   2176  HE2 PHE A 583       4.951  11.261  11.532  1.00  0.00           H  
ATOM   2177  N   LEU A 584      11.056  12.690   9.590  1.00 14.18           N  
ANISOU 2177  N   LEU A 584     1968   2162   1257   -141   -530    -71
ATOM   2178  CA  LEU A 584      11.618  13.686   8.674  1.00 15.20           C  
ANISOU 2178  CA  LEU A 584     2190   2133   1449   -370   -634    -64
ATOM   2179  C   LEU A 584      10.637  14.866   8.561  1.00 16.64           C  
ANISOU 2179  C   LEU A 584     2123   2363   1835   -167     94   -220
ATOM   2180  O   LEU A 584       9.777  14.877   7.687  1.00 18.32           O  
ANISOU 2180  O   LEU A 584     2791   2221   1949    347   -374   -419
ATOM   2181  CB  LEU A 584      11.928  13.019   7.311  1.00 18.92           C  
ANISOU 2181  CB  LEU A 584     2476   3217   1496  -1328     98   -376
ATOM   2182  CG  LEU A 584      13.377  12.503   7.172  1.00 32.65           C  
ANISOU 2182  CG  LEU A 584     4096   5416   2892    434    736  -1067
ATOM   2183  CD1 LEU A 584      13.792  11.533   8.292  1.00 31.28           C  
ANISOU 2183  CD1 LEU A 584     5608   2488   3790    596   2352   1140
ATOM   2184  CD2 LEU A 584      13.614  11.902   5.773  1.00 27.75           C  
ANISOU 2184  CD2 LEU A 584     2950   4797   2793    448    520  -1223
ATOM   2185  H   LEU A 584      10.430  12.012   9.174  1.00  0.00           H  
ATOM   2186  HA  LEU A 584      12.554  14.083   9.073  1.00  0.00           H  
ATOM   2187  HB3 LEU A 584      11.784  13.742   6.510  1.00  0.00           H  
ATOM   2188  HB2 LEU A 584      11.215  12.218   7.109  1.00  0.00           H  
ATOM   2189  HG  LEU A 584      14.033  13.372   7.251  1.00  0.00           H  
ATOM   2190 HD11 LEU A 584      14.614  10.886   7.987  1.00  0.00           H  
ATOM   2191 HD12 LEU A 584      14.133  12.078   9.172  1.00  0.00           H  
ATOM   2192 HD13 LEU A 584      12.962  10.897   8.599  1.00  0.00           H  
ATOM   2193 HD21 LEU A 584      14.496  12.341   5.306  1.00  0.00           H  
ATOM   2194 HD22 LEU A 584      13.759  10.822   5.804  1.00  0.00           H  
ATOM   2195 HD23 LEU A 584      12.774  12.090   5.102  1.00  0.00           H  
ATOM   2196  N   HIS A 585      10.770  15.836   9.475  1.00 15.88           N  
ANISOU 2196  N   HIS A 585     2294   2141   1598    -60   -604    -79
ATOM   2197  CA  HIS A 585       9.981  17.063   9.514  1.00 16.72           C  
ANISOU 2197  CA  HIS A 585     2494   1914   1945    -22   -210    -32
ATOM   2198  C   HIS A 585      10.339  17.995   8.343  1.00 17.36           C  
ANISOU 2198  C   HIS A 585     2547   2322   1726    377    -46   -181
ATOM   2199  O   HIS A 585      11.507  18.355   8.186  1.00 18.25           O  
ANISOU 2199  O   HIS A 585     2650   1684   2600    -75   -221    -16
ATOM   2200  CB  HIS A 585      10.180  17.751  10.871  1.00 16.33           C  
ANISOU 2200  CB  HIS A 585     2466   1889   1849    -41    -15     15
ATOM   2201  CG  HIS A 585       9.396  19.026  11.026  1.00 18.41           C  
ANISOU 2201  CG  HIS A 585     2261   2257   2475    134   -272    166
ATOM   2202  ND1 HIS A 585       8.006  19.056  10.903  1.00 18.36           N  
ANISOU 2202  ND1 HIS A 585     2413   2497   2063    575     49    200
ATOM   2203  CE1 HIS A 585       7.674  20.327  11.063  1.00 17.31           C  
ANISOU 2203  CE1 HIS A 585     2099   2295   2182    334   -346     86
ATOM   2204  NE2 HIS A 585       8.730  21.110  11.275  1.00 18.47           N  
ANISOU 2204  NE2 HIS A 585     2406   2157   2453    297     -5   -308
ATOM   2205  CD2 HIS A 585       9.854  20.306  11.256  1.00 19.48           C  
ANISOU 2205  CD2 HIS A 585     1634   2513   3255    -52   -556   -239
ATOM   2206  H   HIS A 585      11.515  15.771  10.158  1.00  0.00           H  
ATOM   2207  HA  HIS A 585       8.932  16.778   9.447  1.00  0.00           H  
ATOM   2208  HB3 HIS A 585      11.234  17.973  11.029  1.00  0.00           H  
ATOM   2209  HB2 HIS A 585       9.874  17.075  11.669  1.00  0.00           H  
ATOM   2210  HE1 HIS A 585       6.658  20.691  11.012  1.00  0.00           H  
ATOM   2211  HD2 HIS A 585      10.851  20.699  11.384  1.00  0.00           H  
ATOM   2212  HE2 HIS A 585       8.703  22.118  11.389  1.00  0.00           H  
ATOM   2213  N   GLU A 586       9.317  18.333   7.537  1.00 20.93           N  
ANISOU 2213  N   GLU A 586     2580   3194   2178    962    286    321
ATOM   2214  CA  GLU A 586       9.396  19.067   6.266  1.00 24.88           C  
ANISOU 2214  CA  GLU A 586     3725   3485   2243    947    385    527
ATOM   2215  C   GLU A 586      10.307  18.363   5.231  1.00 28.25           C  
ANISOU 2215  C   GLU A 586     2869   4026   3836    857   1087   1019
ATOM   2216  O   GLU A 586      10.927  19.027   4.402  1.00 40.15           O  
ANISOU 2216  O   GLU A 586     5459   6288   3508    474    886   3010
ATOM   2217  CB  GLU A 586       9.779  20.554   6.501  1.00 33.83           C  
ANISOU 2217  CB  GLU A 586     6176   3094   3585   1390   -249    479
ATOM   2218  CG  GLU A 586       8.853  21.344   7.461  1.00 37.51           C  
ANISOU 2218  CG  GLU A 586     7688   4189   2373   1469    604   1155
ATOM   2219  CD  GLU A 586       7.504  21.820   6.892  1.00 53.53           C  
ANISOU 2219  CD  GLU A 586     7927   7291   5120    777  -1472    953
ATOM   2220  OE1 GLU A 586       7.200  21.534   5.712  1.00 68.74           O  
ANISOU 2220  OE1 GLU A 586    11587   8061   6469  -1751   -674   -749
ATOM   2221  OE2 GLU A 586       6.790  22.497   7.665  1.00 51.15           O1-
ANISOU 2221  OE2 GLU A 586     8488   4023   6922    669   -617   1772
ATOM   2222  H   GLU A 586       8.398  17.970   7.758  1.00  0.00           H  
ATOM   2223  HA  GLU A 586       8.393  19.033   5.841  1.00  0.00           H  
ATOM   2224  HB3 GLU A 586       9.842  21.081   5.548  1.00  0.00           H  
ATOM   2225  HB2 GLU A 586      10.788  20.593   6.901  1.00  0.00           H  
ATOM   2226  HG3 GLU A 586       9.391  22.230   7.800  1.00  0.00           H  
ATOM   2227  HG2 GLU A 586       8.662  20.762   8.362  1.00  0.00           H  
ATOM   2228  N   ASP A 587      10.393  17.023   5.340  1.00 35.09           N  
ANISOU 2228  N   ASP A 587     5975   4372   2985    792    105    138
ATOM   2229  CA  ASP A 587      11.236  16.102   4.565  1.00 30.91           C  
ANISOU 2229  CA  ASP A 587     3819   5471   2451    943  -1314   -298
ATOM   2230  C   ASP A 587      12.754  16.211   4.848  1.00 27.02           C  
ANISOU 2230  C   ASP A 587     3565   4546   2152   -188   1142     96
ATOM   2231  O   ASP A 587      13.502  15.423   4.268  1.00 32.97           O  
ANISOU 2231  O   ASP A 587     4098   5336   3091   1054    165  -1053
ATOM   2232  CB  ASP A 587      10.972  16.104   3.027  1.00 36.28           C  
ANISOU 2232  CB  ASP A 587     5328   6572   1883   1151     13   -747
ATOM   2233  CG  ASP A 587       9.514  15.992   2.532  1.00 39.00           C  
ANISOU 2233  CG  ASP A 587     5704   6507   2605   -303   -451   -132
ATOM   2234  OD1 ASP A 587       8.622  15.588   3.310  1.00 40.41           O  
ANISOU 2234  OD1 ASP A 587     5359   5948   4045   1081    293   1268
ATOM   2235  OD2 ASP A 587       9.330  16.204   1.314  1.00 50.35           O1-
ANISOU 2235  OD2 ASP A 587     7353   8703   3072  -1516  -1183    701
ATOM   2236  H   ASP A 587       9.834  16.577   6.054  1.00  0.00           H  
ATOM   2237  HA  ASP A 587      10.961  15.111   4.920  1.00  0.00           H  
ATOM   2238  HB3 ASP A 587      11.500  15.260   2.579  1.00  0.00           H  
ATOM   2239  HB2 ASP A 587      11.402  17.008   2.591  1.00  0.00           H  
ATOM   2240  N   ASN A 588      13.198  17.165   5.693  1.00 33.46           N  
ANISOU 2240  N   ASN A 588     3151   5894   3666    925   1028  -1776
ATOM   2241  CA  ASN A 588      14.606  17.584   5.784  1.00 29.41           C  
ANISOU 2241  CA  ASN A 588     3423   5093   2659    450     89   1027
ATOM   2242  C   ASN A 588      15.206  17.502   7.196  1.00 32.40           C  
ANISOU 2242  C   ASN A 588     2348   7137   2824   1006    249    736
ATOM   2243  O   ASN A 588      16.423  17.338   7.277  1.00 35.61           O  
ANISOU 2243  O   ASN A 588     2481   9224   1824   1495    438   1596
ATOM   2244  CB  ASN A 588      14.756  19.032   5.251  1.00 41.54           C  
ANISOU 2244  CB  ASN A 588     7005   5968   2810    945  -1285   2426
ATOM   2245  CG  ASN A 588      14.453  19.207   3.758  1.00 36.57           C  
ANISOU 2245  CG  ASN A 588     6379   5257   2258   -487    865   1112
ATOM   2246  OD1 ASN A 588      14.612  18.281   2.965  1.00 58.21           O  
ANISOU 2246  OD1 ASN A 588    10385   7977   3754    423     89  -1951
ATOM   2247  ND2 ASN A 588      14.042  20.413   3.363  1.00 58.07           N  
ANISOU 2247  ND2 ASN A 588     6950   4067  11046   -654   2388   2492
ATOM   2248  H   ASN A 588      12.524  17.753   6.162  1.00  0.00           H  
ATOM   2249  HA  ASN A 588      15.222  16.934   5.162  1.00  0.00           H  
ATOM   2250  HB3 ASN A 588      15.783  19.372   5.393  1.00  0.00           H  
ATOM   2251  HB2 ASN A 588      14.125  19.707   5.829  1.00  0.00           H  
ATOM   2252 HD22 ASN A 588      13.828  20.580   2.391  1.00  0.00           H  
ATOM   2253 HD21 ASN A 588      13.931  21.166   4.026  1.00  0.00           H  
ATOM   2254  N   THR A 589      14.401  17.636   8.264  1.00 27.56           N  
ANISOU 2254  N   THR A 589     3355   4757   2358    961    275   1513
ATOM   2255  CA  THR A 589      14.913  17.686   9.637  1.00 20.98           C  
ANISOU 2255  CA  THR A 589     3700   2241   2030   -133    526    668
ATOM   2256  C   THR A 589      14.429  16.475  10.441  1.00 17.42           C  
ANISOU 2256  C   THR A 589     2487   1968   2161    -41    117    608
ATOM   2257  O   THR A 589      13.229  16.332  10.653  1.00 18.88           O  
ANISOU 2257  O   THR A 589     2443   1941   2788     75   -385    166
ATOM   2258  CB  THR A 589      14.468  18.971  10.382  1.00 20.45           C  
ANISOU 2258  CB  THR A 589     2914   1850   3007   -998    129    487
ATOM   2259  OG1 THR A 589      14.983  20.084   9.685  1.00 24.60           O  
ANISOU 2259  OG1 THR A 589     3522   2775   3050   -251    943   1257
ATOM   2260  CG2 THR A 589      14.958  19.083  11.840  1.00 22.61           C  
ANISOU 2260  CG2 THR A 589     4589   1521   2481   -755   -331   -564
ATOM   2261  H   THR A 589      13.403  17.761   8.148  1.00  0.00           H  
ATOM   2262  HA  THR A 589      16.000  17.681   9.637  1.00  0.00           H  
ATOM   2263  HB  THR A 589      13.380  19.056  10.364  1.00  0.00           H  
ATOM   2264  HG1 THR A 589      14.496  20.188   8.860  1.00  0.00           H  
ATOM   2265 HG21 THR A 589      14.661  20.035  12.276  1.00  0.00           H  
ATOM   2266 HG22 THR A 589      14.537  18.308  12.477  1.00  0.00           H  
ATOM   2267 HG23 THR A 589      16.044  19.012  11.904  1.00  0.00           H  
ATOM   2268  N   VAL A 590      15.375  15.661  10.931  1.00 13.40           N  
ANISOU 2268  N   VAL A 590     1848   2278    965   -143    188    163
ATOM   2269  CA  VAL A 590      15.116  14.558  11.861  1.00 14.69           C  
ANISOU 2269  CA  VAL A 590     2305   2152   1124   -176    174     97
ATOM   2270  C   VAL A 590      14.506  15.067  13.183  1.00 14.02           C  
ANISOU 2270  C   VAL A 590     2414   1712   1199   -184    122     42
ATOM   2271  O   VAL A 590      14.986  16.067  13.703  1.00 17.39           O  
ANISOU 2271  O   VAL A 590     2649   1715   2242   -395    276   -172
ATOM   2272  CB  VAL A 590      16.437  13.796  12.169  1.00 18.17           C  
ANISOU 2272  CB  VAL A 590     2268   2313   2321    -73    644    443
ATOM   2273  CG1 VAL A 590      16.451  12.942  13.455  1.00 19.54           C  
ANISOU 2273  CG1 VAL A 590     2462   2428   2533    483   -347    501
ATOM   2274  CG2 VAL A 590      16.879  12.959  10.956  1.00 18.82           C  
ANISOU 2274  CG2 VAL A 590     2387   1845   2917   -304    159   -127
ATOM   2275  H   VAL A 590      16.347  15.854  10.729  1.00  0.00           H  
ATOM   2276  HA  VAL A 590      14.424  13.870  11.378  1.00  0.00           H  
ATOM   2277  HB  VAL A 590      17.206  14.549  12.317  1.00  0.00           H  
ATOM   2278 HG11 VAL A 590      17.304  12.268  13.472  1.00  0.00           H  
ATOM   2279 HG12 VAL A 590      16.529  13.566  14.346  1.00  0.00           H  
ATOM   2280 HG13 VAL A 590      15.551  12.338  13.556  1.00  0.00           H  
ATOM   2281 HG21 VAL A 590      17.837  12.477  11.142  1.00  0.00           H  
ATOM   2282 HG22 VAL A 590      16.153  12.180  10.725  1.00  0.00           H  
ATOM   2283 HG23 VAL A 590      17.000  13.577  10.065  1.00  0.00           H  
ATOM   2284  N   LYS A 591      13.484  14.364  13.691  1.00 15.21           N  
ANISOU 2284  N   LYS A 591     2331   2025   1423   -335      6    -73
ATOM   2285  CA  LYS A 591      12.871  14.566  15.002  1.00 14.46           C  
ANISOU 2285  CA  LYS A 591     2326   1535   1633   -258    157    -26
ATOM   2286  C   LYS A 591      12.787  13.184  15.650  1.00 15.53           C  
ANISOU 2286  C   LYS A 591     2373   1707   1819    -67   -470    171
ATOM   2287  O   LYS A 591      11.978  12.358  15.221  1.00 15.88           O  
ANISOU 2287  O   LYS A 591     2333   2073   1624   -419   -304    428
ATOM   2288  CB  LYS A 591      11.452  15.173  14.889  1.00 14.96           C  
ANISOU 2288  CB  LYS A 591     2222   1826   1633   -169    419   -108
ATOM   2289  CG  LYS A 591      11.342  16.484  14.105  1.00 15.19           C  
ANISOU 2289  CG  LYS A 591     2307   1727   1737   -281     46   -212
ATOM   2290  CD  LYS A 591      12.054  17.663  14.768  1.00 16.78           C  
ANISOU 2290  CD  LYS A 591     2408   1317   2649   -242    550   -595
ATOM   2291  CE  LYS A 591      11.886  18.937  13.935  1.00 17.45           C  
ANISOU 2291  CE  LYS A 591     2546   1923   2158   -268    409   -262
ATOM   2292  NZ  LYS A 591      12.666  20.046  14.491  1.00 16.37           N1+
ANISOU 2292  NZ  LYS A 591     2413   1540   2263   -265    468     65
ATOM   2293  H   LYS A 591      13.110  13.594  13.151  1.00  0.00           H  
ATOM   2294  HA  LYS A 591      13.492  15.211  15.626  1.00  0.00           H  
ATOM   2295  HB3 LYS A 591      11.043  15.322  15.890  1.00  0.00           H  
ATOM   2296  HB2 LYS A 591      10.785  14.463  14.409  1.00  0.00           H  
ATOM   2297  HG3 LYS A 591      10.288  16.733  13.993  1.00  0.00           H  
ATOM   2298  HG2 LYS A 591      11.723  16.341  13.094  1.00  0.00           H  
ATOM   2299  HD3 LYS A 591      13.111  17.433  14.897  1.00  0.00           H  
ATOM   2300  HD2 LYS A 591      11.647  17.808  15.769  1.00  0.00           H  
ATOM   2301  HE3 LYS A 591      10.837  19.227  13.883  1.00  0.00           H  
ATOM   2302  HE2 LYS A 591      12.230  18.767  12.917  1.00  0.00           H  
ATOM   2303  HZ1 LYS A 591      12.316  20.271  15.414  1.00  0.00           H  
ATOM   2304  HZ2 LYS A 591      13.637  19.770  14.569  1.00  0.00           H  
ATOM   2305  HZ3 LYS A 591      12.591  20.861  13.896  1.00  0.00           H  
ATOM   2306  N   ILE A 592      13.634  12.954  16.659  1.00 12.03           N  
ANISOU 2306  N   ILE A 592     1981   1418   1172   -197   -111    -21
ATOM   2307  CA  ILE A 592      13.646  11.718  17.432  1.00 13.04           C  
ANISOU 2307  CA  ILE A 592     1849   1317   1787   -284    111    100
ATOM   2308  C   ILE A 592      12.621  11.822  18.574  1.00 12.86           C  
ANISOU 2308  C   ILE A 592     1522   1504   1859   -185   -158   -188
ATOM   2309  O   ILE A 592      12.583  12.824  19.287  1.00 14.65           O  
ANISOU 2309  O   ILE A 592     2192   1646   1728    -74    345   -159
ATOM   2310  CB  ILE A 592      15.055  11.419  18.017  1.00 13.63           C  
ANISOU 2310  CB  ILE A 592     1704   1691   1780      3    354    110
ATOM   2311  CG1 ILE A 592      16.089  11.251  16.880  1.00 15.85           C  
ANISOU 2311  CG1 ILE A 592     1772   1542   2709    309    716     52
ATOM   2312  CG2 ILE A 592      15.086  10.182  18.940  1.00 15.00           C  
ANISOU 2312  CG2 ILE A 592     2042   2190   1467   -152     14    287
ATOM   2313  CD1 ILE A 592      17.543  11.176  17.358  1.00 19.27           C  
ANISOU 2313  CD1 ILE A 592     2058   1982   3282    291    313   -280
ATOM   2314  H   ILE A 592      14.300  13.663  16.938  1.00  0.00           H  
ATOM   2315  HA  ILE A 592      13.376  10.886  16.779  1.00  0.00           H  
ATOM   2316  HB  ILE A 592      15.356  12.279  18.613  1.00  0.00           H  
ATOM   2317 HG13 ILE A 592      16.015  12.077  16.175  1.00  0.00           H  
ATOM   2318 HG12 ILE A 592      15.852  10.353  16.307  1.00  0.00           H  
ATOM   2319 HG21 ILE A 592      16.096   9.972  19.292  1.00  0.00           H  
ATOM   2320 HG22 ILE A 592      14.478  10.313  19.834  1.00  0.00           H  
ATOM   2321 HG23 ILE A 592      14.729   9.294  18.417  1.00  0.00           H  
ATOM   2322 HD11 ILE A 592      18.183  11.808  16.745  1.00  0.00           H  
ATOM   2323 HD12 ILE A 592      17.658  11.499  18.393  1.00  0.00           H  
ATOM   2324 HD13 ILE A 592      17.915  10.155  17.282  1.00  0.00           H  
ATOM   2325  N   GLY A 593      11.816  10.768  18.715  1.00 13.92           N  
ANISOU 2325  N   GLY A 593     2156   1696   1435   -496   -235   -106
ATOM   2326  CA  GLY A 593      10.794  10.644  19.743  1.00 16.36           C  
ANISOU 2326  CA  GLY A 593     2307   1735   2173   -187    253   -209
ATOM   2327  C   GLY A 593      10.404   9.170  19.830  1.00 13.08           C  
ANISOU 2327  C   GLY A 593     1792   1882   1295   -139     81    -18
ATOM   2328  O   GLY A 593      10.984   8.329  19.147  1.00 14.66           O  
ANISOU 2328  O   GLY A 593     1971   1745   1853    -51    -31     13
ATOM   2329  H   GLY A 593      11.911   9.980  18.086  1.00  0.00           H  
ATOM   2330  HA3 GLY A 593       9.925  11.240  19.470  1.00  0.00           H  
ATOM   2331  HA2 GLY A 593      11.153  10.990  20.708  1.00  0.00           H  
ATOM   2332  N   ASP A 594       9.390   8.866  20.648  1.00 14.91           N  
ANISOU 2332  N   ASP A 594     1341   2191   2130     84    234   -229
ATOM   2333  CA  ASP A 594       8.684   7.589  20.613  1.00 13.04           C  
ANISOU 2333  CA  ASP A 594     1583   1609   1760    477    506   -131
ATOM   2334  C   ASP A 594       7.284   7.915  20.083  1.00 12.90           C  
ANISOU 2334  C   ASP A 594     1699   1623   1580    -98    212   -115
ATOM   2335  O   ASP A 594       6.467   8.477  20.811  1.00 14.94           O  
ANISOU 2335  O   ASP A 594     2137   2116   1420    -23    394   -212
ATOM   2336  CB  ASP A 594       8.658   6.881  21.984  1.00 17.03           C  
ANISOU 2336  CB  ASP A 594     1994   2070   2405     23    443    719
ATOM   2337  CG  ASP A 594       8.309   5.391  21.889  1.00 21.45           C  
ANISOU 2337  CG  ASP A 594     2791   2021   3336    -12   -359    123
ATOM   2338  OD1 ASP A 594       7.132   5.078  21.603  1.00 20.02           O  
ANISOU 2338  OD1 ASP A 594     2373   2257   2976   -586    174    670
ATOM   2339  OD2 ASP A 594       9.258   4.584  21.970  1.00 22.86           O1-
ANISOU 2339  OD2 ASP A 594     2893   2403   3388    -37   -166    467
ATOM   2340  H   ASP A 594       8.961   9.591  21.209  1.00  0.00           H  
ATOM   2341  HA  ASP A 594       9.162   6.906  19.910  1.00  0.00           H  
ATOM   2342  HB3 ASP A 594       7.936   7.357  22.644  1.00  0.00           H  
ATOM   2343  HB2 ASP A 594       9.621   7.006  22.482  1.00  0.00           H  
ATOM   2344  N   PHE A 595       7.070   7.589  18.802  1.00 16.60           N  
ANISOU 2344  N   PHE A 595     2443   1756   2108   -511     43   -570
ATOM   2345  CA  PHE A 595       5.868   7.904  18.034  1.00 16.15           C  
ANISOU 2345  CA  PHE A 595     2564   1625   1947    285     14   -417
ATOM   2346  C   PHE A 595       4.774   6.818  18.114  1.00 15.56           C  
ANISOU 2346  C   PHE A 595     2554   1442   1913    420     56   -612
ATOM   2347  O   PHE A 595       3.670   7.067  17.628  1.00 19.71           O  
ANISOU 2347  O   PHE A 595     2287   2212   2988   -139     88    244
ATOM   2348  CB  PHE A 595       6.278   8.206  16.575  1.00 15.75           C  
ANISOU 2348  CB  PHE A 595     2086   2112   1786    -10   -103   -366
ATOM   2349  CG  PHE A 595       7.028   9.517  16.372  1.00 14.89           C  
ANISOU 2349  CG  PHE A 595     2042   1749   1864    415    187   -429
ATOM   2350  CD1 PHE A 595       8.406   9.617  16.657  1.00 16.88           C  
ANISOU 2350  CD1 PHE A 595     2131   2208   2075   -176   -172    287
ATOM   2351  CE1 PHE A 595       9.063  10.831  16.511  1.00 14.68           C  
ANISOU 2351  CE1 PHE A 595     1686   1716   2175    543    126    526
ATOM   2352  CZ  PHE A 595       8.359  11.970  16.146  1.00 15.80           C  
ANISOU 2352  CZ  PHE A 595     1984   1600   2418    631    100    183
ATOM   2353  CD2 PHE A 595       6.323  10.689  16.029  1.00 18.87           C  
ANISOU 2353  CD2 PHE A 595     2009   1809   3350    226    437    308
ATOM   2354  CE2 PHE A 595       6.992  11.901  15.913  1.00 17.28           C  
ANISOU 2354  CE2 PHE A 595     1959   1451   3155    395    270    404
ATOM   2355  H   PHE A 595       7.799   7.108  18.291  1.00  0.00           H  
ATOM   2356  HA  PHE A 595       5.419   8.814  18.437  1.00  0.00           H  
ATOM   2357  HB3 PHE A 595       5.397   8.225  15.931  1.00  0.00           H  
ATOM   2358  HB2 PHE A 595       6.903   7.396  16.195  1.00  0.00           H  
ATOM   2359  HD1 PHE A 595       8.957   8.754  16.994  1.00  0.00           H  
ATOM   2360  HE1 PHE A 595      10.124  10.894  16.693  1.00  0.00           H  
ATOM   2361  HZ  PHE A 595       8.876  12.914  16.046  1.00  0.00           H  
ATOM   2362  HD2 PHE A 595       5.263  10.642  15.837  1.00  0.00           H  
ATOM   2363  HE2 PHE A 595       6.446  12.791  15.636  1.00  0.00           H  
ATOM   2364  N   GLY A 596       5.066   5.660  18.738  1.00 17.99           N  
ANISOU 2364  N   GLY A 596     2231   1833   2769    359     61    -50
ATOM   2365  CA  GLY A 596       4.121   4.556  18.944  1.00 22.19           C  
ANISOU 2365  CA  GLY A 596     2576   2392   3461    -65   -320   -557
ATOM   2366  C   GLY A 596       3.663   3.945  17.608  1.00 22.16           C  
ANISOU 2366  C   GLY A 596     2320   2200   3896   -449    151  -1329
ATOM   2367  O   GLY A 596       4.466   3.813  16.686  1.00 21.47           O  
ANISOU 2367  O   GLY A 596     2056   2690   3409    106   -105   -996
ATOM   2368  H   GLY A 596       5.991   5.534  19.125  1.00  0.00           H  
ATOM   2369  HA3 GLY A 596       3.271   4.913  19.523  1.00  0.00           H  
ATOM   2370  HA2 GLY A 596       4.611   3.781  19.535  1.00  0.00           H  
ATOM   2371  N   LEU A 597       2.378   3.569  17.510  1.00 22.89           N  
ANISOU 2371  N   LEU A 597     2203   2542   3950   -472    503  -1199
ATOM   2372  CA  LEU A 597       1.755   3.073  16.278  1.00 25.52           C  
ANISOU 2372  CA  LEU A 597     3250   2737   3708   -177    442  -1275
ATOM   2373  C   LEU A 597       0.905   4.155  15.604  1.00 21.51           C  
ANISOU 2373  C   LEU A 597     2019   3188   2964   -352    659   -763
ATOM   2374  O   LEU A 597       0.308   4.984  16.288  1.00 19.41           O  
ANISOU 2374  O   LEU A 597     1610   3004   2761     68   -115   -860
ATOM   2375  CB  LEU A 597       0.801   1.901  16.585  1.00 32.07           C  
ANISOU 2375  CB  LEU A 597     3546   2487   6150   -368    714  -1661
ATOM   2376  CG  LEU A 597       1.433   0.613  17.126  1.00 40.08           C  
ANISOU 2376  CG  LEU A 597     4144   4514   6568   -100    737   -170
ATOM   2377  CD1 LEU A 597       0.355  -0.482  17.208  1.00 52.28           C  
ANISOU 2377  CD1 LEU A 597     4925   5765   9174   -810    867    765
ATOM   2378  CD2 LEU A 597       2.640   0.137  16.294  1.00 44.42           C  
ANISOU 2378  CD2 LEU A 597     5754   5910   5214  -1771   1691  -1936
ATOM   2379  H   LEU A 597       1.750   3.734  18.287  1.00  0.00           H  
ATOM   2380  HA  LEU A 597       2.516   2.750  15.567  1.00  0.00           H  
ATOM   2381  HB3 LEU A 597       0.266   1.644  15.669  1.00  0.00           H  
ATOM   2382  HB2 LEU A 597       0.042   2.233  17.295  1.00  0.00           H  
ATOM   2383  HG  LEU A 597       1.769   0.822  18.140  1.00  0.00           H  
ATOM   2384 HD11 LEU A 597       0.778  -1.476  17.338  1.00  0.00           H  
ATOM   2385 HD12 LEU A 597      -0.317  -0.299  18.044  1.00  0.00           H  
ATOM   2386 HD13 LEU A 597      -0.252  -0.519  16.305  1.00  0.00           H  
ATOM   2387 HD21 LEU A 597       2.733  -0.949  16.286  1.00  0.00           H  
ATOM   2388 HD22 LEU A 597       2.562   0.456  15.255  1.00  0.00           H  
ATOM   2389 HD23 LEU A 597       3.572   0.538  16.694  1.00  0.00           H  
ATOM   2390  N   ALA A 598       0.777   4.025  14.276  1.00 27.87           N  
ANISOU 2390  N   ALA A 598     3562   3653   3373    242   -417   -970
ATOM   2391  CA  ALA A 598      -0.233   4.692  13.457  1.00 24.75           C  
ANISOU 2391  CA  ALA A 598     3748   3157   2496    227   -439  -1261
ATOM   2392  C   ALA A 598      -0.876   3.720  12.451  1.00 22.76           C  
ANISOU 2392  C   ALA A 598     1998   3538   3111   -337    -94  -1129
ATOM   2393  O   ALA A 598      -1.407   4.166  11.434  1.00 29.12           O  
ANISOU 2393  O   ALA A 598     2973   5040   3051   -263    460   -757
ATOM   2394  CB  ALA A 598       0.351   5.952  12.806  1.00 26.07           C  
ANISOU 2394  CB  ALA A 598     2816   4102   2985     69   -111   -926
ATOM   2395  H   ALA A 598       1.326   3.320  13.798  1.00  0.00           H  
ATOM   2396  HA  ALA A 598      -1.056   5.008  14.099  1.00  0.00           H  
ATOM   2397  HB1 ALA A 598      -0.386   6.472  12.194  1.00  0.00           H  
ATOM   2398  HB2 ALA A 598       0.673   6.654  13.571  1.00  0.00           H  
ATOM   2399  HB3 ALA A 598       1.208   5.721  12.175  1.00  0.00           H  
ATOM   2400  N   THR A 599      -0.870   2.414  12.780  1.00 24.53           N  
ANISOU 2400  N   THR A 599     2058   3491   3771    139   -233  -1338
ATOM   2401  CA  THR A 599      -1.645   1.368  12.105  1.00 26.84           C  
ANISOU 2401  CA  THR A 599     1895   4488   3813      4   -515  -1671
ATOM   2402  C   THR A 599      -3.161   1.601  12.285  1.00 24.28           C  
ANISOU 2402  C   THR A 599     1730   4229   3263   -468   -296  -1453
ATOM   2403  O   THR A 599      -3.564   2.296  13.217  1.00 24.86           O  
ANISOU 2403  O   THR A 599     2333   3014   4096   -483    685  -1309
ATOM   2404  CB  THR A 599      -1.301  -0.042  12.672  1.00 30.02           C  
ANISOU 2404  CB  THR A 599     2532   4493   4379    226   -516  -1300
ATOM   2405  OG1 THR A 599      -1.846  -0.292  13.958  1.00 28.61           O  
ANISOU 2405  OG1 THR A 599     2966   2787   5118    326     36   -805
ATOM   2406  CG2 THR A 599       0.198  -0.372  12.691  1.00 32.81           C  
ANISOU 2406  CG2 THR A 599     2623   4529   5314     15   -527  -1976
ATOM   2407  H   THR A 599      -0.411   2.128  13.633  1.00  0.00           H  
ATOM   2408  HA  THR A 599      -1.408   1.396  11.040  1.00  0.00           H  
ATOM   2409  HB  THR A 599      -1.763  -0.773  12.009  1.00  0.00           H  
ATOM   2410  HG1 THR A 599      -1.486  -1.120  14.287  1.00  0.00           H  
ATOM   2411 HG21 THR A 599       0.368  -1.415  12.960  1.00  0.00           H  
ATOM   2412 HG22 THR A 599       0.649  -0.204  11.712  1.00  0.00           H  
ATOM   2413 HG23 THR A 599       0.732   0.242  13.417  1.00  0.00           H  
ATOM   2414  N   GLU A 600      -3.984   1.013  11.403  1.00 28.96           N  
ANISOU 2414  N   GLU A 600     2575   4732   3696   -211   -350  -2622
ATOM   2415  CA  GLU A 600      -5.438   1.164  11.468  1.00 27.25           C  
ANISOU 2415  CA  GLU A 600     2505   4058   3791    112    202  -2370
ATOM   2416  C   GLU A 600      -6.051   0.574  12.753  1.00 23.54           C  
ANISOU 2416  C   GLU A 600     2235   2474   4234   -177   -831  -1410
ATOM   2417  O   GLU A 600      -6.932   1.210  13.326  1.00 26.42           O  
ANISOU 2417  O   GLU A 600     2841   2617   4579   -182   -192  -1511
ATOM   2418  CB  GLU A 600      -6.090   0.618  10.179  1.00 26.82           C  
ANISOU 2418  CB  GLU A 600     2008   3736   4444   -520   -260  -1795
ATOM   2419  CG  GLU A 600      -7.611   0.878  10.059  1.00 27.80           C  
ANISOU 2419  CG  GLU A 600     1949   4334   4279   -443   -260  -1467
ATOM   2420  CD  GLU A 600      -8.007   2.364  10.063  1.00 28.62           C  
ANISOU 2420  CD  GLU A 600     3488   3634   3752  -1590    622   -536
ATOM   2421  OE1 GLU A 600      -9.043   2.674  10.689  1.00 32.02           O  
ANISOU 2421  OE1 GLU A 600     3873   4192   4101   -271    148   -307
ATOM   2422  OE2 GLU A 600      -7.285   3.179   9.446  1.00 29.17           O1-
ANISOU 2422  OE2 GLU A 600     2700   4020   4360   -366   1451    158
ATOM   2423  H   GLU A 600      -3.613   0.460  10.641  1.00  0.00           H  
ATOM   2424  HA  GLU A 600      -5.619   2.240  11.503  1.00  0.00           H  
ATOM   2425  HB3 GLU A 600      -5.915  -0.457  10.120  1.00  0.00           H  
ATOM   2426  HB2 GLU A 600      -5.583   1.038   9.309  1.00  0.00           H  
ATOM   2427  HG3 GLU A 600      -8.143   0.346  10.849  1.00  0.00           H  
ATOM   2428  HG2 GLU A 600      -7.970   0.447   9.124  1.00  0.00           H  
ATOM   2429  N   LYS A 601      -5.526  -0.571  13.226  1.00 24.99           N  
ANISOU 2429  N   LYS A 601     1892   2540   5062    166  -1043  -1339
ATOM   2430  CA  LYS A 601      -5.899  -1.177  14.509  1.00 28.42           C  
ANISOU 2430  CA  LYS A 601     2767   3193   4835    -49   -127  -2185
ATOM   2431  C   LYS A 601      -5.574  -0.297  15.731  1.00 25.92           C  
ANISOU 2431  C   LYS A 601     2499   3272   4075   -135    363  -1969
ATOM   2432  O   LYS A 601      -6.335  -0.340  16.697  1.00 24.56           O  
ANISOU 2432  O   LYS A 601     2469   3341   3520   -103    187   -474
ATOM   2433  CB  LYS A 601      -5.229  -2.555  14.667  1.00  0.00           C  
ATOM   2434  CG  LYS A 601      -5.663  -3.633  13.657  1.00  0.00           C  
ATOM   2435  CD  LYS A 601      -7.167  -3.969  13.676  1.00  0.00           C  
ATOM   2436  CE  LYS A 601      -7.539  -5.233  12.880  1.00  0.00           C  
ATOM   2437  NZ  LYS A 601      -7.010  -6.468  13.493  1.00  0.00           N1+
ATOM   2438  H   LYS A 601      -4.796  -1.036  12.703  1.00  0.00           H  
ATOM   2439  HA  LYS A 601      -6.982  -1.310  14.500  1.00  0.00           H  
ATOM   2440  HB2 LYS A 601      -4.145  -2.438  14.619  1.00  0.00           H  
ATOM   2441  HB3 LYS A 601      -5.442  -2.931  15.668  1.00  0.00           H  
ATOM   2442  HG2 LYS A 601      -5.400  -3.319  12.650  1.00  0.00           H  
ATOM   2443  HG3 LYS A 601      -5.071  -4.527  13.847  1.00  0.00           H  
ATOM   2444  HD2 LYS A 601      -7.530  -4.040  14.699  1.00  0.00           H  
ATOM   2445  HD3 LYS A 601      -7.712  -3.132  13.238  1.00  0.00           H  
ATOM   2446  HE2 LYS A 601      -8.624  -5.323  12.826  1.00  0.00           H  
ATOM   2447  HE3 LYS A 601      -7.175  -5.157  11.855  1.00  0.00           H  
ATOM   2448  HZ1 LYS A 601      -7.365  -6.555  14.435  1.00  0.00           H  
ATOM   2449  HZ2 LYS A 601      -7.298  -7.269  12.949  1.00  0.00           H  
ATOM   2450  HZ3 LYS A 601      -6.001  -6.427  13.522  1.00  0.00           H  
ATOM   2451  N   SER A 602      -4.500   0.512  15.659  1.00 28.31           N  
ANISOU 2451  N   SER A 602     2623   3534   4598   -493   -863  -1989
ATOM   2452  CA  SER A 602      -4.130   1.474  16.702  1.00 24.93           C  
ANISOU 2452  CA  SER A 602     1989   3199   4282   -214  -1171  -1580
ATOM   2453  C   SER A 602      -5.086   2.664  16.862  1.00 23.79           C  
ANISOU 2453  C   SER A 602     2340   3006   3691   -149   -466   -650
ATOM   2454  O   SER A 602      -5.016   3.336  17.889  1.00 24.78           O  
ANISOU 2454  O   SER A 602     2869   3166   3378    -41   -249   -715
ATOM   2455  CB  SER A 602      -2.649   1.881  16.573  1.00 25.06           C  
ANISOU 2455  CB  SER A 602     1843   3416   4259    188   -978   -694
ATOM   2456  OG  SER A 602      -2.412   2.902  15.630  1.00 22.50           O  
ANISOU 2456  OG  SER A 602     2155   2598   3795   -114   -940  -1071
ATOM   2457  H   SER A 602      -3.916   0.500  14.833  1.00  0.00           H  
ATOM   2458  HA  SER A 602      -4.227   0.946  17.639  1.00  0.00           H  
ATOM   2459  HB3 SER A 602      -2.032   1.014  16.348  1.00  0.00           H  
