CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 2410311535072900400

Job options:

ID        	=	 2410311535072900400
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

ATOM      1  N   PRO A   1     -27.070  29.560  23.307  1.00 64.58           N  
ANISOU    1  N   PRO A   1     6986   9930   7620   2937  -2295  -2016       N  
ATOM      2  CA  PRO A   1     -27.302  30.181  24.607  1.00 67.49           C  
ANISOU    2  CA  PRO A   1     7087  10627   7929   3407  -2350  -2459       C  
ATOM      3  C   PRO A   1     -25.991  30.328  25.389  1.00 64.24           C  
ANISOU    3  C   PRO A   1     7002   9814   7591   3188  -2183  -2335       C  
ATOM      4  O   PRO A   1     -24.934  29.977  24.878  1.00 59.67           O  
ANISOU    4  O   PRO A   1     6827   8738   7107   2708  -2045  -1926       O  
ATOM      5  CB  PRO A   1     -28.222  29.171  25.298  1.00 68.68           C  
ANISOU    5  CB  PRO A   1     6483  11806   7805   3249  -1986  -2601       C  
ATOM      6  CG  PRO A   1     -27.728  27.838  24.789  1.00 63.64           C  
ANISOU    6  CG  PRO A   1     5941  11087   7151   2485  -1614  -2088       C  
ATOM      7  CD  PRO A   1     -27.281  28.095  23.349  1.00 62.10           C  
ANISOU    7  CD  PRO A   1     6295  10144   7155   2388  -1839  -1798       C  
ATOM      8  N   GLN A   2     -26.065  30.864  26.604  1.00 66.39           N  
ANISOU    8  N   GLN A   2     7069  10360   7796   3556  -2209  -2726       N  
ATOM      9  CA  GLN A   2     -24.899  30.921  27.475  1.00 63.99           C  
ANISOU    9  CA  GLN A   2     6985   9809   7518   3329  -2021  -2631       C  
ATOM     10  C   GLN A   2     -24.957  29.741  28.435  1.00 61.69           C  
ANISOU   10  C   GLN A   2     6178  10253   7008   2936  -1522  -2556       C  
ATOM     11  O   GLN A   2     -26.005  29.432  28.997  1.00 64.83           O  
ANISOU   11  O   GLN A   2     5981  11478   7174   3076  -1421  -2837       O  
ATOM     12  CB  GLN A   2     -24.859  32.240  28.259  1.00 68.36           C  
ANISOU   12  CB  GLN A   2     7692  10167   8114   3929  -2382  -3102       C  
ATOM     13  CG  GLN A   2     -23.570  32.481  29.047  1.00 67.03           C  
ANISOU   13  CG  GLN A   2     7846   9638   7983   3688  -2264  -2994       C  
ATOM     14  CD  GLN A   2     -23.771  33.459  30.203  1.00 73.66           C  
ANISOU   14  CD  GLN A   2     8595  10628   8765   4260  -2489  -3568       C  
ATOM     15  OE1 GLN A   2     -24.495  33.173  31.164  1.00 76.74           O  
ANISOU   15  OE1 GLN A   2     8360  11868   8931   4474  -2290  -3943       O  
ATOM     16  NE2 GLN A   2     -23.128  34.619  30.113  1.00 75.54           N  
ANISOU   16  NE2 GLN A   2     9462  10071   9168   4470  -2926  -3651       N  
ATOM     17  N   ILE A   3     -23.831  29.067  28.619  1.00 56.86           N  
ANISOU   17  N   ILE A   3     5787   9379   6437   2418  -1240  -2174       N  
ATOM     18  CA  ILE A   3     -23.817  27.960  29.574  1.00 55.12           C  
ANISOU   18  CA  ILE A   3     5178   9754   6012   2023   -854  -2055       C  
ATOM     19  C   ILE A   3     -22.669  28.004  30.597  1.00 52.03           C  
ANISOU   19  C   ILE A   3     4940   9212   5618   1864   -708  -1981       C  
ATOM     20  O   ILE A   3     -21.506  28.226  30.258  1.00 49.15           O  
ANISOU   20  O   ILE A   3     5032   8210   5433   1727   -742  -1763       O  
ATOM     21  CB  ILE A   3     -23.974  26.566  28.902  1.00 52.46           C  
ANISOU   21  CB  ILE A   3     4771   9521   5639   1483   -632  -1654       C  
ATOM     22  CG1 ILE A   3     -22.642  25.970  28.523  1.00 48.48           C  
ANISOU   22  CG1 ILE A   3     4698   8418   5304   1087   -504  -1253       C  
ATOM     23  CG2 ILE A   3     -24.878  26.644  27.679  1.00 55.72           C  
ANISOU   23  CG2 ILE A   3     5154   9920   6096   1616   -813  -1683       C  
ATOM     24  CD1 ILE A   3     -22.781  24.588  27.964  1.00 48.12           C  
ANISOU   24  CD1 ILE A   3     4621   8433   5230    622   -343   -934       C  
ATOM     25  N   THR A   4     -23.053  27.839  31.860  1.00 52.64           N  
ANISOU   25  N   THR A   4     4586   9974   5441   1876   -557  -2193       N  
ATOM     26  CA  THR A   4     -22.119  27.703  32.970  1.00 49.37           C  
ANISOU   26  CA  THR A   4     4215   9590   4953   1670   -392  -2112       C  
ATOM     27  C   THR A   4     -21.493  26.310  32.956  1.00 44.09           C  
ANISOU   27  C   THR A   4     3621   8859   4273   1057   -145  -1599       C  
ATOM     28  O   THR A   4     -21.907  25.434  32.200  1.00 42.62           O  
ANISOU   28  O   THR A   4     3411   8683   4102    791    -94  -1359       O  
ATOM     29  CB  THR A   4     -22.838  27.810  34.299  1.00 53.80           C  
ANISOU   29  CB  THR A   4     4233  11039   5169   1790   -297  -2476       C  
ATOM     30  OG1 THR A   4     -23.963  26.922  34.275  1.00 56.28           O  
ANISOU   30  OG1 THR A   4     4060  12105   5218   1534   -157  -2431       O  
ATOM     31  CG2 THR A   4     -23.287  29.238  34.576  1.00 58.60           C  
ANISOU   31  CG2 THR A   4     4779  11704   5784   2495   -580  -3093       C  
ATOM     32  N   LEU A   5     -20.536  26.093  33.848  1.00 40.14           N  
ANISOU   32  N   LEU A   5     3208   8312   3732    854    -29  -1461       N  
ATOM     33  CA  LEU A   5     -19.709  24.893  33.770  1.00 35.36           C  
ANISOU   33  CA  LEU A   5     2791   7459   3185    387    102  -1002       C  
ATOM     34  C   LEU A   5     -19.730  24.042  35.043  1.00 36.72           C  
ANISOU   34  C   LEU A   5     2715   8160   3075     16    241   -840       C  
ATOM     35  O   LEU A   5     -18.847  23.228  35.267  1.00 34.18           O  
ANISOU   35  O   LEU A   5     2599   7583   2806   -280    276   -507       O  
ATOM     36  CB  LEU A   5     -18.283  25.278  33.350  1.00 31.52           C  
ANISOU   36  CB  LEU A   5     2739   6284   2951    434     50   -884       C  
ATOM     37  CG  LEU A   5     -18.094  25.813  31.903  1.00 26.77           C  
ANISOU   37  CG  LEU A   5     2456   5132   2585    583    -92   -884       C  
ATOM     38  CD1 LEU A   5     -16.711  26.453  31.694  1.00 23.04           C  
ANISOU   38  CD1 LEU A   5     2339   4170   2247    579   -154   -831       C  
ATOM     39  CD2 LEU A   5     -18.350  24.724  30.846  1.00 21.85           C  
ANISOU   39  CD2 LEU A   5     1875   4389   2036    342    -44   -633       C  
ATOM     40  N   TRP A   6     -20.769  24.232  35.862  1.00 40.32           N  
ANISOU   40  N   TRP A   6     2713   9404   3202     35    291  -1092       N  
ATOM     41  CA  TRP A   6     -20.977  23.432  37.064  1.00 42.60           C  
ANISOU   41  CA  TRP A   6     2722  10345   3120   -421    407   -921       C  
ATOM     42  C   TRP A   6     -21.244  21.973  36.709  1.00 42.85           C  
ANISOU   42  C   TRP A   6     2837  10356   3087   -996    408   -447       C  
ATOM     43  O   TRP A   6     -20.910  21.065  37.468  1.00 44.48           O  
ANISOU   43  O   TRP A   6     3104  10682   3115  -1471    410    -98       O  
ATOM     44  CB  TRP A   6     -22.120  24.024  37.878  1.00 46.65           C  
ANISOU   44  CB  TRP A   6     2649  11842   3235   -270    465  -1371       C  
ATOM     45  CG  TRP A   6     -21.844  25.439  38.211  1.00 45.08           C  
ANISOU   45  CG  TRP A   6     2447  11555   3126    340    388  -1877       C  
ATOM     46  CD1 TRP A   6     -22.277  26.534  37.533  1.00 46.24           C  
ANISOU   46  CD1 TRP A   6     2616  11492   3460    948    218  -2312       C  
ATOM     47  CD2 TRP A   6     -21.054  25.921  39.298  1.00 43.20           C  
ANISOU   47  CD2 TRP A   6     2244  11372   2797    396    418  -1997       C  
ATOM     48  NE1 TRP A   6     -21.808  27.677  38.132  1.00 47.50           N  
ANISOU   48  NE1 TRP A   6     2867  11519   3661   1380    111  -2705       N  
ATOM     49  CE2 TRP A   6     -21.054  27.328  39.219  1.00 44.86           C  
ANISOU   49  CE2 TRP A   6     2521  11373   3152   1043    255  -2532       C  
ATOM     50  CE3 TRP A   6     -20.348  25.300  40.336  1.00 43.69           C  
ANISOU   50  CE3 TRP A   6     2318  11622   2662    -45    525  -1698       C  
ATOM     51  CZ2 TRP A   6     -20.377  28.131  40.141  1.00 46.54           C  
ANISOU   51  CZ2 TRP A   6     2804  11567   3312   1242    218  -2799       C  
ATOM     52  CZ3 TRP A   6     -19.664  26.104  41.252  1.00 43.91           C  
ANISOU   52  CZ3 TRP A   6     2371  11684   2631    161    518  -1954       C  
ATOM     53  CH2 TRP A   6     -19.681  27.502  41.141  1.00 44.82           C  
ANISOU   53  CH2 TRP A   6     2548  11592   2890    788    376  -2507       C  
ATOM     54  N   GLN A   7     -21.804  21.757  35.523  1.00 41.35           N  
ANISOU   54  N   GLN A   7     2713   9946   3051   -955    356   -424       N  
ATOM     55  CA  GLN A   7     -22.004  20.426  34.988  1.00 41.00           C  
ANISOU   55  CA  GLN A   7     2848   9723   3006  -1456    304    -11       C  
ATOM     56  C   GLN A   7     -21.275  20.335  33.654  1.00 36.58           C  
ANISOU   56  C   GLN A   7     2742   8274   2884  -1240    222     79       C  
ATOM     57  O   GLN A   7     -20.936  21.356  33.060  1.00 34.53           O  
ANISOU   57  O   GLN A   7     2571   7696   2851   -772    212   -175       O  
ATOM     58  CB  GLN A   7     -23.492  20.183  34.776  1.00 44.54           C  
ANISOU   58  CB  GLN A   7     2879  10893   3150  -1681    326    -99       C  
ATOM     59  CG  GLN A   7     -24.323  20.367  36.015  1.00 51.52           C  
ANISOU   59  CG  GLN A   7     3191  12864   3521  -1885    429   -281       C  
ATOM     60  CD  GLN A   7     -24.478  19.097  36.825  1.00 58.93           C  
ANISOU   60  CD  GLN A   7     4123  14187   4079  -2719    408    186       C  
ATOM     61  OE1 GLN A   7     -23.597  18.737  37.624  1.00 58.45           O  
ANISOU   61  OE1 GLN A   7     4312  13896   4001  -2935    371    450       O  
ATOM     62  NE2 GLN A   7     -25.635  18.424  36.659  1.00 62.83           N  
ANISOU   62  NE2 GLN A   7     4329  15320   4223  -3237    397    302       N  
ATOM     63  N   ARG A   8     -20.994  19.125  33.191  1.00 35.82           N  
ANISOU   63  N   ARG A   8     2954   7773   2882  -1594    130    429       N  
ATOM     64  CA  ARG A   8     -20.424  18.936  31.818  1.00 32.87           C  
ANISOU   64  CA  ARG A   8     2942   6682   2863  -1410     60    457       C  
ATOM     65  C   ARG A   8     -21.302  19.611  30.767  1.00 31.80           C  
ANISOU   65  C   ARG A   8     2653   6655   2773  -1174     77    218       C  
ATOM     66  O   ARG A   8     -22.519  19.469  30.819  1.00 33.91           O  
ANISOU   66  O   ARG A   8     2610   7470   2805  -1353     86    175       O  
ATOM     67  CB  ARG A   8     -20.351  17.457  31.493  1.00 33.95           C  
ANISOU   67  CB  ARG A   8     3379   6489   3030  -1829    -88    791       C  
ATOM     68  CG  ARG A   8     -19.144  16.793  32.117  1.00 36.68           C  
ANISOU   68  CG  ARG A   8     4035   6424   3477  -1892   -204   1004       C  
ATOM     69  CD  ARG A   8     -19.279  15.294  32.126  1.00 44.84           C  
ANISOU   69  CD  ARG A   8     5384   7187   4466  -2354   -452   1347       C  
ATOM     70  NE  ARG A   8     -17.959  14.685  32.270  1.00 49.47           N  
ANISOU   70  NE  ARG A   8     6345   7175   5275  -2204   -636   1456       N  
ATOM     71  CZ  ARG A   8     -17.708  13.504  32.834  1.00 55.48           C  
ANISOU   71  CZ  ARG A   8     7440   7649   5990  -2531   -941   1779       C  
ATOM     72  NH1 ARG A   8     -18.700  12.758  33.336  1.00 61.52           N  
ANISOU   72  NH1 ARG A   8     8244   8677   6453  -3156  -1092   2091       N  
ATOM     73  NH2 ARG A   8     -16.449  13.063  32.886  1.00 54.74           N  
ANISOU   73  NH2 ARG A   8     7650   7018   6132  -2245  -1134   1790       N  
ATOM     74  N   PRO A   9     -20.689  20.393  29.856  1.00 29.03           N  
ANISOU   74  N   PRO A   9     2497   5849   2682   -796     60     64       N  
ATOM     75  CA  PRO A   9     -21.406  21.123  28.820  1.00 29.06           C  
ANISOU   75  CA  PRO A   9     2430   5867   2743   -549      9   -133       C  
ATOM     76  C   PRO A   9     -21.819  20.168  27.676  1.00 29.89           C  
ANISOU   76  C   PRO A   9     2664   5795   2900   -804    -40     23       C  
ATOM     77  O   PRO A   9     -21.250  20.199  26.572  1.00 26.97           O  
ANISOU   77  O   PRO A   9     2561   4964   2722   -714    -80     31       O  
ATOM     78  CB  PRO A   9     -20.391  22.190  28.379  1.00 26.30           C  
ANISOU   78  CB  PRO A   9     2336   5053   2606   -203    -34   -257       C  
ATOM     79  CG  PRO A   9     -19.053  21.549  28.578  1.00 25.31           C  
ANISOU   79  CG  PRO A   9     2461   4567   2590   -351     17    -73       C  
ATOM     80  CD  PRO A   9     -19.231  20.653  29.810  1.00 25.41           C  
ANISOU   80  CD  PRO A   9     2331   4890   2434   -627     62     86       C  
ATOM     81  N   LEU A  10     -22.799  19.319  27.975  1.00 27.90           N  
ANISOU   81  N   LEU A  10     2542   5107   2951   -406    170  -1251       N  
ATOM     82  CA  LEU A  10     -23.303  18.315  27.015  1.00 28.25           C  
ANISOU   82  CA  LEU A  10     2678   5006   3049   -403    137  -1017       C  
ATOM     83  C   LEU A  10     -24.415  18.909  26.184  1.00 28.19           C  
ANISOU   83  C   LEU A  10     2682   4848   3182   -234     85  -1177       C  
ATOM     84  O   LEU A  10     -25.273  19.611  26.718  1.00 31.04           O  
ANISOU   84  O   LEU A  10     2868   5392   3535   -156     84  -1460       O  
ATOM     85  CB  LEU A  10     -23.840  17.076  27.745  1.00 29.68           C  
ANISOU   85  CB  LEU A  10     2705   5523   3048   -591    153   -840       C  
ATOM     86  CG  LEU A  10     -22.733  16.217  28.361  1.00 31.61           C  
ANISOU   86  CG  LEU A  10     2964   5838   3209   -766    142   -571       C  
ATOM     87  CD1 LEU A  10     -23.336  15.275  29.406  1.00 36.30           C  
ANISOU   87  CD1 LEU A  10     3353   6848   3592  -1012    119   -401       C  
ATOM     88  CD2 LEU A  10     -21.986  15.440  27.281  1.00 32.97           C  
ANISOU   88  CD2 LEU A  10     3345   5626   3557   -713     82   -348       C  
ATOM     89  N   VAL A  11     -24.396  18.647  24.884  1.00 25.63           N  
ANISOU   89  N   VAL A  11     2535   4220   2983   -176     31  -1021       N  
ATOM     90  CA  VAL A  11     -25.418  19.181  23.991  1.00 25.92           C  
ANISOU   90  CA  VAL A  11     2590   4104   3156    -32    -48  -1118       C  
ATOM     91  C   VAL A  11     -25.907  18.053  23.088  1.00 24.51           C  
ANISOU   91  C   VAL A  11     2474   3880   2960    -80    -60   -911       C  
ATOM     92  O   VAL A  11     -25.243  17.027  22.929  1.00 23.12           O  
ANISOU   92  O   VAL A  11     2375   3677   2734   -187    -33   -715       O  
ATOM     93  CB  VAL A  11     -24.893  20.380  23.100  1.00 25.83           C  
ANISOU   93  CB  VAL A  11     2745   3731   3338     76   -155  -1147       C  
ATOM     94  CG1 VAL A  11     -24.566  21.608  23.939  1.00 30.96           C  
ANISOU   94  CG1 VAL A  11     3334   4359   4070    139   -191  -1398       C  
ATOM     95  CG2 VAL A  11     -23.690  19.958  22.245  1.00 26.54           C  
ANISOU   95  CG2 VAL A  11     3026   3650   3406    -18   -145   -901       C  
ATOM     96  N  ATHR A  12     -27.074  18.246  22.501  0.50 25.02           N  
ANISOU   96  N  ATHR A  12     2492   3929   3087     10   -118   -979       N  
ATOM     97  N  BTHR A  12     -27.059  18.258  22.470  0.50 25.19           N  
ANISOU   97  N  BTHR A  12     2518   3941   3112     11   -120   -977       N  
ATOM     98  CA ATHR A  12     -27.579  17.295  21.544  0.50 24.03           C  
ANISOU   98  CA ATHR A  12     2429   3749   2953    -36   -143   -814       C  
ATOM     99  CA BTHR A  12     -27.598  17.275  21.554  0.50 24.46           C  
ANISOU   99  CA BTHR A  12     2480   3808   3005    -38   -143   -814       C  
ATOM    100  C  ATHR A  12     -26.967  17.630  20.184  0.50 23.96           C  
ANISOU  100  C  ATHR A  12     2617   3446   3040      5   -206   -714       C  
ATOM    101  C  BTHR A  12     -27.136  17.603  20.132  0.50 24.32           C  
ANISOU  101  C  BTHR A  12     2653   3500   3088     10   -212   -718       C  
ATOM    102  O  ATHR A  12     -26.779  18.808  19.842  0.50 23.99           O  
ANISOU  102  O  ATHR A  12     2674   3287   3152     93   -283   -772       O  
ATOM    103  O  BTHR A  12     -27.230  18.762  19.691  0.50 24.67           O  
ANISOU  103  O  BTHR A  12     2735   3391   3249    113   -303   -783       O  
ATOM    104  CB ATHR A  12     -29.107  17.325  21.503  0.50 25.90           C  
ANISOU  104  CB ATHR A  12     2505   4151   3184     17   -180   -919       C  
ATOM    105  CB BTHR A  12     -29.122  17.236  21.634  0.50 26.38           C  
ANISOU  105  CB BTHR A  12     2549   4247   3227      2   -170   -918       C  
ATOM    106  OG1ATHR A  12     -29.604  17.072  22.821  0.50 26.68           O  
ANISOU  106  OG1ATHR A  12     2379   4622   3137    -63   -112  -1023       O  
ATOM    107  OG1BTHR A  12     -29.648  18.530  21.316  0.50 27.88           O  
ANISOU  107  OG1BTHR A  12     2700   4325   3569    193   -260  -1107       O  
ATOM    108  CG2ATHR A  12     -29.654  16.266  20.555  0.50 24.38           C  
ANISOU  108  CG2ATHR A  12     2372   3921   2970    -61   -210   -751       C  
ATOM    109  CG2BTHR A  12     -29.553  16.864  23.039  0.50 27.30           C  
ANISOU  109  CG2BTHR A  12     2437   4758   3176   -106    -96  -1000       C  
ATOM    110  N   ILE A  13     -26.618  16.586  19.435  1.00 22.82           N  
ANISOU  110  N   ILE A  13     2565   3250   2857    -78   -191   -569       N  
ATOM    111  CA  ILE A  13     -26.111  16.755  18.079  1.00 22.53           C  
ANISOU  111  CA  ILE A  13     2666   3054   2842    -81   -235   -493       C  
ATOM    112  C   ILE A  13     -26.886  15.814  17.162  1.00 23.68           C  
ANISOU  112  C   ILE A  13     2813   3224   2960   -120   -262   -448       C  
ATOM    113  O   ILE A  13     -27.410  14.767  17.611  1.00 23.35           O  
ANISOU  113  O   ILE A  13     2706   3268   2898   -173   -242   -438       O  
ATOM    114  CB  ILE A  13     -24.591  16.490  17.936  1.00 21.37           C  
ANISOU  114  CB  ILE A  13     2604   2858   2656   -141   -181   -439       C  
ATOM    115  CG1 ILE A  13     -24.282  14.988  18.090  1.00 19.32           C  
ANISOU  115  CG1 ILE A  13     2326   2635   2380   -195   -138   -408       C  
ATOM    116  CG2 ILE A  13     -23.775  17.387  18.914  1.00 21.68           C  
ANISOU  116  CG2 ILE A  13     2638   2889   2710   -129   -155   -479       C  
ATOM    117  CD1 ILE A  13     -22.784  14.594  17.912  1.00 22.25           C  
ANISOU  117  CD1 ILE A  13     2738   2975   2741   -216    -98   -401       C  
ATOM    118  N   LYS A  14     -26.996  16.221  15.906  1.00 23.34           N  
ANISOU  118  N   LYS A  14     2836   3122   2910   -122   -329   -405       N  
ATOM    119  CA  LYS A  14     -27.602  15.375  14.893  1.00 24.44           C  
ANISOU  119  CA  LYS A  14     2979   3307   3000   -176   -355   -385       C  
ATOM    120  C   LYS A  14     -26.563  15.261  13.793  1.00 24.58           C  
ANISOU  120  C   LYS A  14     3076   3330   2934   -249   -343   -363       C  
ATOM    121  O   LYS A  14     -26.033  16.265  13.336  1.00 24.44           O  
ANISOU  121  O   LYS A  14     3105   3296   2884   -274   -386   -292       O  
ATOM    122  CB  LYS A  14     -28.906  15.968  14.381  1.00 25.04           C  
ANISOU  122  CB  LYS A  14     3004   3408   3102   -133   -458   -364       C  
ATOM    123  CG  LYS A  14     -29.629  15.004  13.434  1.00 26.91           C  
ANISOU  123  CG  LYS A  14     3228   3728   3269   -210   -481   -355       C  
ATOM    124  CD  LYS A  14     -30.887  15.596  12.837  1.00 29.77           C  
ANISOU  124  CD  LYS A  14     3526   4136   3648   -173   -598   -313       C  
ATOM    125  CE  LYS A  14     -31.556  14.549  11.954  1.00 32.85           C  
ANISOU  125  CE  LYS A  14     3899   4634   3949   -276   -611   -318       C  
ATOM    126  NZ  LYS A  14     -32.816  15.060  11.369  1.00 34.98           N  
ANISOU  126  NZ  LYS A  14     4087   4979   4224   -249   -733   -263       N  
ATOM    127  N   ILE A  15     -26.229  14.024  13.442  1.00 25.78           N  
ANISOU  127  N   ILE A  15     3224   3515   3058   -292   -298   -439       N  
ATOM    128  CA  ILE A  15     -25.191  13.706  12.456  1.00 27.15           C  
ANISOU  128  CA  ILE A  15     3413   3771   3133   -350   -264   -509       C  
ATOM    129  C   ILE A  15     -25.529  12.372  11.790  1.00 28.95           C  
ANISOU  129  C   ILE A  15     3605   4028   3366   -375   -274   -652       C  
ATOM    130  O   ILE A  15     -26.002  11.424  12.437  1.00 28.68           O  
ANISOU  130  O   ILE A  15     3557   3878   3461   -351   -297   -682       O  
ATOM    131  CB  ILE A  15     -23.761  13.695  13.078  1.00 27.14           C  
ANISOU  131  CB  ILE A  15     3415   3749   3150   -325   -192   -545       C  
ATOM    132  CG1 ILE A  15     -22.715  13.368  11.998  1.00 28.93           C  
ANISOU  132  CG1 ILE A  15     3601   4143   3249   -381   -150   -668       C  
ATOM    133  CG2 ILE A  15     -23.690  12.745  14.281  1.00 27.16           C  
ANISOU  133  CG2 ILE A  15     3392   3627   3300   -265   -178   -573       C  
ATOM    134  CD1 ILE A  15     -21.262  13.459  12.455  1.00 28.26           C  
ANISOU  134  CD1 ILE A  15     3488   4095   3157   -361    -83   -710       C  
ATOM    135  N   GLY A  16     -25.376  12.329  10.468  1.00 30.17           N  
ANISOU  135  N   GLY A  16     3735   4356   3372   -453   -278   -731       N  
ATOM    136  CA  GLY A  16     -25.717  11.135   9.697  1.00 31.21           C  
ANISOU  136  CA  GLY A  16     3819   4537   3502   -481   -297   -927       C  
ATOM    137  C   GLY A  16     -27.102  10.593   9.995  1.00 30.92           C  
ANISOU  137  C   GLY A  16     3792   4387   3569   -486   -369   -881       C  
ATOM    138  O   GLY A  16     -27.287   9.368  10.041  1.00 32.09           O  
ANISOU  138  O   GLY A  16     3925   4427   3842   -484   -410  -1021       O  
ATOM    139  N   GLY A  17     -28.075  11.493  10.159  1.00 29.28           N  
ANISOU  139  N   GLY A  17     3595   4205   3325   -496   -409   -696       N  
ATOM    140  CA  GLY A  17     -29.454  11.139  10.520  1.00 28.39           C  
ANISOU  140  CA  GLY A  17     3453   4055   3278   -508   -470   -639       C  
ATOM    141  C   GLY A  17     -29.690  10.680  11.971  1.00 26.56           C  
ANISOU  141  C   GLY A  17     3207   3692   3193   -476   -467   -586       C  
ATOM    142  O   GLY A  17     -30.814  10.337  12.332  1.00 26.97           O  
ANISOU  142  O   GLY A  17     3205   3773   3268   -522   -515   -534       O  
ATOM    143  N   GLN A  18     -28.643  10.682  12.796  1.00 24.41           N  
ANISOU  143  N   GLN A  18     2961   3326   2989   -426   -416   -583       N  
ATOM    144  CA  GLN A  18     -28.704  10.119  14.152  1.00 23.40           C  
ANISOU  144  CA  GLN A  18     2804   3117   2969   -445   -430   -507       C  
ATOM    145  C   GLN A  18     -28.580  11.208  15.193  1.00 21.73           C  
ANISOU  145  C   GLN A  18     2562   2971   2724   -389   -372   -425       C  
ATOM    146  O   GLN A  18     -27.871  12.199  14.977  1.00 21.67           O  
ANISOU  146  O   GLN A  18     2593   2964   2676   -319   -327   -441       O  
ATOM    147  CB  GLN A  18     -27.561   9.130  14.363  1.00 24.11           C  
ANISOU  147  CB  GLN A  18     2926   3044   3191   -438   -451   -571       C  
ATOM    148  CG  GLN A  18     -27.577   7.995  13.367  1.00 28.43           C  
ANISOU  148  CG  GLN A  18     3485   3495   3822   -464   -528   -737       C  
ATOM    149  CD  GLN A  18     -26.385   7.119  13.529  1.00 32.69           C  
ANISOU  149  CD  GLN A  18     4029   3850   4543   -403   -576   -854       C  
ATOM    150  OE1 GLN A  18     -26.188   6.543  14.600  1.00 34.96           O  
ANISOU  150  OE1 GLN A  18     4313   3982   4988   -429   -659   -723       O  
ATOM    151  NE2 GLN A  18     -25.559   7.011  12.475  1.00 33.94           N  
ANISOU  151  NE2 GLN A  18     4167   4056   4674   -329   -537  -1104       N  
ATOM    152  N   LEU A  19     -29.192  10.973  16.353  1.00 20.42           N  
ANISOU  152  N   LEU A  19     2313   2879   2568   -445   -385   -345       N  
ATOM    153  CA  LEU A  19     -29.157  11.943  17.444  1.00 19.59           C  
ANISOU  153  CA  LEU A  19     2136   2892   2417   -398   -328   -332       C  
ATOM    154  C   LEU A  19     -28.240  11.416  18.513  1.00 19.62           C  
ANISOU  154  C   LEU A  19     2134   2871   2449   -458   -314   -259       C  
ATOM    155  O   LEU A  19     -28.403  10.273  18.944  1.00 19.69           O  
ANISOU  155  O   LEU A  19     2117   2862   2502   -589   -386   -152       O  
ATOM    156  CB  LEU A  19     -30.555  12.155  18.051  1.00 19.59           C  
ANISOU  156  CB  LEU A  19     1977   3117   2347   -434   -341   -332       C  
ATOM    157  CG  LEU A  19     -31.666  12.515  17.067  1.00 23.70           C  
ANISOU  157  CG  LEU A  19     2467   3683   2854   -384   -388   -382       C  
ATOM    158  CD1 LEU A  19     -33.032  12.479  17.804  1.00 24.64           C  
ANISOU  158  CD1 LEU A  19     2380   4086   2896   -438   -400   -398       C  
ATOM    159  CD2 LEU A  19     -31.380  13.893  16.423  1.00 25.91           C  
ANISOU  159  CD2 LEU A  19     2801   3870   3174   -221   -398   -448       C  
ATOM    160  N   LYS A  20     -27.320  12.263  18.961  1.00 19.07           N  
ANISOU  160  N   LYS A  20     2084   2799   2364   -385   -248   -293       N  
ATOM    161  CA  LYS A  20     -26.319  11.877  19.955  1.00 20.67           C  
ANISOU  161  CA  LYS A  20     2275   2996   2582   -438   -238   -217       C  
ATOM    162  C   LYS A  20     -26.147  13.006  20.950  1.00 20.68           C  
ANISOU  162  C   LYS A  20     2201   3159   2496   -407   -165   -271       C  
ATOM    163  O   LYS A  20     -26.574  14.124  20.707  1.00 21.62           O  
ANISOU  163  O   LYS A  20     2308   3308   2600   -308   -140   -393       O  
ATOM    164  CB  LYS A  20     -24.961  11.586  19.279  1.00 20.08           C  
ANISOU  164  CB  LYS A  20     2305   2731   2592   -374   -236   -247       C  
ATOM    165  CG  LYS A  20     -24.999  10.379  18.313  1.00 23.84           C  
ANISOU  165  CG  LYS A  20     2828   3047   3182   -384   -318   -277       C  
ATOM    166  CD  LYS A  20     -23.631  10.111  17.719  1.00 29.46           C  
ANISOU  166  CD  LYS A  20     3582   3646   3966   -301   -307   -379       C  
ATOM    167  CE  LYS A  20     -23.654   8.866  16.823  1.00 35.57           C  
ANISOU  167  CE  LYS A  20     4366   4265   4883   -287   -404   -494       C  
ATOM    168  NZ  LYS A  20     -24.074   7.649  17.577  1.00 39.73           N  
ANISOU  168  NZ  LYS A  20     4871   4637   5588   -377   -562   -362       N  
ATOM    169  N   GLU A  21     -25.515  12.695  22.073  1.00 21.39           N  
ANISOU  169  N   GLU A  21     2233   3344   2549   -496   -158   -185       N  
ATOM    170  CA  GLU A  21     -25.080  13.695  23.052  1.00 23.18           C  
ANISOU  170  CA  GLU A  21     2389   3732   2688   -481    -87   -267       C  
ATOM    171  C   GLU A  21     -23.585  13.849  22.902  1.00 21.22           C  
ANISOU  171  C   GLU A  21     2244   3326   2494   -436    -67   -246       C  
ATOM    172  O   GLU A  21     -22.887  12.838  22.729  1.00 21.69           O  
ANISOU  172  O   GLU A  21     2347   3263   2631   -471   -119   -126       O  
ATOM    173  CB  GLU A  21     -25.354  13.224  24.472  1.00 24.85           C  
ANISOU  173  CB  GLU A  21     2429   4249   2763   -661    -94   -167       C  
ATOM    174  CG  GLU A  21     -26.837  13.218  24.842  1.00 32.97           C  
ANISOU  174  CG  GLU A  21     3286   5571   3671   -738    -92   -219       C  
ATOM    175  CD  GLU A  21     -27.271  14.482  25.549  1.00 41.92           C  
ANISOU  175  CD  GLU A  21     4256   6980   4692   -661     -7   -487       C  
ATOM    176  OE1 GLU A  21     -26.715  15.570  25.274  1.00 44.89           O  
ANISOU  176  OE1 GLU A  21     4711   7187   5158   -490     26   -664       O  
ATOM    177  OE2 GLU A  21     -28.175  14.381  26.405  1.00 47.16           O  
ANISOU  177  OE2 GLU A  21     4691   8050   5179   -787     13   -535       O  
ATOM    178  N   ALA A  22     -23.101  15.090  22.978  1.00 20.15           N  
ANISOU  178  N   ALA A  22     2132   3186   2339   -361    -14   -373       N  
ATOM    179  CA  ALA A  22     -21.673  15.372  22.835  1.00 19.55           C  
ANISOU  179  CA  ALA A  22     2135   3007   2284   -343      9   -355       C  
ATOM    180  C   ALA A  22     -21.236  16.533  23.724  1.00 20.00           C  
ANISOU  180  C   ALA A  22     2149   3168   2283   -348     51   -463       C  
ATOM    181  O   ALA A  22     -22.049  17.411  24.059  1.00 20.66           O  
ANISOU  181  O   ALA A  22     2170   3322   2359   -303     51   -621       O  
ATOM    182  CB  ALA A  22     -21.333  15.667  21.379  1.00 18.75           C  
ANISOU  182  CB  ALA A  22     2162   2721   2243   -271     -3   -380       C  
ATOM    183  N   LEU A  23     -19.953  16.522  24.089  1.00 19.77           N  
ANISOU  183  N   LEU A  23     2135   3148   2229   -392     74   -408       N  
ATOM    184  CA  LEU A  23     -19.369  17.469  25.011  1.00 21.94           C  
ANISOU  184  CA  LEU A  23     2363   3535   2439   -429    107   -503       C  
ATOM    185  C   LEU A  23     -18.795  18.654  24.239  1.00 21.79           C  
ANISOU  185  C   LEU A  23     2464   3327   2487   -380     88   -581       C  
ATOM    186  O   LEU A  23     -17.971  18.468  23.321  1.00 22.77           O  
ANISOU  186  O   LEU A  23     2677   3344   2630   -386     83   -485       O  
ATOM    187  CB  LEU A  23     -18.257  16.751  25.804  1.00 22.77           C  
ANISOU  187  CB  LEU A  23     2410   3764   2478   -527    119   -361       C  
ATOM    188  CG  LEU A  23     -17.593  17.381  27.022  1.00 25.37           C  
ANISOU  188  CG  LEU A  23     2648   4300   2690   -619    154   -418       C  
ATOM    189  CD1 LEU A  23     -18.544  17.410  28.221  1.00 28.96           C  
ANISOU  189  CD1 LEU A  23     2929   5068   3005   -708    173   -500       C  
ATOM    190  CD2 LEU A  23     -16.305  16.597  27.350  1.00 27.03           C  
ANISOU  190  CD2 LEU A  23     2833   4554   2885   -686    134   -228       C  
ATOM    191  N   LEU A  24     -19.226  19.875  24.579  1.00 22.65           N  
ANISOU  191  N   LEU A  24     2560   3406   2641   -342     55   -761       N  
ATOM    192  CA  LEU A  24     -18.538  21.060  24.034  1.00 22.59           C  
ANISOU  192  CA  LEU A  24     2669   3197   2719   -349    -13   -789       C  
ATOM    193  C   LEU A  24     -17.164  21.168  24.696  1.00 23.46           C  
ANISOU  193  C   LEU A  24     2765   3410   2738   -459     34   -754       C  
ATOM    194  O   LEU A  24     -17.052  21.426  25.910  1.00 24.81           O  
ANISOU  194  O   LEU A  24     2832   3750   2847   -496     67   -882       O  
ATOM    195  CB  LEU A  24     -19.347  22.335  24.242  1.00 23.76           C  
ANISOU  195  CB  LEU A  24     2803   3211   3015   -261   -117  -1012       C  
ATOM    196  CG  LEU A  24     -20.783  22.348  23.704  1.00 24.16           C  
ANISOU  196  CG  LEU A  24     2828   3182   3172   -131   -182  -1078       C  
ATOM    197  CD1 LEU A  24     -21.438  23.666  24.107  1.00 27.81           C  