ATOM   2460  HB2 SER A 602      -2.303   2.267  17.530  1.00  0.00           H  
ATOM   2461  HG  SER A 602      -2.713   2.601  14.765  1.00  0.00           H  
ATOM   2462  N   ARG A 603      -5.973   2.877  15.878  1.00 19.89           N  
ANISOU 2462  N   ARG A 603     2401   2171   2983    -60   -381  -1193
ATOM   2463  CA  ARG A 603      -7.026   3.889  15.908  1.00 21.36           C  
ANISOU 2463  CA  ARG A 603     2307   2592   3214      1     52   -534
ATOM   2464  C   ARG A 603      -8.317   3.416  16.606  1.00 18.72           C  
ANISOU 2464  C   ARG A 603     1732   2937   2442    368   -338   -674
ATOM   2465  O   ARG A 603      -9.218   4.236  16.776  1.00 21.81           O  
ANISOU 2465  O   ARG A 603     1886   2703   3698    375    328   -491
ATOM   2466  CB  ARG A 603      -7.321   4.370  14.476  1.00 19.74           C  
ANISOU 2466  CB  ARG A 603     1991   3236   2271      6   -186  -1277
ATOM   2467  CG  ARG A 603      -6.079   4.908  13.737  1.00 21.58           C  
ANISOU 2467  CG  ARG A 603     1856   3860   2483     14     25  -1391
ATOM   2468  CD  ARG A 603      -6.373   5.395  12.310  1.00 24.82           C  
ANISOU 2468  CD  ARG A 603     3273   3736   2421    -72    239  -1295
ATOM   2469  NE  ARG A 603      -7.199   6.617  12.302  1.00 26.11           N  
ANISOU 2469  NE  ARG A 603     2547   3921   3453   -175      3   -210
ATOM   2470  CZ  ARG A 603      -8.524   6.748  12.089  1.00 25.63           C  
ANISOU 2470  CZ  ARG A 603     2439   3331   3966   -415   -108     32
ATOM   2471  NH1 ARG A 603      -9.325   5.716  11.786  1.00 23.72           N  
ANISOU 2471  NH1 ARG A 603     2081   3092   3837     15    -71    -82
ATOM   2472  NH2 ARG A 603      -9.067   7.968  12.185  1.00 21.78           N1+
ANISOU 2472  NH2 ARG A 603     2009   3449   2818   -324   -498   -467
ATOM   2473  H   ARG A 603      -5.968   2.272  15.067  1.00  0.00           H  
ATOM   2474  HA  ARG A 603      -6.652   4.748  16.460  1.00  0.00           H  
ATOM   2475  HB3 ARG A 603      -8.077   5.155  14.520  1.00  0.00           H  
ATOM   2476  HB2 ARG A 603      -7.769   3.564  13.895  1.00  0.00           H  
ATOM   2477  HG3 ARG A 603      -5.269   4.182  13.706  1.00  0.00           H  
ATOM   2478  HG2 ARG A 603      -5.694   5.744  14.322  1.00  0.00           H  
ATOM   2479  HD3 ARG A 603      -6.913   4.611  11.786  1.00  0.00           H  
ATOM   2480  HD2 ARG A 603      -5.451   5.536  11.747  1.00  0.00           H  
ATOM   2481  HE  ARG A 603      -6.697   7.460  12.547  1.00  0.00           H  
ATOM   2482 HH12 ARG A 603     -10.310   5.856  11.621  1.00  0.00           H  
ATOM   2483 HH11 ARG A 603      -8.935   4.790  11.659  1.00  0.00           H  
ATOM   2484 HH22 ARG A 603     -10.052   8.107  12.014  1.00  0.00           H  
ATOM   2485 HH21 ARG A 603      -8.484   8.765  12.402  1.00  0.00           H  
ATOM   2486  N   TRP A 604      -8.394   2.132  17.002  1.00 21.16           N  
ANISOU 2486  N   TRP A 604     2137   3063   2838   -161   -299   -688
ATOM   2487  CA  TRP A 604      -9.564   1.517  17.642  1.00 21.32           C  
ANISOU 2487  CA  TRP A 604     2306   2670   3122   -295   -432   -259
ATOM   2488  C   TRP A 604      -9.155   0.732  18.901  1.00 26.34           C  
ANISOU 2488  C   TRP A 604     2587   3760   3658   -174   -813    497
ATOM   2489  O   TRP A 604      -8.008   0.833  19.330  1.00 37.38           O  
ANISOU 2489  O   TRP A 604     3928   5561   4711  -2325  -1488    832
ATOM   2490  CB  TRP A 604     -10.330   0.653  16.615  1.00 22.20           C  
ANISOU 2490  CB  TRP A 604     1986   3412   3036   -270   -469   -380
ATOM   2491  CG  TRP A 604     -10.667   1.338  15.326  1.00 22.53           C  
ANISOU 2491  CG  TRP A 604     1711   3736   3112   -238   -291   -191
ATOM   2492  CD1 TRP A 604      -9.999   1.169  14.165  1.00 20.66           C  
ANISOU 2492  CD1 TRP A 604     1564   2934   3351    115   -143   -267
ATOM   2493  NE1 TRP A 604     -10.503   2.025  13.212  1.00 22.52           N  
ANISOU 2493  NE1 TRP A 604     1908   3953   2693   -296     27    244
ATOM   2494  CE2 TRP A 604     -11.548   2.778  13.702  1.00 22.60           C  
ANISOU 2494  CE2 TRP A 604     2026   3768   2792   -212   -533   -340
ATOM   2495  CD2 TRP A 604     -11.677   2.359  15.061  1.00 22.60           C  
ANISOU 2495  CD2 TRP A 604     2009   3517   3058     12     -3   -162
ATOM   2496  CE3 TRP A 604     -12.684   2.987  15.831  1.00 21.93           C  
ANISOU 2496  CE3 TRP A 604     2351   2991   2988   -144    209   -483
ATOM   2497  CZ3 TRP A 604     -13.527   3.969  15.271  1.00 22.69           C  
ANISOU 2497  CZ3 TRP A 604     2638   3205   2778   -164    132     37
ATOM   2498  CH2 TRP A 604     -13.376   4.355  13.925  1.00 21.85           C  
ANISOU 2498  CH2 TRP A 604     2782   3159   2359     90   -233   -726
ATOM   2499  CZ2 TRP A 604     -12.377   3.760  13.133  1.00 21.25           C  
ANISOU 2499  CZ2 TRP A 604     2436   2978   2658    -71   -365   -875
ATOM   2500  H   TRP A 604      -7.602   1.521  16.858  1.00  0.00           H  
ATOM   2501  HA  TRP A 604     -10.237   2.303  17.986  1.00  0.00           H  
ATOM   2502  HB3 TRP A 604     -11.262   0.288  17.048  1.00  0.00           H  
ATOM   2503  HB2 TRP A 604      -9.741  -0.229  16.369  1.00  0.00           H  
ATOM   2504  HD1 TRP A 604      -9.184   0.475  14.031  1.00  0.00           H  
ATOM   2505  HE1 TRP A 604     -10.116   2.088  12.274  1.00  0.00           H  
ATOM   2506  HE3 TRP A 604     -12.812   2.704  16.864  1.00  0.00           H  
ATOM   2507  HZ3 TRP A 604     -14.291   4.430  15.880  1.00  0.00           H  
ATOM   2508  HH2 TRP A 604     -14.023   5.109  13.502  1.00  0.00           H  
ATOM   2509  HZ2 TRP A 604     -12.250   4.050  12.100  1.00  0.00           H  
ATOM   2510  N   SER A 605     -10.121   0.020  19.504  1.00 31.77           N  
ANISOU 2510  N   SER A 605     2831   5071   4165   -275    484   -206
ATOM   2511  CA  SER A 605     -10.026  -0.537  20.860  1.00 35.22           C  
ANISOU 2511  CA  SER A 605     4060   4334   4985   -381   1382    929
ATOM   2512  C   SER A 605      -9.622  -2.024  20.961  1.00 40.60           C  
ANISOU 2512  C   SER A 605     5910   3348   6167   -739   1385  -1841
ATOM   2513  O   SER A 605      -9.560  -2.533  22.080  1.00 64.13           O  
ANISOU 2513  O   SER A 605    12599   5075   6692     62   3681   -639
ATOM   2514  CB  SER A 605     -11.369  -0.278  21.574  1.00 38.62           C  
ANISOU 2514  CB  SER A 605     3373   6473   4826   1119    453    292
ATOM   2515  OG  SER A 605     -11.428   1.071  21.986  1.00 42.36           O  
ANISOU 2515  OG  SER A 605     5132   7264   3696    588   -450   -319
ATOM   2516  H   SER A 605     -11.041  -0.004  19.089  1.00  0.00           H  
ATOM   2517  HA  SER A 605      -9.256   0.001  21.411  1.00  0.00           H  
ATOM   2518  HB3 SER A 605     -11.479  -0.887  22.472  1.00  0.00           H  
ATOM   2519  HB2 SER A 605     -12.220  -0.507  20.931  1.00  0.00           H  
ATOM   2520  HG  SER A 605     -12.284   1.230  22.402  1.00  0.00           H  
ATOM   2521  N   GLY A 606      -9.361  -2.705  19.831  1.00 38.74           N  
ANISOU 2521  N   GLY A 606     3920   3614   7182  -1334   2547  -2298
ATOM   2522  CA  GLY A 606      -9.090  -4.147  19.780  1.00 51.86           C  
ANISOU 2522  CA  GLY A 606     6871   3927   8903   -231   -417  -1584
ATOM   2523  C   GLY A 606      -7.692  -4.534  20.305  1.00 55.10           C  
ANISOU 2523  C   GLY A 606     8994   4106   7832   1140  -1802  -2402
ATOM   2524  O   GLY A 606      -6.959  -3.711  20.854  1.00 48.06           O  
ANISOU 2524  O   GLY A 606    10269   2710   5281   -412   -908   -937
ATOM   2525  H   GLY A 606      -9.380  -2.216  18.947  1.00  0.00           H  
ATOM   2526  HA3 GLY A 606      -9.203  -4.479  18.750  1.00  0.00           H  
ATOM   2527  HA2 GLY A 606      -9.844  -4.681  20.360  1.00  0.00           H  
ATOM   2528  N   SER A 607      -7.339  -5.823  20.141  1.00 54.27           N  
ANISOU 2528  N   SER A 607     9838   4344   6439    655  -1448  -2674
ATOM   2529  CA  SER A 607      -6.098  -6.445  20.623  1.00 60.74           C  
ANISOU 2529  CA  SER A 607     8101   7714   7263    614   -368  -1409
ATOM   2530  C   SER A 607      -4.791  -5.888  20.016  1.00 58.67           C  
ANISOU 2530  C   SER A 607     5935   8558   7799    323  -2373   -429
ATOM   2531  O   SER A 607      -3.779  -5.866  20.717  1.00 64.45           O  
ANISOU 2531  O   SER A 607     8528   7794   8165   2058  -4515  -1656
ATOM   2532  CB  SER A 607      -6.206  -7.977  20.456  1.00 51.04           C  
ANISOU 2532  CB  SER A 607     6110   6786   6497   3078   1040  -1581
ATOM   2533  OG  SER A 607      -6.148  -8.380  19.100  1.00 51.85           O  
ANISOU 2533  OG  SER A 607     9647   4712   5340    628  -1164  -1854
ATOM   2534  H   SER A 607      -7.979  -6.453  19.680  1.00  0.00           H  
ATOM   2535  HA  SER A 607      -6.054  -6.243  21.695  1.00  0.00           H  
ATOM   2536  HB3 SER A 607      -7.129  -8.350  20.900  1.00  0.00           H  
ATOM   2537  HB2 SER A 607      -5.390  -8.467  20.989  1.00  0.00           H  
ATOM   2538  HG  SER A 607      -5.253  -8.253  18.775  1.00  0.00           H  
ATOM   2539  N   HIS A 608      -4.836  -5.438  18.751  1.00 53.19           N  
ANISOU 2539  N   HIS A 608     4484   7202   8522  -1231   -775    777
ATOM   2540  CA  HIS A 608      -3.718  -4.814  18.034  1.00 40.66           C  
ANISOU 2540  CA  HIS A 608     5890   3128   6431   -509   -892    154
ATOM   2541  C   HIS A 608      -3.626  -3.289  18.257  1.00 44.82           C  
ANISOU 2541  C   HIS A 608     5828   3234   7967  -1841    847   -128
ATOM   2542  O   HIS A 608      -2.903  -2.636  17.501  1.00 45.97           O  
ANISOU 2542  O   HIS A 608     6567   4395   6502  -1056    562   1183
ATOM   2543  CB  HIS A 608      -3.809  -5.161  16.527  1.00  0.00           C  
ATOM   2544  CG  HIS A 608      -3.253  -6.501  16.130  1.00  0.00           C  
ATOM   2545  ND1 HIS A 608      -4.032  -7.660  16.077  1.00  0.00           N  
ATOM   2546  CD2 HIS A 608      -1.969  -6.803  15.727  1.00  0.00           C  
ATOM   2547  CE1 HIS A 608      -3.202  -8.603  15.650  1.00  0.00           C  
ATOM   2548  NE2 HIS A 608      -1.967  -8.152  15.424  1.00  0.00           N  
ATOM   2549  H   HIS A 608      -5.710  -5.484  18.242  1.00  0.00           H  
ATOM   2550  HA  HIS A 608      -2.774  -5.213  18.411  1.00  0.00           H  
ATOM   2551  HB2 HIS A 608      -4.842  -5.115  16.192  1.00  0.00           H  
ATOM   2552  HB3 HIS A 608      -3.272  -4.439  15.911  1.00  0.00           H  
ATOM   2553  HD2 HIS A 608      -1.089  -6.185  15.627  1.00  0.00           H  
ATOM   2554  HE1 HIS A 608      -3.497  -9.632  15.502  1.00  0.00           H  
ATOM   2555  HE2 HIS A 608      -1.181  -8.696  15.097  1.00  0.00           H  
ATOM   2556  N   GLN A 609      -4.328  -2.733  19.268  1.00 44.09           N  
ANISOU 2556  N   GLN A 609     6401   4663   5686  -1513   -506   -239
ATOM   2557  CA  GLN A 609      -4.318  -1.295  19.558  1.00 32.25           C  
ANISOU 2557  CA  GLN A 609     3879   4828   3545   -303  -1046   -551
ATOM   2558  C   GLN A 609      -2.917  -0.723  19.833  1.00 32.43           C  
ANISOU 2558  C   GLN A 609     3496   4353   4472   -197   -154  -1566
ATOM   2559  O   GLN A 609      -2.595   0.322  19.284  1.00 43.98           O  
ANISOU 2559  O   GLN A 609     4394   4958   7357  -1046  -2758   -421
ATOM   2560  CB  GLN A 609      -5.332  -0.903  20.656  1.00 30.36           C  
ANISOU 2560  CB  GLN A 609     3228   4012   4293     50   -548   -580
ATOM   2561  CG  GLN A 609      -5.326   0.614  20.994  1.00 35.90           C  
ANISOU 2561  CG  GLN A 609     4795   3816   5026    763   -671   -191
ATOM   2562  CD  GLN A 609      -6.359   1.072  22.027  1.00 43.92           C  
ANISOU 2562  CD  GLN A 609     6382   3447   6856   -253   1539    -46
ATOM   2563  OE1 GLN A 609      -6.576   2.272  22.178  1.00 52.70           O  
ANISOU 2563  OE1 GLN A 609     6982   3414   9625    885   2993    246
ATOM   2564  NE2 GLN A 609      -6.990   0.149  22.755  1.00 39.31           N  
ANISOU 2564  NE2 GLN A 609     3130   5592   6212   -679   -206    567
ATOM   2565  H   GLN A 609      -4.910  -3.311  19.859  1.00  0.00           H  
ATOM   2566  HA  GLN A 609      -4.680  -0.838  18.643  1.00  0.00           H  
ATOM   2567  HB3 GLN A 609      -5.134  -1.487  21.556  1.00  0.00           H  
ATOM   2568  HB2 GLN A 609      -6.331  -1.181  20.318  1.00  0.00           H  
ATOM   2569  HG3 GLN A 609      -5.480   1.191  20.081  1.00  0.00           H  
ATOM   2570  HG2 GLN A 609      -4.356   0.925  21.381  1.00  0.00           H  
ATOM   2571 HE22 GLN A 609      -7.668   0.429  23.448  1.00  0.00           H  
ATOM   2572 HE21 GLN A 609      -6.803  -0.833  22.611  1.00  0.00           H  
ATOM   2573  N   PHE A 610      -2.117  -1.409  20.656  1.00 38.59           N  
ANISOU 2573  N   PHE A 610     3238   5636   5788   -599   -305    167
ATOM   2574  CA  PHE A 610      -0.767  -0.981  21.029  1.00 43.72           C  
ANISOU 2574  CA  PHE A 610     4463   5444   6703  -1368   -974  -2059
ATOM   2575  C   PHE A 610       0.289  -1.881  20.378  1.00 51.56           C  
ANISOU 2575  C   PHE A 610     3721   6855   9013  -1394    853   -695
ATOM   2576  O   PHE A 610      -0.022  -3.018  20.014  1.00 44.07           O  
ANISOU 2576  O   PHE A 610     6142   6617   3984  -2002     21   -554
ATOM   2577  CB  PHE A 610      -0.658  -0.987  22.563  1.00 44.56           C  
ANISOU 2577  CB  PHE A 610     5551   4671   6709   1190  -1092  -1661
ATOM   2578  CG  PHE A 610      -1.459   0.112  23.240  1.00 47.71           C  
ANISOU 2578  CG  PHE A 610     5911   5557   6659    175   1268  -2080
ATOM   2579  CD1 PHE A 610      -0.916   1.409  23.347  1.00 42.35           C  
ANISOU 2579  CD1 PHE A 610     5606   4037   6446   1087  -2077   -102
ATOM   2580  CE1 PHE A 610      -1.669   2.432  23.903  1.00 43.29           C  
ANISOU 2580  CE1 PHE A 610     4767   3943   7735    636    -92   1544
ATOM   2581  CZ  PHE A 610      -2.976   2.202  24.312  1.00 51.24           C  
ANISOU 2581  CZ  PHE A 610     5770   6037   7660   1170   1280   -138
ATOM   2582  CD2 PHE A 610      -2.800  -0.101  23.624  1.00 44.19           C  
ANISOU 2582  CD2 PHE A 610     4425   5874   6490    -57   -763   -281
ATOM   2583  CE2 PHE A 610      -3.541   0.940  24.169  1.00 42.91           C  
ANISOU 2583  CE2 PHE A 610     4801   6736   4764    108    283    777
ATOM   2584  H   PHE A 610      -2.432  -2.285  21.047  1.00  0.00           H  
ATOM   2585  HA  PHE A 610      -0.568   0.036  20.684  1.00  0.00           H  
ATOM   2586  HB3 PHE A 610       0.384  -0.867  22.858  1.00  0.00           H  
ATOM   2587  HB2 PHE A 610      -0.972  -1.953  22.961  1.00  0.00           H  
ATOM   2588  HD1 PHE A 610       0.094   1.609  23.015  1.00  0.00           H  
ATOM   2589  HE1 PHE A 610      -1.227   3.408  24.017  1.00  0.00           H  
ATOM   2590  HZ  PHE A 610      -3.554   3.009  24.738  1.00  0.00           H  
ATOM   2591  HD2 PHE A 610      -3.254  -1.074  23.502  1.00  0.00           H  
ATOM   2592  HE2 PHE A 610      -4.561   0.771  24.477  1.00  0.00           H  
ATOM   2593  N   GLU A 611       1.520  -1.351  20.233  1.00 46.93           N  
ANISOU 2593  N   GLU A 611     3859   6411   7559  -1294    492    980
ATOM   2594  CA  GLU A 611       2.645  -2.078  19.634  1.00 50.78           C  
ANISOU 2594  CA  GLU A 611     5809   5527   7957    -93    427   2431
ATOM   2595  C   GLU A 611       3.035  -3.279  20.503  1.00 53.65           C  
ANISOU 2595  C   GLU A 611     7456   6530   6397   2237   -648   2133
ATOM   2596  O   GLU A 611       3.051  -3.186  21.731  1.00 60.93           O  
ANISOU 2596  O   GLU A 611     9623   6689   6836   1987   1091   2006
ATOM   2597  CB  GLU A 611       3.843  -1.134  19.356  1.00  0.00           C  
ATOM   2598  CG  GLU A 611       4.768  -0.800  20.547  1.00  0.00           C  
ATOM   2599  CD  GLU A 611       5.850   0.253  20.266  1.00  0.00           C  
ATOM   2600  OE1 GLU A 611       6.135   0.536  19.080  1.00  0.00           O  
ATOM   2601  OE2 GLU A 611       6.374   0.783  21.268  1.00  0.00           O1-
ATOM   2602  H   GLU A 611       1.716  -0.419  20.570  1.00  0.00           H  
ATOM   2603  HA  GLU A 611       2.303  -2.454  18.669  1.00  0.00           H  
ATOM   2604  HB2 GLU A 611       4.438  -1.568  18.551  1.00  0.00           H  
ATOM   2605  HB3 GLU A 611       3.468  -0.193  18.964  1.00  0.00           H  
ATOM   2606  HG2 GLU A 611       4.154  -0.444  21.370  1.00  0.00           H  
ATOM   2607  HG3 GLU A 611       5.278  -1.697  20.899  1.00  0.00           H  
ATOM   2608  N   GLN A 612       3.354  -4.378  19.816  1.00 49.61           N  
ANISOU 2608  N   GLN A 612     6345   6934   5568    966   1431   2067
ATOM   2609  CA  GLN A 612       3.924  -5.578  20.410  1.00 48.13           C  
ANISOU 2609  CA  GLN A 612     3485   6860   7940    580  -1012   1961
ATOM   2610  C   GLN A 612       5.457  -5.475  20.386  1.00 49.07           C  
ANISOU 2610  C   GLN A 612     3602   7844   7196    474   -158   2676
ATOM   2611  O   GLN A 612       6.010  -4.643  19.662  1.00 48.89           O  
ANISOU 2611  O   GLN A 612     5790   6643   6140   -240   -461   2200
ATOM   2612  CB  GLN A 612       3.423  -6.797  19.601  1.00  0.00           C  
ATOM   2613  CG  GLN A 612       1.890  -6.995  19.608  1.00  0.00           C  
ATOM   2614  CD  GLN A 612       1.313  -7.206  21.010  1.00  0.00           C  
ATOM   2615  OE1 GLN A 612       1.748  -8.100  21.732  1.00  0.00           O  
ATOM   2616  NE2 GLN A 612       0.324  -6.397  21.395  1.00  0.00           N  
ATOM   2617  H   GLN A 612       3.315  -4.362  18.807  1.00  0.00           H  
ATOM   2618  HA  GLN A 612       3.612  -5.673  21.452  1.00  0.00           H  
ATOM   2619  HB2 GLN A 612       3.750  -6.700  18.566  1.00  0.00           H  
ATOM   2620  HB3 GLN A 612       3.897  -7.705  19.975  1.00  0.00           H  
ATOM   2621  HG2 GLN A 612       1.399  -6.147  19.128  1.00  0.00           H  
ATOM   2622  HG3 GLN A 612       1.636  -7.868  19.006  1.00  0.00           H  
ATOM   2623 HE22 GLN A 612      -0.090  -6.505  22.309  1.00  0.00           H  
ATOM   2624 HE21 GLN A 612      -0.009  -5.663  20.785  1.00  0.00           H  
ATOM   2625  N   LEU A 613       6.119  -6.363  21.149  1.00 49.22           N  
ANISOU 2625  N   LEU A 613     4826   7024   6848    834    230   2437
ATOM   2626  CA  LEU A 613       7.579  -6.540  21.163  1.00 48.26           C  
ANISOU 2626  CA  LEU A 613     4090   7040   7204   -187   1566   2043
ATOM   2627  C   LEU A 613       8.161  -6.842  19.763  1.00 46.04           C  
ANISOU 2627  C   LEU A 613     4824   4779   7890   -496   1593  -1102
ATOM   2628  O   LEU A 613       9.284  -6.426  19.484  1.00 54.44           O  
ANISOU 2628  O   LEU A 613     4481   5649  10552    440   1058   2144
ATOM   2629  CB  LEU A 613       7.960  -7.665  22.159  1.00  0.00           C  
ATOM   2630  CG  LEU A 613       8.027  -7.246  23.648  1.00  0.00           C  
ATOM   2631  CD1 LEU A 613       6.685  -6.738  24.211  1.00  0.00           C  
ATOM   2632  CD2 LEU A 613       8.600  -8.393  24.510  1.00  0.00           C  
ATOM   2633  H   LEU A 613       5.594  -7.003  21.727  1.00  0.00           H  
ATOM   2634  HA  LEU A 613       8.026  -5.603  21.500  1.00  0.00           H  
ATOM   2635  HB2 LEU A 613       7.290  -8.518  22.035  1.00  0.00           H  
ATOM   2636  HB3 LEU A 613       8.952  -8.035  21.894  1.00  0.00           H  
ATOM   2637  HG  LEU A 613       8.736  -6.420  23.719  1.00  0.00           H  
ATOM   2638 HD11 LEU A 613       6.602  -6.899  25.286  1.00  0.00           H  
ATOM   2639 HD12 LEU A 613       6.576  -5.667  24.043  1.00  0.00           H  
ATOM   2640 HD13 LEU A 613       5.836  -7.237  23.743  1.00  0.00           H  
ATOM   2641 HD21 LEU A 613       9.481  -8.060  25.060  1.00  0.00           H  
ATOM   2642 HD22 LEU A 613       7.883  -8.764  25.243  1.00  0.00           H  
ATOM   2643 HD23 LEU A 613       8.904  -9.250  23.909  1.00  0.00           H  
ATOM   2644  N   SER A 614       7.357  -7.500  18.905  1.00 50.11           N  
ANISOU 2644  N   SER A 614     3068   9146   6825   -764   1843   -330
ATOM   2645  CA  SER A 614       7.623  -7.809  17.498  1.00 52.05           C  
ANISOU 2645  CA  SER A 614     4482   8536   6756  -1299    322   -743
ATOM   2646  C   SER A 614       7.882  -6.591  16.587  1.00 45.78           C  
ANISOU 2646  C   SER A 614     3030   3984  10378   -492   1060  -2715
ATOM   2647  O   SER A 614       8.548  -6.755  15.567  1.00 59.16           O  
ANISOU 2647  O   SER A 614     4238   5535  12705  -1334   2610  -2671
ATOM   2648  CB  SER A 614       6.466  -8.679  16.962  1.00 62.87           C  
ANISOU 2648  CB  SER A 614     6542   8606   8736  -2069  -2160    573
ATOM   2649  OG  SER A 614       5.271  -7.940  16.783  1.00 51.10           O  
ANISOU 2649  OG  SER A 614     8610   6108   4696  -1524    235   2650
ATOM   2650  H   SER A 614       6.440  -7.772  19.229  1.00  0.00           H  
ATOM   2651  HA  SER A 614       8.525  -8.421  17.480  1.00  0.00           H  
ATOM   2652  HB3 SER A 614       6.272  -9.518  17.631  1.00  0.00           H  
ATOM   2653  HB2 SER A 614       6.741  -9.111  15.999  1.00  0.00           H  
ATOM   2654  HG  SER A 614       4.593  -8.529  16.443  1.00  0.00           H  
ATOM   2655  N   GLY A 615       7.382  -5.400  16.962  1.00 32.47           N  
ANISOU 2655  N   GLY A 615     2105   3720   6509    -29    767   -585
ATOM   2656  CA  GLY A 615       7.561  -4.161  16.202  1.00 41.16           C  
ANISOU 2656  CA  GLY A 615     3722   5483   6432   -284    -83    409
ATOM   2657  C   GLY A 615       8.972  -3.566  16.350  1.00 37.23           C  
ANISOU 2657  C   GLY A 615     3004   6617   4522    603   -328   1402
ATOM   2658  O   GLY A 615       9.291  -2.615  15.636  1.00 55.01           O  
ANISOU 2658  O   GLY A 615     5263   8518   7118  -1086   2588   1313
ATOM   2659  H   GLY A 615       6.854  -5.333  17.822  1.00  0.00           H  
ATOM   2660  HA3 GLY A 615       6.836  -3.430  16.560  1.00  0.00           H  
ATOM   2661  HA2 GLY A 615       7.343  -4.332  15.146  1.00  0.00           H  
ATOM   2662  N   SER A 616       9.797  -4.110  17.263  1.00 20.38           N  
ANISOU 2662  N   SER A 616     2823   1848   3071   -161    466    339
ATOM   2663  CA  SER A 616      11.091  -3.560  17.661  1.00 20.87           C  
ANISOU 2663  CA  SER A 616     2958   2156   2813   -516    314   -331
ATOM   2664  C   SER A 616      12.250  -4.561  17.504  1.00 19.41           C  
ANISOU 2664  C   SER A 616     3039   1806   2530   -633    555   -358
ATOM   2665  O   SER A 616      13.394  -4.121  17.615  1.00 17.77           O  
ANISOU 2665  O   SER A 616     2381   2112   2257   -132    319     -2
ATOM   2666  CB  SER A 616      10.976  -3.116  19.131  1.00 23.31           C  
ANISOU 2666  CB  SER A 616     2913   2602   3342    233    211  -1205
ATOM   2667  OG  SER A 616      10.037  -2.070  19.249  1.00 23.96           O  
ANISOU 2667  OG  SER A 616     2785   2140   4179    -75   -102   -551
ATOM   2668  H   SER A 616       9.460  -4.881  17.823  1.00  0.00           H  
ATOM   2669  HA  SER A 616      11.347  -2.688  17.057  1.00  0.00           H  
ATOM   2670  HB3 SER A 616      11.934  -2.759  19.513  1.00  0.00           H  
ATOM   2671  HB2 SER A 616      10.660  -3.940  19.770  1.00  0.00           H  
ATOM   2672  HG  SER A 616      10.508  -1.263  19.497  1.00  0.00           H  
ATOM   2673  N   ILE A 617      11.967  -5.860  17.263  1.00 17.85           N  
ANISOU 2673  N   ILE A 617     2820   1849   2112   -800    331     29
ATOM   2674  CA  ILE A 617      12.968  -6.939  17.254  1.00 21.30           C  
ANISOU 2674  CA  ILE A 617     3663   2266   2162   -193    611    446
ATOM   2675  C   ILE A 617      14.148  -6.766  16.279  1.00 17.31           C  
ANISOU 2675  C   ILE A 617     2928   1454   2194   -255    241     67
ATOM   2676  O   ILE A 617      15.235  -7.219  16.619  1.00 19.84           O  
ANISOU 2676  O   ILE A 617     2992   2438   2108   -372   -224     66
ATOM   2677  CB  ILE A 617      12.383  -8.367  17.037  1.00 24.57           C  
ANISOU 2677  CB  ILE A 617     3577   2791   2967   -691     63    687
ATOM   2678  CG1 ILE A 617      11.644  -8.585  15.694  1.00 27.99           C  
ANISOU 2678  CG1 ILE A 617     4675   2701   3258   -556    -94    242
ATOM   2679  CG2 ILE A 617      11.542  -8.822  18.240  1.00 23.33           C  
ANISOU 2679  CG2 ILE A 617     3362   2402   3101   -915    263   -174
ATOM   2680  CD1 ILE A 617      11.519 -10.063  15.289  1.00 35.89           C  
ANISOU 2680  CD1 ILE A 617     6905   2905   3824     -1    544   -218
ATOM   2681  H   ILE A 617      11.005  -6.148  17.156  1.00  0.00           H  
ATOM   2682  HA  ILE A 617      13.411  -6.926  18.249  1.00  0.00           H  
ATOM   2683  HB  ILE A 617      13.234  -9.048  17.015  1.00  0.00           H  
ATOM   2684 HG13 ILE A 617      12.146  -8.067  14.879  1.00  0.00           H  
ATOM   2685 HG12 ILE A 617      10.652  -8.145  15.752  1.00  0.00           H  
ATOM   2686 HG21 ILE A 617      11.234  -9.862  18.145  1.00  0.00           H  
ATOM   2687 HG22 ILE A 617      12.105  -8.737  19.169  1.00  0.00           H  
ATOM   2688 HG23 ILE A 617      10.645  -8.219  18.341  1.00  0.00           H  
ATOM   2689 HD11 ILE A 617      11.182 -10.153  14.256  1.00  0.00           H  
ATOM   2690 HD12 ILE A 617      12.474 -10.583  15.367  1.00  0.00           H  
ATOM   2691 HD13 ILE A 617      10.797 -10.587  15.914  1.00  0.00           H  
ATOM   2692  N   LEU A 618      13.952  -6.097  15.129  1.00 15.94           N  
ANISOU 2692  N   LEU A 618     2376   1651   2026   -269   -158   -243
ATOM   2693  CA  LEU A 618      15.018  -5.844  14.150  1.00 17.11           C  
ANISOU 2693  CA  LEU A 618     2450   2079   1969   -124   -110    -24
ATOM   2694  C   LEU A 618      16.113  -4.885  14.657  1.00 15.96           C  
ANISOU 2694  C   LEU A 618     1897   2675   1489    224    -81   -547
ATOM   2695  O   LEU A 618      17.236  -4.966  14.166  1.00 14.64           O  
ANISOU 2695  O   LEU A 618     1791   1720   2051    211     10   -369
ATOM   2696  CB  LEU A 618      14.411  -5.310  12.834  1.00 16.41           C  
ANISOU 2696  CB  LEU A 618     2733   1732   1767      8     -4    -29
ATOM   2697  CG  LEU A 618      13.482  -6.297  12.096  1.00 16.60           C  
ANISOU 2697  CG  LEU A 618     2307   2399   1600     31   -256    162
ATOM   2698  CD1 LEU A 618      12.870  -5.633  10.851  1.00 19.22           C  
ANISOU 2698  CD1 LEU A 618     2637   3022   1642    323   -413     73
ATOM   2699  CD2 LEU A 618      14.184  -7.614  11.737  1.00 20.30           C  
ANISOU 2699  CD2 LEU A 618     2491   2563   2657   -257   -415   -392
ATOM   2700  H   LEU A 618      13.032  -5.744  14.901  1.00  0.00           H  
ATOM   2701  HA  LEU A 618      15.515  -6.794  13.950  1.00  0.00           H  
ATOM   2702  HB3 LEU A 618      15.213  -5.022  12.153  1.00  0.00           H  
ATOM   2703  HB2 LEU A 618      13.865  -4.393  13.044  1.00  0.00           H  
ATOM   2704  HG  LEU A 618      12.655  -6.545  12.759  1.00  0.00           H  
ATOM   2705 HD11 LEU A 618      11.918  -6.095  10.589  1.00  0.00           H  
ATOM   2706 HD12 LEU A 618      12.686  -4.569  11.005  1.00  0.00           H  
ATOM   2707 HD13 LEU A 618      13.534  -5.729   9.993  1.00  0.00           H  
ATOM   2708 HD21 LEU A 618      13.900  -7.979  10.751  1.00  0.00           H  
ATOM   2709 HD22 LEU A 618      15.265  -7.486  11.734  1.00  0.00           H  
ATOM   2710 HD23 LEU A 618      13.939  -8.398  12.455  1.00  0.00           H  
ATOM   2711  N   TRP A 619      15.773  -4.020  15.627  1.00 14.68           N  
ANISOU 2711  N   TRP A 619     2170   1731   1676    160    171     30
ATOM   2712  CA  TRP A 619      16.657  -3.012  16.213  1.00 16.59           C  
ANISOU 2712  CA  TRP A 619     2179   2648   1475    -16   -270    -25
ATOM   2713  C   TRP A 619      17.210  -3.405  17.590  1.00 16.03           C  
ANISOU 2713  C   TRP A 619     2486   2197   1406     47    123    400
ATOM   2714  O   TRP A 619      18.092  -2.699  18.076  1.00 17.32           O  
ANISOU 2714  O   TRP A 619     2765   2080   1733    -75     37     94
ATOM   2715  CB  TRP A 619      15.902  -1.677  16.292  1.00 16.89           C  
ANISOU 2715  CB  TRP A 619     2098   2302   2015   -122   -364   -223
ATOM   2716  CG  TRP A 619      15.486  -1.112  14.973  1.00 13.12           C  
ANISOU 2716  CG  TRP A 619     1452   2133   1399    -31    319   -511
ATOM   2717  CD1 TRP A 619      16.222  -0.271  14.216  1.00 13.88           C  
ANISOU 2717  CD1 TRP A 619     1443   2210   1621   -222    -79   -152
ATOM   2718  NE1 TRP A 619      15.563  -0.031  13.031  1.00 13.95           N  
ANISOU 2718  NE1 TRP A 619     1690   2206   1401    232    370     41
ATOM   2719  CE2 TRP A 619      14.367  -0.707  12.958  1.00 14.19           C  
ANISOU 2719  CE2 TRP A 619     1890   2013   1487     -9    -35   -203
ATOM   2720  CD2 TRP A 619      14.282  -1.400  14.201  1.00 15.33           C  
ANISOU 2720  CD2 TRP A 619     1787   2493   1542   -228     45   -111
ATOM   2721  CE3 TRP A 619      13.123  -2.176  14.423  1.00 14.29           C  
ANISOU 2721  CE3 TRP A 619     1616   2177   1633    -55    146   -424
ATOM   2722  CZ3 TRP A 619      12.105  -2.262  13.454  1.00 17.64           C  
ANISOU 2722  CZ3 TRP A 619     1983   3078   1640   -218     21   -333
ATOM   2723  CH2 TRP A 619      12.222  -1.577  12.230  1.00 16.05           C  
ANISOU 2723  CH2 TRP A 619     1820   2470   1807    -23   -149   -193
ATOM   2724  CZ2 TRP A 619      13.360  -0.791  11.980  1.00 17.13           C  
ANISOU 2724  CZ2 TRP A 619     2031   2621   1853   -210   -246   -141
ATOM   2725  H   TRP A 619      14.831  -4.039  15.992  1.00  0.00           H  
ATOM   2726  HA  TRP A 619      17.518  -2.851  15.568  1.00  0.00           H  
ATOM   2727  HB3 TRP A 619      16.494  -0.923  16.812  1.00  0.00           H  
ATOM   2728  HB2 TRP A 619      14.997  -1.827  16.877  1.00  0.00           H  
ATOM   2729  HD1 TRP A 619      17.184   0.125  14.500  1.00  0.00           H  
ATOM   2730  HE1 TRP A 619      15.950   0.536  12.280  1.00  0.00           H  
ATOM   2731  HE3 TRP A 619      13.018  -2.714  15.351  1.00  0.00           H  
ATOM   2732  HZ3 TRP A 619      11.231  -2.861  13.654  1.00  0.00           H  
ATOM   2733  HH2 TRP A 619      11.439  -1.649  11.491  1.00  0.00           H  
ATOM   2734  HZ2 TRP A 619      13.445  -0.250  11.054  1.00  0.00           H  
ATOM   2735  N   MET A 620      16.712  -4.503  18.191  1.00 15.87           N  
ANISOU 2735  N   MET A 620     2729   1992   1310   -211     86     64
ATOM   2736  CA  MET A 620      17.206  -5.031  19.465  1.00 17.32           C  
ANISOU 2736  CA  MET A 620     2688   2164   1726   -383   -480    158
ATOM   2737  C   MET A 620      18.622  -5.604  19.326  1.00 17.90           C  
ANISOU 2737  C   MET A 620     2734   1969   2098   -380   -359   -110
ATOM   2738  O   MET A 620      18.861  -6.454  18.468  1.00 15.03           O  
ANISOU 2738  O   MET A 620     2452   1818   1438   -282    -51    269
ATOM   2739  CB  MET A 620      16.277  -6.133  20.005  1.00 15.64           C  
ANISOU 2739  CB  MET A 620     2955   1367   1620    -55   -111    -48
ATOM   2740  CG  MET A 620      14.908  -5.653  20.488  1.00 20.99           C  
ANISOU 2740  CG  MET A 620     3365   2396   2213   -414    193     -8
ATOM   2741  SD  MET A 620      13.887  -7.002  21.138  1.00 23.45           S  
ANISOU 2741  SD  MET A 620     3564   2697   2646   -739    773     -7
ATOM   2742  CE  MET A 620      12.342  -6.102  21.408  1.00 25.64           C  
ANISOU 2742  CE  MET A 620     4275   2593   2872   -100    -36    211
ATOM   2743  H   MET A 620      15.983  -5.033  17.737  1.00  0.00           H  
ATOM   2744  HA  MET A 620      17.221  -4.219  20.194  1.00  0.00           H  
ATOM   2745  HB3 MET A 620      16.761  -6.623  20.850  1.00  0.00           H  
ATOM   2746  HB2 MET A 620      16.139  -6.903  19.246  1.00  0.00           H  
ATOM   2747  HG3 MET A 620      14.371  -5.166  19.679  1.00  0.00           H  
ATOM   2748  HG2 MET A 620      15.030  -4.912  21.277  1.00  0.00           H  
ATOM   2749  HE1 MET A 620      11.593  -6.759  21.851  1.00  0.00           H  
ATOM   2750  HE2 MET A 620      12.501  -5.255  22.075  1.00  0.00           H  
ATOM   2751  HE3 MET A 620      11.957  -5.734  20.459  1.00  0.00           H  