ANISOU  197  CD1 LEU A  24     3234   3507   3827    -10   -310  -1362       C  
ATOM    198  CD2 LEU A  24     -20.803  22.186  22.225  1.00 23.54           C  
ANISOU  198  CD2 LEU A  24     2888   2916   3139   -143   -251   -866       C  
ATOM    199  N   ASP A  25     -16.116  20.996  23.900  1.00 22.43           N  
ANISOU  199  N   ASP A  25     2715   3230   2578   -523     37   -599       N  
ATOM    200  CA  ASP A  25     -14.788  20.763  24.458  1.00 21.52           C  
ANISOU  200  CA  ASP A  25     2553   3264   2360   -617     93   -536       C  
ATOM    201  C   ASP A  25     -13.735  21.745  23.952  1.00 22.11           C  
ANISOU  201  C   ASP A  25     2708   3266   2427   -729     45   -496       C  
ATOM    202  O   ASP A  25     -13.077  21.483  22.943  1.00 20.94           O  
ANISOU  202  O   ASP A  25     2591   3136   2229   -777     51   -375       O  
ATOM    203  CB  ASP A  25     -14.359  19.323  24.155  1.00 22.16           C  
ANISOU  203  CB  ASP A  25     2581   3440   2398   -591    145   -402       C  
ATOM    204  CG  ASP A  25     -13.102  18.907  24.908  1.00 21.90           C  
ANISOU  204  CG  ASP A  25     2456   3577   2287   -656    180   -336       C  
ATOM    205  OD1 ASP A  25     -12.439  19.791  25.469  1.00 23.62           O  
ANISOU  205  OD1 ASP A  25     2668   3858   2448   -747    183   -379       O  
ATOM    206  OD2 ASP A  25     -12.805  17.691  24.975  1.00 23.70           O  
ANISOU  206  OD2 ASP A  25     2611   3860   2535   -613    180   -245       O  
ATOM    207  N   THR A  26     -13.542  22.849  24.673  1.00 22.10           N  
ANISOU  207  N   THR A  26     2718   3219   2462   -792     -8   -612       N  
ATOM    208  CA  THR A  26     -12.579  23.872  24.248  1.00 22.99           C  
ANISOU  208  CA  THR A  26     2916   3237   2583   -943    -92   -549       C  
ATOM    209  C   THR A  26     -11.109  23.379  24.244  1.00 22.78           C  
ANISOU  209  C   THR A  26     2825   3442   2387  -1063     -8   -420       C  
ATOM    210  O   THR A  26     -10.242  23.997  23.588  1.00 23.04           O  
ANISOU  210  O   THR A  26     2908   3472   2374  -1223    -64   -310       O  
ATOM    211  CB  THR A  26     -12.708  25.180  25.071  1.00 25.00           C  
ANISOU  211  CB  THR A  26     3194   3343   2961   -980   -201   -744       C  
ATOM    212  OG1 THR A  26     -12.400  24.934  26.454  1.00 22.69           O  
ANISOU  212  OG1 THR A  26     2770   3292   2561   -990   -102   -889       O  
ATOM    213  CG2 THR A  26     -14.118  25.767  24.966  1.00 25.47           C  
ANISOU  213  CG2 THR A  26     3288   3157   3233   -830   -317   -914       C  
ATOM    214  N   GLY A  27     -10.842  22.273  24.948  1.00 20.49           N  
ANISOU  214  N   GLY A  27     2411   3364   2012  -1000    100   -415       N  
ATOM    215  CA  GLY A  27      -9.501  21.675  24.993  1.00 21.85           C  
ANISOU  215  CA  GLY A  27     2483   3755   2063  -1062    161   -315       C  
ATOM    216  C   GLY A  27      -9.220  20.696  23.856  1.00 22.23           C  
ANISOU  216  C   GLY A  27     2493   3862   2091   -990    197   -237       C  
ATOM    217  O   GLY A  27      -8.118  20.185  23.747  1.00 22.28           O  
ANISOU  217  O   GLY A  27     2386   4056   2021  -1007    237   -200       O  
ATOM    218  N   ALA A  28     -10.223  20.435  23.014  1.00 21.20           N  
ANISOU  218  N   ALA A  28     2433   3592   2031   -902    179   -247       N  
ATOM    219  CA  ALA A  28     -10.073  19.551  21.867  1.00 21.53           C  
ANISOU  219  CA  ALA A  28     2429   3701   2051   -837    208   -235       C  
ATOM    220  C   ALA A  28      -9.888  20.390  20.589  1.00 22.96           C  
ANISOU  220  C   ALA A  28     2675   3911   2139   -984    170   -179       C  
ATOM    221  O   ALA A  28     -10.784  21.158  20.227  1.00 22.55           O  
ANISOU  221  O   ALA A  28     2749   3671   2146  -1023     87   -141       O  
ATOM    222  CB  ALA A  28     -11.338  18.685  21.729  1.00 19.69           C  
ANISOU  222  CB  ALA A  28     2221   3328   1932   -683    200   -270       C  
ATOM    223  N   ASP A  29      -8.765  20.213  19.898  1.00 24.55           N  
ANISOU  223  N   ASP A  29     2766   4371   2192  -1072    213   -169       N  
ATOM    224  CA  ASP A  29      -8.554  20.855  18.588  1.00 26.47           C  
ANISOU  224  CA  ASP A  29     3026   4749   2281  -1266    173    -83       C  
ATOM    225  C   ASP A  29      -9.599  20.374  17.581  1.00 27.37           C  
ANISOU  225  C   ASP A  29     3177   4805   2418  -1187    160   -112       C  
ATOM    226  O   ASP A  29     -10.131  21.182  16.807  1.00 28.16           O  
ANISOU  226  O   ASP A  29     3379   4841   2480  -1335     61     19       O  
ATOM    227  CB  ASP A  29      -7.157  20.515  18.030  1.00 27.83           C  
ANISOU  227  CB  ASP A  29     2997   5334   2244  -1364    252   -124       C  
ATOM    228  CG  ASP A  29      -6.034  21.050  18.885  1.00 29.91           C  
ANISOU  228  CG  ASP A  29     3206   5709   2448  -1484    258    -75       C  
ATOM    229  OD1 ASP A  29      -6.288  21.955  19.732  1.00 30.79           O  
ANISOU  229  OD1 ASP A  29     3461   5584   2653  -1560    182      9       O  
ATOM    230  OD2 ASP A  29      -4.882  20.565  18.710  1.00 28.75           O  
ANISOU  230  OD2 ASP A  29     2851   5909   2165  -1497    335   -153       O  
ATOM    231  N   ASP A  30      -9.881  19.063  17.609  1.00 26.52           N  
ANISOU  231  N   ASP A  30     2984   4705   2389   -968    231   -266       N  
ATOM    232  CA AASP A  30     -10.735  18.372  16.629  0.50 27.22           C  
ANISOU  232  CA AASP A  30     3069   4786   2487   -885    232   -344       C  
ATOM    233  CA BASP A  30     -10.803  18.501  16.639  0.50 27.24           C  
ANISOU  233  CA BASP A  30     3090   4771   2491   -900    223   -325       C  
ATOM    234  C   ASP A  30     -11.939  17.692  17.268  1.00 25.42           C  
ANISOU  234  C   ASP A  30     2918   4269   2472   -690    211   -385       C  
ATOM    235  O   ASP A  30     -11.898  17.270  18.426  1.00 25.75           O  
ANISOU  235  O   ASP A  30     2945   4201   2637   -586    218   -396       O  
ATOM    236  CB AASP A  30      -9.953  17.281  15.866  0.50 28.66           C  
ANISOU  236  CB AASP A  30     3044   5268   2580   -810    313   -551       C  
ATOM    237  CB BASP A  30     -10.047  17.720  15.552  0.50 28.92           C  
ANISOU  237  CB BASP A  30     3109   5335   2543   -903    296   -489       C  
ATOM    238  CG AASP A  30      -8.479  17.585  15.738  0.50 30.56           C  
ANISOU  238  CG AASP A  30     3121   5859   2632   -940    366   -575       C  
ATOM    239  CG BASP A  30      -9.044  18.587  14.799  0.50 31.48           C  
ANISOU  239  CG BASP A  30     3349   6024   2589  -1179    304   -400       C  
ATOM    240  OD1AASP A  30      -8.136  18.746  15.430  0.50 34.05           O  
ANISOU  240  OD1AASP A  30     3610   6431   2896  -1202    333   -395       O  
ATOM    241  OD1BASP A  30      -9.433  19.620  14.201  0.50 32.66           O  
ANISOU  241  OD1BASP A  30     3609   6170   2629  -1408    214   -192       O  
ATOM    242  OD2AASP A  30      -7.660  16.659  15.939  0.50 31.31           O  
ANISOU  242  OD2AASP A  30     3028   6095   2773   -785    418   -767       O  
ATOM    243  OD2BASP A  30      -7.854  18.225  14.784  0.50 36.30           O  
ANISOU  243  OD2BASP A  30     3763   6940   3088  -1182    381   -526       O  
ATOM    244  N   THR A  31     -12.998  17.549  16.501  1.00 25.23           N  
ANISOU  244  N   THR A  31     2954   4169   2464   -670    176   -391       N  
ATOM    245  CA  THR A  31     -14.176  16.823  16.930  1.00 23.21           C  
ANISOU  245  CA  THR A  31     2745   3698   2377   -518    154   -429       C  
ATOM    246  C   THR A  31     -13.957  15.320  16.791  1.00 24.09           C  
ANISOU  246  C   THR A  31     2741   3837   2574   -373    180   -589       C  
ATOM    247  O   THR A  31     -13.468  14.859  15.766  1.00 25.49           O  
ANISOU  247  O   THR A  31     2819   4200   2667   -372    209   -732       O  
ATOM    248  CB  THR A  31     -15.321  17.288  16.058  1.00 24.14           C  
ANISOU  248  CB  THR A  31     2952   3749   2471   -567     92   -372       C  
ATOM    249  OG1 THR A  31     -15.563  18.671  16.382  1.00 21.96           O  
ANISOU  249  OG1 THR A  31     2780   3353   2210   -663     13   -234       O  
ATOM    250  CG2 THR A  31     -16.603  16.400  16.245  1.00 20.06           C  
ANISOU  250  CG2 THR A  31     2456   3073   2094   -432     72   -428       C  
ATOM    251  N   VAL A  32     -14.294  14.563  17.826  1.00 22.95           N  
ANISOU  251  N   VAL A  32     2594   3523   2601   -266    147   -574       N  
ATOM    252  CA  VAL A  32     -14.085  13.115  17.786  1.00 24.29           C  
ANISOU  252  CA  VAL A  32     2667   3631   2933   -129    104   -698       C  
ATOM    253  C   VAL A  32     -15.325  12.452  18.345  1.00 23.00           C  
ANISOU  253  C   VAL A  32     2567   3250   2923    -94     24   -618       C  
ATOM    254  O   VAL A  32     -15.701  12.690  19.489  1.00 22.52           O  
ANISOU  254  O   VAL A  32     2538   3135   2882   -139      4   -467       O  
ATOM    255  CB  VAL A  32     -12.921  12.617  18.679  1.00 25.70           C  
ANISOU  255  CB  VAL A  32     2733   3824   3208    -64     79   -693       C  
ATOM    256  CG1 VAL A  32     -12.427  11.243  18.185  1.00 26.92           C  
ANISOU  256  CG1 VAL A  32     2750   3926   3553    103      5   -899       C  
ATOM    257  CG2 VAL A  32     -11.816  13.613  18.731  1.00 26.32           C  
ANISOU  257  CG2 VAL A  32     2769   4122   3108   -157    159   -672       C  
ATOM    258  N   LEU A  33     -15.915  11.581  17.539  1.00 25.80           N  
ANISOU  258  N   LEU A  33     2741   3295   3767   -426    -13   -530       N  
ATOM    259  CA  LEU A  33     -17.106  10.874  17.929  1.00 26.49           C  
ANISOU  259  CA  LEU A  33     2746   3119   4199   -559   -144   -453       C  
ATOM    260  C   LEU A  33     -16.842   9.390  18.097  1.00 29.59           C  
ANISOU  260  C   LEU A  33     3165   3186   4892   -541   -366   -506       C  
ATOM    261  O   LEU A  33     -15.985   8.820  17.404  1.00 29.43           O  
ANISOU  261  O   LEU A  33     3279   3128   4774   -307   -501   -804       O  
ATOM    262  CB  LEU A  33     -18.202  11.100  16.874  1.00 27.82           C  
ANISOU  262  CB  LEU A  33     2890   3260   4420   -590   -336   -578       C  
ATOM    263  CG  LEU A  33     -18.584  12.569  16.616  1.00 26.90           C  
ANISOU  263  CG  LEU A  33     2752   3388   4078   -599   -209   -513       C  
ATOM    264  CD1 LEU A  33     -19.774  12.663  15.650  1.00 27.75           C  
ANISOU  264  CD1 LEU A  33     2806   3445   4290   -639   -440   -598       C  
ATOM    265  CD2 LEU A  33     -18.898  13.301  17.935  1.00 26.08           C  
ANISOU  265  CD2 LEU A  33     2556   3365   3989   -630      1   -279       C  
ATOM    266  N   GLU A  34     -17.598   8.758  18.993  1.00 31.26           N  
ANISOU  266  N   GLU A  34     3218   3189   5469   -752   -436   -185       N  
ATOM    267  CA  GLU A  34     -17.475   7.328  19.194  1.00 36.85           C  
ANISOU  267  CA  GLU A  34     3936   3464   6603   -809   -778   -132       C  
ATOM    268  C   GLU A  34     -17.907   6.608  17.919  1.00 40.87           C  
ANISOU  268  C   GLU A  34     4574   3600   7356   -731  -1291   -512       C  
ATOM    269  O   GLU A  34     -18.474   7.221  16.994  1.00 40.63           O  
ANISOU  269  O   GLU A  34     4571   3714   7154   -686  -1327   -720       O  
ATOM    270  CB  GLU A  34     -18.325   6.870  20.371  1.00 38.98           C  
ANISOU  270  CB  GLU A  34     3913   3663   7234  -1121   -768    469       C  
ATOM    271  CG  GLU A  34     -18.080   7.636  21.662  1.00 38.72           C  
ANISOU  271  CG  GLU A  34     3774   4093   6845  -1098   -289    796       C  
ATOM    272  CD  GLU A  34     -19.132   7.302  22.728  1.00 46.45           C  
ANISOU  272  CD  GLU A  34     4367   5247   8036  -1329   -198   1464       C  
ATOM    273  OE1 GLU A  34     -20.317   7.149  22.371  1.00 49.98           O  
ANISOU  273  OE1 GLU A  34     4545   5653   8791  -1521   -344   1684       O  
ATOM    274  OE2 GLU A  34     -18.779   7.195  23.920  1.00 49.60           O  
ANISOU  274  OE2 GLU A  34     4686   5890   8268  -1309     18   1819       O  
ATOM    275  N   GLU A  35     -17.626   5.313  17.865  1.00 45.69           N  
ANISOU  275  N   GLU A  35     5295   3699   8366   -678  -1761   -631       N  
ATOM    276  CA  GLU A  35     -17.962   4.495  16.713  1.00 51.04           C  
ANISOU  276  CA  GLU A  35     6178   3914   9301   -513  -2415  -1099       C  
ATOM    277  C   GLU A  35     -19.363   4.789  16.147  1.00 52.22           C  
ANISOU  277  C   GLU A  35     6191   3987   9662   -774  -2652  -1008       C  
ATOM    278  O   GLU A  35     -20.365   4.765  16.859  1.00 52.55           O  
ANISOU  278  O   GLU A  35     5891   3949  10125  -1213  -2656   -420       O  
ATOM    279  CB  GLU A  35     -17.804   3.004  17.068  1.00 57.00           C  
ANISOU  279  CB  GLU A  35     7018   3932  10710   -552  -3053  -1067       C  
ATOM    280  CG  GLU A  35     -17.808   2.043  15.870  1.00 65.50           C  
ANISOU  280  CG  GLU A  35     8448   4431  12008   -181  -3879  -1769       C  
ATOM    281  CD  GLU A  35     -16.939   2.547  14.727  1.00 67.27           C  
ANISOU  281  CD  GLU A  35     8951   5185  11424    491  -3656  -2508       C  
ATOM    282  OE1 GLU A  35     -15.731   2.812  14.942  1.00 66.36           O  
ANISOU  282  OE1 GLU A  35     8850   5516  10847    820  -3184  -2600       O  
ATOM    283  OE2 GLU A  35     -17.476   2.699  13.612  1.00 71.02           O  
ANISOU  283  OE2 GLU A  35     9583   5696  11707    684  -3951  -2930       O  
ATOM    284  N   MET A  36     -19.401   5.084  14.857  1.00 53.46           N  
ANISOU  284  N   MET A  36     6574   4261   9476   -464  -2829  -1555       N  
ATOM    285  CA  MET A  36     -20.649   5.211  14.119  1.00 56.87           C  
ANISOU  285  CA  MET A  36     6942   4542  10125   -641  -3214  -1586       C  
ATOM    286  C   MET A  36     -20.326   5.064  12.643  1.00 60.55           C  
ANISOU  286  C   MET A  36     7799   5035  10173   -123  -3600  -2352       C  
ATOM    287  O   MET A  36     -19.163   5.190  12.243  1.00 60.41           O  
ANISOU  287  O   MET A  36     7995   5396   9563    367  -3342  -2739       O  
ATOM    288  CB  MET A  36     -21.308   6.566  14.392  1.00 52.09           C  
ANISOU  288  CB  MET A  36     6046   4483   9264   -867  -2640  -1190       C  
ATOM    289  CG  MET A  36     -20.508   7.770  13.916  1.00 47.26           C  
ANISOU  289  CG  MET A  36     5577   4497   7883   -556  -2109  -1417       C  
ATOM    290  SD  MET A  36     -21.376   9.327  14.151  1.00 43.65           S  
ANISOU  290  SD  MET A  36     4851   4482   7250   -766  -1667  -1037       S  
ATOM    291  CE  MET A  36     -22.924   8.971  13.303  1.00 46.95           C  
ANISOU  291  CE  MET A  36     5149   4587   8103   -951  -2270  -1069       C  
ATOM    292  N   ASN A  37     -21.340   4.786  11.834  1.00 65.61           N  
ANISOU  292  N   ASN A  37     8501   5342  11087   -193  -4230  -2548       N  
ATOM    293  CA  ASN A  37     -21.153   4.814  10.398  1.00 69.65           C  
ANISOU  293  CA  ASN A  37     9385   6032  11048    352  -4565  -3270       C  
ATOM    294  C   ASN A  37     -21.377   6.218   9.881  1.00 65.78           C  
ANISOU  294  C   ASN A  37     8776   6278   9937    353  -4012  -3127       C  
ATOM    295  O   ASN A  37     -22.485   6.767   9.956  1.00 65.03           O  
ANISOU  295  O   ASN A  37     8431   6154  10123    -52  -4030  -2761       O  
ATOM    296  CB  ASN A  37     -22.053   3.807   9.666  1.00 77.28           C  
ANISOU  296  CB  ASN A  37    10564   6234  12566    357  -5666  -3661       C  
ATOM    297  CG  ASN A  37     -21.643   3.600   8.206  1.00 82.80           C  
ANISOU  297  CG  ASN A  37    11761   7125  12573   1134  -6109  -4581       C  
ATOM    298  OD1 ASN A  37     -20.704   4.245   7.710  1.00 80.58           O  
ANISOU  298  OD1 ASN A  37    11585   7670  11363   1649  -5505  -4821       O  
ATOM    299  ND2 ASN A  37     -22.352   2.691   7.510  1.00 90.52           N  
ANISOU  299  ND2 ASN A  37    13025   7374  13995   1239  -7216  -5066       N  
ATOM    300  N   LEU A  38     -20.296   6.816   9.400  1.00 64.35           N  
ANISOU  300  N   LEU A  38     8721   6782   8947    801  -3522  -3336       N  
ATOM    301  CA  LEU A  38     -20.406   7.990   8.569  1.00 63.16           C  
ANISOU  301  CA  LEU A  38     8540   7292   8166    905  -3210  -3278       C  
ATOM    302  C   LEU A  38     -20.227   7.543   7.135  1.00 70.09           C  
ANISOU  302  C   LEU A  38     9772   8391   8466   1540  -3680  -3960       C  
ATOM    303  O   LEU A  38     -19.319   6.760   6.823  1.00 74.11           O  
ANISOU  303  O   LEU A  38    10517   8983   8660   2112  -3823  -4458       O  
ATOM    304  CB  LEU A  38     -19.393   9.068   8.941  1.00 58.16           C  
ANISOU  304  CB  LEU A  38     7727   7331   7039    911  -2410  -2893       C  
ATOM    305  CG  LEU A  38     -19.749   9.949  10.134  1.00 51.79           C  
ANISOU  305  CG  LEU A  38     6619   6455   6604    370  -1975  -2272       C  
ATOM    306  CD1 LEU A  38     -18.764  11.085  10.223  1.00 50.35           C  
ANISOU  306  CD1 LEU A  38     6328   6867   5936    410  -1408  -1963       C  
ATOM    307  CD2 LEU A  38     -21.156  10.502  10.029  1.00 50.92           C  
ANISOU  307  CD2 LEU A  38     6367   6178   6801     42  -2158  -2062       C  
ATOM    308  N   PRO A  39     -21.097   8.033   6.248  1.00 72.27           N  
ANISOU  308  N   PRO A  39    10096   8808   8557   1520  -3948  -4018       N  
ATOM    309  CA  PRO A  39     -20.985   7.520   4.899  1.00 79.75           C  
ANISOU  309  CA  PRO A  39    11426   9976   8898   2199  -4483  -4730       C  
ATOM    310  C   PRO A  39     -19.866   8.278   4.189  1.00 80.10           C  
ANISOU  310  C   PRO A  39    11445  11134   7855   2720  -3850  -4691       C  
ATOM    311  O   PRO A  39     -19.555   9.419   4.574  1.00 74.72           O  
ANISOU  311  O   PRO A  39    10438  10920   7031   2373  -3158  -4022       O  
ATOM    312  CB  PRO A  39     -22.363   7.807   4.289  1.00 81.54           C  
ANISOU  312  CB  PRO A  39    11669   9954   9361   1924  -5016  -4713       C  
ATOM    313  CG  PRO A  39     -22.982   8.878   5.136  1.00 74.22           C  
ANISOU  313  CG  PRO A  39    10300   9030   8871   1214  -4491  -3911       C  
ATOM    314  CD  PRO A  39     -22.133   9.077   6.374  1.00 68.98           C  
ANISOU  314  CD  PRO A  39     9408   8429   8372   1001  -3794  -3497       C  
ATOM    315  N   GLY A  40     -19.234   7.626   3.213  1.00 87.03           N  
ANISOU  315  N   GLY A  40    12634  12435   7997   3569  -4120  -5371       N  
ATOM    316  CA  GLY A  40     -18.242   8.290   2.370  1.00 89.25           C  
ANISOU  316  CA  GLY A  40    12810  13962   7137   4141  -3547  -5264       C  
ATOM    317  C   GLY A  40     -16.793   7.887   2.573  1.00 90.51           C  
ANISOU  317  C   GLY A  40    12872  14667   6850   4701  -3096  -5379       C  
ATOM    318  O   GLY A  40     -16.494   6.876   3.224  1.00 91.29           O  
ANISOU  318  O   GLY A  40    13118  14120   7449   4831  -3363  -5771       O  
ATOM    319  N   ARG A  41     -15.895   8.688   1.998  1.00 91.43           N  
ANISOU  319  N   ARG A  41    12690  16002   6048   5020  -2439  -4959       N  
ATOM    320  CA  ARG A  41     -14.455   8.462   2.112  1.00 93.14           C  
ANISOU  320  CA  ARG A  41    12664  16966   5757   5562  -1915  -4912       C  
ATOM    321  C   ARG A  41     -13.892   8.963   3.444  1.00 84.25           C  
ANISOU  321  C   ARG A  41    11144  15557   5311   4828  -1369  -4169       C  
ATOM    322  O   ARG A  41     -14.372   9.981   4.018  1.00 77.39           O  
ANISOU  322  O   ARG A  41    10064  14416   4927   3980  -1148  -3463       O  
ATOM    323  CB  ARG A  41     -13.702   9.103   0.948  1.00 99.94           C  
ANISOU  323  CB  ARG A  41    13245  19374   5352   6191  -1430  -4614       C  
ATOM    324  CG  ARG A  41     -13.911  10.612   0.821  1.00 96.91           C  
ANISOU  324  CG  ARG A  41    12457  19475   4889   5464   -980  -3547       C  
ATOM    325  CD  ARG A  41     -13.528  11.069  -0.608  1.00106.63           C  
ANISOU  325  CD  ARG A  41    13511  22200   4803   6150   -741  -3333       C  
ATOM    326  NE  ARG A  41     -12.979  12.430  -0.570  1.00105.19           N  
ANISOU  326  NE  ARG A  41    12707  22774   4485   5572   -109  -2066       N  
ATOM    327  CZ  ARG A  41     -12.495  13.105  -1.630  1.00112.82           C  
ANISOU  327  CZ  ARG A  41    13294  25158   4413   5918    253  -1425       C  
ATOM    328  NH1 ARG A  41     -12.487  12.556  -2.850  1.00121.54           N  
ANISOU  328  NH1 ARG A  41    14599  27221   4358   6954    115  -2005       N  
ATOM    329  NH2 ARG A  41     -12.017  14.339  -1.466  1.00111.12           N  
ANISOU  329  NH2 ARG A  41    12492  25412   4317   5238    698   -168       N  
ATOM    330  N   TRP A  42     -12.878   8.233   3.928  1.00 84.64           N  
ANISOU  330  N   TRP A  42    11123  15656   5380   5225  -1219  -4389       N  
ATOM    331  CA  TRP A  42     -12.167   8.609   5.148  1.00 77.46           C  
ANISOU  331  CA  TRP A  42     9851  14577   5003   4664   -744  -3752       C  
ATOM    332  C   TRP A  42     -10.676   8.330   5.031  1.00 82.06           C  
ANISOU  332  C   TRP A  42    10109  16057   5014   5327   -307  -3709       C  
ATOM    333  O   TRP A  42     -10.232   7.646   4.101  1.00 89.61           O  
ANISOU  333  O   TRP A  42    11171  17674   5202   6322   -410  -4312       O  
ATOM    334  CB  TRP A  42     -12.748   7.903   6.373  1.00 72.05           C  
ANISOU  334  CB  TRP A  42     9407  12592   5377   4162  -1129  -3957       C  
ATOM    335  CG  TRP A  42     -12.778   6.406   6.292  1.00 76.38           C  
ANISOU  335  CG  TRP A  42    10360  12542   6119   4766  -1760  -4844       C  
ATOM    336  CD1 TRP A  42     -13.783   5.643   5.782  1.00 78.91           C  
ANISOU  336  CD1 TRP A  42    11129  12192   6660   4948  -2546  -5508       C  
ATOM    337  CD2 TRP A  42     -11.781   5.492   6.772  1.00 78.29           C  
ANISOU  337  CD2 TRP A  42    10604  12683   6462   5237  -1778  -5145       C  
ATOM    338  NE1 TRP A  42     -13.480   4.316   5.905  1.00 85.14           N  
ANISOU  338  NE1 TRP A  42    12229  12404   7714   5495  -3114  -6214       N  
ATOM    339  CE2 TRP A  42     -12.252   4.188   6.500  1.00 84.61           C  
ANISOU  339  CE2 TRP A  42    11903  12688   7557   5717  -2637  -6026       C  
ATOM    340  CE3 TRP A  42     -10.528   5.646   7.391  1.00 75.82           C  
ANISOU  340  CE3 TRP A  42     9910  12841   6057   5307  -1222  -4750       C  
ATOM    341  CZ2 TRP A  42     -11.515   3.036   6.822  1.00 88.60           C  
ANISOU  341  CZ2 TRP A  42    12569  12829   8267   6303  -2964  -6548       C  
ATOM    342  CZ3 TRP A  42      -9.796   4.500   7.715  1.00 80.59           C  
ANISOU  342  CZ3 TRP A  42    10636  13161   6824   5891  -1476  -5255       C  
ATOM    343  CH2 TRP A  42     -10.296   3.212   7.429  1.00 87.00           C  
ANISOU  343  CH2 TRP A  42    11979  13149   7928   6399  -2342  -6156       C  
ATOM    344  N   LYS A  43      -9.903   8.886   5.962  1.00 77.18           N  
ANISOU  344  N   LYS A  43     9075  15510   4738   4827    154  -3002       N  
ATOM    345  CA  LYS A  43      -8.457   8.672   6.005  1.00 81.62           C  
ANISOU  345  CA  LYS A  43     9217  16896   4897   5345    580  -2822       C  
ATOM    346  C   LYS A  43      -8.019   8.279   7.416  1.00 76.47           C  
ANISOU  346  C   LYS A  43     8534  15452   5071   4944    569  -2729       C  
ATOM    347  O   LYS A  43      -8.540   8.822   8.388  1.00 69.14           O  
ANISOU  347  O   LYS A  43     7646  13770   4854   4075    531  -2326       O  
ATOM    348  CB  LYS A  43      -7.713   9.925   5.544  1.00 83.24           C  
ANISOU  348  CB  LYS A  43     8776  18293   4560   5151   1178  -1816       C  
ATOM    349  CG  LYS A  43      -7.933  10.255   4.061  1.00 90.80           C  
ANISOU  349  CG  LYS A  43     9672  20317   4509   5692   1263  -1809       C  
ATOM    350  CD  LYS A  43      -6.847  11.254   3.595  1.00 95.40           C  
ANISOU  350  CD  LYS A  43     9449  22312   4487   5663   1897   -697       C  
ATOM    351  CE  LYS A  43      -7.092  11.507   2.079  1.00104.66           C  
ANISOU  351  CE  LYS A  43    10560  24673   4533   6286   1990   -665       C  
ATOM    352  NZ  LYS A  43      -6.660  10.323   1.221  1.00113.27           N  
ANISOU  352  NZ  LYS A  43    11802  26599   4636   7692   1975  -1615       N  
ATOM    353  N   PRO A  44      -7.071   7.321   7.534  1.00 81.31           N  
ANISOU  353  N   PRO A  44     9082  16264   5549   5648    578  -3127       N  
ATOM    354  CA  PRO A  44      -6.547   6.936   8.848  1.00 77.18           C  
ANISOU  354  CA  PRO A  44     8495  15080   5750   5314    565  -2984       C  
ATOM    355  C   PRO A  44      -5.770   8.076   9.487  1.00 73.79           C  
ANISOU  355  C   PRO A  44     7496  15090   5451   4665   1071  -1977       C  
ATOM    356  O   PRO A  44      -5.092   8.836   8.798  1.00 77.21           O  
ANISOU  356  O   PRO A  44     7421  16620   5296   4800   1492  -1414       O  
ATOM    357  CB  PRO A  44      -5.597   5.765   8.533  1.00 84.95           C  
ANISOU  357  CB  PRO A  44     9463  16434   6380   6389    481  -3619       C  
ATOM    358  CG  PRO A  44      -5.948   5.321   7.168  1.00 92.33           C  
ANISOU  358  CG  PRO A  44    10668  17877   6535   7294    251  -4347       C  
ATOM    359  CD  PRO A  44      -6.436   6.541   6.454  1.00 91.01           C  
ANISOU  359  CD  PRO A  44    10300  18377   5901   6878    572  -3764       C  
ATOM    360  N   LYS A  45      -5.874   8.188  10.806  1.00 67.88           N  
ANISOU  360  N   LYS A  45     6822  13495   5475   3968    972  -1717       N  
ATOM    361  CA  LYS A  45      -5.256   9.285  11.537  1.00 65.09           C  
ANISOU  361  CA  LYS A  45     6041  13326   5364   3299   1262   -847       C  
ATOM    362  C   LYS A  45      -5.107   8.878  13.008  1.00 60.38           C  
ANISOU  362  C   LYS A  45     5592  11873   5475   2923   1084   -848       C  
ATOM    363  O   LYS A  45      -5.811   7.991  13.497  1.00 58.14           O  
ANISOU  363  O   LYS A  45     5751  10766   5574   2942    747  -1357       O  
ATOM    364  CB  LYS A  45      -6.125  10.548  11.401  1.00 61.97           C  
ANISOU  364  CB  LYS A  45     5687  12805   5054   2608   1259   -392       C  
ATOM    365  CG  LYS A  45      -5.404  11.873  11.625  1.00 63.55           C  
ANISOU  365  CG  LYS A  45     5383  13442   5321   2060   1474    552       C  
ATOM    366  CD  LYS A  45      -6.408  12.983  11.961  1.00 60.33           C  
ANISOU  366  CD  LYS A  45     5194  12443   5285   1331   1271    835       C  
ATOM    367  CE  LYS A  45      -5.823  14.042  12.907  1.00 59.55           C  
ANISOU  367  CE  LYS A  45     4846  12123   5655    684   1189   1531       C  
ATOM    368  NZ  LYS A  45      -4.580  14.718  12.396  1.00 66.01           N  
ANISOU  368  NZ  LYS A  45     4986  13833   6263    621   1378   2368       N  
ATOM    369  N   MET A  46      -4.177   9.525  13.699  1.00 59.51           N  
ANISOU  369  N   MET A  46     5082  11984   5544   2571   1263   -215       N  
ATOM    370  CA  MET A  46      -3.919   9.255  15.107  1.00 56.06           C  
ANISOU  370  CA  MET A  46     4751  10869   5681   2234   1099   -143       C  
ATOM    371  C   MET A  46      -3.977  10.555  15.895  1.00 51.66           C  
ANISOU  371  C   MET A  46     4100  10094   5434   1456   1069    478       C  
ATOM    372  O   MET A  46      -3.380  11.561  15.493  1.00 53.87           O  
ANISOU  372  O   MET A  46     3954  10944   5570   1242   1204   1079       O  
ATOM    373  CB  MET A  46      -2.548   8.617  15.274  1.00 61.12           C  
ANISOU  373  CB  MET A  46     5012  11951   6260   2703   1215    -82       C  
ATOM    374  CG  MET A  46      -2.487   7.660  16.428  1.00 61.61           C  
ANISOU  374  CG  MET A  46     5358  11235   6815   2704    941   -366       C  
ATOM    375  SD  MET A  46      -1.493   6.230  16.002  1.00 74.20           S  
ANISOU  375  SD  MET A  46     6808  13163   8223   3717    909   -874       S  
ATOM    376  CE  MET A  46      -2.213   5.770  14.415  1.00 78.17           C  
ANISOU  376  CE  MET A  46     7554  14010   8136   4437    877  -1570       C  
ATOM    377  N   ILE A  47      -4.711  10.541  17.002  1.00 45.71           N  
ANISOU  377  N   ILE A  47     3734   8534   5099   1063    844    356       N  
ATOM    378  CA  ILE A  47      -4.807  11.709  17.856  1.00 42.71           C  
ANISOU  378  CA  ILE A  47     3367   7876   4984    466    715    780       C  
ATOM    379  C   ILE A  47      -4.407  11.345  19.270  1.00 41.56           C  
ANISOU  379  C   ILE A  47     3337   7289   5166    334    551    796       C  
ATOM    380  O   ILE A  47      -4.658  10.230  19.731  1.00 40.29           O  
ANISOU  380  O   ILE A  47     3400   6788   5120    549    502    454       O  
ATOM    381  CB  ILE A  47      -6.226  12.372  17.842  1.00 39.09           C  
ANISOU  381  CB  ILE A  47     3259   7010   4585    161    604    656       C  
ATOM    382  CG1 ILE A  47      -7.306  11.390  18.310  1.00 35.52           C  
ANISOU  382  CG1 ILE A  47     3198   6013   4285    260    523    182       C  
ATOM    383  CG2 ILE A  47      -6.545  12.933  16.447  1.00 41.51           C  
ANISOU  383  CG2 ILE A  47     3424   7785   4562    228    717    755       C  
ATOM    384  CD1 ILE A  47      -8.640  12.034  18.542  1.00 32.01           C  
ANISOU  384  CD1 ILE A  47     3003   5223   3936    -24    433    134       C  
ATOM    385  N   GLY A  48      -3.776  12.288  19.957  1.00 41.99           N  
ANISOU  385  N   GLY A  48     3239   7321   5394    -28    391   1226       N  
ATOM    386  CA  GLY A  48      -3.287  12.017  21.294  1.00 42.35           C  
ANISOU  386  CA  GLY A  48     3384   7027   5679   -122    193   1263       C  
ATOM    387  C   GLY A  48      -3.968  12.821  22.372  1.00 40.63           C  
ANISOU  387  C   GLY A  48     3529   6318   5590   -458    -81   1252       C  
ATOM    388  O   GLY A  48      -4.295  14.001  22.190  1.00 40.89           O  
ANISOU  388  O   GLY A  48     3600   6286   5649   -721   -247   1402       O  
ATOM    389  N   GLY A  49      -4.158  12.189  23.520  1.00 39.23           N  
ANISOU  389  N   GLY A  49     3614   5820   5471   -399   -166   1086       N  
ATOM    390  CA  GLY A  49      -4.623  12.928  24.659  1.00 37.77           C  
ANISOU  390  CA  GLY A  49     3744   5320   5285   -576   -429   1061       C  
ATOM    391  C   GLY A  49      -3.918  12.531  25.907  1.00 38.16           C  
ANISOU  391  C   GLY A  49     3861   5254   5384   -542   -630   1137       C  
ATOM    392  O   GLY A  49      -2.763  12.092  25.881  1.00 39.68           O  
ANISOU  392  O   GLY A  49     3767   5597   5712   -499   -671   1331       O  
ATOM    393  N   ILE A  50      -4.625  12.695  27.014  1.00 36.77           N  
ANISOU  393  N   ILE A  50     4038   4882   5052   -512   -752    998       N  
ATOM    394  CA  ILE A  50      -4.126  12.310  28.302  1.00 38.04           C  
ANISOU  394  CA  ILE A  50     4326   4979   5149   -437   -951   1064       C  