ATOM   2752  N   ALA A 621      19.513  -5.168  20.227  1.00 16.12           N  
ANISOU 2752  N   ALA A 621     2386   1907   1829   -329   -238   -163
ATOM   2753  CA  ALA A 621      20.845  -5.728  20.429  1.00 16.60           C  
ANISOU 2753  CA  ALA A 621     2697   1442   2167   -289   -501   -250
ATOM   2754  C   ALA A 621      20.768  -7.184  20.931  1.00 15.74           C  
ANISOU 2754  C   ALA A 621     2435   1707   1836   -374     71    140
ATOM   2755  O   ALA A 621      19.756  -7.535  21.539  1.00 16.65           O  
ANISOU 2755  O   ALA A 621     2561   1714   2048   -714    -96    162
ATOM   2756  CB  ALA A 621      21.572  -4.840  21.444  1.00 14.98           C  
ANISOU 2756  CB  ALA A 621     2668    852   2172   -573    105   -439
ATOM   2757  H   ALA A 621      19.241  -4.435  20.869  1.00  0.00           H  
ATOM   2758  HA  ALA A 621      21.363  -5.684  19.478  1.00  0.00           H  
ATOM   2759  HB1 ALA A 621      22.607  -5.152  21.560  1.00  0.00           H  
ATOM   2760  HB2 ALA A 621      21.581  -3.797  21.129  1.00  0.00           H  
ATOM   2761  HB3 ALA A 621      21.096  -4.882  22.424  1.00  0.00           H  
ATOM   2762  N   PRO A 622      21.822  -8.002  20.696  1.00 19.19           N  
ANISOU 2762  N   PRO A 622     3016   2005   2269   -138    526    -13
ATOM   2763  CA  PRO A 622      21.914  -9.380  21.216  1.00 18.87           C  
ANISOU 2763  CA  PRO A 622     3099   1911   2157   -373    440   -254
ATOM   2764  C   PRO A 622      21.535  -9.584  22.693  1.00 17.30           C  
ANISOU 2764  C   PRO A 622     2618   2049   1907   -254   -222     70
ATOM   2765  O   PRO A 622      20.753 -10.485  22.962  1.00 16.92           O  
ANISOU 2765  O   PRO A 622     2731   1968   1726   -179     40    183
ATOM   2766  CB  PRO A 622      23.357  -9.796  20.910  1.00 22.29           C  
ANISOU 2766  CB  PRO A 622     3441   2706   2319    255    643   -293
ATOM   2767  CG  PRO A 622      23.666  -9.045  19.630  1.00 19.94           C  
ANISOU 2767  CG  PRO A 622     2465   2209   2900   -345    491   -142
ATOM   2768  CD  PRO A 622      22.970  -7.706  19.838  1.00 20.28           C  
ANISOU 2768  CD  PRO A 622     2920   2139   2647   -284    625    -90
ATOM   2769  HA  PRO A 622      21.253  -9.988  20.597  1.00  0.00           H  
ATOM   2770  HB3 PRO A 622      23.468 -10.874  20.793  1.00  0.00           H  
ATOM   2771  HB2 PRO A 622      24.035  -9.469  21.702  1.00  0.00           H  
ATOM   2772  HG3 PRO A 622      23.198  -9.562  18.793  1.00  0.00           H  
ATOM   2773  HG2 PRO A 622      24.730  -8.960  19.419  1.00  0.00           H  
ATOM   2774  HD2 PRO A 622      23.626  -7.006  20.350  1.00  0.00           H  
ATOM   2775  HD3 PRO A 622      22.685  -7.286  18.875  1.00  0.00           H  
ATOM   2776  N   GLU A 623      22.015  -8.720  23.605  1.00 19.83           N  
ANISOU 2776  N   GLU A 623     2888   2190   2455   -347    -50   -216
ATOM   2777  CA  GLU A 623      21.691  -8.760  25.035  1.00 20.14           C  
ANISOU 2777  CA  GLU A 623     3251   2128   2272    -75   -492    272
ATOM   2778  C   GLU A 623      20.254  -8.327  25.388  1.00 18.60           C  
ANISOU 2778  C   GLU A 623     3746   1769   1550    418   -102    120
ATOM   2779  O   GLU A 623      19.802  -8.671  26.478  1.00 22.13           O  
ANISOU 2779  O   GLU A 623     4024   2734   1650    279    -48    238
ATOM   2780  CB  GLU A 623      22.744  -7.977  25.859  1.00 21.15           C  
ANISOU 2780  CB  GLU A 623     3256   2456   2323   -596   -145     51
ATOM   2781  CG  GLU A 623      22.735  -6.432  25.744  1.00 21.01           C  
ANISOU 2781  CG  GLU A 623     3291   2424   2267    -14   -173   -131
ATOM   2782  CD  GLU A 623      23.370  -5.826  24.484  1.00 21.05           C  
ANISOU 2782  CD  GLU A 623     3013   2445   2539   -183    145   -247
ATOM   2783  OE1 GLU A 623      24.012  -6.551  23.693  1.00 18.14           O  
ANISOU 2783  OE1 GLU A 623     2754   1793   2344    247   -662   -129
ATOM   2784  OE2 GLU A 623      23.216  -4.599  24.333  1.00 17.29           O1-
ANISOU 2784  OE2 GLU A 623     2321   2367   1880    162   -493    249
ATOM   2785  H   GLU A 623      22.652  -7.984  23.321  1.00  0.00           H  
ATOM   2786  HA  GLU A 623      21.762  -9.804  25.341  1.00  0.00           H  
ATOM   2787  HB3 GLU A 623      23.741  -8.359  25.639  1.00  0.00           H  
ATOM   2788  HB2 GLU A 623      22.593  -8.224  26.911  1.00  0.00           H  
ATOM   2789  HG3 GLU A 623      23.288  -6.034  26.595  1.00  0.00           H  
ATOM   2790  HG2 GLU A 623      21.722  -6.043  25.857  1.00  0.00           H  
ATOM   2791  N   VAL A 624      19.560  -7.607  24.491  1.00 19.95           N  
ANISOU 2791  N   VAL A 624     3845   1956   1778    458   -404   -108
ATOM   2792  CA  VAL A 624      18.156  -7.225  24.659  1.00 19.81           C  
ANISOU 2792  CA  VAL A 624     3557   2442   1527    -40   -399     97
ATOM   2793  C   VAL A 624      17.222  -8.353  24.174  1.00 19.71           C  
ANISOU 2793  C   VAL A 624     2974   2475   2039    113    107      0
ATOM   2794  O   VAL A 624      16.338  -8.759  24.928  1.00 20.67           O  
ANISOU 2794  O   VAL A 624     3280   2475   2098    -79    285    -17
ATOM   2795  CB  VAL A 624      17.815  -5.898  23.915  1.00 18.59           C  
ANISOU 2795  CB  VAL A 624     2969   2599   1495     81   -327    322
ATOM   2796  CG1 VAL A 624      16.323  -5.511  23.969  1.00 22.40           C  
ANISOU 2796  CG1 VAL A 624     3489   3022   1998     96    -52    328
ATOM   2797  CG2 VAL A 624      18.654  -4.717  24.440  1.00 16.84           C  
ANISOU 2797  CG2 VAL A 624     3066   1840   1492    263    436    249
ATOM   2798  H   VAL A 624      19.984  -7.369  23.604  1.00  0.00           H  
ATOM   2799  HA  VAL A 624      17.946  -7.073  25.718  1.00  0.00           H  
ATOM   2800  HB  VAL A 624      18.074  -6.019  22.863  1.00  0.00           H  
ATOM   2801 HG11 VAL A 624      16.153  -4.547  23.490  1.00  0.00           H  
ATOM   2802 HG12 VAL A 624      15.687  -6.230  23.454  1.00  0.00           H  
ATOM   2803 HG13 VAL A 624      15.972  -5.435  24.999  1.00  0.00           H  
ATOM   2804 HG21 VAL A 624      18.466  -3.815  23.857  1.00  0.00           H  
ATOM   2805 HG22 VAL A 624      18.413  -4.489  25.478  1.00  0.00           H  
ATOM   2806 HG23 VAL A 624      19.724  -4.919  24.387  1.00  0.00           H  
ATOM   2807  N   ILE A 625      17.447  -8.849  22.942  1.00 18.75           N  
ANISOU 2807  N   ILE A 625     2828   2584   1711   -352    608    363
ATOM   2808  CA  ILE A 625      16.608  -9.860  22.287  1.00 21.17           C  
ANISOU 2808  CA  ILE A 625     3313   2578   2153   -606    245    596
ATOM   2809  C   ILE A 625      16.782 -11.288  22.857  1.00 18.90           C  
ANISOU 2809  C   ILE A 625     2479   2145   2555   -437    426    252
ATOM   2810  O   ILE A 625      15.891 -12.116  22.671  1.00 19.29           O  
ANISOU 2810  O   ILE A 625     2653   2251   2425   -710   -111    651
ATOM   2811  CB  ILE A 625      16.868  -9.882  20.751  1.00 19.83           C  
ANISOU 2811  CB  ILE A 625     3089   2181   2264   -795    390    111
ATOM   2812  CG1 ILE A 625      15.699 -10.507  19.960  1.00 18.64           C  
ANISOU 2812  CG1 ILE A 625     3008   1730   2341   -337   -120    326
ATOM   2813  CG2 ILE A 625      18.205 -10.526  20.338  1.00 22.13           C  
ANISOU 2813  CG2 ILE A 625     3603   2313   2492   -472    649    424
ATOM   2814  CD1 ILE A 625      15.688 -10.108  18.482  1.00 25.09           C  
ANISOU 2814  CD1 ILE A 625     4126   3052   2355   -557   -611    130
ATOM   2815  H   ILE A 625      18.209  -8.477  22.390  1.00  0.00           H  
ATOM   2816  HA  ILE A 625      15.569  -9.572  22.458  1.00  0.00           H  
ATOM   2817  HB  ILE A 625      16.931  -8.841  20.442  1.00  0.00           H  
ATOM   2818 HG13 ILE A 625      14.747 -10.206  20.399  1.00  0.00           H  
ATOM   2819 HG12 ILE A 625      15.738 -11.593  20.039  1.00  0.00           H  
ATOM   2820 HG21 ILE A 625      18.436 -10.325  19.293  1.00  0.00           H  
ATOM   2821 HG22 ILE A 625      19.024 -10.129  20.931  1.00  0.00           H  
ATOM   2822 HG23 ILE A 625      18.191 -11.609  20.464  1.00  0.00           H  
ATOM   2823 HD11 ILE A 625      14.775 -10.447  17.994  1.00  0.00           H  
ATOM   2824 HD12 ILE A 625      15.734  -9.028  18.375  1.00  0.00           H  
ATOM   2825 HD13 ILE A 625      16.528 -10.541  17.939  1.00  0.00           H  
ATOM   2826  N   ARG A 626      17.901 -11.544  23.555  1.00 18.16           N  
ANISOU 2826  N   ARG A 626     3390   1614   1895     75     40    272
ATOM   2827  CA  ARG A 626      18.209 -12.805  24.233  1.00 19.03           C  
ANISOU 2827  CA  ARG A 626     3949    630   2651   -665    811     14
ATOM   2828  C   ARG A 626      17.321 -13.067  25.468  1.00 19.68           C  
ANISOU 2828  C   ARG A 626     3136   1575   2764   -355    438    182
ATOM   2829  O   ARG A 626      17.092 -14.234  25.787  1.00 23.04           O  
ANISOU 2829  O   ARG A 626     4459   1589   2707   -490     26    150
ATOM   2830  CB  ARG A 626      19.727 -12.816  24.513  1.00 26.90           C  
ANISOU 2830  CB  ARG A 626     3973   2404   3841  -1022    463    683
ATOM   2831  CG  ARG A 626      20.324 -14.022  25.250  1.00 39.46           C  
ANISOU 2831  CG  ARG A 626     5001   2947   7044   -740    269    333
ATOM   2832  CD  ARG A 626      21.861 -14.131  25.108  1.00 46.97           C  
ANISOU 2832  CD  ARG A 626     6272   4821   6752   -808   1066   -644
ATOM   2833  NE  ARG A 626      22.603 -12.941  25.583  1.00 40.52           N  
ANISOU 2833  NE  ARG A 626     5171   4361   5864    445  -1021    675
ATOM   2834  CZ  ARG A 626      23.535 -12.205  24.938  1.00 37.01           C  
ANISOU 2834  CZ  ARG A 626     5015   3897   5149     97   -840  -1058
ATOM   2835  NH1 ARG A 626      24.178 -11.245  25.613  1.00 42.45           N  
ANISOU 2835  NH1 ARG A 626     5363   2776   7990   -174  -1297  -1167
ATOM   2836  NH2 ARG A 626      23.862 -12.393  23.653  1.00 40.52           N1+
ANISOU 2836  NH2 ARG A 626     4614   5688   5093    449    353   1031
ATOM   2837  H   ARG A 626      18.598 -10.817  23.642  1.00  0.00           H  
ATOM   2838  HA  ARG A 626      18.004 -13.615  23.530  1.00  0.00           H  
ATOM   2839  HB3 ARG A 626      19.992 -11.912  25.063  1.00  0.00           H  
ATOM   2840  HB2 ARG A 626      20.232 -12.766  23.549  1.00  0.00           H  
ATOM   2841  HG3 ARG A 626      19.907 -14.898  24.751  1.00  0.00           H  
ATOM   2842  HG2 ARG A 626      20.005 -14.095  26.289  1.00  0.00           H  
ATOM   2843  HD3 ARG A 626      22.159 -14.500  24.129  1.00  0.00           H  
ATOM   2844  HD2 ARG A 626      22.180 -14.905  25.806  1.00  0.00           H  
ATOM   2845  HE  ARG A 626      22.384 -12.678  26.534  1.00  0.00           H  
ATOM   2846 HH12 ARG A 626      24.879 -10.677  25.158  1.00  0.00           H  
ATOM   2847 HH11 ARG A 626      23.969 -11.080  26.587  1.00  0.00           H  
ATOM   2848 HH22 ARG A 626      24.574 -11.831  23.212  1.00  0.00           H  
ATOM   2849 HH21 ARG A 626      23.366 -13.082  23.098  1.00  0.00           H  
ATOM   2850  N   MET A 627      16.789 -11.996  26.095  1.00 21.10           N  
ANISOU 2850  N   MET A 627     3860   2065   2090     73    475     95
ATOM   2851  CA  MET A 627      15.797 -12.017  27.182  1.00 22.13           C  
ANISOU 2851  CA  MET A 627     3390   2681   2336   -152    394    491
ATOM   2852  C   MET A 627      16.267 -12.773  28.446  1.00 23.24           C  
ANISOU 2852  C   MET A 627     3665   2321   2843   -370   -170    459
ATOM   2853  O   MET A 627      15.471 -13.466  29.080  1.00 23.39           O  
ANISOU 2853  O   MET A 627     3694   2560   2633   -255    628    111
ATOM   2854  CB  MET A 627      14.411 -12.471  26.657  1.00 23.40           C  
ANISOU 2854  CB  MET A 627     2455   3181   3252    386   1038    -84
ATOM   2855  CG  MET A 627      13.815 -11.517  25.606  1.00 31.54           C  
ANISOU 2855  CG  MET A 627     4290   5091   2600   -217     74    282
ATOM   2856  SD  MET A 627      12.211 -12.027  24.931  1.00 39.39           S  
ANISOU 2856  SD  MET A 627     4915   6712   3339   -593    -23    816
ATOM   2857  CE  MET A 627      12.725 -13.383  23.842  1.00 49.17           C  
ANISOU 2857  CE  MET A 627     8313   6668   3699   -483   -455   1095
ATOM   2858  H   MET A 627      17.022 -11.075  25.752  1.00  0.00           H  
ATOM   2859  HA  MET A 627      15.673 -10.984  27.502  1.00  0.00           H  
ATOM   2860  HB3 MET A 627      13.702 -12.533  27.484  1.00  0.00           H  
ATOM   2861  HB2 MET A 627      14.478 -13.479  26.248  1.00  0.00           H  
ATOM   2862  HG3 MET A 627      14.502 -11.380  24.773  1.00  0.00           H  
ATOM   2863  HG2 MET A 627      13.685 -10.530  26.052  1.00  0.00           H  
ATOM   2864  HE1 MET A 627      11.856 -13.812  23.344  1.00  0.00           H  
ATOM   2865  HE2 MET A 627      13.410 -13.019  23.078  1.00  0.00           H  
ATOM   2866  HE3 MET A 627      13.220 -14.173  24.406  1.00  0.00           H  
ATOM   2867  N   GLN A 628      17.558 -12.616  28.783  1.00 22.88           N  
ANISOU 2867  N   GLN A 628     3574   2243   2874   -117   -117   1021
ATOM   2868  CA  GLN A 628      18.214 -13.200  29.959  1.00 24.79           C  
ANISOU 2868  CA  GLN A 628     4795   2355   2266   -148   -435    934
ATOM   2869  C   GLN A 628      18.745 -12.114  30.916  1.00 21.23           C  
ANISOU 2869  C   GLN A 628     3317   2574   2174    147    -57    668
ATOM   2870  O   GLN A 628      19.611 -12.402  31.742  1.00 23.31           O  
ANISOU 2870  O   GLN A 628     4222   2860   1775    -81   -562    185
ATOM   2871  CB  GLN A 628      19.334 -14.158  29.498  1.00 29.10           C  
ANISOU 2871  CB  GLN A 628     5937   2676   2444    258   -534    754
ATOM   2872  CG  GLN A 628      18.808 -15.416  28.785  1.00 26.29           C  
ANISOU 2872  CG  GLN A 628     5894   2431   1662    724   -630    731
ATOM   2873  CD  GLN A 628      19.926 -16.383  28.390  1.00 30.08           C  
ANISOU 2873  CD  GLN A 628     3976   2928   4523     -9   -433    320
ATOM   2874  OE1 GLN A 628      21.074 -15.987  28.193  1.00 39.65           O  
ANISOU 2874  OE1 GLN A 628     4253   2965   7848   -259    808   -482
ATOM   2875  NE2 GLN A 628      19.585 -17.664  28.246  1.00 45.15           N  
ANISOU 2875  NE2 GLN A 628     6429   2184   8541   1233    964  -2510
ATOM   2876  H   GLN A 628      18.145 -12.033  28.202  1.00  0.00           H  
ATOM   2877  HA  GLN A 628      17.497 -13.777  30.544  1.00  0.00           H  
ATOM   2878  HB3 GLN A 628      19.922 -14.485  30.357  1.00  0.00           H  
ATOM   2879  HB2 GLN A 628      20.027 -13.625  28.846  1.00  0.00           H  
ATOM   2880  HG3 GLN A 628      18.265 -15.143  27.883  1.00  0.00           H  
ATOM   2881  HG2 GLN A 628      18.099 -15.933  29.433  1.00  0.00           H  
ATOM   2882 HE22 GLN A 628      20.281 -18.344  27.977  1.00  0.00           H  
ATOM   2883 HE21 GLN A 628      18.632 -17.962  28.399  1.00  0.00           H  
ATOM   2884  N   ASP A 629      18.221 -10.885  30.791  1.00 20.74           N  
ANISOU 2884  N   ASP A 629     3691   2636   1553     36   -770    614
ATOM   2885  CA  ASP A 629      18.636  -9.717  31.559  1.00 21.06           C  
ANISOU 2885  CA  ASP A 629     3283   3237   1481   -113   -373     74
ATOM   2886  C   ASP A 629      17.385  -8.846  31.760  1.00 22.20           C  
ANISOU 2886  C   ASP A 629     3244   3545   1645   -179   -151   -314
ATOM   2887  O   ASP A 629      16.719  -8.510  30.781  1.00 22.48           O  
ANISOU 2887  O   ASP A 629     3088   2820   2634   -390   -535    188
ATOM   2888  CB  ASP A 629      19.828  -9.013  30.854  1.00 22.48           C  
ANISOU 2888  CB  ASP A 629     3660   3113   1767   -265   -480   -114
ATOM   2889  CG  ASP A 629      20.477  -7.783  31.512  1.00 21.91           C  
ANISOU 2889  CG  ASP A 629     3092   2650   2580   -322   -684    383
ATOM   2890  OD1 ASP A 629      20.043  -7.347  32.602  1.00 23.25           O  
ANISOU 2890  OD1 ASP A 629     3482   2863   2488   -723    -58    419
ATOM   2891  OD2 ASP A 629      21.449  -7.294  30.896  1.00 24.49           O1-
ANISOU 2891  OD2 ASP A 629     3450   2870   2985   -673   -306    -72
ATOM   2892  H   ASP A 629      17.507 -10.720  30.096  1.00  0.00           H  
ATOM   2893  HA  ASP A 629      18.970 -10.052  32.543  1.00  0.00           H  
ATOM   2894  HB3 ASP A 629      19.536  -8.750  29.839  1.00  0.00           H  
ATOM   2895  HB2 ASP A 629      20.619  -9.752  30.720  1.00  0.00           H  
ATOM   2896  N   LYS A 630      17.085  -8.524  33.031  1.00 20.21           N  
ANISOU 2896  N   LYS A 630     3605   2696   1376   -584    199    258
ATOM   2897  CA  LYS A 630      15.916  -7.747  33.455  1.00 24.54           C  
ANISOU 2897  CA  LYS A 630     3350   3501   2473   -567    417    715
ATOM   2898  C   LYS A 630      15.994  -6.251  33.086  1.00 23.53           C  
ANISOU 2898  C   LYS A 630     2632   3314   2992   -207   -431    391
ATOM   2899  O   LYS A 630      14.944  -5.621  32.961  1.00 26.05           O  
ANISOU 2899  O   LYS A 630     2897   4368   2631    272     65     92
ATOM   2900  CB  LYS A 630      15.701  -7.965  34.972  1.00  0.00           C  
ATOM   2901  CG  LYS A 630      14.408  -7.334  35.533  1.00  0.00           C  
ATOM   2902  CD  LYS A 630      14.110  -7.692  36.997  1.00  0.00           C  
ATOM   2903  CE  LYS A 630      15.093  -7.056  37.996  1.00  0.00           C  
ATOM   2904  NZ  LYS A 630      14.715  -7.347  39.390  1.00  0.00           N1+
ATOM   2905  H   LYS A 630      17.697  -8.838  33.773  1.00  0.00           H  
ATOM   2906  HA  LYS A 630      15.049  -8.158  32.934  1.00  0.00           H  
ATOM   2907  HB2 LYS A 630      15.662  -9.038  35.163  1.00  0.00           H  
ATOM   2908  HB3 LYS A 630      16.567  -7.591  35.518  1.00  0.00           H  
ATOM   2909  HG2 LYS A 630      14.447  -6.248  35.449  1.00  0.00           H  
ATOM   2910  HG3 LYS A 630      13.565  -7.652  34.918  1.00  0.00           H  
ATOM   2911  HD2 LYS A 630      13.091  -7.377  37.229  1.00  0.00           H  
ATOM   2912  HD3 LYS A 630      14.121  -8.777  37.107  1.00  0.00           H  
ATOM   2913  HE2 LYS A 630      16.106  -7.424  37.828  1.00  0.00           H  
ATOM   2914  HE3 LYS A 630      15.118  -5.974  37.864  1.00  0.00           H  
ATOM   2915  HZ1 LYS A 630      14.718  -8.347  39.539  1.00  0.00           H  
ATOM   2916  HZ2 LYS A 630      15.378  -6.914  40.018  1.00  0.00           H  
ATOM   2917  HZ3 LYS A 630      13.791  -6.983  39.574  1.00  0.00           H  
ATOM   2918  N   ASN A 631      17.210  -5.716  32.890  1.00 19.55           N  
ANISOU 2918  N   ASN A 631     3280   1658   2489   -521    -15     77
ATOM   2919  CA  ASN A 631      17.430  -4.333  32.475  1.00 17.58           C  
ANISOU 2919  CA  ASN A 631     2543   1671   2466   -376     22    238
ATOM   2920  C   ASN A 631      18.564  -4.286  31.431  1.00 18.11           C  
ANISOU 2920  C   ASN A 631     3005   2094   1781   -394     55    367
ATOM   2921  O   ASN A 631      19.662  -3.834  31.758  1.00 18.43           O  
ANISOU 2921  O   ASN A 631     2712   2177   2114    266   -221   -282
ATOM   2922  CB  ASN A 631      17.682  -3.439  33.718  1.00 23.84           C  
ANISOU 2922  CB  ASN A 631     3026   2648   3382   -554   -524   -315
ATOM   2923  CG  ASN A 631      17.594  -1.933  33.437  1.00 29.43           C  
ANISOU 2923  CG  ASN A 631     3630   2352   5200     -2   -359   -789
ATOM   2924  OD1 ASN A 631      17.303  -1.504  32.322  1.00 32.65           O  
ANISOU 2924  OD1 ASN A 631     3166   3180   6059     44   -467    584
ATOM   2925  ND2 ASN A 631      17.845  -1.116  34.461  1.00 32.49           N  
ANISOU 2925  ND2 ASN A 631     5985   2124   4235    642    242   -347
ATOM   2926  H   ASN A 631      18.037  -6.294  32.978  1.00  0.00           H  
ATOM   2927  HA  ASN A 631      16.550  -3.939  31.964  1.00  0.00           H  
ATOM   2928  HB3 ASN A 631      18.641  -3.676  34.182  1.00  0.00           H  
ATOM   2929  HB2 ASN A 631      16.923  -3.656  34.470  1.00  0.00           H  
ATOM   2930 HD22 ASN A 631      17.809  -0.115  34.335  1.00  0.00           H  
ATOM   2931 HD21 ASN A 631      18.039  -1.494  35.378  1.00  0.00           H  
ATOM   2932  N   PRO A 632      18.295  -4.768  30.195  1.00 20.75           N  
ANISOU 2932  N   PRO A 632     3199   2423   2259   -261   -421    -33
ATOM   2933  CA  PRO A 632      19.324  -4.865  29.151  1.00 20.38           C  
ANISOU 2933  CA  PRO A 632     3524   2181   2036     96   -470    351
ATOM   2934  C   PRO A 632      19.566  -3.558  28.378  1.00 19.36           C  
ANISOU 2934  C   PRO A 632     3231   1966   2156     -4    -16    103
ATOM   2935  O   PRO A 632      20.426  -3.550  27.501  1.00 21.58           O  
ANISOU 2935  O   PRO A 632     3605   2306   2285    371    358    421
ATOM   2936  CB  PRO A 632      18.746  -5.943  28.231  1.00 20.79           C  
ANISOU 2936  CB  PRO A 632     3969   2183   1745    -27    223   -172
ATOM   2937  CG  PRO A 632      17.248  -5.674  28.251  1.00 23.91           C  
ANISOU 2937  CG  PRO A 632     4346   2517   2220    192   -254      0
ATOM   2938  CD  PRO A 632      16.996  -5.231  29.691  1.00 17.93           C  
ANISOU 2938  CD  PRO A 632     2617   2180   2016    153      5    450
ATOM   2939  HA  PRO A 632      20.280  -5.197  29.557  1.00  0.00           H  
ATOM   2940  HB3 PRO A 632      18.951  -6.924  28.657  1.00  0.00           H  
ATOM   2941  HB2 PRO A 632      19.174  -5.933  27.230  1.00  0.00           H  
ATOM   2942  HG3 PRO A 632      16.646  -6.532  27.950  1.00  0.00           H  
ATOM   2943  HG2 PRO A 632      17.015  -4.854  27.570  1.00  0.00           H  
ATOM   2944  HD2 PRO A 632      16.232  -4.454  29.735  1.00  0.00           H  
ATOM   2945  HD3 PRO A 632      16.651  -6.075  30.279  1.00  0.00           H  
ATOM   2946  N   TYR A 633      18.788  -2.504  28.673  1.00 20.11           N  
ANISOU 2946  N   TYR A 633     4220   2161   1257    366    603    467
ATOM   2947  CA  TYR A 633      18.832  -1.236  27.960  1.00 17.94           C  
ANISOU 2947  CA  TYR A 633     4040   1492   1284    627    942     35
ATOM   2948  C   TYR A 633      19.919  -0.318  28.534  1.00 23.02           C  
ANISOU 2948  C   TYR A 633     4510   1906   2328      5    876    418
ATOM   2949  O   TYR A 633      20.009  -0.146  29.749  1.00 23.91           O  
ANISOU 2949  O   TYR A 633     4944   1782   2356    407    677    712
ATOM   2950  CB  TYR A 633      17.443  -0.582  27.999  1.00 20.02           C  
ANISOU 2950  CB  TYR A 633     3799   1774   2033    355   1076    501
ATOM   2951  CG  TYR A 633      16.366  -1.371  27.272  1.00 21.69           C  
ANISOU 2951  CG  TYR A 633     3445   2248   2548      0    904    152
ATOM   2952  CD1 TYR A 633      16.363  -1.429  25.863  1.00 22.80           C  
ANISOU 2952  CD1 TYR A 633     3804   2170   2686    337    372   -198
ATOM   2953  CE1 TYR A 633      15.369  -2.151  25.178  1.00 27.37           C  
ANISOU 2953  CE1 TYR A 633     3798   2481   4119    261    -88   -432
ATOM   2954  CZ  TYR A 633      14.376  -2.837  25.903  1.00 32.01           C  
ANISOU 2954  CZ  TYR A 633     4164   3113   4883    534   1618  -1469
ATOM   2955  OH  TYR A 633      13.408  -3.537  25.242  1.00 43.69           O  
ANISOU 2955  OH  TYR A 633     2458   1871  12267   -395    271    525
ATOM   2956  CE2 TYR A 633      14.381  -2.796  27.311  1.00 31.79           C  
ANISOU 2956  CE2 TYR A 633     4112   3729   4237  -1227   1461    686
ATOM   2957  CD2 TYR A 633      15.370  -2.060  27.995  1.00 26.25           C  
ANISOU 2957  CD2 TYR A 633     3279   2986   3706    -43    796    995
ATOM   2958  H   TYR A 633      18.101  -2.580  29.409  1.00  0.00           H  
ATOM   2959  HA  TYR A 633      19.060  -1.443  26.915  1.00  0.00           H  
ATOM   2960  HB3 TYR A 633      17.512   0.396  27.528  1.00  0.00           H  
ATOM   2961  HB2 TYR A 633      17.133  -0.403  29.029  1.00  0.00           H  
ATOM   2962  HD1 TYR A 633      17.127  -0.924  25.298  1.00  0.00           H  
ATOM   2963  HE1 TYR A 633      15.373  -2.182  24.099  1.00  0.00           H  
ATOM   2964  HH  TYR A 633      13.376  -3.346  24.299  1.00  0.00           H  
ATOM   2965  HE2 TYR A 633      13.621  -3.322  27.869  1.00  0.00           H  
ATOM   2966  HD2 TYR A 633      15.362  -2.032  29.074  1.00  0.00           H  
ATOM   2967  N   SER A 634      20.716   0.255  27.626  1.00 18.81           N  
ANISOU 2967  N   SER A 634     3969   2004   1171    619    413     -2
ATOM   2968  CA  SER A 634      21.843   1.135  27.913  1.00 20.70           C  
ANISOU 2968  CA  SER A 634     4168   1692   2004    393     10    476
ATOM   2969  C   SER A 634      22.086   2.072  26.718  1.00 18.70           C  
ANISOU 2969  C   SER A 634     3524   1430   2151   -147   -125    443
ATOM   2970  O   SER A 634      21.406   1.965  25.694  1.00 17.89           O  
ANISOU 2970  O   SER A 634     2488   1879   2427   -137     37     63
ATOM   2971  CB  SER A 634      23.080   0.276  28.270  1.00 20.80           C  
ANISOU 2971  CB  SER A 634     4539   1135   2226    646    -16   -347
ATOM   2972  OG  SER A 634      23.650  -0.329  27.129  1.00 19.20           O  
ANISOU 2972  OG  SER A 634     3452   1959   1884    934     40   -185
ATOM   2973  H   SER A 634      20.584   0.040  26.645  1.00  0.00           H  
ATOM   2974  HA  SER A 634      21.590   1.758  28.771  1.00  0.00           H  
ATOM   2975  HB3 SER A 634      22.831  -0.496  28.999  1.00  0.00           H  
ATOM   2976  HB2 SER A 634      23.849   0.893  28.734  1.00  0.00           H  
ATOM   2977  HG  SER A 634      23.262  -1.205  27.012  1.00  0.00           H  
ATOM   2978  N   PHE A 635      23.101   2.942  26.849  1.00 18.50           N  
ANISOU 2978  N   PHE A 635     3330   1774   1921    -28   -171   -290
ATOM   2979  CA  PHE A 635      23.637   3.734  25.739  1.00 17.54           C  
ANISOU 2979  CA  PHE A 635     2996   1666   1999     -8   -387     81
ATOM   2980  C   PHE A 635      24.187   2.856  24.598  1.00 16.68           C  
ANISOU 2980  C   PHE A 635     2657   1490   2188    295   -406    143
ATOM   2981  O   PHE A 635      24.044   3.224  23.436  1.00 16.96           O  
ANISOU 2981  O   PHE A 635     2588   2093   1760   -328   -105    -68
ATOM   2982  CB  PHE A 635      24.762   4.665  26.235  1.00 19.62           C  
ANISOU 2982  CB  PHE A 635     3264   1914   2275     -4   -719   -382
ATOM   2983  CG  PHE A 635      24.434   5.702  27.295  1.00 26.07           C  
ANISOU 2983  CG  PHE A 635     4445   2398   3060    506  -1123   -899
ATOM   2984  CD1 PHE A 635      23.162   6.311  27.383  1.00 20.32           C  
ANISOU 2984  CD1 PHE A 635     3761   1789   2168   -313   -385   -314
ATOM   2985  CE1 PHE A 635      22.943   7.332  28.299  1.00 17.52           C  
ANISOU 2985  CE1 PHE A 635     3561   1505   1590    545   -783    379
ATOM   2986  CZ  PHE A 635      23.982   7.784  29.102  1.00 30.16           C  
ANISOU 2986  CZ  PHE A 635     4608   3621   3229   1527  -1800  -1747
ATOM   2987  CD2 PHE A 635      25.487   6.208  28.087  1.00 33.15           C  
ANISOU 2987  CD2 PHE A 635     4557   4345   3692   1658  -1998  -1957
ATOM   2988  CE2 PHE A 635      25.251   7.233  28.990  1.00 35.65           C  
ANISOU 2988  CE2 PHE A 635     5418   3875   4250   2361  -2159  -1787
ATOM   2989  H   PHE A 635      23.601   3.000  27.727  1.00  0.00           H  
ATOM   2990  HA  PHE A 635      22.822   4.329  25.327  1.00  0.00           H  
ATOM   2991  HB3 PHE A 635      25.168   5.212  25.385  1.00  0.00           H  
ATOM   2992  HB2 PHE A 635      25.582   4.053  26.616  1.00  0.00           H  
ATOM   2993  HD1 PHE A 635      22.350   5.997  26.744  1.00  0.00           H  
ATOM   2994  HE1 PHE A 635      21.965   7.786  28.374  1.00  0.00           H  
ATOM   2995  HZ  PHE A 635      23.817   8.580  29.810  1.00  0.00           H  
ATOM   2996  HD2 PHE A 635      26.483   5.801  27.991  1.00  0.00           H  
ATOM   2997  HE2 PHE A 635      26.058   7.609  29.602  1.00  0.00           H  
ATOM   2998  N   GLN A 636      24.775   1.701  24.950  1.00 14.65           N  
ANISOU 2998  N   GLN A 636     1750   1812   2004    516   -281    -24
ATOM   2999  CA  GLN A 636      25.335   0.723  24.023  1.00 18.28           C  
ANISOU 2999  CA  GLN A 636     2142   2397   2406    433   -228   -485
ATOM   3000  C   GLN A 636      24.265   0.070  23.133  1.00 16.07           C  
ANISOU 3000  C   GLN A 636     1911   2071   2122    293   -115    -87
ATOM   3001  O   GLN A 636      24.507  -0.094  21.939  1.00 17.33           O  
ANISOU 3001  O   GLN A 636     2379   1813   2392   -106    210   -134
ATOM   3002  CB  GLN A 636      26.140  -0.362  24.776  1.00 20.87           C  
ANISOU 3002  CB  GLN A 636     1576   2867   3487    565   -229    -26
ATOM   3003  CG  GLN A 636      27.463   0.074  25.440  1.00 28.88           C  
ANISOU 3003  CG  GLN A 636     2630   4147   4195   -144   -667   -669
ATOM   3004  CD  GLN A 636      27.365   1.066  26.603  1.00 35.10           C  
ANISOU 3004  CD  GLN A 636     4071   4805   4460   -666  -1020   -942
ATOM   3005  OE1 GLN A 636      26.398   1.072  27.362  1.00 34.66           O  
ANISOU 3005  OE1 GLN A 636     4227   6352   2589   -203  -1443    -59
ATOM   3006  NE2 GLN A 636      28.398   1.894  26.766  1.00 44.11           N  
ANISOU 3006  NE2 GLN A 636     4338   7930   4490  -2180  -1554    880
ATOM   3007  H   GLN A 636      24.847   1.462  25.931  1.00  0.00           H  
ATOM   3008  HA  GLN A 636      26.022   1.255  23.362  1.00  0.00           H  
ATOM   3009  HB3 GLN A 636      26.414  -1.118  24.042  1.00  0.00           H  
ATOM   3010  HB2 GLN A 636      25.515  -0.878  25.502  1.00  0.00           H  
ATOM   3011  HG3 GLN A 636      28.103   0.491  24.668  1.00  0.00           H  
ATOM   3012  HG2 GLN A 636      27.976  -0.809  25.822  1.00  0.00           H  
ATOM   3013 HE22 GLN A 636      28.399   2.562  27.522  1.00  0.00           H  
ATOM   3014 HE21 GLN A 636      29.191   1.848  26.140  1.00  0.00           H  
ATOM   3015  N   SER A 637      23.103  -0.291  23.704  1.00 14.63           N  
ANISOU 3015  N   SER A 637     2412   1776   1371   -123    -17   -681
ATOM   3016  CA  SER A 637      21.980  -0.851  22.945  1.00 13.00           C  
ANISOU 3016  CA  SER A 637     1957   1761   1219    -90   -111    -68
ATOM   3017  C   SER A 637      21.258   0.188  22.063  1.00 12.90           C  
ANISOU 3017  C   SER A 637     2046   1437   1415   -100     62    -29
ATOM   3018  O   SER A 637      20.790  -0.186  20.989  1.00 14.26           O  
ANISOU 3018  O   SER A 637     2215   1492   1709     -9   -225    -56
ATOM   3019  CB  SER A 637      21.056  -1.655  23.876  1.00 15.04           C  
ANISOU 3019  CB  SER A 637     2160   1914   1639   -223     76     39
ATOM   3020  OG  SER A 637      20.503  -0.855  24.889  1.00 15.66           O  
ANISOU 3020  OG  SER A 637     2623   1970   1357    143   -146    144
ATOM   3021  H   SER A 637      22.951  -0.139  24.692  1.00  0.00           H  
ATOM   3022  HA  SER A 637      22.394  -1.583  22.250  1.00  0.00           H  
ATOM   3023  HB3 SER A 637      21.600  -2.472  24.344  1.00  0.00           H  
ATOM   3024  HB2 SER A 637      20.244  -2.110  23.309  1.00  0.00           H  
ATOM   3025  HG  SER A 637      19.848  -0.264  24.498  1.00  0.00           H  
ATOM   3026  N   ASP A 638      21.260   1.477  22.452  1.00 12.32           N  
ANISOU 3026  N   ASP A 638     2019   1435   1225   -206    -42    -39
ATOM   3027  CA  ASP A 638      20.885   2.589  21.565  1.00 12.05           C  
ANISOU 3027  CA  ASP A 638     1559   1526   1492    -78   -232   -129
ATOM   3028  C   ASP A 638      21.830   2.755  20.365  1.00 12.19           C  
ANISOU 3028  C   ASP A 638     1757   1507   1366    127   -234    -36
ATOM   3029  O   ASP A 638      21.348   3.073  19.278  1.00 12.50           O  
ANISOU 3029  O   ASP A 638     2010   1612   1125    303   -212   -312
ATOM   3030  CB  ASP A 638      20.775   3.946  22.294  1.00 13.10           C  
ANISOU 3030  CB  ASP A 638     1898   1496   1581    230   -169   -106
ATOM   3031  CG  ASP A 638      19.545   4.169  23.179  1.00 15.25           C  
ANISOU 3031  CG  ASP A 638     2083   1611   2099    -72    222     49
ATOM   3032  OD1 ASP A 638      18.532   3.455  23.029  1.00 14.83           O  
ANISOU 3032  OD1 ASP A 638     2120   1502   2012    -78     72   -192
ATOM   3033  OD2 ASP A 638      19.583   5.169  23.920  1.00 13.12           O1-
ANISOU 3033  OD2 ASP A 638     1961   1808   1215   -269    104    -30
ATOM   3034  H   ASP A 638      21.648   1.729  23.352  1.00  0.00           H  
ATOM   3035  HA  ASP A 638      19.914   2.341  21.134  1.00  0.00           H  
ATOM   3036  HB3 ASP A 638      20.822   4.764  21.577  1.00  0.00           H  
ATOM   3037  HB2 ASP A 638      21.649   4.064  22.932  1.00  0.00           H  
ATOM   3038  N   VAL A 639      23.138   2.524  20.568  1.00 13.40           N  
ANISOU 3038  N   VAL A 639     1843   1733   1515   -150   -415    -71
ATOM   3039  CA  VAL A 639      24.137   2.529  19.500  1.00 14.51           C  
ANISOU 3039  CA  VAL A 639     1843   1634   2037    -27   -122   -125
ATOM   3040  C   VAL A 639      23.941   1.369  18.506  1.00 13.90           C  
ANISOU 3040  C   VAL A 639     1835   1551   1894    -59   -445    -20
ATOM   3041  O   VAL A 639      24.090   1.603  17.309  1.00 14.83           O  
ANISOU 3041  O   VAL A 639     2210   1329   2095    -79     87     75
ATOM   3042  CB  VAL A 639      25.590   2.522  20.054  1.00 14.06           C  
ANISOU 3042  CB  VAL A 639     1698   1619   2023    422    -98    -56
ATOM   3043  CG1 VAL A 639      26.667   2.127  19.022  1.00 14.89           C  
ANISOU 3043  CG1 VAL A 639     1474   1861   2320     64    102   -120
ATOM   3044  CG2 VAL A 639      25.925   3.879  20.693  1.00 14.84           C  
ANISOU 3044  CG2 VAL A 639     1836   1704   2097    137    285     86
ATOM   3045  H   VAL A 639      23.470   2.299  21.496  1.00  0.00           H  
ATOM   3046  HA  VAL A 639      24.003   3.457  18.939  1.00  0.00           H  
ATOM   3047  HB  VAL A 639      25.651   1.793  20.856  1.00  0.00           H  
ATOM   3048 HG11 VAL A 639      27.665   2.251  19.419  1.00  0.00           H  
ATOM   3049 HG12 VAL A 639      26.591   1.078  18.739  1.00  0.00           H  
ATOM   3050 HG13 VAL A 639      26.593   2.728  18.116  1.00  0.00           H  
ATOM   3051 HG21 VAL A 639      26.863   3.845  21.241  1.00  0.00           H  
ATOM   3052 HG22 VAL A 639      26.004   4.662  19.942  1.00  0.00           H  
ATOM   3053 HG23 VAL A 639      25.163   4.193  21.403  1.00  0.00           H  
ATOM   3054  N   TYR A 640      23.576   0.168  18.994  1.00 12.96           N  
ANISOU 3054  N   TYR A 640     1673   1439   1810    -37     71   -258
ATOM   3055  CA  TYR A 640      23.227  -0.972  18.142  1.00 13.24           C  
ANISOU 3055  CA  TYR A 640     1678   1512   1839     70   -113   -289
ATOM   3056  C   TYR A 640      22.000  -0.687  17.266  1.00 12.07           C  
ANISOU 3056  C   TYR A 640     1553   1330   1701    -84     91   -230
ATOM   3057  O   TYR A 640      22.040  -0.974  16.071  1.00 14.00           O  
ANISOU 3057  O   TYR A 640     1808   1863   1648    170    -93   -301
ATOM   3058  CB  TYR A 640      23.039  -2.253  18.978  1.00 13.30           C  
ANISOU 3058  CB  TYR A 640     1744   1912   1396     57    -63    -23
ATOM   3059  CG  TYR A 640      22.749  -3.494  18.146  1.00 15.53           C  
ANISOU 3059  CG  TYR A 640     2140   1843   1916    185   -146   -208
ATOM   3060  CD1 TYR A 640      21.442  -3.741  17.674  1.00 15.28           C  
ANISOU 3060  CD1 TYR A 640     2146   2112   1546    337    -94    -86
ATOM   3061  CE1 TYR A 640      21.185  -4.822  16.816  1.00 14.53           C  
ANISOU 3061  CE1 TYR A 640     2297   1790   1432    125   -179    228
ATOM   3062  CZ  TYR A 640      22.230  -5.690  16.453  1.00 16.36           C  
ANISOU 3062  CZ  TYR A 640     2188   2204   1821     73   -101   -279
ATOM   3063  OH  TYR A 640      21.984  -6.739  15.620  1.00 16.30           O  
ANISOU 3063  OH  TYR A 640     2872   1802   1518    260    -83    -69
ATOM   3064  CE2 TYR A 640      23.530  -5.473  16.950  1.00 15.60           C  
ANISOU 3064  CE2 TYR A 640     2178   2241   1508     34     49   -314
ATOM   3065  CD2 TYR A 640      23.792  -4.373  17.790  1.00 14.42           C  
ANISOU 3065  CD2 TYR A 640     2447   1964   1068    406   -115    -85
ATOM   3066  H   TYR A 640      23.489   0.038  19.993  1.00  0.00           H  
ATOM   3067  HA  TYR A 640      24.058  -1.142  17.460  1.00  0.00           H  
ATOM   3068  HB3 TYR A 640      22.229  -2.115  19.693  1.00  0.00           H  
ATOM   3069  HB2 TYR A 640      23.935  -2.432  19.568  1.00  0.00           H  
ATOM   3070  HD1 TYR A 640      20.633  -3.081  17.948  1.00  0.00           H  
ATOM   3071  HE1 TYR A 640      20.183  -4.982  16.446  1.00  0.00           H  
ATOM   3072  HH  TYR A 640      21.071  -6.754  15.305  1.00  0.00           H  
ATOM   3073  HE2 TYR A 640      24.330  -6.144  16.676  1.00  0.00           H  
ATOM   3074  HD2 TYR A 640      24.798  -4.197  18.142  1.00  0.00           H  
ATOM   3075  N   ALA A 641      20.951  -0.118  17.879  1.00 14.12           N  
ANISOU 3075  N   ALA A 641     1459   1552   2352     73     26     86
ATOM   3076  CA  ALA A 641      19.730   0.307  17.203  1.00 14.22           C  
ANISOU 3076  CA  ALA A 641     1444   1950   2009      2    -46   -410
ATOM   3077  C   ALA A 641      19.982   1.379  16.129  1.00 14.13           C  
ANISOU 3077  C   ALA A 641     1533   2080   1755    -53   -368   -181
ATOM   3078  O   ALA A 641      19.357   1.322  15.072  1.00 13.09           O  
ANISOU 3078  O   ALA A 641     1816   1783   1373    -11   -181   -136
ATOM   3079  CB  ALA A 641      18.740   0.798  18.260  1.00 13.69           C  
ANISOU 3079  CB  ALA A 641     1417   1902   1879   -498    311   -356
ATOM   3080  H   ALA A 641      20.998   0.070  18.871  1.00  0.00           H  
ATOM   3081  HA  ALA A 641      19.299  -0.565  16.707  1.00  0.00           H  
ATOM   3082  HB1 ALA A 641      17.825   1.137  17.789  1.00  0.00           H  
ATOM   3083  HB2 ALA A 641      18.475   0.001  18.955  1.00  0.00           H  
ATOM   3084  HB3 ALA A 641      19.143   1.629  18.837  1.00  0.00           H  
ATOM   3085  N   PHE A 642      20.949   2.279  16.383  1.00 13.52           N  
ANISOU 3085  N   PHE A 642     1920   1645   1572     -2   -256    154
ATOM   3086  CA  PHE A 642      21.461   3.237  15.406  1.00 12.18           C  
ANISOU 3086  CA  PHE A 642     1723   1401   1504    -69    -99     35
ATOM   3087  C   PHE A 642      22.252   2.581  14.263  1.00 13.93           C  
ANISOU 3087  C   PHE A 642     1806   1729   1755     50    -61     17
ATOM   3088  O   PHE A 642      22.140   3.046  13.134  1.00 14.46           O  
ANISOU 3088  O   PHE A 642     1810   1933   1750   -287   -119     54
ATOM   3089  CB  PHE A 642      22.259   4.341  16.123  1.00 12.36           C  
ANISOU 3089  CB  PHE A 642     1738   1944   1014     75     19   -280
ATOM   3090  CG  PHE A 642      22.880   5.394  15.223  1.00 13.85           C  
ANISOU 3090  CG  PHE A 642     2076   1784   1402    109     13   -164
ATOM   3091  CD1 PHE A 642      22.074   6.428  14.706  1.00 15.34           C  
ANISOU 3091  CD1 PHE A 642     2364   2000   1465    -93   -401    158
ATOM   3092  CE1 PHE A 642      22.604   7.324  13.788  1.00 17.07           C  
ANISOU 3092  CE1 PHE A 642     2658   2551   1274   -120   -214    409
ATOM   3093  CZ  PHE A 642      23.913   7.188  13.350  1.00 17.59           C  
ANISOU 3093  CZ  PHE A 642     2352   2191   2138   -545   -181   -195
ATOM   3094  CD2 PHE A 642      24.202   5.252  14.752  1.00 18.27           C  
ANISOU 3094  CD2 PHE A 642     2304   2929   1709   -369     74   -448
ATOM   3095  CE2 PHE A 642      24.706   6.154  13.825  1.00 19.59           C  
ANISOU 3095  CE2 PHE A 642     2414   3139   1890     40    -72     29
ATOM   3096  H   PHE A 642      21.410   2.270  17.283  1.00  0.00           H  
ATOM   3097  HA  PHE A 642      20.595   3.722  14.954  1.00  0.00           H  
ATOM   3098  HB3 PHE A 642      23.037   3.910  16.752  1.00  0.00           H  
ATOM   3099  HB2 PHE A 642      21.579   4.856  16.796  1.00  0.00           H  
ATOM   3100  HD1 PHE A 642      21.044   6.514  15.016  1.00  0.00           H  
ATOM   3101  HE1 PHE A 642      21.995   8.120  13.396  1.00  0.00           H  
ATOM   3102  HZ  PHE A 642      24.310   7.880  12.623  1.00  0.00           H  
ATOM   3103  HD2 PHE A 642      24.820   4.435  15.098  1.00  0.00           H  
ATOM   3104  HE2 PHE A 642      25.717   6.044  13.462  1.00  0.00           H  
ATOM   3105  N   GLY A 643      22.998   1.502  14.556  1.00 14.87           N  
ANISOU 3105  N   GLY A 643     2045   1805   1799    265    102    -67
ATOM   3106  CA  GLY A 643      23.730   0.703  13.571  1.00 14.14           C  
ANISOU 3106  CA  GLY A 643     1710   1905   1756    -29     28   -251
ATOM   3107  C   GLY A 643      22.780  -0.021  12.604  1.00 13.81           C  
ANISOU 3107  C   GLY A 643     1416   2091   1738     36     30   -138
ATOM   3108  O   GLY A 643      23.128  -0.193  11.437  1.00 15.27           O  
ANISOU 3108  O   GLY A 643     2336   1798   1666    234    -63   -439
ATOM   3109  H   GLY A 643      23.047   1.192  15.518  1.00  0.00           H  
ATOM   3110  HA3 GLY A 643      24.321  -0.044  14.098  1.00  0.00           H  
ATOM   3111  HA2 GLY A 643      24.423   1.337  13.016  1.00  0.00           H  
ATOM   3112  N   ILE A 644      21.576  -0.399  13.069  1.00 12.80           N  
ANISOU 3112  N   ILE A 644     1986   1840   1035   -182    238   -180
ATOM   3113  CA  ILE A 644      20.504  -0.931  12.228  1.00 13.64           C  
ANISOU 3113  CA  ILE A 644     1666   2088   1428    -17     19   -162
ATOM   3114  C   ILE A 644      19.813   0.184  11.411  1.00 12.50           C  
ANISOU 3114  C   ILE A 644     1968   1362   1418   -259    201   -312
ATOM   3115  O   ILE A 644      19.441  -0.073  10.271  1.00 13.46           O  
ANISOU 3115  O   ILE A 644     1866   1813   1436     50   -184    -26
ATOM   3116  CB  ILE A 644      19.446  -1.726  13.049  1.00 14.69           C  
ANISOU 3116  CB  ILE A 644     2111   1959   1509   -110    121   -111
ATOM   3117  CG1 ILE A 644      20.069  -2.938  13.786  1.00 15.29           C  
ANISOU 3117  CG1 ILE A 644     2216   1942   1651     23    -73   -264
ATOM   3118  CG2 ILE A 644      18.211  -2.163  12.230  1.00 15.89           C  
ANISOU 3118  CG2 ILE A 644     1940   2476   1621    101     54   -483
ATOM   3119  CD1 ILE A 644      20.411  -4.145  12.902  1.00 17.01           C  
ANISOU 3119  CD1 ILE A 644     2352   1811   2299    -22    -21   -366
ATOM   3120  H   ILE A 644      21.352  -0.255  14.044  1.00  0.00           H  
ATOM   3121  HA  ILE A 644      20.954  -1.618  11.510  1.00  0.00           H  
ATOM   3122  HB  ILE A 644      19.084  -1.061  13.833  1.00  0.00           H  
ATOM   3123 HG13 ILE A 644      19.382  -3.279  14.557  1.00  0.00           H  
ATOM   3124 HG12 ILE A 644      20.959  -2.635  14.334  1.00  0.00           H  
ATOM   3125 HG21 ILE A 644      17.540  -2.785  12.817  1.00  0.00           H  
ATOM   3126 HG22 ILE A 644      17.621  -1.316  11.884  1.00  0.00           H  
ATOM   3127 HG23 ILE A 644      18.511  -2.718  11.343  1.00  0.00           H  
ATOM   3128 HD11 ILE A 644      21.122  -4.797  13.409  1.00  0.00           H  
ATOM   3129 HD12 ILE A 644      19.526  -4.742  12.691  1.00  0.00           H  
ATOM   3130 HD13 ILE A 644      20.847  -3.849  11.948  1.00  0.00           H  
ATOM   3131  N   VAL A 645      19.708   1.411  11.953  1.00 12.34           N  
ANISOU 3131  N   VAL A 645     1508   1654   1524    -73      9   -522
ATOM   3132  CA  VAL A 645      19.254   2.589  11.202  1.00 13.09           C  
ANISOU 3132  CA  VAL A 645     1423   1797   1751    -33     90   -347
ATOM   3133  C   VAL A 645      20.236   2.999  10.081  1.00 13.16           C  
ANISOU 3133  C   VAL A 645     1597   1853   1548   -167   -104     -6
ATOM   3134  O   VAL A 645      19.773   3.345   8.995  1.00 14.66           O  
ANISOU 3134  O   VAL A 645     1968   1882   1721     51   -303    257
ATOM   3135  CB  VAL A 645      18.913   3.786  12.137  1.00 13.77           C  
ANISOU 3135  CB  VAL A 645     1907   1550   1774      4     73   -240
ATOM   3136  CG1 VAL A 645      18.785   5.158  11.444  1.00 15.57           C  
ANISOU 3136  CG1 VAL A 645     2295   2007   1613    -62   -121     51
ATOM   3137  CG2 VAL A 645      17.631   3.500  12.941  1.00 15.31           C  
ANISOU 3137  CG2 VAL A 645     2211   2108   1496   -182     70   -402
ATOM   3138  H   VAL A 645      20.012   1.570  12.904  1.00  0.00           H  
ATOM   3139  HA  VAL A 645      18.334   2.315  10.693  1.00  0.00           H  
ATOM   3140  HB  VAL A 645      19.719   3.886  12.860  1.00  0.00           H  
ATOM   3141 HG11 VAL A 645      18.470   5.922  12.153  1.00  0.00           H  
ATOM   3142 HG12 VAL A 645      19.739   5.498  11.042  1.00  0.00           H  
ATOM   3143 HG13 VAL A 645      18.056   5.134  10.633  1.00  0.00           H  
ATOM   3144 HG21 VAL A 645      17.437   4.282  13.675  1.00  0.00           H  
ATOM   3145 HG22 VAL A 645      16.762   3.438  12.286  1.00  0.00           H  
ATOM   3146 HG23 VAL A 645      17.694   2.558  13.484  1.00  0.00           H  
ATOM   3147  N   LEU A 646      21.556   2.874  10.324  1.00 11.24           N  
ANISOU 3147  N   LEU A 646     1551   1687   1030    -42   -229    103
ATOM   3148  CA  LEU A 646      22.597   3.008   9.299  1.00 14.32           C  
ANISOU 3148  CA  LEU A 646     1763   2083   1593    188    153     58
ATOM   3149  C   LEU A 646      22.489   1.919   8.220  1.00 15.58           C  
ANISOU 3149  C   LEU A 646     2007   1940   1969   -461     23    123
ATOM   3150  O   LEU A 646      22.692   2.236   7.050  1.00 16.52           O  
ANISOU 3150  O   LEU A 646     2363   2100   1812      2    156    -90
ATOM   3151  CB  LEU A 646      24.014   2.973   9.916  1.00 15.16           C  
ANISOU 3151  CB  LEU A 646     1910   2599   1251    337    -54    205
ATOM   3152  CG  LEU A 646      24.403   4.166  10.811  1.00 14.92           C  
ANISOU 3152  CG  LEU A 646     1541   2652   1476    115    125    288
ATOM   3153  CD1 LEU A 646      25.821   3.958  11.387  1.00 18.12           C  
ANISOU 3153  CD1 LEU A 646     1455   3440   1990   -689    -86    371
ATOM   3154  CD2 LEU A 646      24.250   5.523  10.096  1.00 18.87           C  
ANISOU 3154  CD2 LEU A 646     2017   2904   2248     14   -512    555
ATOM   3155  H   LEU A 646      21.867   2.614  11.251  1.00  0.00           H  
ATOM   3156  HA  LEU A 646      22.444   3.965   8.800  1.00  0.00           H  
ATOM   3157  HB3 LEU A 646      24.750   2.909   9.111  1.00  0.00           H  
ATOM   3158  HB2 LEU A 646      24.129   2.057  10.493  1.00  0.00           H  
ATOM   3159  HG  LEU A 646      23.724   4.194  11.659  1.00  0.00           H  
ATOM   3160 HD11 LEU A 646      26.457   4.838  11.286  1.00  0.00           H  
ATOM   3161 HD12 LEU A 646      25.776   3.714  12.448  1.00  0.00           H  
ATOM   3162 HD13 LEU A 646      26.346   3.141  10.894  1.00  0.00           H  
ATOM   3163 HD21 LEU A 646      25.074   6.204  10.308  1.00  0.00           H  
ATOM   3164 HD22 LEU A 646      24.199   5.416   9.012  1.00  0.00           H  
ATOM   3165 HD23 LEU A 646      23.335   6.021  10.418  1.00  0.00           H  
ATOM   3166  N   TYR A 647      22.135   0.681   8.616  1.00 14.43           N  
ANISOU 3166  N   TYR A 647     2099   1837   1547   -262     66     -1
ATOM   3167  CA  TYR A 647      21.865  -0.424   7.697  1.00 16.04           C  
ANISOU 3167  CA  TYR A 647     1924   2089   2078   -187   -373   -307
ATOM   3168  C   TYR A 647      20.705  -0.100   6.743  1.00 15.03           C  
ANISOU 3168  C   TYR A 647     1811   2162   1735   -327    -61   -149
ATOM   3169  O   TYR A 647      20.886  -0.229   5.539  1.00 16.23           O  
ANISOU 3169  O   TYR A 647     2054   2642   1470    590   -179     37
ATOM   3170  CB  TYR A 647      21.647  -1.744   8.469  1.00 15.27           C  
ANISOU 3170  CB  TYR A 647     2311   2373   1117     90   -528   -249
ATOM   3171  CG  TYR A 647      21.510  -2.977   7.597  1.00 15.43           C  
ANISOU 3171  CG  TYR A 647     2836   2109    915    218   -281   -248
ATOM   3172  CD1 TYR A 647      20.256  -3.373   7.083  1.00 16.10           C  
ANISOU 3172  CD1 TYR A 647     2766   2173   1177   -192    148   -223
ATOM   3173  CE1 TYR A 647      20.159  -4.500   6.242  1.00 18.01           C  
ANISOU 3173  CE1 TYR A 647     2940   2486   1414    -56     62   -444
ATOM   3174  CZ  TYR A 647      21.314  -5.247   5.935  1.00 20.07           C  
ANISOU 3174  CZ  TYR A 647     3445   2274   1903    -88    408   -775
ATOM   3175  OH  TYR A 647      21.241  -6.323   5.100  1.00 23.78           O  
ANISOU 3175  OH  TYR A 647     5377   1884   1772   -386    306   -480
ATOM   3176  CE2 TYR A 647      22.559  -4.860   6.467  1.00 19.23           C  
ANISOU 3176  CE2 TYR A 647     3168   2569   1566    634    153   -471
ATOM   3177  CD2 TYR A 647      22.659  -3.726   7.287  1.00 19.19           C  
ANISOU 3177  CD2 TYR A 647     2595   2869   1827     86   -131   -645
ATOM   3178  H   TYR A 647      21.995   0.493   9.600  1.00  0.00           H  
ATOM   3179  HA  TYR A 647      22.758  -0.550   7.082  1.00  0.00           H  
ATOM   3180  HB3 TYR A 647      20.760  -1.698   9.091  1.00  0.00           H  
ATOM   3181  HB2 TYR A 647      22.480  -1.903   9.155  1.00  0.00           H  
ATOM   3182  HD1 TYR A 647      19.368  -2.801   7.310  1.00  0.00           H  
ATOM   3183  HE1 TYR A 647      19.203  -4.779   5.825  1.00  0.00           H  
ATOM   3184  HH  TYR A 647      22.111  -6.658   4.861  1.00  0.00           H  
ATOM   3185  HE2 TYR A 647      23.455  -5.414   6.250  1.00  0.00           H  
ATOM   3186  HD2 TYR A 647      23.622  -3.431   7.678  1.00  0.00           H  
ATOM   3187  N   GLU A 648      19.568   0.377   7.275  1.00 14.69           N  
ANISOU 3187  N   GLU A 648     1935   1967   1680    -45     58   -122
ATOM   3188  CA  GLU A 648      18.409   0.797   6.483  1.00 14.21           C  
ANISOU 3188  CA  GLU A 648     2218   1570   1610   -191     -3    351
ATOM   3189  C   GLU A 648      18.702   1.938   5.498  1.00 15.37           C  
ANISOU 3189  C   GLU A 648     2219   2078   1543   -435    161    411
ATOM   3190  O   GLU A 648      18.235   1.874   4.363  1.00 15.39           O  
ANISOU 3190  O   GLU A 648     2163   2037   1647   -106    -17   -257
ATOM   3191  CB  GLU A 648      17.258   1.201   7.410  1.00 14.97           C  
ANISOU 3191  CB  GLU A 648     2334   1581   1770   -227   -101   -199
ATOM   3192  CG  GLU A 648      16.715   0.061   8.281  1.00 14.43           C  
ANISOU 3192  CG  GLU A 648     1704   1871   1906   -244    -99   -120
ATOM   3193  CD  GLU A 648      15.725   0.631   9.290  1.00 14.51           C  
ANISOU 3193  CD  GLU A 648     2063   1820   1629   -273    -91   -407
ATOM   3194  OE1 GLU A 648      16.162   1.018  10.392  1.00 15.87           O  
ANISOU 3194  OE1 GLU A 648     2517   2154   1356   -353    -94   -204
ATOM   3195  OE2 GLU A 648      14.538   0.717   8.924  1.00 15.29           O1-
ANISOU 3195  OE2 GLU A 648     2051   1977   1779    -36   -215    -42
ATOM   3196  H   GLU A 648      19.481   0.464   8.279  1.00  0.00           H  
ATOM   3197  HA  GLU A 648      18.088  -0.055   5.889  1.00  0.00           H  
ATOM   3198  HB3 GLU A 648      16.434   1.590   6.810  1.00  0.00           H  
ATOM   3199  HB2 GLU A 648      17.583   2.028   8.045  1.00  0.00           H  
ATOM   3200  HG3 GLU A 648      17.506  -0.472   8.801  1.00  0.00           H  
ATOM   3201  HG2 GLU A 648      16.222  -0.683   7.654  1.00  0.00           H  
ATOM   3202  N   LEU A 649      19.474   2.945   5.942  1.00 15.81           N  
ANISOU 3202  N   LEU A 649     2180   2042   1783     29     39    -70
ATOM   3203  CA  LEU A 649      19.889   4.093   5.134  1.00 16.08           C  
ANISOU 3203  CA  LEU A 649     2534   1935   1640   -173    -12   -115
ATOM   3204  C   LEU A 649      20.802   3.703   3.958  1.00 16.33           C  
ANISOU 3204  C   LEU A 649     1789   2344   2070    128     44    -17
ATOM   3205  O   LEU A 649      20.641   4.260   2.873  1.00 18.61           O  
ANISOU 3205  O   LEU A 649     2448   2735   1889    299     76   -277
ATOM   3206  CB  LEU A 649      20.594   5.129   6.041  1.00 13.50           C  
ANISOU 3206  CB  LEU A 649     1725   2263   1139    -19   -184     79
ATOM   3207  CG  LEU A 649      19.637   5.960   6.923  1.00 14.21           C  
ANISOU 3207  CG  LEU A 649     2121   2366    911    -45     47    172
ATOM   3208  CD1 LEU A 649      20.398   6.674   8.057  1.00 17.71           C  
ANISOU 3208  CD1 LEU A 649     2560   2733   1436   -639    -39     74
ATOM   3209  CD2 LEU A 649      18.820   6.967   6.096  1.00 15.30           C  
ANISOU 3209  CD2 LEU A 649     2341   1842   1628   -171    -98    174
ATOM   3210  H   LEU A 649      19.802   2.931   6.898  1.00  0.00           H  
ATOM   3211  HA  LEU A 649      18.995   4.546   4.706  1.00  0.00           H  
ATOM   3212  HB3 LEU A 649      21.184   5.824   5.443  1.00  0.00           H  
ATOM   3213  HB2 LEU A 649      21.316   4.601   6.666  1.00  0.00           H  
ATOM   3214  HG  LEU A 649      18.932   5.278   7.399  1.00  0.00           H  
ATOM   3215 HD11 LEU A 649      19.858   6.585   8.998  1.00  0.00           H  
ATOM   3216 HD12 LEU A 649      21.392   6.257   8.216  1.00  0.00           H  
ATOM   3217 HD13 LEU A 649      20.525   7.739   7.857  1.00  0.00           H  
ATOM   3218 HD21 LEU A 649      18.514   7.823   6.695  1.00  0.00           H  
ATOM   3219 HD22 LEU A 649      19.398   7.360   5.261  1.00  0.00           H  
ATOM   3220 HD23 LEU A 649      17.915   6.510   5.696  1.00  0.00           H  
ATOM   3221  N   MET A 650      21.739   2.771   4.193  1.00 15.48           N  
ANISOU 3221  N   MET A 650     2060   2318   1500    317    174    -26
ATOM   3222  CA  MET A 650      22.794   2.413   3.244  1.00 16.90           C  
ANISOU 3222  CA  MET A 650     2209   2162   2051    539    409    -49
ATOM   3223  C   MET A 650      22.475   1.200   2.361  1.00 19.15           C  
ANISOU 3223  C   MET A 650     2180   2657   2437    -38    472   -234
ATOM   3224  O   MET A 650      23.170   1.034   1.362  1.00 21.50           O  
ANISOU 3224  O   MET A 650     3344   2983   1842    -60    660   -224
ATOM   3225  CB  MET A 650      24.097   2.167   4.021  1.00 19.61           C  
ANISOU 3225  CB  MET A 650     2787   2572   2089    359    -62    135
ATOM   3226  CG  MET A 650      24.658   3.413   4.722  1.00 20.89           C  
ANISOU 3226  CG  MET A 650     2672   2745   2520    331  -1047    344
ATOM   3227  SD  MET A 650      25.134   4.771   3.616  1.00 28.68           S  
ANISOU 3227  SD  MET A 650     4479   3568   2851   -821   -241    346
ATOM   3228  CE  MET A 650      23.911   6.016   4.086  1.00 30.08           C  
ANISOU 3228  CE  MET A 650     3504   4810   3114   -347     56   -597
ATOM   3229  H   MET A 650      21.805   2.354   5.113  1.00  0.00           H  
ATOM   3230  HA  MET A 650      22.961   3.244   2.557  1.00  0.00           H  
ATOM   3231  HB3 MET A 650      24.866   1.773   3.355  1.00  0.00           H  
ATOM   3232  HB2 MET A 650      23.914   1.388   4.759  1.00  0.00           H  
ATOM   3233  HG3 MET A 650      25.544   3.116   5.279  1.00  0.00           H  
ATOM   3234  HG2 MET A 650      23.957   3.792   5.463  1.00  0.00           H  
ATOM   3235  HE1 MET A 650      24.099   6.947   3.552  1.00  0.00           H  
ATOM   3236  HE2 MET A 650      22.914   5.664   3.832  1.00  0.00           H  
ATOM   3237  HE3 MET A 650      23.953   6.219   5.157  1.00  0.00           H  
ATOM   3238  N   THR A 651      21.466   0.390   2.717  1.00 18.37           N  
ANISOU 3238  N   THR A 651     2311   2370   2296    -58    648   -251
ATOM   3239  CA  THR A 651      21.019  -0.771   1.937  1.00 18.70           C  
ANISOU 3239  CA  THR A 651     2536   2840   1727   -181    522   -142
ATOM   3240  C   THR A 651      19.655  -0.515   1.262  1.00 19.41           C  
ANISOU 3240  C   THR A 651     2794   3078   1500   -174      2   -910
ATOM   3241  O   THR A 651      19.382  -1.136   0.235  1.00 20.96           O  
ANISOU 3241  O   THR A 651     2970   3681   1313   -477    172  -1045
ATOM   3242  CB  THR A 651      20.868  -2.046   2.822  1.00 17.25           C  
ANISOU 3242  CB  THR A 651     2458   2468   1627    -52    383   -433
ATOM   3243  OG1 THR A 651      19.765  -1.996   3.703  1.00 16.62           O  
ANISOU 3243  OG1 THR A 651     2257   2361   1694   -213    383   -415
ATOM   3244  CG2 THR A 651      22.107  -2.406   3.654  1.00 18.38           C  
ANISOU 3244  CG2 THR A 651     2287   2113   2581   -170    489   -135
ATOM   3245  H   THR A 651      20.970   0.564   3.581  1.00  0.00           H  
ATOM   3246  HA  THR A 651      21.733  -0.998   1.143  1.00  0.00           H  
ATOM   3247  HB  THR A 651      20.673  -2.893   2.161  1.00  0.00           H  
ATOM   3248  HG1 THR A 651      20.009  -1.448   4.458  1.00  0.00           H  
ATOM   3249 HG21 THR A 651      21.886  -3.216   4.339  1.00  0.00           H  
ATOM   3250 HG22 THR A 651      22.915  -2.755   3.032  1.00  0.00           H  
ATOM   3251 HG23 THR A 651      22.491  -1.574   4.240  1.00  0.00           H  
ATOM   3252  N   GLY A 652      18.821   0.363   1.852  1.00 19.38           N  
ANISOU 3252  N   GLY A 652     2840   2883   1641     37    -22   -441
ATOM   3253  CA  GLY A 652      17.427   0.579   1.458  1.00 20.80           C  
ANISOU 3253  CA  GLY A 652     2944   3341   1616    196    -70   -167
ATOM   3254  C   GLY A 652      16.499  -0.560   1.921  1.00 22.76           C  
ANISOU 3254  C   GLY A 652     3110   3394   2143    312   -348    -77
ATOM   3255  O   GLY A 652      15.359  -0.613   1.465  1.00 23.05           O  
ANISOU 3255  O   GLY A 652     3275   3999   1483     82   -440     92
ATOM   3256  H   GLY A 652      19.123   0.849   2.684  1.00  0.00           H  
ATOM   3257  HA3 GLY A 652      17.354   0.699   0.376  1.00  0.00           H  
ATOM   3258  HA2 GLY A 652      17.072   1.507   1.904  1.00  0.00           H  
ATOM   3259  N   GLN A 653      16.981  -1.471   2.786  1.00 18.88           N  
ANISOU 3259  N   GLN A 653     3430   2349   1392     52    -90   -578
ATOM   3260  CA  GLN A 653      16.290  -2.680   3.232  1.00 21.42           C  
ANISOU 3260  CA  GLN A 653     3295   2908   1936   -343   -270   -155
ATOM   3261  C   GLN A 653      16.295  -2.775   4.762  1.00 18.29           C  
ANISOU 3261  C   GLN A 653     2696   2396   1856   -107     74   -343
ATOM   3262  O   GLN A 653      17.238  -2.329   5.414  1.00 19.11           O  
ANISOU 3262  O   GLN A 653     2511   2859   1887    -86     51   -186
ATOM   3263  CB  GLN A 653      17.016  -3.928   2.679  1.00 25.52           C  
ANISOU 3263  CB  GLN A 653     4260   2636   2798  -1120    144  -1279
ATOM   3264  CG  GLN A 653      17.076  -4.024   1.143  1.00 30.19           C  
ANISOU 3264  CG  GLN A 653     5453   2943   3075  -1201   -226  -1022
ATOM   3265  CD  GLN A 653      17.853  -5.253   0.663  1.00 31.23           C  
ANISOU 3265  CD  GLN A 653     6169   2941   2756  -1039    352  -1516
ATOM   3266  OE1 GLN A 653      17.959  -6.258   1.365  1.00 45.43           O  
ANISOU 3266  OE1 GLN A 653     7942   5161   4157  -1370   1760  -2197
ATOM   3267  NE2 GLN A 653      18.390  -5.185  -0.555  1.00 29.50           N  
ANISOU 3267  NE2 GLN A 653     4212   3274   3723   -325    150  -1497
ATOM   3268  H   GLN A 653      17.928  -1.372   3.127  1.00  0.00           H  
ATOM   3269  HA  GLN A 653      15.256  -2.678   2.887  1.00  0.00           H  
ATOM   3270  HB3 GLN A 653      16.514  -4.820   3.060  1.00  0.00           H  
ATOM   3271  HB2 GLN A 653      18.031  -3.968   3.077  1.00  0.00           H  
ATOM   3272  HG3 GLN A 653      17.551  -3.134   0.731  1.00  0.00           H  
ATOM   3273  HG2 GLN A 653      16.066  -4.061   0.733  1.00  0.00           H  
ATOM   3274 HE22 GLN A 653      18.906  -5.968  -0.928  1.00  0.00           H  
ATOM   3275 HE21 GLN A 653      18.288  -4.347  -1.110  1.00  0.00           H  
ATOM   3276  N   LEU A 654      15.277  -3.465   5.293  1.00 18.40           N  
ANISOU 3276  N   LEU A 654     2561   2599   1828   -203    -74   -125
ATOM   3277  CA  LEU A 654      15.267  -4.013   6.647  1.00 17.93           C  
ANISOU 3277  CA  LEU A 654     2725   2504   1583      0     49   -666
ATOM   3278  C   LEU A 654      16.239  -5.211   6.721  1.00 17.43           C  
ANISOU 3278  C   LEU A 654     2622   2207   1793    -59    -12   -401
ATOM   3279  O   LEU A 654      16.298  -5.979   5.758  1.00 18.69           O  
ANISOU 3279  O   LEU A 654     3133   1973   1994    191   -170   -391
ATOM   3280  CB  LEU A 654      13.832  -4.496   6.948  1.00 22.52           C  
ANISOU 3280  CB  LEU A 654     3070   3443   2043   -351    547   -505
ATOM   3281  CG  LEU A 654      12.827  -3.355   7.209  1.00 23.19           C  
ANISOU 3281  CG  LEU A 654     3169   3313   2330   -272    193     25
ATOM   3282  CD1 LEU A 654      11.381  -3.880   7.242  1.00 26.77           C  
ANISOU 3282  CD1 LEU A 654     2598   4703   2866    288   -241    -99
ATOM   3283  CD2 LEU A 654      13.172  -2.556   8.480  1.00 20.46           C  
ANISOU 3283  CD2 LEU A 654     2669   2703   2399    428   -270    306
ATOM   3284  H   LEU A 654      14.542  -3.802   4.683  1.00  0.00           H  
ATOM   3285  HA  LEU A 654      15.563  -3.220   7.333  1.00  0.00           H  
ATOM   3286  HB3 LEU A 654      13.837  -5.155   7.816  1.00  0.00           H  
ATOM   3287  HB2 LEU A 654      13.485  -5.116   6.119  1.00  0.00           H  
ATOM   3288  HG  LEU A 654      12.881  -2.671   6.361  1.00  0.00           H  
ATOM   3289 HD11 LEU A 654      10.705  -3.189   6.736  1.00  0.00           H  
ATOM   3290 HD12 LEU A 654      11.282  -4.846   6.749  1.00  0.00           H  
ATOM   3291 HD13 LEU A 654      11.023  -4.008   8.262  1.00  0.00           H  
ATOM   3292 HD21 LEU A 654      12.298  -2.341   9.093  1.00  0.00           H  
ATOM   3293 HD22 LEU A 654      13.889  -3.075   9.115  1.00  0.00           H  
ATOM   3294 HD23 LEU A 654      13.614  -1.603   8.206  1.00  0.00           H  
ATOM   3295  N   PRO A 655      16.975  -5.377   7.845  1.00 16.78           N  
ANISOU 3295  N   PRO A 655     2130   2294   1949    -48    172   -441
ATOM   3296  CA  PRO A 655      17.834  -6.559   8.044  1.00 19.83           C  
ANISOU 3296  CA  PRO A 655     2921   2420   2191    189    -45     49
ATOM   3297  C   PRO A 655      17.007  -7.851   8.158  1.00 21.13           C  
ANISOU 3297  C   PRO A 655     3052   2765   2209     76   -100   -245
ATOM   3298  O   PRO A 655      15.914  -7.823   8.723  1.00 21.59           O  
ANISOU 3298  O   PRO A 655     2855   3194   2151    124    -19   -632
ATOM   3299  CB  PRO A 655      18.573  -6.244   9.353  1.00 16.89           C  
ANISOU 3299  CB  PRO A 655     2154   2006   2257   -301    165   -298
ATOM   3300  CG  PRO A 655      17.586  -5.398  10.138  1.00 17.90           C  
ANISOU 3300  CG  PRO A 655     2295   1926   2580     20    170    -89
ATOM   3301  CD  PRO A 655      16.931  -4.548   9.054  1.00 17.04           C  
ANISOU 3301  CD  PRO A 655     2282   1958   2234    -11    586   -486
ATOM   3302  HA  PRO A 655      18.550  -6.662   7.227  1.00  0.00           H  
ATOM   3303  HB3 PRO A 655      19.467  -5.658   9.135  1.00  0.00           H  
ATOM   3304  HB2 PRO A 655      18.893  -7.131   9.902  1.00  0.00           H  
ATOM   3305  HG3 PRO A 655      18.049  -4.821  10.933  1.00  0.00           H  
ATOM   3306  HG2 PRO A 655      16.839  -6.045  10.598  1.00  0.00           H  
ATOM   3307  HD2 PRO A 655      15.919  -4.270   9.348  1.00  0.00           H  
ATOM   3308  HD3 PRO A 655      17.504  -3.636   8.878  1.00  0.00           H  
ATOM   3309  N   TYR A 656      17.556  -8.956   7.631  1.00 22.32           N  
ANISOU 3309  N   TYR A 656     3311   2525   2643     34     95   -418
ATOM   3310  CA  TYR A 656      16.991 -10.313   7.695  1.00 19.51           C  
ANISOU 3310  CA  TYR A 656     2938   2117   2356    403     47   -215
ATOM   3311  C   TYR A 656      15.721 -10.500   6.843  1.00 22.32           C  
ANISOU 3311  C   TYR A 656     3597   2667   2213    140   -422   -229
ATOM   3312  O   TYR A 656      14.940 -11.402   7.144  1.00 26.08           O  
ANISOU 3312  O   TYR A 656     4330   2994   2583   -558   -398  -1263
ATOM   3313  CB  TYR A 656      16.726 -10.772   9.156  1.00 17.60           C  
ANISOU 3313  CB  TYR A 656     2407   1852   2428    387   -133   -239
ATOM   3314  CG  TYR A 656      17.728 -10.314  10.196  1.00 17.06           C  
ANISOU 3314  CG  TYR A 656     2369   1891   2220     25    -10   -270
ATOM   3315  CD1 TYR A 656      19.098 -10.578  10.028  1.00 19.50           C  
ANISOU 3315  CD1 TYR A 656     2520   2696   2193     39    -66   -392