ATOM    395  C   ILE A  50      -4.157  10.769  28.258  1.00 37.96           C  
ANISOU  395  C   ILE A  50     4217   4989   5217   -288   -682   1110       C  
ATOM    396  O   ILE A  50      -5.177  10.178  27.908  1.00 37.52           O  
ANISOU  396  O   ILE A  50     4223   4889   5142   -234   -439   1014       O  
ATOM    397  CB  ILE A  50      -5.053  12.912  29.397  1.00 38.27           C  
ANISOU  397  CB  ILE A  50     4753   4948   4841   -324  -1091    882       C  
ATOM    398  CG1 ILE A  50      -4.281  13.852  30.319  1.00 39.63           C  
ANISOU  398  CG1 ILE A  50     5107   4996   4956   -333  -1646    853       C  
ATOM    399  CG2 ILE A  50      -5.800  11.845  30.152  1.00 39.48           C  
ANISOU  399  CG2 ILE A  50     5005   5215   4781   -153   -828    936       C  
ATOM    400  CD1 ILE A  50      -5.157  14.665  31.241  1.00 39.89           C  
ANISOU  400  CD1 ILE A  50     5563   5014   4579    -75  -1860    542       C  
ATOM    401  N   GLY A  51      -3.059  10.115  28.564  1.00 39.69           N  
ANISOU  401  N   GLY A  51     4268   5222   5590   -226   -798   1269       N  
ATOM    402  CA  GLY A  51      -3.063   8.638  28.528  1.00 40.33           C  
ANISOU  402  CA  GLY A  51     4291   5205   5826    -49   -671   1292       C  
ATOM    403  C   GLY A  51      -2.517   8.020  27.246  1.00 40.31           C  
ANISOU  403  C   GLY A  51     3994   5293   6028    147   -531   1180       C  
ATOM    404  O   GLY A  51      -2.244   6.819  27.189  1.00 42.28           O  
ANISOU  404  O   GLY A  51     4194   5400   6470    377   -565   1139       O  
ATOM    405  N   GLY A  52      -2.354   8.846  26.223  1.00 38.79           N  
ANISOU  405  N   GLY A  52     3608   5361   5771    105   -414   1136       N  
ATOM    406  CA  GLY A  52      -1.758   8.400  24.992  1.00 40.31           C  
ANISOU  406  CA  GLY A  52     3475   5846   5997    392   -245   1047       C  
ATOM    407  C   GLY A  52      -2.633   8.670  23.797  1.00 38.34           C  
ANISOU  407  C   GLY A  52     3264   5716   5588    431    -34    828       C  
ATOM    408  O   GLY A  52      -3.435   9.603  23.795  1.00 36.47           O  
ANISOU  408  O   GLY A  52     3186   5416   5253    153    -23    851       O  
ATOM    409  N   PHE A  53      -2.523   7.787  22.816  1.00 40.09           N  
ANISOU  409  N   PHE A  53     3381   6076   5774    844     78    560       N  
ATOM    410  CA APHE A  53      -3.102   8.026  21.509  0.50 39.82           C  
ANISOU  410  CA APHE A  53     3324   6296   5509    981    254    347       C  
ATOM    411  CA BPHE A  53      -3.092   8.009  21.496  0.50 39.86           C  
ANISOU  411  CA BPHE A  53     3327   6306   5514    990    255    343       C  
ATOM    412  C   PHE A  53      -4.199   7.021  21.130  1.00 39.56           C  
ANISOU  412  C   PHE A  53     3627   5845   5558   1177    151    -95       C  
ATOM    413  O   PHE A  53      -4.223   5.889  21.625  1.00 41.42           O  
ANISOU  413  O   PHE A  53     4018   5656   6064   1340    -69   -243       O  
ATOM    414  CB APHE A  53      -1.983   8.041  20.461  0.50 44.14           C  
ANISOU  414  CB APHE A  53     3403   7554   5813   1389    449    413       C  
ATOM    415  CB BPHE A  53      -1.980   7.914  20.450  0.50 44.31           C  
ANISOU  415  CB BPHE A  53     3437   7558   5841   1435    442    373       C  
ATOM    416  CG APHE A  53      -1.096   9.269  20.526  0.50 45.16           C  
ANISOU  416  CG APHE A  53     3100   8153   5907   1063    517   1000       C  
ATOM    417  CG BPHE A  53      -1.431   6.524  20.266  0.50 48.31           C  
ANISOU  417  CG BPHE A  53     3919   8038   6399   2061    362      9       C  
ATOM    418  CD1APHE A  53      -1.205  10.274  19.559  0.50 45.95           C  
ANISOU  418  CD1APHE A  53     2961   8729   5769    916    676   1267       C  
ATOM    419  CD1BPHE A  53      -0.360   6.078  21.029  0.50 50.48           C  
ANISOU  419  CD1BPHE A  53     3984   8316   6880   2189    262    187       C  
ATOM    420  CD2APHE A  53      -0.148   9.419  21.542  0.50 45.16           C  
ANISOU  420  CD2APHE A  53     2914   8088   6157    873    340   1343       C  
ATOM    421  CD2BPHE A  53      -1.983   5.662  19.324  0.50 51.22           C  
ANISOU  421  CD2BPHE A  53     4498   8330   6634   2564    298   -551       C  
ATOM    422  CE1APHE A  53      -0.391  11.413  19.607  0.50 47.85           C  
ANISOU  422  CE1APHE A  53     2761   9321   6099    533    619   1927       C  
ATOM    423  CE1BPHE A  53       0.153   4.796  20.856  0.50 55.60           C  
ANISOU  423  CE1BPHE A  53     4622   8888   7614   2833    123   -182       C  
ATOM    424  CE2APHE A  53       0.669  10.554  21.604  0.50 47.30           C  
ANISOU  424  CE2APHE A  53     2767   8693   6511    510    258   1933       C  
ATOM    425  CE2BPHE A  53      -1.478   4.377  19.146  0.50 56.84           C  
ANISOU  425  CE2BPHE A  53     5245   8919   7432   3227     95   -976       C  
ATOM    426  CZ APHE A  53       0.551  11.551  20.635  0.50 48.30           C  
ANISOU  426  CZ APHE A  53     2632   9244   6477    316    379   2256       C  
ATOM    427  CZ BPHE A  53      -0.406   3.944  19.912  0.50 58.53           C  
ANISOU  427  CZ BPHE A  53     5238   9134   7866   3375     20   -789       C  
ATOM    428  N   ILE A  54      -5.109   7.449  20.252  1.00 37.34           N  
ANISOU  428  N   ILE A  54     3444   5641   5101   1128    232   -257       N  
ATOM    429  CA  ILE A  54      -6.039   6.515  19.592  1.00 36.94           C  
ANISOU  429  CA  ILE A  54     3652   5255   5130   1366     49   -702       C  
ATOM    430  C   ILE A  54      -5.997   6.672  18.080  1.00 38.42           C  
ANISOU  430  C   ILE A  54     3745   5943   4909   1766    163   -995       C  
ATOM    431  O   ILE A  54      -5.725   7.746  17.566  1.00 38.23           O  
ANISOU  431  O   ILE A  54     3485   6476   4566   1657    424   -731       O  
ATOM    432  CB  ILE A  54      -7.504   6.637  20.080  1.00 33.40           C  
ANISOU  432  CB  ILE A  54     3462   4322   4906    931    -65   -641       C  
ATOM    433  CG1 ILE A  54      -8.066   8.055  19.829  1.00 29.71           C  
ANISOU  433  CG1 ILE A  54     2951   4137   4200    613    148   -454       C  
ATOM    434  CG2 ILE A  54      -7.615   6.150  21.537  1.00 32.48           C  
ANISOU  434  CG2 ILE A  54     3431   3785   5124    672   -198   -357       C  
ATOM    435  CD1 ILE A  54      -9.585   8.144  19.903  1.00 26.83           C  
ANISOU  435  CD1 ILE A  54     2768   3446   3979    350     63   -486       C  
ATOM    436  N   LYS A  55      -6.285   5.576  17.381  1.00 37.23           N  
ANISOU  436  N   LYS A  55     3797   5570   4781   2245   -107  -1528       N  
ATOM    437  CA  LYS A  55      -6.428   5.553  15.933  1.00 40.15           C  
ANISOU  437  CA  LYS A  55     4179   6384   4691   2737    -90  -1933       C  
ATOM    438  C   LYS A  55      -7.882   5.963  15.621  1.00 37.64           C  
ANISOU  438  C   LYS A  55     4107   5741   4453   2342   -220  -1981       C  
ATOM    439  O   LYS A  55      -8.821   5.490  16.277  1.00 40.13           O  
ANISOU  439  O   LYS A  55     4655   5328   5263   1996   -522  -1989       O  
ATOM    440  CB  LYS A  55      -6.181   4.150  15.412  1.00 49.57           C  
ANISOU  440  CB  LYS A  55     5578   7340   5917   3487   -488  -2601       C  
ATOM    441  CG  LYS A  55      -4.697   3.647  15.483  1.00 56.03           C  
ANISOU  441  CG  LYS A  55     6113   8603   6571   4106   -369  -2669       C  
ATOM    442  CD  LYS A  55      -4.524   2.214  14.956  1.00 71.96           C  
ANISOU  442  CD  LYS A  55     8414  10282   8647   4975   -885  -3463       C  
ATOM    443  CE  LYS A  55      -4.958   1.187  16.030  1.00 71.48           C  
ANISOU  443  CE  LYS A  55     8686   9042   9431   4668  -1471  -3499       C  
ATOM    444  NZ  LYS A  55      -4.643  -0.147  15.578  1.00 79.49           N  
ANISOU  444  NZ  LYS A  55     9967   9647  10588   5522  -2073  -4240       N  
ATOM    445  N   VAL A  56      -8.053   6.834  14.624  1.00 42.55           N  
ANISOU  445  N   VAL A  56     4617   6952   4598   2392      2  -1934       N  
ATOM    446  CA  VAL A  56      -9.367   7.332  14.258  1.00 41.08           C  
ANISOU  446  CA  VAL A  56     4614   6539   4457   2050   -111  -1950       C  
ATOM    447  C   VAL A  56      -9.541   7.340  12.756  1.00 46.06           C  
ANISOU  447  C   VAL A  56     5296   7673   4532   2544   -158  -2321       C  
ATOM    448  O   VAL A  56      -8.571   7.229  12.007  1.00 50.89           O  
ANISOU  448  O   VAL A  56     5719   9013   4606   3132     28  -2442       O  
ATOM    449  CB  VAL A  56      -9.644   8.758  14.807  1.00 36.38           C  
ANISOU  449  CB  VAL A  56     3858   6059   3905   1420    169  -1360       C  
ATOM    450  CG1 VAL A  56      -9.692   8.757  16.338  1.00 32.60           C  
ANISOU  450  CG1 VAL A  56     3407   5086   3894    993    156  -1075       C  
ATOM    451  CG2 VAL A  56      -8.633   9.783  14.277  1.00 37.37           C  
ANISOU  451  CG2 VAL A  56     3620   6993   3587   1470    511   -955       C  
ATOM    452  N   ARG A  57     -10.790   7.449  12.320  1.00 45.15           N  
ANISOU  452  N   ARG A  57     5407   7237   4512   2350   -414  -2486       N  
ATOM    453  CA  ARG A  57     -11.090   7.632  10.908  1.00 49.13           C  
ANISOU  453  CA  ARG A  57     5982   8244   4440   2755   -482  -2785       C  
ATOM    454  C   ARG A  57     -11.452   9.100  10.718  1.00 45.12           C  
ANISOU  454  C   ARG A  57     5270   8124   3750   2269   -166  -2211       C  
ATOM    455  O   ARG A  57     -12.281   9.638  11.455  1.00 40.24           O  
ANISOU  455  O   ARG A  57     4687   7009   3593   1671   -202  -1929       O  
ATOM    456  CB  ARG A  57     -12.227   6.699  10.473  1.00 51.84           C  
ANISOU  456  CB  ARG A  57     6730   7904   5061   2895  -1125  -3387       C  
ATOM    457  CG  ARG A  57     -11.841   5.221  10.437  1.00 58.87           C  
ANISOU  457  CG  ARG A  57     7882   8353   6132   3487  -1620  -4037       C  
ATOM    458  CD  ARG A  57     -13.005   4.332   9.992  1.00 65.94           C  
ANISOU  458  CD  ARG A  57     9183   8444   7428   3548  -2432  -4587       C  
ATOM    459  NE  ARG A  57     -13.860   3.946  11.113  1.00 65.78           N  
ANISOU  459  NE  ARG A  57     9176   7467   8349   2822  -2739  -4247       N  
ATOM    460  CZ  ARG A  57     -15.145   4.268  11.249  1.00 64.81           C  
ANISOU  460  CZ  ARG A  57     9031   6958   8635   2227  -2924  -3971       C  
ATOM    461  NH1 ARG A  57     -15.775   4.990  10.333  1.00 65.65           N  
ANISOU  461  NH1 ARG A  57     9158   7436   8351   2237  -2894  -4042       N  
ATOM    462  NH2 ARG A  57     -15.811   3.859  12.315  1.00 63.73           N  
ANISOU  462  NH2 ARG A  57     8803   6121   9292   1633  -3137  -3560       N  
ATOM    463  N   GLN A  58     -10.797   9.759   9.772  1.00 48.08           N  
ANISOU  463  N   GLN A  58     5394   9419   3456   2552    133  -1987       N  
ATOM    464  CA  GLN A  58     -11.059  11.158   9.524  1.00 45.90           C  
ANISOU  464  CA  GLN A  58     4912   9475   3054   2091    339  -1374       C  
ATOM    465  C   GLN A  58     -11.997  11.317   8.334  1.00 48.99           C  
ANISOU  465  C   GLN A  58     5486  10062   3067   2269    128  -1608       C  
ATOM    466  O   GLN A  58     -11.671  10.903   7.219  1.00 54.30           O  
ANISOU  466  O   GLN A  58     6169  11407   3056   2924    123  -1917       O  
ATOM    467  CB  GLN A  58      -9.767  11.932   9.298  1.00 48.64           C  
ANISOU  467  CB  GLN A  58     4767  10711   3003   2125    757   -723       C  
ATOM    468  CG  GLN A  58      -9.986  13.421   9.030  1.00 48.37           C  
ANISOU  468  CG  GLN A  58     4509  10928   2942   1596    844      9       C  
ATOM    469  CD  GLN A  58      -8.705  14.166   8.689  1.00 55.04           C  
ANISOU  469  CD  GLN A  58     4777  12691   3446   1572   1173    806       C  
ATOM    470  OE1 GLN A  58      -7.672  13.976   9.319  1.00 57.78           O  
ANISOU  470  OE1 GLN A  58     4853  13164   3939   1580   1331   1019       O  
ATOM    471  NE2 GLN A  58      -8.782  15.039   7.707  1.00 58.71           N  
ANISOU  471  NE2 GLN A  58     5005  13803   3500   1498   1241   1341       N  
ATOM    472  N   TYR A  59     -13.160  11.907   8.610  1.00 44.81           N  
ANISOU  472  N   TYR A  59     5092   8979   2954   1745    -59  -1481       N  
ATOM    473  CA  TYR A  59     -14.181  12.242   7.628  1.00 47.17           C  
ANISOU  473  CA  TYR A  59     5538   9360   3023   1769   -301  -1596       C  
ATOM    474  C   TYR A  59     -14.257  13.760   7.438  1.00 46.13           C  
ANISOU  474  C   TYR A  59     5164   9552   2811   1335   -114   -872       C  
ATOM    475  O   TYR A  59     -14.448  14.513   8.403  1.00 42.06           O  
ANISOU  475  O   TYR A  59     4575   8584   2821    810    -71   -502       O  
ATOM    476  CB  TYR A  59     -15.543  11.728   8.102  1.00 44.35           C  
ANISOU  476  CB  TYR A  59     5460   8087   3302   1500   -726  -1956       C  
ATOM    477  CG  TYR A  59     -15.691  10.225   8.087  1.00 47.26           C  
ANISOU  477  CG  TYR A  59     6105   8001   3852   1875  -1135  -2639       C  
ATOM    478  CD1 TYR A  59     -16.217   9.570   6.959  1.00 52.96           C  
ANISOU  478  CD1 TYR A  59     7107   8750   4267   2335  -1615  -3224       C  
ATOM    479  CD2 TYR A  59     -15.319   9.451   9.195  1.00 44.24           C  
ANISOU  479  CD2 TYR A  59     5733   7105   3974   1778  -1144  -2701       C  
ATOM    480  CE1 TYR A  59     -16.367   8.194   6.938  1.00 55.33           C  
ANISOU  480  CE1 TYR A  59     7706   8483   4835   2681  -2166  -3883       C  
ATOM    481  CE2 TYR A  59     -15.462   8.066   9.182  1.00 48.47           C  
ANISOU  481  CE2 TYR A  59     6530   7104   4785   2088  -1644  -3275       C  
ATOM    482  CZ  TYR A  59     -15.990   7.446   8.039  1.00 54.66           C  
ANISOU  482  CZ  TYR A  59     7608   7832   5328   2540  -2194  -3883       C  
ATOM    483  OH  TYR A  59     -16.152   6.085   7.994  1.00 58.78           O  
ANISOU  483  OH  TYR A  59     8436   7689   6208   2856  -2861  -4488       O  
ATOM    484  N   ASP A  60     -14.124  14.206   6.196  1.00 50.88           N  
ANISOU  484  N   ASP A  60     5657  10930   2745   1595    -64   -676       N  
ATOM    485  CA  ASP A  60     -14.131  15.630   5.882  1.00 51.25           C  
ANISOU  485  CA  ASP A  60     5450  11299   2723   1187     28    106       C  
ATOM    486  C   ASP A  60     -15.496  16.105   5.413  1.00 50.56           C  
ANISOU  486  C   ASP A  60     5576  10869   2766    994   -318     28       C  
ATOM    487  O   ASP A  60     -16.293  15.323   4.888  1.00 51.52           O  
ANISOU  487  O   ASP A  60     5982  10834   2757   1301   -605   -587       O  
ATOM    488  CB  ASP A  60     -13.060  15.947   4.832  1.00 58.38           C  
ANISOU  488  CB  ASP A  60     5976  13407   2801   1529    334    620       C  
ATOM    489  CG  ASP A  60     -11.660  15.648   5.337  1.00 60.61           C  
ANISOU  489  CG  ASP A  60     5918  14094   3017   1666    694    856       C  
ATOM    490  OD1 ASP A  60     -11.420  15.801   6.556  1.00 57.56           O  
ANISOU  490  OD1 ASP A  60     5511  13048   3311   1234    693    974       O  
ATOM    491  OD2 ASP A  60     -10.809  15.247   4.531  1.00 68.82           O  
ANISOU  491  OD2 ASP A  60     6699  16154   3295   2258    966    908       O  
ATOM    492  N   GLN A  61     -15.770  17.387   5.643  1.00 48.80           N  
ANISOU  492  N   GLN A  61     5218  10454   2869    488   -373    640       N  
ATOM    493  CA  GLN A  61     -16.973  18.032   5.138  1.00 49.15           C  
ANISOU  493  CA  GLN A  61     5390  10260   3023    315   -696    694       C  
ATOM    494  C   GLN A  61     -18.222  17.223   5.525  1.00 45.94           C  
ANISOU  494  C   GLN A  61     5284   9132   3040    358   -978    -14       C  
ATOM    495  O   GLN A  61     -19.064  16.886   4.687  1.00 47.86           O  
ANISOU  495  O   GLN A  61     5691   9417   3076    557  -1272   -336       O  
ATOM    496  CB  GLN A  61     -16.860  18.277   3.620  1.00 56.43           C  
ANISOU  496  CB  GLN A  61     6223  12085   3132    614   -717    962       C  
ATOM    497  CG  GLN A  61     -15.554  18.986   3.241  1.00 62.82           C  
ANISOU  497  CG  GLN A  61     6597  13755   3516    555   -398   1831       C  
ATOM    498  CD  GLN A  61     -15.298  19.013   1.753  1.00 74.79           C  
ANISOU  498  CD  GLN A  61     7959  16419   4039    991   -308   2113       C  
ATOM    499  OE1 GLN A  61     -15.268  17.967   1.080  1.00 80.03           O  
ANISOU  499  OE1 GLN A  61     8797  17583   4028   1665   -264   1461       O  
ATOM    500  NE2 GLN A  61     -15.101  20.218   1.220  1.00 80.09           N  
ANISOU  500  NE2 GLN A  61     8306  17532   4593    644   -335   3104       N  
ATOM    501  N   ILE A  62     -18.312  16.902   6.812  1.00 40.71           N  
ANISOU  501  N   ILE A  62     4653   7847   2969    161   -915   -191       N  
ATOM    502  CA  ILE A  62     -19.480  16.250   7.376  1.00 39.16           C  
ANISOU  502  CA  ILE A  62     4598   6998   3281     90  -1148   -626       C  
ATOM    503  C   ILE A  62     -20.406  17.307   7.968  1.00 37.08           C  
ANISOU  503  C   ILE A  62     4259   6330   3499   -244  -1245   -352       C  
ATOM    504  O   ILE A  62     -19.963  18.180   8.696  1.00 34.83           O  
ANISOU  504  O   ILE A  62     3890   5946   3399   -436  -1107    -15       O  
ATOM    505  CB  ILE A  62     -19.084  15.208   8.470  1.00 36.37           C  
ANISOU  505  CB  ILE A  62     4277   6291   3252    110  -1018   -905       C  
ATOM    506  CG1 ILE A  62     -18.388  13.988   7.845  1.00 40.01           C  
ANISOU  506  CG1 ILE A  62     4868   7017   3317    553  -1066  -1339       C  
ATOM    507  CG2 ILE A  62     -20.294  14.778   9.277  1.00 34.32           C  
ANISOU  507  CG2 ILE A  62     4020   5413   3609    -94  -1208  -1068       C  
ATOM    508  CD1 ILE A  62     -19.221  13.244   6.773  1.00 44.25           C  
ANISOU  508  CD1 ILE A  62     5624   7508   3679    843  -1536  -1837       C  
ATOM    509  N   LEU A  63     -21.696  17.210   7.666  1.00 29.16           N  
ANISOU  509  N   LEU A  63     3595   5073   2413  -1145   -392    -69       N  
ATOM    510  CA  LEU A  63     -22.704  18.095   8.255  1.00 29.44           C  
ANISOU  510  CA  LEU A  63     3745   4766   2673  -1063   -543    140       C  
ATOM    511  C   LEU A  63     -23.070  17.648   9.663  1.00 28.65           C  
ANISOU  511  C   LEU A  63     3686   4365   2836   -810   -467     -8       C  
ATOM    512  O   LEU A  63     -23.451  16.476   9.867  1.00 28.01           O  
ANISOU  512  O   LEU A  63     3563   4280   2798   -700   -374   -203       O  
ATOM    513  CB  LEU A  63     -23.980  18.116   7.381  1.00 30.17           C  
ANISOU  513  CB  LEU A  63     3826   4908   2729  -1114   -669    240       C  
ATOM    514  CG  LEU A  63     -25.162  18.905   7.977  1.00 29.68           C  
ANISOU  514  CG  LEU A  63     3835   4506   2935   -975   -833    385       C  
ATOM    515  CD1 LEU A  63     -24.877  20.432   8.033  1.00 30.98           C  
ANISOU  515  CD1 LEU A  63     4075   4491   3204  -1065  -1045    669       C  
ATOM    516  CD2 LEU A  63     -26.453  18.640   7.253  1.00 32.70           C  
ANISOU  516  CD2 LEU A  63     4175   4954   3297   -979   -926    424       C  
ATOM    517  N   ILE A  64     -22.999  18.570  10.624  1.00 28.48           N  
ANISOU  517  N   ILE A  64     3731   4103   2985   -741   -527     85       N  
ATOM    518  CA  ILE A  64     -23.471  18.285  11.995  1.00 28.96           C  
ANISOU  518  CA  ILE A  64     3797   3956   3251   -538   -468    -42       C  
ATOM    519  C   ILE A  64     -24.364  19.418  12.473  1.00 29.38           C  
ANISOU  519  C   ILE A  64     3882   3787   3496   -453   -623     41       C  
ATOM    520  O   ILE A  64     -24.105  20.579  12.175  1.00 30.98           O  
ANISOU  520  O   ILE A  64     4139   3888   3745   -532   -776    200       O  
ATOM    521  CB  ILE A  64     -22.339  18.181  13.061  1.00 28.07           C  
ANISOU  521  CB  ILE A  64     3686   3810   3170   -498   -356   -123       C  
ATOM    522  CG1 ILE A  64     -21.205  17.276  12.650  1.00 30.89           C  
ANISOU  522  CG1 ILE A  64     3988   4368   3381   -557   -235   -223       C  
ATOM    523  CG2 ILE A  64     -22.859  17.543  14.362  1.00 26.55           C  
ANISOU  523  CG2 ILE A  64     3457   3517   3112   -346   -286   -247       C  
ATOM    524  CD1 ILE A  64     -20.473  16.729  13.920  1.00 34.05           C  
ANISOU  524  CD1 ILE A  64     4362   4701   3873   -456   -134   -326       C  
ATOM    525  N   GLU A  65     -25.418  19.080  13.201  1.00 29.11           N  
ANISOU  525  N   GLU A  65     3795   3684   3582   -300   -605    -75       N  
ATOM    526  CA  GLU A  65     -26.212  20.107  13.841  1.00 31.34           C  
ANISOU  526  CA  GLU A  65     4054   3787   4068   -170   -734    -98       C  
ATOM    527  C   GLU A  65     -25.915  20.047  15.327  1.00 30.54           C  
ANISOU  527  C   GLU A  65     3906   3667   4031    -72   -621   -268       C  
ATOM    528  O   GLU A  65     -26.089  19.007  15.951  1.00 28.91           O  
ANISOU  528  O   GLU A  65     3636   3590   3761    -51   -485   -362       O  
ATOM    529  CB  GLU A  65     -27.699  19.944  13.551  1.00 32.01           C  
ANISOU  529  CB  GLU A  65     4058   3891   4214    -80   -812   -123       C  
ATOM    530  CG  GLU A  65     -28.481  21.189  13.892  1.00 35.73           C  
ANISOU  530  CG  GLU A  65     4482   4168   4928     70  -1006   -157       C  
ATOM    531  CD  GLU A  65     -29.876  21.208  13.299  0.50 37.05           C  
ANISOU  531  CD  GLU A  65     4559   4359   5159    145  -1135   -135       C  
ATOM    532  OE1 GLU A  65     -30.122  20.494  12.301  0.50 37.05           O  
ANISOU  532  OE1 GLU A  65     4576   4506   4997     25  -1117    -16       O  
ATOM    533  OE2 GLU A  65     -30.720  21.956  13.836  0.50 39.11           O  
ANISOU  533  OE2 GLU A  65     4713   4507   5638    333  -1260   -266       O  
ATOM    534  N   ILE A  66     -25.422  21.151  15.868  1.00 31.89           N  
ANISOU  534  N   ILE A  66     4108   3685   4324    -43   -700   -290       N  
ATOM    535  CA  ILE A  66     -25.002  21.204  17.269  1.00 32.25           C  
ANISOU  535  CA  ILE A  66     4099   3758   4397     17   -596   -460       C  
ATOM    536  C   ILE A  66     -25.950  22.165  17.956  1.00 34.88           C  
ANISOU  536  C   ILE A  66     4335   3981   4938    187   -715   -650       C  
ATOM    537  O   ILE A  66     -25.958  23.376  17.670  1.00 35.80           O  
ANISOU  537  O   ILE A  66     4501   3848   5253    229   -917   -633       O  
ATOM    538  CB  ILE A  66     -23.515  21.676  17.416  1.00 32.35           C  
ANISOU  538  CB  ILE A  66     4203   3717   4372    -97   -579   -391       C  
ATOM    539  CG1 ILE A  66     -22.566  20.727  16.667  1.00 30.80           C  
ANISOU  539  CG1 ILE A  66     4053   3676   3975   -238   -466   -261       C  
ATOM    540  CG2 ILE A  66     -23.100  21.799  18.885  1.00 31.57           C  
ANISOU  540  CG2 ILE A  66     4036   3670   4290    -49   -485   -570       C  
ATOM    541  CD1 ILE A  66     -21.240  21.369  16.314  1.00 33.93           C  
ANISOU  541  CD1 ILE A  66     4525   4058   4308   -389   -498   -141       C  
ATOM    542  N   CYS A  67     -26.776  21.597  18.830  1.00 36.14           N  
ANISOU  542  N   CYS A  67     4336   4338   5056    274   -612   -832       N  
ATOM    543  CA  CYS A  67     -27.762  22.337  19.599  1.00 39.64           C  
ANISOU  543  CA  CYS A  67     4610   4796   5655    453   -687  -1103       C  
ATOM    544  C   CYS A  67     -28.506  23.325  18.673  1.00 41.11           C  
ANISOU  544  C   CYS A  67     4818   4711   6090    576   -940  -1074       C  
ATOM    545  O   CYS A  67     -28.735  24.494  19.022  1.00 43.46           O  
ANISOU  545  O   CYS A  67     5062   4803   6646    730  -1113  -1262       O  
ATOM    546  CB  CYS A  67     -27.079  23.005  20.808  1.00 40.48           C  
ANISOU  546  CB  CYS A  67     4666   4911   5803    482   -652  -1319       C  
ATOM    547  SG  CYS A  67     -28.204  23.697  22.020  1.00 52.32           S  
ANISOU  547  SG  CYS A  67     5874   6580   7425    697   -681  -1780       S  
ATOM    548  N   GLY A  68     -28.869  22.842  17.481  1.00 39.79           N  
ANISOU  548  N   GLY A  68     4722   4536   5860    504   -986   -840       N  
ATOM    549  CA  GLY A  68     -29.629  23.644  16.522  1.00 41.68           C  
ANISOU  549  CA  GLY A  68     4972   4558   6308    586  -1247   -743       C  
ATOM    550  C   GLY A  68     -28.821  24.569  15.622  1.00 42.55           C  
ANISOU  550  C   GLY A  68     5265   4365   6535    469  -1467   -477       C  
ATOM    551  O   GLY A  68     -29.398  25.366  14.869  1.00 45.78           O  
ANISOU  551  O   GLY A  68     5686   4552   7157    517  -1746   -349       O  
ATOM    552  N   HIS A  69     -27.495  24.482  15.701  1.00 39.76           N  
ANISOU  552  N   HIS A  69     5041   4021   6047    297  -1367   -371       N  
ATOM    553  CA  HIS A  69     -26.607  25.247  14.832  1.00 40.14           C  
ANISOU  553  CA  HIS A  69     5249   3876   6127    107  -1553    -78       C  
ATOM    554  C   HIS A  69     -25.921  24.288  13.889  1.00 37.63           C  
ANISOU  554  C   HIS A  69     5000   3826   5472   -129  -1399    145       C  
ATOM    555  O   HIS A  69     -25.232  23.387  14.336  1.00 35.44           O  
ANISOU  555  O   HIS A  69     4713   3756   4995   -173  -1148     53       O  
ATOM    556  CB  HIS A  69     -25.517  25.949  15.649  1.00 40.24           C  
ANISOU  556  CB  HIS A  69     5325   3741   6225     68  -1560   -156       C  
ATOM    557  CG  HIS A  69     -26.000  27.127  16.431  1.00 43.98           C  
ANISOU  557  CG  HIS A  69     5742   3895   7074    276  -1776   -394       C  
ATOM    558  ND1 HIS A  69     -26.919  27.016  17.452  1.00 45.14           N  
ANISOU  558  ND1 HIS A  69     5703   4125   7324    534  -1694   -780       N  
ATOM    559  CD2 HIS A  69     -25.681  28.442  16.348  1.00 46.19           C  
ANISOU  559  CD2 HIS A  69     6107   3779   7663    257  -2089   -327       C  
ATOM    560  CE1 HIS A  69     -27.164  28.216  17.949  1.00 48.10           C  
ANISOU  560  CE1 HIS A  69     6034   4179   8064    703  -1937   -998       C  
ATOM    561  NE2 HIS A  69     -26.413  29.095  17.306  1.00 49.70           N  
ANISOU  561  NE2 HIS A  69     6415   4044   8425    544  -2194   -723       N  
ATOM    562  N   LYS A  70     -26.069  24.511  12.590  1.00 38.01           N  
ANISOU  562  N   LYS A  70     5098   3881   5463   -287  -1569    429       N  
ATOM    563  CA  LYS A  70     -25.441  23.660  11.579  1.00 36.56           C  
ANISOU  563  CA  LYS A  70     4939   4015   4938   -521  -1435    589       C  
ATOM    564  C   LYS A  70     -23.986  24.052  11.325  1.00 36.41           C  
ANISOU  564  C   LYS A  70     4998   4060   4776   -763  -1435    753       C  
ATOM    565  O   LYS A  70     -23.664  25.228  11.242  1.00 38.44           O  
ANISOU  565  O   LYS A  70     5329   4088   5189   -864  -1676    941       O  
ATOM    566  CB  LYS A  70     -26.241  23.722  10.272  1.00 38.08           C  
ANISOU  566  CB  LYS A  70     5115   4286   5069   -629  -1614    818       C  
ATOM    567  CG  LYS A  70     -27.634  23.135  10.392  1.00 39.52           C  
ANISOU  567  CG  LYS A  70     5197   4494   5324   -426  -1581    658       C  
ATOM    568  CD  LYS A  70     -28.365  23.242   9.064  1.00 43.66           C  
ANISOU  568  CD  LYS A  70     5699   5117   5772   -557  -1774    907       C  
ATOM    569  CE  LYS A  70     -29.847  23.512   9.234  1.00 48.85           C  
ANISOU  569  CE  LYS A  70     6261   5623   6676   -329  -1932    839       C  
ATOM    570  NZ  LYS A  70     -30.528  22.368   9.874  1.00 47.56           N  
ANISOU  570  NZ  LYS A  70     5995   5633   6441   -170  -1679    543       N  
ATOM    571  N   ALA A  71     -23.124  23.051  11.194  1.00 34.05           N  
ANISOU  571  N   ALA A  71     4668   4071   4198   -858  -1185    674       N  
ATOM    572  CA  ALA A  71     -21.715  23.238  10.877  1.00 34.10           C  
ANISOU  572  CA  ALA A  71     4697   4256   4006  -1096  -1144    794       C  
ATOM    573  C   ALA A  71     -21.302  22.130   9.908  1.00 33.75           C  
ANISOU  573  C   ALA A  71     4561   4641   3621  -1231   -969    754       C  
ATOM    574  O   ALA A  71     -21.901  21.045   9.890  1.00 32.11           O  
ANISOU  574  O   ALA A  71     4295   4524   3381  -1089   -829    557       O  
ATOM    575  CB  ALA A  71     -20.864  23.217  12.170  1.00 32.83           C  
ANISOU  575  CB  ALA A  71     4546   4008   3920   -994   -999    609       C  
ATOM    576  N   ILE A  72     -20.336  22.421   9.048  1.00 34.90           N  
ANISOU  576  N   ILE A  72     4678   5072   3512  -1524  -1001    931       N  
ATOM    577  CA  ILE A  72     -19.791  21.407   8.159  1.00 35.64           C  
ANISOU  577  CA  ILE A  72     4637   5639   3265  -1648   -823    808       C  
ATOM    578  C   ILE A  72     -18.308  21.396   8.417  1.00 36.27           C  
ANISOU  578  C   ILE A  72     4657   5932   3190  -1759   -697    751       C  
ATOM    579  O   ILE A  72     -17.644  22.447   8.358  1.00 37.50           O  
ANISOU  579  O   ILE A  72     4856   6084   3307  -1986   -836   1004       O  
ATOM    580  CB  ILE A  72     -20.084  21.663   6.653  1.00 38.62           C  
ANISOU  580  CB  ILE A  72     4954   6347   3374  -1947   -966   1048       C  
ATOM    581  CG1 ILE A  72     -21.539  21.332   6.315  1.00 38.35           C  
ANISOU  581  CG1 ILE A  72     4933   6192   3446  -1815  -1041   1034       C  
ATOM    582  CG2 ILE A  72     -19.217  20.761   5.774  1.00 40.50           C  
ANISOU  582  CG2 ILE A  72     5005   7169   3213  -2113   -771    862       C  
ATOM    583  CD1 ILE A  72     -21.934  21.684   4.894  1.00 40.11           C  
ANISOU  583  CD1 ILE A  72     5098   6724   3420  -2120  -1221   1316       C  
ATOM    584  N   GLY A  73     -17.782  20.223   8.758  1.00 34.68           N  
ANISOU  584  N   GLY A  73     4355   5888   2935  -1599   -462    425       N  
ATOM    585  CA  GLY A  73     -16.356  20.154   9.052  1.00 34.72           C  
ANISOU  585  CA  GLY A  73     4272   6111   2811  -1670   -342    341       C  
ATOM    586  C   GLY A  73     -15.861  18.741   9.184  1.00 33.56           C  
ANISOU  586  C   GLY A  73     3977   6150   2624  -1480   -128    -35       C  
ATOM    587  O   GLY A  73     -16.587  17.774   8.933  1.00 32.62           O  
ANISOU  587  O   GLY A  73     3825   6009   2559  -1328    -79   -231       O  
ATOM    588  N   THR A  74     -14.608  18.637   9.585  1.00 34.01           N  
ANISOU  588  N   THR A  74     3939   6373   2613  -1492    -28   -134       N  
ATOM    589  CA  THR A  74     -13.987  17.349   9.809  1.00 33.68           C  
ANISOU  589  CA  THR A  74     3739   6460   2598  -1286    132   -494       C  
ATOM    590  C   THR A  74     -14.470  16.687  11.084  1.00 31.14           C  
ANISOU  590  C   THR A  74     3513   5699   2619   -986    150   -592       C  
ATOM    591  O   THR A  74     -14.458  17.277  12.205  1.00 29.66           O  
ANISOU  591  O   THR A  74     3443   5235   2591   -941    116   -447       O  
ATOM    592  CB  THR A  74     -12.437  17.453   9.769  1.00 35.75           C  