ATOM   3316  CE1 TYR A 656      20.017 -10.081  10.965  1.00 17.96           C  
ANISOU 3316  CE1 TYR A 656     2334   2454   2035    646   -233   -113
ATOM   3317  CZ  TYR A 656      19.586  -9.315  12.062  1.00 14.58           C  
ANISOU 3317  CZ  TYR A 656     2103   1888   1546     95   -278    157
ATOM   3318  OH  TYR A 656      20.497  -8.833  12.953  1.00 18.22           O  
ANISOU 3318  OH  TYR A 656     2391   2669   1860   -345   -230   -533
ATOM   3319  CE2 TYR A 656      18.213  -9.062  12.239  1.00 16.89           C  
ANISOU 3319  CE2 TYR A 656     2103   2071   2241     37   -185    -93
ATOM   3320  CD2 TYR A 656      17.288  -9.575  11.312  1.00 16.76           C  
ANISOU 3320  CD2 TYR A 656     1762   2273   2334     10    116   -255
ATOM   3321  H   TYR A 656      18.471  -8.887   7.203  1.00  0.00           H  
ATOM   3322  HA  TYR A 656      17.743 -10.976   7.265  1.00  0.00           H  
ATOM   3323  HB3 TYR A 656      16.643 -11.857   9.202  1.00  0.00           H  
ATOM   3324  HB2 TYR A 656      15.752 -10.394   9.473  1.00  0.00           H  
ATOM   3325  HD1 TYR A 656      19.448 -11.151   9.182  1.00  0.00           H  
ATOM   3326  HE1 TYR A 656      21.056 -10.309  10.837  1.00  0.00           H  
ATOM   3327  HH  TYR A 656      20.104  -8.243  13.606  1.00  0.00           H  
ATOM   3328  HE2 TYR A 656      17.860  -8.488  13.082  1.00  0.00           H  
ATOM   3329  HD2 TYR A 656      16.236  -9.396  11.453  1.00  0.00           H  
ATOM   3330  N   SER A 657      15.521  -9.667   5.806  1.00 27.16           N  
ANISOU 3330  N   SER A 657     3997   2640   3679   -300   -660    499
ATOM   3331  CA  SER A 657      14.344  -9.704   4.924  1.00 29.29           C  
ANISOU 3331  CA  SER A 657     4005   3747   3376     10   -576    343
ATOM   3332  C   SER A 657      14.157 -11.034   4.156  1.00 33.20           C  
ANISOU 3332  C   SER A 657     4660   4255   3697   -993  -1211    272
ATOM   3333  O   SER A 657      13.029 -11.357   3.787  1.00 34.84           O  
ANISOU 3333  O   SER A 657     6012   3405   3820  -1695  -2739      0
ATOM   3334  CB  SER A 657      14.360  -8.466   4.003  1.00 27.67           C  
ANISOU 3334  CB  SER A 657     2686   4851   2973    622  -1046    524
ATOM   3335  OG  SER A 657      15.292  -8.575   2.943  1.00 36.71           O  
ANISOU 3335  OG  SER A 657     3985   6264   3699  -1067     20   -439
ATOM   3336  H   SER A 657      16.196  -8.939   5.619  1.00  0.00           H  
ATOM   3337  HA  SER A 657      13.475  -9.602   5.577  1.00  0.00           H  
ATOM   3338  HB3 SER A 657      14.557  -7.558   4.574  1.00  0.00           H  
ATOM   3339  HB2 SER A 657      13.373  -8.331   3.558  1.00  0.00           H  
ATOM   3340  HG  SER A 657      16.167  -8.737   3.307  1.00  0.00           H  
ATOM   3341  N   ASN A 658      15.253 -11.794   3.987  1.00 35.07           N  
ANISOU 3341  N   ASN A 658     5215   4914   3193   -250  -1650   -661
ATOM   3342  CA  ASN A 658      15.299 -13.144   3.421  1.00 44.00           C  
ANISOU 3342  CA  ASN A 658     6941   4937   4841   -412   -289   -680
ATOM   3343  C   ASN A 658      14.806 -14.256   4.377  1.00 41.14           C  
ANISOU 3343  C   ASN A 658     8042   3754   3832   -565    144  -1904
ATOM   3344  O   ASN A 658      14.510 -15.348   3.894  1.00 45.18           O  
ANISOU 3344  O   ASN A 658     9462   3812   3890    -10    128  -2219
ATOM   3345  CB  ASN A 658      16.735 -13.435   2.908  1.00 47.17           C  
ANISOU 3345  CB  ASN A 658     7044   4822   6055   -409    768  -1777
ATOM   3346  CG  ASN A 658      17.825 -13.526   3.992  1.00 47.40           C  
ANISOU 3346  CG  ASN A 658     8928   4369   4712   -378    453  -2083
ATOM   3347  OD1 ASN A 658      17.947 -12.649   4.847  1.00 39.78           O  
ANISOU 3347  OD1 ASN A 658     7092   5231   2790  -1684    141  -1512
ATOM   3348  ND2 ASN A 658      18.634 -14.586   3.953  1.00 47.86           N  
ANISOU 3348  ND2 ASN A 658     9251   3466   5465  -1193   1684  -1090
ATOM   3349  H   ASN A 658      16.139 -11.439   4.321  1.00  0.00           H  
ATOM   3350  HA  ASN A 658      14.633 -13.169   2.557  1.00  0.00           H  
ATOM   3351  HB3 ASN A 658      17.032 -12.659   2.202  1.00  0.00           H  
ATOM   3352  HB2 ASN A 658      16.727 -14.365   2.337  1.00  0.00           H  
ATOM   3353 HD22 ASN A 658      19.367 -14.686   4.639  1.00  0.00           H  
ATOM   3354 HD21 ASN A 658      18.521 -15.292   3.240  1.00  0.00           H  
ATOM   3355  N   ILE A 659      14.744 -13.980   5.692  1.00 37.90           N  
ANISOU 3355  N   ILE A 659     8734   2739   2925   -722   -905    -58
ATOM   3356  CA  ILE A 659      14.333 -14.930   6.726  1.00 35.92           C  
ANISOU 3356  CA  ILE A 659     6669   2613   4364  -1463  -1150    225
ATOM   3357  C   ILE A 659      12.886 -14.613   7.131  1.00 41.45           C  
ANISOU 3357  C   ILE A 659     6657   4041   5049   -989  -1193   -213
ATOM   3358  O   ILE A 659      12.626 -13.563   7.718  1.00 41.58           O  
ANISOU 3358  O   ILE A 659     6776   4333   4687    314   -752    331
ATOM   3359  CB  ILE A 659      15.263 -14.866   7.975  1.00 33.60           C  
ANISOU 3359  CB  ILE A 659     5780   3042   3941   -234   -632   -696
ATOM   3360  CG1 ILE A 659      16.702 -15.276   7.584  1.00 43.73           C  
ANISOU 3360  CG1 ILE A 659     5891   6042   4682  -1036   -648   -518
ATOM   3361  CG2 ILE A 659      14.769 -15.728   9.162  1.00 38.09           C  
ANISOU 3361  CG2 ILE A 659     6711   2880   4880   -217  -1083    371
ATOM   3362  CD1 ILE A 659      17.757 -14.954   8.644  1.00 40.08           C  
ANISOU 3362  CD1 ILE A 659     6062   6517   2649     36   -350   -426
ATOM   3363  H   ILE A 659      14.980 -13.052   6.019  1.00  0.00           H  
ATOM   3364  HA  ILE A 659      14.375 -15.951   6.339  1.00  0.00           H  
ATOM   3365  HB  ILE A 659      15.300 -13.831   8.319  1.00  0.00           H  
ATOM   3366 HG13 ILE A 659      17.006 -14.778   6.665  1.00  0.00           H  
ATOM   3367 HG12 ILE A 659      16.728 -16.344   7.362  1.00  0.00           H  
ATOM   3368 HG21 ILE A 659      15.466 -15.705   9.999  1.00  0.00           H  
ATOM   3369 HG22 ILE A 659      13.814 -15.382   9.552  1.00  0.00           H  
ATOM   3370 HG23 ILE A 659      14.648 -16.770   8.864  1.00  0.00           H  
ATOM   3371 HD11 ILE A 659      18.755 -14.976   8.206  1.00  0.00           H  
ATOM   3372 HD12 ILE A 659      17.604 -13.965   9.072  1.00  0.00           H  
ATOM   3373 HD13 ILE A 659      17.738 -15.683   9.453  1.00  0.00           H  
ATOM   3374  N   ASN A 660      11.973 -15.530   6.781  1.00 41.74           N  
ANISOU 3374  N   ASN A 660     6539   5126   4191  -1498  -2046    814
ATOM   3375  CA  ASN A 660      10.520 -15.367   6.913  1.00 38.94           C  
ANISOU 3375  CA  ASN A 660     5954   5847   2993  -2487   -297    206
ATOM   3376  C   ASN A 660       9.981 -15.687   8.324  1.00 40.47           C  
ANISOU 3376  C   ASN A 660     5419   6965   2992  -1675   -586    735
ATOM   3377  O   ASN A 660       8.798 -15.451   8.568  1.00 52.89           O  
ANISOU 3377  O   ASN A 660     6162   8734   5199  -1783    574   1968
ATOM   3378  CB  ASN A 660       9.829 -16.251   5.845  1.00  0.00           C  
ATOM   3379  CG  ASN A 660      10.181 -15.842   4.409  1.00  0.00           C  
ATOM   3380  OD1 ASN A 660       9.634 -14.874   3.887  1.00  0.00           O  
ATOM   3381  ND2 ASN A 660      11.093 -16.574   3.765  1.00  0.00           N  
ATOM   3382  H   ASN A 660      12.280 -16.365   6.305  1.00  0.00           H  
ATOM   3383  HA  ASN A 660      10.279 -14.323   6.701  1.00  0.00           H  
ATOM   3384  HB2 ASN A 660      10.073 -17.303   6.002  1.00  0.00           H  
ATOM   3385  HB3 ASN A 660       8.744 -16.174   5.942  1.00  0.00           H  
ATOM   3386 HD22 ASN A 660      11.357 -16.328   2.822  1.00  0.00           H  
ATOM   3387 HD21 ASN A 660      11.524 -17.373   4.205  1.00  0.00           H  
ATOM   3388  N   ASN A 661      10.834 -16.212   9.219  1.00 34.91           N  
ANISOU 3388  N   ASN A 661     4231   5166   3868   -915   -340    150
ATOM   3389  CA  ASN A 661      10.477 -16.644  10.568  1.00 39.01           C  
ANISOU 3389  CA  ASN A 661     5492   5065   4264  -1655   -774    169
ATOM   3390  C   ASN A 661      11.046 -15.639  11.589  1.00 34.24           C  
ANISOU 3390  C   ASN A 661     4625   3718   4665  -2289     61    597
ATOM   3391  O   ASN A 661      12.266 -15.524  11.710  1.00 38.55           O  
ANISOU 3391  O   ASN A 661     4741   4289   5616   -461   -738   -758
ATOM   3392  CB  ASN A 661      11.034 -18.079  10.756  1.00 46.84           C  
ANISOU 3392  CB  ASN A 661     8464   3762   5570  -2367  -1924     83
ATOM   3393  CG  ASN A 661      10.503 -18.837  11.980  1.00 52.45           C  
ANISOU 3393  CG  ASN A 661     9853   3455   6620  -3223  -1028   -397
ATOM   3394  OD1 ASN A 661      10.234 -18.251  13.026  1.00 51.41           O  
ANISOU 3394  OD1 ASN A 661     9095   4090   6345  -1031  -2091   -428
ATOM   3395  ND2 ASN A 661      10.376 -20.160  11.865  1.00 60.02           N  
ANISOU 3395  ND2 ASN A 661    11334   3432   8037  -3734  -3546    970
ATOM   3396  H   ASN A 661      11.799 -16.348   8.954  1.00  0.00           H  
ATOM   3397  HA  ASN A 661       9.395 -16.676  10.713  1.00  0.00           H  
ATOM   3398  HB3 ASN A 661      12.122 -18.077  10.767  1.00  0.00           H  
ATOM   3399  HB2 ASN A 661      10.754 -18.668   9.880  1.00  0.00           H  
ATOM   3400 HD22 ASN A 661      10.039 -20.703  12.648  1.00  0.00           H  
ATOM   3401 HD21 ASN A 661      10.618 -20.629  11.004  1.00  0.00           H  
ATOM   3402  N   ARG A 662      10.151 -14.948  12.322  1.00 41.62           N  
ANISOU 3402  N   ARG A 662     4516   5362   5935  -1079   -208    616
ATOM   3403  CA  ARG A 662      10.510 -13.995  13.382  1.00 41.08           C  
ANISOU 3403  CA  ARG A 662     3831   5389   6385   -887    -10    470
ATOM   3404  C   ARG A 662      11.178 -14.654  14.600  1.00 41.86           C  
ANISOU 3404  C   ARG A 662     5072   4361   6471  -1445      6   1086
ATOM   3405  O   ARG A 662      12.076 -14.044  15.177  1.00 35.33           O  
ANISOU 3405  O   ARG A 662     3733   4204   5486   -144    -53   1073
ATOM   3406  CB  ARG A 662       9.280 -13.190  13.849  1.00  0.00           C  
ATOM   3407  CG  ARG A 662       8.622 -12.336  12.750  1.00  0.00           C  
ATOM   3408  CD  ARG A 662       7.529 -11.385  13.281  1.00  0.00           C  
ATOM   3409  NE  ARG A 662       6.323 -12.096  13.745  1.00  0.00           N  
ATOM   3410  CZ  ARG A 662       5.257 -12.464  13.009  1.00  0.00           C  
ATOM   3411  NH1 ARG A 662       5.163 -12.191  11.698  1.00  0.00           N  
ATOM   3412  NH2 ARG A 662       4.259 -13.129  13.604  1.00  0.00           N1+
ATOM   3413  H   ARG A 662       9.164 -15.096  12.170  1.00  0.00           H  
ATOM   3414  HA  ARG A 662      11.231 -13.291  12.962  1.00  0.00           H  
ATOM   3415  HB2 ARG A 662       8.543 -13.867  14.285  1.00  0.00           H  
ATOM   3416  HB3 ARG A 662       9.589 -12.524  14.657  1.00  0.00           H  
ATOM   3417  HG2 ARG A 662       9.355 -11.778  12.168  1.00  0.00           H  
ATOM   3418  HG3 ARG A 662       8.163 -13.034  12.048  1.00  0.00           H  
ATOM   3419  HD2 ARG A 662       7.911 -10.901  14.181  1.00  0.00           H  
ATOM   3420  HD3 ARG A 662       7.318 -10.571  12.586  1.00  0.00           H  
ATOM   3421  HE  ARG A 662       6.343 -12.379  14.715  1.00  0.00           H  
ATOM   3422 HH12 ARG A 662       4.356 -12.481  11.166  1.00  0.00           H  
ATOM   3423 HH11 ARG A 662       5.909 -11.693  11.234  1.00  0.00           H  
ATOM   3424 HH22 ARG A 662       3.450 -13.422  13.075  1.00  0.00           H  
ATOM   3425 HH21 ARG A 662       4.310 -13.357  14.587  1.00  0.00           H  
ATOM   3426  N   ASP A 663      10.753 -15.878  14.956  1.00 38.49           N  
ANISOU 3426  N   ASP A 663     4980   4216   5428  -1783    -64    347
ATOM   3427  CA  ASP A 663      11.327 -16.667  16.054  1.00 37.03           C  
ANISOU 3427  CA  ASP A 663     4757   3308   6004   -969   -246    462
ATOM   3428  C   ASP A 663      12.753 -17.151  15.747  1.00 33.73           C  
ANISOU 3428  C   ASP A 663     5309   3027   4480    -84   -721   -204
ATOM   3429  O   ASP A 663      13.558 -17.240  16.673  1.00 29.82           O  
ANISOU 3429  O   ASP A 663     4042   2518   4767   -784   -640    -44
ATOM   3430  CB  ASP A 663      10.439 -17.860  16.490  1.00 42.30           C  
ANISOU 3430  CB  ASP A 663     4692   4379   6999  -1640    189     39
ATOM   3431  CG  ASP A 663       8.993 -17.519  16.896  1.00 49.30           C  
ANISOU 3431  CG  ASP A 663     5858   5427   7443  -2122   1382   -454
ATOM   3432  OD1 ASP A 663       8.735 -16.363  17.304  1.00 56.84           O  
ANISOU 3432  OD1 ASP A 663     6101   6442   9052   -922   1541  -1801
ATOM   3433  OD2 ASP A 663       8.180 -18.469  16.912  1.00 57.87           O1-
ANISOU 3433  OD2 ASP A 663     6308   5677  10003  -2614   1135     56
ATOM   3434  H   ASP A 663      10.013 -16.325  14.431  1.00  0.00           H  
ATOM   3435  HA  ASP A 663      11.415 -16.000  16.913  1.00  0.00           H  
ATOM   3436  HB3 ASP A 663      10.898 -18.363  17.343  1.00  0.00           H  
ATOM   3437  HB2 ASP A 663      10.396 -18.593  15.682  1.00  0.00           H  
ATOM   3438  N   GLN A 664      13.056 -17.403  14.461  1.00 34.83           N  
ANISOU 3438  N   GLN A 664     4489   4029   4713   -185   -447   -809
ATOM   3439  CA  GLN A 664      14.402 -17.724  13.990  1.00 34.47           C  
ANISOU 3439  CA  GLN A 664     5628   3012   4456     72     27   -712
ATOM   3440  C   GLN A 664      15.338 -16.504  14.103  1.00 30.34           C  
ANISOU 3440  C   GLN A 664     4810   3424   3295     17    332   -844
ATOM   3441  O   GLN A 664      16.473 -16.675  14.536  1.00 30.53           O  
ANISOU 3441  O   GLN A 664     5516   2920   3164   -753   -388     96
ATOM   3442  CB  GLN A 664      14.325 -18.261  12.549  1.00 38.53           C  
ANISOU 3442  CB  GLN A 664     7593   2714   4330   -632  -1477   -992
ATOM   3443  CG  GLN A 664      15.623 -18.922  12.051  1.00 44.71           C  
ANISOU 3443  CG  GLN A 664     7620   4568   4796   -279   -570  -1402
ATOM   3444  CD  GLN A 664      15.611 -19.214  10.548  1.00 47.41           C  
ANISOU 3444  CD  GLN A 664     8059   5174   4779   -336   -523  -1394
ATOM   3445  OE1 GLN A 664      14.554 -19.320   9.928  1.00 49.49           O  
ANISOU 3445  OE1 GLN A 664     8674   4901   5229   1603   -148  -1300
ATOM   3446  NE2 GLN A 664      16.795 -19.363   9.954  1.00 46.74           N  
ANISOU 3446  NE2 GLN A 664     9030   3580   5146    124  -1754   -440
ATOM   3447  H   GLN A 664      12.338 -17.316  13.756  1.00  0.00           H  
ATOM   3448  HA  GLN A 664      14.798 -18.518  14.627  1.00  0.00           H  
ATOM   3449  HB3 GLN A 664      14.053 -17.443  11.881  1.00  0.00           H  
ATOM   3450  HB2 GLN A 664      13.521 -18.995  12.482  1.00  0.00           H  
ATOM   3451  HG3 GLN A 664      15.797 -19.853  12.591  1.00  0.00           H  
ATOM   3452  HG2 GLN A 664      16.472 -18.280  12.265  1.00  0.00           H  
ATOM   3453 HE22 GLN A 664      16.842 -19.566   8.966  1.00  0.00           H  
ATOM   3454 HE21 GLN A 664      17.650 -19.288  10.487  1.00  0.00           H  
ATOM   3455  N   ILE A 665      14.843 -15.295  13.774  1.00 31.71           N  
ANISOU 3455  N   ILE A 665     3974   4408   3666   -413   -229    -27
ATOM   3456  CA  ILE A 665      15.573 -14.035  13.958  1.00 28.22           C  
ANISOU 3456  CA  ILE A 665     3960   3827   2934   -353    367     54
ATOM   3457  C   ILE A 665      15.887 -13.752  15.442  1.00 23.95           C  
ANISOU 3457  C   ILE A 665     3443   2677   2977   -474    652   -393
ATOM   3458  O   ILE A 665      17.033 -13.432  15.753  1.00 25.02           O  
ANISOU 3458  O   ILE A 665     3424   2563   3517   -344      2    177
ATOM   3459  CB  ILE A 665      14.832 -12.817  13.320  1.00 27.66           C  
ANISOU 3459  CB  ILE A 665     3448   4030   3029   -759   -585     61
ATOM   3460  CG1 ILE A 665      14.805 -12.949  11.779  1.00 29.48           C  
ANISOU 3460  CG1 ILE A 665     3385   4907   2906   -689    305   1245
ATOM   3461  CG2 ILE A 665      15.390 -11.430  13.725  1.00 28.66           C  
ANISOU 3461  CG2 ILE A 665     3746   4204   2940  -1377   -790    329
ATOM   3462  CD1 ILE A 665      13.779 -12.041  11.086  1.00 34.67           C  
ANISOU 3462  CD1 ILE A 665     4101   4414   4656   -122   -399    939
ATOM   3463  H   ILE A 665      13.897 -15.220  13.424  1.00  0.00           H  
ATOM   3464  HA  ILE A 665      16.529 -14.145  13.443  1.00  0.00           H  
ATOM   3465  HB  ILE A 665      13.797 -12.850  13.658  1.00  0.00           H  
ATOM   3466 HG13 ILE A 665      14.577 -13.976  11.497  1.00  0.00           H  
ATOM   3467 HG12 ILE A 665      15.799 -12.749  11.378  1.00  0.00           H  
ATOM   3468 HG21 ILE A 665      14.876 -10.623  13.207  1.00  0.00           H  
ATOM   3469 HG22 ILE A 665      15.266 -11.224  14.788  1.00  0.00           H  
ATOM   3470 HG23 ILE A 665      16.452 -11.352  13.491  1.00  0.00           H  
ATOM   3471 HD11 ILE A 665      13.635 -12.348  10.049  1.00  0.00           H  
ATOM   3472 HD12 ILE A 665      12.808 -12.086  11.579  1.00  0.00           H  
ATOM   3473 HD13 ILE A 665      14.102 -11.001  11.075  1.00  0.00           H  
ATOM   3474  N   ILE A 666      14.888 -13.926  16.326  1.00 23.85           N  
ANISOU 3474  N   ILE A 666     3348   2834   2878   -445    399   -466
ATOM   3475  CA  ILE A 666      15.011 -13.757  17.778  1.00 23.68           C  
ANISOU 3475  CA  ILE A 666     3269   2943   2783   -875    451   -449
ATOM   3476  C   ILE A 666      16.056 -14.699  18.410  1.00 26.03           C  
ANISOU 3476  C   ILE A 666     4161   2485   3242   -841    -12    -87
ATOM   3477  O   ILE A 666      16.899 -14.230  19.177  1.00 22.15           O  
ANISOU 3477  O   ILE A 666     3595   1981   2840   -350    179    -54
ATOM   3478  CB  ILE A 666      13.629 -13.911  18.490  1.00 27.09           C  
ANISOU 3478  CB  ILE A 666     3642   2957   3692  -1105    830      8
ATOM   3479  CG1 ILE A 666      12.707 -12.716  18.151  1.00 27.52           C  
ANISOU 3479  CG1 ILE A 666     3999   2545   3912   -917    864     47
ATOM   3480  CG2 ILE A 666      13.675 -14.111  20.024  1.00 35.42           C  
ANISOU 3480  CG2 ILE A 666     5793   3871   3791  -1626    304   -518
ATOM   3481  CD1 ILE A 666      11.213 -12.995  18.376  1.00 33.51           C  
ANISOU 3481  CD1 ILE A 666     4072   3103   5555  -1295    486     90
ATOM   3482  H   ILE A 666      13.971 -14.190  15.988  1.00  0.00           H  
ATOM   3483  HA  ILE A 666      15.367 -12.743  17.943  1.00  0.00           H  
ATOM   3484  HB  ILE A 666      13.164 -14.805  18.074  1.00  0.00           H  
ATOM   3485 HG13 ILE A 666      12.842 -12.409  17.115  1.00  0.00           H  
ATOM   3486 HG12 ILE A 666      13.002 -11.852  18.747  1.00  0.00           H  
ATOM   3487 HG21 ILE A 666      12.672 -14.168  20.445  1.00  0.00           H  
ATOM   3488 HG22 ILE A 666      14.175 -15.036  20.310  1.00  0.00           H  
ATOM   3489 HG23 ILE A 666      14.189 -13.286  20.518  1.00  0.00           H  
ATOM   3490 HD11 ILE A 666      10.602 -12.434  17.669  1.00  0.00           H  
ATOM   3491 HD12 ILE A 666      10.969 -14.050  18.249  1.00  0.00           H  
ATOM   3492 HD13 ILE A 666      10.907 -12.702  19.381  1.00  0.00           H  
ATOM   3493  N   GLU A 667      16.000 -15.989  18.035  1.00 30.00           N  
ANISOU 3493  N   GLU A 667     4706   2685   4007   -562   -510   -344
ATOM   3494  CA  GLU A 667      16.926 -17.034  18.464  1.00 31.63           C  
ANISOU 3494  CA  GLU A 667     5631   2283   4104   -549   -500    847
ATOM   3495  C   GLU A 667      18.370 -16.785  18.000  1.00 30.01           C  
ANISOU 3495  C   GLU A 667     5466   3256   2680   -310   -603    320
ATOM   3496  O   GLU A 667      19.280 -16.784  18.830  1.00 24.52           O  
ANISOU 3496  O   GLU A 667     4449   2291   2576    395   -170    586
ATOM   3497  CB  GLU A 667      16.387 -18.411  17.996  1.00 35.71           C  
ANISOU 3497  CB  GLU A 667     7400   2018   4148   -875   -422   1073
ATOM   3498  CG  GLU A 667      17.304 -19.643  18.223  1.00 50.28           C  
ANISOU 3498  CG  GLU A 667     8143   3128   7833    188    320    348
ATOM   3499  CD  GLU A 667      17.590 -20.028  19.687  1.00 62.83           C  
ANISOU 3499  CD  GLU A 667     9259   5751   8861   2244    691    743
ATOM   3500  OE1 GLU A 667      16.879 -19.544  20.595  1.00 73.87           O  
ANISOU 3500  OE1 GLU A 667     9017   6444  12604  -1150   2446  -2490
ATOM   3501  OE2 GLU A 667      18.525 -20.838  19.877  1.00 79.87           O1-
ANISOU 3501  OE2 GLU A 667    10505   5464  14376   3786   2904    550
ATOM   3502  H   GLU A 667      15.270 -16.283  17.400  1.00  0.00           H  
ATOM   3503  HA  GLU A 667      16.932 -17.022  19.555  1.00  0.00           H  
ATOM   3504  HB3 GLU A 667      16.160 -18.356  16.930  1.00  0.00           H  
ATOM   3505  HB2 GLU A 667      15.424 -18.595  18.474  1.00  0.00           H  
ATOM   3506  HG3 GLU A 667      18.248 -19.512  17.694  1.00  0.00           H  
ATOM   3507  HG2 GLU A 667      16.831 -20.507  17.755  1.00  0.00           H  
ATOM   3508  N   MET A 668      18.546 -16.602  16.680  1.00 28.79           N  
ANISOU 3508  N   MET A 668     5657   2403   2875    321     76    590
ATOM   3509  CA  MET A 668      19.860 -16.526  16.050  1.00 25.05           C  
ANISOU 3509  CA  MET A 668     4718   1552   3247    351    102   -361
ATOM   3510  C   MET A 668      20.625 -15.224  16.337  1.00 26.33           C  
ANISOU 3510  C   MET A 668     3985   1879   4140    529    284   -720
ATOM   3511  O   MET A 668      21.838 -15.302  16.518  1.00 27.08           O  
ANISOU 3511  O   MET A 668     4133   2456   3700    198   -288   -152
ATOM   3512  CB  MET A 668      19.777 -16.817  14.544  1.00 29.91           C  
ANISOU 3512  CB  MET A 668     5593   2277   3491    100     48   -763
ATOM   3513  CG  MET A 668      19.285 -18.231  14.199  1.00 37.82           C  
ANISOU 3513  CG  MET A 668     7046   2884   4440   -277   -977  -1228
ATOM   3514  SD  MET A 668      19.574 -18.768  12.488  1.00 44.99           S  
ANISOU 3514  SD  MET A 668     8483   3789   4820   -629    -39  -1496
ATOM   3515  CE  MET A 668      19.029 -17.325  11.530  1.00 63.57           C  
ANISOU 3515  CE  MET A 668     9815   6069   8267   -608  -2349    -12
ATOM   3516  H   MET A 668      17.746 -16.596  16.060  1.00  0.00           H  
ATOM   3517  HA  MET A 668      20.453 -17.334  16.474  1.00  0.00           H  
ATOM   3518  HB3 MET A 668      20.768 -16.702  14.115  1.00  0.00           H  
ATOM   3519  HB2 MET A 668      19.136 -16.078  14.068  1.00  0.00           H  
ATOM   3520  HG3 MET A 668      18.228 -18.350  14.420  1.00  0.00           H  
ATOM   3521  HG2 MET A 668      19.791 -18.945  14.843  1.00  0.00           H  
ATOM   3522  HE1 MET A 668      18.843 -17.611  10.496  1.00  0.00           H  
ATOM   3523  HE2 MET A 668      18.126 -16.879  11.942  1.00  0.00           H  
ATOM   3524  HE3 MET A 668      19.804 -16.566  11.516  1.00  0.00           H  
ATOM   3525  N   VAL A 669      19.940 -14.066  16.406  1.00 20.57           N  
ANISOU 3525  N   VAL A 669     2981   1965   2867    205   -233     -9
ATOM   3526  CA  VAL A 669      20.587 -12.799  16.781  1.00 19.99           C  
ANISOU 3526  CA  VAL A 669     3240   2246   2108     18   -188   -138
ATOM   3527  C   VAL A 669      20.939 -12.761  18.282  1.00 20.10           C  
ANISOU 3527  C   VAL A 669     3123   2432   2080    207    -76   -297
ATOM   3528  O   VAL A 669      21.985 -12.214  18.633  1.00 23.55           O  
ANISOU 3528  O   VAL A 669     3055   2420   3472    290     63   -130
ATOM   3529  CB  VAL A 669      19.753 -11.535  16.423  1.00 20.47           C  
ANISOU 3529  CB  VAL A 669     2611   2437   2726   -125   -428    204
ATOM   3530  CG1 VAL A 669      20.429 -10.214  16.864  1.00 22.51           C  
ANISOU 3530  CG1 VAL A 669     3501   2757   2293   -232   -355    -34
ATOM   3531  CG2 VAL A 669      19.474 -11.458  14.913  1.00 20.20           C  
ANISOU 3531  CG2 VAL A 669     2779   2171   2723   -559   -357    211
ATOM   3532  H   VAL A 669      18.941 -14.041  16.246  1.00  0.00           H  
ATOM   3533  HA  VAL A 669      21.526 -12.734  16.230  1.00  0.00           H  
ATOM   3534  HB  VAL A 669      18.787 -11.599  16.926  1.00  0.00           H  
ATOM   3535 HG11 VAL A 669      19.978  -9.350  16.385  1.00  0.00           H  
ATOM   3536 HG12 VAL A 669      20.372 -10.053  17.941  1.00  0.00           H  
ATOM   3537 HG13 VAL A 669      21.480 -10.199  16.578  1.00  0.00           H  
ATOM   3538 HG21 VAL A 669      18.812 -10.623  14.683  1.00  0.00           H  
ATOM   3539 HG22 VAL A 669      20.396 -11.321  14.348  1.00  0.00           H  
ATOM   3540 HG23 VAL A 669      18.995 -12.359  14.537  1.00  0.00           H  
ATOM   3541  N   GLY A 670      20.102 -13.399  19.121  1.00 22.64           N  
ANISOU 3541  N   GLY A 670     3596   2813   2191    270    -85    354
ATOM   3542  CA  GLY A 670      20.331 -13.557  20.554  1.00 22.56           C  
ANISOU 3542  CA  GLY A 670     4219   1965   2387    136   -729    -97
ATOM   3543  C   GLY A 670      21.595 -14.385  20.827  1.00 30.28           C  
ANISOU 3543  C   GLY A 670     4077   3855   3574     57   -798    340
ATOM   3544  O   GLY A 670      22.427 -13.955  21.619  1.00 27.94           O  
ANISOU 3544  O   GLY A 670     4482   3038   3094   -362   -425   -147
ATOM   3545  H   GLY A 670      19.266 -13.829  18.748  1.00  0.00           H  
ATOM   3546  HA3 GLY A 670      19.470 -14.053  21.001  1.00  0.00           H  
ATOM   3547  HA2 GLY A 670      20.418 -12.576  21.023  1.00  0.00           H  
ATOM   3548  N   ARG A 671      21.769 -15.535  20.150  1.00 29.09           N  
ANISOU 3548  N   ARG A 671     4256   3385   3409    241   -674    729
ATOM   3549  CA  ARG A 671      22.927 -16.422  20.330  1.00 34.46           C  
ANISOU 3549  CA  ARG A 671     5521   3457   4114    353  -1128   1907
ATOM   3550  C   ARG A 671      24.188 -16.003  19.542  1.00 34.26           C  
ANISOU 3550  C   ARG A 671     3879   4799   4339    630  -2117   1079
ATOM   3551  O   ARG A 671      25.239 -16.604  19.763  1.00 39.32           O  
ANISOU 3551  O   ARG A 671     4852   4455   5630   1406  -2105   1410
ATOM   3552  CB  ARG A 671      22.494 -17.883  20.077  1.00 40.21           C  
ANISOU 3552  CB  ARG A 671     6452   3493   5330    543  -2949    535
ATOM   3553  CG  ARG A 671      22.430 -18.326  18.606  1.00 57.14           C  
ANISOU 3553  CG  ARG A 671     7332   8067   6309  -1573  -2503     55
ATOM   3554  CD  ARG A 671      21.659 -19.648  18.447  1.00 78.68           C  
ANISOU 3554  CD  ARG A 671    10861   7870  11162  -1966  -1683   -547
ATOM   3555  NE  ARG A 671      21.599 -20.096  17.047  1.00 79.18           N  
ANISOU 3555  NE  ARG A 671    13869   5246  10969  -4287   1208  -1309
ATOM   3556  CZ  ARG A 671      20.929 -21.154  16.552  1.00 86.48           C  
ANISOU 3556  CZ  ARG A 671    13393   8167  11296  -5712   2037  -1403
ATOM   3557  NH1 ARG A 671      20.175 -21.949  17.325  1.00100.99           N  
ANISOU 3557  NH1 ARG A 671     9579  13565  15228  -4931   4772    302
ATOM   3558  NH2 ARG A 671      21.014 -21.421  15.243  1.00 89.45           N1+
ANISOU 3558  NH2 ARG A 671    17887   6956   9144  -1726   5191   2674
ATOM   3559  H   ARG A 671      21.053 -15.850  19.509  1.00  0.00           H  
ATOM   3560  HA  ARG A 671      23.201 -16.376  21.386  1.00  0.00           H  
ATOM   3561  HB3 ARG A 671      21.528 -18.054  20.557  1.00  0.00           H  
ATOM   3562  HB2 ARG A 671      23.191 -18.547  20.590  1.00  0.00           H  
ATOM   3563  HG3 ARG A 671      23.433 -18.420  18.188  1.00  0.00           H  
ATOM   3564  HG2 ARG A 671      21.935 -17.542  18.039  1.00  0.00           H  
ATOM   3565  HD3 ARG A 671      20.637 -19.496  18.793  1.00  0.00           H  
ATOM   3566  HD2 ARG A 671      22.098 -20.428  19.071  1.00  0.00           H  
ATOM   3567  HE  ARG A 671      22.111 -19.515  16.392  1.00  0.00           H  
ATOM   3568 HH12 ARG A 671      19.687 -22.742  16.937  1.00  0.00           H  
ATOM   3569 HH11 ARG A 671      20.028 -21.713  18.300  1.00  0.00           H  
ATOM   3570 HH22 ARG A 671      20.516 -22.206  14.848  1.00  0.00           H  
ATOM   3571 HH21 ARG A 671      21.573 -20.835  14.640  1.00  0.00           H  
ATOM   3572  N   GLY A 672      24.087 -14.984  18.670  1.00 35.19           N  
ANISOU 3572  N   GLY A 672     4044   4635   4689   -375  -1683   1266
ATOM   3573  CA  GLY A 672      25.226 -14.416  17.947  1.00 31.28           C  
ANISOU 3573  CA  GLY A 672     4708   2750   4427    141   -738   -465
ATOM   3574  C   GLY A 672      25.536 -15.131  16.621  1.00 33.13           C  
ANISOU 3574  C   GLY A 672     4048   3745   4793   1103     76   -350
ATOM   3575  O   GLY A 672      26.577 -14.846  16.032  1.00 39.95           O  
ANISOU 3575  O   GLY A 672     4915   3743   6521    563    926  -1016
ATOM   3576  H   GLY A 672      23.189 -14.538  18.538  1.00  0.00           H  
ATOM   3577  HA3 GLY A 672      26.120 -14.419  18.574  1.00  0.00           H  
ATOM   3578  HA2 GLY A 672      25.009 -13.372  17.736  1.00  0.00           H  
ATOM   3579  N   SER A 673      24.667 -16.041  16.146  1.00 31.11           N  
ANISOU 3579  N   SER A 673     4789   2724   4304   1051    223   -324
ATOM   3580  CA  SER A 673      24.823 -16.772  14.882  1.00 32.49           C  
ANISOU 3580  CA  SER A 673     5380   2844   4119    961   -187   -120
ATOM   3581  C   SER A 673      24.238 -16.038  13.654  1.00 32.18           C  
ANISOU 3581  C   SER A 673     5005   3485   3735   1147    -87   -580
ATOM   3582  O   SER A 673      24.454 -16.506  12.537  1.00 35.47           O  
ANISOU 3582  O   SER A 673     6068   3471   3935   2225   -203   -666
ATOM   3583  CB  SER A 673      24.232 -18.186  15.051  1.00 32.93           C  
ANISOU 3583  CB  SER A 673     5171   3494   3847     84   -612   -236
ATOM   3584  OG  SER A 673      22.820 -18.180  15.039  1.00 43.24           O  
ANISOU 3584  OG  SER A 673     6131   3840   6455    406    784    675
ATOM   3585  H   SER A 673      23.812 -16.220  16.655  1.00  0.00           H  
ATOM   3586  HA  SER A 673      25.890 -16.900  14.690  1.00  0.00           H  
ATOM   3587  HB3 SER A 673      24.586 -18.647  15.973  1.00  0.00           H  
ATOM   3588  HB2 SER A 673      24.569 -18.828  14.236  1.00  0.00           H  
ATOM   3589  HG  SER A 673      22.527 -17.930  14.157  1.00  0.00           H  
ATOM   3590  N   LEU A 674      23.517 -14.927  13.875  1.00 27.75           N  
ANISOU 3590  N   LEU A 674     4202   2955   3383   1146   -317   1024
ATOM   3591  CA  LEU A 674      22.939 -14.080  12.834  1.00 22.17           C  
ANISOU 3591  CA  LEU A 674     3160   2090   3172    743   -217    444
ATOM   3592  C   LEU A 674      23.256 -12.617  13.142  1.00 23.67           C  
ANISOU 3592  C   LEU A 674     3235   2335   3423    116    161    254
ATOM   3593  O   LEU A 674      23.160 -12.193  14.292  1.00 26.07           O  
ANISOU 3593  O   LEU A 674     3822   3333   2751    586    -77    538
ATOM   3594  CB  LEU A 674      21.421 -14.336  12.754  1.00 24.84           C  
ANISOU 3594  CB  LEU A 674     3508   1822   4106    -97   -391  -1098
ATOM   3595  CG  LEU A 674      20.613 -13.476  11.757  1.00 24.84           C  
ANISOU 3595  CG  LEU A 674     2946   2528   3962    428    471   -325
ATOM   3596  CD1 LEU A 674      21.066 -13.681  10.296  1.00 26.86           C  
ANISOU 3596  CD1 LEU A 674     4495   2186   3525   -135    311   -267
ATOM   3597  CD2 LEU A 674      19.096 -13.685  11.943  1.00 25.46           C  
ANISOU 3597  CD2 LEU A 674     3077   2701   3894   -755    122   -836
ATOM   3598  H   LEU A 674      23.365 -14.617  14.825  1.00  0.00           H  
ATOM   3599  HA  LEU A 674      23.385 -14.328  11.870  1.00  0.00           H  
ATOM   3600  HB3 LEU A 674      20.999 -14.193  13.747  1.00  0.00           H  
ATOM   3601  HB2 LEU A 674      21.283 -15.381  12.499  1.00  0.00           H  
ATOM   3602  HG  LEU A 674      20.790 -12.434  12.014  1.00  0.00           H  
ATOM   3603 HD11 LEU A 674      20.226 -13.789   9.613  1.00  0.00           H  
ATOM   3604 HD12 LEU A 674      21.644 -12.824   9.950  1.00  0.00           H  
ATOM   3605 HD13 LEU A 674      21.693 -14.565  10.181  1.00  0.00           H  
ATOM   3606 HD21 LEU A 674      18.565 -12.733  11.947  1.00  0.00           H  