ANISOU  592  CB  THR A  74     3823   7098   2662  -1399    220   -574       C  
ATOM    593  OG1 THR A  74     -12.048  17.733   8.432  1.00 38.36           O  
ANISOU  593  OG1 THR A  74     3994   7967   2615  -1690    224   -553       O  
ATOM    594  CG2 THR A  74     -11.774  16.139  10.209  1.00 34.92           C  
ANISOU  594  CG2 THR A  74     3552   7028   2688  -1120    341   -954       C  
ATOM    595  N   VAL A  75     -14.901  15.447  10.919  1.00 30.70           N  
ANISOU  595  N   VAL A  75     3393   5600   2669   -804    189   -841       N  
ATOM    596  CA  VAL A  75     -15.246  14.641  12.071  1.00 29.15           C  
ANISOU  596  CA  VAL A  75     3252   5049   2775   -567    185   -915       C  
ATOM    597  C   VAL A  75     -14.331  13.429  12.104  1.00 30.24           C  
ANISOU  597  C   VAL A  75     3213   5280   2995   -408    237  -1219       C  
ATOM    598  O   VAL A  75     -14.143  12.763  11.089  1.00 31.86           O  
ANISOU  598  O   VAL A  75     3271   5726   3109   -394    266  -1483       O  
ATOM    599  CB  VAL A  75     -16.720  14.219  12.043  1.00 27.55           C  
ANISOU  599  CB  VAL A  75     3152   4606   2711   -494    121   -893       C  
ATOM    600  CG1 VAL A  75     -17.040  13.303  13.216  1.00 26.76           C  
ANISOU  600  CG1 VAL A  75     3080   4198   2887   -310     96   -935       C  
ATOM    601  CG2 VAL A  75     -17.599  15.447  12.086  1.00 28.53           C  
ANISOU  601  CG2 VAL A  75     3418   4618   2802   -606     45   -624       C  
ATOM    602  N   LEU A  76     -13.760  13.173  13.278  1.00 29.87           N  
ANISOU  602  N   LEU A  76     3164   5054   3129   -288    231  -1194       N  
ATOM    603  CA  LEU A  76     -12.971  11.970  13.530  1.00 31.27           C  
ANISOU  603  CA  LEU A  76     3183   5207   3490    -93    219  -1447       C  
ATOM    604  C   LEU A  76     -13.849  10.949  14.252  1.00 30.65           C  
ANISOU  604  C   LEU A  76     3188   4728   3730     57    106  -1430       C  
ATOM    605  O   LEU A  76     -14.640  11.299  15.133  1.00 28.67           O  
ANISOU  605  O   LEU A  76     3087   4261   3545     14     69  -1179       O  
ATOM    606  CB  LEU A  76     -11.718  12.292  14.345  1.00 31.38           C  
ANISOU  606  CB  LEU A  76     3118   5305   3500    -82    249  -1392       C  
ATOM    607  CG  LEU A  76     -10.906  13.530  13.942  1.00 31.78           C  
ANISOU  607  CG  LEU A  76     3129   5710   3235   -300    335  -1291       C  
ATOM    608  CD1 LEU A  76      -9.734  13.744  14.898  1.00 34.07           C  
ANISOU  608  CD1 LEU A  76     3343   6048   3552   -281    353  -1236       C  
ATOM    609  CD2 LEU A  76     -10.411  13.431  12.526  1.00 34.78           C  
ANISOU  609  CD2 LEU A  76     3316   6539   3360   -387    403  -1528       C  
ATOM    610  N   VAL A  77     -13.722   9.690  13.853  1.00 32.17           N  
ANISOU  610  N   VAL A  77     3262   4842   4118    218     36  -1713       N  
ATOM    611  CA  VAL A  77     -14.486   8.616  14.442  1.00 32.35           C  
ANISOU  611  CA  VAL A  77     3351   4474   4465    324   -118  -1684       C  
ATOM    612  C   VAL A  77     -13.520   7.568  14.992  1.00 34.59           C  
ANISOU  612  C   VAL A  77     3495   4588   5061    519   -246  -1829       C  
ATOM    613  O   VAL A  77     -12.616   7.111  14.281  1.00 36.74           O  
ANISOU  613  O   VAL A  77     3570   5024   5366    652   -237  -2184       O  
ATOM    614  CB  VAL A  77     -15.420   7.977  13.392  1.00 34.25           C  
ANISOU  614  CB  VAL A  77     3600   4680   4735    332   -158  -1889       C  
ATOM    615  CG1 VAL A  77     -16.241   6.847  14.016  1.00 34.49           C  
ANISOU  615  CG1 VAL A  77     3705   4286   5113    399   -349  -1824       C  
ATOM    616  CG2 VAL A  77     -16.350   9.052  12.783  1.00 32.17           C  
ANISOU  616  CG2 VAL A  77     3453   4604   4166    141    -57  -1725       C  
ATOM    617  N   GLY A  78     -13.700   7.193  16.254  1.00 33.13           N  
ANISOU  617  N   GLY A  78     3384   4105   5099    528   -381  -1562       N  
ATOM    618  CA  GLY A  78     -12.857   6.162  16.861  1.00 35.08           C  
ANISOU  618  CA  GLY A  78     3507   4128   5694    701   -568  -1626       C  
ATOM    619  C   GLY A  78     -13.184   5.970  18.329  1.00 33.93           C  
ANISOU  619  C   GLY A  78     3457   3737   5697    612   -714  -1214       C  
ATOM    620  O   GLY A  78     -14.143   6.577  18.831  1.00 31.85           O  
ANISOU  620  O   GLY A  78     3340   3502   5261    429   -652   -942       O  
ATOM    621  N   PRO A  79     -12.357   5.177  19.042  1.00 35.71           N  
ANISOU  621  N   PRO A  79     3573   3768   6226    731   -913  -1170       N  
ATOM    622  CA  PRO A  79     -12.653   4.748  20.410  1.00 35.30           C  
ANISOU  622  CA  PRO A  79     3579   3489   6343    617  -1116   -756       C  
ATOM    623  C   PRO A  79     -12.363   5.806  21.471  1.00 33.20           C  
ANISOU  623  C   PRO A  79     3339   3489   5785    449   -980   -458       C  
ATOM    624  O   PRO A  79     -11.637   5.539  22.431  1.00 33.92           O  
ANISOU  624  O   PRO A  79     3349   3543   5995    446  -1115   -263       O  
ATOM    625  CB  PRO A  79     -11.755   3.524  20.595  1.00 39.09           C  
ANISOU  625  CB  PRO A  79     3908   3662   7285    827  -1412   -851       C  
ATOM    626  CG  PRO A  79     -10.606   3.753  19.682  1.00 40.74           C  
ANISOU  626  CG  PRO A  79     3935   4102   7443   1049  -1272  -1292       C  
ATOM    627  CD  PRO A  79     -11.072   4.635  18.558  1.00 37.77           C  
ANISOU  627  CD  PRO A  79     3615   4053   6683    978   -974  -1520       C  
ATOM    628  N   THR A  80     -12.920   6.999  21.283  1.00 29.78           N  
ANISOU  628  N   THR A  80     3008   3313   4992    314   -737   -439       N  
ATOM    629  CA  THR A  80     -12.946   8.015  22.321  1.00 28.48           C  
ANISOU  629  CA  THR A  80     2886   3366   4571    138   -627   -192       C  
ATOM    630  C   THR A  80     -13.983   7.569  23.373  1.00 29.77           C  
ANISOU  630  C   THR A  80     3101   3432   4778    -38   -767    128       C  
ATOM    631  O   THR A  80     -15.003   6.966  23.015  1.00 29.45           O  
ANISOU  631  O   THR A  80     3123   3225   4842    -66   -853    140       O  
ATOM    632  CB  THR A  80     -13.303   9.422  21.757  1.00 26.63           C  
ANISOU  632  CB  THR A  80     2741   3370   4007     62   -379   -293       C  
ATOM    633  OG1 THR A  80     -13.533  10.318  22.838  1.00 22.39           O  
ANISOU  633  OG1 THR A  80     2241   2988   3278    -96   -311    -97       O  
ATOM    634  CG2 THR A  80     -14.554   9.383  20.869  1.00 22.37           C  
ANISOU  634  CG2 THR A  80     2302   2754   3442     50   -349   -381       C  
ATOM    635  N   PRO A  81     -13.723   7.847  24.662  1.00 30.00           N  
ANISOU  635  N   PRO A  81     3084   3613   4702   -185   -796    387       N  
ATOM    636  CA  PRO A  81     -14.734   7.420  25.636  1.00 31.11           C  
ANISOU  636  CA  PRO A  81     3233   3765   4822   -403   -925    693       C  
ATOM    637  C   PRO A  81     -16.001   8.271  25.634  1.00 29.15           C  
ANISOU  637  C   PRO A  81     3056   3717   4303   -528   -751    659       C  
ATOM    638  O   PRO A  81     -17.003   7.860  26.192  1.00 29.49           O  
ANISOU  638  O   PRO A  81     3087   3806   4313   -704   -842    854       O  
ATOM    639  CB  PRO A  81     -13.998   7.550  26.977  1.00 31.31           C  
ANISOU  639  CB  PRO A  81     3152   3987   4758   -541   -990    949       C  
ATOM    640  CG  PRO A  81     -12.968   8.522  26.747  1.00 30.92           C  
ANISOU  640  CG  PRO A  81     3081   4097   4568   -432   -801    746       C  
ATOM    641  CD  PRO A  81     -12.549   8.448  25.324  1.00 29.90           C  
ANISOU  641  CD  PRO A  81     2985   3802   4574   -195   -736    428       C  
ATOM    642  N   VAL A  82     -15.950   9.440  24.991  1.00 27.60           N  
ANISOU  642  N   VAL A  82     2916   3643   3928   -445   -527    419       N  
ATOM    643  CA  VAL A  82     -17.003  10.441  25.056  1.00 27.19           C  
ANISOU  643  CA  VAL A  82     2907   3773   3652   -524   -379    354       C  
ATOM    644  C   VAL A  82     -17.026  11.148  23.706  1.00 25.31           C  
ANISOU  644  C   VAL A  82     2764   3463   3391   -383   -250    104       C  
ATOM    645  O   VAL A  82     -15.950  11.398  23.151  1.00 25.40           O  
ANISOU  645  O   VAL A  82     2775   3457   3417   -288   -203     -8       O  
ATOM    646  CB  VAL A  82     -16.647  11.438  26.213  1.00 28.21           C  
ANISOU  646  CB  VAL A  82     2967   4193   3559   -638   -285    392       C  
ATOM    647  CG1 VAL A  82     -17.324  12.766  26.064  1.00 29.97           C  
ANISOU  647  CG1 VAL A  82     3230   4547   3612   -630   -129    202       C  
ATOM    648  CG2 VAL A  82     -17.016  10.822  27.585  1.00 32.59           C  
ANISOU  648  CG2 VAL A  82     3400   4940   4041   -856   -404    661       C  
ATOM    649  N   ASN A  83     -18.215  11.422  23.159  1.00 22.94           N  
ANISOU  649  N   ASN A  83     2521   3153   3043   -388   -211     37       N  
ATOM    650  CA  ASN A  83     -18.361  12.266  21.981  1.00 22.05           C  
ANISOU  650  CA  ASN A  83     2489   3019   2871   -304   -113   -140       C  
ATOM    651  C   ASN A  83     -17.922  13.694  22.323  1.00 21.10           C  
ANISOU  651  C   ASN A  83     2383   3026   2608   -326    -13   -190       C  
ATOM    652  O   ASN A  83     -18.451  14.312  23.259  1.00 21.31           O  
ANISOU  652  O   ASN A  83     2373   3173   2552   -389     10   -177       O  
ATOM    653  CB  ASN A  83     -19.806  12.343  21.487  1.00 21.80           C  
ANISOU  653  CB  ASN A  83     2496   2968   2819   -316   -116   -171       C  
ATOM    654  CG  ASN A  83     -20.378  11.001  20.985  1.00 25.31           C  
ANISOU  654  CG  ASN A  83     2943   3266   3408   -315   -227   -144       C  
ATOM    655  OD1 ASN A  83     -19.697  10.221  20.300  1.00 24.78           O  
ANISOU  655  OD1 ASN A  83     2882   3061   3475   -239   -281   -220       O  
ATOM    656  ND2 ASN A  83     -21.676  10.757  21.299  1.00 22.71           N  
ANISOU  656  ND2 ASN A  83     2592   2982   3053   -402   -268    -67       N  
ATOM    657  N  AILE A  84     -16.944  14.220  21.596  0.50 20.58           N  
ANISOU  657  N  AILE A  84     2350   2958   2512   -291     33   -264       N  
ATOM    658  N  BILE A  84     -16.997  14.207  21.517  0.50 20.82           N  
ANISOU  658  N  BILE A  84     2385   2982   2545   -288     32   -269       N  
ATOM    659  CA AILE A  84     -16.451  15.561  21.892  0.50 20.21           C  
ANISOU  659  CA AILE A  84     2329   2988   2362   -341     88   -290       C  
ATOM    660  CA BILE A  84     -16.358  15.491  21.730  0.50 20.70           C  
ANISOU  660  CA BILE A  84     2393   3044   2428   -335     88   -294       C  
ATOM    661  C  AILE A  84     -16.486  16.479  20.664  0.50 20.18           C  
ANISOU  661  C  AILE A  84     2412   2942   2313   -349     96   -342       C  
ATOM    662  C  BILE A  84     -16.618  16.436  20.551  0.50 20.42           C  
ANISOU  662  C  BILE A  84     2448   2963   2349   -344     93   -345       C  
ATOM    663  O  AILE A  84     -15.979  16.134  19.599  0.50 21.09           O  
ANISOU  663  O  AILE A  84     2525   3085   2402   -342    106   -370       O  
ATOM    664  O  BILE A  84     -16.365  16.077  19.407  0.50 21.31           O  
ANISOU  664  O  BILE A  84     2568   3087   2442   -332     95   -375       O  
ATOM    665  CB AILE A  84     -15.035  15.535  22.562  0.50 20.59           C  
ANISOU  665  CB AILE A  84     2310   3137   2377   -376    107   -253       C  
ATOM    666  CB BILE A  84     -14.826  15.279  21.874  0.50 21.35           C  
ANISOU  666  CB BILE A  84     2413   3206   2492   -342    107   -282       C  
ATOM    667  CG1AILE A  84     -13.988  14.868  21.656  0.50 20.42           C  
ANISOU  667  CG1AILE A  84     2244   3124   2389   -316    108   -297       C  
ATOM    668  CG1BILE A  84     -14.497  14.546  23.183  0.50 20.78           C  
ANISOU  668  CG1BILE A  84     2247   3186   2464   -362     64   -177       C  
ATOM    669  CG2AILE A  84     -15.080  14.832  23.925  0.50 19.96           C  
ANISOU  669  CG2AILE A  84     2137   3130   2318   -418     65   -143       C  
ATOM    670  CG2BILE A  84     -14.069  16.610  21.775  0.50 21.72           C  
ANISOU  670  CG2BILE A  84     2497   3330   2427   -425    151   -302       C  
ATOM    671  CD1AILE A  84     -12.555  14.954  22.201  0.50 18.86           C  
ANISOU  671  CD1AILE A  84     1957   3056   2152   -341    126   -275       C  
ATOM    672  CD1BILE A  84     -13.134  13.886  23.191  0.50 20.07           C  
ANISOU  672  CD1BILE A  84     2064   3131   2431   -316     36   -163       C  
ATOM    673  N   ILE A  85     -17.124  17.634  20.830  1.00 20.31           N  
ANISOU  673  N   ILE A  85     2483   2908   2325   -373     72   -362       N  
ATOM    674  CA  ILE A  85     -17.148  18.702  19.837  1.00 20.77           C  
ANISOU  674  CA  ILE A  85     2629   2893   2369   -420     18   -345       C  
ATOM    675  C   ILE A  85     -15.942  19.621  20.071  1.00 20.56           C  
ANISOU  675  C   ILE A  85     2622   2902   2289   -527     14   -315       C  
ATOM    676  O   ILE A  85     -15.868  20.321  21.075  1.00 20.38           O  
ANISOU  676  O   ILE A  85     2595   2848   2302   -540     -1   -364       O  
ATOM    677  CB  ILE A  85     -18.474  19.525  19.895  1.00 21.65           C  
ANISOU  677  CB  ILE A  85     2781   2869   2577   -369    -66   -388       C  
ATOM    678  CG1 ILE A  85     -19.693  18.593  19.811  1.00 20.98           C  
ANISOU  678  CG1 ILE A  85     2651   2798   2521   -286    -55   -416       C  
ATOM    679  CG2 ILE A  85     -18.533  20.629  18.771  1.00 22.29           C  
ANISOU  679  CG2 ILE A  85     2961   2823   2686   -438   -191   -303       C  
ATOM    680  CD1 ILE A  85     -19.704  17.682  18.585  1.00 18.38           C  
ANISOU  680  CD1 ILE A  85     2342   2491   2151   -296    -47   -367       C  
ATOM    681  N   GLY A  86     -15.024  19.635  19.109  1.00 21.42           N  
ANISOU  681  N   GLY A  86     2991   2806   2340   -736    -32   -403       N  
ATOM    682  CA  GLY A  86     -13.788  20.366  19.260  1.00 21.09           C  
ANISOU  682  CA  GLY A  86     2911   2897   2206   -742     30   -450       C  
ATOM    683  C   GLY A  86     -13.811  21.713  18.600  1.00 21.39           C  
ANISOU  683  C   GLY A  86     3033   3017   2076   -939    -27   -349       C  
ATOM    684  O   GLY A  86     -14.784  22.062  17.952  1.00 22.39           O  
ANISOU  684  O   GLY A  86     3248   3085   2176  -1013   -130   -261       O  
ATOM    685  N   ARG A  87     -12.723  22.473  18.746  1.00 21.78           N  
ANISOU  685  N   ARG A  87     3080   3204   1993  -1053      0   -348       N  
ATOM    686  CA  ARG A  87     -12.696  23.862  18.251  1.00 23.10           C  
ANISOU  686  CA  ARG A  87     3431   3363   1983  -1315   -142   -190       C  
ATOM    687  C   ARG A  87     -12.984  23.977  16.736  1.00 24.95           C  
ANISOU  687  C   ARG A  87     3745   3721   2016  -1589   -213   -156       C  
ATOM    688  O   ARG A  87     -13.548  24.976  16.289  1.00 26.69           O  
ANISOU  688  O   ARG A  87     4198   3784   2158  -1743   -433     31       O  
ATOM    689  CB  ARG A  87     -11.379  24.539  18.596  1.00 23.03           C  
ANISOU  689  CB  ARG A  87     3409   3537   1805  -1510   -110   -184       C  
ATOM    690  CG  ARG A  87     -11.066  24.590  20.130  1.00 20.66           C  
ANISOU  690  CG  ARG A  87     3051   3126   1672  -1271    -65   -198       C  
ATOM    691  CD  ARG A  87      -9.807  25.426  20.383  1.00 22.80           C  
ANISOU  691  CD  ARG A  87     3334   3595   1734  -1540    -69   -170       C  
ATOM    692  NE  ARG A  87      -8.616  24.768  19.824  1.00 26.38           N  
ANISOU  692  NE  ARG A  87     3505   4534   1983  -1676    103   -352       N  
ATOM    693  CZ  ARG A  87      -7.997  25.098  18.690  1.00 29.50           C  
ANISOU  693  CZ  ARG A  87     3856   5312   2039  -2086    111   -365       C  
ATOM    694  NH1 ARG A  87      -8.421  26.103  17.924  1.00 28.52           N  
ANISOU  694  NH1 ARG A  87     4029   5069   1739  -2471    -80   -136       N  
ATOM    695  NH2 ARG A  87      -6.934  24.405  18.314  1.00 31.19           N  
ANISOU  695  NH2 ARG A  87     3715   6076   2060  -2112    284   -627       N  
ATOM    696  N   ASN A  88     -12.609  22.972  15.945  1.00 26.03           N  
ANISOU  696  N   ASN A  88     3705   4126   2058  -1634    -70   -353       N  
ATOM    697  CA  ASN A  88     -12.874  23.038  14.510  1.00 27.96           C  
ANISOU  697  CA  ASN A  88     3995   4557   2069  -1920   -123   -342       C  
ATOM    698  C   ASN A  88     -14.360  23.261  14.212  1.00 27.95           C  
ANISOU  698  C   ASN A  88     4170   4259   2190  -1856   -307   -172       C  
ATOM    699  O   ASN A  88     -14.717  23.885  13.194  1.00 29.77           O  
ANISOU  699  O   ASN A  88     4552   4536   2222  -2130   -469    -28       O  
ATOM    700  CB  ASN A  88     -12.345  21.809  13.772  1.00 29.45           C  
ANISOU  700  CB  ASN A  88     3946   5087   2157  -1888     49   -672       C  
ATOM    701  CG  ASN A  88     -13.246  20.590  13.927  1.00 29.51           C  
ANISOU  701  CG  ASN A  88     3947   4829   2439  -1575     53   -796       C  
ATOM    702  OD1 ASN A  88     -13.506  20.159  15.038  1.00 27.54           O  
ANISOU  702  OD1 ASN A  88     3709   4298   2457  -1302     51   -772       O  
ATOM    703  ND2 ASN A  88     -13.723  20.034  12.803  1.00 27.63           N  
ANISOU  703  ND2 ASN A  88     3703   4700   2093  -1678     39   -913       N  
ATOM    704  N   LEU A  89     -15.232  22.752  15.081  1.00 25.14           N  
ANISOU  704  N   LEU A  89     3775   3658   2120  -1527   -303   -185       N  
ATOM    705  CA  LEU A  89     -16.677  22.982  14.895  1.00 25.42           C  
ANISOU  705  CA  LEU A  89     3888   3527   2243  -1438   -476    -65       C  
ATOM    706  C   LEU A  89     -17.223  24.085  15.807  1.00 25.02           C  
ANISOU  706  C   LEU A  89     3947   3253   2307  -1240   -662     64       C  
ATOM    707  O   LEU A  89     -18.197  24.759  15.449  1.00 26.29           O  
ANISOU  707  O   LEU A  89     4216   3310   2464  -1175   -903    158       O  
ATOM    708  CB  LEU A  89     -17.481  21.686  15.047  1.00 23.95           C  
ANISOU  708  CB  LEU A  89     3557   3335   2206  -1296   -386   -175       C  
ATOM    709  CG  LEU A  89     -17.194  20.606  13.985  1.00 26.57           C  
ANISOU  709  CG  LEU A  89     3842   3818   2434  -1445   -291   -354       C  
ATOM    710  CD1 LEU A  89     -18.068  19.355  14.191  1.00 28.68           C  
ANISOU  710  CD1 LEU A  89     4062   3985   2851  -1362   -283   -426       C  
ATOM    711  CD2 LEU A  89     -17.388  21.143  12.577  1.00 26.36           C  
ANISOU  711  CD2 LEU A  89     3895   3958   2161  -1717   -393   -295       C  
ATOM    712  N   LEU A  90     -16.604  24.255  16.975  1.00 23.62           N  
ANISOU  712  N   LEU A  90     3732   3018   2224  -1106   -580     31       N  
ATOM    713  CA  LEU A  90     -17.035  25.287  17.922  1.00 23.98           C  
ANISOU  713  CA  LEU A  90     3870   2875   2366   -880   -757     75       C  
ATOM    714  C   LEU A  90     -16.954  26.655  17.247  1.00 25.93           C  
ANISOU  714  C   LEU A  90     4451   2921   2481  -1031  -1079    220       C  
ATOM    715  O   LEU A  90     -17.855  27.488  17.408  1.00 27.77           O  
ANISOU  715  O   LEU A  90     4819   2948   2785   -792  -1373    234       O  
ATOM    716  CB  LEU A  90     -16.216  25.244  19.227  1.00 22.64           C  
ANISOU  716  CB  LEU A  90     3619   2710   2274   -776   -610     13       C  
ATOM    717  CG  LEU A  90     -16.415  23.996  20.123  1.00 21.96           C  
ANISOU  717  CG  LEU A  90     3275   2749   2319   -622   -392    -75       C  
ATOM    718  CD1 LEU A  90     -15.472  24.091  21.328  1.00 19.88           C  
ANISOU  718  CD1 LEU A  90     2966   2494   2092   -557   -292   -104       C  
ATOM    719  CD2 LEU A  90     -17.872  23.786  20.567  1.00 20.36           C  
ANISOU  719  CD2 LEU A  90     2926   2617   2193   -429   -449    -98       C  
ATOM    720  N   THR A  91     -15.886  26.894  16.488  1.00 27.00           N  
ANISOU  720  N   THR A  91     4723   3140   2398  -1435  -1066    317       N  
ATOM    721  CA  THR A  91     -15.726  28.183  15.818  1.00 30.90           C  
ANISOU  721  CA  THR A  91     5609   3424   2707  -1720  -1428    528       C  
ATOM    722  C   THR A  91     -16.880  28.429  14.837  1.00 33.75           C  
ANISOU  722  C   THR A  91     6116   3664   3046  -1683  -1712    629       C  
ATOM    723  O   THR A  91     -17.388  29.556  14.721  1.00 35.73           O  
ANISOU  723  O   THR A  91     6719   3556   3303  -1609  -2152    760       O  
ATOM    724  CB  THR A  91     -14.377  28.305  15.069  1.00 32.42           C  
ANISOU  724  CB  THR A  91     5859   3896   2561  -2298  -1342    631       C  
ATOM    725  OG1 THR A  91     -14.211  27.200  14.175  1.00 32.32           O  
ANISOU  725  OG1 THR A  91     5567   4294   2420  -2444  -1071    515       O  
ATOM    726  CG2 THR A  91     -13.234  28.325  16.033  1.00 31.81           C  
ANISOU  726  CG2 THR A  91     5671   3939   2477  -2340  -1152    550       C  
ATOM    727  N   GLN A  92     -17.336  27.359  14.176  1.00 33.37           N  
ANISOU  727  N   GLN A  92     5812   3884   2985  -1693  -1504    548       N  
ATOM    728  CA  GLN A  92     -18.379  27.503  13.162  1.00 36.70           C  
ANISOU  728  CA  GLN A  92     6329   4267   3347  -1705  -1753    644       C  
ATOM    729  C   GLN A  92     -19.738  27.838  13.748  1.00 37.04           C  
ANISOU  729  C   GLN A  92     6334   4120   3621  -1192  -1986    569       C  
ATOM    730  O   GLN A  92     -20.588  28.385  13.064  1.00 41.31           O  
ANISOU  730  O   GLN A  92     7034   4538   4124  -1119  -2338    664       O  
ATOM    731  CB  GLN A  92     -18.478  26.247  12.292  1.00 35.75           C  
ANISOU  731  CB  GLN A  92     5950   4504   3129  -1879  -1474    545       C  
ATOM    732  CG  GLN A  92     -17.117  25.697  11.981  1.00 40.12           C  
ANISOU  732  CG  GLN A  92     6395   5363   3485  -2223  -1179    462       C  
ATOM    733  CD  GLN A  92     -17.062  24.854  10.754  1.00 47.37           C  
ANISOU  733  CD  GLN A  92     7178   6629   4189  -2488  -1039    368       C  
ATOM    734  OE1 GLN A  92     -16.015  24.776  10.107  1.00 54.36           O  
ANISOU  734  OE1 GLN A  92     8015   7859   4781  -2855   -915    319       O  
ATOM    735  NE2 GLN A  92     -18.178  24.229  10.396  1.00 48.67           N  
ANISOU  735  NE2 GLN A  92     7254   6780   4456  -2331  -1063    314       N  
ATOM    736  N   ILE A  93     -19.971  27.479  14.996  1.00 34.92           N  
ANISOU  736  N   ILE A  93     5815   3896   3557   -835  -1802    381       N  
ATOM    737  CA  ILE A  93     -21.233  27.834  15.611  1.00 36.03           C  
ANISOU  737  CA  ILE A  93     5830   4009   3852   -347  -2007    245       C  
ATOM    738  C   ILE A  93     -21.064  29.103  16.457  1.00 37.91           C  
ANISOU  738  C   ILE A  93     6320   3910   4175    -59  -2314    193       C  
ATOM    739  O   ILE A  93     -21.987  29.499  17.166  1.00 39.99           O  
ANISOU  739  O   ILE A  93     6445   4192   4557    430  -2489    -14       O  
ATOM    740  CB  ILE A  93     -21.861  26.643  16.413  1.00 33.86           C  
ANISOU  740  CB  ILE A  93     5086   4102   3677   -176  -1663     61       C  
ATOM    741  CG1 ILE A  93     -21.053  26.341  17.685  1.00 32.60           C  
ANISOU  741  CG1 ILE A  93     4820   3967   3599   -142  -1392    -19       C  
ATOM    742  CG2 ILE A  93     -22.016  25.393  15.506  1.00 33.61           C  
ANISOU  742  CG2 ILE A  93     4904   4303   3562   -486  -1438    105       C  
ATOM    743  CD1 ILE A  93     -21.638  25.261  18.559  1.00 30.85           C  
ANISOU  743  CD1 ILE A  93     4213   4077   3432    -56  -1130   -136       C  
ATOM    744  N   GLY A  94     -19.879  29.720  16.392  1.00 38.60           N  
ANISOU  744  N   GLY A  94     6753   3741   4172   -374  -2384    346       N  
ATOM    745  CA  GLY A  94     -19.634  31.025  17.035  1.00 41.43           C  
ANISOU  745  CA  GLY A  94     7480   3676   4584   -191  -2766    329       C  
ATOM    746  C   GLY A  94     -19.523  30.929  18.550  1.00 41.25           C  
ANISOU  746  C   GLY A  94     7213   3748   4711    150  -2557     76       C  
ATOM    747  O   GLY A  94     -19.890  31.853  19.299  1.00 43.18           O  
ANISOU  747  O   GLY A  94     7606   3743   5059    560  -2874   -104       O  
ATOM    748  N   CYS A  95     -19.000  29.803  19.002  1.00 37.81           N  
ANISOU  748  N   CYS A  95     6422   3669   4275    -11  -2056     44       N  
ATOM    749  CA  CYS A  95     -18.888  29.529  20.405  1.00 37.41           C  
ANISOU  749  CA  CYS A  95     6107   3784   4324    231  -1826   -150       C  
ATOM    750  C   CYS A  95     -17.685  30.250  20.994  1.00 37.57           C  
ANISOU  750  C   CYS A  95     6395   3572   4308     66  -1875   -107       C  
ATOM    751  O   CYS A  95     -16.570  30.151  20.452  1.00 36.29           O  
ANISOU  751  O   CYS A  95     6375   3401   4011   -393  -1771     82       O  
ATOM    752  CB  CYS A  95     -18.741  28.027  20.620  1.00 34.59           C  
ANISOU  752  CB  CYS A  95     5354   3817   3971     84  -1360   -152       C  
ATOM    753  SG  CYS A  95     -18.950  27.612  22.292  1.00 37.46           S  
ANISOU  753  SG  CYS A  95     5373   4449   4410    354  -1140   -346       S  
ATOM    754  N   THR A  96     -17.925  30.960  22.106  1.00 38.86           N  
ANISOU  754  N   THR A  96     6586   3622   4557    433  -2031   -317       N  
ATOM    755  CA  THR A  96     -16.891  31.702  22.820  1.00 39.20           C  
ANISOU  755  CA  THR A  96     6886   3442   4569    307  -2110   -315       C  
ATOM    756  C   THR A  96     -16.811  31.319  24.304  1.00 38.11           C  
ANISOU  756  C   THR A  96     6403   3591   4487    549  -1834   -537       C  
ATOM    757  O   THR A  96     -17.809  30.897  24.903  1.00 38.31           O  
ANISOU  757  O   THR A  96     6067   3922   4569    915  -1733   -751       O  
ATOM    758  CB  THR A  96     -17.109  33.248  22.700  1.00 43.84           C  
ANISOU  758  CB  THR A  96     8023   3460   5174    476  -2723   -359       C  
ATOM    759  OG1 THR A  96     -18.326  33.629  23.358  1.00 45.40           O  
ANISOU  759  OG1 THR A  96     8077   3664   5507   1146  -2942   -719       O  
ATOM    760  CG2 THR A  96     -17.170  33.683  21.241  1.00 46.05           C  
ANISOU  760  CG2 THR A  96     8708   3432   5356    164  -3067    -76       C  
ATOM    761  N   LEU A  97     -15.617  31.440  24.879  1.00 36.74           N  
ANISOU  761  N   LEU A  97     6313   3395   4252    290  -1712   -474       N  
ATOM    762  CA  LEU A  97     -15.436  31.359  26.315  1.00 36.73           C  
ANISOU  762  CA  LEU A  97     6089   3595   4271    487  -1547   -669       C  
ATOM    763  C   LEU A  97     -15.445  32.778  26.883  1.00 40.14           C  
ANISOU  763  C   LEU A  97     6890   3646   4717    709  -1960   -863       C  
ATOM    764  O   LEU A  97     -14.847  33.691  26.300  1.00 42.36           O  
ANISOU  764  O   LEU A  97     7666   3485   4944    443  -2289   -716       O  
ATOM    765  CB  LEU A  97     -14.092  30.713  26.632  1.00 34.62           C  
ANISOU  765  CB  LEU A  97     5708   3522   3924    106  -1226   -510       C  
ATOM    766  CG  LEU A  97     -13.953  29.208  26.713  1.00 33.38           C  
ANISOU  766  CG  LEU A  97     5150   3751   3781     25   -828   -432       C  
ATOM    767  CD1 LEU A  97     -12.463  28.910  26.883  1.00 33.30           C  
ANISOU  767  CD1 LEU A  97     5119   3851   3680   -295   -652   -319       C  
ATOM    768  CD2 LEU A  97     -14.737  28.668  27.912  1.00 33.05           C  
ANISOU  768  CD2 LEU A  97     4768   4010   3779    321   -682   -592       C  
ATOM    769  N   ASN A  98     -16.103  32.954  28.026  1.00 42.09           N  
ANISOU  769  N   ASN A  98     6908   4083   5000   1157  -1966  -1200       N  
ATOM    770  CA  ASN A  98     -16.269  34.273  28.651  1.00 46.86           C  
ANISOU  770  CA  ASN A  98     7837   4336   5631   1502  -2397  -1505       C  
ATOM    771  C   ASN A  98     -16.056  34.212  30.174  1.00 46.65           C  
ANISOU  771  C   ASN A  98     7523   4658   5544   1668  -2191  -1775       C  
ATOM    772  O   ASN A  98     -16.650  33.378  30.836  1.00 45.02           O  
ANISOU  772  O   ASN A  98     6787   5028   5291   1836  -1867  -1907       O  
ATOM    773  CB  ASN A  98     -17.704  34.809  28.403  1.00 50.91           C  
ANISOU  773  CB  ASN A  98     8339   4771   6233   2111  -2766  -1829       C  
ATOM    774  CG  ASN A  98     -18.233  34.558  26.974  1.00 52.99           C  
ANISOU  774  CG  ASN A  98     8701   4893   6539   2012  -2886  -1585       C  
ATOM    775  OD1 ASN A  98     -18.895  33.538  26.677  1.00 50.77           O  
ANISOU  775  OD1 ASN A  98     7969   5074   6246   2024  -2575  -1539       O  
ATOM    776  ND2 ASN A  98     -17.990  35.526  26.101  1.00 57.77           N  
ANISOU  776  ND2 ASN A  98     9930   4852   7170   1891  -3387  -1427       N  
ATOM    777  N   PHE A  99     -15.257  35.122  30.733  1.00 48.78           N  
ANISOU  777  N   PHE A  99     8157   4599   5780   1584  -2413  -1853       N  
ATOM    778  CA  PHE A  99     -15.120  35.247  32.192  1.00 50.02           C  
ANISOU  778  CA  PHE A  99     8085   5063   5859   1782  -2291  -2166       C  
ATOM    779  C   PHE A  99     -14.577  36.633  32.572  1.00 54.34           C  
ANISOU  779  C   PHE A  99     9201   5043   6401   1825  -2761  -2357       C  
ATOM    780  O   PHE A  99     -14.479  37.015  33.760  1.00 55.98           O  
ANISOU  780  O   PHE A  99     9327   5404   6540   2037  -2774  -2694       O  
ATOM    781  CB  PHE A  99     -14.229  34.129  32.767  1.00 45.99           C  
ANISOU  781  CB  PHE A  99     7201   5031   5244   1364  -1767  -1907       C  
ATOM    782  CG  PHE A  99     -12.782  34.248  32.379  1.00 45.95           C  
ANISOU  782  CG  PHE A  99     7506   4765   5188    802  -1749  -1564       C  
ATOM    783  CD1 PHE A  99     -12.338  33.763  31.152  1.00 44.14           C  
ANISOU  783  CD1 PHE A  99     7360   4442   4967    420  -1664  -1202       C  
ATOM    784  CD2 PHE A  99     -11.862  34.862  33.241  1.00 48.01           C  
ANISOU  784  CD2 PHE A  99     7938   4953   5349    636  -1820  -1637       C  
ATOM    785  CE1 PHE A  99     -11.016  33.889  30.785  1.00 44.22           C  
ANISOU  785  CE1 PHE A  99     7570   4370   4864   -111  -1640   -938       C  
ATOM    786  CE2 PHE A  99     -10.527  34.993  32.878  1.00 47.76           C  
ANISOU  786  CE2 PHE A  99     8133   4795   5217     75  -1807  -1337       C  
ATOM    787  CZ  PHE A  99     -10.098  34.501  31.651  1.00 44.11           C  
ANISOU  787  CZ  PHE A  99     7699   4323   4737   -300  -1708   -996       C  
ATOM    788  OXT PHE A  99     -14.215  37.407  31.676  1.00 56.36           O  
ANISOU  788  OXT PHE A  99    10051   4665   6699   1598  -3169  -2162       O  
TER     789      PHE A  99                                                      
ATOM    790  N   PRO B   1     -12.096  38.200  30.141  1.00 64.30           N  
ANISOU  790  N   PRO B   1    11963   4795   7672    168  -3220  -1103       N  
ATOM    791  CA  PRO B   1     -12.521  38.703  28.836  1.00 67.01           C  
ANISOU  791  CA  PRO B   1    12850   4630   7980    126  -3615   -925       C  
ATOM    792  C   PRO B   1     -13.306  37.649  28.037  1.00 63.40           C  
ANISOU  792  C   PRO B   1    11931   4558   7601    310  -3346   -829       C  
ATOM    793  O   PRO B   1     -13.541  36.551  28.530  1.00 58.81           O  
ANISOU  793  O   PRO B   1    10658   4595   7091    462  -2884   -906       O  
ATOM    794  CB  PRO B   1     -11.188  38.996  28.147  1.00 68.28           C  
ANISOU  794  CB  PRO B   1    13431   4587   7925   -774  -3612   -513       C  
ATOM    795  CG  PRO B   1     -10.267  37.915  28.684  1.00 63.56           C  
ANISOU  795  CG  PRO B   1    12131   4705   7314  -1100  -2976   -428       C  
ATOM    796  CD  PRO B   1     -10.719  37.661  30.112  1.00 61.82           C  
ANISOU  796  CD  PRO B   1    11461   4785   7244   -543  -2827   -793       C  
ATOM    797  N   GLN B   2     -13.728  37.995  26.825  1.00 65.47           N  
ANISOU  797  N   GLN B   2    12626   4430   7821    266  -3675   -653       N  
ATOM    798  CA  GLN B   2     -14.343  37.017  25.930  1.00 62.83           C  
ANISOU  798  CA  GLN B   2    11916   4438   7518    313  -3425   -513       C  
ATOM    799  C   GLN B   2     -13.271  36.463  24.997  1.00 60.24           C  
ANISOU  799  C   GLN B   2    11604   4243   7040   -472  -3111    -96       C  
ATOM    800  O   GLN B   2     -12.448  37.205  24.475  1.00 63.22           O  
ANISOU  800  O   GLN B   2    12535   4251   7234  -1034  -3341    135       O  
ATOM    801  CB  GLN B   2     -15.487  37.639  25.110  1.00 66.99           C  
ANISOU  801  CB  GLN B   2    12838   4546   8067    754  -3965   -584       C  
ATOM    802  CG  GLN B   2     -16.305  36.619  24.302  1.00 65.07           C  
ANISOU  802  CG  GLN B   2    12145   4727   7853    874  -3716   -501       C  
ATOM    803  CD  GLN B   2     -16.999  37.219  23.083  1.00 70.84           C  
ANISOU  803  CD  GLN B   2    13399   4987   8531    992  -4243   -379       C  
ATOM    804  OE1 GLN B   2     -16.353  37.554  22.086  1.00 73.28           O  
ANISOU  804  OE1 GLN B   2    14245   4912   8684    397  -4405     -7       O  
ATOM    805  NE2 GLN B   2     -18.322  37.342  23.153  1.00 73.45           N  
ANISOU  805  NE2 GLN B   2    13546   5412   8949   1736  -4521   -702       N  
ATOM    806  N   ILE B   3     -13.310  35.154  24.781  1.00 55.41           N  
ANISOU  806  N   ILE B   3    10395   4191   6469   -522  -2611    -26       N  
ATOM    807  CA  ILE B   3     -12.296  34.432  24.016  1.00 52.85           C  
ANISOU  807  CA  ILE B   3     9928   4145   6006  -1143  -2249    254       C  
ATOM    808  C   ILE B   3     -12.953  33.601  22.881  1.00 50.08           C  
ANISOU  808  C   ILE B   3     9415   3965   5648  -1126  -2116    378       C  
ATOM    809  O   ILE B   3     -13.756  32.712  23.165  1.00 47.43           O  
ANISOU  809  O   ILE B   3     8639   3942   5439   -734  -1907    246       O  
ATOM    810  CB  ILE B   3     -11.524  33.475  24.985  1.00 49.18           C  
ANISOU  810  CB  ILE B   3     8882   4210   5596  -1184  -1762    171       C  
ATOM    811  CG1 ILE B   3     -10.848  34.282  26.106  1.00 52.49           C  
ANISOU  811  CG1 ILE B   3     9441   4505   5999  -1242  -1882     54       C  
ATOM    812  CG2 ILE B   3     -10.487  32.656  24.262  1.00 47.96           C  
ANISOU  812  CG2 ILE B   3     8498   4420   5305  -1679  -1405    352       C  
ATOM    813  CD1 ILE B   3     -10.465  33.486  27.335  1.00 50.42           C  
ANISOU  813  CD1 ILE B   3     8638   4695   5825  -1083  -1528    -91       C  
ATOM    814  N   THR B   4     -12.621  33.904  21.622  1.00 50.42           N  
ANISOU  814  N   THR B   4     9832   3827   5498  -1609  -2250    632       N  
ATOM    815  CA  THR B   4     -12.951  33.026  20.486  1.00 46.96           C  
ANISOU  815  CA  THR B   4     9216   3627   5000  -1736  -2050    765       C  
ATOM    816  C   THR B   4     -12.044  31.781  20.459  1.00 41.77           C  
ANISOU  816  C   THR B   4     8037   3532   4300  -1994  -1496    765       C  
ATOM    817  O   THR B   4     -11.074  31.688  21.200  1.00 40.74           O  
ANISOU  817  O   THR B   4     7711   3610   4159  -2131  -1300    699       O  
ATOM    818  CB  THR B   4     -12.741  33.733  19.162  1.00 51.13           C  
ANISOU  818  CB  THR B   4    10304   3852   5271  -2267  -2352   1038       C  
ATOM    819  OG1 THR B   4     -11.484  34.414  19.206  1.00 54.31           O  
ANISOU  819  OG1 THR B   4    10988   4202   5444  -2894  -2396   1163       O  
ATOM    820  CG2 THR B   4     -13.880  34.715  18.860  1.00 56.09           C  
ANISOU  820  CG2 THR B   4    11472   3895   5946  -1908  -2967   1050       C  
ATOM    821  N   LEU B   5     -12.334  30.845  19.563  1.00 37.73           N  
ANISOU  821  N   LEU B   5     7329   3259   3749  -2047  -1284    820       N  
ATOM    822  CA  LEU B   5     -11.713  29.524  19.638  1.00 33.19           C  
ANISOU  822  CA  LEU B   5     6269   3159   3183  -2080   -827    736       C  
ATOM    823  C   LEU B   5     -10.982  29.117  18.347  1.00 34.01           C  
ANISOU  823  C   LEU B   5     6353   3533   3036  -2572   -643    824       C  
ATOM    824  O   LEU B   5     -10.719  27.943  18.112  1.00 31.73           O  
ANISOU  824  O   LEU B   5     5723   3585   2749  -2509   -332    718       O  
ATOM    825  CB  LEU B   5     -12.767  28.493  20.063  1.00 30.15           C  
ANISOU  825  CB  LEU B   5     5585   2884   2987  -1600   -702    625       C  
ATOM    826  CG  LEU B   5     -13.259  28.613  21.526  1.00 28.23           C  
ANISOU  826  CG  LEU B   5     5182   2619   2925  -1174   -758    470       C  
ATOM    827  CD1 LEU B   5     -14.583  27.855  21.720  1.00 24.55           C  
ANISOU  827  CD1 LEU B   5     4503   2291   2536   -832   -732    394       C  
ATOM    828  CD2 LEU B   5     -12.195  28.108  22.507  1.00 24.01           C  
ANISOU  828  CD2 LEU B   5     4377   2317   2430  -1200   -513    385       C  
ATOM    829  N   TRP B   6     -10.632  30.116  17.533  1.00 37.25           N  
ANISOU  829  N   TRP B   6     7166   3793   3196  -3084   -870   1002       N  
ATOM    830  CA  TRP B   6      -9.811  29.915  16.335  1.00 39.57           C  
ANISOU  830  CA  TRP B   6     7432   4452   3151  -3685   -701   1071       C  
ATOM    831  C   TRP B   6      -8.421  29.398  16.693  1.00 39.68           C  
ANISOU  831  C   TRP B   6     6991   5041   3045  -3876   -343    883       C  
ATOM    832  O   TRP B   6      -7.804  28.658  15.929  1.00 40.97           O  
ANISOU  832  O   TRP B   6     6852   5707   3008  -4092    -63    765       O  
ATOM    833  CB  TRP B   6      -9.712  31.219  15.535  1.00 44.27           C  
ANISOU  833  CB  TRP B   6     8632   4750   3439  -4300  -1087   1342       C  
ATOM    834  CG  TRP B   6     -11.062  31.686  15.166  1.00 45.06           C  
ANISOU  834  CG  TRP B   6     9163   4297   3662  -4012  -1494   1487       C  
ATOM    835  CD1 TRP B   6     -11.795  32.638  15.799  1.00 47.31           C  
ANISOU  835  CD1 TRP B   6     9851   4002   4121  -3659  -1945   1520       C  
ATOM    836  CD2 TRP B   6     -11.880  31.171  14.120  1.00 44.76           C  
ANISOU  836  CD2 TRP B   6     9145   4278   3583  -3969  -1500   1561       C  
ATOM    837  NE1 TRP B   6     -13.020  32.766  15.197  1.00 49.16           N  
ANISOU  837  NE1 TRP B   6    10329   3924   4425  -3366  -2253   1597       N  
ATOM    838  CE2 TRP B   6     -13.096  31.877  14.159  1.00 47.12           C  
ANISOU  838  CE2 TRP B   6     9846   4025   4032  -3585  -1980   1651       C  
ATOM    839  CE3 TRP B   6     -11.697  30.189  13.138  1.00 45.36           C  
ANISOU  839  CE3 TRP B   6     8936   4805   3493  -4202  -1165   1529       C  
ATOM    840  CZ2 TRP B   6     -14.129  31.640  13.248  1.00 49.02           C  
ANISOU  840  CZ2 TRP B   6    10192   4177   4255  -3461  -2134   1742       C  
ATOM    841  CZ3 TRP B   6     -12.727  29.946  12.235  1.00 46.08           C  
ANISOU  841  CZ3 TRP B   6     9173   4768   3567  -4116  -1302   1633       C  
ATOM    842  CH2 TRP B   6     -13.930  30.665  12.301  1.00 47.44           C  
ANISOU  842  CH2 TRP B   6     9724   4413   3887  -3762  -1778   1753       C  
ATOM    843  N   GLN B   7      -7.953  29.783  17.873  0.50 38.63           N  
ANISOU  843  N   GLN B   7     6786   4863   3027  -3748   -372    814       N  
ATOM    844  CA AGLN B   7      -6.705  29.272  18.407  0.50 38.80           C  
ANISOU  844  CA AGLN B   7     6328   5436   2976  -3803    -74    607       C  
ATOM    845  CA BGLN B   7      -6.709  29.265  18.412  0.50 38.74           C  
ANISOU  845  CA BGLN B   7     6319   5428   2971  -3799    -73    606       C  
ATOM    846  C   GLN B   7      -6.991  28.579  19.750  1.00 35.07           C  
ANISOU  846  C   GLN B   7     5582   4872   2872  -3129     10    450       C  
ATOM    847  O   GLN B   7      -8.069  28.769  20.341  1.00 33.38           O  
ANISOU  847  O   GLN B   7     5568   4209   2904  -2747   -173    510       O  
ATOM    848  CB AGLN B   7      -5.672  30.408  18.539  0.50 42.91           C  
ANISOU  848  CB AGLN B   7     7013   6102   3188  -4451   -191    691       C  
ATOM    849  CB BGLN B   7      -5.690  30.393  18.591  0.50 42.78           C  
ANISOU  849  CB BGLN B   7     6991   6075   3188  -4423   -191    687       C  
ATOM    850  CG AGLN B   7      -6.175  31.653  19.291  0.50 44.38           C  
ANISOU  850  CG AGLN B   7     7744   5631   3486  -4443   -597    861       C  
ATOM    851  CG BGLN B   7      -5.224  31.019  17.293  0.50 47.69           C  
ANISOU  851  CG BGLN B   7     7866   6916   3337  -5254   -262    852       C  
ATOM    852  CD AGLN B   7      -5.284  32.893  19.128  0.50 50.47           C  
ANISOU  852  CD AGLN B   7     8894   6419   3864  -5259   -815   1022       C  
ATOM    853  CD BGLN B   7      -4.026  31.969  17.484  0.50 55.20           C  
ANISOU  853  CD BGLN B   7     8895   8181   3897  -6010   -328    910       C  
ATOM    854  OE1AGLN B   7      -4.547  33.035  18.144  0.50 56.30           O  
ANISOU  854  OE1AGLN B   7     9626   7593   4173  -5980   -736   1101       O  
ATOM    855  OE1BGLN B   7      -4.089  32.790  18.501  0.50 57.68           O  
ANISOU  855  OE1BGLN B   7     9521   8044   4349  -5939   -585    988       O  
ATOM    856  NE2AGLN B   7      -5.368  33.803  20.089  0.50 50.73           N  
ANISOU  856  NE2AGLN B   7     9280   5995   3998  -5195  -1107   1063       N  
ATOM    857  NE2BGLN B   7      -3.016  31.860  16.502  0.50 60.10           N  
ANISOU  857  NE2BGLN B   7     9237   9593   4004  -6739   -109    851       N  
ATOM    858  N   ARG B   8      -6.061  27.754  20.221  1.00 34.19           N  
ANISOU  858  N   ARG B   8     5005   5221   2764  -2975    261    233       N  
ATOM    859  CA  ARG B   8      -6.202  27.142  21.576  1.00 31.56           C  
ANISOU  859  CA  ARG B   8     4465   4802   2723  -2426    292    122       C  
ATOM    860  C   ARG B   8      -6.367  28.268  22.615  1.00 30.64           C  
ANISOU  860  C   ARG B   8     4586   4370   2686  -2462     76    218       C  
ATOM    861  O   ARG B   8      -5.654  29.267  22.539  1.00 32.68           O  
ANISOU  861  O   ARG B   8     4986   4696   2735  -2928    -15    277       O  
ATOM    862  CB  ARG B   8      -4.954  26.337  21.902  1.00 33.24           C  
ANISOU  862  CB  ARG B   8     4199   5561   2869  -2317    501   -123       C  
ATOM    863  CG  ARG B   8      -4.943  24.927  21.290  1.00 36.75           C  
ANISOU  863  CG  ARG B   8     4414   6206   3342  -1989    657   -312       C  
ATOM    864  CD  ARG B   8      -3.602  24.276  21.574  1.00 44.56           C  
ANISOU  864  CD  ARG B   8     4927   7769   4234  -1825    790   -619       C  
ATOM    865  NE  ARG B   8      -3.673  22.814  21.641  1.00 49.42           N  
ANISOU  865  NE  ARG B   8     5415   8362   5001  -1256    808   -825       N  
ATOM    866  CZ  ARG B   8      -3.083  21.987  20.775  1.00 53.02           C  
ANISOU  866  CZ  ARG B   8     5618   9215   5312  -1114    920  -1127       C  
ATOM    867  NH1 ARG B   8      -2.372  22.469  19.758  1.00 57.76           N  
ANISOU  867  NH1 ARG B   8     5985  10385   5578  -1553   1077  -1265       N  
ATOM    868  NH2 ARG B   8      -3.193  20.670  20.927  1.00 52.71           N  
ANISOU  868  NH2 ARG B   8     5583   9019   5424   -553    848  -1313       N  
ATOM    869  N   PRO B   9      -7.345  28.131  23.528  1.00 28.14           N  
ANISOU  869  N   PRO B   9     4336   3731   2625  -2019    -23    220       N  
ATOM    870  CA  PRO B   9      -7.612  29.111  24.574  1.00 28.20           C  
ANISOU  870  CA  PRO B   9     4537   3460   2716  -1948   -229    231       C  
ATOM    871  C   PRO B   9      -6.588  28.971  25.720  1.00 29.08           C  
ANISOU  871  C   PRO B   9     4360   3859   2832  -1924   -124    118       C  
ATOM    872  O   PRO B   9      -6.893  28.462  26.803  1.00 26.38           O  
ANISOU  872  O   PRO B   9     3851   3523   2650  -1563    -96     44       O  
ATOM    873  CB  PRO B   9      -9.044  28.785  24.988  1.00 25.24           C  
ANISOU  873  CB  PRO B   9     4206   2841   2545  -1489   -313    210       C  
ATOM    874  CG  PRO B   9      -9.153  27.308  24.807  1.00 24.55           C  
ANISOU  874  CG  PRO B   9     3831   2986   2513  -1295    -89    175       C  
ATOM    875  CD  PRO B   9      -8.307  27.006  23.572  1.00 25.55           C  
ANISOU  875  CD  PRO B   9     3904   3333   2471  -1604     49    191       C  
ATOM    876  N   LEU B  10      -5.368  29.427  25.433  1.00 28.35           N  
ANISOU  876  N   LEU B  10     4386   3474   2913  -1373  -1053    768       N  
ATOM    877  CA  LEU B  10      -4.244  29.352  26.375  1.00 28.56           C  
ANISOU  877  CA  LEU B  10     4308   3560   2983  -1281   -842    626       C  
ATOM    878  C   LEU B  10      -4.195  30.601  27.224  1.00 28.58           C  
ANISOU  878  C   LEU B  10     4373   3363   3125  -1131  -1029    670       C  
ATOM    879  O   LEU B  10      -4.374  31.710  26.706  1.00 31.79           O  
ANISOU  879  O   LEU B  10     4983   3588   3509  -1269  -1315    824       O  
ATOM    880  CB  LEU B  10      -2.916  29.230  25.634  1.00 30.07           C  
ANISOU  880  CB  LEU B  10     4542   3929   2953  -1635   -670    558       C  
ATOM    881  CG  LEU B  10      -2.676  27.883  24.965  1.00 32.35           C  
ANISOU  881  CG  LEU B  10     4699   4439   3152  -1755   -416    391       C  
ATOM    882  CD1 LEU B  10      -1.495  28.010  23.982  1.00 38.14           C  
ANISOU  882  CD1 LEU B  10     5472   5389   3631  -2200   -269    278       C  
ATOM    883  CD2 LEU B  10      -2.428  26.808  26.014  1.00 34.79           C  
ANISOU  883  CD2 LEU B  10     4775   4771   3674  -1431   -231    212       C  
ATOM    884  N   VAL B  11      -3.972  30.429  28.523  1.00 25.65           N  
ANISOU  884  N   VAL B  11     3846   3005   2896   -874   -902    540       N  
ATOM    885  CA  VAL B  11      -3.892  31.569  29.428  1.00 26.06           C  
ANISOU  885  CA  VAL B  11     3932   2890   3080   -734  -1041    525       C  
ATOM    886  C   VAL B  11      -2.658  31.433  30.331  1.00 24.65           C  
ANISOU  886  C   VAL B  11     3674   2816   2876   -724   -844    420       C  
ATOM    887  O   VAL B  11      -2.140  30.337  30.548  1.00 23.06           O  
ANISOU  887  O   VAL B  11     3339   2783   2641   -711   -632    337       O  
ATOM    888  CB  VAL B  11      -5.185  31.749  30.298  1.00 25.65           C  
ANISOU  888  CB  VAL B  11     3747   2745   3255   -415  -1141    430       C  
ATOM    889  CG1 VAL B  11      -6.401  32.070  29.433  1.00 30.78           C  
ANISOU  889  CG1 VAL B  11     4445   3256   3993   -392  -1410    514       C  
ATOM    890  CG2 VAL B  11      -5.445  30.499  31.145  1.00 25.63           C  
ANISOU  890  CG2 VAL B  11     3540   2945   3253   -279   -889    304       C  
ATOM    891  N   THR B  12      -2.216  32.555  30.871  1.00 24.77           N  
ANISOU  891  N   THR B  12     3772   2703   2936   -720   -953    419       N  
ATOM    892  CA  THR B  12      -1.168  32.561  31.857  1.00 25.05           C  
ANISOU  892  CA  THR B  12     3727   2825   2965   -693   -811    322       C  
ATOM    893  C   THR B  12      -1.757  32.234  33.240  1.00 24.73           C  
ANISOU  893  C   THR B  12     3532   2810   3053   -423   -749    203       C  
ATOM    894  O   THR B  12      -2.815  32.778  33.625  1.00 25.37           O  
ANISOU  894  O   THR B  12     3597   2778   3264   -265   -868    148       O  
ATOM    895  CB  THR B  12      -0.525  33.923  31.888  1.00 27.01           C  
ANISOU  895  CB  THR B  12     4143   2928   3190   -833   -959    365       C  
ATOM    896  OG1 THR B  12       0.004  34.182  30.589  1.00 28.79           O  
ANISOU  896  OG1 THR B  12     4537   3175   3229  -1180  -1013    484       O  
ATOM    897  CG2 THR B  12       0.619  33.956  32.879  1.00 28.37           C  
ANISOU  897  CG2 THR B  12     4225   3212   3342   -832   -819    262       C  
ATOM    898  N   ILE B  13      -1.090  31.321  33.955  1.00 22.98           N  
ANISOU  898  N   ILE B  13     3188   2746   2799   -395   -584    146       N  
ATOM    899  CA  ILE B  13      -1.462  30.989  35.325  1.00 22.55           C  
ANISOU  899  CA  ILE B  13     3032   2754   2784   -252   -533     63       C  
ATOM    900  C   ILE B  13      -0.252  31.198  36.232  1.00 23.44           C  
ANISOU  900  C   ILE B  13     3127   2918   2863   -297   -500     30       C  
ATOM    901  O   ILE B  13       0.912  31.152  35.780  1.00 23.49           O  
ANISOU  901  O   ILE B  13     3132   2957   2835   -408   -476     49       O  
ATOM    902  CB  ILE B  13      -1.995  29.549  35.470  1.00 21.92           C  
ANISOU  902  CB  ILE B  13     2861   2785   2684   -208   -444     74       C  
ATOM    903  CG1 ILE B  13      -0.860  28.522  35.243  1.00 20.72           C  
ANISOU  903  CG1 ILE B  13     2665   2690   2518   -268   -384    102       C  
ATOM    904  CG2 ILE B  13      -3.171  29.331  34.511  1.00 23.25           C  
ANISOU  904  CG2 ILE B  13     3035   2924   2875   -185   -474    102       C  
ATOM    905  CD1 ILE B  13      -1.218  27.059  35.557  1.00 21.06           C  
ANISOU  905  CD1 ILE B  13     2654   2775   2573   -230   -359    125       C  
ATOM    906  N   LYS B  14      -0.539  31.471  37.492  1.00 23.08           N  
ANISOU  906  N   LYS B  14     3049   2906   2815   -238   -496    -50       N  
ATOM    907  CA  LYS B  14       0.491  31.576  38.490  1.00 24.01           C  
ANISOU  907  CA  LYS B  14     3152   3092   2881   -295   -486    -71       C  
ATOM    908  C   LYS B  14       0.077  30.627  39.608  1.00 24.09           C  
ANISOU  908  C   LYS B  14     3105   3231   2818   -296   -452    -75       C  
ATOM    909  O   LYS B  14      -1.042  30.700  40.118  1.00 24.49           O  
ANISOU  909  O   LYS B  14     3130   3338   2836   -278   -413   -165       O  
ATOM    910  CB  LYS B  14       0.652  33.024  38.967  1.00 25.00           C  
ANISOU  910  CB  LYS B  14     3344   3134   3023   -314   -538   -165       C  
ATOM    911  CG  LYS B  14       1.829  33.186  39.943  1.00 26.06           C  
ANISOU  911  CG  LYS B  14     3466   3354   3083   -406   -533   -179       C  
ATOM    912  CD  LYS B  14       1.916  34.594  40.501  1.00 29.56           C  
ANISOU  912  CD  LYS B  14     3982   3710   3539   -436   -576   -299       C  
ATOM    913  CE  LYS B  14       3.082  34.683  41.465  1.00 32.94           C  
ANISOU  913  CE  LYS B  14     4394   4252   3871   -552   -573   -305       C  
ATOM    914  NZ  LYS B  14       3.189  36.065  41.987  1.00 35.82           N  
ANISOU  914  NZ  LYS B  14     4842   4524   4246   -599   -610   -440       N  
ATOM    915  N   ILE B  15       0.978  29.706  39.933  1.00 25.30           N  
ANISOU  915  N   ILE B  15     3232   3429   2951   -339   -491     12       N  
ATOM    916  CA  ILE B  15       0.736  28.635  40.894  1.00 26.61           C  
ANISOU  916  CA  ILE B  15     3404   3675   3032   -401   -538     82       C  
ATOM    917  C   ILE B  15       2.053  28.240  41.563  1.00 28.31           C  
ANISOU  917  C   ILE B  15     3607   3888   3259   -451   -675    157       C  
ATOM    918  O   ILE B  15       3.099  28.110  40.904  1.00 28.41           O  
ANISOU  918  O   ILE B  15     3542   3842   3411   -388   -717    150       O  
ATOM    919  CB  ILE B  15       0.034  27.400  40.241  1.00 26.78           C  
ANISOU  919  CB  ILE B  15     3422   3666   3088   -368   -535    156       C  
ATOM    920  CG1 ILE B  15      -0.355  26.385  41.335  1.00 29.27           C  
ANISOU  920  CG1 ILE B  15     3803   4051   3269   -506   -618    254       C  
ATOM    921  CG2 ILE B  15       0.908  26.766  39.146  1.00 26.59           C  
ANISOU  921  CG2 ILE B  15     3338   3540   3224   -287   -571    181       C  
ATOM    922  CD1 ILE B  15      -1.084  25.146  40.818  1.00 29.58           C  
ANISOU  922  CD1 ILE B  15     3870   4046   3324   -514   -636    334       C  
ATOM    923  N   GLY B  16       2.011  28.123  42.885  1.00 29.65           N  
ANISOU  923  N   GLY B  16     3840   4148   3276   -592   -749    202       N  
ATOM    924  CA  GLY B  16       3.205  27.823  43.682  1.00 30.76           C  
ANISOU  924  CA  GLY B  16     3985   4284   3420   -661   -942    295       C  
ATOM    925  C   GLY B  16       4.365  28.753  43.405  1.00 30.54           C  
ANISOU  925  C   GLY B  16     3871   4245   3489   -607   -931    207       C  
ATOM    926  O   GLY B  16       5.508  28.302  43.390  1.00 31.74           O  
ANISOU  926  O   GLY B  16     3932   4353   3775   -567  -1087    240       O  
ATOM    927  N   GLY B  17       4.067  30.039  43.182  1.00 28.87           N  
ANISOU  927  N   GLY B  17     3678   4061   3231   -611   -774     78       N  
ATOM    928  CA  GLY B  17       5.080  31.054  42.870  1.00 27.98           C  
ANISOU  928  CA  GLY B  17     3526   3936   3169   -621   -757      0       C  
ATOM    929  C   GLY B  17       5.608  31.048  41.433  1.00 26.19           C  
ANISOU  929  C   GLY B  17     3216   3651   3083   -555   -704    -36       C  
ATOM    930  O   GLY B  17       6.494  31.833  41.096  1.00 26.92           O  
ANISOU  930  O   GLY B  17     3278   3765   3185   -628   -684   -102       O  
ATOM    931  N   GLN B  18       5.078  30.150  40.607  1.00 24.08           N  
ANISOU  931  N   GLN B  18     2916   3339   2894   -468   -676     -7       N  
ATOM    932  CA  GLN B  18       5.596  29.905  39.247  1.00 23.27           C  
ANISOU  932  CA  GLN B  18     2713   3231   2896   -456   -612    -73       C  
ATOM    933  C   GLN B  18       4.599  30.349  38.209  1.00 21.54           C  
ANISOU  933  C   GLN B  18     2598   2958   2630   -470   -509    -64       C  
ATOM    934  O   GLN B  18       3.381  30.228  38.419  1.00 21.63           O  
ANISOU  934  O   GLN B  18     2689   2920   2608   -406   -503    -13       O  
ATOM    935  CB  GLN B  18       5.867  28.418  39.058  1.00 23.85           C  
ANISOU  935  CB  GLN B  18     2654   3281   3126   -352   -689    -77       C  
ATOM    936  CG  GLN B  18       6.881  27.870  40.036  1.00 26.88           C  
ANISOU  936  CG  GLN B  18     2931   3666   3618   -317   -887    -69       C  
ATOM    937  CD  GLN B  18       7.019  26.388  39.896  1.00 30.60           C  
ANISOU  937  CD  GLN B  18     3299   4027   4300   -186  -1040    -69       C  
ATOM    938  OE1 GLN B  18       7.408  25.894  38.835  1.00 31.72           O  
ANISOU  938  OE1 GLN B  18     3275   4168   4611   -119   -974   -236       O  
ATOM    939  NE2 GLN B  18       6.691  25.651  40.965  1.00 32.74           N  
ANISOU  939  NE2 GLN B  18     3682   4203   4556   -181  -1261    107       N  
ATOM    940  N   LEU B  19       5.112  30.779  37.061  1.00 20.25           N  
ANISOU  940  N   LEU B  19     2420   2821   2453   -586   -442   -122       N  
ATOM    941  CA  LEU B  19       4.265  31.228  35.959  1.00 19.76           C  
ANISOU  941  CA  LEU B  19     2486   2691   2329   -652   -405    -78       C  
ATOM    942  C   LEU B  19       4.254  30.171  34.884  1.00 19.75           C  
ANISOU  942  C   LEU B  19     2388   2754   2363   -669   -326   -124       C  
ATOM    943  O   LEU B  19       5.318  29.747  34.438  1.00 19.93           O  
ANISOU  943  O   LEU B  19     2252   2899   2423   -751   -259   -261       O  
ATOM    944  CB  LEU B  19       4.803  32.522  35.327  1.00 19.80           C  
ANISOU  944  CB  LEU B  19     2612   2682   2229   -878   -417    -78       C  
ATOM    945  CG  LEU B  19       5.072  33.646  36.314  1.00 24.13           C  
ANISOU  945  CG  LEU B  19     3251   3160   2757   -894   -495    -74       C  
ATOM    946  CD1 LEU B  19       5.670  34.873  35.562  1.00 25.36           C  
ANISOU  946  CD1 LEU B  19     3566   3274   2795  -1177   -538    -52       C  
ATOM    947  CD2 LEU B  19       3.819  33.983  37.124  1.00 24.34           C  
ANISOU  947  CD2 LEU B  19     3363   3045   2841   -711   -567    -51       C  
ATOM    948  N   LYS B  20       3.059  29.787  34.457  1.00 19.32           N  
ANISOU  948  N   LYS B  20     2405   2631   2304   -601   -328    -51       N  
ATOM    949  CA  LYS B  20       2.898  28.757  33.445  1.00 20.86           C  
ANISOU  949  CA  LYS B  20     2527   2878   2522   -625   -251   -101       C  
ATOM    950  C   LYS B  20       1.818  29.157  32.452  1.00 20.93           C  
ANISOU  950  C   LYS B  20     2688   2834   2432   -713   -268     -4       C  
ATOM    951  O   LYS B  20       1.070  30.108  32.673  1.00 21.67           O  
ANISOU  951  O   LYS B  20     2920   2812   2502   -688   -376     96       O  
ATOM    952  CB  LYS B  20       2.510  27.418  34.110  1.00 20.56           C  
ANISOU  952  CB  LYS B  20     2401   2802   2609   -433   -279    -97       C  
ATOM    953  CG  LYS B  20       3.591  26.865  35.044  1.00 23.90           C  
ANISOU  953  CG  LYS B  20     2684   3233   3163   -347   -350   -165       C  
ATOM    954  CD  LYS B  20       3.057  25.621  35.754  1.00 29.11           C  
ANISOU  954  CD  LYS B  20     3347   3798   3916   -212   -458    -90       C  
ATOM    955  CE  LYS B  20       4.132  24.988  36.632  1.00 34.40           C  
ANISOU  955  CE  LYS B  20     3901   4419   4749   -131   -623   -124       C  
ATOM    956  NZ  LYS B  20       5.205  24.454  35.767  1.00 39.40           N  
ANISOU  956  NZ  LYS B  20     4307   5079   5584    -98   -594   -359       N  
ATOM    957  N   GLU B  21       1.751  28.420  31.354  1.00 21.40           N  
ANISOU  957  N   GLU B  21     2705   2968   2456   -815   -184    -59       N  
ATOM    958  CA  GLU B  21       0.692  28.555  30.366  1.00 23.34           C  
ANISOU  958  CA  GLU B  21     3085   3176   2606   -911   -225     45       C  
ATOM    959  C   GLU B  21      -0.195  27.334  30.511  1.00 21.27           C  
ANISOU  959  C   GLU B  21     2750   2896   2433   -737   -196     41       C  
ATOM    960  O   GLU B  21       0.323  26.231  30.683  1.00 21.42           O  
ANISOU  960  O   GLU B  21     2628   2961   2550   -667   -115    -80       O  
ATOM    961  CB  GLU B  21       1.284  28.528  28.966  1.00 24.85           C  
ANISOU  961  CB  GLU B  21     3291   3516   2635  -1237   -128    -33       C  
ATOM    962  CG  GLU B  21       2.099  29.762  28.640  1.00 32.69           C  
ANISOU  962  CG  GLU B  21     4403   4548   3468  -1523   -166     -5       C  
ATOM    963  CD  GLU B  21       1.293  30.746  27.849  1.00 40.86           C  
ANISOU  963  CD  GLU B  21     5718   5456   4349  -1728   -364    217       C  
ATOM    964  OE1 GLU B  21       0.034  30.702  27.946  1.00 43.68           O  
ANISOU  964  OE1 GLU B  21     6144   5654   4800  -1532   -507    345       O  
ATOM    965  OE2 GLU B  21       1.919  31.538  27.110  1.00 44.59           O  
ANISOU  965  OE2 GLU B  21     6341   5995   4607  -2111   -397    257       O  
ATOM    966  N   ALA B  22      -1.508  27.536  30.415  1.00 20.14           N  
ANISOU  966  N   ALA B  22     2698   2676   2277   -675   -288    158       N  
ATOM    967  CA  ALA B  22      -2.485  26.453  30.572  1.00 19.29           C  
ANISOU  967  CA  ALA B  22     2536   2572   2222   -554   -264    163       C  
ATOM    968  C   ALA B  22      -3.700  26.648  29.683  1.00 19.72           C  
ANISOU  968  C   ALA B  22     2668   2606   2217   -612   -344    249       C  
ATOM    969  O   ALA B  22      -4.081  27.783  29.365  1.00 20.64           O  
ANISOU  969  O   ALA B  22     2889   2640   2313   -654   -495    335       O  
ATOM    970  CB  ALA B  22      -2.930  26.326  32.043  1.00 18.57           C  
ANISOU  970  CB  ALA B  22     2400   2451   2206   -370   -295    172       C  
ATOM    971  N   LEU B  23      -4.335  25.542  29.329  1.00 19.62           N  
ANISOU  971  N   LEU B  23     2612   2642   2200   -608   -283    232       N  
ATOM    972  CA  LEU B  23      -5.415  25.537  28.373  1.00 21.73           C  
ANISOU  972  CA  LEU B  23     2934   2919   2404   -690   -356    303       C  
ATOM    973  C   LEU B  23      -6.733  25.594  29.139  1.00 21.24           C  
ANISOU  973  C   LEU B  23     2808   2835   2426   -512   -437    322       C  
ATOM    974  O   LEU B  23      -6.968  24.777  30.039  1.00 22.41           O  
ANISOU  974  O   LEU B  23     2877   3031   2608   -423   -350    270       O  
ATOM    975  CB  LEU B  23      -5.283  24.238  27.545  1.00 21.98           C  
ANISOU  975  CB  LEU B  23     2933   3040   2378   -813   -218    225       C  
ATOM    976  CG  LEU B  23      -6.181  23.866  26.380  1.00 25.65           C  
ANISOU  976  CG  LEU B  23     3449   3561   2736   -967   -244    269       C  
ATOM    977  CD1 LEU B  23      -5.928  24.798  25.193  1.00 28.42           C  
ANISOU  977  CD1 LEU B  23     3940   3940   2917  -1240   -338    351       C  
ATOM    978  CD2 LEU B  23      -5.917  22.393  26.002  1.00 25.42           C  
ANISOU  978  CD2 LEU B  23     3351   3594   2713  -1023    -74    122       C  
ATOM    979  N   LEU B  24      -7.593  26.561  28.810  1.00 22.31           N  
ANISOU  979  N   LEU B  24     2973   2900   2602   -482   -625    378       N  
ATOM    980  CA  LEU B  24      -8.962  26.546  29.347  1.00 22.15           C  
ANISOU  980  CA  LEU B  24     2822   2909   2685   -328   -689    316       C  
ATOM    981  C   LEU B  24      -9.773  25.437  28.671  1.00 23.12           C  
ANISOU  981  C   LEU B  24     2908   3140   2735   -415   -635    332       C  
ATOM    982  O   LEU B  24     -10.098  25.514  27.475  1.00 24.42           O  
ANISOU  982  O   LEU B  24     3149   3286   2842   -540   -749    423       O  
ATOM    983  CB  LEU B  24      -9.644  27.893  29.207  1.00 23.27           C  
ANISOU  983  CB  LEU B  24     2957   2906   2976   -221   -957    318       C  
ATOM    984  CG  LEU B  24      -8.929  29.142  29.749  1.00 23.83           C  
ANISOU  984  CG  LEU B  24     3095   2820   3139   -150  -1062    301       C  
ATOM    985  CD1 LEU B  24      -9.752  30.348  29.370  1.00 25.93           C  
ANISOU  985  CD1 LEU B  24     3373   2874   3606    -41  -1409    308       C  
ATOM    986  CD2 LEU B  24      -8.743  29.081  31.233  1.00 25.70           C  
ANISOU  986  CD2 LEU B  24     3199   3143   3422    -17   -896    133       C  
ATOM    987  N   ASP B  25     -10.132  24.426  29.451  1.00 21.74           N  
ANISOU  987  N   ASP B  25     2641   3080   2540   -389   -485    257       N  