ATOM   3607 HD22 LEU A 674      18.661 -14.299  11.159  1.00  0.00           H  
ATOM   3608 HD23 LEU A 674      18.865 -14.176  12.886  1.00  0.00           H  
ATOM   3609  N   SER A 675      23.589 -11.875  12.081  1.00 22.97           N  
ANISOU 3609  N   SER A 675     2811   2800   3114      9    -11    353
ATOM   3610  CA  SER A 675      23.863 -10.443  12.093  1.00 20.81           C  
ANISOU 3610  CA  SER A 675     2557   2602   2745    338   -222     48
ATOM   3611  C   SER A 675      23.558  -9.853  10.703  1.00 20.30           C  
ANISOU 3611  C   SER A 675     2880   2432   2400     31    479   -321
ATOM   3612  O   SER A 675      23.499 -10.624   9.741  1.00 20.03           O  
ANISOU 3612  O   SER A 675     2692   2633   2284    738     37   -442
ATOM   3613  CB  SER A 675      25.313 -10.211  12.553  1.00 23.20           C  
ANISOU 3613  CB  SER A 675     2595   3663   2554    -69    174    510
ATOM   3614  OG  SER A 675      26.256 -10.748  11.646  1.00 28.89           O  
ANISOU 3614  OG  SER A 675     2421   4586   3967    649    230    448
ATOM   3615  H   SER A 675      23.644 -12.313  11.170  1.00  0.00           H  
ATOM   3616  HA  SER A 675      23.176 -10.005  12.816  1.00  0.00           H  
ATOM   3617  HB3 SER A 675      25.476 -10.635  13.541  1.00  0.00           H  
ATOM   3618  HB2 SER A 675      25.505  -9.143  12.632  1.00  0.00           H  
ATOM   3619  HG  SER A 675      26.050 -11.677  11.506  1.00  0.00           H  
ATOM   3620  N   PRO A 676      23.320  -8.521  10.606  1.00 18.44           N  
ANISOU 3620  N   PRO A 676     2378   2479   2147    375    651   -582
ATOM   3621  CA  PRO A 676      22.933  -7.876   9.333  1.00 16.86           C  
ANISOU 3621  CA  PRO A 676     2529   2253   1623     47    653   -812
ATOM   3622  C   PRO A 676      23.978  -8.073   8.223  1.00 17.65           C  
ANISOU 3622  C   PRO A 676     1995   2849   1861    191    479   -848
ATOM   3623  O   PRO A 676      25.163  -7.852   8.471  1.00 21.65           O  
ANISOU 3623  O   PRO A 676     2026   3299   2900   1091    204   -511
ATOM   3624  CB  PRO A 676      22.752  -6.393   9.704  1.00 20.85           C  
ANISOU 3624  CB  PRO A 676     2911   2244   2764    249    627   -573
ATOM   3625  CG  PRO A 676      22.480  -6.400  11.195  1.00 19.98           C  
ANISOU 3625  CG  PRO A 676     2002   2870   2717    -25    325   -590
ATOM   3626  CD  PRO A 676      23.358  -7.537  11.692  1.00 19.36           C  
ANISOU 3626  CD  PRO A 676     2368   2719   2267   -238    351   -604
ATOM   3627  HA  PRO A 676      21.970  -8.292   9.032  1.00  0.00           H  
ATOM   3628  HB3 PRO A 676      21.943  -5.920   9.148  1.00  0.00           H  
ATOM   3629  HB2 PRO A 676      23.661  -5.821   9.511  1.00  0.00           H  
ATOM   3630  HG3 PRO A 676      21.431  -6.642  11.372  1.00  0.00           H  
ATOM   3631  HG2 PRO A 676      22.692  -5.448  11.679  1.00  0.00           H  
ATOM   3632  HD2 PRO A 676      24.385  -7.194  11.817  1.00  0.00           H  
ATOM   3633  HD3 PRO A 676      23.000  -7.891  12.656  1.00  0.00           H  
ATOM   3634  N   ASP A 677      23.523  -8.540   7.049  1.00 21.27           N  
ANISOU 3634  N   ASP A 677     3472   3040   1567     -9    232   -562
ATOM   3635  CA  ASP A 677      24.377  -8.843   5.901  1.00 19.38           C  
ANISOU 3635  CA  ASP A 677     2842   2665   1857    -30    307   -389
ATOM   3636  C   ASP A 677      24.863  -7.537   5.247  1.00 19.47           C  
ANISOU 3636  C   ASP A 677     2478   2615   2304    -37    235   -554
ATOM   3637  O   ASP A 677      24.138  -6.960   4.436  1.00 18.84           O  
ANISOU 3637  O   ASP A 677     2309   2560   2289   -307   -185   -193
ATOM   3638  CB  ASP A 677      23.660  -9.774   4.890  1.00 20.99           C  
ANISOU 3638  CB  ASP A 677     3720   2243   2010    -30    162   -651
ATOM   3639  CG  ASP A 677      24.508 -10.277   3.707  1.00 21.62           C  
ANISOU 3639  CG  ASP A 677     3036   3117   2061   -615    158   -602
ATOM   3640  OD1 ASP A 677      25.757 -10.224   3.778  1.00 20.44           O  
ANISOU 3640  OD1 ASP A 677     2515   2646   2603    305    555   -680
ATOM   3641  OD2 ASP A 677      23.886 -10.815   2.767  1.00 26.77           O1-
ANISOU 3641  OD2 ASP A 677     3684   3928   2558  -1080    320  -1286
ATOM   3642  H   ASP A 677      22.532  -8.708   6.931  1.00  0.00           H  
ATOM   3643  HA  ASP A 677      25.247  -9.382   6.284  1.00  0.00           H  
ATOM   3644  HB3 ASP A 677      22.765  -9.279   4.506  1.00  0.00           H  
ATOM   3645  HB2 ASP A 677      23.282 -10.647   5.420  1.00  0.00           H  
ATOM   3646  N   LEU A 678      26.077  -7.100   5.624  1.00 19.00           N  
ANISOU 3646  N   LEU A 678     2230   3004   1983    117    -43   -131
ATOM   3647  CA  LEU A 678      26.682  -5.846   5.175  1.00 20.49           C  
ANISOU 3647  CA  LEU A 678     1846   3035   2902   -139    365   -570
ATOM   3648  C   LEU A 678      27.100  -5.843   3.693  1.00 19.73           C  
ANISOU 3648  C   LEU A 678     2043   2386   3067     61    265   -598
ATOM   3649  O   LEU A 678      27.371  -4.764   3.173  1.00 20.13           O  
ANISOU 3649  O   LEU A 678     2296   2857   2495   -587    187   -307
ATOM   3650  CB  LEU A 678      27.871  -5.451   6.085  1.00 24.84           C  
ANISOU 3650  CB  LEU A 678     3038   3469   2931   -377   -565   -125
ATOM   3651  CG  LEU A 678      27.563  -5.350   7.599  1.00 27.25           C  
ANISOU 3651  CG  LEU A 678     2973   4291   3089    282   -701    220
ATOM   3652  CD1 LEU A 678      28.794  -4.838   8.375  1.00 32.96           C  
ANISOU 3652  CD1 LEU A 678     3888   5042   3593   -526  -1254    534
ATOM   3653  CD2 LEU A 678      26.309  -4.512   7.914  1.00 27.08           C  
ANISOU 3653  CD2 LEU A 678     3608   4009   2671    593   -597   -661
ATOM   3654  H   LEU A 678      26.619  -7.646   6.282  1.00  0.00           H  
ATOM   3655  HA  LEU A 678      25.915  -5.075   5.257  1.00  0.00           H  
ATOM   3656  HB3 LEU A 678      28.251  -4.483   5.754  1.00  0.00           H  
ATOM   3657  HB2 LEU A 678      28.689  -6.159   5.939  1.00  0.00           H  
ATOM   3658  HG  LEU A 678      27.370  -6.361   7.958  1.00  0.00           H  
ATOM   3659 HD11 LEU A 678      29.012  -5.483   9.226  1.00  0.00           H  
ATOM   3660 HD12 LEU A 678      29.689  -4.814   7.753  1.00  0.00           H  
ATOM   3661 HD13 LEU A 678      28.651  -3.827   8.759  1.00  0.00           H  
ATOM   3662 HD21 LEU A 678      26.417  -3.924   8.825  1.00  0.00           H  
ATOM   3663 HD22 LEU A 678      26.075  -3.816   7.110  1.00  0.00           H  
ATOM   3664 HD23 LEU A 678      25.441  -5.154   8.053  1.00  0.00           H  
ATOM   3665  N   SER A 679      27.093  -7.005   3.010  1.00 20.55           N  
ANISOU 3665  N   SER A 679     2250   2551   3004      6    288   -862
ATOM   3666  CA  SER A 679      27.264  -7.087   1.553  1.00 21.08           C  
ANISOU 3666  CA  SER A 679     2432   3026   2551    412   -312  -1168
ATOM   3667  C   SER A 679      26.106  -6.443   0.756  1.00 19.09           C  
ANISOU 3667  C   SER A 679     2619   2670   1964    336    241   -757
ATOM   3668  O   SER A 679      26.300  -6.140  -0.421  1.00 22.06           O  
ANISOU 3668  O   SER A 679     2897   3470   2016    -64    388   -375
ATOM   3669  CB  SER A 679      27.535  -8.549   1.129  1.00 24.02           C  
ANISOU 3669  CB  SER A 679     2063   3363   3698    484   -229  -1598
ATOM   3670  OG  SER A 679      26.362  -9.332   1.028  1.00 25.03           O  
ANISOU 3670  OG  SER A 679     2636   3545   3328   -206     80   -808
ATOM   3671  H   SER A 679      26.854  -7.865   3.486  1.00  0.00           H  
ATOM   3672  HA  SER A 679      28.165  -6.519   1.314  1.00  0.00           H  
ATOM   3673  HB3 SER A 679      28.230  -9.031   1.817  1.00  0.00           H  
ATOM   3674  HB2 SER A 679      28.015  -8.559   0.150  1.00  0.00           H  
ATOM   3675  HG  SER A 679      26.113  -9.629   1.913  1.00  0.00           H  
ATOM   3676  N   LYS A 680      24.948  -6.230   1.408  1.00 20.30           N  
ANISOU 3676  N   LYS A 680     2511   3225   1974   -175    314   -524
ATOM   3677  CA  LYS A 680      23.760  -5.611   0.822  1.00 19.52           C  
ANISOU 3677  CA  LYS A 680     2263   2955   2198   -660     77   -138
ATOM   3678  C   LYS A 680      23.781  -4.076   0.816  1.00 18.76           C  
ANISOU 3678  C   LYS A 680     2634   2817   1675   -192     14   -265
ATOM   3679  O   LYS A 680      22.856  -3.495   0.247  1.00 20.27           O  
ANISOU 3679  O   LYS A 680     2537   2997   2168    -85    135    213
ATOM   3680  CB  LYS A 680      22.497  -6.144   1.526  1.00 20.43           C  
ANISOU 3680  CB  LYS A 680     1866   3505   2391    393    216    137
ATOM   3681  CG  LYS A 680      22.355  -7.663   1.362  1.00 31.20           C  
ANISOU 3681  CG  LYS A 680     3580   3374   4902    275   -233    418
ATOM   3682  CD  LYS A 680      20.911  -8.160   1.522  1.00 46.00           C  
ANISOU 3682  CD  LYS A 680     5145   4664   7666   -584  -2300    204
ATOM   3683  CE  LYS A 680      20.746  -9.669   1.275  1.00 53.97           C  
ANISOU 3683  CE  LYS A 680     7569   5772   7162    153  -1872  -1665
ATOM   3684  NZ  LYS A 680      21.098 -10.072  -0.100  1.00 43.91           N1+
ANISOU 3684  NZ  LYS A 680     6733   3305   6646  -2065  -1097     25
ATOM   3685  H   LYS A 680      24.867  -6.510   2.376  1.00  0.00           H  
ATOM   3686  HA  LYS A 680      23.702  -5.908  -0.227  1.00  0.00           H  
ATOM   3687  HB3 LYS A 680      21.620  -5.663   1.088  1.00  0.00           H  
ATOM   3688  HB2 LYS A 680      22.490  -5.873   2.582  1.00  0.00           H  
ATOM   3689  HG3 LYS A 680      22.996  -8.164   2.087  1.00  0.00           H  
ATOM   3690  HG2 LYS A 680      22.734  -7.945   0.380  1.00  0.00           H  
ATOM   3691  HD3 LYS A 680      20.255  -7.608   0.849  1.00  0.00           H  
ATOM   3692  HD2 LYS A 680      20.567  -7.928   2.531  1.00  0.00           H  
ATOM   3693  HE3 LYS A 680      19.713  -9.963   1.455  1.00  0.00           H  
ATOM   3694  HE2 LYS A 680      21.360 -10.228   1.976  1.00  0.00           H  
ATOM   3695  HZ1 LYS A 680      22.070  -9.853  -0.278  1.00  0.00           H  
ATOM   3696  HZ2 LYS A 680      20.961 -11.068  -0.203  1.00  0.00           H  
ATOM   3697  HZ3 LYS A 680      20.515  -9.581  -0.761  1.00  0.00           H  
ATOM   3698  N   VAL A 681      24.805  -3.430   1.415  1.00 20.01           N  
ANISOU 3698  N   VAL A 681     1887   3062   2650     87    505  -1001
ATOM   3699  CA  VAL A 681      24.968  -1.975   1.322  1.00 26.10           C  
ANISOU 3699  CA  VAL A 681     3529   3119   3268    299    892   -531
ATOM   3700  C   VAL A 681      25.296  -1.594  -0.131  1.00 27.99           C  
ANISOU 3700  C   VAL A 681     4284   3321   3028    599   1255   -985
ATOM   3701  O   VAL A 681      26.075  -2.295  -0.782  1.00 31.14           O  
ANISOU 3701  O   VAL A 681     6004   3621   2205    650   2153   -736
ATOM   3702  CB  VAL A 681      26.053  -1.391   2.278  1.00 29.07           C  
ANISOU 3702  CB  VAL A 681     4044   4095   2904    944    189   -821
ATOM   3703  CG1 VAL A 681      25.790  -1.751   3.751  1.00 26.73           C  
ANISOU 3703  CG1 VAL A 681     3624   3163   3367     99    532   -489
ATOM   3704  CG2 VAL A 681      27.521  -1.648   1.890  1.00 36.18           C  
ANISOU 3704  CG2 VAL A 681     4075   5871   3800     27    -31   -166
ATOM   3705  H   VAL A 681      25.545  -3.948   1.868  1.00  0.00           H  
ATOM   3706  HA  VAL A 681      24.020  -1.507   1.583  1.00  0.00           H  
ATOM   3707  HB  VAL A 681      25.939  -0.306   2.238  1.00  0.00           H  
ATOM   3708 HG11 VAL A 681      26.566  -1.348   4.401  1.00  0.00           H  
ATOM   3709 HG12 VAL A 681      24.840  -1.338   4.087  1.00  0.00           H  
ATOM   3710 HG13 VAL A 681      25.756  -2.827   3.912  1.00  0.00           H  
ATOM   3711 HG21 VAL A 681      28.192  -1.316   2.681  1.00  0.00           H  
ATOM   3712 HG22 VAL A 681      27.711  -2.703   1.703  1.00  0.00           H  
ATOM   3713 HG23 VAL A 681      27.799  -1.093   0.994  1.00  0.00           H  
ATOM   3714  N   ARG A 682      24.658  -0.514  -0.610  1.00 24.51           N  
ANISOU 3714  N   ARG A 682     3709   3234   2368   -369   1105   -208
ATOM   3715  CA  ARG A 682      24.802   0.014  -1.967  1.00 32.03           C  
ANISOU 3715  CA  ARG A 682     5057   4397   2714   -704   1208    357
ATOM   3716  C   ARG A 682      26.272   0.302  -2.307  1.00 28.35           C  
ANISOU 3716  C   ARG A 682     5424   3277   2069  -1027   1309    -30
ATOM   3717  O   ARG A 682      27.039   0.677  -1.422  1.00 26.60           O  
ANISOU 3717  O   ARG A 682     3787   3445   2873   -277   1575   -517
ATOM   3718  CB  ARG A 682      23.951   1.293  -2.112  1.00  0.00           C  
ATOM   3719  CG  ARG A 682      22.432   1.107  -1.898  1.00  0.00           C  
ATOM   3720  CD  ARG A 682      21.689   0.285  -2.965  1.00  0.00           C  
ATOM   3721  NE  ARG A 682      21.603   0.999  -4.252  1.00  0.00           N  
ATOM   3722  CZ  ARG A 682      21.099   0.537  -5.411  1.00  0.00           C  
ATOM   3723  NH1 ARG A 682      20.585  -0.697  -5.525  1.00  0.00           N  
ATOM   3724  NH2 ARG A 682      21.112   1.338  -6.484  1.00  0.00           N1+
ATOM   3725  H   ARG A 682      24.040   0.004   0.002  1.00  0.00           H  
ATOM   3726  HA  ARG A 682      24.444  -0.749  -2.659  1.00  0.00           H  
ATOM   3727  HB2 ARG A 682      24.311   2.044  -1.407  1.00  0.00           H  
ATOM   3728  HB3 ARG A 682      24.114   1.722  -3.101  1.00  0.00           H  
ATOM   3729  HG2 ARG A 682      22.181   0.734  -0.907  1.00  0.00           H  
ATOM   3730  HG3 ARG A 682      22.029   2.118  -1.930  1.00  0.00           H  
ATOM   3731  HD2 ARG A 682      22.264  -0.614  -3.179  1.00  0.00           H  
ATOM   3732  HD3 ARG A 682      20.718  -0.055  -2.602  1.00  0.00           H  
ATOM   3733  HE  ARG A 682      21.958   1.944  -4.236  1.00  0.00           H  
ATOM   3734 HH12 ARG A 682      20.208  -1.023  -6.403  1.00  0.00           H  
ATOM   3735 HH11 ARG A 682      20.560  -1.306  -4.720  1.00  0.00           H  
ATOM   3736 HH22 ARG A 682      20.739   1.019  -7.366  1.00  0.00           H  
ATOM   3737 HH21 ARG A 682      21.492   2.272  -6.420  1.00  0.00           H  
ATOM   3738  N   SER A 683      26.643   0.101  -3.580  1.00 33.87           N  
ANISOU 3738  N   SER A 683     5954   4854   2060  -1035   1239   -658
ATOM   3739  CA  SER A 683      28.017   0.236  -4.077  1.00 38.91           C  
ANISOU 3739  CA  SER A 683     5722   5289   3771   -782   1264  -1262
ATOM   3740  C   SER A 683      28.651   1.630  -3.873  1.00 32.76           C  
ANISOU 3740  C   SER A 683     4742   5251   2455   -717   1336  -1301
ATOM   3741  O   SER A 683      29.874   1.714  -3.771  1.00 38.63           O  
ANISOU 3741  O   SER A 683     4688   5707   4281   -500   2623   -848
ATOM   3742  CB  SER A 683      28.053  -0.220  -5.549  1.00 41.40           C  
ANISOU 3742  CB  SER A 683     5726   7053   2950  -1096    948   -195
ATOM   3743  OG  SER A 683      27.329   0.659  -6.389  1.00 42.86           O  
ANISOU 3743  OG  SER A 683     7407   6799   2078  -1110    343    287
ATOM   3744  H   SER A 683      25.958  -0.196  -4.261  1.00  0.00           H  
ATOM   3745  HA  SER A 683      28.623  -0.468  -3.504  1.00  0.00           H  
ATOM   3746  HB3 SER A 683      27.647  -1.227  -5.649  1.00  0.00           H  
ATOM   3747  HB2 SER A 683      29.084  -0.263  -5.902  1.00  0.00           H  
ATOM   3748  HG  SER A 683      27.435   0.370  -7.299  1.00  0.00           H  
ATOM   3749  N   ASN A 684      27.808   2.672  -3.772  1.00 30.53           N  
ANISOU 3749  N   ASN A 684     5796   3772   2031   -787   1343    -98
ATOM   3750  CA  ASN A 684      28.195   4.057  -3.502  1.00 27.23           C  
ANISOU 3750  CA  ASN A 684     4611   4257   1478  -1284    -91   -481
ATOM   3751  C   ASN A 684      28.230   4.421  -2.000  1.00 23.97           C  
ANISOU 3751  C   ASN A 684     3993   3483   1631   -440    456   -391
ATOM   3752  O   ASN A 684      28.572   5.564  -1.699  1.00 27.36           O  
ANISOU 3752  O   ASN A 684     3549   3576   3267  -1269    405    407
ATOM   3753  CB  ASN A 684      27.302   5.020  -4.325  1.00 32.27           C  
ANISOU 3753  CB  ASN A 684     4703   4662   2895   -731   -510   -584
ATOM   3754  CG  ASN A 684      25.834   5.133  -3.884  1.00 33.01           C  
ANISOU 3754  CG  ASN A 684     5059   4758   2723    507   -827   -581
ATOM   3755  OD1 ASN A 684      25.262   4.207  -3.312  1.00 39.61           O  
ANISOU 3755  OD1 ASN A 684     3971   5800   5278    -79   -829   -321
ATOM   3756  ND2 ASN A 684      25.211   6.277  -4.171  1.00 40.30           N  
ANISOU 3756  ND2 ASN A 684     5632   5556   4125    936  -1147    -40
ATOM   3757  H   ASN A 684      26.815   2.508  -3.861  1.00  0.00           H  
ATOM   3758  HA  ASN A 684      29.220   4.217  -3.842  1.00  0.00           H  
ATOM   3759  HB3 ASN A 684      27.317   4.724  -5.375  1.00  0.00           H  
ATOM   3760  HB2 ASN A 684      27.741   6.019  -4.292  1.00  0.00           H  
ATOM   3761 HD22 ASN A 684      24.242   6.402  -3.915  1.00  0.00           H  
ATOM   3762 HD21 ASN A 684      25.700   7.021  -4.647  1.00  0.00           H  
ATOM   3763  N   CYS A 685      27.904   3.475  -1.094  1.00 22.97           N  
ANISOU 3763  N   CYS A 685     3014   4166   1547   -175    183    -82
ATOM   3764  CA  CYS A 685      28.093   3.597   0.358  1.00 22.24           C  
ANISOU 3764  CA  CYS A 685     2908   3807   1734    199    158   -657
ATOM   3765  C   CYS A 685      29.602   3.750   0.644  1.00 26.47           C  
ANISOU 3765  C   CYS A 685     2777   4262   3019    208    497   -649
ATOM   3766  O   CYS A 685      30.342   2.813   0.332  1.00 24.43           O  
ANISOU 3766  O   CYS A 685     2235   4469   2578    -42    613   -236
ATOM   3767  CB  CYS A 685      27.534   2.364   1.112  1.00 24.80           C  
ANISOU 3767  CB  CYS A 685     2454   4787   2180    -15    214    195
ATOM   3768  SG  CYS A 685      27.830   2.440   2.910  1.00 29.77           S  
ANISOU 3768  SG  CYS A 685     3015   6128   2165   -264    404    -18
ATOM   3769  H   CYS A 685      27.621   2.559  -1.419  1.00  0.00           H  
ATOM   3770  HA  CYS A 685      27.511   4.452   0.694  1.00  0.00           H  
ATOM   3771  HB3 CYS A 685      28.004   1.448   0.755  1.00  0.00           H  
ATOM   3772  HB2 CYS A 685      26.462   2.264   0.939  1.00  0.00           H  
ATOM   3773  HG  CYS A 685      29.162   2.356   2.840  1.00  0.00           H  
ATOM   3774  N   PRO A 686      30.041   4.902   1.208  1.00 24.53           N  
ANISOU 3774  N   PRO A 686     2895   3934   2489    -13   -196    198
ATOM   3775  CA  PRO A 686      31.440   5.080   1.642  1.00 26.84           C  
ANISOU 3775  CA  PRO A 686     2937   4501   2759    -72    290   -108
ATOM   3776  C   PRO A 686      31.900   3.995   2.627  1.00 24.85           C  
ANISOU 3776  C   PRO A 686     2374   4186   2881   -653    164    -60
ATOM   3777  O   PRO A 686      31.129   3.616   3.510  1.00 23.84           O  
ANISOU 3777  O   PRO A 686     2114   4331   2610   -532    167   -431
ATOM   3778  CB  PRO A 686      31.440   6.462   2.309  1.00 29.01           C  
ANISOU 3778  CB  PRO A 686     4381   4341   2298   -566   -564    150
ATOM   3779  CG  PRO A 686      30.261   7.197   1.700  1.00 33.20           C  
ANISOU 3779  CG  PRO A 686     4776   4332   3504     -1   -984   -425
ATOM   3780  CD  PRO A 686      29.241   6.088   1.520  1.00 29.96           C  
ANISOU 3780  CD  PRO A 686     4276   4015   3091    426   -533     98
ATOM   3781  HA  PRO A 686      32.069   5.093   0.750  1.00  0.00           H  
ATOM   3782  HB3 PRO A 686      32.380   6.994   2.164  1.00  0.00           H  
ATOM   3783  HB2 PRO A 686      31.272   6.362   3.382  1.00  0.00           H  
ATOM   3784  HG3 PRO A 686      30.544   7.596   0.725  1.00  0.00           H  
ATOM   3785  HG2 PRO A 686      29.897   8.022   2.310  1.00  0.00           H  
ATOM   3786  HD2 PRO A 686      28.691   5.910   2.446  1.00  0.00           H  
ATOM   3787  HD3 PRO A 686      28.529   6.365   0.744  1.00  0.00           H  
ATOM   3788  N   LYS A 687      33.135   3.503   2.447  1.00 24.33           N  
ANISOU 3788  N   LYS A 687     2478   4370   2397   -635    645    141
ATOM   3789  CA  LYS A 687      33.708   2.450   3.286  1.00 25.60           C  
ANISOU 3789  CA  LYS A 687     1871   5107   2745     58   -118   -694
ATOM   3790  C   LYS A 687      33.891   2.866   4.762  1.00 22.93           C  
ANISOU 3790  C   LYS A 687     1823   4235   2651   -507    327   -655
ATOM   3791  O   LYS A 687      33.842   1.996   5.630  1.00 25.12           O  
ANISOU 3791  O   LYS A 687     2951   4838   1756     13    305   -657
ATOM   3792  CB  LYS A 687      35.005   1.925   2.642  1.00 28.04           C  
ANISOU 3792  CB  LYS A 687     2433   5458   2760    622    542    144
ATOM   3793  CG  LYS A 687      35.489   0.598   3.252  1.00 35.48           C  
ANISOU 3793  CG  LYS A 687     3470   5762   4249   1332    990    314
ATOM   3794  CD  LYS A 687      36.612  -0.062   2.444  1.00 36.79           C  
ANISOU 3794  CD  LYS A 687     4380   5867   3730    868   1745   -563
ATOM   3795  CE  LYS A 687      36.976  -1.448   3.000  1.00 39.75           C  
ANISOU 3795  CE  LYS A 687     4679   5724   4699   1054   1039   -591
ATOM   3796  NZ  LYS A 687      38.032  -2.097   2.205  1.00 37.93           N1+
ANISOU 3796  NZ  LYS A 687     4286   5945   4179    651   1876    859
ATOM   3797  H   LYS A 687      33.712   3.846   1.690  1.00  0.00           H  
ATOM   3798  HA  LYS A 687      32.988   1.630   3.279  1.00  0.00           H  
ATOM   3799  HB3 LYS A 687      35.792   2.680   2.684  1.00  0.00           H  
ATOM   3800  HB2 LYS A 687      34.809   1.750   1.584  1.00  0.00           H  
ATOM   3801  HG3 LYS A 687      34.646  -0.091   3.314  1.00  0.00           H  
ATOM   3802  HG2 LYS A 687      35.833   0.758   4.274  1.00  0.00           H  
ATOM   3803  HD3 LYS A 687      37.489   0.587   2.457  1.00  0.00           H  
ATOM   3804  HD2 LYS A 687      36.307  -0.148   1.400  1.00  0.00           H  
ATOM   3805  HE3 LYS A 687      36.100  -2.097   3.004  1.00  0.00           H  
ATOM   3806  HE2 LYS A 687      37.318  -1.364   4.032  1.00  0.00           H  
ATOM   3807  HZ1 LYS A 687      38.223  -3.011   2.598  1.00  0.00           H  
ATOM   3808  HZ2 LYS A 687      37.726  -2.200   1.249  1.00  0.00           H  
ATOM   3809  HZ3 LYS A 687      38.873  -1.537   2.233  1.00  0.00           H  
ATOM   3810  N   ARG A 688      34.019   4.182   5.022  1.00 24.54           N  
ANISOU 3810  N   ARG A 688     2347   3775   3199   -436    668     66
ATOM   3811  CA  ARG A 688      33.993   4.782   6.357  1.00 23.60           C  
ANISOU 3811  CA  ARG A 688     2332   2973   3662   -565    432   -353
ATOM   3812  C   ARG A 688      32.639   4.595   7.071  1.00 24.26           C  
ANISOU 3812  C   ARG A 688     2784   4022   2411    -65    578    115
ATOM   3813  O   ARG A 688      32.640   4.276   8.259  1.00 21.50           O  
ANISOU 3813  O   ARG A 688     2438   3744   1985   -374    134     29
ATOM   3814  CB  ARG A 688      34.393   6.270   6.263  1.00 25.43           C  
ANISOU 3814  CB  ARG A 688     3022   3120   3520  -1008    530    -95
ATOM   3815  CG  ARG A 688      34.640   6.925   7.637  1.00 37.06           C  
ANISOU 3815  CG  ARG A 688     4690   4774   4618  -1607   -151   -632
ATOM   3816  CD  ARG A 688      35.034   8.414   7.598  1.00 32.36           C  
ANISOU 3816  CD  ARG A 688     3666   4252   4377  -1511     -2   -521
ATOM   3817  NE  ARG A 688      36.356   8.660   6.997  1.00 36.82           N  
ANISOU 3817  NE  ARG A 688     3760   6764   3465  -1768   -761    635
ATOM   3818  CZ  ARG A 688      37.568   8.502   7.562  1.00 45.04           C  
ANISOU 3818  CZ  ARG A 688     3938   8866   4309  -1003   -268   1152
ATOM   3819  NH1 ARG A 688      38.654   8.807   6.842  1.00 58.90           N  
ANISOU 3819  NH1 ARG A 688     6346   9960   6070  -1565   1049   2726
ATOM   3820  NH2 ARG A 688      37.731   8.056   8.816  1.00 49.23           N1+
ANISOU 3820  NH2 ARG A 688     5335  10544   2824  -3303  -1584    155
ATOM   3821  H   ARG A 688      34.075   4.830   4.248  1.00  0.00           H  
ATOM   3822  HA  ARG A 688      34.753   4.266   6.948  1.00  0.00           H  
ATOM   3823  HB3 ARG A 688      33.625   6.826   5.724  1.00  0.00           H  
ATOM   3824  HB2 ARG A 688      35.302   6.354   5.666  1.00  0.00           H  
ATOM   3825  HG3 ARG A 688      35.472   6.364   8.061  1.00  0.00           H  
ATOM   3826  HG2 ARG A 688      33.813   6.788   8.334  1.00  0.00           H  
ATOM   3827  HD3 ARG A 688      34.894   8.910   8.559  1.00  0.00           H  
ATOM   3828  HD2 ARG A 688      34.362   8.915   6.905  1.00  0.00           H  
ATOM   3829  HE  ARG A 688      36.330   8.978   6.039  1.00  0.00           H  
ATOM   3830 HH12 ARG A 688      39.576   8.714   7.244  1.00  0.00           H  
ATOM   3831 HH11 ARG A 688      38.562   9.169   5.904  1.00  0.00           H  
ATOM   3832 HH22 ARG A 688      38.651   7.971   9.221  1.00  0.00           H  
ATOM   3833 HH21 ARG A 688      36.926   7.798   9.377  1.00  0.00           H  
ATOM   3834  N   MET A 689      31.520   4.757   6.338  1.00 24.79           N  
ANISOU 3834  N   MET A 689     2482   3634   3300   -227    289   -221
ATOM   3835  CA  MET A 689      30.168   4.500   6.845  1.00 19.98           C  
ANISOU 3835  CA  MET A 689     2014   3795   1782   -301   -423   -465
ATOM   3836  C   MET A 689      29.896   3.005   7.072  1.00 21.50           C  
ANISOU 3836  C   MET A 689     2159   3746   2263    110    230   -663
ATOM   3837  O   MET A 689      29.265   2.664   8.070  1.00 21.23           O  
ANISOU 3837  O   MET A 689     2738   3252   2074    -76    135   -768
ATOM   3838  CB  MET A 689      29.114   5.132   5.913  1.00 20.67           C  
ANISOU 3838  CB  MET A 689     2084   3383   2384   -503   -685   -440
ATOM   3839  CG  MET A 689      27.647   4.882   6.297  1.00 22.79           C  
ANISOU 3839  CG  MET A 689     2247   3988   2422    172   -249     35
ATOM   3840  SD  MET A 689      27.132   5.476   7.932  1.00 28.31           S  
ANISOU 3840  SD  MET A 689     2603   5480   2674    128    431    -86
ATOM   3841  CE  MET A 689      26.743   7.203   7.541  1.00 36.03           C  
ANISOU 3841  CE  MET A 689     5003   4540   4144    776    846   -742
ATOM   3842  H   MET A 689      31.592   4.993   5.359  1.00  0.00           H  
ATOM   3843  HA  MET A 689      30.085   4.997   7.814  1.00  0.00           H  
ATOM   3844  HB3 MET A 689      29.264   4.793   4.888  1.00  0.00           H  
ATOM   3845  HB2 MET A 689      29.268   6.202   5.895  1.00  0.00           H  
ATOM   3846  HG3 MET A 689      27.422   3.819   6.239  1.00  0.00           H  
ATOM   3847  HG2 MET A 689      27.011   5.366   5.561  1.00  0.00           H  
ATOM   3848  HE1 MET A 689      26.415   7.725   8.439  1.00  0.00           H  
ATOM   3849  HE2 MET A 689      27.621   7.713   7.149  1.00  0.00           H  
ATOM   3850  HE3 MET A 689      25.945   7.259   6.800  1.00  0.00           H  
ATOM   3851  N   LYS A 690      30.386   2.148   6.161  1.00 21.83           N  
ANISOU 3851  N   LYS A 690     2610   4004   1677   -525    676   -535
ATOM   3852  CA  LYS A 690      30.265   0.693   6.259  1.00 19.67           C  
ANISOU 3852  CA  LYS A 690     1468   3964   2041   -721    419   -463
ATOM   3853  C   LYS A 690      31.016   0.121   7.477  1.00 20.65           C  
ANISOU 3853  C   LYS A 690     1804   3813   2229   -279    416   -275
ATOM   3854  O   LYS A 690      30.511  -0.801   8.118  1.00 19.56           O  
ANISOU 3854  O   LYS A 690     2112   3888   1429   -369    222   -749
ATOM   3855  CB  LYS A 690      30.737   0.056   4.937  1.00 24.37           C  
ANISOU 3855  CB  LYS A 690     2877   3434   2946   -567    574  -1126
ATOM   3856  CG  LYS A 690      30.486  -1.459   4.863  1.00 23.65           C  
ANISOU 3856  CG  LYS A 690     2337   3343   3305    -77    361  -1139
ATOM   3857  CD  LYS A 690      30.951  -2.084   3.544  1.00 26.79           C  
ANISOU 3857  CD  LYS A 690     2593   3613   3972    448    496  -1855
ATOM   3858  CE  LYS A 690      30.623  -3.583   3.502  1.00 27.99           C  
ANISOU 3858  CE  LYS A 690     3108   3495   4031     50    109  -1109
ATOM   3859  NZ  LYS A 690      30.933  -4.184   2.195  1.00 28.68           N1+
ANISOU 3859  NZ  LYS A 690     3901   2977   4016    611    914  -1023
ATOM   3860  H   LYS A 690      30.876   2.508   5.353  1.00  0.00           H  
ATOM   3861  HA  LYS A 690      29.207   0.461   6.386  1.00  0.00           H  
ATOM   3862  HB3 LYS A 690      31.797   0.260   4.785  1.00  0.00           H  
ATOM   3863  HB2 LYS A 690      30.213   0.532   4.107  1.00  0.00           H  
ATOM   3864  HG3 LYS A 690      29.420  -1.649   5.001  1.00  0.00           H  
ATOM   3865  HG2 LYS A 690      30.994  -1.970   5.680  1.00  0.00           H  
ATOM   3866  HD3 LYS A 690      32.027  -1.937   3.435  1.00  0.00           H  
ATOM   3867  HD2 LYS A 690      30.487  -1.563   2.705  1.00  0.00           H  
ATOM   3868  HE3 LYS A 690      29.565  -3.728   3.707  1.00  0.00           H  
ATOM   3869  HE2 LYS A 690      31.172  -4.115   4.279  1.00  0.00           H  
ATOM   3870  HZ1 LYS A 690      30.415  -3.703   1.469  1.00  0.00           H  
ATOM   3871  HZ2 LYS A 690      31.921  -4.102   2.006  1.00  0.00           H  
ATOM   3872  HZ3 LYS A 690      30.670  -5.159   2.200  1.00  0.00           H  
ATOM   3873  N   ARG A 691      32.188   0.702   7.786  1.00 18.96           N  
ANISOU 3873  N   ARG A 691     1995   2749   2459    -52    347   -644
ATOM   3874  CA  ARG A 691      32.973   0.381   8.972  1.00 18.25           C  
ANISOU 3874  CA  ARG A 691     2107   2916   1910   -342    529   -466
ATOM   3875  C   ARG A 691      32.303   0.895  10.256  1.00 19.59           C  
ANISOU 3875  C   ARG A 691     2133   2963   2345     11    642   -487
ATOM   3876  O   ARG A 691      32.212   0.125  11.206  1.00 17.07           O  
ANISOU 3876  O   ARG A 691     1638   2611   2237   -301   -402   -487
ATOM   3877  CB  ARG A 691      34.417   0.889   8.788  1.00 21.88           C  
ANISOU 3877  CB  ARG A 691     2318   3509   2483   -501    738   -320
ATOM   3878  CG  ARG A 691      35.393   0.583   9.945  1.00 23.96           C  
ANISOU 3878  CG  ARG A 691     2813   3573   2714    -68    223   -741
ATOM   3879  CD  ARG A 691      35.420  -0.904  10.340  1.00 21.65           C  
ANISOU 3879  CD  ARG A 691     1988   3661   2575   -516    508   -600
ATOM   3880  NE  ARG A 691      36.503  -1.219  11.283  1.00 25.21           N  
ANISOU 3880  NE  ARG A 691     2852   3447   3277    -12   -164  -1085
ATOM   3881  CZ  ARG A 691      37.757  -1.607  10.991  1.00 31.02           C  
ANISOU 3881  CZ  ARG A 691     2546   5018   4220   -528    120  -1051
ATOM   3882  NH1 ARG A 691      38.196  -1.728   9.729  1.00 29.93           N  
ANISOU 3882  NH1 ARG A 691     3472   4502   3394   -415   -661  -1092
ATOM   3883  NH2 ARG A 691      38.597  -1.887  11.994  1.00 28.22           N1+
ANISOU 3883  NH2 ARG A 691     2160   3771   4791    742    158  -1046
ATOM   3884  H   ARG A 691      32.544   1.447   7.202  1.00  0.00           H  
ATOM   3885  HA  ARG A 691      33.013  -0.707   9.043  1.00  0.00           H  
ATOM   3886  HB3 ARG A 691      34.406   1.962   8.602  1.00  0.00           H  
ATOM   3887  HB2 ARG A 691      34.820   0.449   7.877  1.00  0.00           H  
ATOM   3888  HG3 ARG A 691      35.035   1.147  10.807  1.00  0.00           H  
ATOM   3889  HG2 ARG A 691      36.394   0.968   9.745  1.00  0.00           H  
ATOM   3890  HD3 ARG A 691      35.380  -1.570   9.479  1.00  0.00           H  
ATOM   3891  HD2 ARG A 691      34.528  -1.123  10.926  1.00  0.00           H  
ATOM   3892  HE  ARG A 691      36.256  -1.127  12.263  1.00  0.00           H  
ATOM   3893 HH12 ARG A 691      39.142  -2.023   9.539  1.00  0.00           H  
ATOM   3894 HH11 ARG A 691      37.575  -1.532   8.953  1.00  0.00           H  
ATOM   3895 HH22 ARG A 691      39.545  -2.178  11.806  1.00  0.00           H  
ATOM   3896 HH21 ARG A 691      38.286  -1.834  12.957  1.00  0.00           H  
ATOM   3897  N   LEU A 692      31.794   2.140  10.251  1.00 18.79           N  
ANISOU 3897  N   LEU A 692     2418   2640   2080   -264    -23   -514