ATOM    988  CA  ASP B  25     -10.586  23.166  28.895  1.00 20.99           C  
ANISOU  988  CA  ASP B  25     2550   3068   2357   -508   -400    272       C  
ATOM    989  C   ASP B  25     -11.953  22.729  29.447  1.00 21.56           C  
ANISOU  989  C   ASP B  25     2479   3281   2432   -489   -383    194       C  
ATOM    990  O   ASP B  25     -12.039  22.027  30.455  1.00 20.64           O  
ANISOU  990  O   ASP B  25     2331   3246   2264   -522   -271    146       O  
ATOM    991  CB  ASP B  25      -9.516  22.082  29.122  1.00 21.36           C  
ANISOU  991  CB  ASP B  25     2666   3086   2364   -571   -255    266       C  
ATOM    992  CG  ASP B  25      -9.839  20.774  28.419  1.00 21.27           C  
ANISOU  992  CG  ASP B  25     2685   3105   2293   -698   -185    259       C  
ATOM    993  OD1 ASP B  25     -10.961  20.643  27.874  1.00 23.24           O  
ANISOU  993  OD1 ASP B  25     2901   3437   2492   -760   -223    274       O  
ATOM    994  OD2 ASP B  25      -8.952  19.885  28.389  1.00 22.46           O  
ANISOU  994  OD2 ASP B  25     2880   3182   2473   -729   -113    215       O  
ATOM    995  N   THR B  26     -13.013  23.141  28.757  1.00 21.52           N  
ANISOU  995  N   THR B  26     2390   3313   2473   -473   -518    182       N  
ATOM    996  CA  THR B  26     -14.369  22.814  29.165  1.00 22.41           C  
ANISOU  996  CA  THR B  26     2310   3604   2602   -467   -504     56       C  
ATOM    997  C   THR B  26     -14.683  21.308  29.132  1.00 22.07           C  
ANISOU  997  C   THR B  26     2307   3682   2398   -659   -348     78       C  
ATOM    998  O   THR B  26     -15.640  20.865  29.789  1.00 22.60           O  
ANISOU  998  O   THR B  26     2231   3940   2417   -727   -276    -37       O  
ATOM    999  CB  THR B  26     -15.407  23.584  28.332  1.00 24.09           C  
ANISOU  999  CB  THR B  26     2399   3804   2949   -387   -744     30       C  
ATOM   1000  OG1 THR B  26     -15.335  23.164  26.956  1.00 22.17           O  
ANISOU 1000  OG1 THR B  26     2311   3512   2601   -544   -820    200       O  
ATOM   1001  CG2 THR B  26     -15.154  25.089  28.422  1.00 23.92           C  
ANISOU 1001  CG2 THR B  26     2362   3597   3129   -194   -966      7       C  
ATOM   1002  N   GLY B  27     -13.865  20.538  28.405  1.00 20.04           N  
ANISOU 1002  N   GLY B  27     2233   3319   2062   -768   -296    192       N  
ATOM   1003  CA  GLY B  27     -13.981  19.070  28.366  1.00 21.21           C  
ANISOU 1003  CA  GLY B  27     2460   3498   2101   -937   -183    208       C  
ATOM   1004  C   GLY B  27     -13.302  18.320  29.514  1.00 21.61           C  
ANISOU 1004  C   GLY B  27     2600   3486   2125   -972   -105    221       C  
ATOM   1005  O   GLY B  27     -13.394  17.104  29.598  1.00 22.05           O  
ANISOU 1005  O   GLY B  27     2751   3510   2117  -1116    -71    250       O  
ATOM   1006  N   ALA B  28     -12.614  19.050  30.386  1.00 20.93           N  
ANISOU 1006  N   ALA B  28     2502   3356   2092   -857   -115    213       N  
ATOM   1007  CA  ALA B  28     -11.930  18.459  31.523  1.00 21.02           C  
ANISOU 1007  CA  ALA B  28     2613   3300   2074   -905   -102    255       C  
ATOM   1008  C   ALA B  28     -12.728  18.734  32.820  1.00 22.72           C  
ANISOU 1008  C   ALA B  28     2736   3723   2174   -997    -63    190       C  
ATOM   1009  O   ALA B  28     -12.964  19.898  33.177  1.00 22.55           O  
ANISOU 1009  O   ALA B  28     2566   3801   2199   -881    -53     78       O  
ATOM   1010  CB  ALA B  28     -10.531  19.065  31.629  1.00 20.44           C  
ANISOU 1010  CB  ALA B  28     2583   3070   2113   -757   -135    274       C  
ATOM   1011  N   ASP B  29     -13.131  17.675  33.517  1.00 24.59           N  
ANISOU 1011  N   ASP B  29     3064   4025   2255  -1236    -48    239       N  
ATOM   1012  CA  ASP B  29     -13.776  17.802  34.839  1.00 26.74           C  
ANISOU 1012  CA  ASP B  29     3273   4546   2340  -1436     15    162       C  
ATOM   1013  C   ASP B  29     -12.828  18.466  35.846  1.00 27.70           C  
ANISOU 1013  C   ASP B  29     3435   4619   2469  -1375    -13    175       C  
ATOM   1014  O   ASP B  29     -13.251  19.325  36.648  1.00 28.58           O  
ANISOU 1014  O   ASP B  29     3389   4955   2516  -1401     72      4       O  
ATOM   1015  CB  ASP B  29     -14.157  16.417  35.379  1.00 28.08           C  
ANISOU 1015  CB  ASP B  29     3629   4748   2293  -1793    -11    281       C  
ATOM   1016  CG  ASP B  29     -15.239  15.737  34.564  1.00 32.03           C  
ANISOU 1016  CG  ASP B  29     4081   5354   2737  -1922     37    245       C  
ATOM   1017  OD1 ASP B  29     -15.896  16.389  33.699  1.00 31.86           O  
ANISOU 1017  OD1 ASP B  29     3838   5446   2820  -1756     95    105       O  
ATOM   1018  OD2 ASP B  29     -15.439  14.526  34.795  1.00 32.79           O  
ANISOU 1018  OD2 ASP B  29     4377   5400   2681  -2211    -19    373       O  
ATOM   1019  N  AASP B  30     -11.552  18.069  35.757  0.50 26.40           N  
ANISOU 1019  N  AASP B  30     3454   4169   2407  -1287   -135    338       N  
ATOM   1020  N  BASP B  30     -11.561  18.061  35.849  0.50 26.54           N  
ANISOU 1020  N  BASP B  30     3476   4196   2413  -1302   -136    340       N  
ATOM   1021  CA AASP B  30     -10.502  18.436  36.710  0.50 27.30           C  
ANISOU 1021  CA AASP B  30     3647   4201   2526  -1261   -210    398       C  
ATOM   1022  CA BASP B  30     -10.627  18.580  36.849  0.50 27.58           C  
ANISOU 1022  CA BASP B  30     3659   4284   2537  -1277   -191    374       C  
ATOM   1023  C  AASP B  30      -9.386  19.277  36.080  0.50 24.85           C  
ANISOU 1023  C  AASP B  30     3286   3713   2441   -960   -237    376       C  
ATOM   1024  C  BASP B  30      -9.318  19.078  36.237  0.50 25.21           C  
ANISOU 1024  C  BASP B  30     3365   3744   2470   -995   -258    402       C  
ATOM   1025  O  AASP B  30      -9.152  19.266  34.852  0.50 23.77           O  
ANISOU 1025  O  AASP B  30     3122   3460   2450   -814   -229    361       O  
ATOM   1026  O  BASP B  30      -8.903  18.647  35.164  0.50 25.26           O  
ANISOU 1026  O  BASP B  30     3394   3580   2623   -881   -287    426       O  
ATOM   1027  CB AASP B  30      -9.863  17.180  37.337  0.50 28.41           C  
ANISOU 1027  CB AASP B  30     4042   4143   2611  -1449   -401    608       C  
ATOM   1028  CB BASP B  30     -10.362  17.551  37.960  0.50 28.92           C  
ANISOU 1028  CB BASP B  30     4056   4406   2524  -1577   -328    550       C  
ATOM   1029  CG AASP B  30     -10.872  16.109  37.687  0.50 29.85           C  
ANISOU 1029  CG AASP B  30     4348   4430   2563  -1803   -420    684       C  
ATOM   1030  CG BASP B  30     -11.621  17.169  38.735  0.50 32.22           C  
ANISOU 1030  CG BASP B  30     4478   5141   2625  -1966   -235    504       C  
ATOM   1031  OD1AASP B  30     -12.013  16.454  38.062  0.50 31.51           O  
ANISOU 1031  OD1AASP B  30     4430   4981   2562  -1996   -253    549       O  
ATOM   1032  OD1BASP B  30     -12.334  18.062  39.260  0.50 32.12           O  
ANISOU 1032  OD1BASP B  30     4259   5452   2491  -2031    -58    282       O  
ATOM   1033  OD2AASP B  30     -10.520  14.909  37.589  0.50 31.31           O  
ANISOU 1033  OD2AASP B  30     4751   4353   2793  -1899   -615    855       O  
ATOM   1034  OD2BASP B  30     -11.880  15.953  38.847  0.50 36.31           O  
ANISOU 1034  OD2BASP B  30     5199   5582   3015  -2234   -348    666       O  
ATOM   1035  N   THR B  31      -8.697  20.019  36.933  1.00 25.11           N  
ANISOU 1035  N   THR B  31     3315   3757   2468   -921   -259    364       N  
ATOM   1036  CA  THR B  31      -7.468  20.662  36.516  1.00 23.21           C  
ANISOU 1036  CA  THR B  31     3060   3352   2407   -707   -303    364       C  
ATOM   1037  C   THR B  31      -6.281  19.718  36.640  1.00 24.32           C  
ANISOU 1037  C   THR B  31     3322   3265   2654   -696   -463    484       C  
ATOM   1038  O   THR B  31      -6.109  19.047  37.666  1.00 25.44           O  
ANISOU 1038  O   THR B  31     3593   3366   2709   -853   -601    604       O  
ATOM   1039  CB  THR B  31      -7.296  21.895  37.352  1.00 24.30           C  
ANISOU 1039  CB  THR B  31     3128   3599   2505   -673   -265    276       C  
ATOM   1040  OG1 THR B  31      -8.361  22.793  37.005  1.00 22.55           O  
ANISOU 1040  OG1 THR B  31     2755   3520   2294   -609   -165    113       O  
ATOM   1041  CG2 THR B  31      -5.872  22.554  37.170  1.00 19.59           C  
ANISOU 1041  CG2 THR B  31     2540   2849   2054   -514   -324    293       C  
ATOM   1042  N   VAL B  32      -5.484  19.628  35.583  1.00 22.94           N  
ANISOU 1042  N   VAL B  32     3101   2944   2671   -538   -468    434       N  
ATOM   1043  CA  VAL B  32      -4.316  18.729  35.593  1.00 24.30           C  
ANISOU 1043  CA  VAL B  32     3312   2887   3033   -474   -632    457       C  
ATOM   1044  C   VAL B  32      -3.130  19.484  35.054  1.00 23.09           C  
ANISOU 1044  C   VAL B  32     3030   2712   3033   -318   -588    331       C  
ATOM   1045  O   VAL B  32      -3.157  19.937  33.915  1.00 21.99           O  
ANISOU 1045  O   VAL B  32     2810   2637   2910   -284   -446    220       O  
ATOM   1046  CB  VAL B  32      -4.469  17.483  34.645  1.00 25.22           C  
ANISOU 1046  CB  VAL B  32     3453   2852   3279   -470   -664    415       C  
ATOM   1047  CG1 VAL B  32      -3.521  16.371  35.082  1.00 25.23           C  
ANISOU 1047  CG1 VAL B  32     3516   2565   3505   -418   -929    445       C  
ATOM   1048  CG2 VAL B  32      -5.876  17.000  34.609  1.00 26.53           C  
ANISOU 1048  CG2 VAL B  32     3705   3115   3261   -642   -610    488       C  
ATOM   1049  N   LEU B  33      -2.077  19.564  35.862  1.00 25.92           N  
ANISOU 1049  N   LEU B  33     2841   3148   3861   -375   -604    398       N  
ATOM   1050  CA  LEU B  33      -0.852  20.213  35.460  1.00 26.36           C  
ANISOU 1050  CA  LEU B  33     2505   3156   4356   -261   -644    258       C  
ATOM   1051  C   LEU B  33       0.287  19.232  35.252  1.00 29.17           C  
ANISOU 1051  C   LEU B  33     2734   3345   5003    -79   -872    140       C  
ATOM   1052  O   LEU B  33       0.356  18.199  35.921  1.00 29.11           O  
ANISOU 1052  O   LEU B  33     3030   3203   4825     27  -1209    173       O  
ATOM   1053  CB  LEU B  33      -0.433  21.247  36.528  1.00 27.50           C  
ANISOU 1053  CB  LEU B  33     2577   3276   4596   -257   -858    122       C  
ATOM   1054  CG  LEU B  33      -1.441  22.360  36.860  1.00 26.84           C  
ANISOU 1054  CG  LEU B  33     2562   3319   4316   -419   -646    169       C  
ATOM   1055  CD1 LEU B  33      -0.828  23.407  37.771  1.00 27.78           C  
ANISOU 1055  CD1 LEU B  33     2551   3392   4612   -409   -841    -22       C  
ATOM   1056  CD2 LEU B  33      -1.972  23.045  35.586  1.00 25.53           C  
ANISOU 1056  CD2 LEU B  33     2214   3235   4250   -478   -242    253       C  
ATOM   1057  N   GLU B  34       1.211  19.582  34.358  1.00 30.40           N  
ANISOU 1057  N   GLU B  34     2469   3457   5624    -44   -665    -28       N  
ATOM   1058  CA  GLU B  34       2.413  18.788  34.187  1.00 35.51           C  
ANISOU 1058  CA  GLU B  34     2849   3923   6718    137   -863   -266       C  
ATOM   1059  C   GLU B  34       3.244  18.819  35.460  1.00 39.53           C  
ANISOU 1059  C   GLU B  34     3280   4284   7456    336  -1479   -489       C  
ATOM   1060  O   GLU B  34       2.985  19.616  36.382  1.00 39.60           O  
ANISOU 1060  O   GLU B  34     3420   4347   7281    293  -1665   -474       O  
ATOM   1061  CB  GLU B  34       3.237  19.282  33.004  1.00 36.98           C  
ANISOU 1061  CB  GLU B  34     2584   4062   7405     63   -377   -480       C  
ATOM   1062  CG  GLU B  34       2.460  19.334  31.694  1.00 37.75           C  
ANISOU 1062  CG  GLU B  34     2894   4269   7179    -94    174   -264       C  
ATOM   1063  CD  GLU B  34       3.317  19.819  30.523  1.00 44.82           C  
ANISOU 1063  CD  GLU B  34     3517   5045   8467   -206    754   -465       C  
ATOM   1064  OE1 GLU B  34       4.407  19.247  30.292  1.00 49.96           O  
ANISOU 1064  OE1 GLU B  34     3803   5536   9644   -139    803   -792       O  
ATOM   1065  OE2 GLU B  34       2.890  20.772  29.834  1.00 47.28           O  
ANISOU 1065  OE2 GLU B  34     4019   5382   8565   -360   1181   -315       O  
ATOM   1066  N   GLU B  35       4.241  17.945  35.514  1.00 44.14           N  
ANISOU 1066  N   GLU B  35     3663   4662   8446    585  -1845   -736       N  
ATOM   1067  CA  GLU B  35       5.083  17.815  36.693  1.00 49.50           C  
ANISOU 1067  CA  GLU B  35     4310   5147   9350    877  -2607   -997       C  
ATOM   1068  C   GLU B  35       5.565  19.159  37.234  1.00 50.78           C  
ANISOU 1068  C   GLU B  35     4114   5356   9824    824  -2696  -1268       C  
ATOM   1069  O   GLU B  35       6.097  20.001  36.510  1.00 50.65           O  
ANISOU 1069  O   GLU B  35     3517   5369  10360    665  -2233  -1516       O  
ATOM   1070  CB  GLU B  35       6.266  16.875  36.431  1.00 54.25           C  
ANISOU 1070  CB  GLU B  35     4521   5492  10600   1190  -2966  -1366       C  
ATOM   1071  CG  GLU B  35       6.889  16.294  37.716  1.00 62.26           C  
ANISOU 1071  CG  GLU B  35     5786   6232  11638   1617  -3984  -1542       C  
ATOM   1072  CD  GLU B  35       5.856  15.580  38.596  1.00 63.85           C  
ANISOU 1072  CD  GLU B  35     7018   6363  10880   1648  -4278  -1051       C  
ATOM   1073  OE1 GLU B  35       5.087  14.734  38.070  1.00 63.06           O  
ANISOU 1073  OE1 GLU B  35     7287   6265  10409   1519  -3915   -723       O  
ATOM   1074  OE2 GLU B  35       5.805  15.874  39.811  1.00 66.96           O  
ANISOU 1074  OE2 GLU B  35     7879   6675  10887   1772  -4826  -1024       O  
ATOM   1075  N   MET B  36       5.333  19.335  38.523  1.00 52.55           N  
ANISOU 1075  N   MET B  36     4773   5552   9642    933  -3248  -1216       N  
ATOM   1076  CA  MET B  36       5.809  20.490  39.264  1.00 55.69           C  
ANISOU 1076  CA  MET B  36     4906   5961  10291    936  -3500  -1521       C  
ATOM   1077  C   MET B  36       5.790  20.142  40.744  1.00 59.74           C  
ANISOU 1077  C   MET B  36     6059   6338  10300   1200  -4346  -1514       C  
ATOM   1078  O   MET B  36       5.102  19.202  41.159  1.00 60.07           O  
ANISOU 1078  O   MET B  36     6870   6302   9652   1258  -4506  -1155       O  
ATOM   1079  CB  MET B  36       4.931  21.721  38.981  1.00 50.70           C  
ANISOU 1079  CB  MET B  36     4279   5559   9426    564  -2831  -1317       C  
ATOM   1080  CG  MET B  36       3.476  21.601  39.410  1.00 47.01           C  
ANISOU 1080  CG  MET B  36     4541   5236   8085    401  -2660   -860       C  
ATOM   1081  SD  MET B  36       2.600  23.171  39.271  1.00 44.00           S  
ANISOU 1081  SD  MET B  36     4068   5057   7594     73  -2074   -766       S  
ATOM   1082  CE  MET B  36       3.607  24.206  40.353  1.00 47.97           C  
ANISOU 1082  CE  MET B  36     4274   5461   8493    173  -2572  -1233       C  
ATOM   1083  N   ASN B  37       6.556  20.888  41.529  1.00 64.66           N  
ANISOU 1083  N   ASN B  37     6419   6894  11255   1350  -4872  -1934       N  
ATOM   1084  CA  ASN B  37       6.490  20.794  42.975  1.00 69.26           C  
ANISOU 1084  CA  ASN B  37     7720   7352  11243   1581  -5665  -1943       C  
ATOM   1085  C   ASN B  37       5.344  21.635  43.493  1.00 65.78           C  
ANISOU 1085  C   ASN B  37     7780   7114  10100   1237  -5226  -1651       C  
ATOM   1086  O   ASN B  37       5.394  22.869  43.439  1.00 64.91           O  
ANISOU 1086  O   ASN B  37     7206   7147  10311   1037  -4934  -1860       O  
ATOM   1087  CB  ASN B  37       7.788  21.302  43.616  1.00 76.08           C  
ANISOU 1087  CB  ASN B  37     8059   8061  12786   1907  -6489  -2608       C  
ATOM   1088  CG  ASN B  37       8.852  20.225  43.751  1.00 83.86           C  
ANISOU 1088  CG  ASN B  37     8910   8732  14220   2432  -7381  -2941       C  
ATOM   1089  OD1 ASN B  37       8.729  19.127  43.191  1.00 84.22           O  
ANISOU 1089  OD1 ASN B  37     9132   8673  14195   2525  -7275  -2689       O  
ATOM   1090  ND2 ASN B  37       9.921  20.539  44.504  1.00 91.77           N  
ANISOU 1090  ND2 ASN B  37     9566   9557  15746   2809  -8326  -3570       N  
ATOM   1091  N   LEU B  38       4.302  20.971  43.975  1.00 64.84           N  
ANISOU 1091  N   LEU B  38     8588   6971   9078   1146  -5118  -1206       N  
ATOM   1092  CA  LEU B  38       3.322  21.644  44.798  1.00 64.21           C  
ANISOU 1092  CA  LEU B  38     9087   7001   8308    884  -4863  -1048       C  
ATOM   1093  C   LEU B  38       3.627  21.276  46.238  1.00 71.50           C  
ANISOU 1093  C   LEU B  38    10901   7665   8601   1168  -5709  -1130       C  
ATOM   1094  O   LEU B  38       3.844  20.098  46.556  1.00 75.20           O  
ANISOU 1094  O   LEU B  38    12001   7852   8720   1442  -6202   -981       O  
ATOM   1095  CB  LEU B  38       1.893  21.280  44.406  1.00 59.32           C  
ANISOU 1095  CB  LEU B  38     8876   6505   7158    524  -4063   -600       C  
ATOM   1096  CG  LEU B  38       1.362  22.051  43.200  1.00 53.15           C  
ANISOU 1096  CG  LEU B  38     7366   5998   6829    234  -3276   -548       C  
ATOM   1097  CD1 LEU B  38      -0.091  21.690  42.957  1.00 49.86           C  
ANISOU 1097  CD1 LEU B  38     7337   5683   5923    -72  -2632   -216       C  
ATOM   1098  CD2 LEU B  38       1.516  23.561  43.393  1.00 51.58           C  
ANISOU 1098  CD2 LEU B  38     6721   5929   6947    122  -3164   -814       C  
ATOM   1099  N   PRO B  39       3.692  22.288  47.113  1.00 74.29           N  
ANISOU 1099  N   PRO B  39    11363   8070   8794   1134  -5927  -1385       N  
ATOM   1100  CA  PRO B  39       4.023  21.939  48.484  1.00 81.86           C  
ANISOU 1100  CA  PRO B  39    13288   8753   9062   1442  -6806  -1482       C  
ATOM   1101  C   PRO B  39       2.799  21.333  49.170  1.00 82.36           C  
ANISOU 1101  C   PRO B  39    14618   8698   7976   1188  -6389  -1017       C  
ATOM   1102  O   PRO B  39       1.662  21.646  48.783  1.00 77.13           O  
ANISOU 1102  O   PRO B  39    13889   8249   7165    726  -5419   -787       O  
ATOM   1103  CB  PRO B  39       4.432  23.282  49.110  1.00 83.98           C  
ANISOU 1103  CB  PRO B  39    13212   9136   9559   1435  -7078  -1950       C  
ATOM   1104  CG  PRO B  39       3.842  24.350  48.251  1.00 76.69           C  
ANISOU 1104  CG  PRO B  39    11462   8537   9140    992  -6093  -1932       C  
ATOM   1105  CD  PRO B  39       3.464  23.737  46.920  1.00 71.55           C  
ANISOU 1105  CD  PRO B  39    10379   7982   8826    840  -5425  -1592       C  
ATOM   1106  N   GLY B  40       3.038  20.444  50.135  1.00 89.14           N  
ANISOU 1106  N   GLY B  40    16622   9173   8073   1495  -7105   -909       N  
ATOM   1107  CA  GLY B  40       1.966  19.898  50.970  1.00 91.35           C  
ANISOU 1107  CA  GLY B  40    18293   9239   7179   1224  -6689   -520       C  
ATOM   1108  C   GLY B  40       1.550  18.460  50.716  1.00 91.45           C  
ANISOU 1108  C   GLY B  40    19013   8945   6790   1209  -6477    -73       C  
ATOM   1109  O   GLY B  40       2.263  17.701  50.042  1.00 91.49           O  
ANISOU 1109  O   GLY B  40    18599   8830   7332   1549  -6919    -60       O  
ATOM   1110  N   ARG B  41       0.383  18.103  51.273  1.00 91.96           N  
ANISOU 1110  N   ARG B  41    20140   8853   5948    783  -5736    243       N  
ATOM   1111  CA  ARG B  41      -0.161  16.747  51.213  1.00 92.96           C  
ANISOU 1111  CA  ARG B  41    21148   8605   5567    669  -5402    663       C  
ATOM   1112  C   ARG B  41      -0.847  16.481  49.877  1.00 84.02           C  
ANISOU 1112  C   ARG B  41    19045   7754   5126    327  -4509    786       C  
ATOM   1113  O   ARG B  41      -1.584  17.347  49.345  1.00 77.80           O  
ANISOU 1113  O   ARG B  41    17438   7386   4735    -68  -3733    664       O  
ATOM   1114  CB  ARG B  41      -1.189  16.525  52.334  1.00 98.48           C  
ANISOU 1114  CB  ARG B  41    23357   8990   5071    249  -4786    879       C  
ATOM   1115  CG  ARG B  41      -0.634  16.555  53.750  1.00108.48           C  
ANISOU 1115  CG  ARG B  41    26015   9853   5349    578  -5646    839       C  
ATOM   1116  CD  ARG B  41      -0.090  15.188  54.161  1.00116.61           C  
ANISOU 1116  CD  ARG B  41    28311  10229   5765   1018  -6418   1157       C  
ATOM   1117  NE  ARG B  41       0.731  15.253  55.374  1.00127.62           N  
ANISOU 1117  NE  ARG B  41    30891  11240   6360   1545  -7617   1051       N  
ATOM   1118  CZ  ARG B  41       1.970  15.751  55.422  1.00129.22           C  
ANISOU 1118  CZ  ARG B  41    30413  11562   7125   2179  -8889    646       C  
ATOM   1119  NH1 ARG B  41       2.551  16.256  54.322  1.00121.20           N  
ANISOU 1119  NH1 ARG B  41    27549  11025   7475   2310  -9009    323       N  
ATOM   1120  NH2 ARG B  41       2.630  15.751  56.578  1.00138.71           N  
ANISOU 1120  NH2 ARG B  41    32817  12371   7517   2674 -10034    524       N  
ATOM   1121  N   TRP B  42      -0.614  15.270  49.357  1.00 83.37           N  
ANISOU 1121  N   TRP B  42    19113   7402   5163    510  -4675   1009       N  
ATOM   1122  CA  TRP B  42      -1.295  14.812  48.155  1.00 75.93           C  
ANISOU 1122  CA  TRP B  42    17465   6646   4739    203  -3887   1130       C  
ATOM   1123  C   TRP B  42      -1.806  13.389  48.313  1.00 79.54           C  
ANISOU 1123  C   TRP B  42    18952   6612   4656     75  -3608   1474       C  
ATOM   1124  O   TRP B  42      -1.443  12.692  49.262  1.00 86.37           O  
ANISOU 1124  O   TRP B  42    21079   6947   4792    318  -4147   1656       O  
ATOM   1125  CB  TRP B  42      -0.383  14.929  46.931  1.00 70.96           C  
ANISOU 1125  CB  TRP B  42    15522   6289   5149    531  -4264    943       C  
ATOM   1126  CG  TRP B  42       0.927  14.252  47.105  1.00 75.18           C  
ANISOU 1126  CG  TRP B  42    16224   6486   5856   1147  -5338    872       C  
ATOM   1127  CD1 TRP B  42       2.044  14.779  47.680  1.00 78.66           C  
ANISOU 1127  CD1 TRP B  42    16546   6876   6466   1607  -6301    567       C  
ATOM   1128  CD2 TRP B  42       1.272  12.926  46.692  1.00 76.83           C  
ANISOU 1128  CD2 TRP B  42    16679   6336   6177   1404  -5612   1036       C  
ATOM   1129  NE1 TRP B  42       3.067  13.865  47.658  1.00 84.48           N  
ANISOU 1129  NE1 TRP B  42    17408   7240   7450   2164  -7203    501       N  
ATOM   1130  CE2 TRP B  42       2.622  12.713  47.060  1.00 83.45           C  
ANISOU 1130  CE2 TRP B  42    17529   6905   7273   2056  -6792    807       C  
ATOM   1131  CE3 TRP B  42       0.571  11.890  46.058  1.00 74.95           C  
ANISOU 1131  CE3 TRP B  42    16633   5953   5891   1156  -5001   1304       C  
ATOM   1132  CZ2 TRP B  42       3.293  11.503  46.811  1.00 86.65           C  
ANISOU 1132  CZ2 TRP B  42    18137   6888   7899   2494  -7384    853       C  
ATOM   1133  CZ3 TRP B  42       1.240  10.684  45.806  1.00 78.94           C  
ANISOU 1133  CZ3 TRP B  42    17376   6044   6574   1557  -5543   1379       C  
ATOM   1134  CH2 TRP B  42       2.589  10.506  46.183  1.00 84.27           C  
ANISOU 1134  CH2 TRP B  42    18064   6444   7512   2231  -6726   1161       C  
ATOM   1135  N   LYS B  43      -2.669  12.972  47.390  1.00 74.38           N  
ANISOU 1135  N   LYS B  43    17814   6099   4346   -306  -2777   1545       N  
ATOM   1136  CA  LYS B  43      -3.207  11.609  47.370  1.00 77.67           C  
ANISOU 1136  CA  LYS B  43    19040   6056   4415   -492  -2391   1819       C  
ATOM   1137  C   LYS B  43      -3.071  11.030  45.960  1.00 72.35           C  
ANISOU 1137  C   LYS B  43    17376   5556   4558   -407  -2309   1789       C  
ATOM   1138  O   LYS B  43      -3.267  11.757  44.978  1.00 65.52           O  
ANISOU 1138  O   LYS B  43    15314   5215   4364   -515  -2011   1582       O  
ATOM   1139  CB  LYS B  43      -4.689  11.603  47.775  1.00 78.73           C  
ANISOU 1139  CB  LYS B  43    19699   6124   4090  -1197  -1235   1846       C  
ATOM   1140  CG  LYS B  43      -4.995  12.092  49.195  1.00 85.65           C  
ANISOU 1140  CG  LYS B  43    21714   6775   4055  -1399  -1084   1861       C  
ATOM   1141  CD  LYS B  43      -4.760  10.983  50.241  1.00 95.45           C  
ANISOU 1141  CD  LYS B  43    24738   7235   4292  -1290  -1357   2205       C  
ATOM   1142  CE  LYS B  43      -5.021  11.496  51.657  1.00104.19           C  
ANISOU 1142  CE  LYS B  43    27113   8097   4377  -1482  -1212   2211       C  
ATOM   1143  NZ  LYS B  43      -4.150  12.739  52.022  1.00102.82           N  
ANISOU 1143  NZ  LYS B  43    26459   8307   4299  -1050  -2100   1964       N  
ATOM   1144  N   PRO B  44      -2.743   9.725  45.850  1.00 76.21           N  
ANISOU 1144  N   PRO B  44    18430   5569   4956   -203  -2574   1990       N  
ATOM   1145  CA  PRO B  44      -2.658   9.086  44.535  1.00 71.99           C  
ANISOU 1145  CA  PRO B  44    17049   5160   5143   -150  -2443   1936       C  
ATOM   1146  C   PRO B  44      -4.039   8.998  43.912  1.00 68.69           C  
ANISOU 1146  C   PRO B  44    16292   4951   4857   -764  -1369   1884       C  
ATOM   1147  O   PRO B  44      -5.026   8.769  44.619  1.00 71.64           O  
ANISOU 1147  O   PRO B  44    17460   5072   4689  -1225   -711   1969       O  
ATOM   1148  CB  PRO B  44      -2.139   7.668  44.853  1.00 78.67           C  
ANISOU 1148  CB  PRO B  44    18866   5321   5705    164  -2924   2176       C  
ATOM   1149  CG  PRO B  44      -1.652   7.720  46.254  1.00 85.93           C  
ANISOU 1149  CG  PRO B  44    21012   5802   5834    443  -3582   2332       C  
ATOM   1150  CD  PRO B  44      -2.453   8.771  46.937  1.00 85.02           C  
ANISOU 1150  CD  PRO B  44    21087   5961   5258     -3  -3009   2278       C  
ATOM   1151  N   LYS B  45      -4.101   9.191  42.596  1.00 63.27           N  
ANISOU 1151  N   LYS B  45    14445   4697   4899   -771  -1192   1696       N  
ATOM   1152  CA  LYS B  45      -5.358   9.196  41.870  1.00 60.80           C  
ANISOU 1152  CA  LYS B  45    13641   4630   4828  -1261   -342   1550       C  
ATOM   1153  C   LYS B  45      -5.077   8.830  40.417  1.00 56.50           C  
ANISOU 1153  C   LYS B  45    12205   4318   4944  -1092   -420   1426       C  
ATOM   1154  O   LYS B  45      -3.960   9.016  39.924  1.00 54.49           O  
ANISOU 1154  O   LYS B  45    11476   4188   5039   -662   -997   1391       O  
ATOM   1155  CB  LYS B  45      -5.979  10.595  41.933  1.00 58.01           C  
ANISOU 1155  CB  LYS B  45    12723   4756   4564  -1492     -8   1349       C  
ATOM   1156  CG  LYS B  45      -7.490  10.606  41.970  1.00 60.76           C  
ANISOU 1156  CG  LYS B  45    13057   5145   4883  -2069    890   1173       C  
ATOM   1157  CD  LYS B  45      -8.017  11.885  41.353  1.00 59.44           C  
ANISOU 1157  CD  LYS B  45    11893   5533   5160  -2147   1080    895       C  
ATOM   1158  CE  LYS B  45      -9.511  11.784  41.065  1.00 62.79           C  
ANISOU 1158  CE  LYS B  45    12017   6022   5816  -2638   1868    589       C  
ATOM   1159  NZ  LYS B  45      -9.962  12.937  40.218  1.00 59.46           N  
ANISOU 1159  NZ  LYS B  45    10572   6109   5910  -2583   1876    312       N  
ATOM   1160  N   MET B  46      -6.084   8.299  39.736  1.00 55.76           N  
ANISOU 1160  N   MET B  46    11887   4259   5041  -1445    182   1305       N  
ATOM   1161  CA  MET B  46      -5.970   8.016  38.309  1.00 52.23           C  
ANISOU 1161  CA  MET B  46    10637   4062   5147  -1328    163   1144       C  
ATOM   1162  C   MET B  46      -7.092   8.686  37.530  1.00 48.56           C  
ANISOU 1162  C   MET B  46     9448   4036   4965  -1632    656    867       C  
ATOM   1163  O   MET B  46      -8.246   8.689  37.974  1.00 50.46           O  
ANISOU 1163  O   MET B  46     9866   4218   5090  -2054   1203    739       O  
ATOM   1164  CB  MET B  46      -5.904   6.514  38.050  1.00 56.02           C  
ANISOU 1164  CB  MET B  46    11531   4095   5661  -1324    200   1211       C  
ATOM   1165  CG  MET B  46      -4.570   5.910  38.465  1.00 60.44           C  
ANISOU 1165  CG  MET B  46    12567   4263   6136   -842   -501   1416       C  
ATOM   1166  SD  MET B  46      -4.263   4.297  37.764  1.00 69.14           S  
ANISOU 1166  SD  MET B  46    13838   4926   7506   -704   -570   1417       S  
ATOM   1167  CE  MET B  46      -4.452   3.260  39.222  1.00 74.85           C  
ANISOU 1167  CE  MET B  46    16079   4814   7545   -806   -560   1761       C  
ATOM   1168  N   ILE B  47      -6.739   9.293  36.395  1.00 43.43           N  
ANISOU 1168  N   ILE B  47     8017   3792   4694  -1408    459    743       N  
ATOM   1169  CA  ILE B  47      -7.713   9.960  35.552  1.00 40.84           C  
ANISOU 1169  CA  ILE B  47     7051   3849   4616  -1577    751    481       C  
ATOM   1170  C   ILE B  47      -7.594   9.458  34.123  1.00 39.48           C  
ANISOU 1170  C   ILE B  47     6440   3809   4750  -1436    679    343       C  
ATOM   1171  O   ILE B  47      -6.503   9.143  33.648  1.00 38.46           O  
ANISOU 1171  O   ILE B  47     6264   3631   4716  -1141    377    439       O  
ATOM   1172  CB  ILE B  47      -7.582  11.510  35.572  1.00 38.31           C  
ANISOU 1172  CB  ILE B  47     6325   3893   4340  -1460    619    460       C  
ATOM   1173  CG1 ILE B  47      -6.165  11.944  35.168  1.00 36.26           C  
ANISOU 1173  CG1 ILE B  47     5853   3724   4201  -1070    174    590       C  
ATOM   1174  CG2 ILE B  47      -7.993  12.063  36.951  1.00 41.00           C  
ANISOU 1174  CG2 ILE B  47     7063   4137   4378  -1675    795    499       C  
ATOM   1175  CD1 ILE B  47      -6.075  13.350  34.726  1.00 33.72           C  
ANISOU 1175  CD1 ILE B  47     5054   3735   4023   -973    129    530       C  
ATOM   1176  N   GLY B  48      -8.724   9.391  33.437  1.00 39.72           N  
ANISOU 1176  N   GLY B  48     6136   3995   4961  -1642    949     57       N  
ATOM   1177  CA  GLY B  48      -8.735   8.836  32.101  1.00 39.90           C  
ANISOU 1177  CA  GLY B  48     5845   4118   5197  -1529    876   -117       C  
ATOM   1178  C   GLY B  48      -9.072   9.849  31.037  1.00 38.45           C  
ANISOU 1178  C   GLY B  48     5148   4336   5124  -1381    746   -292       C  
ATOM   1179  O   GLY B  48      -9.907  10.747  31.231  1.00 38.76           O  
ANISOU 1179  O   GLY B  48     4962   4557   5209  -1474    811   -434       O  
ATOM   1180  N   GLY B  49      -8.444   9.691  29.885  1.00 37.33           N  
ANISOU 1180  N   GLY B  49     4874   4294   5016  -1142    570   -304       N  
ATOM   1181  CA  GLY B  49      -8.841  10.482  28.750  1.00 35.99           C  
ANISOU 1181  CA  GLY B  49     4404   4421   4847   -995    441   -469       C  
ATOM   1182  C   GLY B  49      -8.908   9.658  27.508  1.00 36.59           C  
ANISOU 1182  C   GLY B  49     4445   4508   4949   -917    388   -680       C  
ATOM   1183  O   GLY B  49      -9.142   8.454  27.558  1.00 38.03           O  
ANISOU 1183  O   GLY B  49     4710   4492   5248  -1067    503   -818       O  
ATOM   1184  N   ILE B  50      -8.683  10.325  26.381  1.00 35.58           N  
ANISOU 1184  N   ILE B  50     4270   4576   4674   -688    234   -705       N  
ATOM   1185  CA  ILE B  50      -8.599   9.662  25.106  1.00 36.94           C  
ANISOU 1185  CA  ILE B  50     4509   4766   4761   -579    178   -899       C  
ATOM   1186  C   ILE B  50      -7.258   8.904  25.143  1.00 36.91           C  
ANISOU 1186  C   ILE B  50     4649   4563   4813   -536    339   -738       C  
ATOM   1187  O   ILE B  50      -6.233   9.456  25.509  1.00 36.62           O  
ANISOU 1187  O   ILE B  50     4631   4492   4790   -446    393   -502       O  
ATOM   1188  CB  ILE B  50      -8.644  10.735  23.986  1.00 37.54           C  
ANISOU 1188  CB  ILE B  50     4679   5042   4542   -337     -3   -910       C  
ATOM   1189  CG1 ILE B  50      -9.795  10.500  23.024  1.00 38.79           C  
ANISOU 1189  CG1 ILE B  50     4806   5308   4624   -259   -293  -1300       C  
ATOM   1190  CG2 ILE B  50      -7.319  10.870  23.273  1.00 38.35           C  
ANISOU 1190  CG2 ILE B  50     5019   5095   4457   -202    177   -732       C  
ATOM   1191  CD1 ILE B  50     -10.076  11.691  22.144  1.00 39.15           C  
ANISOU 1191  CD1 ILE B  50     5054   5491   4330     20   -590  -1289       C  
ATOM   1192  N   GLY B  51      -7.243   7.636  24.795  1.00 38.89           N  
ANISOU 1192  N   GLY B  51     4954   4652   5172   -590    399   -917       N  
ATOM   1193  CA  GLY B  51      -5.960   6.904  24.851  1.00 39.32           C  
ANISOU 1193  CA  GLY B  51     5096   4476   5369   -503    507   -819       C  
ATOM   1194  C   GLY B  51      -5.688   6.160  26.158  1.00 38.97           C  
ANISOU 1194  C   GLY B  51     5166   4111   5530   -590    501   -659       C  
ATOM   1195  O   GLY B  51      -4.787   5.335  26.231  1.00 40.60           O  
ANISOU 1195  O   GLY B  51     5452   4054   5920   -483    494   -645       O  
ATOM   1196  N   GLY B  52      -6.469   6.452  27.189  1.00 37.67           N  
ANISOU 1196  N   GLY B  52     5064   3928   5320   -770    501   -558       N  
ATOM   1197  CA  GLY B  52      -6.383   5.711  28.431  1.00 38.56           C  
ANISOU 1197  CA  GLY B  52     5487   3677   5489   -886    527   -397       C  
ATOM   1198  C   GLY B  52      -6.192   6.576  29.647  1.00 36.80           C  
ANISOU 1198  C   GLY B  52     5396   3454   5134   -891    449   -132       C  
ATOM   1199  O   GLY B  52      -6.640   7.710  29.686  1.00 35.55           O  
ANISOU 1199  O   GLY B  52     5041   3583   4884   -930    462   -130       O  
ATOM   1200  N   PHE B  53      -5.454   6.050  30.612  1.00 38.00           N  
ANISOU 1200  N   PHE B  53     5912   3255   5271   -806    308     75       N  
ATOM   1201  CA APHE B  53      -5.358   6.643  31.938  0.50 37.75           C  
ANISOU 1201  CA APHE B  53     6175   3135   5035   -833    207    306       C  
ATOM   1202  CA BPHE B  53      -5.371   6.667  31.922  0.50 37.65           C  
ANISOU 1202  CA BPHE B  53     6151   3132   5023   -835    210    303       C  
ATOM   1203  C   PHE B  53      -3.955   7.123  32.298  1.00 37.31           C  
ANISOU 1203  C   PHE B  53     6074   3042   5063   -486   -186    440       C  
ATOM   1204  O   PHE B  53      -2.955   6.565  31.832  1.00 38.95           O  
ANISOU 1204  O   PHE B  53     6165   3102   5532   -227   -384    373       O  
ATOM   1205  CB APHE B  53      -5.793   5.615  32.986  0.50 41.38           C  
ANISOU 1205  CB APHE B  53     7297   3119   5307  -1036    328    429       C  
ATOM   1206  CB BPHE B  53      -5.933   5.703  32.982  0.50 41.13           C  
ANISOU 1206  CB BPHE B  53     7239   3123   5265  -1073    368    414       C  
ATOM   1207  CG APHE B  53      -4.744   4.579  33.293  0.50 44.51           C  
ANISOU 1207  CG APHE B  53     8102   3054   5756   -760      2    568       C  
ATOM   1208  CG BPHE B  53      -7.450   5.579  32.967  0.50 41.84           C  
ANISOU 1208  CG BPHE B  53     7302   3262   5335  -1514    852    210       C  
ATOM   1209  CD1APHE B  53      -4.695   3.387  32.579  0.50 46.49           C  
ANISOU 1209  CD1APHE B  53     8371   3067   6226   -739     72    438       C  
ATOM   1210  CD1BPHE B  53      -8.223   6.190  33.962  0.50 42.42           C  
ANISOU 1210  CD1BPHE B  53     7579   3339   5198  -1796   1114    238       C  
ATOM   1211  CD2APHE B  53      -3.801   4.800  34.296  0.50 46.69           C  
ANISOU 1211  CD2APHE B  53     8739   3111   5891   -482   -440    785       C  
ATOM   1212  CD2BPHE B  53      -8.100   4.845  31.974  0.50 41.42           C  
ANISOU 1212  CD2BPHE B  53     6983   3229   5523  -1653   1054    -85       C  
ATOM   1213  CE1APHE B  53      -3.729   2.422  32.859  0.50 50.71           C  
ANISOU 1213  CE1APHE B  53     9272   3126   6869   -438   -274    536       C  
ATOM   1214  CE1BPHE B  53      -9.621   6.085  33.959  0.50 43.78           C  
ANISOU 1214  CE1BPHE B  53     7613   3531   5490  -2221   1607    -63       C  
ATOM   1215  CE2APHE B  53      -2.822   3.851  34.577  0.50 51.32           C  
ANISOU 1215  CE2APHE B  53     9687   3230   6582   -145   -866    864       C  
ATOM   1216  CE2BPHE B  53      -9.496   4.731  31.959  0.50 43.56           C  
ANISOU 1216  CE2BPHE B  53     7112   3528   5909  -2053   1467   -391       C  
ATOM   1217  CZ APHE B  53      -2.791   2.654  33.862  0.50 53.23           C  
ANISOU 1217  CZ APHE B  53     9943   3211   7071   -118   -774    749       C  
ATOM   1218  CZ BPHE B  53     -10.258   5.347  32.950  0.50 44.41           C  
ANISOU 1218  CZ BPHE B  53     7349   3630   5894  -2344   1764   -399       C  
ATOM   1219  N   ILE B  54      -3.880   8.147  33.146  1.00 35.24           N  
ANISOU 1219  N   ILE B  54     5859   2890   4640   -486   -296    561       N  
ATOM   1220  CA  ILE B  54      -2.605   8.488  33.801  1.00 34.78           C  
ANISOU 1220  CA  ILE B  54     5834   2706   4675   -172   -742    638       C  
ATOM   1221  C   ILE B  54      -2.782   8.530  35.308  1.00 35.91           C  
ANISOU 1221  C   ILE B  54     6615   2599   4431   -222   -924    836       C  
ATOM   1222  O   ILE B  54      -3.852   8.811  35.812  1.00 35.94           O  
ANISOU 1222  O   ILE B  54     6870   2660   4124   -540   -598    894       O  
ATOM   1223  CB  ILE B  54      -1.978   9.798  33.299  1.00 31.74           C  
ANISOU 1223  CB  ILE B  54     4868   2667   4525    -53   -774    533       C  
ATOM   1224  CG1 ILE B  54      -2.920  10.992  33.554  1.00 29.84           C  
ANISOU 1224  CG1 ILE B  54     4559   2728   4049   -289   -542    582       C  
ATOM   1225  CG2 ILE B  54      -1.558   9.653  31.822  1.00 31.17           C  
ANISOU 1225  CG2 ILE B  54     4332   2736   4774     24   -580    340       C  
ATOM   1226  CD1 ILE B  54      -2.236  12.359  33.499  1.00 27.65           C  
ANISOU 1226  CD1 ILE B  54     3891   2667   3947   -177   -626    535       C  
ATOM   1227  N   LYS B  55      -1.712   8.229  36.031  1.00 35.30           N  
ANISOU 1227  N   LYS B  55     6823   2210   4379    111  -1464    896       N  
ATOM   1228  CA  LYS B  55      -1.621   8.348  37.495  1.00 38.02           C  
ANISOU 1228  CA  LYS B  55     7881   2281   4283    167  -1794   1076       C  
ATOM   1229  C   LYS B  55      -1.182   9.806  37.799  1.00 36.05           C  
ANISOU 1229  C   LYS B  55     7212   2365   4119    248  -1978    979       C  
ATOM   1230  O   LYS B  55      -0.273  10.361  37.153  1.00 38.17           O  
ANISOU 1230  O   LYS B  55     6784   2831   4889    468  -2162    775       O  
ATOM   1231  CB  LYS B  55      -0.598   7.388  38.037  1.00 46.75           C  
ANISOU 1231  CB  LYS B  55     9466   2878   5420    587  -2449   1128       C  
ATOM   1232  CG  LYS B  55      -1.030   5.872  38.070  1.00 54.06           C  
ANISOU 1232  CG  LYS B  55    11088   3304   6147    516  -2317   1287       C  
ATOM   1233  CD  LYS B  55       0.037   5.014  38.682  1.00 66.68           C  
ANISOU 1233  CD  LYS B  55    13229   4337   7768   1021  -3095   1345       C  
ATOM   1234  CE  LYS B  55       1.171   4.856  37.655  1.00 66.02           C  
ANISOU 1234  CE  LYS B  55    12237   4356   8492   1408  -3421   1014       C  
ATOM   1235  NZ  LYS B  55       2.068   3.839  38.073  1.00 72.53           N  
ANISOU 1235  NZ  LYS B  55    13505   4590   9462   1903  -4140   1003       N  
ATOM   1236  N   VAL B  56      -1.849  10.417  38.775  1.00 40.73           N  
ANISOU 1236  N   VAL B  56     8241   2989   4246     29  -1849   1089       N  
ATOM   1237  CA  VAL B  56      -1.642  11.812  39.113  1.00 39.55           C  
ANISOU 1237  CA  VAL B  56     7748   3140   4140     38  -1937    989       C  
ATOM   1238  C   VAL B  56      -1.541  11.941  40.624  1.00 44.69           C  
ANISOU 1238  C   VAL B  56     9210   3525   4244     94  -2292   1098       C  
ATOM   1239  O   VAL B  56      -1.900  11.017  41.362  1.00 48.99           O  
ANISOU 1239  O   VAL B  56    10663   3668   4282     29  -2298   1293       O  
ATOM   1240  CB  VAL B  56      -2.781  12.730  38.586  1.00 35.42           C  
ANISOU 1240  CB  VAL B  56     6804   3025   3631   -335  -1303    934       C  
ATOM   1241  CG1 VAL B  56      -2.795  12.789  37.036  1.00 31.57           C  
ANISOU 1241  CG1 VAL B  56     5582   2805   3608   -329  -1050    815       C  
ATOM   1242  CG2 VAL B  56      -4.139  12.313  39.131  1.00 36.22           C  
ANISOU 1242  CG2 VAL B  56     7461   3010   3290   -734   -803   1021       C  
ATOM   1243  N   ARG B  57      -1.008  13.064  41.078  1.00 44.33           N  
ANISOU 1243  N   ARG B  57     8907   3656   4279    218  -2591    961       N  
ATOM   1244  CA  ARG B  57      -1.036  13.390  42.502  1.00 48.58           C  
ANISOU 1244  CA  ARG B  57    10225   4006   4228    232  -2882   1021       C  
ATOM   1245  C   ARG B  57      -2.109  14.460  42.697  1.00 45.08           C  
ANISOU 1245  C   ARG B  57     9654   3880   3592   -189  -2253    983       C  
ATOM   1246  O   ARG B  57      -2.166  15.436  41.954  1.00 40.52           O  
ANISOU 1246  O   ARG B  57     8241   3681   3474   -256  -2026    829       O  
ATOM   1247  CB  ARG B  57       0.339  13.841  42.993  1.00 51.80           C  
ANISOU 1247  CB  ARG B  57    10463   4336   4881    698  -3754    810       C  
ATOM   1248  CG  ARG B  57       1.407  12.732  42.931  1.00 57.81           C  
ANISOU 1248  CG  ARG B  57    11374   4709   5882   1180  -4482    773       C  
ATOM   1249  CD  ARG B  57       2.804  13.268  43.231  1.00 63.60           C  
ANISOU 1249  CD  ARG B  57    11637   5409   7118   1656  -5353    404       C  
ATOM   1250  NE  ARG B  57       3.099  14.475  42.452  1.00 61.52           N  
ANISOU 1250  NE  ARG B  57    10243   5588   7543   1523  -5027    110       N  
ATOM   1251  CZ  ARG B  57       4.119  15.293  42.688  1.00 64.71           C  
ANISOU 1251  CZ  ARG B  57    10082   6049   8457   1771  -5539   -285       C  
ATOM   1252  NH1 ARG B  57       4.961  15.045  43.688  1.00 74.98           N  
ANISOU 1252  NH1 ARG B  57    11784   7026   9680   2222  -6522   -478       N  
ATOM   1253  NH2 ARG B  57       4.297  16.362  41.926  1.00 60.23           N  
ANISOU 1253  NH2 ARG B  57     8583   5819   8483   1576  -5088   -513       N  
ATOM   1254  N   GLN B  58      -3.005  14.227  43.645  1.00 48.05           N  
ANISOU 1254  N   GLN B  58    10895   4057   3306   -489  -1911   1110       N  
ATOM   1255  CA  GLN B  58      -4.096  15.140  43.889  1.00 46.30           C  
ANISOU 1255  CA  GLN B  58    10558   4083   2951   -900  -1267   1006       C  
ATOM   1256  C   GLN B  58      -3.759  16.042  45.072  1.00 49.80           C  
ANISOU 1256  C   GLN B  58    11409   4505   3007   -834  -1579    917       C  
ATOM   1257  O   GLN B  58      -3.554  15.561  46.195  1.00 55.00           O  
ANISOU 1257  O   GLN B  58    13119   4786   2991   -768  -1867   1036       O  
ATOM   1258  CB  GLN B  58      -5.402  14.386  44.131  1.00 48.42           C  
ANISOU 1258  CB  GLN B  58    11403   4151   2844  -1367   -507   1083       C  
ATOM   1259  CG  GLN B  58      -6.611  15.307  44.312  1.00 48.18           C  
ANISOU 1259  CG  GLN B  58    11106   4370   2831  -1801    210    863       C  
ATOM   1260  CD  GLN B  58      -7.886  14.581  44.707  1.00 54.43           C  
ANISOU 1260  CD  GLN B  58    12462   4903   3314  -2318   1037    824       C  
ATOM   1261  OE1 GLN B  58      -8.287  13.601  44.082  1.00 56.65           O  
ANISOU 1261  OE1 GLN B  58    12696   5054   3774  -2445   1307    859       O  
ATOM   1262  NE2 GLN B  58      -8.544  15.085  45.723  1.00 58.01           N  
ANISOU 1262  NE2 GLN B  58    13410   5273   3356  -2651   1503    693       N  
ATOM   1263  N   TYR B  59      -3.679  17.340  44.780  1.00 46.03           N  
ANISOU 1263  N   TYR B  59    10150   4398   2942   -833  -1546    707       N  
ATOM   1264  CA  TYR B  59      -3.466  18.392  45.758  1.00 48.98           C  
ANISOU 1264  CA  TYR B  59    10715   4821   3072   -818  -1753    543       C  
ATOM   1265  C   TYR B  59      -4.746  19.208  45.935  1.00 47.91           C  
ANISOU 1265  C   TYR B  59    10456   4885   2862  -1259   -973    407       C  
ATOM   1266  O   TYR B  59      -5.288  19.751  44.955  1.00 43.47           O  
ANISOU 1266  O   TYR B  59     9053   4614   2848  -1376   -583    312       O  
ATOM   1267  CB  TYR B  59      -2.345  19.329  45.293  1.00 46.42           C  
ANISOU 1267  CB  TYR B  59     9531   4717   3389   -491  -2281    337       C  
ATOM   1268  CG  TYR B  59      -0.966  18.715  45.258  1.00 48.86           C  
ANISOU 1268  CG  TYR B  59     9828   4823   3913    -25  -3116    309       C  
ATOM   1269  CD1 TYR B  59      -0.096  18.825  46.360  1.00 54.32           C  
ANISOU 1269  CD1 TYR B  59    11032   5296   4313    285  -3908    167       C  
ATOM   1270  CD2 TYR B  59      -0.513  18.050  44.124  1.00 45.09           C  
ANISOU 1270  CD2 TYR B  59     8802   4358   3971    132  -3156    355       C  
ATOM   1271  CE1 TYR B  59       1.176  18.268  46.321  1.00 57.26           C  
ANISOU 1271  CE1 TYR B  59    11293   5457   5008    769  -4762     43       C  
ATOM   1272  CE2 TYR B  59       0.750  17.491  44.075  1.00 48.76           C  
ANISOU 1272  CE2 TYR B  59     9154   4617   4755    567  -3897    241       C  
ATOM   1273  CZ  TYR B  59       1.593  17.609  45.177  1.00 55.22           C  
ANISOU 1273  CZ  TYR B  59    10405   5210   5365    900  -4725     67       C  
ATOM   1274  OH  TYR B  59       2.841  17.056  45.115  1.00 59.37           O  
ANISOU 1274  OH  TYR B  59    10723   5509   6324   1380  -5533   -136       O  
ATOM   1275  N   ASP B  60      -5.200  19.321  47.180  1.00 52.62           N  
ANISOU 1275  N   ASP B  60    11914   5295   2784  -1476   -777    365       N  
ATOM   1276  CA  ASP B  60      -6.428  20.038  47.499  1.00 52.86           C  
ANISOU 1276  CA  ASP B  60    11877   5455   2751  -1915     11    155       C  
ATOM   1277  C   ASP B  60      -6.164  21.455  47.991  1.00 52.62           C  
ANISOU 1277  C   ASP B  60    11556   5620   2817  -1855   -165   -102       C  
ATOM   1278  O   ASP B  60      -5.094  21.755  48.528  1.00 54.19           O  
ANISOU 1278  O   ASP B  60    11975   5757   2856  -1541   -877   -127       O  
ATOM   1279  CB  ASP B  60      -7.256  19.233  48.514  1.00 59.56           C  
ANISOU 1279  CB  ASP B  60    13885   5933   2812  -2310    587    213       C  
ATOM   1280  CG  ASP B  60      -7.641  17.846  47.978  1.00 61.22           C  
ANISOU 1280  CG  ASP B  60    14335   5912   3012  -2438    882    428       C  
ATOM   1281  OD1 ASP B  60      -7.971  17.727  46.775  1.00 57.81           O  
ANISOU 1281  OD1 ASP B  60    12991   5716   3260  -2442   1055    386       O  
ATOM   1282  OD2 ASP B  60      -7.595  16.872  48.749  1.00 70.05           O  
ANISOU 1282  OD2 ASP B  60    16614   6581   3420  -2521    917    636       O  
ATOM   1283  N   GLN B  61      -7.137  22.335  47.770  1.00 50.50           N  
ANISOU 1283  N   GLN B  61    10728   5570   2889  -2132    446   -344       N  
ATOM   1284  CA  GLN B  61      -7.080  23.696  48.280  1.00 51.05           C  
ANISOU 1284  CA  GLN B  61    10555   5784   3057  -2137    413   -623       C  
ATOM   1285  C   GLN B  61      -5.755  24.383  47.890  1.00 48.37           C  
ANISOU 1285  C   GLN B  61     9659   5572   3148  -1716   -360   -629       C  
ATOM   1286  O   GLN B  61      -5.055  24.963  48.722  1.00 50.81           O  
ANISOU 1286  O   GLN B  61    10239   5829   3236  -1582   -801   -781       O  
ATOM   1287  CB  GLN B  61      -7.349  23.707  49.793  1.00 58.07           C  
ANISOU 1287  CB  GLN B  61    12521   6439   3104  -2373    615   -748       C  
ATOM   1288  CG  GLN B  61      -8.564  22.858  50.171  1.00 62.83           C  
ANISOU 1288  CG  GLN B  61    13763   6824   3285  -2848   1488   -752       C  
ATOM   1289  CD  GLN B  61      -8.489  22.323  51.588  1.00 74.14           C  
ANISOU 1289  CD  GLN B  61    16663   7867   3640  -3012   1558   -688       C  
ATOM   1290  OE1 GLN B  61      -8.244  21.119  51.807  1.00 79.04           O  
ANISOU 1290  OE1 GLN B  61    18154   8155   3721  -2981   1423   -379       O  
ATOM   1291  NE2 GLN B  61      -8.700  23.216  52.565  1.00 77.45           N  
ANISOU 1291  NE2 GLN B  61    17449   8281   3698  -3181   1768   -982       N  
ATOM   1292  N   ILE B  62      -5.422  24.282  46.605  1.00 42.94           N  
ANISOU 1292  N   ILE B  62     8208   5025   3084  -1533   -486   -504       N  
ATOM   1293  CA  ILE B  62      -4.274  24.969  46.022  1.00 41.35           C  
ANISOU 1293  CA  ILE B  62     7349   4922   3442  -1225   -993   -561       C  
ATOM   1294  C   ILE B  62      -4.738  26.300  45.427  1.00 38.50           C  
ANISOU 1294  C   ILE B  62     6254   4748   3627  -1312   -644   -728       C  
ATOM   1295  O   ILE B  62      -5.734  26.343  44.723  1.00 35.78           O  
ANISOU 1295  O   ILE B  62     5613   4499   3482  -1453   -172   -692       O  
ATOM   1296  CB  ILE B  62      -3.607  24.102  44.904  1.00 38.81           C  
ANISOU 1296  CB  ILE B  62     6684   4591   3469  -1001  -1234   -349       C  
ATOM   1297  CG1 ILE B  62      -2.953  22.838  45.485  1.00 43.37           C  
ANISOU 1297  CG1 ILE B  62     7956   4922   3601   -819  -1727   -209       C  
ATOM   1298  CG2 ILE B  62      -2.598  24.911  44.092  1.00 37.23           C  
ANISOU 1298  CG2 ILE B  62     5700   4481   3964   -792  -1486   -461       C  
ATOM   1299  CD1 ILE B  62      -1.772  23.100  46.434  1.00 47.79           C  
ANISOU 1299  CD1 ILE B  62     8788   5337   4032   -532  -2498   -397       C  
ATOM   1300  N   LEU B  63      -4.007  27.377  45.697  1.00 29.24           N  
ANISOU 1300  N   LEU B  63     3791   5000   2320  -1398   -207   -275       N  
ATOM   1301  CA  LEU B  63      -4.301  28.687  45.109  1.00 29.51           C  
ANISOU 1301  CA  LEU B  63     3657   4968   2586  -1123    -90   -545       C  
ATOM   1302  C   LEU B  63      -3.714  28.791  43.715  1.00 28.41           C  
ANISOU 1302  C   LEU B  63     3534   4528   2732   -812   -189   -395       C  
ATOM   1303  O   LEU B  63      -2.510  28.522  43.523  1.00 27.83           O  
ANISOU 1303  O   LEU B  63     3557   4309   2709   -774   -319   -190       O  
ATOM   1304  CB  LEU B  63      -3.741  29.828  45.992  1.00 31.26           C  
ANISOU 1304  CB  LEU B  63     3863   5253   2763  -1177    -57   -726       C  
ATOM   1305  CG  LEU B  63      -3.832  31.256  45.408  1.00 30.85           C  
ANISOU 1305  CG  LEU B  63     3694   5037   2993   -890    -22   -971       C  
ATOM   1306  CD1 LEU B  63      -5.286  31.713  45.227  1.00 32.84           C  
ANISOU 1306  CD1 LEU B  63     3731   5382   3364   -792    105  -1325       C  
ATOM   1307  CD2 LEU B  63      -3.056  32.259  46.232  1.00 33.79           C  
ANISOU 1307  CD2 LEU B  63     4095   5419   3323   -957    -24  -1097       C  
ATOM   1308  N   ILE B  64      -4.533  29.210  42.748  1.00 28.44           N  
ANISOU 1308  N   ILE B  64     3431   4456   2918   -615   -140   -518       N  
ATOM   1309  CA  ILE B  64      -4.047  29.455  41.367  1.00 28.62           C  
ANISOU 1309  CA  ILE B  64     3488   4226   3160   -396   -229   -393       C  
ATOM   1310  C   ILE B  64      -4.593  30.780  40.895  1.00 28.98           C  
ANISOU 1310  C   ILE B  64     3454   4160   3398   -223   -246   -595       C  
ATOM   1311  O   ILE B  64      -5.725  31.139  41.214  1.00 30.79           O  
ANISOU 1311  O   ILE B  64     3537   4490   3670   -190   -186   -844       O  
ATOM   1312  CB  ILE B  64      -4.550  28.428  40.304  1.00 28.57           C  
ANISOU 1312  CB  ILE B  64     3487   4172   3197   -352   -241   -257       C  
ATOM   1313  CG1 ILE B  64      -4.342  26.990  40.691  1.00 31.34           C  
ANISOU 1313  CG1 ILE B  64     3917   4584   3406   -509   -267    -82       C  
ATOM   1314  CG2 ILE B  64      -3.801  28.585  38.948  1.00 27.04           C  
ANISOU 1314  CG2 ILE B  64     3350   3772   3152   -226   -317   -127       C  
ATOM   1315  CD1 ILE B  64      -4.298  26.114  39.367  1.00 33.20           C  
ANISOU 1315  CD1 ILE B  64     4180   4680   3755   -418   -307     56       C  
ATOM   1316  N   GLU B  65      -3.787  31.516  40.154  1.00 28.75           N  
ANISOU 1316  N   GLU B  65     3513   3920   3492   -131   -349   -507       N  
ATOM   1317  CA  GLU B  65      -4.278  32.739  39.563  1.00 31.26           C  
ANISOU 1317  CA  GLU B  65     3815   4047   4015     17   -458   -635       C  
ATOM   1318  C   GLU B  65      -4.381  32.467  38.077  1.00 30.47           C  
ANISOU 1318  C   GLU B  65     3788   3802   3986     62   -558   -445       C  
ATOM   1319  O   GLU B  65      -3.412  32.041  37.464  1.00 28.59           O  
ANISOU 1319  O   GLU B  65     3653   3538   3672    -25   -558   -252       O  
ATOM   1320  CB  GLU B  65      -3.355  33.910  39.867  1.00 33.09           C  
ANISOU 1320  CB  GLU B  65     4142   4139   4294      8   -535   -673       C  
ATOM   1321  CG  GLU B  65      -4.041  35.238  39.752  1.00 39.06           C  
ANISOU 1321  CG  GLU B  65     4868   4685   5289    158   -679   -889       C  
ATOM   1322  CD  GLU B  65      -3.157  36.360  40.233  1.00 45.84           C  
ANISOU 1322  CD  GLU B  65     5832   5407   6177    117   -747   -950       C  
ATOM   1323  OE1 GLU B  65      -1.920  36.162  40.229  1.00 48.88           O  
ANISOU 1323  OE1 GLU B  65     6337   5831   6405    -30   -714   -757       O  
ATOM   1324  OE2 GLU B  65      -3.688  37.430  40.609  1.00 50.48           O  
ANISOU 1324  OE2 GLU B  65     6367   5846   6968    236   -844  -1219       O  
ATOM   1325  N   ILE B  66      -5.575  32.648  37.524  1.00 31.89           N  
ANISOU 1325  N   ILE B  66     3887   3923   4307    178   -638   -533       N  
ATOM   1326  CA  ILE B  66      -5.838  32.281  36.130  1.00 32.30           C  
ANISOU 1326  CA  ILE B  66     4009   3877   4385    177   -737   -350       C  
ATOM   1327  C   ILE B  66      -6.233  33.556  35.439  1.00 35.07           C  
ANISOU 1327  C   ILE B  66     4426   3951   4949    278  -1006   -373       C  
ATOM   1328  O   ILE B  66      -7.277  34.137  35.734  1.00 36.15           O  
ANISOU 1328  O   ILE B  66     4417   4021   5296    449  -1113   -596       O  
ATOM   1329  CB  ILE B  66      -6.963  31.214  36.009  1.00 32.23           C  
ANISOU 1329  CB  ILE B  66     3862   4039   4347    194   -649   -389       C  
ATOM   1330  CG1 ILE B  66      -6.552  29.918  36.699  1.00 31.14           C  
ANISOU 1330  CG1 ILE B  66     3716   4114   4003     59   -452   -326       C  
ATOM   1331  CG2 ILE B  66      -7.366  30.960  34.534  1.00 31.95           C  
ANISOU 1331  CG2 ILE B  66     3894   3899   4345    185   -775   -225       C  
ATOM   1332  CD1 ILE B  66      -7.746  29.107  37.176  1.00 34.89           C  
ANISOU 1332  CD1 ILE B  66     4043   4800   4414     22   -345   -447       C  
ATOM   1333  N   CYS B  67      -5.349  34.009  34.556  1.00 36.58           N  
ANISOU 1333  N   CYS B  67     4833   3977   5088    148  -1133   -162       N  
ATOM   1334  CA  CYS B  67      -5.526  35.240  33.806  1.00 40.26           C  
ANISOU 1334  CA  CYS B  67     5459   4124   5713    160  -1462    -96       C  
ATOM   1335  C   CYS B  67      -5.966  36.373  34.748  1.00 41.96           C  
ANISOU 1335  C   CYS B  67     5589   4166   6189    363  -1597   -361       C  
ATOM   1336  O   CYS B  67      -6.817  37.199  34.403  1.00 44.66           O  
ANISOU 1336  O   CYS B  67     5923   4237   6810    521  -1907   -443       O  
ATOM   1337  CB  CYS B  67      -6.518  35.014  32.649  1.00 41.21           C  
ANISOU 1337  CB  CYS B  67     5597   4159   5904    177  -1658     15       C  
ATOM   1338  SG  CYS B  67      -6.467  36.289  31.380  1.00 52.19           S  
ANISOU 1338  SG  CYS B  67     7305   5141   7384     42  -2140    254       S  
ATOM   1339  N   GLY B  68      -5.379  36.403  35.949  1.00 40.61           N  
ANISOU 1339  N   GLY B  68     5343   4143   5946    358  -1386   -518       N  
ATOM   1340  CA  GLY B  68      -5.648  37.468  36.915  1.00 42.46           C  
ANISOU 1340  CA  GLY B  68     5490   4248   6396    509  -1464   -820       C  
ATOM   1341  C   GLY B  68      -6.852  37.237  37.818  1.00 43.41           C  
ANISOU 1341  C   GLY B  68     5285   4554   6655    691  -1334  -1203       C  
ATOM   1342  O   GLY B  68      -7.239  38.134  38.581  1.00 46.87           O  
ANISOU 1342  O   GLY B  68     5591   4902   7317    833  -1392  -1550       O  
ATOM   1343  N   HIS B  69      -7.454  36.054  37.725  1.00 40.48           N  
ANISOU 1343  N   HIS B  69     4774   4454   6153    662  -1156  -1177       N  
ATOM   1344  CA  HIS B  69      -8.560  35.658  38.590  1.00 40.99           C  
ANISOU 1344  CA  HIS B  69     4523   4793   6258    733   -976  -1537       C  
ATOM   1345  C   HIS B  69      -8.049  34.585  39.529  1.00 38.30           C  
ANISOU 1345  C   HIS B  69     4177   4819   5556    499   -649  -1485       C  
ATOM   1346  O   HIS B  69      -7.590  33.542  39.079  1.00 35.74           O  
ANISOU 1346  O   HIS B  69     3978   4579   5022    367   -577  -1178       O  
ATOM   1347  CB  HIS B  69      -9.709  35.053  37.771  1.00 41.26           C  
ANISOU 1347  CB  HIS B  69     4418   4870   6387    821  -1046  -1527       C  
ATOM   1348  CG  HIS B  69     -10.485  36.053  36.975  1.00 45.32           C  
ANISOU 1348  CG  HIS B  69     4880   5036   7303   1069  -1425  -1630       C  
ATOM   1349  ND1 HIS B  69      -9.957  36.704  35.881  1.00 46.21           N  
ANISOU 1349  ND1 HIS B  69     5286   4766   7505   1069  -1761  -1311       N  
ATOM   1350  CD2 HIS B  69     -11.757  36.506  37.111  1.00 47.91           C  
ANISOU 1350  CD2 HIS B  69     4891   5335   7978   1306  -1559  -2023       C  
ATOM   1351  CE1 HIS B  69     -10.864  37.533  35.391  1.00 50.49           C  
ANISOU 1351  CE1 HIS B  69     5736   5008   8441   1302  -2137  -1458       C  
ATOM   1352  NE2 HIS B  69     -11.967  37.424  36.113  1.00 51.24           N  
ANISOU 1352  NE2 HIS B  69     5434   5304   8732   1484  -2024  -1910       N  
ATOM   1353  N   LYS B  70      -8.158  34.827  40.827  1.00 38.81           N  
ANISOU 1353  N   LYS B  70     4097   5092   5555    431   -479  -1800       N  
ATOM   1354  CA  LYS B  70      -7.756  33.849  41.839  1.00 37.28           C  
ANISOU 1354  CA  LYS B  70     3924   5244   4998    154   -227  -1744       C  
ATOM   1355  C   LYS B  70      -8.827  32.769  42.072  1.00 37.35           C  
ANISOU 1355  C   LYS B  70     3760   5575   4856     26    -59  -1844       C  
ATOM   1356  O   LYS B  70     -10.013  33.072  42.118  1.00 39.57           O  
ANISOU 1356  O   LYS B  70     3774   5955   5305    127    -31  -2200       O  
ATOM   1357  CB  LYS B  70      -7.443  34.580  43.151  1.00 39.19           C  
ANISOU 1357  CB  LYS B  70     4107   5612   5171     51   -117  -2041       C  
ATOM   1358  CG  LYS B  70      -6.253  35.508  43.048  1.00 39.98           C  
ANISOU 1358  CG  LYS B  70     4407   5432   5350    104   -261  -1908       C  
ATOM   1359  CD  LYS B  70      -5.978  36.191  44.374  1.00 44.19           C  
ANISOU 1359  CD  LYS B  70     4880   6111   5798    -22   -141  -2220       C  
ATOM   1360  CE  LYS B  70      -5.256  37.507  44.189  1.00 49.10           C  
ANISOU 1360  CE  LYS B  70     5629   6392   6636    108   -324  -2252       C  
ATOM   1361  NZ  LYS B  70      -3.970  37.284  43.493  1.00 48.05           N  
ANISOU 1361  NZ  LYS B  70     5768   6095   6396     43   -436  -1786       N  
ATOM   1362  N   ALA B  71      -8.392  31.521  42.221  1.00 34.83           N  
ANISOU 1362  N   ALA B  71     3587   5407   4240   -202     27  -1547       N  
ATOM   1363  CA  ALA B  71      -9.259  30.404  42.570  1.00 35.10           C  
ANISOU 1363  CA  ALA B  71     3530   5750   4057   -420    176  -1588       C  
ATOM   1364  C   ALA B  71      -8.498  29.514  43.531  1.00 34.87           C  
ANISOU 1364  C   ALA B  71     3689   5892   3668   -756    243  -1373       C  
ATOM   1365  O   ALA B  71      -7.268  29.486  43.522  1.00 32.89           O  
ANISOU 1365  O   ALA B  71     3639   5466   3393   -746    137  -1108       O  
ATOM   1366  CB  ALA B  71      -9.661  29.618  41.311  1.00 33.45           C  
ANISOU 1366  CB  ALA B  71     3359   5423   3928   -320     91  -1354       C  
ATOM   1367  N   ILE B  72      -9.221  28.825  44.400  1.00 36.24           N  
ANISOU 1367  N   ILE B  72     3795   6416   3557  -1083    397  -1502       N  
ATOM   1368  CA  ILE B  72      -8.631  27.819  45.267  1.00 36.93           C  
ANISOU 1368  CA  ILE B  72     4111   6640   3280  -1462    384  -1237       C  
ATOM   1369  C   ILE B  72      -9.368  26.532  44.979  1.00 37.73           C  
ANISOU 1369  C   ILE B  72     4257   6852   3224  -1655    397  -1087       C  
ATOM   1370  O   ILE B  72     -10.610  26.492  44.976  1.00 38.87           O  
ANISOU 1370  O   ILE B  72     4183   7252   3334  -1740    554  -1373       O  
ATOM   1371  CB  ILE B  72      -8.698  28.190  46.777  1.00 40.55           C  
ANISOU 1371  CB  ILE B  72     4529   7447   3431  -1830    531  -1496       C  
ATOM   1372  CG1 ILE B  72      -7.671  29.280  47.103  1.00 39.58           C  
ANISOU 1372  CG1 ILE B  72     4446   7164   3428  -1678    471  -1543       C  
ATOM   1373  CG2 ILE B  72      -8.389  26.982  47.658  1.00 42.42           C  
ANISOU 1373  CG2 ILE B  72     5027   7857   3235  -2321    469  -1194       C  
ATOM   1374  CD1 ILE B  72      -7.704  29.752  48.541  1.00 42.02           C  
ANISOU 1374  CD1 ILE B  72     4708   7817   3442  -2039    624  -1836       C  
ATOM   1375  N   GLY B  73      -8.619  25.485  44.663  1.00 35.93           N  
ANISOU 1375  N   GLY B  73     4290   6416   2946  -1703    218   -668       N  
ATOM   1376  CA  GLY B  73      -9.278  24.222  44.385  1.00 35.86           C  
ANISOU 1376  CA  GLY B  73     4362   6465   2797  -1901    199   -511       C  
ATOM   1377  C   GLY B  73      -8.279  23.121  44.229  1.00 34.61           C  
ANISOU 1377  C   GLY B  73     4500   6026   2624  -1947    -51    -83       C  
ATOM   1378  O   GLY B  73      -7.083  23.299  44.475  1.00 33.50           O  
ANISOU 1378  O   GLY B  73     4478   5698   2552  -1863   -205     75       O  
ATOM   1379  N   THR B  74      -8.794  21.980  43.814  1.00 34.98           N  
ANISOU 1379  N   THR B  74     4643   6039   2609  -2076   -105     72       N  
ATOM   1380  CA  THR B  74      -7.986  20.803  43.587  1.00 34.59           C  
ANISOU 1380  CA  THR B  74     4857   5679   2608  -2100   -377    432       C  
ATOM   1381  C   THR B  74      -7.170  20.904  42.318  1.00 31.62           C  
ANISOU 1381  C   THR B  74     4434   4963   2618  -1652   -458    494       C  
ATOM   1382  O   THR B  74      -7.678  21.210  41.205  1.00 30.23           O  
ANISOU 1382  O   THR B  74     4103   4764   2618  -1415   -333    367       O  
ATOM   1383  CB  THR B  74      -8.872  19.544  43.549  1.00 36.55           C  