ATOM   3898  CA  LEU A 692      31.047   2.743  11.363  1.00 19.32           C  
ANISOU 3898  CA  LEU A 692     2306   2774   2260   -382    136   -587
ATOM   3899  C   LEU A 692      29.808   1.925  11.766  1.00 19.59           C  
ANISOU 3899  C   LEU A 692     2238   2805   2398   -435   -405   -317
ATOM   3900  O   LEU A 692      29.569   1.736  12.957  1.00 17.85           O  
ANISOU 3900  O   LEU A 692     1948   2427   2406   -263    144   -437
ATOM   3901  CB  LEU A 692      30.673   4.196  10.991  1.00 20.64           C  
ANISOU 3901  CB  LEU A 692     2716   2862   2265   -117    621   -608
ATOM   3902  CG  LEU A 692      29.812   4.961  12.022  1.00 22.05           C  
ANISOU 3902  CG  LEU A 692     2881   3268   2227      2    889   -381
ATOM   3903  CD1 LEU A 692      30.511   5.090  13.389  1.00 19.12           C  
ANISOU 3903  CD1 LEU A 692     2500   2742   2021    363    884   -255
ATOM   3904  CD2 LEU A 692      29.374   6.322  11.457  1.00 23.04           C  
ANISOU 3904  CD2 LEU A 692     2873   3543   2336   -156   1044   -321
ATOM   3905  H   LEU A 692      31.899   2.717   9.427  1.00  0.00           H  
ATOM   3906  HA  LEU A 692      31.723   2.760  12.220  1.00  0.00           H  
ATOM   3907  HB3 LEU A 692      30.133   4.177  10.045  1.00  0.00           H  
ATOM   3908  HB2 LEU A 692      31.585   4.763  10.801  1.00  0.00           H  
ATOM   3909  HG  LEU A 692      28.886   4.406  12.179  1.00  0.00           H  
ATOM   3910 HD11 LEU A 692      30.540   6.120  13.729  1.00  0.00           H  
ATOM   3911 HD12 LEU A 692      29.989   4.508  14.150  1.00  0.00           H  
ATOM   3912 HD13 LEU A 692      31.544   4.744  13.365  1.00  0.00           H  
ATOM   3913 HD21 LEU A 692      28.334   6.531  11.710  1.00  0.00           H  
ATOM   3914 HD22 LEU A 692      29.984   7.134  11.848  1.00  0.00           H  
ATOM   3915 HD23 LEU A 692      29.455   6.364  10.370  1.00  0.00           H  
ATOM   3916  N   MET A 693      29.074   1.436  10.756  1.00 17.80           N  
ANISOU 3916  N   MET A 693     1702   2948   2111    205   -252   -538
ATOM   3917  CA  MET A 693      27.929   0.543  10.879  1.00 19.49           C  
ANISOU 3917  CA  MET A 693     2278   3080   2047    -81   -286   -342
ATOM   3918  C   MET A 693      28.297  -0.794  11.543  1.00 19.13           C  
ANISOU 3918  C   MET A 693     1719   3069   2479   -121    217   -480
ATOM   3919  O   MET A 693      27.600  -1.196  12.469  1.00 18.83           O  
ANISOU 3919  O   MET A 693     1769   2875   2510   -390     99   -387
ATOM   3920  CB  MET A 693      27.329   0.367   9.474  1.00 19.36           C  
ANISOU 3920  CB  MET A 693     1560   3627   2167   -147   -205   -670
ATOM   3921  CG  MET A 693      26.031  -0.445   9.379  1.00 21.72           C  
ANISOU 3921  CG  MET A 693     2044   3770   2436   -342    -43   -500
ATOM   3922  SD  MET A 693      25.626  -0.984   7.697  1.00 24.77           S  
ANISOU 3922  SD  MET A 693     3519   3248   2643   -429   -715   -210
ATOM   3923  CE  MET A 693      25.874   0.548   6.764  1.00 25.51           C  
ANISOU 3923  CE  MET A 693     4031   4087   1575    225     -5    303
ATOM   3924  H   MET A 693      29.337   1.676   9.809  1.00  0.00           H  
ATOM   3925  HA  MET A 693      27.188   1.036  11.512  1.00  0.00           H  
ATOM   3926  HB3 MET A 693      28.074  -0.070   8.809  1.00  0.00           H  
ATOM   3927  HB2 MET A 693      27.125   1.363   9.080  1.00  0.00           H  
ATOM   3928  HG3 MET A 693      25.199   0.142   9.762  1.00  0.00           H  
ATOM   3929  HG2 MET A 693      26.086  -1.341   9.991  1.00  0.00           H  
ATOM   3930  HE1 MET A 693      25.616   0.385   5.721  1.00  0.00           H  
ATOM   3931  HE2 MET A 693      25.254   1.350   7.160  1.00  0.00           H  
ATOM   3932  HE3 MET A 693      26.915   0.868   6.793  1.00  0.00           H  
ATOM   3933  N   ALA A 694      29.408  -1.419  11.111  1.00 19.98           N  
ANISOU 3933  N   ALA A 694     1807   3065   2721     59    289   -710
ATOM   3934  CA  ALA A 694      29.949  -2.646  11.705  1.00 18.74           C  
ANISOU 3934  CA  ALA A 694     2104   2896   2118     14    218   -451
ATOM   3935  C   ALA A 694      30.385  -2.480  13.173  1.00 17.08           C  
ANISOU 3935  C   ALA A 694     2129   2209   2151     45    376   -749
ATOM   3936  O   ALA A 694      30.143  -3.388  13.967  1.00 20.44           O  
ANISOU 3936  O   ALA A 694     2555   2747   2464   -391    127   -377
ATOM   3937  CB  ALA A 694      31.115  -3.164  10.851  1.00 21.86           C  
ANISOU 3937  CB  ALA A 694     2648   3089   2566    -96    677   -822
ATOM   3938  H   ALA A 694      29.941  -1.017  10.352  1.00  0.00           H  
ATOM   3939  HA  ALA A 694      29.156  -3.396  11.677  1.00  0.00           H  
ATOM   3940  HB1 ALA A 694      31.487  -4.117  11.229  1.00  0.00           H  
ATOM   3941  HB2 ALA A 694      30.803  -3.322   9.820  1.00  0.00           H  
ATOM   3942  HB3 ALA A 694      31.954  -2.467  10.838  1.00  0.00           H  
ATOM   3943  N   GLU A 695      30.974  -1.317  13.507  1.00 17.94           N  
ANISOU 3943  N   GLU A 695     2220   2112   2482     29    166   -562
ATOM   3944  CA  GLU A 695      31.356  -0.930  14.866  1.00 17.22           C  
ANISOU 3944  CA  GLU A 695     1384   2615   2544    -13   -241    -75
ATOM   3945  C   GLU A 695      30.146  -0.726  15.792  1.00 16.66           C  
ANISOU 3945  C   GLU A 695     1946   1988   2392    222    -98   -335
ATOM   3946  O   GLU A 695      30.174  -1.206  16.923  1.00 17.75           O  
ANISOU 3946  O   GLU A 695     2124   1942   2678    182    253   -207
ATOM   3947  CB  GLU A 695      32.261   0.324  14.831  1.00 16.85           C  
ANISOU 3947  CB  GLU A 695     1933   2680   1787   -252      6   -277
ATOM   3948  CG  GLU A 695      33.649   0.098  14.192  1.00 22.38           C  
ANISOU 3948  CG  GLU A 695     1729   3416   3357    628    -52   -602
ATOM   3949  CD  GLU A 695      34.564  -0.888  14.929  1.00 20.22           C  
ANISOU 3949  CD  GLU A 695     1614   3360   2709    207      5   -496
ATOM   3950  OE1 GLU A 695      34.432  -1.032  16.163  1.00 20.07           O  
ANISOU 3950  OE1 GLU A 695     2033   3066   2524    103   -141   -441
ATOM   3951  OE2 GLU A 695      35.402  -1.500  14.234  1.00 21.92           O1-
ANISOU 3951  OE2 GLU A 695     2440   2975   2911    409     61   -779
ATOM   3952  H   GLU A 695      31.153  -0.631  12.785  1.00  0.00           H  
ATOM   3953  HA  GLU A 695      31.928  -1.756  15.285  1.00  0.00           H  
ATOM   3954  HB3 GLU A 695      32.390   0.733  15.832  1.00  0.00           H  
ATOM   3955  HB2 GLU A 695      31.760   1.112  14.271  1.00  0.00           H  
ATOM   3956  HG3 GLU A 695      34.172   1.053  14.127  1.00  0.00           H  
ATOM   3957  HG2 GLU A 695      33.536  -0.253  13.171  1.00  0.00           H  
ATOM   3958  N   CYS A 696      29.091  -0.069  15.284  1.00 16.49           N  
ANISOU 3958  N   CYS A 696     2053   2103   2109    344   -182   -145
ATOM   3959  CA  CYS A 696      27.809   0.108  15.972  1.00 15.04           C  
ANISOU 3959  CA  CYS A 696     1822   2186   1703    141   -394   -145
ATOM   3960  C   CYS A 696      27.103  -1.233  16.253  1.00 17.32           C  
ANISOU 3960  C   CYS A 696     1977   2522   2079   -106   -121   -254
ATOM   3961  O   CYS A 696      26.504  -1.382  17.315  1.00 15.72           O  
ANISOU 3961  O   CYS A 696     1746   1879   2346    -51     14    -92
ATOM   3962  CB  CYS A 696      26.869   1.041  15.186  1.00 14.41           C  
ANISOU 3962  CB  CYS A 696     1883   2431   1161    266     21    -64
ATOM   3963  SG  CYS A 696      27.485   2.746  15.205  1.00 17.88           S  
ANISOU 3963  SG  CYS A 696     2212   2359   2221    246   -204   -332
ATOM   3964  H   CYS A 696      29.151   0.314  14.350  1.00  0.00           H  
ATOM   3965  HA  CYS A 696      28.012   0.568  16.938  1.00  0.00           H  
ATOM   3966  HB3 CYS A 696      25.873   1.043  15.624  1.00  0.00           H  
ATOM   3967  HB2 CYS A 696      26.762   0.715  14.152  1.00  0.00           H  
ATOM   3968  HG  CYS A 696      28.529   2.522  14.400  1.00  0.00           H  
ATOM   3969  N   LEU A 697      27.215  -2.183  15.311  1.00 18.07           N  
ANISOU 3969  N   LEU A 697     2107   2450   2308     95    202   -151
ATOM   3970  CA  LEU A 697      26.558  -3.488  15.339  1.00 16.63           C  
ANISOU 3970  CA  LEU A 697     2004   2342   1972    -45    109    -25
ATOM   3971  C   LEU A 697      27.319  -4.586  16.109  1.00 17.94           C  
ANISOU 3971  C   LEU A 697     1987   2202   2628     37   -152   -458
ATOM   3972  O   LEU A 697      26.814  -5.707  16.120  1.00 20.47           O  
ANISOU 3972  O   LEU A 697     2232   2273   3271   -175    -35   -439
ATOM   3973  CB  LEU A 697      26.282  -3.931  13.881  1.00 16.97           C  
ANISOU 3973  CB  LEU A 697     2100   2064   2283    282   -385    -66
ATOM   3974  CG  LEU A 697      25.179  -3.119  13.170  1.00 14.76           C  
ANISOU 3974  CG  LEU A 697     1643   1962   2002   -226   -389    -98
ATOM   3975  CD1 LEU A 697      25.150  -3.453  11.670  1.00 16.85           C  
ANISOU 3975  CD1 LEU A 697     1628   2514   2259   -232   -304   -353
ATOM   3976  CD2 LEU A 697      23.795  -3.315  13.805  1.00 15.49           C  
ANISOU 3976  CD2 LEU A 697     1580   1963   2341   -307   -286     36
ATOM   3977  H   LEU A 697      27.736  -1.975  14.469  1.00  0.00           H  
ATOM   3978  HA  LEU A 697      25.601  -3.379  15.849  1.00  0.00           H  
ATOM   3979  HB3 LEU A 697      25.993  -4.982  13.839  1.00  0.00           H  
ATOM   3980  HB2 LEU A 697      27.213  -3.866  13.315  1.00  0.00           H  
ATOM   3981  HG  LEU A 697      25.411  -2.059  13.253  1.00  0.00           H  
ATOM   3982 HD11 LEU A 697      24.503  -2.764  11.125  1.00  0.00           H  
ATOM   3983 HD12 LEU A 697      26.146  -3.388  11.232  1.00  0.00           H  
ATOM   3984 HD13 LEU A 697      24.785  -4.464  11.496  1.00  0.00           H  
ATOM   3985 HD21 LEU A 697      23.016  -3.322  13.045  1.00  0.00           H  
ATOM   3986 HD22 LEU A 697      23.727  -4.252  14.355  1.00  0.00           H  
ATOM   3987 HD23 LEU A 697      23.565  -2.506  14.497  1.00  0.00           H  
ATOM   3988  N   LYS A 698      28.476  -4.299  16.742  1.00 17.66           N  
ANISOU 3988  N   LYS A 698     2389   2261   2059    149   -260   -365
ATOM   3989  CA  LYS A 698      29.282  -5.277  17.502  1.00 18.85           C  
ANISOU 3989  CA  LYS A 698     2458   2438   2263    248   -304   -477
ATOM   3990  C   LYS A 698      28.467  -6.063  18.541  1.00 17.62           C  
ANISOU 3990  C   LYS A 698     2473   1973   2248    805   -657    343
ATOM   3991  O   LYS A 698      27.702  -5.452  19.276  1.00 20.89           O  
ANISOU 3991  O   LYS A 698     2558   2426   2953    744   -100    250
ATOM   3992  CB  LYS A 698      30.459  -4.565  18.203  1.00 20.77           C  
ANISOU 3992  CB  LYS A 698     2515   3019   2358     46   -375   -398
ATOM   3993  CG  LYS A 698      31.563  -4.079  17.255  1.00 27.00           C  
ANISOU 3993  CG  LYS A 698     3974   2995   3288    -40    445   -178
ATOM   3994  CD  LYS A 698      32.416  -5.202  16.654  1.00 31.09           C  
ANISOU 3994  CD  LYS A 698     3473   4339   3997     95    841   -733
ATOM   3995  CE  LYS A 698      33.515  -4.647  15.740  1.00 35.50           C  
ANISOU 3995  CE  LYS A 698     4625   5538   3324   -199   1097   -408
ATOM   3996  NZ  LYS A 698      34.353  -5.723  15.188  1.00 42.07           N1+
ANISOU 3996  NZ  LYS A 698     4021   6611   5351    500   -456  -1325
ATOM   3997  H   LYS A 698      28.842  -3.358  16.700  1.00  0.00           H  
ATOM   3998  HA  LYS A 698      29.669  -5.988  16.774  1.00  0.00           H  
ATOM   3999  HB3 LYS A 698      30.919  -5.232  18.934  1.00  0.00           H  
ATOM   4000  HB2 LYS A 698      30.081  -3.719  18.778  1.00  0.00           H  
ATOM   4001  HG3 LYS A 698      32.205  -3.376  17.788  1.00  0.00           H  
ATOM   4002  HG2 LYS A 698      31.109  -3.522  16.441  1.00  0.00           H  
ATOM   4003  HD3 LYS A 698      31.785  -5.883  16.083  1.00  0.00           H  
ATOM   4004  HD2 LYS A 698      32.858  -5.788  17.461  1.00  0.00           H  
ATOM   4005  HE3 LYS A 698      34.156  -3.958  16.290  1.00  0.00           H  
ATOM   4006  HE2 LYS A 698      33.072  -4.085  14.917  1.00  0.00           H  
ATOM   4007  HZ1 LYS A 698      35.049  -5.315  14.578  1.00  0.00           H  
ATOM   4008  HZ2 LYS A 698      34.814  -6.213  15.942  1.00  0.00           H  
ATOM   4009  HZ3 LYS A 698      33.780  -6.364  14.659  1.00  0.00           H  
ATOM   4010  N   LYS A 699      28.615  -7.396  18.569  1.00 21.71           N  
ANISOU 4010  N   LYS A 699     3092   1954   3201    625   -136   -302
ATOM   4011  CA  LYS A 699      27.829  -8.293  19.425  1.00 23.21           C  
ANISOU 4011  CA  LYS A 699     3158   2056   3605   -188   -336   -337
ATOM   4012  C   LYS A 699      28.119  -8.116  20.927  1.00 23.55           C  
ANISOU 4012  C   LYS A 699     3018   2262   3664     68   -302   -613
ATOM   4013  O   LYS A 699      27.177  -8.131  21.721  1.00 25.69           O  
ANISOU 4013  O   LYS A 699     4290   2106   3365    737    484    466
ATOM   4014  CB  LYS A 699      28.025  -9.748  18.959  1.00 32.08           C  
ANISOU 4014  CB  LYS A 699     5038   2310   4840   -124   -346  -1192
ATOM   4015  CG  LYS A 699      27.426 -10.000  17.563  1.00 40.84           C  
ANISOU 4015  CG  LYS A 699     7609   3268   4638   -574   -537   -656
ATOM   4016  CD  LYS A 699      27.921 -11.297  16.911  1.00 45.93           C  
ANISOU 4016  CD  LYS A 699     9336   2841   5271  -1584   -163  -1072
ATOM   4017  CE  LYS A 699      27.443 -11.416  15.455  1.00 53.46           C  
ANISOU 4017  CE  LYS A 699     8513   6242   5556   -309   -884  -2006
ATOM   4018  NZ  LYS A 699      28.070 -12.546  14.751  1.00 59.24           N1+
ANISOU 4018  NZ  LYS A 699     8202   4637   9669    345   -312    583
ATOM   4019  H   LYS A 699      29.275  -7.840  17.944  1.00  0.00           H  
ATOM   4020  HA  LYS A 699      26.781  -8.032  19.272  1.00  0.00           H  
ATOM   4021  HB3 LYS A 699      27.565 -10.441  19.665  1.00  0.00           H  
ATOM   4022  HB2 LYS A 699      29.092  -9.978  18.957  1.00  0.00           H  
ATOM   4023  HG3 LYS A 699      27.667  -9.168  16.903  1.00  0.00           H  
ATOM   4024  HG2 LYS A 699      26.338 -10.015  17.635  1.00  0.00           H  
ATOM   4025  HD3 LYS A 699      27.566 -12.152  17.489  1.00  0.00           H  
ATOM   4026  HD2 LYS A 699      29.011 -11.325  16.951  1.00  0.00           H  
ATOM   4027  HE3 LYS A 699      27.690 -10.510  14.902  1.00  0.00           H  
ATOM   4028  HE2 LYS A 699      26.361 -11.534  15.425  1.00  0.00           H  
ATOM   4029  HZ1 LYS A 699      27.802 -13.411  15.204  1.00  0.00           H  
ATOM   4030  HZ2 LYS A 699      27.756 -12.562  13.791  1.00  0.00           H  
ATOM   4031  HZ3 LYS A 699      29.074 -12.448  14.774  1.00  0.00           H  
ATOM   4032  N   LYS A 700      29.395  -7.870  21.271  1.00 23.05           N  
ANISOU 4032  N   LYS A 700     3030   2187   3538    135   -837    -42
ATOM   4033  CA  LYS A 700      29.817  -7.359  22.573  1.00 26.28           C  
ANISOU 4033  CA  LYS A 700     4173   2334   3475    436   -880   -247
ATOM   4034  C   LYS A 700      29.520  -5.856  22.651  1.00 23.13           C  
ANISOU 4034  C   LYS A 700     3102   2372   3311    337   -381     46
ATOM   4035  O   LYS A 700      30.001  -5.098  21.808  1.00 23.58           O  
ANISOU 4035  O   LYS A 700     2913   2453   3591    335   -123    321
ATOM   4036  CB  LYS A 700      31.316  -7.635  22.784  1.00  0.00           C  
ATOM   4037  CG  LYS A 700      31.626  -9.105  23.104  1.00  0.00           C  
ATOM   4038  CD  LYS A 700      33.126  -9.335  23.331  1.00  0.00           C  
ATOM   4039  CE  LYS A 700      33.452 -10.764  23.787  1.00  0.00           C  
ATOM   4040  NZ  LYS A 700      34.901 -10.946  23.984  1.00  0.00           N1+
ATOM   4041  H   LYS A 700      30.109  -7.882  20.552  1.00  0.00           H  
ATOM   4042  HA  LYS A 700      29.257  -7.876  23.355  1.00  0.00           H  
ATOM   4043  HB2 LYS A 700      31.886  -7.303  21.915  1.00  0.00           H  
ATOM   4044  HB3 LYS A 700      31.674  -7.035  23.622  1.00  0.00           H  
ATOM   4045  HG2 LYS A 700      31.071  -9.405  23.993  1.00  0.00           H  
ATOM   4046  HG3 LYS A 700      31.278  -9.743  22.290  1.00  0.00           H  
ATOM   4047  HD2 LYS A 700      33.651  -9.124  22.398  1.00  0.00           H  
ATOM   4048  HD3 LYS A 700      33.496  -8.614  24.062  1.00  0.00           H  
ATOM   4049  HE2 LYS A 700      32.940 -10.991  24.722  1.00  0.00           H  
ATOM   4050  HE3 LYS A 700      33.106 -11.485  23.046  1.00  0.00           H  
ATOM   4051  HZ1 LYS A 700      35.229 -10.305  24.692  1.00  0.00           H  
ATOM   4052  HZ2 LYS A 700      35.091 -11.895  24.273  1.00  0.00           H  
ATOM   4053  HZ3 LYS A 700      35.382 -10.755  23.116  1.00  0.00           H  
ATOM   4054  N   ARG A 701      28.717  -5.465  23.652  1.00 24.17           N  
ANISOU 4054  N   ARG A 701     3369   3381   2433    146   -187    347
ATOM   4055  CA  ARG A 701      28.211  -4.103  23.806  1.00 23.56           C  
ANISOU 4055  CA  ARG A 701     3063   3413   2474    452   -374   1372
ATOM   4056  C   ARG A 701      29.290  -3.052  24.125  1.00 23.65           C  
ANISOU 4056  C   ARG A 701     2749   3327   2909    798   -827    834
ATOM   4057  O   ARG A 701      29.166  -1.921  23.659  1.00 24.66           O  
ANISOU 4057  O   ARG A 701     3021   3429   2919    251   -551    687
ATOM   4058  CB  ARG A 701      27.030  -4.108  24.795  1.00 23.59           C  
ANISOU 4058  CB  ARG A 701     2739   2329   3895   -901    348   1287
ATOM   4059  CG  ARG A 701      27.369  -4.266  26.286  1.00 29.85           C  
ANISOU 4059  CG  ARG A 701     3237   3737   4365   -372   -222   1177
ATOM   4060  CD  ARG A 701      26.102  -4.137  27.140  1.00 31.47           C  
ANISOU 4060  CD  ARG A 701     2881   4614   4459    196   -525   1810
ATOM   4061  NE  ARG A 701      26.335  -4.458  28.556  1.00 40.71           N  
ANISOU 4061  NE  ARG A 701     5433   5196   4838   2521   -885   1873
ATOM   4062  CZ  ARG A 701      25.409  -4.479  29.532  1.00 53.39           C  
ANISOU 4062  CZ  ARG A 701     7033   8170   5083   1316     33   1243
ATOM   4063  NH1 ARG A 701      25.781  -4.812  30.773  1.00 55.96           N  
ANISOU 4063  NH1 ARG A 701     8696   5409   7156   1026  -4084   1809
ATOM   4064  NH2 ARG A 701      24.124  -4.176  29.303  1.00 37.04           N1+
ANISOU 4064  NH2 ARG A 701     6765   5144   2162   1014    379    706
ATOM   4065  H   ARG A 701      28.363  -6.148  24.307  1.00  0.00           H  
ATOM   4066  HA  ARG A 701      27.801  -3.830  22.836  1.00  0.00           H  
ATOM   4067  HB3 ARG A 701      26.332  -4.892  24.503  1.00  0.00           H  
ATOM   4068  HB2 ARG A 701      26.472  -3.183  24.679  1.00  0.00           H  
ATOM   4069  HG3 ARG A 701      28.017  -3.433  26.552  1.00  0.00           H  
ATOM   4070  HG2 ARG A 701      27.928  -5.177  26.502  1.00  0.00           H  
ATOM   4071  HD3 ARG A 701      25.265  -4.687  26.713  1.00  0.00           H  
ATOM   4072  HD2 ARG A 701      25.816  -3.084  27.147  1.00  0.00           H  
ATOM   4073  HE  ARG A 701      27.295  -4.665  28.809  1.00  0.00           H  
ATOM   4074 HH12 ARG A 701      25.097  -4.838  31.518  1.00  0.00           H  
ATOM   4075 HH11 ARG A 701      26.747  -5.030  30.971  1.00  0.00           H  
ATOM   4076 HH22 ARG A 701      23.447  -4.222  30.057  1.00  0.00           H  
ATOM   4077 HH21 ARG A 701      23.824  -3.884  28.381  1.00  0.00           H  
ATOM   4078  N   ASP A 702      30.339  -3.445  24.866  1.00 24.27           N  
ANISOU 4078  N   ASP A 702     2795   3154   3271    234  -1339    809
ATOM   4079  CA  ASP A 702      31.461  -2.575  25.240  1.00 27.93           C  
ANISOU 4079  CA  ASP A 702     4113   2887   3612   -479  -1025    735
ATOM   4080  C   ASP A 702      32.490  -2.368  24.109  1.00 27.25           C  
ANISOU 4080  C   ASP A 702     3162   3375   3817    -33   -853   -201
ATOM   4081  O   ASP A 702      33.326  -1.475  24.242  1.00 29.27           O  
ANISOU 4081  O   ASP A 702     2906   4283   3933   -292   -631   -310
ATOM   4082  CB  ASP A 702      32.146  -3.010  26.561  1.00 35.91           C  
ANISOU 4082  CB  ASP A 702     4150   4556   4935    404  -2636    812
ATOM   4083  CG  ASP A 702      31.226  -3.097  27.796  1.00 49.49           C  
ANISOU 4083  CG  ASP A 702     8086   6353   4363  -1021  -1411   1144
ATOM   4084  OD1 ASP A 702      30.186  -2.402  27.838  1.00 48.22           O  
ANISOU 4084  OD1 ASP A 702     6040   8870   3410  -2318    494   -810
ATOM   4085  OD2 ASP A 702      31.646  -3.781  28.754  1.00 54.74           O1-
ANISOU 4085  OD2 ASP A 702     8976   7464   4357    955   -968   1113
ATOM   4086  H   ASP A 702      30.383  -4.398  25.206  1.00  0.00           H  
ATOM   4087  HA  ASP A 702      31.049  -1.582  25.426  1.00  0.00           H  
ATOM   4088  HB3 ASP A 702      32.945  -2.310  26.811  1.00  0.00           H  
ATOM   4089  HB2 ASP A 702      32.616  -3.984  26.415  1.00  0.00           H  
ATOM   4090  N   GLU A 703      32.389  -3.133  23.006  1.00 22.96           N  
ANISOU 4090  N   GLU A 703     1725   2940   4056    368   -742   -278
ATOM   4091  CA  GLU A 703      33.158  -2.907  21.776  1.00 26.55           C  
ANISOU 4091  CA  GLU A 703     2390   3358   4337    354   -353    -10
ATOM   4092  C   GLU A 703      32.545  -1.838  20.851  1.00 22.87           C  
ANISOU 4092  C   GLU A 703     2707   2754   3227    217     35   -490
ATOM   4093  O   GLU A 703      33.222  -1.420  19.913  1.00 22.45           O  
ANISOU 4093  O   GLU A 703     1805   2736   3988    134   -180   -475
ATOM   4094  CB  GLU A 703      33.352  -4.232  21.011  1.00 28.03           C  
ANISOU 4094  CB  GLU A 703     2794   3061   4795    886   -405    114
ATOM   4095  CG  GLU A 703      34.231  -5.250  21.769  1.00 34.29           C  
ANISOU 4095  CG  GLU A 703     4398   4784   3844   1773  -1000    242
ATOM   4096  CD  GLU A 703      34.659  -6.486  20.957  1.00 45.79           C  
ANISOU 4096  CD  GLU A 703     5591   4341   7466   2661   -776   -356
ATOM   4097  OE1 GLU A 703      34.160  -6.680  19.824  1.00 43.67           O  
ANISOU 4097  OE1 GLU A 703     5368   4421   6802    665   1182   -692
ATOM   4098  OE2 GLU A 703      35.496  -7.240  21.498  1.00 54.79           O1-
ANISOU 4098  OE2 GLU A 703     5649   6167   8999   2707   -981    359
ATOM   4099  H   GLU A 703      31.681  -3.853  22.962  1.00  0.00           H  
ATOM   4100  HA  GLU A 703      34.150  -2.539  22.044  1.00  0.00           H  
ATOM   4101  HB3 GLU A 703      33.795  -4.025  20.035  1.00  0.00           H  
ATOM   4102  HB2 GLU A 703      32.381  -4.682  20.806  1.00  0.00           H  
ATOM   4103  HG3 GLU A 703      33.710  -5.592  22.664  1.00  0.00           H  
ATOM   4104  HG2 GLU A 703      35.136  -4.748  22.116  1.00  0.00           H  
ATOM   4105  N   ARG A 704      31.299  -1.407  21.116  1.00 19.12           N  
ANISOU 4105  N   ARG A 704     2350   2210   2703   -180   -499    501
ATOM   4106  CA  ARG A 704      30.608  -0.374  20.342  1.00 18.05           C  
ANISOU 4106  CA  ARG A 704     1818   2721   2317   -154   -660    147
ATOM   4107  C   ARG A 704      31.152   1.036  20.653  1.00 17.61           C  
ANISOU 4107  C   ARG A 704     1533   2755   2400   -207   -629    -73
ATOM   4108  O   ARG A 704      31.532   1.292  21.796  1.00 21.52           O  
ANISOU 4108  O   ARG A 704     2722   2897   2555    -70   -977   -187
ATOM   4109  CB  ARG A 704      29.101  -0.428  20.646  1.00 18.45           C  
ANISOU 4109  CB  ARG A 704     1941   2918   2149   -927   -110    392
ATOM   4110  CG  ARG A 704      28.453  -1.769  20.292  1.00 19.87           C  
ANISOU 4110  CG  ARG A 704     2298   2743   2508   -612   -155    -55
ATOM   4111  CD  ARG A 704      26.963  -1.801  20.644  1.00 18.30           C  
ANISOU 4111  CD  ARG A 704     2116   2198   2636    148    -62    192
ATOM   4112  NE  ARG A 704      26.464  -3.176  20.539  1.00 16.26           N  
ANISOU 4112  NE  ARG A 704     1879   2196   2101    130    130     18
ATOM   4113  CZ  ARG A 704      25.581  -3.802  21.331  1.00 15.78           C  
ANISOU 4113  CZ  ARG A 704     1239   2065   2691     58     74   -228
ATOM   4114  NH1 ARG A 704      24.852  -3.146  22.234  1.00 15.01           N  
ANISOU 4114  NH1 ARG A 704     1662   1878   2163    337    -13    -82
ATOM   4115  NH2 ARG A 704      25.444  -5.125  21.228  1.00 18.13           N1+
ANISOU 4115  NH2 ARG A 704     2619   2066   2203    -34   -237   -197
ATOM   4116  H   ARG A 704      30.800  -1.784  21.910  1.00  0.00           H  
ATOM   4117  HA  ARG A 704      30.762  -0.623  19.295  1.00  0.00           H  
ATOM   4118  HB3 ARG A 704      28.588   0.352  20.088  1.00  0.00           H  
ATOM   4119  HB2 ARG A 704      28.928  -0.202  21.698  1.00  0.00           H  
ATOM   4120  HG3 ARG A 704      28.982  -2.618  20.728  1.00  0.00           H  
ATOM   4121  HG2 ARG A 704      28.549  -1.874  19.210  1.00  0.00           H  
ATOM   4122  HD3 ARG A 704      26.399  -1.234  19.904  1.00  0.00           H  
ATOM   4123  HD2 ARG A 704      26.782  -1.331  21.609  1.00  0.00           H  
ATOM   4124  HE  ARG A 704      26.946  -3.751  19.857  1.00  0.00           H  
ATOM   4125 HH12 ARG A 704      24.233  -3.648  22.865  1.00  0.00           H  
ATOM   4126 HH11 ARG A 704      24.913  -2.138  22.290  1.00  0.00           H  
ATOM   4127 HH22 ARG A 704      24.840  -5.630  21.867  1.00  0.00           H  
ATOM   4128 HH21 ARG A 704      26.016  -5.640  20.570  1.00  0.00           H  
ATOM   4129  N   PRO A 705      31.149   1.942  19.649  1.00 15.82           N  
ANISOU 4129  N   PRO A 705     1489   2156   2365   -221   -432    -56
ATOM   4130  CA  PRO A 705      31.508   3.353  19.855  1.00 16.95           C  
ANISOU 4130  CA  PRO A 705     1953   2377   2110   -148   -453   -469
ATOM   4131  C   PRO A 705      30.377   4.113  20.566  1.00 18.10           C  
ANISOU 4131  C   PRO A 705     2498   2216   2161   -383    -31   -382
ATOM   4132  O   PRO A 705      29.213   3.794  20.352  1.00 18.18           O  
ANISOU 4132  O   PRO A 705     2070   2551   2285     95    193   -808
ATOM   4133  CB  PRO A 705      31.720   3.861  18.419  1.00 19.92           C  
ANISOU 4133  CB  PRO A 705     2083   3050   2434    342   -307   -136
ATOM   4134  CG  PRO A 705      30.749   3.050  17.573  1.00 19.17           C  
ANISOU 4134  CG  PRO A 705     2415   2900   1967     -5     -8   -345
ATOM   4135  CD  PRO A 705      30.737   1.694  18.267  1.00 19.05           C  
ANISOU 4135  CD  PRO A 705     2131   2510   2594   -198   -195   -597
ATOM   4136  HA  PRO A 705      32.433   3.443  20.428  1.00  0.00           H  
ATOM   4137  HB3 PRO A 705      32.742   3.641  18.108  1.00  0.00           H  
ATOM   4138  HB2 PRO A 705      31.576   4.937  18.309  1.00  0.00           H  
ATOM   4139  HG3 PRO A 705      31.028   2.995  16.520  1.00  0.00           H  
ATOM   4140  HG2 PRO A 705      29.754   3.489  17.631  1.00  0.00           H  
ATOM   4141  HD2 PRO A 705      29.754   1.233  18.203  1.00  0.00           H  
ATOM   4142  HD3 PRO A 705      31.467   1.029  17.812  1.00  0.00           H  
ATOM   4143  N   SER A 706      30.717   5.107  21.394  1.00 17.29           N  
ANISOU 4143  N   SER A 706     2397   1894   2276   -467   -574     40
ATOM   4144  CA  SER A 706      29.731   6.022  21.980  1.00 21.02           C  
ANISOU 4144  CA  SER A 706     2915   2709   2361    344   -355    411
ATOM   4145  C   SER A 706      29.323   7.110  20.960  1.00 16.49           C  
ANISOU 4145  C   SER A 706     1682   2277   2303    117   -393     78
ATOM   4146  O   SER A 706      30.013   7.290  19.957  1.00 18.53           O  
ANISOU 4146  O   SER A 706     1916   2616   2507   -389   -150    240
ATOM   4147  CB  SER A 706      30.316   6.596  23.284  1.00 28.09           C  
ANISOU 4147  CB  SER A 706     3986   3462   3224    589  -1178    -25
ATOM   4148  OG  SER A 706      30.244   5.649  24.329  1.00 40.62           O  
ANISOU 4148  OG  SER A 706     4948   5352   5133    523    -25   1351
ATOM   4149  H   SER A 706      31.692   5.326  21.550  1.00  0.00           H  
ATOM   4150  HA  SER A 706      28.820   5.474  22.229  1.00  0.00           H  
ATOM   4151  HB3 SER A 706      29.769   7.480  23.611  1.00  0.00           H  
ATOM   4152  HB2 SER A 706      31.357   6.876  23.160  1.00  0.00           H  
ATOM   4153  HG  SER A 706      30.658   6.026  25.109  1.00  0.00           H  
ATOM   4154  N   PHE A 707      28.204   7.815  21.202  1.00 16.27           N  
ANISOU 4154  N   PHE A 707     2044   2243   1894    430   -203     16
ATOM   4155  CA  PHE A 707      27.681   8.831  20.278  1.00 16.08           C  
ANISOU 4155  CA  PHE A 707     1827   2354   1925    254   -353    -18
ATOM   4156  C   PHE A 707      28.543  10.066  19.925  1.00 18.57           C  
ANISOU 4156  C   PHE A 707     1801   3007   2249    -76   -121    -37
ATOM   4157  O   PHE A 707      28.410  10.519  18.788  1.00 18.49           O  
ANISOU 4157  O   PHE A 707     2310   2552   2160   -333    -75   -139
ATOM   4158  CB  PHE A 707      26.221   9.216  20.575  1.00 17.38           C  
ANISOU 4158  CB  PHE A 707     1805   3048   1749    376   -149    574
ATOM   4159  CG  PHE A 707      25.194   8.305  19.935  1.00 18.03           C  
ANISOU 4159  CG  PHE A 707     2087   2756   2007    245   -128    245
ATOM   4160  CD1 PHE A 707      24.895   8.426  18.560  1.00 18.82           C  
ANISOU 4160  CD1 PHE A 707     2064   2946   2140    164     90    319
ATOM   4161  CE1 PHE A 707      24.006   7.540  17.967  1.00 17.80           C  
ANISOU 4161  CE1 PHE A 707     2062   3011   1690    512   -304     22
ATOM   4162  CZ  PHE A 707      23.414   6.537  18.725  1.00 16.37           C  
ANISOU 4162  CZ  PHE A 707     1726   2624   1869    656    -98     98
ATOM   4163  CD2 PHE A 707      24.648   7.233  20.663  1.00 17.76           C  
ANISOU 4163  CD2 PHE A 707     1650   2946   2149    -24   -902    550
ATOM   4164  CE2 PHE A 707      23.735   6.379  20.064  1.00 14.96           C  
ANISOU 4164  CE2 PHE A 707      948   2760   1975    408   -485     68
ATOM   4165  H   PHE A 707      27.666   7.645  22.044  1.00  0.00           H  
ATOM   4166  HA  PHE A 707      27.636   8.303  19.328  1.00  0.00           H  
ATOM   4167  HB3 PHE A 707      26.012  10.210  20.187  1.00  0.00           H  
ATOM   4168  HB2 PHE A 707      26.050   9.275  21.651  1.00  0.00           H  
ATOM   4169  HD1 PHE A 707      25.351   9.208  17.970  1.00  0.00           H  
ATOM   4170  HE1 PHE A 707      23.765   7.639  16.919  1.00  0.00           H  
ATOM   4171  HZ  PHE A 707      22.701   5.867  18.281  1.00  0.00           H  
ATOM   4172  HD2 PHE A 707      24.937   7.082  21.689  1.00  0.00           H  
ATOM   4173  HE2 PHE A 707      23.287   5.578  20.634  1.00  0.00           H  
ATOM   4174  N   PRO A 708      29.465  10.538  20.800  1.00 18.45           N  
ANISOU 4174  N   PRO A 708     2359   2496   2155   -606    249   -616
ATOM   4175  CA  PRO A 708      30.485  11.526  20.397  1.00 21.02           C  
ANISOU 4175  CA  PRO A 708     2131   3545   2310  -1021   -258   -174
ATOM   4176  C   PRO A 708      31.448  11.012  19.307  1.00 20.84           C  
ANISOU 4176  C   PRO A 708     2269   3532   2114   -973   -184    257
ATOM   4177  O   PRO A 708      31.714  11.745  18.357  1.00 23.91           O  
ANISOU 4177  O   PRO A 708     3198   4019   1868  -1454    301    145
ATOM   4178  CB  PRO A 708      31.215  11.883  21.704  1.00 21.38           C  
ANISOU 4178  CB  PRO A 708     1965   3784   2371  -1149   -166   -169
ATOM   4179  CG  PRO A 708      30.257  11.497  22.820  1.00 20.33           C  
ANISOU 4179  CG  PRO A 708     1676   3619   2427   -872     78   -397
ATOM   4180  CD  PRO A 708      29.499  10.309  22.244  1.00 18.68           C  
ANISOU 4180  CD  PRO A 708     1821   2921   2352   -218   -130   -221
ATOM   4181  HA  PRO A 708      29.959  12.410  20.031  1.00  0.00           H  
ATOM   4182  HB3 PRO A 708      31.487  12.938  21.750  1.00  0.00           H  
ATOM   4183  HB2 PRO A 708      32.138  11.311  21.807  1.00  0.00           H  
ATOM   4184  HG3 PRO A 708      29.570  12.319  23.006  1.00  0.00           H  
ATOM   4185  HG2 PRO A 708      30.758  11.270  23.761  1.00  0.00           H  
ATOM   4186  HD2 PRO A 708      30.062   9.401  22.442  1.00  0.00           H  