ANISOU 1383  CB  THR B  74     5238   5987   2664  -2414   -415    554       C  
ATOM   1384  OG1 THR B  74      -9.399  19.331  44.850  1.00 39.63           O  
ANISOU 1384  OG1 THR B  74     5733   6700   2625  -2944   -381    545       O  
ATOM   1385  CG2 THR B  74      -8.079  18.300  43.117  1.00 36.11           C  
ANISOU 1385  CG2 THR B  74     5435   5521   2765  -2361   -736    886       C  
ATOM   1386  N   VAL B  75      -5.893  20.620  42.479  1.00 31.28           N  
ANISOU 1386  N   VAL B  75     4519   4670   2697  -1569   -684    679       N  
ATOM   1387  CA  VAL B  75      -5.010  20.511  41.337  1.00 29.52           C  
ANISOU 1387  CA  VAL B  75     4246   4159   2812  -1221   -762    708       C  
ATOM   1388  C   VAL B  75      -4.405  19.115  41.286  1.00 30.82           C  
ANISOU 1388  C   VAL B  75     4585   4035   3090  -1258  -1054    924       C  
ATOM   1389  O   VAL B  75      -3.864  18.612  42.283  1.00 32.63           O  
ANISOU 1389  O   VAL B  75     4987   4174   3237  -1442  -1313   1107       O  
ATOM   1390  CB  VAL B  75      -3.916  21.585  41.389  1.00 27.91           C  
ANISOU 1390  CB  VAL B  75     3947   3910   2746  -1018   -759    634       C  
ATOM   1391  CG1 VAL B  75      -2.940  21.429  40.239  1.00 26.57           C  
ANISOU 1391  CG1 VAL B  75     3704   3506   2885   -736   -818    623       C  
ATOM   1392  CG2 VAL B  75      -4.549  22.958  41.395  1.00 28.08           C  
ANISOU 1392  CG2 VAL B  75     3818   4144   2709   -964   -524    412       C  
ATOM   1393  N   LEU B  76      -4.529  18.493  40.118  1.00 30.40           N  
ANISOU 1393  N   LEU B  76     4491   3824   3235  -1094  -1039    893       N  
ATOM   1394  CA  LEU B  76      -3.882  17.228  39.814  1.00 31.90           C  
ANISOU 1394  CA  LEU B  76     4790   3682   3649  -1035  -1314   1007       C  
ATOM   1395  C   LEU B  76      -2.540  17.483  39.126  1.00 31.12           C  
ANISOU 1395  C   LEU B  76     4524   3404   3896   -708  -1364    879       C  
ATOM   1396  O   LEU B  76      -2.442  18.323  38.236  1.00 28.88           O  
ANISOU 1396  O   LEU B  76     4062   3233   3679   -540  -1126    699       O  
ATOM   1397  CB  LEU B  76      -4.788  16.414  38.887  1.00 31.93           C  
ANISOU 1397  CB  LEU B  76     4816   3646   3672  -1063  -1235    979       C  
ATOM   1398  CG  LEU B  76      -5.895  15.516  39.447  1.00 35.54           C  
ANISOU 1398  CG  LEU B  76     5483   4158   3863  -1423  -1306   1136       C  
ATOM   1399  CD1 LEU B  76      -6.490  15.907  40.826  1.00 37.54           C  
ANISOU 1399  CD1 LEU B  76     5841   4701   3722  -1795  -1279   1226       C  
ATOM   1400  CD2 LEU B  76      -6.994  15.298  38.405  1.00 34.83           C  
ANISOU 1400  CD2 LEU B  76     5313   4182   3739  -1424  -1084   1022       C  
ATOM   1401  N   VAL B  77      -1.513  16.746  39.528  1.00 32.90           N  
ANISOU 1401  N   VAL B  77     4806   3351   4343   -644  -1698    960       N  
ATOM   1402  CA  VAL B  77      -0.189  16.869  38.924  1.00 33.19           C  
ANISOU 1402  CA  VAL B  77     4630   3242   4737   -350  -1757    775       C  
ATOM   1403  C   VAL B  77       0.257  15.515  38.376  1.00 35.50           C  
ANISOU 1403  C   VAL B  77     4913   3184   5391   -209  -2015    711       C  
ATOM   1404  O   VAL B  77       0.236  14.513  39.090  1.00 38.05           O  
ANISOU 1404  O   VAL B  77     5444   3241   5772   -312  -2388    913       O  
ATOM   1405  CB  VAL B  77       0.855  17.349  39.949  1.00 35.31           C  
ANISOU 1405  CB  VAL B  77     4884   3491   5040   -337  -1965    846       C  
ATOM   1406  CG1 VAL B  77       2.234  17.551  39.267  1.00 36.23           C  
ANISOU 1406  CG1 VAL B  77     4716   3521   5527    -46  -1984    590       C  
ATOM   1407  CG2 VAL B  77       0.394  18.662  40.599  1.00 33.83           C  
ANISOU 1407  CG2 VAL B  77     4721   3630   4502   -495  -1726    882       C  
ATOM   1408  N   GLY B  78       0.670  15.485  37.118  1.00 33.98           N  
ANISOU 1408  N   GLY B  78     4487   2982   5440     -1  -1838    417       N  
ATOM   1409  CA  GLY B  78       1.131  14.242  36.505  1.00 36.31           C  
ANISOU 1409  CA  GLY B  78     4712   2954   6130    161  -2047    249       C  
ATOM   1410  C   GLY B  78       1.440  14.411  35.032  1.00 34.99           C  
ANISOU 1410  C   GLY B  78     4265   2911   6118    302  -1732   -134       C  
ATOM   1411  O   GLY B  78       1.392  15.530  34.519  1.00 32.84           O  
ANISOU 1411  O   GLY B  78     3883   2955   5641    257  -1397   -221       O  
ATOM   1412  N   PRO B  79       1.724  13.291  34.335  1.00 37.24           N  
ANISOU 1412  N   PRO B  79     4454   2942   6753    435  -1851   -370       N  
ATOM   1413  CA  PRO B  79       2.213  13.325  32.957  1.00 36.78           C  
ANISOU 1413  CA  PRO B  79     4092   3013   6868    534  -1568   -813       C  
ATOM   1414  C   PRO B  79       1.130  13.612  31.926  1.00 34.32           C  
ANISOU 1414  C   PRO B  79     3848   2961   6231    344  -1194   -824       C  
ATOM   1415  O   PRO B  79       0.954  12.832  30.991  1.00 35.19           O  
ANISOU 1415  O   PRO B  79     3892   3000   6476    349  -1119  -1060       O  
ATOM   1416  CB  PRO B  79       2.810  11.924  32.757  1.00 41.31           C  
ANISOU 1416  CB  PRO B  79     4554   3180   7964    743  -1885  -1076       C  
ATOM   1417  CG  PRO B  79       2.080  11.057  33.695  1.00 42.74           C  
ANISOU 1417  CG  PRO B  79     5098   3022   8118    662  -2270   -683       C  
ATOM   1418  CD  PRO B  79       1.653  11.912  34.862  1.00 39.81           C  
ANISOU 1418  CD  PRO B  79     4961   2823   7342    474  -2299   -249       C  
ATOM   1419  N   THR B  80       0.406  14.712  32.110  1.00 30.54           N  
ANISOU 1419  N   THR B  80     3493   2761   5350    182   -993   -585       N  
ATOM   1420  CA  THR B  80      -0.472  15.226  31.072  1.00 29.31           C  
ANISOU 1420  CA  THR B  80     3359   2867   4911     19   -674   -608       C  
ATOM   1421  C   THR B  80       0.432  15.914  30.024  1.00 30.41           C  
ANISOU 1421  C   THR B  80     3249   3229   5076      1   -430   -934       C  
ATOM   1422  O   THR B  80       1.459  16.511  30.390  1.00 30.38           O  
ANISOU 1422  O   THR B  80     3102   3276   5163     74   -452  -1023       O  
ATOM   1423  CB  THR B  80      -1.504  16.230  31.648  1.00 26.88           C  
ANISOU 1423  CB  THR B  80     3228   2749   4238   -114   -597   -291       C  
ATOM   1424  OG1 THR B  80      -2.196  16.864  30.577  1.00 24.23           O  
ANISOU 1424  OG1 THR B  80     2882   2640   3685   -243   -351   -329       O  
ATOM   1425  CG2 THR B  80      -0.834  17.303  32.532  1.00 23.83           C  
ANISOU 1425  CG2 THR B  80     2808   2441   3804    -67   -635   -207       C  
ATOM   1426  N   PRO B  81       0.085  15.806  28.729  1.00 30.78           N  
ANISOU 1426  N   PRO B  81     3247   3430   5020   -143   -201  -1120       N  
ATOM   1427  CA  PRO B  81       0.958  16.480  27.759  1.00 31.98           C  
ANISOU 1427  CA  PRO B  81     3188   3841   5122   -263     35  -1425       C  
ATOM   1428  C   PRO B  81       0.833  18.010  27.761  1.00 30.01           C  
ANISOU 1428  C   PRO B  81     3032   3826   4546   -423    145  -1217       C  
ATOM   1429  O   PRO B  81       1.639  18.677  27.144  1.00 30.51           O  
ANISOU 1429  O   PRO B  81     2959   4100   4532   -570    301  -1417       O  
ATOM   1430  CB  PRO B  81       0.485  15.905  26.413  1.00 32.60           C  
ANISOU 1430  CB  PRO B  81     3241   4028   5116   -446    228  -1643       C  
ATOM   1431  CG  PRO B  81      -0.862  15.495  26.630  1.00 31.01           C  
ANISOU 1431  CG  PRO B  81     3284   3711   4789   -462    137  -1339       C  
ATOM   1432  CD  PRO B  81      -0.989  15.049  28.055  1.00 30.87           C  
ANISOU 1432  CD  PRO B  81     3377   3410   4940   -251   -147  -1096       C  
ATOM   1433  N   VAL B  82      -0.167  18.548  28.462  1.00 28.25           N  
ANISOU 1433  N   VAL B  82     3029   3564   4142   -412     52   -848       N  
ATOM   1434  CA  VAL B  82      -0.550  19.955  28.363  1.00 27.46           C  
ANISOU 1434  CA  VAL B  82     3043   3623   3769   -547    111   -656       C  
ATOM   1435  C   VAL B  82      -1.156  20.321  29.708  1.00 25.35           C  
ANISOU 1435  C   VAL B  82     2903   3249   3480   -412    -45   -378       C  
ATOM   1436  O   VAL B  82      -1.920  19.521  30.247  1.00 25.45           O  
ANISOU 1436  O   VAL B  82     2993   3149   3529   -347   -137   -268       O  
ATOM   1437  CB  VAL B  82      -1.623  20.104  27.217  1.00 28.84           C  
ANISOU 1437  CB  VAL B  82     3334   3915   3711   -755    204   -587       C  
ATOM   1438  CG1 VAL B  82      -2.354  21.421  27.274  1.00 29.21           C  
ANISOU 1438  CG1 VAL B  82     3533   4017   3549   -831    146   -335       C  
ATOM   1439  CG2 VAL B  82      -0.954  19.920  25.836  1.00 33.06           C  
ANISOU 1439  CG2 VAL B  82     3755   4628   4178   -994    390   -881       C  
ATOM   1440  N   ASN B  83      -0.777  21.469  30.273  1.00 22.97           N  
ANISOU 1440  N   ASN B  83     2620   2997   3111   -406    -68   -295       N  
ATOM   1441  CA  ASN B  83      -1.452  22.031  31.432  1.00 22.08           C  
ANISOU 1441  CA  ASN B  83     2614   2845   2929   -332   -168    -88       C  
ATOM   1442  C   ASN B  83      -2.899  22.357  31.084  1.00 20.96           C  
ANISOU 1442  C   ASN B  83     2574   2751   2640   -389   -152     34       C  
ATOM   1443  O   ASN B  83      -3.164  23.136  30.148  1.00 20.97           O  
ANISOU 1443  O   ASN B  83     2612   2818   2539   -495   -117     45       O  
ATOM   1444  CB  ASN B  83      -0.801  23.326  31.900  1.00 21.97           C  
ANISOU 1444  CB  ASN B  83     2601   2877   2868   -339   -180    -65       C  
ATOM   1445  CG  ASN B  83       0.641  23.149  32.393  1.00 25.41           C  
ANISOU 1445  CG  ASN B  83     2909   3293   3453   -280   -217   -187       C  
ATOM   1446  OD1 ASN B  83       0.974  22.176  33.079  1.00 24.09           O  
ANISOU 1446  OD1 ASN B  83     2692   3014   3446   -167   -334   -201       O  
ATOM   1447  ND2 ASN B  83       1.491  24.141  32.075  1.00 23.23           N  
ANISOU 1447  ND2 ASN B  83     2588   3113   3125   -375   -156   -264       N  
ATOM   1448  N  AILE B  84      -3.845  21.754  31.795  0.50 20.28           N  
ANISOU 1448  N  AILE B  84     2531   2638   2536   -352   -202    123       N  
ATOM   1449  N  BILE B  84      -3.807  21.794  31.877  0.50 20.52           N  
ANISOU 1449  N  BILE B  84     2561   2667   2568   -347   -207    125       N  
ATOM   1450  CA AILE B  84      -5.253  22.005  31.501  0.50 19.80           C  
ANISOU 1450  CA AILE B  84     2504   2651   2369   -394   -190    186       C  
ATOM   1451  CA BILE B  84      -5.241  21.889  31.664  0.50 20.27           C  
ANISOU 1451  CA BILE B  84     2564   2704   2433   -388   -196    190       C  
ATOM   1452  C  AILE B  84      -6.042  22.486  32.731  0.50 19.65           C  
ANISOU 1452  C  AILE B  84     2481   2690   2295   -357   -227    231       C  
ATOM   1453  C  BILE B  84      -5.934  22.578  32.849  0.50 19.95           C  
ANISOU 1453  C  BILE B  84     2518   2725   2336   -350   -231    231       C  
ATOM   1454  O  AILE B  84      -5.987  21.875  33.800  0.50 20.68           O  
ANISOU 1454  O  AILE B  84     2636   2818   2404   -380   -257    264       O  
ATOM   1455  O  BILE B  84      -5.731  22.182  34.004  0.50 20.89           O  
ANISOU 1455  O  BILE B  84     2658   2842   2438   -360   -264    259       O  
ATOM   1456  CB AILE B  84      -5.953  20.782  30.803  0.50 20.13           C  
ANISOU 1456  CB AILE B  84     2563   2690   2396   -468   -159    177       C  
ATOM   1457  CB BILE B  84      -5.839  20.462  31.490  0.50 20.68           C  
ANISOU 1457  CB BILE B  84     2644   2726   2489   -443   -192    198       C  
ATOM   1458  CG1AILE B  84      -5.938  19.533  31.691  0.50 20.52           C  
ANISOU 1458  CG1AILE B  84     2654   2647   2495   -467   -220    209       C  
ATOM   1459  CG1BILE B  84      -5.372  19.827  30.171  0.50 20.06           C  
ANISOU 1459  CG1BILE B  84     2542   2613   2465   -497   -128     88       C  
ATOM   1460  CG2AILE B  84      -5.322  20.472  29.439  0.50 19.67           C  
ANISOU 1460  CG2AILE B  84     2483   2629   2361   -548    -85     65       C  
ATOM   1461  CG2BILE B  84      -7.378  20.485  31.595  0.50 21.24           C  
ANISOU 1461  CG2BILE B  84     2717   2910   2445   -501   -182    249       C  
ATOM   1462  CD1AILE B  84      -6.747  18.360  31.111  0.50 18.97           C  
ANISOU 1462  CD1AILE B  84     2501   2430   2276   -562   -207    209       C  
ATOM   1463  CD1BILE B  84      -5.500  18.306  30.139  0.50 17.17           C  
ANISOU 1463  CD1BILE B  84     2205   2134   2184   -517   -159     51       C  
ATOM   1464  N   ILE B  85      -6.724  23.616  32.571  1.00 19.72           N  
ANISOU 1464  N   ILE B  85     2458   2748   2288   -322   -247    212       N  
ATOM   1465  CA  ILE B  85      -7.642  24.164  33.582  1.00 20.37           C  
ANISOU 1465  CA  ILE B  85     2468   2925   2346   -285   -255    151       C  
ATOM   1466  C   ILE B  85      -9.025  23.593  33.328  1.00 19.96           C  
ANISOU 1466  C   ILE B  85     2349   2986   2251   -336   -231    119       C  
ATOM   1467  O   ILE B  85      -9.669  23.903  32.325  1.00 20.42           O  
ANISOU 1467  O   ILE B  85     2375   3033   2352   -310   -286    116       O  
ATOM   1468  CB  ILE B  85      -7.707  25.724  33.549  1.00 21.24           C  
ANISOU 1468  CB  ILE B  85     2544   2985   2542   -180   -334     86       C  
ATOM   1469  CG1 ILE B  85      -6.286  26.335  33.631  1.00 21.20           C  
ANISOU 1469  CG1 ILE B  85     2620   2878   2557   -174   -355    125       C  
ATOM   1470  CG2 ILE B  85      -8.700  26.291  34.658  1.00 22.47           C  
ANISOU 1470  CG2 ILE B  85     2556   3261   2718   -125   -320    -89       C  
ATOM   1471  CD1 ILE B  85      -5.489  25.913  34.831  1.00 21.64           C  
ANISOU 1471  CD1 ILE B  85     2680   2972   2570   -196   -306    122       C  
ATOM   1472  N   GLY B  86      -9.510  22.807  34.273  1.00 21.08           N  
ANISOU 1472  N   GLY B  86     2510   3416   2084   -408   -192     84       N  
ATOM   1473  CA  GLY B  86     -10.773  22.130  34.095  1.00 20.56           C  
ANISOU 1473  CA  GLY B  86     2538   3370   1906   -510   -205    162       C  
ATOM   1474  C   GLY B  86     -11.907  22.811  34.821  1.00 21.09           C  
ANISOU 1474  C   GLY B  86     2458   3720   1834   -598   -180     51       C  
ATOM   1475  O   GLY B  86     -11.705  23.812  35.515  1.00 22.12           O  
ANISOU 1475  O   GLY B  86     2459   3969   1976   -538   -172   -101       O  
ATOM   1476  N   ARG B  87     -13.101  22.231  34.707  1.00 21.66           N  
ANISOU 1476  N   ARG B  87     2536   3956   1738   -750   -180     95       N  
ATOM   1477  CA  ARG B  87     -14.322  22.885  35.195  1.00 23.04           C  
ANISOU 1477  CA  ARG B  87     2473   4536   1745   -784   -145    -97       C  
ATOM   1478  C   ARG B  87     -14.275  23.211  36.690  1.00 24.87           C  
ANISOU 1478  C   ARG B  87     2526   5117   1804   -871   -158   -210       C  
ATOM   1479  O   ARG B  87     -14.837  24.222  37.109  1.00 26.72           O  
ANISOU 1479  O   ARG B  87     2534   5629   1990   -726   -137   -495       O  
ATOM   1480  CB  ARG B  87     -15.577  22.076  34.836  1.00 23.26           C  
ANISOU 1480  CB  ARG B  87     2479   4812   1546  -1017   -138    -29       C  
ATOM   1481  CG  ARG B  87     -15.860  21.979  33.292  1.00 21.16           C  
ANISOU 1481  CG  ARG B  87     2342   4270   1429   -911   -119     21       C  
ATOM   1482  CD  ARG B  87     -17.195  21.225  33.017  1.00 24.23           C  
ANISOU 1482  CD  ARG B  87     2670   4993   1541  -1196   -116     69       C  
ATOM   1483  NE  ARG B  87     -17.193  19.857  33.559  1.00 26.92           N  
ANISOU 1483  NE  ARG B  87     3233   5362   1634  -1620   -189    318       N  
ATOM   1484  CZ  ARG B  87     -17.742  19.463  34.715  1.00 30.67           C  
ANISOU 1484  CZ  ARG B  87     3601   6302   1750  -1997   -221    344       C  
ATOM   1485  NH1 ARG B  87     -18.385  20.308  35.520  1.00 29.23           N  
ANISOU 1485  NH1 ARG B  87     2997   6709   1402  -1970   -142     76       N  
ATOM   1486  NH2 ARG B  87     -17.639  18.193  35.074  1.00 32.62           N  
ANISOU 1486  NH2 ARG B  87     4198   6427   1770  -2421   -365    629       N  
ATOM   1487  N   ASN B  88     -13.599  22.385  37.489  1.00 25.65           N  
ANISOU 1487  N   ASN B  88     2745   5195   1804  -1074   -226    -16       N  
ATOM   1488  CA  ASN B  88     -13.480  22.649  38.911  1.00 27.64           C  
ANISOU 1488  CA  ASN B  88     2849   5788   1866  -1208   -246    -96       C  
ATOM   1489  C   ASN B  88     -12.947  24.054  39.220  1.00 27.44           C  
ANISOU 1489  C   ASN B  88     2678   5740   2009   -926   -206   -362       C  
ATOM   1490  O   ASN B  88     -13.337  24.674  40.229  1.00 29.44           O  
ANISOU 1490  O   ASN B  88     2717   6383   2087   -954   -186   -591       O  
ATOM   1491  CB  ASN B  88     -12.658  21.566  39.619  1.00 29.24           C  
ANISOU 1491  CB  ASN B  88     3283   5859   1967  -1429   -397    190       C  
ATOM   1492  CG  ASN B  88     -11.165  21.722  39.417  1.00 29.61           C  
ANISOU 1492  CG  ASN B  88     3433   5517   2302  -1155   -456    237       C  
ATOM   1493  OD1 ASN B  88     -10.696  21.706  38.291  1.00 27.33           O  
ANISOU 1493  OD1 ASN B  88     3231   4903   2252   -934   -431    248       O  
ATOM   1494  ND2 ASN B  88     -10.403  21.858  40.532  1.00 29.72           N  
ANISOU 1494  ND2 ASN B  88     3402   5643   2249  -1202   -535    249       N  
ATOM   1495  N   LEU B  89     -12.088  24.571  38.346  1.00 24.60           N  
ANISOU 1495  N   LEU B  89     2445   4957   1943   -698   -207   -353       N  
ATOM   1496  CA  LEU B  89     -11.568  25.926  38.516  1.00 25.21           C  
ANISOU 1496  CA  LEU B  89     2492   4937   2150   -516   -218   -570       C  
ATOM   1497  C   LEU B  89     -12.236  26.941  37.591  1.00 25.14           C  
ANISOU 1497  C   LEU B  89     2529   4761   2260   -284   -244   -769       C  
ATOM   1498  O   LEU B  89     -12.360  28.115  37.934  1.00 26.48           O  
ANISOU 1498  O   LEU B  89     2699   4915   2446   -118   -322  -1032       O  
ATOM   1499  CB  LEU B  89     -10.042  25.950  38.345  1.00 24.37           C  
ANISOU 1499  CB  LEU B  89     2495   4562   2201   -525   -240   -435       C  
ATOM   1500  CG  LEU B  89      -9.250  25.123  39.366  1.00 26.48           C  
ANISOU 1500  CG  LEU B  89     2724   4972   2363   -663   -294   -282       C  
ATOM   1501  CD1 LEU B  89      -7.738  25.242  39.109  1.00 28.96           C  
ANISOU 1501  CD1 LEU B  89     3051   5133   2818   -612   -321   -224       C  
ATOM   1502  CD2 LEU B  89      -9.576  25.573  40.773  1.00 29.73           C  
ANISOU 1502  CD2 LEU B  89     2996   5727   2573   -772   -308   -429       C  
ATOM   1503  N   LEU B  90     -12.665  26.490  36.416  1.00 23.65           N  
ANISOU 1503  N   LEU B  90     2426   4414   2145   -260   -223   -650       N  
ATOM   1504  CA  LEU B  90     -13.363  27.367  35.483  1.00 24.33           C  
ANISOU 1504  CA  LEU B  90     2589   4330   2324    -41   -300   -804       C  
ATOM   1505  C   LEU B  90     -14.603  27.977  36.140  1.00 26.60           C  
ANISOU 1505  C   LEU B  90     2654   4991   2462    168   -366  -1150       C  
ATOM   1506  O   LEU B  90     -14.878  29.168  35.944  1.00 28.24           O  
ANISOU 1506  O   LEU B  90     2959   5024   2749    464   -531  -1406       O  
ATOM   1507  CB  LEU B  90     -13.738  26.638  34.190  1.00 22.32           C  
ANISOU 1507  CB  LEU B  90     2424   3935   2122    -88   -260   -617       C  
ATOM   1508  CG  LEU B  90     -12.564  26.191  33.288  1.00 20.98           C  
ANISOU 1508  CG  LEU B  90     2448   3432   2092   -211   -209   -378       C  
ATOM   1509  CD1 LEU B  90     -13.149  25.406  32.111  1.00 18.02           C  
ANISOU 1509  CD1 LEU B  90     2141   2985   1720   -252   -169   -246       C  
ATOM   1510  CD2 LEU B  90     -11.676  27.367  32.787  1.00 22.79           C  
ANISOU 1510  CD2 LEU B  90     2863   3356   2442   -198   -285   -416       C  
ATOM   1511  N   THR B  91     -15.332  27.174  36.918  1.00 27.57           N  
ANISOU 1511  N   THR B  91     2498   5644   2333      6   -272  -1180       N  
ATOM   1512  CA  THR B  91     -16.532  27.665  37.600  1.00 31.74           C  
ANISOU 1512  CA  THR B  91     2691   6730   2638    180   -301  -1576       C  
ATOM   1513  C   THR B  91     -16.181  28.792  38.587  1.00 34.86           C  
ANISOU 1513  C   THR B  91     3056   7154   3035    401   -390  -1906       C  
ATOM   1514  O   THR B  91     -16.914  29.791  38.714  1.00 37.05           O  
ANISOU 1514  O   THR B  91     3217   7574   3285    802   -531  -2341       O  
ATOM   1515  CB  THR B  91     -17.310  26.544  38.350  1.00 33.43           C  
ANISOU 1515  CB  THR B  91     2593   7635   2473   -203   -169  -1526       C  
ATOM   1516  OG1 THR B  91     -16.442  25.824  39.223  1.00 31.09           O  
ANISOU 1516  OG1 THR B  91     2395   7332   2085   -566   -116  -1265       O  
ATOM   1517  CG2 THR B  91     -17.909  25.572  37.405  1.00 31.45           C  
ANISOU 1517  CG2 THR B  91     2379   7406   2165   -408   -127  -1286       C  
ATOM   1518  N   GLN B  92     -15.027  28.656  39.247  1.00 34.42           N  
ANISOU 1518  N   GLN B  92     3129   6933   3016    180   -346  -1725       N  
ATOM   1519  CA  GLN B  92     -14.628  29.617  40.269  1.00 37.96           C  
ANISOU 1519  CA  GLN B  92     3563   7430   3428    303   -419  -2011       C  
ATOM   1520  C   GLN B  92     -14.241  30.977  39.694  1.00 38.75           C  
ANISOU 1520  C   GLN B  92     4005   6949   3768    628   -636  -2185       C  
ATOM   1521  O   GLN B  92     -14.261  31.975  40.404  1.00 43.21           O  
ANISOU 1521  O   GLN B  92     4602   7524   4291    845   -772  -2541       O  
ATOM   1522  CB  GLN B  92     -13.457  29.085  41.113  1.00 36.78           C  
ANISOU 1522  CB  GLN B  92     3461   7280   3235    -47   -338  -1748       C  
ATOM   1523  CG  GLN B  92     -13.518  27.615  41.523  1.00 39.54           C  
ANISOU 1523  CG  GLN B  92     3684   7961   3378   -440   -221  -1432       C  
ATOM   1524  CD  GLN B  92     -14.623  27.291  42.502  1.00 46.43           C  
ANISOU 1524  CD  GLN B  92     4207   9580   3855   -613   -155  -1641       C  
ATOM   1525  OE1 GLN B  92     -15.738  26.871  42.111  1.00 50.84           O  
ANISOU 1525  OE1 GLN B  92     4585  10481   4252   -654   -109  -1701       O  
ATOM   1526  NE2 GLN B  92     -14.335  27.480  43.784  1.00 49.50           N  
ANISOU 1526  NE2 GLN B  92     4468  10306   4035   -766   -145  -1765       N  
ATOM   1527  N   ILE B  93     -13.812  31.015  38.445  1.00 36.51           N  
ANISOU 1527  N   ILE B  93     4026   6145   3700    607   -693  -1924       N  
ATOM   1528  CA  ILE B  93     -13.486  32.284  37.817  1.00 37.77           C  
ANISOU 1528  CA  ILE B  93     4601   5725   4025    802   -953  -2031       C  
ATOM   1529  C   ILE B  93     -14.665  32.791  36.975  1.00 40.02           C  
ANISOU 1529  C   ILE B  93     4956   5893   4356   1209  -1163  -2251       C  
ATOM   1530  O   ILE B  93     -14.535  33.789  36.271  1.00 42.19           O  
ANISOU 1530  O   ILE B  93     5668   5609   4754   1372  -1454  -2296       O  
ATOM   1531  CB  ILE B  93     -12.146  32.221  37.022  1.00 35.36           C  
ANISOU 1531  CB  ILE B  93     4612   4967   3857    452   -927  -1638       C  
ATOM   1532  CG1 ILE B  93     -12.294  31.344  35.771  1.00 34.14           C  
ANISOU 1532  CG1 ILE B  93     4452   4743   3778    345   -815  -1341       C  
ATOM   1533  CG2 ILE B  93     -10.974  31.772  37.958  1.00 34.86           C  
ANISOU 1533  CG2 ILE B  93     4418   5097   3730    132   -766  -1489       C  
ATOM   1534  CD1 ILE B  93     -11.052  31.249  34.882  1.00 35.31           C  
ANISOU 1534  CD1 ILE B  93     4824   4586   4005     17   -771  -1029       C  
ATOM   1535  N   GLY B  94     -15.809  32.103  37.054  1.00 40.80           N  
ANISOU 1535  N   GLY B  94     4645   6537   4319   1337  -1048  -2378       N  
ATOM   1536  CA  GLY B  94     -17.038  32.541  36.399  1.00 43.85           C  
ANISOU 1536  CA  GLY B  94     4974   6981   4705   1779  -1253  -2660       C  
ATOM   1537  C   GLY B  94     -17.013  32.368  34.889  1.00 43.34           C  
ANISOU 1537  C   GLY B  94     5203   6462   4802   1711  -1326  -2333       C  
ATOM   1538  O   GLY B  94     -17.604  33.163  34.130  1.00 45.33           O  
ANISOU 1538  O   GLY B  94     5682   6406   5133   2087  -1642  -2499       O  
ATOM   1539  N   CYS B  95     -16.340  31.315  34.447  1.00 39.64           N  
ANISOU 1539  N   CYS B  95     4742   5955   4364   1254  -1066  -1889       N  
ATOM   1540  CA  CYS B  95     -16.129  31.084  33.040  1.00 38.78           C  
ANISOU 1540  CA  CYS B  95     4904   5453   4380   1112  -1090  -1573       C  
ATOM   1541  C   CYS B  95     -17.348  30.393  32.438  1.00 38.85           C  
ANISOU 1541  C   CYS B  95     4647   5814   4301   1208  -1041  -1593       C  
ATOM   1542  O   CYS B  95     -17.838  29.396  32.990  1.00 37.53           O  
ANISOU 1542  O   CYS B  95     4102   6198   3960   1044   -821  -1587       O  
ATOM   1543  CB  CYS B  95     -14.856  30.254  32.828  1.00 35.32           C  
ANISOU 1543  CB  CYS B  95     4552   4877   3991    652   -851  -1179       C  
ATOM   1544  SG  CYS B  95     -14.473  30.119  31.107  1.00 37.51           S  
ANISOU 1544  SG  CYS B  95     5150   4731   4372    460   -878   -865       S  
ATOM   1545  N   THR B  96     -17.840  30.950  31.319  1.00 40.30           N  
ANISOU 1545  N   THR B  96     5062   5684   4566   1425  -1281  -1604       N  
ATOM   1546  CA  THR B  96     -19.014  30.430  30.601  1.00 40.56           C  
ANISOU 1546  CA  THR B  96     4865   6033   4513   1533  -1284  -1632       C  
ATOM   1547  C   THR B  96     -18.740  30.198  29.112  1.00 39.28           C  
ANISOU 1547  C   THR B  96     5034   5440   4451   1323  -1314  -1282       C  
ATOM   1548  O   THR B  96     -17.894  30.868  28.513  1.00 39.30           O  
ANISOU 1548  O   THR B  96     5487   4870   4575   1227  -1465  -1119       O  
ATOM   1549  CB  THR B  96     -20.246  31.379  30.727  1.00 45.40           C  
ANISOU 1549  CB  THR B  96     5324   6856   5071   2147  -1620  -2113       C  
ATOM   1550  OG1 THR B  96     -20.004  32.587  29.995  1.00 46.93           O  
ANISOU 1550  OG1 THR B  96     6067   6332   5434   2430  -2038  -2135       O  
ATOM   1551  CG2 THR B  96     -20.539  31.711  32.174  1.00 47.11           C  
ANISOU 1551  CG2 THR B  96     5184   7563   5151   2393  -1602  -2547       C  
ATOM   1552  N   LEU B  97     -19.433  29.221  28.530  1.00 38.08           N  
ANISOU 1552  N   LEU B  97     4662   5608   4201   1178  -1166  -1163       N  
ATOM   1553  CA  LEU B  97     -19.461  29.044  27.090  1.00 37.66           C  
ANISOU 1553  CA  LEU B  97     4863   5248   4197   1043  -1223   -911       C  
ATOM   1554  C   LEU B  97     -20.707  29.728  26.548  1.00 41.22           C  
ANISOU 1554  C   LEU B  97     5264   5787   4611   1473  -1552  -1146       C  
ATOM   1555  O   LEU B  97     -21.781  29.619  27.132  1.00 43.57           O  
ANISOU 1555  O   LEU B  97     5120   6672   4764   1735  -1568  -1454       O  
ATOM   1556  CB  LEU B  97     -19.551  27.571  26.730  1.00 35.20           C  
ANISOU 1556  CB  LEU B  97     4381   5211   3782    653   -917   -672       C  
ATOM   1557  CG  LEU B  97     -18.334  26.674  26.762  1.00 32.40           C  
ANISOU 1557  CG  LEU B  97     4156   4683   3473    263   -657   -399       C  
ATOM   1558  CD1 LEU B  97     -18.830  25.225  26.635  1.00 30.10           C  
ANISOU 1558  CD1 LEU B  97     3702   4709   3026    -15   -462   -267       C  
ATOM   1559  CD2 LEU B  97     -17.390  27.041  25.615  1.00 30.82           C  
ANISOU 1559  CD2 LEU B  97     4331   3990   3388    118   -702   -199       C  
ATOM   1560  N   ASN B  98     -20.569  30.424  25.431  1.00 43.09           N  
ANISOU 1560  N   ASN B  98     5938   5495   4939   1529  -1834  -1012       N  
ATOM   1561  CA  ASN B  98     -21.705  31.097  24.793  1.00 47.73           C  
ANISOU 1561  CA  ASN B  98     6554   6081   5500   1980  -2232  -1209       C  
ATOM   1562  C   ASN B  98     -21.663  30.961  23.273  1.00 47.19           C  
ANISOU 1562  C   ASN B  98     6826   5671   5434   1726  -2330   -874       C  
ATOM   1563  O   ASN B  98     -20.609  31.052  22.663  1.00 45.03           O  
ANISOU 1563  O   ASN B  98     6974   4924   5210   1327  -2287   -561       O  
ATOM   1564  CB  ASN B  98     -21.775  32.580  25.219  1.00 52.44           C  
ANISOU 1564  CB  ASN B  98     7459   6278   6186   2523  -2723  -1524       C  
ATOM   1565  CG  ASN B  98     -23.077  33.288  24.777  1.00 60.09           C  
ANISOU 1565  CG  ASN B  98     8387   7324   7122   3178  -3214  -1855       C  
ATOM   1566  OD1 ASN B  98     -23.572  33.100  23.660  1.00 63.84           O  
ANISOU 1566  OD1 ASN B  98     8948   7750   7560   3137  -3343  -1683       O  
ATOM   1567  ND2 ASN B  98     -23.609  34.147  25.655  1.00 65.94           N  
ANISOU 1567  ND2 ASN B  98     9006   8183   7866   3829  -3528  -2366       N  
ATOM   1568  N   PHE B  99     -22.833  30.742  22.679  1.00 49.21           N  
ANISOU 1568  N   PHE B  99     6851   6254   5591   1935  -2458   -968       N  
ATOM   1569  CA  PHE B  99     -22.993  30.689  21.231  1.00 50.03           C  
ANISOU 1569  CA  PHE B  99     7256   6087   5665   1751  -2609   -693       C  
ATOM   1570  C   PHE B  99     -24.469  30.932  20.865  1.00 54.35           C  
ANISOU 1570  C   PHE B  99     7533   7003   6116   2246  -2941   -956       C  
ATOM   1571  O   PHE B  99     -24.869  31.012  19.690  1.00 55.61           O  
ANISOU 1571  O   PHE B  99     7903   6999   6228   2212  -3166   -790       O  
ATOM   1572  CB  PHE B  99     -22.486  29.354  20.672  1.00 45.56           C  
ANISOU 1572  CB  PHE B  99     6610   5670   5030   1121  -2137   -357       C  
ATOM   1573  CG  PHE B  99     -23.331  28.174  21.063  1.00 45.74           C  
ANISOU 1573  CG  PHE B  99     6076   6403   4901   1033  -1837   -456       C  
ATOM   1574  CD1 PHE B  99     -23.155  27.555  22.300  1.00 43.63           C  
ANISOU 1574  CD1 PHE B  99     5477   6508   4592    937  -1538   -568       C  
ATOM   1575  CD2 PHE B  99     -24.308  27.680  20.191  1.00 46.91           C  
ANISOU 1575  CD2 PHE B  99     6064   6859   4900    977  -1880   -416       C  
ATOM   1576  CE1 PHE B  99     -23.938  26.480  22.668  1.00 44.08           C  
ANISOU 1576  CE1 PHE B  99     5099   7211   4436    737  -1308   -621       C  
ATOM   1577  CE2 PHE B  99     -25.105  26.593  20.557  1.00 47.45           C  
ANISOU 1577  CE2 PHE B  99     5656   7611   4762    786  -1627   -491       C  
ATOM   1578  CZ  PHE B  99     -24.922  25.991  21.788  1.00 44.04           C  
ANISOU 1578  CZ  PHE B  99     4945   7526   4263    636  -1350   -582       C  
ATOM   1579  OXT PHE B  99     -25.314  31.070  21.761  1.00 56.77           O  
ANISOU 1579  OXT PHE B  99     7358   7854   6358   2707  -3002  -1377       O  
TER    1580      PHE B  99                                                     



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