ATOM   4187  HD3 PRO A 708      28.507  10.211  22.687  1.00  0.00           H  
ATOM   4188  N   ARG A 709      31.910   9.755  19.450  1.00 20.10           N  
ANISOU 4188  N   ARG A 709     2308   3302   2025   -699     53  -1072
ATOM   4189  CA  ARG A 709      32.755   9.036  18.492  1.00 21.62           C  
ANISOU 4189  CA  ARG A 709     2263   3627   2323   -565    274  -1072
ATOM   4190  C   ARG A 709      32.040   8.773  17.154  1.00 22.73           C  
ANISOU 4190  C   ARG A 709     2651   4152   1832   -722    665   -404
ATOM   4191  O   ARG A 709      32.659   8.964  16.107  1.00 23.50           O  
ANISOU 4191  O   ARG A 709     2548   4790   1590  -1150    553   -654
ATOM   4192  CB  ARG A 709      33.262   7.732  19.157  1.00 25.24           C  
ANISOU 4192  CB  ARG A 709     2524   4141   2924     68    509   -963
ATOM   4193  CG  ARG A 709      34.126   6.802  18.291  1.00 30.42           C  
ANISOU 4193  CG  ARG A 709     2539   4854   4164    -88   1338  -1135
ATOM   4194  CD  ARG A 709      35.592   7.253  18.208  1.00 36.17           C  
ANISOU 4194  CD  ARG A 709     2998   4716   6028   -430   1939  -1917
ATOM   4195  NE  ARG A 709      36.330   6.504  17.179  1.00 24.62           N  
ANISOU 4195  NE  ARG A 709     2512   3455   3384   -813    768  -1232
ATOM   4196  CZ  ARG A 709      36.334   6.780  15.862  1.00 26.49           C  
ANISOU 4196  CZ  ARG A 709     3481   3506   3075     22   1102  -1104
ATOM   4197  NH1 ARG A 709      35.658   7.822  15.358  1.00 27.18           N  
ANISOU 4197  NH1 ARG A 709     2822   3456   4048   -356    671  -1099
ATOM   4198  NH2 ARG A 709      37.026   5.998  15.025  1.00 21.89           N1+
ANISOU 4198  NH2 ARG A 709     1980   2406   3932    184    223  -1012
ATOM   4199  H   ARG A 709      31.652   9.233  20.277  1.00  0.00           H  
ATOM   4200  HA  ARG A 709      33.619   9.668  18.280  1.00  0.00           H  
ATOM   4201  HB3 ARG A 709      32.412   7.146  19.500  1.00  0.00           H  
ATOM   4202  HB2 ARG A 709      33.826   7.984  20.054  1.00  0.00           H  
ATOM   4203  HG3 ARG A 709      33.688   6.572  17.318  1.00  0.00           H  
ATOM   4204  HG2 ARG A 709      34.125   5.850  18.824  1.00  0.00           H  
ATOM   4205  HD3 ARG A 709      36.082   6.954  19.135  1.00  0.00           H  
ATOM   4206  HD2 ARG A 709      35.712   8.335  18.143  1.00  0.00           H  
ATOM   4207  HE  ARG A 709      36.837   5.693  17.502  1.00  0.00           H  
ATOM   4208 HH12 ARG A 709      35.688   8.015  14.361  1.00  0.00           H  
ATOM   4209 HH11 ARG A 709      35.098   8.412  15.956  1.00  0.00           H  
ATOM   4210 HH22 ARG A 709      37.025   6.199  14.034  1.00  0.00           H  
ATOM   4211 HH21 ARG A 709      37.545   5.203  15.370  1.00  0.00           H  
ATOM   4212  N   ILE A 710      30.759   8.365  17.216  1.00 19.93           N  
ANISOU 4212  N   ILE A 710     2441   3416   1716   -318    -51   -326
ATOM   4213  CA  ILE A 710      29.906   8.116  16.050  1.00 18.97           C  
ANISOU 4213  CA  ILE A 710     3027   2563   1615   -480   -152   -128
ATOM   4214  C   ILE A 710      29.663   9.388  15.229  1.00 19.28           C  
ANISOU 4214  C   ILE A 710     2628   2625   2073   -399    -39   -176
ATOM   4215  O   ILE A 710      29.856   9.361  14.015  1.00 24.53           O  
ANISOU 4215  O   ILE A 710     3617   3639   2064   -623     91   -394
ATOM   4216  CB  ILE A 710      28.528   7.500  16.437  1.00 17.87           C  
ANISOU 4216  CB  ILE A 710     2562   2584   1644    -77   -297   -139
ATOM   4217  CG1 ILE A 710      28.708   6.073  16.989  1.00 16.75           C  
ANISOU 4217  CG1 ILE A 710     2256   2218   1887   -151    -74   -392
ATOM   4218  CG2 ILE A 710      27.459   7.491  15.319  1.00 19.66           C  
ANISOU 4218  CG2 ILE A 710     2279   3174   2017   -159   -355   -186
ATOM   4219  CD1 ILE A 710      27.477   5.536  17.727  1.00 18.67           C  
ANISOU 4219  CD1 ILE A 710     2397   2032   2664    -54   -154    403
ATOM   4220  H   ILE A 710      30.332   8.218  18.121  1.00  0.00           H  
ATOM   4221  HA  ILE A 710      30.442   7.408  15.422  1.00  0.00           H  
ATOM   4222  HB  ILE A 710      28.123   8.114  17.237  1.00  0.00           H  
ATOM   4223 HG13 ILE A 710      29.554   6.034  17.673  1.00  0.00           H  
ATOM   4224 HG12 ILE A 710      28.962   5.398  16.172  1.00  0.00           H  
ATOM   4225 HG21 ILE A 710      26.539   7.026  15.669  1.00  0.00           H  
ATOM   4226 HG22 ILE A 710      27.173   8.492  14.997  1.00  0.00           H  
ATOM   4227 HG23 ILE A 710      27.805   6.938  14.445  1.00  0.00           H  
ATOM   4228 HD11 ILE A 710      27.772   4.752  18.420  1.00  0.00           H  
ATOM   4229 HD12 ILE A 710      26.976   6.311  18.304  1.00  0.00           H  
ATOM   4230 HD13 ILE A 710      26.749   5.108  17.038  1.00  0.00           H  
ATOM   4231  N   LEU A 711      29.265  10.469  15.921  1.00 20.19           N  
ANISOU 4231  N   LEU A 711     3300   2358   2011    -19   -389   -233
ATOM   4232  CA  LEU A 711      29.014  11.783  15.342  1.00 26.25           C  
ANISOU 4232  CA  LEU A 711     5582   2447   1942   -356   -231   -388
ATOM   4233  C   LEU A 711      30.258  12.336  14.634  1.00 29.18           C  
ANISOU 4233  C   LEU A 711     6384   2640   2062   -583     45   -272
ATOM   4234  O   LEU A 711      30.142  12.699  13.468  1.00 32.32           O  
ANISOU 4234  O   LEU A 711     6931   2694   2653   -316   -250    295
ATOM   4235  CB  LEU A 711      28.466  12.725  16.434  1.00 26.37           C  
ANISOU 4235  CB  LEU A 711     5274   2792   1954   -490   -273   -609
ATOM   4236  CG  LEU A 711      28.154  14.168  15.983  1.00 27.27           C  
ANISOU 4236  CG  LEU A 711     3538   4233   2590    290   -105   -480
ATOM   4237  CD1 LEU A 711      27.132  14.214  14.832  1.00 27.10           C  
ANISOU 4237  CD1 LEU A 711     2136   4604   3556   -285    289  -1046
ATOM   4238  CD2 LEU A 711      27.699  15.013  17.187  1.00 33.62           C  
ANISOU 4238  CD2 LEU A 711     3384   5762   3628    609    279  -1651
ATOM   4239  H   LEU A 711      29.129  10.397  16.922  1.00  0.00           H  
ATOM   4240  HA  LEU A 711      28.234  11.648  14.590  1.00  0.00           H  
ATOM   4241  HB3 LEU A 711      29.185  12.764  17.255  1.00  0.00           H  
ATOM   4242  HB2 LEU A 711      27.559  12.287  16.853  1.00  0.00           H  
ATOM   4243  HG  LEU A 711      29.074  14.627  15.620  1.00  0.00           H  
ATOM   4244 HD11 LEU A 711      26.719  15.215  14.711  1.00  0.00           H  
ATOM   4245 HD12 LEU A 711      27.599  13.955  13.881  1.00  0.00           H  
ATOM   4246 HD13 LEU A 711      26.305  13.524  14.998  1.00  0.00           H  
ATOM   4247 HD21 LEU A 711      26.695  15.409  17.058  1.00  0.00           H  
ATOM   4248 HD22 LEU A 711      27.691  14.429  18.106  1.00  0.00           H  
ATOM   4249 HD23 LEU A 711      28.372  15.855  17.351  1.00  0.00           H  
ATOM   4250  N   ALA A 712      31.419  12.309  15.315  1.00 31.85           N  
ANISOU 4250  N   ALA A 712     5961   3075   3065   -623   -133   -151
ATOM   4251  CA  ALA A 712      32.721  12.720  14.782  1.00 38.26           C  
ANISOU 4251  CA  ALA A 712     7558   4712   2267  -1810    715    244
ATOM   4252  C   ALA A 712      33.132  12.000  13.484  1.00 33.69           C  
ANISOU 4252  C   ALA A 712     6587   3732   2479  -2464     80    158
ATOM   4253  O   ALA A 712      33.680  12.648  12.594  1.00 35.34           O  
ANISOU 4253  O   ALA A 712     7095   3871   2460  -3234    266   -188
ATOM   4254  CB  ALA A 712      33.794  12.526  15.865  1.00 42.81           C  
ANISOU 4254  CB  ALA A 712     8599   5592   2072  -2807    -73   -229
ATOM   4255  H   ALA A 712      31.421  11.977  16.270  1.00  0.00           H  
ATOM   4256  HA  ALA A 712      32.653  13.786  14.557  1.00  0.00           H  
ATOM   4257  HB1 ALA A 712      34.780  12.823  15.504  1.00  0.00           H  
ATOM   4258  HB2 ALA A 712      33.573  13.133  16.743  1.00  0.00           H  
ATOM   4259  HB3 ALA A 712      33.859  11.486  16.188  1.00  0.00           H  
ATOM   4260  N   GLU A 713      32.821  10.695  13.387  1.00 26.14           N  
ANISOU 4260  N   GLU A 713     4155   3240   2538  -1239    129   -253
ATOM   4261  CA  GLU A 713      33.098   9.864  12.216  1.00 22.27           C  
ANISOU 4261  CA  GLU A 713     3065   2891   2506  -1288    543    271
ATOM   4262  C   GLU A 713      32.191  10.204  11.017  1.00 25.06           C  
ANISOU 4262  C   GLU A 713     3765   3098   2657   -491    572    251
ATOM   4263  O   GLU A 713      32.667  10.156   9.882  1.00 26.11           O  
ANISOU 4263  O   GLU A 713     3635   3561   2725  -1025    842    530
ATOM   4264  CB  GLU A 713      32.986   8.377  12.630  1.00 26.60           C  
ANISOU 4264  CB  GLU A 713     3861   3004   3239  -1522   1549    629
ATOM   4265  CG  GLU A 713      33.603   7.357  11.644  1.00 30.16           C  
ANISOU 4265  CG  GLU A 713     3579   3498   4383    -40    460    945
ATOM   4266  CD  GLU A 713      35.143   7.347  11.562  1.00 33.26           C  
ANISOU 4266  CD  GLU A 713     3079   3916   5642   -736    729    727
ATOM   4267  OE1 GLU A 713      35.817   8.098  12.299  1.00 28.03           O  
ANISOU 4267  OE1 GLU A 713     2707   3026   4917     53    890    327
ATOM   4268  OE2 GLU A 713      35.652   6.556  10.744  1.00 33.60           O1-
ANISOU 4268  OE2 GLU A 713     5020   3723   4021  -2019  -1726   -196
ATOM   4269  H   GLU A 713      32.360  10.236  14.161  1.00  0.00           H  
ATOM   4270  HA  GLU A 713      34.124  10.079  11.914  1.00  0.00           H  
ATOM   4271  HB3 GLU A 713      31.933   8.127  12.758  1.00  0.00           H  
ATOM   4272  HB2 GLU A 713      33.418   8.229  13.619  1.00  0.00           H  
ATOM   4273  HG3 GLU A 713      33.194   7.508  10.644  1.00  0.00           H  
ATOM   4274  HG2 GLU A 713      33.286   6.358  11.945  1.00  0.00           H  
ATOM   4275  N   ILE A 714      30.924  10.574  11.285  1.00 22.23           N  
ANISOU 4275  N   ILE A 714     3571   2648   2227      1   -441    112
ATOM   4276  CA  ILE A 714      29.965  11.016  10.267  1.00 22.85           C  
ANISOU 4276  CA  ILE A 714     3176   3369   2136    -74    -25    507
ATOM   4277  C   ILE A 714      30.251  12.455   9.790  1.00 27.05           C  
ANISOU 4277  C   ILE A 714     5610   2671   1997    164    448   -111
ATOM   4278  O   ILE A 714      30.107  12.712   8.596  1.00 29.22           O  
ANISOU 4278  O   ILE A 714     5383   3971   1747    719    501   -222
ATOM   4279  CB  ILE A 714      28.481  10.931  10.741  1.00 22.10           C  
ANISOU 4279  CB  ILE A 714     3586   2927   1884    766    499    -10
ATOM   4280  CG1 ILE A 714      28.094   9.485  11.115  1.00 22.58           C  
ANISOU 4280  CG1 ILE A 714     2913   2851   2816    945    658   -137
ATOM   4281  CG2 ILE A 714      27.475  11.457   9.693  1.00 24.98           C  
ANISOU 4281  CG2 ILE A 714     3891   3231   2368   1190    206   -147
ATOM   4282  CD1 ILE A 714      26.769   9.364  11.881  1.00 22.35           C  
ANISOU 4282  CD1 ILE A 714     2511   2780   3199    709    298   -231
ATOM   4283  H   ILE A 714      30.600  10.588  12.243  1.00  0.00           H  
ATOM   4284  HA  ILE A 714      30.070  10.355   9.404  1.00  0.00           H  
ATOM   4285  HB  ILE A 714      28.379  11.541  11.640  1.00  0.00           H  
ATOM   4286 HG13 ILE A 714      28.869   9.048  11.734  1.00  0.00           H  
ATOM   4287 HG12 ILE A 714      28.053   8.871  10.215  1.00  0.00           H  
ATOM   4288 HG21 ILE A 714      26.447  11.273   9.995  1.00  0.00           H  
ATOM   4289 HG22 ILE A 714      27.569  12.530   9.531  1.00  0.00           H  
ATOM   4290 HG23 ILE A 714      27.617  10.960   8.734  1.00  0.00           H  
ATOM   4291 HD11 ILE A 714      26.772   8.482  12.521  1.00  0.00           H  
ATOM   4292 HD12 ILE A 714      26.589  10.231  12.516  1.00  0.00           H  
ATOM   4293 HD13 ILE A 714      25.926   9.267  11.197  1.00  0.00           H  
ATOM   4294  N   GLU A 715      30.675  13.355  10.699  1.00 32.35           N  
ANISOU 4294  N   GLU A 715     6690   3032   2569   -991    856   -200
ATOM   4295  CA  GLU A 715      31.071  14.727  10.362  1.00 37.00           C  
ANISOU 4295  CA  GLU A 715     7862   3287   2909  -1467    528   -123
ATOM   4296  C   GLU A 715      32.336  14.768   9.483  1.00 40.71           C  
ANISOU 4296  C   GLU A 715     9107   3806   2553    -60   1153    323
ATOM   4297  O   GLU A 715      32.400  15.598   8.576  1.00 48.08           O  
ANISOU 4297  O   GLU A 715    10837   5102   2328  -2063     96    613
ATOM   4298  CB  GLU A 715      31.226  15.608  11.627  1.00 41.58           C  
ANISOU 4298  CB  GLU A 715     9469   2269   4061  -1850    353   -490
ATOM   4299  CG  GLU A 715      29.971  15.652  12.540  1.00 42.36           C  
ANISOU 4299  CG  GLU A 715     8080   5289   2727   -822   -863   -495
ATOM   4300  CD  GLU A 715      29.533  17.038  13.031  1.00 61.23           C  
ANISOU 4300  CD  GLU A 715    10333   3757   9175  -3574   -357  -1825
ATOM   4301  OE1 GLU A 715      30.404  17.850  13.409  1.00 76.74           O  
ANISOU 4301  OE1 GLU A 715     8114  12328   8714  -5692    467  -2445
ATOM   4302  OE2 GLU A 715      28.306  17.278  13.016  1.00 67.40           O1-
ANISOU 4302  OE2 GLU A 715    10189  11013   4404  -4166  -1750   1369
ATOM   4303  H   GLU A 715      30.749  13.088  11.673  1.00  0.00           H  
ATOM   4304  HA  GLU A 715      30.261  15.154   9.768  1.00  0.00           H  
ATOM   4305  HB3 GLU A 715      31.509  16.613  11.310  1.00  0.00           H  
ATOM   4306  HB2 GLU A 715      32.071  15.246  12.215  1.00  0.00           H  
ATOM   4307  HG3 GLU A 715      30.193  15.102  13.450  1.00  0.00           H  
ATOM   4308  HG2 GLU A 715      29.131  15.137  12.069  1.00  0.00           H  
ATOM   4309  N   GLU A 716      33.276  13.834   9.726  1.00 37.43           N  
ANISOU 4309  N   GLU A 716     7356   4331   2535  -1458   -945    804
ATOM   4310  CA  GLU A 716      34.458  13.598   8.895  1.00 43.11           C  
ANISOU 4310  CA  GLU A 716     7295   5430   3651  -2667    365    178
ATOM   4311  C   GLU A 716      34.101  13.029   7.508  1.00 39.13           C  
ANISOU 4311  C   GLU A 716     6216   5156   3494  -2350    730    790
ATOM   4312  O   GLU A 716      34.703  13.451   6.522  1.00 41.25           O  
ANISOU 4312  O   GLU A 716     6264   5826   3580   -791   1742    752
ATOM   4313  CB  GLU A 716      35.455  12.692   9.657  1.00  0.00           C  
ATOM   4314  CG  GLU A 716      36.784  12.383   8.921  1.00  0.00           C  
ATOM   4315  CD  GLU A 716      37.640  13.625   8.614  1.00  0.00           C  
ATOM   4316  OE1 GLU A 716      37.824  14.451   9.536  1.00  0.00           O  
ATOM   4317  OE2 GLU A 716      38.105  13.728   7.457  1.00  0.00           O1-
ATOM   4318  H   GLU A 716      33.156  13.203  10.507  1.00  0.00           H  
ATOM   4319  HA  GLU A 716      34.932  14.568   8.736  1.00  0.00           H  
ATOM   4320  HB2 GLU A 716      35.679  13.142  10.625  1.00  0.00           H  
ATOM   4321  HB3 GLU A 716      34.969  11.745   9.895  1.00  0.00           H  
ATOM   4322  HG2 GLU A 716      37.384  11.718   9.543  1.00  0.00           H  
ATOM   4323  HG3 GLU A 716      36.588  11.823   8.005  1.00  0.00           H  
ATOM   4324  N   LEU A 717      33.115  12.113   7.448  1.00 30.95           N  
ANISOU 4324  N   LEU A 717     5789   3422   2546  -1206   1572    881
ATOM   4325  CA  LEU A 717      32.616  11.549   6.194  1.00 36.86           C  
ANISOU 4325  CA  LEU A 717     5600   4952   3453    -56    940   -337
ATOM   4326  C   LEU A 717      31.905  12.585   5.314  1.00 38.84           C  
ANISOU 4326  C   LEU A 717     6943   4886   2928   -844   2008    722
ATOM   4327  O   LEU A 717      32.162  12.618   4.114  1.00 47.88           O  
ANISOU 4327  O   LEU A 717     8524   6473   3194    604   2751   1245
ATOM   4328  CB  LEU A 717      31.692  10.340   6.460  1.00 41.09           C  
ANISOU 4328  CB  LEU A 717     6908   4156   4545   -276    -36  -1344
ATOM   4329  CG  LEU A 717      31.010   9.746   5.202  1.00 46.23           C  
ANISOU 4329  CG  LEU A 717     6879   4972   5712  -1902   -595  -1125
ATOM   4330  CD1 LEU A 717      32.026   9.233   4.163  1.00 52.06           C  
ANISOU 4330  CD1 LEU A 717     7882   4862   7037  -1464   -676  -3371
ATOM   4331  CD2 LEU A 717      29.991   8.672   5.577  1.00 44.03           C  
ANISOU 4331  CD2 LEU A 717     6607   4822   5300   -965    637   -172
ATOM   4332  H   LEU A 717      32.667  11.800   8.298  1.00  0.00           H  
ATOM   4333  HA  LEU A 717      33.498  11.206   5.654  1.00  0.00           H  
ATOM   4334  HB3 LEU A 717      30.907  10.646   7.151  1.00  0.00           H  
ATOM   4335  HB2 LEU A 717      32.243   9.559   6.981  1.00  0.00           H  
ATOM   4336  HG  LEU A 717      30.424  10.522   4.712  1.00  0.00           H  
ATOM   4337 HD11 LEU A 717      31.673   9.416   3.149  1.00  0.00           H  
ATOM   4338 HD12 LEU A 717      33.005   9.698   4.239  1.00  0.00           H  
ATOM   4339 HD13 LEU A 717      32.198   8.167   4.285  1.00  0.00           H  
ATOM   4340 HD21 LEU A 717      29.899   7.933   4.782  1.00  0.00           H  
ATOM   4341 HD22 LEU A 717      30.265   8.162   6.501  1.00  0.00           H  
ATOM   4342 HD23 LEU A 717      29.005   9.112   5.723  1.00  0.00           H  
ATOM   4343  N   ALA A 718      31.017  13.387   5.920  1.00 33.91           N  
ANISOU 4343  N   ALA A 718     5932   4974   1976   -819    253   -236
ATOM   4344  CA  ALA A 718      30.262  14.446   5.253  1.00 35.36           C  
ANISOU 4344  CA  ALA A 718     5163   5759   2511  -1409    461    485
ATOM   4345  C   ALA A 718      31.164  15.555   4.681  1.00 43.41           C  
ANISOU 4345  C   ALA A 718     4403   7283   4807  -2512    685    504
ATOM   4346  O   ALA A 718      30.807  16.151   3.667  1.00 47.52           O  
ANISOU 4346  O   ALA A 718     8261   6670   3123  -1660    694  -1346
ATOM   4347  CB  ALA A 718      29.242  15.017   6.244  1.00 42.83           C  
ANISOU 4347  CB  ALA A 718     8435   6097   1742  -1165   1207    386
ATOM   4348  H   ALA A 718      30.836  13.267   6.909  1.00  0.00           H  
ATOM   4349  HA  ALA A 718      29.715  13.997   4.421  1.00  0.00           H  
ATOM   4350  HB1 ALA A 718      28.636  15.795   5.778  1.00  0.00           H  
ATOM   4351  HB2 ALA A 718      28.561  14.242   6.597  1.00  0.00           H  
ATOM   4352  HB3 ALA A 718      29.733  15.447   7.118  1.00  0.00           H  
ATOM   4353  N   ARG A 719      32.326  15.769   5.323  1.00 37.01           N  
ANISOU 4353  N   ARG A 719     5555   4574   3931   -758  -1017   -545
ATOM   4354  CA  ARG A 719      33.396  16.654   4.875  1.00 45.80           C  
ANISOU 4354  CA  ARG A 719     7173   5187   5039  -1131   1158   1219
ATOM   4355  C   ARG A 719      34.208  16.053   3.710  1.00 56.48           C  
ANISOU 4355  C   ARG A 719    10409   6423   4628  -2715   2585   1181
ATOM   4356  O   ARG A 719      34.546  16.789   2.783  1.00 68.00           O  
ANISOU 4356  O   ARG A 719    12093   4771   8972  -3264   6792   1978
ATOM   4357  CB  ARG A 719      34.280  16.996   6.096  1.00  0.00           C  
ATOM   4358  CG  ARG A 719      35.452  17.970   5.845  1.00  0.00           C  
ATOM   4359  CD  ARG A 719      35.049  19.373   5.349  1.00  0.00           C  
ATOM   4360  NE  ARG A 719      34.301  20.132   6.369  1.00  0.00           N  
ATOM   4361  CZ  ARG A 719      33.727  21.343   6.227  1.00  0.00           C  
ATOM   4362  NH1 ARG A 719      33.787  22.030   5.076  1.00  0.00           N  
ATOM   4363  NH2 ARG A 719      33.077  21.877   7.269  1.00  0.00           N1+
ATOM   4364  H   ARG A 719      32.524  15.234   6.157  1.00  0.00           H  
ATOM   4365  HA  ARG A 719      32.925  17.571   4.516  1.00  0.00           H  
ATOM   4366  HB2 ARG A 719      33.647  17.401   6.886  1.00  0.00           H  
ATOM   4367  HB3 ARG A 719      34.696  16.078   6.509  1.00  0.00           H  
ATOM   4368  HG2 ARG A 719      35.966  18.080   6.801  1.00  0.00           H  
ATOM   4369  HG3 ARG A 719      36.201  17.539   5.180  1.00  0.00           H  
ATOM   4370  HD2 ARG A 719      35.919  19.923   4.989  1.00  0.00           H  
ATOM   4371  HD3 ARG A 719      34.383  19.274   4.493  1.00  0.00           H  
ATOM   4372  HE  ARG A 719      34.227  19.677   7.268  1.00  0.00           H  
ATOM   4373 HH12 ARG A 719      33.352  22.937   4.990  1.00  0.00           H  
ATOM   4374 HH11 ARG A 719      34.275  21.638   4.283  1.00  0.00           H  
ATOM   4375 HH22 ARG A 719      32.642  22.784   7.189  1.00  0.00           H  
ATOM   4376 HH21 ARG A 719      33.033  21.384   8.150  1.00  0.00           H  
ATOM   4377  N   ALA A 720      34.484  14.736   3.767  1.00 51.23           N  
ANISOU 4377  N   ALA A 720    10218   6833   2412  -2728   1603  -2118
ATOM   4378  CA  ALA A 720      35.165  13.973   2.715  1.00 57.86           C  
ANISOU 4378  CA  ALA A 720    11115   4948   5918  -2504   2549  -2805
ATOM   4379  C   ALA A 720      34.317  13.807   1.439  1.00 54.79           C  
ANISOU 4379  C   ALA A 720    10493   7682   2640  -1628   3790  -1956
ATOM   4380  O   ALA A 720      34.879  13.794   0.345  1.00 50.80           O  
ANISOU 4380  O   ALA A 720     7639   9466   2197  -1847   2130   1292
ATOM   4381  CB  ALA A 720      35.587  12.604   3.274  1.00 52.05           C  
ANISOU 4381  CB  ALA A 720    10017   3997   5761  -4526   6402  -1855
ATOM   4382  H   ALA A 720      34.197  14.206   4.579  1.00  0.00           H  
ATOM   4383  HA  ALA A 720      36.071  14.517   2.443  1.00  0.00           H  
ATOM   4384  HB1 ALA A 720      36.136  12.026   2.530  1.00  0.00           H  
ATOM   4385  HB2 ALA A 720      36.237  12.720   4.142  1.00  0.00           H  
ATOM   4386  HB3 ALA A 720      34.726  12.011   3.583  1.00  0.00           H  
ATOM   4387  N   ALA A 721      32.984  13.719   1.603  1.00 60.36           N  
ANISOU 4387  N   ALA A 721     9659   9120   4153   -876   1224    -30
ATOM   4388  CA  ALA A 721      31.979  13.733   0.539  1.00 63.71           C  
ANISOU 4388  CA  ALA A 721     7429  10544   6232    228    887   1015
ATOM   4389  C   ALA A 721      31.689  15.198   0.290  1.00 48.77           C  
ANISOU 4389  C   ALA A 721     6265  10752   1513   -381    728   2743
ATOM   4390  O   ALA A 721      31.795  15.716  -0.820  1.00 56.46           O  
ANISOU 4390  O   ALA A 721     6557   9535   5358    357   2588   3626
ATOM   4391  CB  ALA A 721      30.713  13.009   1.040  1.00 55.92           C  
ANISOU 4391  CB  ALA A 721     6820  11401   3025   -683    735  -1651
ATOM   4392  H   ALA A 721      32.618  13.692   2.546  1.00  0.00           H  
ATOM   4393  HA  ALA A 721      32.350  13.235  -0.359  1.00  0.00           H  
ATOM   4394  HB1 ALA A 721      29.920  13.024   0.291  1.00  0.00           H  
ATOM   4395  HB2 ALA A 721      30.927  11.963   1.261  1.00  0.00           H  
ATOM   4396  HB3 ALA A 721      30.315  13.457   1.952  1.00  0.00           H  
ATOM   4397  HXT ALA A 721      31.398  15.777   1.166  1.00  0.00           H  
TER    4398      ALA A 721
HETATM 4399  C1  032 A 801       1.967  13.706  21.652  1.00 14.30           C  
ANISOU 4399  C1  032 A 801     2030   1975   1426   -113    376   -598
HETATM 4400  C2  032 A 801       3.177  12.961  22.200  1.00 13.98           C  
ANISOU 4400  C2  032 A 801     2202   1518   1591   -144    459   -226
HETATM 4401  C3  032 A 801       3.237  12.671  23.560  1.00 15.08           C  
ANISOU 4401  C3  032 A 801     2205   1681   1841      7     39    -31
HETATM 4402  C4  032 A 801       4.329  11.990  24.087  1.00 14.85           C  
ANISOU 4402  C4  032 A 801     1773   2070   1798   -166   -299     74
HETATM 4403  C5  032 A 801       5.371  11.556  23.262  1.00 14.94           C  
ANISOU 4403  C5  032 A 801     2134   2052   1489   -193    108    282
HETATM 4404  N1  032 A 801       6.382  10.788  23.866  1.00 14.10           N  
ANISOU 4404  N1  032 A 801     2114   1956   1286   -260     49    220
HETATM 4405  C6  032 A 801       7.626  10.476  23.425  1.00 16.18           C  
ANISOU 4405  C6  032 A 801     2289   2137   1718   -127     54    150
HETATM 4406  O1  032 A 801       8.141  10.944  22.408  1.00 15.84           O  
ANISOU 4406  O1  032 A 801     2423   1980   1616    -76    415   -120
HETATM 4407  C7  032 A 801       8.360   9.533  24.269  1.00 18.34           C  
ANISOU 4407  C7  032 A 801     2779   2596   1592    177   -260    274
HETATM 4408  N2  032 A 801       7.662   8.663  24.992  1.00 23.31           N  
ANISOU 4408  N2  032 A 801     2883   3199   2774   -219     11    214
HETATM 4409  C8  032 A 801       8.408   7.854  25.690  1.00 22.40           C  
ANISOU 4409  C8  032 A 801     2980   2610   2918   -178    238    724
HETATM 4410  S1  032 A 801       7.736   6.565  26.811  1.00 35.49           S  
ANISOU 4410  S1  032 A 801     5963   4220   3299    510   1436   2113
HETATM 4411  C9  032 A 801       7.557   5.244  25.523  1.00 44.26           C  
ANISOU 4411  C9  032 A 801     6840   5317   4656  -1032   1399    712
HETATM 4412  O2  032 A 801       8.909   6.157  27.703  1.00 51.47           O  
ANISOU 4412  O2  032 A 801     7103   8351   4102   -481     99   2011
HETATM 4413  S2  032 A 801      10.102   8.068  25.480  1.00 23.71           S  
ANISOU 4413  S2  032 A 801     3029   3501   2477    332    -91    713
HETATM 4414  C10 032 A 801       9.765   9.351  24.336  1.00 19.32           C  
ANISOU 4414  C10 032 A 801     2937   2626   1775    -25   -135     -3
HETATM 4415  C11 032 A 801      10.932  10.049  23.712  1.00 14.92           C  
ANISOU 4415  C11 032 A 801     2295   1706   1665     12   -686   -363
HETATM 4416  C12 032 A 801      12.042   9.327  23.255  1.00 19.18           C  
ANISOU 4416  C12 032 A 801     2759   1830   2698     98   -136   -235
HETATM 4417  C13 032 A 801      13.139   9.995  22.718  1.00 20.48           C  
ANISOU 4417  C13 032 A 801     2546   2089   3145    189   -305   -393
HETATM 4418  C14 032 A 801      13.124  11.383  22.624  1.00 21.75           C  
ANISOU 4418  C14 032 A 801     2312   2071   3878    135   -500   -147
HETATM 4419  F1  032 A 801      14.183  12.023  22.087  1.00 26.43           F  
ANISOU 4419  F1  032 A 801     3109   1714   5217    305    298     -4
HETATM 4420  C15 032 A 801      12.024  12.112  23.068  1.00 19.08           C  
ANISOU 4420  C15 032 A 801     2080   1812   3358    -79    -45   -555
HETATM 4421  C16 032 A 801      10.932  11.442  23.612  1.00 17.89           C  
ANISOU 4421  C16 032 A 801     2465   1616   2715    139    143   -460
HETATM 4422  C17 032 A 801       5.321  11.857  21.896  1.00 13.82           C  
ANISOU 4422  C17 032 A 801     2239   1760   1251     54    520   -271
HETATM 4423  C18 032 A 801       4.242  12.573  21.373  1.00 13.47           C  
ANISOU 4423  C18 032 A 801     2131   1590   1396   -272    388   -166
HETATM 4424  N3  032 A 801       4.244  12.889  20.012  1.00 15.08           N  
ANISOU 4424  N3  032 A 801     2353   1737   1640    -70    314    116
HETATM 4425  C19 032 A 801       3.714  12.113  18.986  1.00 12.79           C  
ANISOU 4425  C19 032 A 801     1646   1496   1717     91    410     47
HETATM 4426  N4  032 A 801       3.304  10.852  19.277  1.00 15.50           N  
ANISOU 4426  N4  032 A 801     2439   1432   2018   -464    319   -311
HETATM 4427  C20 032 A 801       2.780  10.141  18.256  1.00 14.03           C  
ANISOU 4427  C20 032 A 801     1690   1945   1695     35    208   -338
HETATM 4428  C21 032 A 801       2.644  10.665  16.975  1.00 14.78           C  
ANISOU 4428  C21 032 A 801     2199   1521   1894    121    206   -106
HETATM 4429  C22 032 A 801       3.097  11.973  16.750  1.00 14.17           C  
ANISOU 4429  C22 032 A 801     1919   1689   1773   -199   -270    -71
HETATM 4430  C23 032 A 801       3.026  12.633  15.409  1.00 15.28           C  
ANISOU 4430  C23 032 A 801     1555   2359   1888     61   -386    279
HETATM 4431  C24 032 A 801       2.541  11.951  14.280  1.00 18.58           C  
ANISOU 4431  C24 032 A 801     2934   2199   1926    -34   -309     53
HETATM 4432  C25 032 A 801       2.497  12.573  13.037  1.00 17.58           C  
ANISOU 4432  C25 032 A 801     2396   2336   1945   -128    126    115
HETATM 4433  C26 032 A 801       2.937  13.887  12.940  1.00 17.32           C  
ANISOU 4433  C26 032 A 801     2769   2242   1567   -210   -121    163
HETATM 4434  N5  032 A 801       3.409  14.584  14.002  1.00 15.96           N  
ANISOU 4434  N5  032 A 801     2110   2022   1930    -90   -336    175
HETATM 4435  C27 032 A 801       3.451  13.957  15.203  1.00 15.07           C  
ANISOU 4435  C27 032 A 801     2047   2179   1499    316   -314   -339
HETATM 4436  N6  032 A 801       3.643  12.700  17.767  1.00 13.61           N  
ANISOU 4436  N6  032 A 801     1971   1630   1567    192   -243   -147
HETATM 4437 H1_1 032 A 801       2.290  14.593  21.111  1.00  0.00           H  
HETATM 4438 H1_2 032 A 801       1.414  13.077  20.953  1.00  0.00           H  
HETATM 4439 H1_3 032 A 801       1.289  14.033  22.438  1.00  0.00           H  
HETATM 4440  HC3 032 A 801       2.437  12.981  24.211  1.00  0.00           H  
HETATM 4441  HC4 032 A 801       4.348  11.805  25.150  1.00  0.00           H  
HETATM 4442  HN1 032 A 801       6.107  10.387  24.753  1.00  0.00           H  
HETATM 4443 H9_1 032 A 801       7.128   4.346  25.965  1.00  0.00           H  
HETATM 4444 H9_2 032 A 801       6.904   5.581  24.718  1.00  0.00           H  
HETATM 4445 H9_3 032 A 801       8.525   4.987  25.100  1.00  0.00           H  
HETATM 4446 HC12 032 A 801      12.062   8.248  23.315  1.00  0.00           H  
HETATM 4447 HC13 032 A 801      13.996   9.439  22.371  1.00  0.00           H  
HETATM 4448 HC15 032 A 801      12.018  13.190  22.991  1.00  0.00           H  
HETATM 4449 HC16 032 A 801      10.085  12.001  23.971  1.00  0.00           H  
HETATM 4450 HC17 032 A 801       6.096  11.522  21.224  1.00  0.00           H  
HETATM 4451  HN3 032 A 801       4.487  13.843  19.776  1.00  0.00           H  
HETATM 4452 HC20 032 A 801       2.438   9.145  18.486  1.00  0.00           H  
HETATM 4453 HC21 032 A 801       2.187  10.064  16.211  1.00  0.00           H  
HETATM 4454 HC24 032 A 801       2.194  10.933  14.333  1.00  0.00           H  
HETATM 4455 HC25 032 A 801       2.126  12.043  12.174  1.00  0.00           H  
HETATM 4456 HC26 032 A 801       2.894  14.394  11.992  1.00  0.00           H  
HETATM 4457 HC27 032 A 801       3.839  14.558  16.013  1.00  0.00           H  
CONECT 4389 4397
CONECT 4399 4400 4437 4438 4439
CONECT 4400 4399 4401 4423
CONECT 4400 4423
CONECT 4401 4400 4402 4440
CONECT 4401 4402
CONECT 4402 4401 4403 4441
CONECT 4402 4401
CONECT 4403 4402 4404 4422
CONECT 4403 4422
CONECT 4404 4403 4405 4442
CONECT 4405 4404 4406 4407
CONECT 4405 4406
CONECT 4406 4405
CONECT 4406 4405
CONECT 4407 4405 4408 4414
CONECT 4407 4414
CONECT 4408 4407 4409
CONECT 4408 4409
CONECT 4409 4408 4410 4413
CONECT 4409 4408
CONECT 4410 4409 4411 4412
CONECT 4410 4412
CONECT 4411 4410 4443 4444 4445
CONECT 4412 4410
CONECT 4412 4410
CONECT 4413 4409 4414
CONECT 4414 4407 4413 4415
CONECT 4414 4407
CONECT 4415 4414 4416 4421
CONECT 4415 4421
CONECT 4416 4415 4417 4446
CONECT 4416 4417
CONECT 4417 4416 4418 4447
CONECT 4417 4416
CONECT 4418 4417 4419 4420
CONECT 4418 4420
CONECT 4419 4418
CONECT 4420 4418 4421 4448
CONECT 4420 4418
CONECT 4421 4415 4420 4449
CONECT 4421 4415
CONECT 4422 4403 4423 4450
CONECT 4422 4403
CONECT 4423 4400 4422 4424
CONECT 4423 4400
CONECT 4424 4423 4425 4451
CONECT 4425 4424 4426 4436
CONECT 4425 4436
CONECT 4426 4425 4427
CONECT 4426 4427
CONECT 4427 4426 4428 4452
CONECT 4427 4426
CONECT 4428 4427 4429 4453
CONECT 4428 4429
CONECT 4429 4428 4430 4436
CONECT 4429 4428
CONECT 4430 4429 4431 4435
CONECT 4430 4435
CONECT 4431 4430 4432 4454
CONECT 4431 4432
CONECT 4432 4431 4433 4455
CONECT 4432 4431
CONECT 4433 4432 4434 4456
CONECT 4433 4434
CONECT 4434 4433 4435
CONECT 4434 4433
CONECT 4435 4430 4434 4457
CONECT 4435 4430
CONECT 4436 4425 4429
CONECT 4436 4425
CONECT 4397 4389
CONECT    8   15
CONECT 4437 4399
CONECT 4438 4399
CONECT 4439 4399
CONECT 4440 4401
CONECT 4441 4402
CONECT 4442 4404
CONECT 4443 4411
CONECT 4444 4411
CONECT 4445 4411
CONECT 4446 4416
CONECT 4447 4417
CONECT 4448 4420
CONECT 4449 4421
CONECT 4450 4422
CONECT 4451 4424
CONECT 4452 4427
CONECT 4453 4428
CONECT 4454 4431
CONECT 4455 4432
CONECT 4456 4433
CONECT 4457 4435
CONECT   15    8
END   



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